Nutrient chapter

Sulforaphane / SFN, stereochemistry specified per study

Sulforaphane is a broccoli-derived isothiocyanate formed from glucoraphanin. Its exposure depends on myrosinase and microbial conversion; its effects involve electrophile sensing, glutathione metabolism and other targets. It is not an essential vitamin, and no sulforaphane-deficiency syndrome is established.

124 recorded mechanisms · 6 availability situations · 9 preserved sources. Draft and verified records are labeled separately.

Read recorded mechanisms Open recursive mind map

The mechanisms

What the sources say this nutrient does, one relationship at a time. Plain wording comes first; the technical statement follows.

Myrosinase hydrolysis of glucoraphanin after broccoli tissue disruption enabled sulforaphane formation.
Broccoli myrosinase, study-resolved enzyme → Sulforaphane / SFN, stereochemistry specified per study source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/15184012.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3a1b248b03fcfc77ee38ab6b4189c6c565b24f2071912565f0377ce00e8de0e6", "start_char": 0, "end_char": 1665, "text_sha256": "3a1b248b03fcfc77ee38ab6b4189c6c565b24f2071912565f0377ce00e8de0e6"}
experimental_model
Food processing and enzyme-activity experiments
exposure
Heating before homogenization, including 60 and at least 70 degrees C
limitations
Time, cultivar, food matrix and enzyme heat sensitivities matter; not a universal cooking prescription.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Broccoli florets and sprouts; mouse hepatoma bioassay
plain_language
The precursor and plant enzyme must come together before this product is formed.
primary_references
[sulforaphane-p15184012] Heating decreases epithiospecifier protein activity and increases sulforaphane formation in broccoli. (2004). https://pubmed.ncbi.nlm.nih.gov/15184012/ DOI: 10.1016/j.phytochem.2004.04.013
tissue_or_cell_type
Plant tissue hydrolysis
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 138–149
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Food processing and enzyme-activity experiments · source_derived_draft · unverified_draft
### sulforaphane-myrosinase-formation Myrosinase hydrolysis of glucoraphanin after broccoli tissue disruption enabled sulforaphane formation. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The precursor and plant enzyme must come together before this product is formed. organism: Broccoli florets and sprouts; mouse hepatoma bioassay tissue_or_cell_type: Plant tissue hydrolysis experimental_model: Food processing and enzyme-activity experiments limitations: Time, cultivar, food matrix and enzyme heat sensitivities matter; not a universal cooking prescription. exposure: Heating before homogenization, including 60 and at least 70 degrees C evidence_span: {"source_cache": "artifacts/sulforaphane-research/15184012.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3a1b248b03fcfc77ee38ab6b4189c6c565b24f2071912565f0377ce00e8de0e6", "start_char": 0, "end_char": 1665, "text_sha256": "3a1b248b03fcfc77ee38ab6b4189c6c565b24f2071912565f0377ce00e8de0e6"} [sulforaphane-p15184012] Heating decreases epithiospecifier protein activity and increases sulforaphane formation in broccoli. (2004). https://pubmed.ncbi.nlm.nih.gov/15184012/ DOI: 10.1016/j.phytochem.2004.04.013
Complete structured claim and evidence
Ascorbate accelerated hydrolysis of the glycosyl-enzyme intermediate and occupied a position supporting its role as the catalytic base.
L-Ascorbate → Mustard myrosinase, study-resolved enzyme source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/10978344.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ed373ac9a91fa7b03d25c21c32adaf57dd2f0f9b65e1f99e9da49aab4c22b0aa", "start_char": 0, "end_char": 1511, "text_sha256": "ed373ac9a91fa7b03d25c21c32adaf57dd2f0f9b65e1f99e9da49aab4c22b0aa"}
experimental_model
High-resolution crystallography and reactivation kinetics
exposure
Ascorbate with substrate analogues and a trapped glycosyl-enzyme intermediate
limitations
Plant enzyme chemistry; does not show that vitamin C pills increase systemic sulforaphane in people.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Mustard plant myrosinase
plain_language
Vitamin C can help the plant enzyme carry out its reaction.
primary_references
[sulforaphane-p10978344] High resolution X-ray crystallography shows that ascorbate is a cofactor for myrosinase and substitutes for the function of the catalytic base. (2000). https://pubmed.ncbi.nlm.nih.gov/10978344/ DOI: 10.1074/jbc.m006796200
tissue_or_cell_type
Enzyme active site
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 190–201
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · High-resolution crystallography and reactivation kinetics · source_derived_draft · unverified_draft
### sulforaphane-ascorbate-myrosinase Ascorbate accelerated hydrolysis of the glycosyl-enzyme intermediate and occupied a position supporting its role as the catalytic base. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Vitamin C can help the plant enzyme carry out its reaction. organism: Mustard plant myrosinase tissue_or_cell_type: Enzyme active site experimental_model: High-resolution crystallography and reactivation kinetics limitations: Plant enzyme chemistry; does not show that vitamin C pills increase systemic sulforaphane in people. exposure: Ascorbate with substrate analogues and a trapped glycosyl-enzyme intermediate evidence_span: {"source_cache": "artifacts/sulforaphane-research/10978344.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ed373ac9a91fa7b03d25c21c32adaf57dd2f0f9b65e1f99e9da49aab4c22b0aa", "start_char": 0, "end_char": 1511, "text_sha256": "ed373ac9a91fa7b03d25c21c32adaf57dd2f0f9b65e1f99e9da49aab4c22b0aa"} [sulforaphane-p10978344] High resolution X-ray crystallography shows that ascorbate is a cofactor for myrosinase and substitutes for the function of the catalytic base. (2000). https://pubmed.ncbi.nlm.nih.gov/10978344/ DOI: 10.1074/jbc.m006796200
Complete structured claim and evidence
Recombinant broccoli ESP redirected myrosinase-dependent glucoraphanin hydrolysis toward sulforaphane nitrile rather than sulforaphane.
Broccoli epithiospecifier protein / ESP → Sulforaphane nitrile source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/16536577.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e3636614520a0c9f83132284992ffc10ca42943f97619933f8009ceb697ddfa9", "start_char": 0, "end_char": 1301, "text_sha256": "e3636614520a0c9f83132284992ffc10ca42943f97619933f8009ceb697ddfa9"}
experimental_model
Recombinant protein and glucosinolate product analysis
exposure
Purified recombinant ESP in a model hydrolysis system
limitations
Plant chemistry; does not establish a human health effect of the nitrile product.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Broccoli cv. Packman ESP expressed in E. coli
plain_language
A second plant protein changes which molecule is produced.
primary_references
[sulforaphane-p16536577] Epithiospecifier protein from broccoli (Brassica oleracea L. ssp. italica) inhibits formation of the anticancer agent sulforaphane. (2006). https://pubmed.ncbi.nlm.nih.gov/16536577/ DOI: 10.1021/jf0525277
tissue_or_cell_type
Myrosinase-dependent glucoraphanin conversion
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 177–188
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant protein and glucosinolate product analysis · source_derived_draft · unverified_draft
### sulforaphane-esp-nitrile Recombinant broccoli ESP redirected myrosinase-dependent glucoraphanin hydrolysis toward sulforaphane nitrile rather than sulforaphane. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: A second plant protein changes which molecule is produced. organism: Broccoli cv. Packman ESP expressed in E. coli tissue_or_cell_type: Myrosinase-dependent glucoraphanin conversion experimental_model: Recombinant protein and glucosinolate product analysis limitations: Plant chemistry; does not establish a human health effect of the nitrile product. exposure: Purified recombinant ESP in a model hydrolysis system evidence_span: {"source_cache": "artifacts/sulforaphane-research/16536577.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e3636614520a0c9f83132284992ffc10ca42943f97619933f8009ceb697ddfa9", "start_char": 0, "end_char": 1301, "text_sha256": "e3636614520a0c9f83132284992ffc10ca42943f97619933f8009ceb697ddfa9"} [sulforaphane-p16536577] Epithiospecifier protein from broccoli (Brassica oleracea L. ssp. italica) inhibits formation of the anticancer agent sulforaphane. (2006). https://pubmed.ncbi.nlm.nih.gov/16536577/ DOI: 10.1021/jf0525277
Complete structured claim and evidence
Myrosinase increased mean urinary-metabolite-based recovery from 18.6% to 39.8%, and early conversion during the first eight hours from 8.0% to 25.4%.
Glucoraphanin plus active myrosinase preparation → Systemic sulforaphane exposure measured by study-specific biomarkers source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/41692762.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "67e337141c8012ea573d9720d5e4774bfdd1ae098c056b68991752169fbdb32a", "start_char": 0, "end_char": 1248, "text_sha256": "67e337141c8012ea573d9720d5e4774bfdd1ae098c056b68991752169fbdb32a"}
experimental_model
Randomized double-blind crossover single-dose study
exposure
Broccoli seed glucoraphanin with versus without mustard myrosinase; both arms contained ascorbic acid
limitations
Both arms included ascorbic acid, so its independent benefit cannot be inferred; conversion biomarker is not clinical efficacy.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human, 16 adults, nine women and seven men
plain_language
A recent controlled product comparison confirms the importance of enzyme activity.
primary_references
[sulforaphane-p41692762] Exogenous myrosinase from mustard seed increases bioavailability of sulforaphane from a glucoraphanin-rich broccoli seed extract in a randomized clinical study. (2026). https://pubmed.ncbi.nlm.nih.gov/41692762/ DOI: 10.1038/s41598-026-39389-4
tissue_or_cell_type
Urinary metabolites and fecal microbial genes
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 996–1007
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized double-blind crossover single-dose study · source_derived_draft · unverified_draft
### sulforaphane-mustard-seed-trial Myrosinase increased mean urinary-metabolite-based recovery from 18.6% to 39.8%, and early conversion during the first eight hours from 8.0% to 25.4%. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: A recent controlled product comparison confirms the importance of enzyme activity. organism: Human, 16 adults, nine women and seven men tissue_or_cell_type: Urinary metabolites and fecal microbial genes experimental_model: Randomized double-blind crossover single-dose study limitations: Both arms included ascorbic acid, so its independent benefit cannot be inferred; conversion biomarker is not clinical efficacy. exposure: Broccoli seed glucoraphanin with versus without mustard myrosinase; both arms contained ascorbic acid evidence_span: {"source_cache": "artifacts/sulforaphane-research/41692762.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "67e337141c8012ea573d9720d5e4774bfdd1ae098c056b68991752169fbdb32a", "start_char": 0, "end_char": 1248, "text_sha256": "67e337141c8012ea573d9720d5e4774bfdd1ae098c056b68991752169fbdb32a"} [sulforaphane-p41692762] Exogenous myrosinase from mustard seed increases bioavailability of sulforaphane from a glucoraphanin-rich broccoli seed extract in a randomized clinical study. (2026). https://pubmed.ncbi.nlm.nih.gov/41692762/ DOI: 10.1038/s41598-026-39389-4
Complete structured claim and evidence
Revised mass spectrometry detected sulforaphane modification of at least four KEAP1 cysteines, including readily modified C151.
Sulforaphane / SFN, stereochemistry specified per study → Human KEAP1 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/21391649.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d1ecbe68352504813e0a666dc7474fba7f0a3f3aeb5d0b2fea681d376df999ac", "start_char": 0, "end_char": 1511, "text_sha256": "d1ecbe68352504813e0a666dc7474fba7f0a3f3aeb5d0b2fea681d376df999ac"}
experimental_model
Mass spectrometry with revised sample preparation
exposure
Sulforaphane exposure; omission of iodoacetamide and shorter processing
limitations
Explains an assay-dependent detection problem; not an unresolved universal C151 disagreement or a human efficacy trial.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
KEAP1 protein cysteine mapping
plain_language
The molecule changes a sensor protein that controls the stress-response program.
primary_references
[sulforaphane-p21391649] Modification of keap1 cysteine residues by sulforaphane. (2011). https://pubmed.ncbi.nlm.nih.gov/21391649/ DOI: 10.1021/tx100389r
tissue_or_cell_type
Reversible electrophile-thiol adducts
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 424–435
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Mass spectrometry with revised sample preparation · source_derived_draft · unverified_draft
### sulforaphane-keap1-cysteines Revised mass spectrometry detected sulforaphane modification of at least four KEAP1 cysteines, including readily modified C151. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The molecule changes a sensor protein that controls the stress-response program. organism: KEAP1 protein cysteine mapping tissue_or_cell_type: Reversible electrophile-thiol adducts experimental_model: Mass spectrometry with revised sample preparation limitations: Explains an assay-dependent detection problem; not an unresolved universal C151 disagreement or a human efficacy trial. exposure: Sulforaphane exposure; omission of iodoacetamide and shorter processing evidence_span: {"source_cache": "artifacts/sulforaphane-research/21391649.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d1ecbe68352504813e0a666dc7474fba7f0a3f3aeb5d0b2fea681d376df999ac", "start_char": 0, "end_char": 1511, "text_sha256": "d1ecbe68352504813e0a666dc7474fba7f0a3f3aeb5d0b2fea681d376df999ac"} [sulforaphane-p21391649] Modification of keap1 cysteine residues by sulforaphane. (2011). https://pubmed.ncbi.nlm.nih.gov/21391649/ DOI: 10.1021/tx100389r
Complete structured claim and evidence
Sulforaphane inhibited KEAP1-dependent ubiquitination of Nrf2.
Sulforaphane / SFN, stereochemistry specified per study → KEAP1-dependent Nrf2 ubiquitination source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/15572695.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d120b0ea48a77a99b12e9147e4acb02fd63026ed729a37d5e2edf174c5674765", "start_char": 0, "end_char": 1484, "text_sha256": "d120b0ea48a77a99b12e9147e4acb02fd63026ed729a37d5e2edf174c5674765"}
experimental_model
Cell transfection, coimmunoprecipitation and ubiquitination assays
exposure
Sulforaphane or quinone stress; C151S KEAP1 comparison
limitations
The measured interaction is ubiquitin-ligase regulation; do not describe it as obligatory physical release of all bound Nrf2.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human protein constructs in mammalian cell systems
plain_language
Less disposal allows the regulator to persist.
primary_references
[sulforaphane-p15572695] Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex. (2004). https://pubmed.ncbi.nlm.nih.gov/15572695/ DOI: 10.1128/mcb.24.24.10941-10953.2004
tissue_or_cell_type
KEAP1-CUL3-RBX1 control of Nrf2
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 476–487
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cell transfection, coimmunoprecipitation and ubiquitination assays · source_derived_draft · unverified_draft
### sulforaphane-sfn-ubiquitination Sulforaphane inhibited KEAP1-dependent ubiquitination of Nrf2. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Less disposal allows the regulator to persist. organism: Human protein constructs in mammalian cell systems tissue_or_cell_type: KEAP1-CUL3-RBX1 control of Nrf2 experimental_model: Cell transfection, coimmunoprecipitation and ubiquitination assays limitations: The measured interaction is ubiquitin-ligase regulation; do not describe it as obligatory physical release of all bound Nrf2. exposure: Sulforaphane or quinone stress; C151S KEAP1 comparison evidence_span: {"source_cache": "artifacts/sulforaphane-research/15572695.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d120b0ea48a77a99b12e9147e4acb02fd63026ed729a37d5e2edf174c5674765", "start_char": 0, "end_char": 1484, "text_sha256": "d120b0ea48a77a99b12e9147e4acb02fd63026ed729a37d5e2edf174c5674765"} [sulforaphane-p15572695] Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex. (2004). https://pubmed.ncbi.nlm.nih.gov/15572695/ DOI: 10.1128/mcb.24.24.10941-10953.2004
Complete structured claim and evidence
Sulforaphane increased nuclear localization of stabilized Nrf2 and Nrf2-dependent gene activation.
Sulforaphane / SFN, stereochemistry specified per study → Nrf2 nuclear localization source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/14585973.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bc2e1304879d9bd3d1b4946981f93a78d3f604c580ea252af17f645e237cadd0", "start_char": 0, "end_char": 1647, "text_sha256": "bc2e1304879d9bd3d1b4946981f93a78d3f604c580ea252af17f645e237cadd0"}
experimental_model
KEAP1 mutagenesis and Nrf2 stability/localization assays
exposure
Sulforaphane or oxidative stress; C151/C273/C288 variants
limitations
Individual cysteines have different roles; activating Nrf2 does not establish prevention or treatment of cancer in humans.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human KEAP1 constructs in cellular experiments
plain_language
The regulator accumulates where it can influence gene expression.
primary_references
[sulforaphane-p14585973] Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress. (2003). https://pubmed.ncbi.nlm.nih.gov/14585973/ DOI: 10.1128/mcb.23.22.8137-8151.2003
tissue_or_cell_type
Ubiquitination, protein turnover and nuclear localization
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 528–539
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · KEAP1 mutagenesis and Nrf2 stability/localization assays · source_derived_draft · unverified_draft
### sulforaphane-nrf2-nuclear Sulforaphane increased nuclear localization of stabilized Nrf2 and Nrf2-dependent gene activation. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The regulator accumulates where it can influence gene expression. organism: Human KEAP1 constructs in cellular experiments tissue_or_cell_type: Ubiquitination, protein turnover and nuclear localization experimental_model: KEAP1 mutagenesis and Nrf2 stability/localization assays limitations: Individual cysteines have different roles; activating Nrf2 does not establish prevention or treatment of cancer in humans. exposure: Sulforaphane or oxidative stress; C151/C273/C288 variants evidence_span: {"source_cache": "artifacts/sulforaphane-research/14585973.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bc2e1304879d9bd3d1b4946981f93a78d3f604c580ea252af17f645e237cadd0", "start_char": 0, "end_char": 1647, "text_sha256": "bc2e1304879d9bd3d1b4946981f93a78d3f604c580ea252af17f645e237cadd0"} [sulforaphane-p14585973] Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress. (2003). https://pubmed.ncbi.nlm.nih.gov/14585973/ DOI: 10.1128/mcb.23.22.8137-8151.2003
Complete structured claim and evidence
GSTP1-1 catalyzed sulforaphane conjugation with glutathione in the human enzyme comparison.
Human glutathione S-transferase P1 / GSTP1 → Sulforaphane-glutathione conjugate / SFN-GSH source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/7826396.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5dee3c3a8c8069c33fac2653f16f3521cdd17ef5e8ebddd0f82cfa3a5c95c0fe", "start_char": 0, "end_char": 989, "text_sha256": "5dee3c3a8c8069c33fac2653f16f3521cdd17ef5e8ebddd0f82cfa3a5c95c0fe"}
experimental_model
Recombinant human GST conjugation and reverse-reaction kinetics
exposure
Four isothiocyanates and GSTP1-1, GSTM1-1, GSTA1-1 and GSTM2-2
limitations
Relative enzyme rates are not whole-person clearance predictions; reverse reactions were slower and inhibited by high GSH.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human GST isoenzymes
plain_language
Glutathione attaches to sulforaphane during its handling.
primary_references
[sulforaphane-p7826396] Reversible conjugation of isothiocyanates with glutathione catalyzed by human glutathione transferases. (1995). https://pubmed.ncbi.nlm.nih.gov/7826396/ DOI: 10.1006/bbrc.1995.1106
tissue_or_cell_type
Isothiocyanate-glutathione chemistry
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 255–266
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human GST conjugation and reverse-reaction kinetics · source_derived_draft · unverified_draft
### sulforaphane-gstp-conjugation GSTP1-1 catalyzed sulforaphane conjugation with glutathione in the human enzyme comparison. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Glutathione attaches to sulforaphane during its handling. organism: Human GST isoenzymes tissue_or_cell_type: Isothiocyanate-glutathione chemistry experimental_model: Recombinant human GST conjugation and reverse-reaction kinetics limitations: Relative enzyme rates are not whole-person clearance predictions; reverse reactions were slower and inhibited by high GSH. exposure: Four isothiocyanates and GSTP1-1, GSTM1-1, GSTA1-1 and GSTM2-2 evidence_span: {"source_cache": "artifacts/sulforaphane-research/7826396.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5dee3c3a8c8069c33fac2653f16f3521cdd17ef5e8ebddd0f82cfa3a5c95c0fe", "start_char": 0, "end_char": 989, "text_sha256": "5dee3c3a8c8069c33fac2653f16f3521cdd17ef5e8ebddd0f82cfa3a5c95c0fe"} [sulforaphane-p7826396] Reversible conjugation of isothiocyanates with glutathione catalyzed by human glutathione transferases. (1995). https://pubmed.ncbi.nlm.nih.gov/7826396/ DOI: 10.1006/bbrc.1995.1106
Complete structured claim and evidence
Sulforaphane increased TXNRD1 mRNA up to fourfold; TXNRD2 mRNA did not show this induction.
Sulforaphane / SFN, stereochemistry specified per study → Human TXNRD1 mRNA abundance source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/12663510.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "95f1de031ede41aa12f975dff28193dcb426465d4bda94bb84d4e60ef6c292b9", "start_char": 0, "end_char": 1535, "text_sha256": "95f1de031ede41aa12f975dff28193dcb426465d4bda94bb84d4e60ef6c292b9"}
experimental_model
Transcription/translation and inhibitor experiments
exposure
Sulforaphane, sodium selenite, combined treatment and pathway inhibitors
limitations
Cell-culture synergy at specified exposures is not a clinical supplement recommendation; TXNRD1 and TXNRD2 were not interchangeable.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human HepG2 hepatoma cells
plain_language
One cytosolic enzyme gene responded while the mitochondrial counterpart did not.
primary_references
[sulforaphane-p12663510] Synergy between sulforaphane and selenium in the induction of thioredoxin reductase 1 requires both transcriptional and translational modulation. (2003). https://pubmed.ncbi.nlm.nih.gov/12663510/ DOI: 10.1093/carcin/24.3.497
tissue_or_cell_type
Thioredoxin reductase regulation
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 697–708
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Transcription/translation and inhibitor experiments · source_derived_draft · unverified_draft
### sulforaphane-txnrd1-transcription Sulforaphane increased TXNRD1 mRNA up to fourfold; TXNRD2 mRNA did not show this induction. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: One cytosolic enzyme gene responded while the mitochondrial counterpart did not. organism: Human HepG2 hepatoma cells tissue_or_cell_type: Thioredoxin reductase regulation experimental_model: Transcription/translation and inhibitor experiments limitations: Cell-culture synergy at specified exposures is not a clinical supplement recommendation; TXNRD1 and TXNRD2 were not interchangeable. exposure: Sulforaphane, sodium selenite, combined treatment and pathway inhibitors evidence_span: {"source_cache": "artifacts/sulforaphane-research/12663510.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "95f1de031ede41aa12f975dff28193dcb426465d4bda94bb84d4e60ef6c292b9", "start_char": 0, "end_char": 1535, "text_sha256": "95f1de031ede41aa12f975dff28193dcb426465d4bda94bb84d4e60ef6c292b9"} [sulforaphane-p12663510] Synergy between sulforaphane and selenium in the induction of thioredoxin reductase 1 requires both transcriptional and translational modulation. (2003). https://pubmed.ncbi.nlm.nih.gov/12663510/ DOI: 10.1093/carcin/24.3.497
Complete structured claim and evidence
Selenite increased TXNRD1 protein 2.1-fold and activity 4.8-fold without increasing its mRNA.
Selenite ion → Human TXNRD1 protein abundance source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/12663510.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "95f1de031ede41aa12f975dff28193dcb426465d4bda94bb84d4e60ef6c292b9", "start_char": 0, "end_char": 1535, "text_sha256": "95f1de031ede41aa12f975dff28193dcb426465d4bda94bb84d4e60ef6c292b9"}
experimental_model
Transcription/translation and inhibitor experiments
exposure
Sulforaphane, sodium selenite, combined treatment and pathway inhibitors
limitations
Cell-culture synergy at specified exposures is not a clinical supplement recommendation; TXNRD1 and TXNRD2 were not interchangeable.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human HepG2 hepatoma cells
plain_language
Selenium supported an increase at the protein-production level.
primary_references
[sulforaphane-p12663510] Synergy between sulforaphane and selenium in the induction of thioredoxin reductase 1 requires both transcriptional and translational modulation. (2003). https://pubmed.ncbi.nlm.nih.gov/12663510/ DOI: 10.1093/carcin/24.3.497
tissue_or_cell_type
Thioredoxin reductase regulation
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 710–721
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Transcription/translation and inhibitor experiments · source_derived_draft · unverified_draft
### sulforaphane-selenite-translation Selenite increased TXNRD1 protein 2.1-fold and activity 4.8-fold without increasing its mRNA. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Selenium supported an increase at the protein-production level. organism: Human HepG2 hepatoma cells tissue_or_cell_type: Thioredoxin reductase regulation experimental_model: Transcription/translation and inhibitor experiments limitations: Cell-culture synergy at specified exposures is not a clinical supplement recommendation; TXNRD1 and TXNRD2 were not interchangeable. exposure: Sulforaphane, sodium selenite, combined treatment and pathway inhibitors evidence_span: {"source_cache": "artifacts/sulforaphane-research/12663510.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "95f1de031ede41aa12f975dff28193dcb426465d4bda94bb84d4e60ef6c292b9", "start_char": 0, "end_char": 1535, "text_sha256": "95f1de031ede41aa12f975dff28193dcb426465d4bda94bb84d4e60ef6c292b9"} [sulforaphane-p12663510] Synergy between sulforaphane and selenium in the induction of thioredoxin reductase 1 requires both transcriptional and translational modulation. (2003). https://pubmed.ncbi.nlm.nih.gov/12663510/ DOI: 10.1093/carcin/24.3.497
Complete structured claim and evidence
Combined treatment increased TXNRD1 protein 5.5-fold, activity 13-fold and mRNA 6.5-fold in HepG2 cells.
Sulforaphane plus selenite, study-specific combination → Human TXNRD1 enzyme activity source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/12663510.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "95f1de031ede41aa12f975dff28193dcb426465d4bda94bb84d4e60ef6c292b9", "start_char": 0, "end_char": 1535, "text_sha256": "95f1de031ede41aa12f975dff28193dcb426465d4bda94bb84d4e60ef6c292b9"}
experimental_model
Transcription/translation and inhibitor experiments
exposure
Sulforaphane, sodium selenite, combined treatment and pathway inhibitors
limitations
Cell-culture synergy at specified exposures is not a clinical supplement recommendation; TXNRD1 and TXNRD2 were not interchangeable.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human HepG2 hepatoma cells
plain_language
Gene expression and enzyme production can combine to produce a larger response.
primary_references
[sulforaphane-p12663510] Synergy between sulforaphane and selenium in the induction of thioredoxin reductase 1 requires both transcriptional and translational modulation. (2003). https://pubmed.ncbi.nlm.nih.gov/12663510/ DOI: 10.1093/carcin/24.3.497
tissue_or_cell_type
Thioredoxin reductase regulation
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 736–747
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Transcription/translation and inhibitor experiments · source_derived_draft · unverified_draft
### sulforaphane-selenium-sfn-synergy Combined treatment increased TXNRD1 protein 5.5-fold, activity 13-fold and mRNA 6.5-fold in HepG2 cells. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Gene expression and enzyme production can combine to produce a larger response. organism: Human HepG2 hepatoma cells tissue_or_cell_type: Thioredoxin reductase regulation experimental_model: Transcription/translation and inhibitor experiments limitations: Cell-culture synergy at specified exposures is not a clinical supplement recommendation; TXNRD1 and TXNRD2 were not interchangeable. exposure: Sulforaphane, sodium selenite, combined treatment and pathway inhibitors evidence_span: {"source_cache": "artifacts/sulforaphane-research/12663510.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "95f1de031ede41aa12f975dff28193dcb426465d4bda94bb84d4e60ef6c292b9", "start_char": 0, "end_char": 1535, "text_sha256": "95f1de031ede41aa12f975dff28193dcb426465d4bda94bb84d4e60ef6c292b9"} [sulforaphane-p12663510] Synergy between sulforaphane and selenium in the induction of thioredoxin reductase 1 requires both transcriptional and translational modulation. (2003). https://pubmed.ncbi.nlm.nih.gov/12663510/ DOI: 10.1093/carcin/24.3.497
Complete structured claim and evidence
Neither oral dose consistently induced the measured Nrf2 target genes despite detectable plasma metabolites.
Sulforaphane / SFN, stereochemistry specified per study → Nrf2-target gene expression in COPD airway cells source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/27832073.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "cc345cf4434bd2d27451706ec614763c7be7562ac3e368f0e21b38c0f4d21003", "start_char": 0, "end_char": 1709, "text_sha256": "cc345cf4434bd2d27451706ec614763c7be7562ac3e368f0e21b38c0f4d21003"}
experimental_model
Randomized double-blind placebo-controlled phase 2 trial
exposure
25 or 150 micromol sulforaphane daily for four weeks
limitations
Absorption was documented; cell-based target engagement cannot be assumed after oral dosing in patients.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human, 89 COPD patients
plain_language
Reaching the bloodstream did not guarantee the intended lung-cell response.
primary_references
[sulforaphane-p27832073] Lack of Effect of Oral Sulforaphane Administration on Nrf2 Expression in COPD: A Randomized, Double-Blind, Placebo Controlled Trial. (2016). https://pubmed.ncbi.nlm.nih.gov/27832073/ DOI: 10.1371/journal.pone.0163716
tissue_or_cell_type
Alveolar macrophages, bronchial epithelium and pulmonary function
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1087–1098
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized double-blind placebo-controlled phase 2 trial · source_derived_draft · unverified_draft
### sulforaphane-copd-target-null Neither oral dose consistently induced the measured Nrf2 target genes despite detectable plasma metabolites. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Reaching the bloodstream did not guarantee the intended lung-cell response. organism: Human, 89 COPD patients tissue_or_cell_type: Alveolar macrophages, bronchial epithelium and pulmonary function experimental_model: Randomized double-blind placebo-controlled phase 2 trial limitations: Absorption was documented; cell-based target engagement cannot be assumed after oral dosing in patients. exposure: 25 or 150 micromol sulforaphane daily for four weeks evidence_span: {"source_cache": "artifacts/sulforaphane-research/27832073.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "cc345cf4434bd2d27451706ec614763c7be7562ac3e368f0e21b38c0f4d21003", "start_char": 0, "end_char": 1709, "text_sha256": "cc345cf4434bd2d27451706ec614763c7be7562ac3e368f0e21b38c0f4d21003"} [sulforaphane-p27832073] Lack of Effect of Oral Sulforaphane Administration on Nrf2 Expression in COPD: A Randomized, Double-Blind, Placebo Controlled Trial. (2016). https://pubmed.ncbi.nlm.nih.gov/27832073/ DOI: 10.1371/journal.pone.0163716
Complete structured claim and evidence
Heating to 60 degrees C before homogenization reduced ESP activity and nitrile formation while increasing sulforaphane yield.
Broccoli epithiospecifier protein / ESP → Sulforaphane / SFN, stereochemistry specified per study source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/15184012.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3a1b248b03fcfc77ee38ab6b4189c6c565b24f2071912565f0377ce00e8de0e6", "start_char": 0, "end_char": 1665, "text_sha256": "3a1b248b03fcfc77ee38ab6b4189c6c565b24f2071912565f0377ce00e8de0e6"}
experimental_model
Food processing and enzyme-activity experiments
exposure
Heating before homogenization, including 60 and at least 70 degrees C
limitations
Time, cultivar, food matrix and enzyme heat sensitivities matter; not a universal cooking prescription.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Broccoli florets and sprouts; mouse hepatoma bioassay
plain_language
Mild heating can suppress a competing route before destroying all useful enzyme activity.
primary_references
[sulforaphane-p15184012] Heating decreases epithiospecifier protein activity and increases sulforaphane formation in broccoli. (2004). https://pubmed.ncbi.nlm.nih.gov/15184012/ DOI: 10.1016/j.phytochem.2004.04.013
tissue_or_cell_type
Plant tissue hydrolysis
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 151–162
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Food processing and enzyme-activity experiments · source_derived_draft · unverified_draft
### sulforaphane-heat-esp Heating to 60 degrees C before homogenization reduced ESP activity and nitrile formation while increasing sulforaphane yield. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Mild heating can suppress a competing route before destroying all useful enzyme activity. organism: Broccoli florets and sprouts; mouse hepatoma bioassay tissue_or_cell_type: Plant tissue hydrolysis experimental_model: Food processing and enzyme-activity experiments limitations: Time, cultivar, food matrix and enzyme heat sensitivities matter; not a universal cooking prescription. exposure: Heating before homogenization, including 60 and at least 70 degrees C evidence_span: {"source_cache": "artifacts/sulforaphane-research/15184012.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3a1b248b03fcfc77ee38ab6b4189c6c565b24f2071912565f0377ce00e8de0e6", "start_char": 0, "end_char": 1665, "text_sha256": "3a1b248b03fcfc77ee38ab6b4189c6c565b24f2071912565f0377ce00e8de0e6"} [sulforaphane-p15184012] Heating decreases epithiospecifier protein activity and increases sulforaphane formation in broccoli. (2004). https://pubmed.ncbi.nlm.nih.gov/15184012/ DOI: 10.1016/j.phytochem.2004.04.013
Complete structured claim and evidence
Heating broccoli florets to 70 degrees C or above decreased formation of both measured products; the same reduction did not occur in sprouts.
Glucoraphanin → Sulforaphane / SFN, stereochemistry specified per study source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/sulforaphane-research/15184012.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3a1b248b03fcfc77ee38ab6b4189c6c565b24f2071912565f0377ce00e8de0e6", "start_char": 0, "end_char": 1665, "text_sha256": "3a1b248b03fcfc77ee38ab6b4189c6c565b24f2071912565f0377ce00e8de0e6"}
experimental_model
Food processing and enzyme-activity experiments
exposure
Heating before homogenization, including 60 and at least 70 degrees C
limitations
Time, cultivar, food matrix and enzyme heat sensitivities matter; not a universal cooking prescription.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Broccoli florets and sprouts; mouse hepatoma bioassay
plain_language
The response to heat depended on which plant material was tested.
primary_references
[sulforaphane-p15184012] Heating decreases epithiospecifier protein activity and increases sulforaphane formation in broccoli. (2004). https://pubmed.ncbi.nlm.nih.gov/15184012/ DOI: 10.1016/j.phytochem.2004.04.013
tissue_or_cell_type
Plant tissue hydrolysis
trigger_kind
machinery_impairment Imported condition classification; unverified.
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 164–175
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Food processing and enzyme-activity experiments · source_derived_draft · unverified_draft
### sulforaphane-hotter-processing Heating broccoli florets to 70 degrees C or above decreased formation of both measured products; the same reduction did not occur in sprouts. Condition category: machinery_impairment nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The response to heat depended on which plant material was tested. organism: Broccoli florets and sprouts; mouse hepatoma bioassay tissue_or_cell_type: Plant tissue hydrolysis experimental_model: Food processing and enzyme-activity experiments limitations: Time, cultivar, food matrix and enzyme heat sensitivities matter; not a universal cooking prescription. exposure: Heating before homogenization, including 60 and at least 70 degrees C evidence_span: {"source_cache": "artifacts/sulforaphane-research/15184012.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3a1b248b03fcfc77ee38ab6b4189c6c565b24f2071912565f0377ce00e8de0e6", "start_char": 0, "end_char": 1665, "text_sha256": "3a1b248b03fcfc77ee38ab6b4189c6c565b24f2071912565f0377ce00e8de0e6"} [sulforaphane-p15184012] Heating decreases epithiospecifier protein activity and increases sulforaphane formation in broccoli. (2004). https://pubmed.ncbi.nlm.nih.gov/15184012/ DOI: 10.1016/j.phytochem.2004.04.013
Complete structured claim and evidence
In vitro isothiocyanate formation required BT2158 together with either BT2156 or BT2157.
Bacteroides thetaiotaomicron BT2158 → Glucosinolate-to-isothiocyanate conversion by B. thetaiotaomicron enzymes source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/32084341.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "08eaa102da24fdee1f16fa9376338c557ba4f3919adb1122f3e13d509a171293", "start_char": 0, "end_char": 1031, "text_sha256": "08eaa102da24fdee1f16fa9376338c557ba4f3919adb1122f3e13d509a171293"}
experimental_model
Bacterial genetics, purified-enzyme reconstitution and gnotobiotic mice
exposure
BT2159-BT2156 transfer; individual enzyme combinations and BT2157 mutant
limitations
Microbial enzymes are distinct from plant myrosinase; general glucosinolate experiments do not prove every substrate follows identical kinetics.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
B. thetaiotaomicron, engineered B. fragilis and monoassociated mice
plain_language
The bacterial route uses cooperating proteins.
primary_references
[sulforaphane-p32084341] A Metabolic Pathway for Activation of Dietary Glucosinolates by a Human Gut Symbiont. (2020). https://pubmed.ncbi.nlm.nih.gov/32084341/ DOI: 10.1016/j.cell.2020.01.023
tissue_or_cell_type
Microbial glucosinolate activation
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 203–214
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Bacterial genetics, purified-enzyme reconstitution and gnotobiotic mice · source_derived_draft · unverified_draft
### sulforaphane-bt2158 In vitro isothiocyanate formation required BT2158 together with either BT2156 or BT2157. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The bacterial route uses cooperating proteins. organism: B. thetaiotaomicron, engineered B. fragilis and monoassociated mice tissue_or_cell_type: Microbial glucosinolate activation experimental_model: Bacterial genetics, purified-enzyme reconstitution and gnotobiotic mice limitations: Microbial enzymes are distinct from plant myrosinase; general glucosinolate experiments do not prove every substrate follows identical kinetics. exposure: BT2159-BT2156 transfer; individual enzyme combinations and BT2157 mutant evidence_span: {"source_cache": "artifacts/sulforaphane-research/32084341.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "08eaa102da24fdee1f16fa9376338c557ba4f3919adb1122f3e13d509a171293", "start_char": 0, "end_char": 1031, "text_sha256": "08eaa102da24fdee1f16fa9376338c557ba4f3919adb1122f3e13d509a171293"} [sulforaphane-p32084341] A Metabolic Pathway for Activation of Dietary Glucosinolates by a Human Gut Symbiont. (2020). https://pubmed.ncbi.nlm.nih.gov/32084341/ DOI: 10.1016/j.cell.2020.01.023
Complete structured claim and evidence
BT2156 supported glucosinolate activation when combined with BT2158 in the biochemical reconstitution.
Bacteroides thetaiotaomicron BT2156 → Glucosinolate-to-isothiocyanate conversion by B. thetaiotaomicron enzymes source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/32084341.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "08eaa102da24fdee1f16fa9376338c557ba4f3919adb1122f3e13d509a171293", "start_char": 0, "end_char": 1031, "text_sha256": "08eaa102da24fdee1f16fa9376338c557ba4f3919adb1122f3e13d509a171293"}
experimental_model
Bacterial genetics, purified-enzyme reconstitution and gnotobiotic mice
exposure
BT2159-BT2156 transfer; individual enzyme combinations and BT2157 mutant
limitations
Microbial enzymes are distinct from plant myrosinase; general glucosinolate experiments do not prove every substrate follows identical kinetics.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
B. thetaiotaomicron, engineered B. fragilis and monoassociated mice
plain_language
One partner can support this conversion.
primary_references
[sulforaphane-p32084341] A Metabolic Pathway for Activation of Dietary Glucosinolates by a Human Gut Symbiont. (2020). https://pubmed.ncbi.nlm.nih.gov/32084341/ DOI: 10.1016/j.cell.2020.01.023
tissue_or_cell_type
Microbial glucosinolate activation
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 216–227
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Bacterial genetics, purified-enzyme reconstitution and gnotobiotic mice · source_derived_draft · unverified_draft
### sulforaphane-bt2156 BT2156 supported glucosinolate activation when combined with BT2158 in the biochemical reconstitution. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: One partner can support this conversion. organism: B. thetaiotaomicron, engineered B. fragilis and monoassociated mice tissue_or_cell_type: Microbial glucosinolate activation experimental_model: Bacterial genetics, purified-enzyme reconstitution and gnotobiotic mice limitations: Microbial enzymes are distinct from plant myrosinase; general glucosinolate experiments do not prove every substrate follows identical kinetics. exposure: BT2159-BT2156 transfer; individual enzyme combinations and BT2157 mutant evidence_span: {"source_cache": "artifacts/sulforaphane-research/32084341.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "08eaa102da24fdee1f16fa9376338c557ba4f3919adb1122f3e13d509a171293", "start_char": 0, "end_char": 1031, "text_sha256": "08eaa102da24fdee1f16fa9376338c557ba4f3919adb1122f3e13d509a171293"} [sulforaphane-p32084341] A Metabolic Pathway for Activation of Dietary Glucosinolates by a Human Gut Symbiont. (2020). https://pubmed.ncbi.nlm.nih.gov/32084341/ DOI: 10.1016/j.cell.2020.01.023
Complete structured claim and evidence
BT2157 supported glucosinolate activation when combined with BT2158 in vitro.
Bacteroides thetaiotaomicron BT2157 → Glucosinolate-to-isothiocyanate conversion by B. thetaiotaomicron enzymes source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/32084341.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "08eaa102da24fdee1f16fa9376338c557ba4f3919adb1122f3e13d509a171293", "start_char": 0, "end_char": 1031, "text_sha256": "08eaa102da24fdee1f16fa9376338c557ba4f3919adb1122f3e13d509a171293"}
experimental_model
Bacterial genetics, purified-enzyme reconstitution and gnotobiotic mice
exposure
BT2159-BT2156 transfer; individual enzyme combinations and BT2157 mutant
limitations
Microbial enzymes are distinct from plant myrosinase; general glucosinolate experiments do not prove every substrate follows identical kinetics.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
B. thetaiotaomicron, engineered B. fragilis and monoassociated mice
plain_language
An alternative partner was active in the enzyme assay.
primary_references
[sulforaphane-p32084341] A Metabolic Pathway for Activation of Dietary Glucosinolates by a Human Gut Symbiont. (2020). https://pubmed.ncbi.nlm.nih.gov/32084341/ DOI: 10.1016/j.cell.2020.01.023
tissue_or_cell_type
Microbial glucosinolate activation
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 229–240
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Bacterial genetics, purified-enzyme reconstitution and gnotobiotic mice · source_derived_draft · unverified_draft
### sulforaphane-bt2157 BT2157 supported glucosinolate activation when combined with BT2158 in vitro. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: An alternative partner was active in the enzyme assay. organism: B. thetaiotaomicron, engineered B. fragilis and monoassociated mice tissue_or_cell_type: Microbial glucosinolate activation experimental_model: Bacterial genetics, purified-enzyme reconstitution and gnotobiotic mice limitations: Microbial enzymes are distinct from plant myrosinase; general glucosinolate experiments do not prove every substrate follows identical kinetics. exposure: BT2159-BT2156 transfer; individual enzyme combinations and BT2157 mutant evidence_span: {"source_cache": "artifacts/sulforaphane-research/32084341.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "08eaa102da24fdee1f16fa9376338c557ba4f3919adb1122f3e13d509a171293", "start_char": 0, "end_char": 1031, "text_sha256": "08eaa102da24fdee1f16fa9376338c557ba4f3919adb1122f3e13d509a171293"} [sulforaphane-p32084341] A Metabolic Pathway for Activation of Dietary Glucosinolates by a Human Gut Symbiont. (2020). https://pubmed.ncbi.nlm.nih.gov/32084341/ DOI: 10.1016/j.cell.2020.01.023
Complete structured claim and evidence
Mice monoassociated with the BT2157-mutant strain had lower gastrointestinal isothiocyanate production.
B. thetaiotaomicron BT2157 loss in a monoassociated mouse experiment → Glucosinolate-to-isothiocyanate conversion by B. thetaiotaomicron enzymes source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/sulforaphane-research/32084341.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "08eaa102da24fdee1f16fa9376338c557ba4f3919adb1122f3e13d509a171293", "start_char": 0, "end_char": 1031, "text_sha256": "08eaa102da24fdee1f16fa9376338c557ba4f3919adb1122f3e13d509a171293"}
experimental_model
Bacterial genetics, purified-enzyme reconstitution and gnotobiotic mice
exposure
BT2159-BT2156 transfer; individual enzyme combinations and BT2157 mutant
limitations
Microbial enzymes are distinct from plant myrosinase; general glucosinolate experiments do not prove every substrate follows identical kinetics.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
B. thetaiotaomicron, engineered B. fragilis and monoassociated mice
plain_language
Losing microbial conversion capacity can reduce activation of the precursor.
primary_references
[sulforaphane-p32084341] A Metabolic Pathway for Activation of Dietary Glucosinolates by a Human Gut Symbiont. (2020). https://pubmed.ncbi.nlm.nih.gov/32084341/ DOI: 10.1016/j.cell.2020.01.023
tissue_or_cell_type
Microbial glucosinolate activation
trigger_kind
machinery_impairment Imported condition classification; unverified.
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 242–253
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Bacterial genetics, purified-enzyme reconstitution and gnotobiotic mice · source_derived_draft · unverified_draft
### sulforaphane-microbial-loss Mice monoassociated with the BT2157-mutant strain had lower gastrointestinal isothiocyanate production. Condition category: machinery_impairment nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Losing microbial conversion capacity can reduce activation of the precursor. organism: B. thetaiotaomicron, engineered B. fragilis and monoassociated mice tissue_or_cell_type: Microbial glucosinolate activation experimental_model: Bacterial genetics, purified-enzyme reconstitution and gnotobiotic mice limitations: Microbial enzymes are distinct from plant myrosinase; general glucosinolate experiments do not prove every substrate follows identical kinetics. exposure: BT2159-BT2156 transfer; individual enzyme combinations and BT2157 mutant evidence_span: {"source_cache": "artifacts/sulforaphane-research/32084341.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "08eaa102da24fdee1f16fa9376338c557ba4f3919adb1122f3e13d509a171293", "start_char": 0, "end_char": 1031, "text_sha256": "08eaa102da24fdee1f16fa9376338c557ba4f3919adb1122f3e13d509a171293"} [sulforaphane-p32084341] A Metabolic Pathway for Activation of Dietary Glucosinolates by a Human Gut Symbiont. (2020). https://pubmed.ncbi.nlm.nih.gov/32084341/ DOI: 10.1016/j.cell.2020.01.023
Complete structured claim and evidence
GSTM1-1 was among the efficient tested human GST catalysts for isothiocyanate conjugation.
Human glutathione S-transferase M1 → Sulforaphane-glutathione conjugate / SFN-GSH source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/7826396.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5dee3c3a8c8069c33fac2653f16f3521cdd17ef5e8ebddd0f82cfa3a5c95c0fe", "start_char": 0, "end_char": 989, "text_sha256": "5dee3c3a8c8069c33fac2653f16f3521cdd17ef5e8ebddd0f82cfa3a5c95c0fe"}
experimental_model
Recombinant human GST conjugation and reverse-reaction kinetics
exposure
Four isothiocyanates and GSTP1-1, GSTM1-1, GSTA1-1 and GSTM2-2
limitations
Relative enzyme rates are not whole-person clearance predictions; reverse reactions were slower and inhibited by high GSH.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human GST isoenzymes
plain_language
Different GST isoenzymes can participate in this route.
primary_references
[sulforaphane-p7826396] Reversible conjugation of isothiocyanates with glutathione catalyzed by human glutathione transferases. (1995). https://pubmed.ncbi.nlm.nih.gov/7826396/ DOI: 10.1006/bbrc.1995.1106
tissue_or_cell_type
Isothiocyanate-glutathione chemistry
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 268–279
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human GST conjugation and reverse-reaction kinetics · source_derived_draft · unverified_draft
### sulforaphane-gstm-conjugation GSTM1-1 was among the efficient tested human GST catalysts for isothiocyanate conjugation. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Different GST isoenzymes can participate in this route. organism: Human GST isoenzymes tissue_or_cell_type: Isothiocyanate-glutathione chemistry experimental_model: Recombinant human GST conjugation and reverse-reaction kinetics limitations: Relative enzyme rates are not whole-person clearance predictions; reverse reactions were slower and inhibited by high GSH. exposure: Four isothiocyanates and GSTP1-1, GSTM1-1, GSTA1-1 and GSTM2-2 evidence_span: {"source_cache": "artifacts/sulforaphane-research/7826396.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5dee3c3a8c8069c33fac2653f16f3521cdd17ef5e8ebddd0f82cfa3a5c95c0fe", "start_char": 0, "end_char": 989, "text_sha256": "5dee3c3a8c8069c33fac2653f16f3521cdd17ef5e8ebddd0f82cfa3a5c95c0fe"} [sulforaphane-p7826396] Reversible conjugation of isothiocyanates with glutathione catalyzed by human glutathione transferases. (1995). https://pubmed.ncbi.nlm.nih.gov/7826396/ DOI: 10.1006/bbrc.1995.1106
Complete structured claim and evidence
Sulforaphane underwent both nonenzymatic and GST-catalyzed conjugation with glutathione.
GSH → Sulforaphane / SFN, stereochemistry specified per study source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/7826396.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5dee3c3a8c8069c33fac2653f16f3521cdd17ef5e8ebddd0f82cfa3a5c95c0fe", "start_char": 0, "end_char": 989, "text_sha256": "5dee3c3a8c8069c33fac2653f16f3521cdd17ef5e8ebddd0f82cfa3a5c95c0fe"}
experimental_model
Recombinant human GST conjugation and reverse-reaction kinetics
exposure
Four isothiocyanates and GSTP1-1, GSTM1-1, GSTA1-1 and GSTM2-2
limitations
Relative enzyme rates are not whole-person clearance predictions; reverse reactions were slower and inhibited by high GSH.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human GST isoenzymes
plain_language
Glutathione is a reacting molecule here, not merely an antioxidant label.
primary_references
[sulforaphane-p7826396] Reversible conjugation of isothiocyanates with glutathione catalyzed by human glutathione transferases. (1995). https://pubmed.ncbi.nlm.nih.gov/7826396/ DOI: 10.1006/bbrc.1995.1106
tissue_or_cell_type
Isothiocyanate-glutathione chemistry
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 281–292
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human GST conjugation and reverse-reaction kinetics · source_derived_draft · unverified_draft
### sulforaphane-gsh-conjugation Sulforaphane underwent both nonenzymatic and GST-catalyzed conjugation with glutathione. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Glutathione is a reacting molecule here, not merely an antioxidant label. organism: Human GST isoenzymes tissue_or_cell_type: Isothiocyanate-glutathione chemistry experimental_model: Recombinant human GST conjugation and reverse-reaction kinetics limitations: Relative enzyme rates are not whole-person clearance predictions; reverse reactions were slower and inhibited by high GSH. exposure: Four isothiocyanates and GSTP1-1, GSTM1-1, GSTA1-1 and GSTM2-2 evidence_span: {"source_cache": "artifacts/sulforaphane-research/7826396.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5dee3c3a8c8069c33fac2653f16f3521cdd17ef5e8ebddd0f82cfa3a5c95c0fe", "start_char": 0, "end_char": 989, "text_sha256": "5dee3c3a8c8069c33fac2653f16f3521cdd17ef5e8ebddd0f82cfa3a5c95c0fe"} [sulforaphane-p7826396] Reversible conjugation of isothiocyanates with glutathione catalyzed by human glutathione transferases. (1995). https://pubmed.ncbi.nlm.nih.gov/7826396/ DOI: 10.1006/bbrc.1995.1106
Complete structured claim and evidence
GSTs also catalyzed reverse cleavage of isothiocyanate-GSH conjugates; those reactions were slow and inhibited by high GSH.
Sulforaphane-glutathione conjugate / SFN-GSH → Sulforaphane / SFN, stereochemistry specified per study source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/7826396.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5dee3c3a8c8069c33fac2653f16f3521cdd17ef5e8ebddd0f82cfa3a5c95c0fe", "start_char": 0, "end_char": 989, "text_sha256": "5dee3c3a8c8069c33fac2653f16f3521cdd17ef5e8ebddd0f82cfa3a5c95c0fe"}
experimental_model
Recombinant human GST conjugation and reverse-reaction kinetics
exposure
Four isothiocyanates and GSTP1-1, GSTM1-1, GSTA1-1 and GSTM2-2
limitations
Relative enzyme rates are not whole-person clearance predictions; reverse reactions were slower and inhibited by high GSH.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human GST isoenzymes
plain_language
Conjugation is reversible, so bound and free exposure are related but different.
primary_references
[sulforaphane-p7826396] Reversible conjugation of isothiocyanates with glutathione catalyzed by human glutathione transferases. (1995). https://pubmed.ncbi.nlm.nih.gov/7826396/ DOI: 10.1006/bbrc.1995.1106
tissue_or_cell_type
Isothiocyanate-glutathione chemistry
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 294–305
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human GST conjugation and reverse-reaction kinetics · source_derived_draft · unverified_draft
### sulforaphane-reverse-conjugation GSTs also catalyzed reverse cleavage of isothiocyanate-GSH conjugates; those reactions were slow and inhibited by high GSH. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Conjugation is reversible, so bound and free exposure are related but different. organism: Human GST isoenzymes tissue_or_cell_type: Isothiocyanate-glutathione chemistry experimental_model: Recombinant human GST conjugation and reverse-reaction kinetics limitations: Relative enzyme rates are not whole-person clearance predictions; reverse reactions were slower and inhibited by high GSH. exposure: Four isothiocyanates and GSTP1-1, GSTM1-1, GSTA1-1 and GSTM2-2 evidence_span: {"source_cache": "artifacts/sulforaphane-research/7826396.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5dee3c3a8c8069c33fac2653f16f3521cdd17ef5e8ebddd0f82cfa3a5c95c0fe", "start_char": 0, "end_char": 989, "text_sha256": "5dee3c3a8c8069c33fac2653f16f3521cdd17ef5e8ebddd0f82cfa3a5c95c0fe"} [sulforaphane-p7826396] Reversible conjugation of isothiocyanates with glutathione catalyzed by human glutathione transferases. (1995). https://pubmed.ncbi.nlm.nih.gov/7826396/ DOI: 10.1006/bbrc.1995.1106
Complete structured claim and evidence
MRP1-overexpressing human cells supported rapid export of accumulated sulforaphane, mainly as its glutathione conjugate.
Human multidrug resistance-associated protein 1 / ABCC1 / MRP1 → Sulforaphane/glutathione-conjugate efflux source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/11988104.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5759bc0af52a1e906602549a3920ebba5641d09b63cc87f0dc61ea8efcb724a9", "start_char": 0, "end_char": 1567, "text_sha256": "5759bc0af52a1e906602549a3920ebba5641d09b63cc87f0dc61ea8efcb724a9"}
experimental_model
Transporter-overexpression and temperature/inhibitor experiments
exposure
Sulforaphane loading; ABCC1 or ABCB1 expression
limitations
Cancer-cell transport experiments; not a measured clinical drug interaction.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human HL60 leukemia and 8226 myeloma cells
plain_language
A transporter can shorten intracellular exposure.
primary_references
[sulforaphane-p11988104] High cellular accumulation of sulphoraphane, a dietary anticarcinogen, is followed by rapid transporter-mediated export as a glutathione conjugate. (2002). https://pubmed.ncbi.nlm.nih.gov/11988104/ DOI: 10.1042/bj3640301
tissue_or_cell_type
Intracellular retention and export
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 307–318
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Transporter-overexpression and temperature/inhibitor experiments · source_derived_draft · unverified_draft
### sulforaphane-abcc1-efflux MRP1-overexpressing human cells supported rapid export of accumulated sulforaphane, mainly as its glutathione conjugate. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: A transporter can shorten intracellular exposure. organism: Human HL60 leukemia and 8226 myeloma cells tissue_or_cell_type: Intracellular retention and export experimental_model: Transporter-overexpression and temperature/inhibitor experiments limitations: Cancer-cell transport experiments; not a measured clinical drug interaction. exposure: Sulforaphane loading; ABCC1 or ABCB1 expression evidence_span: {"source_cache": "artifacts/sulforaphane-research/11988104.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5759bc0af52a1e906602549a3920ebba5641d09b63cc87f0dc61ea8efcb724a9", "start_char": 0, "end_char": 1567, "text_sha256": "5759bc0af52a1e906602549a3920ebba5641d09b63cc87f0dc61ea8efcb724a9"} [sulforaphane-p11988104] High cellular accumulation of sulphoraphane, a dietary anticarcinogen, is followed by rapid transporter-mediated export as a glutathione conjugate. (2002). https://pubmed.ncbi.nlm.nih.gov/11988104/ DOI: 10.1042/bj3640301
Complete structured claim and evidence
P-glycoprotein overexpression also implicated ABCB1 in export of intracellular sulforaphane/conjugate pools.
Human P-glycoprotein / ABCB1 / MDR1 → Sulforaphane/glutathione-conjugate efflux source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/11988104.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5759bc0af52a1e906602549a3920ebba5641d09b63cc87f0dc61ea8efcb724a9", "start_char": 0, "end_char": 1567, "text_sha256": "5759bc0af52a1e906602549a3920ebba5641d09b63cc87f0dc61ea8efcb724a9"}
experimental_model
Transporter-overexpression and temperature/inhibitor experiments
exposure
Sulforaphane loading; ABCC1 or ABCB1 expression
limitations
Cancer-cell transport experiments; not a measured clinical drug interaction.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human HL60 leukemia and 8226 myeloma cells
plain_language
The measured pool can be influenced by more than one transporter.
primary_references
[sulforaphane-p11988104] High cellular accumulation of sulphoraphane, a dietary anticarcinogen, is followed by rapid transporter-mediated export as a glutathione conjugate. (2002). https://pubmed.ncbi.nlm.nih.gov/11988104/ DOI: 10.1042/bj3640301
tissue_or_cell_type
Intracellular retention and export
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 320–331
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Transporter-overexpression and temperature/inhibitor experiments · source_derived_draft · unverified_draft
### sulforaphane-abcb1-efflux P-glycoprotein overexpression also implicated ABCB1 in export of intracellular sulforaphane/conjugate pools. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The measured pool can be influenced by more than one transporter. organism: Human HL60 leukemia and 8226 myeloma cells tissue_or_cell_type: Intracellular retention and export experimental_model: Transporter-overexpression and temperature/inhibitor experiments limitations: Cancer-cell transport experiments; not a measured clinical drug interaction. exposure: Sulforaphane loading; ABCC1 or ABCB1 expression evidence_span: {"source_cache": "artifacts/sulforaphane-research/11988104.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5759bc0af52a1e906602549a3920ebba5641d09b63cc87f0dc61ea8efcb724a9", "start_char": 0, "end_char": 1567, "text_sha256": "5759bc0af52a1e906602549a3920ebba5641d09b63cc87f0dc61ea8efcb724a9"} [sulforaphane-p11988104] High cellular accumulation of sulphoraphane, a dietary anticarcinogen, is followed by rapid transporter-mediated export as a glutathione conjugate. (2002). https://pubmed.ncbi.nlm.nih.gov/11988104/ DOI: 10.1042/bj3640301
Complete structured claim and evidence
Sulforaphane-glutathione was separately quantified in human urine after broccoli sprout exposure.
Sulforaphane / SFN, stereochemistry specified per study → Sulforaphane-glutathione conjugate / SFN-GSH source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/18729326.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1b30293ede979c158852939b48f68a2cd71fa605bbca813a9fe2325f99e5c1d3", "start_char": 0, "end_char": 2172, "text_sha256": "1b30293ede979c158852939b48f68a2cd71fa605bbca813a9fe2325f99e5c1d3"}
experimental_model
Isotope-dilution LC-MS/MS assay validation in intervention urines
exposure
Broccoli sprout intervention specimens with equivalent administered preparation
limitations
Analytical exposure study; metabolite concentration is not tissue efficacy and does not identify each responsible human enzyme.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human, 98 urine specimens
plain_language
This metabolite has its own identity and can be measured separately from the parent.
primary_references
[sulforaphane-p18729326] Quantification of sulforaphane mercapturic acid pathway conjugates in human urine by high-performance liquid chromatography and isotope-dilution tandem mass spectrometry. (2008). https://pubmed.ncbi.nlm.nih.gov/18729326/ DOI: 10.1021/tx800210k
tissue_or_cell_type
Urinary mercapturic-acid pathway species
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 333–344
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Isotope-dilution LC-MS/MS assay validation in intervention urines · source_derived_draft · unverified_draft
### sulforaphane-urine-gsh Sulforaphane-glutathione was separately quantified in human urine after broccoli sprout exposure. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: This metabolite has its own identity and can be measured separately from the parent. organism: Human, 98 urine specimens tissue_or_cell_type: Urinary mercapturic-acid pathway species experimental_model: Isotope-dilution LC-MS/MS assay validation in intervention urines limitations: Analytical exposure study; metabolite concentration is not tissue efficacy and does not identify each responsible human enzyme. exposure: Broccoli sprout intervention specimens with equivalent administered preparation evidence_span: {"source_cache": "artifacts/sulforaphane-research/18729326.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1b30293ede979c158852939b48f68a2cd71fa605bbca813a9fe2325f99e5c1d3", "start_char": 0, "end_char": 2172, "text_sha256": "1b30293ede979c158852939b48f68a2cd71fa605bbca813a9fe2325f99e5c1d3"} [sulforaphane-p18729326] Quantification of sulforaphane mercapturic acid pathway conjugates in human urine by high-performance liquid chromatography and isotope-dilution tandem mass spectrometry. (2008). https://pubmed.ncbi.nlm.nih.gov/18729326/ DOI: 10.1021/tx800210k
Complete structured claim and evidence
Sulforaphane-cysteinylglycine was separately quantified in human urine after broccoli sprout exposure.
Sulforaphane / SFN, stereochemistry specified per study → Sulforaphane-cysteinylglycine conjugate source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/18729326.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1b30293ede979c158852939b48f68a2cd71fa605bbca813a9fe2325f99e5c1d3", "start_char": 0, "end_char": 2172, "text_sha256": "1b30293ede979c158852939b48f68a2cd71fa605bbca813a9fe2325f99e5c1d3"}
experimental_model
Isotope-dilution LC-MS/MS assay validation in intervention urines
exposure
Broccoli sprout intervention specimens with equivalent administered preparation
limitations
Analytical exposure study; metabolite concentration is not tissue efficacy and does not identify each responsible human enzyme.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human, 98 urine specimens
plain_language
This metabolite has its own identity and can be measured separately from the parent.
primary_references
[sulforaphane-p18729326] Quantification of sulforaphane mercapturic acid pathway conjugates in human urine by high-performance liquid chromatography and isotope-dilution tandem mass spectrometry. (2008). https://pubmed.ncbi.nlm.nih.gov/18729326/ DOI: 10.1021/tx800210k
tissue_or_cell_type
Urinary mercapturic-acid pathway species
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 346–357
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Isotope-dilution LC-MS/MS assay validation in intervention urines · source_derived_draft · unverified_draft
### sulforaphane-urine-cysgly Sulforaphane-cysteinylglycine was separately quantified in human urine after broccoli sprout exposure. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: This metabolite has its own identity and can be measured separately from the parent. organism: Human, 98 urine specimens tissue_or_cell_type: Urinary mercapturic-acid pathway species experimental_model: Isotope-dilution LC-MS/MS assay validation in intervention urines limitations: Analytical exposure study; metabolite concentration is not tissue efficacy and does not identify each responsible human enzyme. exposure: Broccoli sprout intervention specimens with equivalent administered preparation evidence_span: {"source_cache": "artifacts/sulforaphane-research/18729326.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1b30293ede979c158852939b48f68a2cd71fa605bbca813a9fe2325f99e5c1d3", "start_char": 0, "end_char": 2172, "text_sha256": "1b30293ede979c158852939b48f68a2cd71fa605bbca813a9fe2325f99e5c1d3"} [sulforaphane-p18729326] Quantification of sulforaphane mercapturic acid pathway conjugates in human urine by high-performance liquid chromatography and isotope-dilution tandem mass spectrometry. (2008). https://pubmed.ncbi.nlm.nih.gov/18729326/ DOI: 10.1021/tx800210k
Complete structured claim and evidence
Sulforaphane-cysteine was separately quantified in human urine after broccoli sprout exposure.
Sulforaphane / SFN, stereochemistry specified per study → Sulforaphane-cysteine conjugate / SFN-Cys source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/18729326.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1b30293ede979c158852939b48f68a2cd71fa605bbca813a9fe2325f99e5c1d3", "start_char": 0, "end_char": 2172, "text_sha256": "1b30293ede979c158852939b48f68a2cd71fa605bbca813a9fe2325f99e5c1d3"}
experimental_model
Isotope-dilution LC-MS/MS assay validation in intervention urines
exposure
Broccoli sprout intervention specimens with equivalent administered preparation
limitations
Analytical exposure study; metabolite concentration is not tissue efficacy and does not identify each responsible human enzyme.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human, 98 urine specimens
plain_language
This metabolite has its own identity and can be measured separately from the parent.
primary_references
[sulforaphane-p18729326] Quantification of sulforaphane mercapturic acid pathway conjugates in human urine by high-performance liquid chromatography and isotope-dilution tandem mass spectrometry. (2008). https://pubmed.ncbi.nlm.nih.gov/18729326/ DOI: 10.1021/tx800210k
tissue_or_cell_type
Urinary mercapturic-acid pathway species
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 359–370
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Isotope-dilution LC-MS/MS assay validation in intervention urines · source_derived_draft · unverified_draft
### sulforaphane-urine-cys Sulforaphane-cysteine was separately quantified in human urine after broccoli sprout exposure. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: This metabolite has its own identity and can be measured separately from the parent. organism: Human, 98 urine specimens tissue_or_cell_type: Urinary mercapturic-acid pathway species experimental_model: Isotope-dilution LC-MS/MS assay validation in intervention urines limitations: Analytical exposure study; metabolite concentration is not tissue efficacy and does not identify each responsible human enzyme. exposure: Broccoli sprout intervention specimens with equivalent administered preparation evidence_span: {"source_cache": "artifacts/sulforaphane-research/18729326.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1b30293ede979c158852939b48f68a2cd71fa605bbca813a9fe2325f99e5c1d3", "start_char": 0, "end_char": 2172, "text_sha256": "1b30293ede979c158852939b48f68a2cd71fa605bbca813a9fe2325f99e5c1d3"} [sulforaphane-p18729326] Quantification of sulforaphane mercapturic acid pathway conjugates in human urine by high-performance liquid chromatography and isotope-dilution tandem mass spectrometry. (2008). https://pubmed.ncbi.nlm.nih.gov/18729326/ DOI: 10.1021/tx800210k
Complete structured claim and evidence
Sulforaphane-N-acetylcysteine was separately quantified in human urine after broccoli sprout exposure.
Sulforaphane / SFN, stereochemistry specified per study → Sulforaphane-N-acetylcysteine conjugate / SFN-NAC source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/18729326.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1b30293ede979c158852939b48f68a2cd71fa605bbca813a9fe2325f99e5c1d3", "start_char": 0, "end_char": 2172, "text_sha256": "1b30293ede979c158852939b48f68a2cd71fa605bbca813a9fe2325f99e5c1d3"}
experimental_model
Isotope-dilution LC-MS/MS assay validation in intervention urines
exposure
Broccoli sprout intervention specimens with equivalent administered preparation
limitations
Analytical exposure study; metabolite concentration is not tissue efficacy and does not identify each responsible human enzyme.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human, 98 urine specimens
plain_language
This metabolite has its own identity and can be measured separately from the parent.
primary_references
[sulforaphane-p18729326] Quantification of sulforaphane mercapturic acid pathway conjugates in human urine by high-performance liquid chromatography and isotope-dilution tandem mass spectrometry. (2008). https://pubmed.ncbi.nlm.nih.gov/18729326/ DOI: 10.1021/tx800210k
tissue_or_cell_type
Urinary mercapturic-acid pathway species
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 372–383
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Isotope-dilution LC-MS/MS assay validation in intervention urines · source_derived_draft · unverified_draft
### sulforaphane-urine-nac Sulforaphane-N-acetylcysteine was separately quantified in human urine after broccoli sprout exposure. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: This metabolite has its own identity and can be measured separately from the parent. organism: Human, 98 urine specimens tissue_or_cell_type: Urinary mercapturic-acid pathway species experimental_model: Isotope-dilution LC-MS/MS assay validation in intervention urines limitations: Analytical exposure study; metabolite concentration is not tissue efficacy and does not identify each responsible human enzyme. exposure: Broccoli sprout intervention specimens with equivalent administered preparation evidence_span: {"source_cache": "artifacts/sulforaphane-research/18729326.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1b30293ede979c158852939b48f68a2cd71fa605bbca813a9fe2325f99e5c1d3", "start_char": 0, "end_char": 2172, "text_sha256": "1b30293ede979c158852939b48f68a2cd71fa605bbca813a9fe2325f99e5c1d3"} [sulforaphane-p18729326] Quantification of sulforaphane mercapturic acid pathway conjugates in human urine by high-performance liquid chromatography and isotope-dilution tandem mass spectrometry. (2008). https://pubmed.ncbi.nlm.nih.gov/18729326/ DOI: 10.1021/tx800210k
Complete structured claim and evidence
Interindividual precursor conversion varied over 100-fold in the studied intervention samples despite equivalent administered preparation.
Glucoraphanin → Sulforaphane / SFN, stereochemistry specified per study source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/18729326.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1b30293ede979c158852939b48f68a2cd71fa605bbca813a9fe2325f99e5c1d3", "start_char": 0, "end_char": 2172, "text_sha256": "1b30293ede979c158852939b48f68a2cd71fa605bbca813a9fe2325f99e5c1d3"}
experimental_model
Isotope-dilution LC-MS/MS assay validation in intervention urines
exposure
Broccoli sprout intervention specimens with equivalent administered preparation
limitations
Analytical exposure study; metabolite concentration is not tissue efficacy and does not identify each responsible human enzyme.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human, 98 urine specimens
plain_language
The same precursor dose did not produce the same exposure in everyone.
primary_references
[sulforaphane-p18729326] Quantification of sulforaphane mercapturic acid pathway conjugates in human urine by high-performance liquid chromatography and isotope-dilution tandem mass spectrometry. (2008). https://pubmed.ncbi.nlm.nih.gov/18729326/ DOI: 10.1021/tx800210k
tissue_or_cell_type
Urinary mercapturic-acid pathway species
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 385–396
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Isotope-dilution LC-MS/MS assay validation in intervention urines · source_derived_draft · unverified_draft
### sulforaphane-conversion-variability Interindividual precursor conversion varied over 100-fold in the studied intervention samples despite equivalent administered preparation. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The same precursor dose did not produce the same exposure in everyone. organism: Human, 98 urine specimens tissue_or_cell_type: Urinary mercapturic-acid pathway species experimental_model: Isotope-dilution LC-MS/MS assay validation in intervention urines limitations: Analytical exposure study; metabolite concentration is not tissue efficacy and does not identify each responsible human enzyme. exposure: Broccoli sprout intervention specimens with equivalent administered preparation evidence_span: {"source_cache": "artifacts/sulforaphane-research/18729326.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1b30293ede979c158852939b48f68a2cd71fa605bbca813a9fe2325f99e5c1d3", "start_char": 0, "end_char": 2172, "text_sha256": "1b30293ede979c158852939b48f68a2cd71fa605bbca813a9fe2325f99e5c1d3"} [sulforaphane-p18729326] Quantification of sulforaphane mercapturic acid pathway conjugates in human urine by high-performance liquid chromatography and isotope-dilution tandem mass spectrometry. (2008). https://pubmed.ncbi.nlm.nih.gov/18729326/ DOI: 10.1021/tx800210k
Complete structured claim and evidence
Human jejunal perfusion detected sulforaphane-GSH returned into the lumen after uptake.
Sulforaphane / SFN, stereochemistry specified per study → Sulforaphane-glutathione conjugate / SFN-GSH source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/12756216.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "98a56e8d1e84bffe3a4213eb3619d52869f85d999355d0e0f487d412149101af", "start_char": 0, "end_char": 1816, "text_sha256": "98a56e8d1e84bffe3a4213eb3619d52869f85d999355d0e0f487d412149101af"}
experimental_model
Human jejunal perfusion and parallel Caco-2 experiments
exposure
Dietary-concentration onion/broccoli extract perfusion
limitations
Human perfusion used a mixture; isolated Caco-2 comparisons help distinguish components. Local permeability is not systemic oral bioavailability.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human intestinal segment and human intestinal cell line
plain_language
Some absorbed material was processed and sent back into the gut.
primary_references
[sulforaphane-p12756216] Absorption/metabolism of sulforaphane and quercetin, and regulation of phase II enzymes, in human jejunum in vivo. (2003). https://pubmed.ncbi.nlm.nih.gov/12756216/ DOI: 10.1124/dmd.31.6.805
tissue_or_cell_type
Absorption, luminal return and gene expression
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 398–409
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human jejunal perfusion and parallel Caco-2 experiments · source_derived_draft · unverified_draft
### sulforaphane-intestinal-return Human jejunal perfusion detected sulforaphane-GSH returned into the lumen after uptake. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Some absorbed material was processed and sent back into the gut. organism: Human intestinal segment and human intestinal cell line tissue_or_cell_type: Absorption, luminal return and gene expression experimental_model: Human jejunal perfusion and parallel Caco-2 experiments limitations: Human perfusion used a mixture; isolated Caco-2 comparisons help distinguish components. Local permeability is not systemic oral bioavailability. exposure: Dietary-concentration onion/broccoli extract perfusion evidence_span: {"source_cache": "artifacts/sulforaphane-research/12756216.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "98a56e8d1e84bffe3a4213eb3619d52869f85d999355d0e0f487d412149101af", "start_char": 0, "end_char": 1816, "text_sha256": "98a56e8d1e84bffe3a4213eb3619d52869f85d999355d0e0f487d412149101af"} [sulforaphane-p12756216] Absorption/metabolism of sulforaphane and quercetin, and regulation of phase II enzymes, in human jejunum in vivo. (2003). https://pubmed.ncbi.nlm.nih.gov/12756216/ DOI: 10.1124/dmd.31.6.805
Complete structured claim and evidence
Parallel differentiated Caco-2 experiments assigned GSTA1 induction to sulforaphane; perfusion with mixed extract increased GSTA1 mRNA 2.0-fold.
Sulforaphane / SFN, stereochemistry specified per study → Human glutathione S-transferase A1 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/12756216.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "98a56e8d1e84bffe3a4213eb3619d52869f85d999355d0e0f487d412149101af", "start_char": 0, "end_char": 1816, "text_sha256": "98a56e8d1e84bffe3a4213eb3619d52869f85d999355d0e0f487d412149101af"}
experimental_model
Human jejunal perfusion and parallel Caco-2 experiments
exposure
Dietary-concentration onion/broccoli extract perfusion
limitations
Human perfusion used a mixture; isolated Caco-2 comparisons help distinguish components. Local permeability is not systemic oral bioavailability.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human intestinal segment and human intestinal cell line
plain_language
The mixture and the isolated-component experiment provide different levels of attribution.
primary_references
[sulforaphane-p12756216] Absorption/metabolism of sulforaphane and quercetin, and regulation of phase II enzymes, in human jejunum in vivo. (2003). https://pubmed.ncbi.nlm.nih.gov/12756216/ DOI: 10.1124/dmd.31.6.805
tissue_or_cell_type
Absorption, luminal return and gene expression
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 411–422
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human jejunal perfusion and parallel Caco-2 experiments · source_derived_draft · unverified_draft
### sulforaphane-gsta1-induction Parallel differentiated Caco-2 experiments assigned GSTA1 induction to sulforaphane; perfusion with mixed extract increased GSTA1 mRNA 2.0-fold. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The mixture and the isolated-component experiment provide different levels of attribution. organism: Human intestinal segment and human intestinal cell line tissue_or_cell_type: Absorption, luminal return and gene expression experimental_model: Human jejunal perfusion and parallel Caco-2 experiments limitations: Human perfusion used a mixture; isolated Caco-2 comparisons help distinguish components. Local permeability is not systemic oral bioavailability. exposure: Dietary-concentration onion/broccoli extract perfusion evidence_span: {"source_cache": "artifacts/sulforaphane-research/12756216.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "98a56e8d1e84bffe3a4213eb3619d52869f85d999355d0e0f487d412149101af", "start_char": 0, "end_char": 1816, "text_sha256": "98a56e8d1e84bffe3a4213eb3619d52869f85d999355d0e0f487d412149101af"} [sulforaphane-p12756216] Absorption/metabolism of sulforaphane and quercetin, and regulation of phase II enzymes, in human jejunum in vivo. (2003). https://pubmed.ncbi.nlm.nih.gov/12756216/ DOI: 10.1124/dmd.31.6.805
Complete structured claim and evidence
Iodoacetamide-based sample preparation caused loss of reversible sulforaphane adducts at reactive KEAP1 cysteines including C151.
Sulforaphane modification of KEAP1 cysteine residues → Iodoacetamide-containing KEAP1 mass-spectrometry sample preparation source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/21391649.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d1ecbe68352504813e0a666dc7474fba7f0a3f3aeb5d0b2fea681d376df999ac", "start_char": 0, "end_char": 1511, "text_sha256": "d1ecbe68352504813e0a666dc7474fba7f0a3f3aeb5d0b2fea681d376df999ac"}
experimental_model
Mass spectrometry with revised sample preparation
exposure
Sulforaphane exposure; omission of iodoacetamide and shorter processing
limitations
Explains an assay-dependent detection problem; not an unresolved universal C151 disagreement or a human efficacy trial.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
KEAP1 protein cysteine mapping
plain_language
An apparent missing binding site was explained by how the sample was prepared.
primary_references
[sulforaphane-p21391649] Modification of keap1 cysteine residues by sulforaphane. (2011). https://pubmed.ncbi.nlm.nih.gov/21391649/ DOI: 10.1021/tx100389r
tissue_or_cell_type
Reversible electrophile-thiol adducts
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 437–448
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Mass spectrometry with revised sample preparation · source_derived_draft · unverified_draft
### sulforaphane-adduct-loss-in-assay Iodoacetamide-based sample preparation caused loss of reversible sulforaphane adducts at reactive KEAP1 cysteines including C151. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: An apparent missing binding site was explained by how the sample was prepared. organism: KEAP1 protein cysteine mapping tissue_or_cell_type: Reversible electrophile-thiol adducts experimental_model: Mass spectrometry with revised sample preparation limitations: Explains an assay-dependent detection problem; not an unresolved universal C151 disagreement or a human efficacy trial. exposure: Sulforaphane exposure; omission of iodoacetamide and shorter processing evidence_span: {"source_cache": "artifacts/sulforaphane-research/21391649.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d1ecbe68352504813e0a666dc7474fba7f0a3f3aeb5d0b2fea681d376df999ac", "start_char": 0, "end_char": 1511, "text_sha256": "d1ecbe68352504813e0a666dc7474fba7f0a3f3aeb5d0b2fea681d376df999ac"} [sulforaphane-p21391649] Modification of keap1 cysteine residues by sulforaphane. (2011). https://pubmed.ncbi.nlm.nih.gov/21391649/ DOI: 10.1021/tx100389r
Complete structured claim and evidence
KEAP1 acted as a substrate adaptor in a functional CUL3-RBX1 ubiquitin-ligase complex.
Human KEAP1 → Human KEAP1-CUL3-RBX1 ubiquitin-ligase complex source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/15572695.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d120b0ea48a77a99b12e9147e4acb02fd63026ed729a37d5e2edf174c5674765", "start_char": 0, "end_char": 1484, "text_sha256": "d120b0ea48a77a99b12e9147e4acb02fd63026ed729a37d5e2edf174c5674765"}
experimental_model
Cell transfection, coimmunoprecipitation and ubiquitination assays
exposure
Sulforaphane or quinone stress; C151S KEAP1 comparison
limitations
The measured interaction is ubiquitin-ligase regulation; do not describe it as obligatory physical release of all bound Nrf2.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human protein constructs in mammalian cell systems
plain_language
The sensor helps bring the protein targeted for disposal to the disposal machinery.
primary_references
[sulforaphane-p15572695] Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex. (2004). https://pubmed.ncbi.nlm.nih.gov/15572695/ DOI: 10.1128/mcb.24.24.10941-10953.2004
tissue_or_cell_type
KEAP1-CUL3-RBX1 control of Nrf2
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 450–461
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cell transfection, coimmunoprecipitation and ubiquitination assays · source_derived_draft · unverified_draft
### sulforaphane-keap1-ligase KEAP1 acted as a substrate adaptor in a functional CUL3-RBX1 ubiquitin-ligase complex. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The sensor helps bring the protein targeted for disposal to the disposal machinery. organism: Human protein constructs in mammalian cell systems tissue_or_cell_type: KEAP1-CUL3-RBX1 control of Nrf2 experimental_model: Cell transfection, coimmunoprecipitation and ubiquitination assays limitations: The measured interaction is ubiquitin-ligase regulation; do not describe it as obligatory physical release of all bound Nrf2. exposure: Sulforaphane or quinone stress; C151S KEAP1 comparison evidence_span: {"source_cache": "artifacts/sulforaphane-research/15572695.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d120b0ea48a77a99b12e9147e4acb02fd63026ed729a37d5e2edf174c5674765", "start_char": 0, "end_char": 1484, "text_sha256": "d120b0ea48a77a99b12e9147e4acb02fd63026ed729a37d5e2edf174c5674765"} [sulforaphane-p15572695] Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex. (2004). https://pubmed.ncbi.nlm.nih.gov/15572695/ DOI: 10.1128/mcb.24.24.10941-10953.2004
Complete structured claim and evidence
The KEAP1-CUL3-RBX1 complex targeted multiple lysines in the Nrf2 Neh2 domain for ubiquitination.
Human KEAP1-CUL3-RBX1 ubiquitin-ligase complex → Human Nrf2 / NFE2L2 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/15572695.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d120b0ea48a77a99b12e9147e4acb02fd63026ed729a37d5e2edf174c5674765", "start_char": 0, "end_char": 1484, "text_sha256": "d120b0ea48a77a99b12e9147e4acb02fd63026ed729a37d5e2edf174c5674765"}
experimental_model
Cell transfection, coimmunoprecipitation and ubiquitination assays
exposure
Sulforaphane or quinone stress; C151S KEAP1 comparison
limitations
The measured interaction is ubiquitin-ligase regulation; do not describe it as obligatory physical release of all bound Nrf2.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human protein constructs in mammalian cell systems
plain_language
Nrf2 is normally marked for turnover.
primary_references
[sulforaphane-p15572695] Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex. (2004). https://pubmed.ncbi.nlm.nih.gov/15572695/ DOI: 10.1128/mcb.24.24.10941-10953.2004
tissue_or_cell_type
KEAP1-CUL3-RBX1 control of Nrf2
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 463–474
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cell transfection, coimmunoprecipitation and ubiquitination assays · source_derived_draft · unverified_draft
### sulforaphane-ligase-nrf2 The KEAP1-CUL3-RBX1 complex targeted multiple lysines in the Nrf2 Neh2 domain for ubiquitination. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Nrf2 is normally marked for turnover. organism: Human protein constructs in mammalian cell systems tissue_or_cell_type: KEAP1-CUL3-RBX1 control of Nrf2 experimental_model: Cell transfection, coimmunoprecipitation and ubiquitination assays limitations: The measured interaction is ubiquitin-ligase regulation; do not describe it as obligatory physical release of all bound Nrf2. exposure: Sulforaphane or quinone stress; C151S KEAP1 comparison evidence_span: {"source_cache": "artifacts/sulforaphane-research/15572695.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d120b0ea48a77a99b12e9147e4acb02fd63026ed729a37d5e2edf174c5674765", "start_char": 0, "end_char": 1484, "text_sha256": "d120b0ea48a77a99b12e9147e4acb02fd63026ed729a37d5e2edf174c5674765"} [sulforaphane-p15572695] Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex. (2004). https://pubmed.ncbi.nlm.nih.gov/15572695/ DOI: 10.1128/mcb.24.24.10941-10953.2004
Complete structured claim and evidence
Sulforaphane did not disrupt the KEAP1-Nrf2 association in the tested interaction assays.
Sulforaphane / SFN, stereochemistry specified per study → KEAP1-Nrf2 association source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/15572695.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d120b0ea48a77a99b12e9147e4acb02fd63026ed729a37d5e2edf174c5674765", "start_char": 0, "end_char": 1484, "text_sha256": "d120b0ea48a77a99b12e9147e4acb02fd63026ed729a37d5e2edf174c5674765"}
experimental_model
Cell transfection, coimmunoprecipitation and ubiquitination assays
exposure
Sulforaphane or quinone stress; C151S KEAP1 comparison
limitations
The measured interaction is ubiquitin-ligase regulation; do not describe it as obligatory physical release of all bound Nrf2.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human protein constructs in mammalian cell systems
plain_language
Activating this pathway did not require complete separation of these proteins in the assay.
primary_references
[sulforaphane-p15572695] Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex. (2004). https://pubmed.ncbi.nlm.nih.gov/15572695/ DOI: 10.1128/mcb.24.24.10941-10953.2004
tissue_or_cell_type
KEAP1-CUL3-RBX1 control of Nrf2
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 489–500
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cell transfection, coimmunoprecipitation and ubiquitination assays · source_derived_draft · unverified_draft
### sulforaphane-binding-not-release Sulforaphane did not disrupt the KEAP1-Nrf2 association in the tested interaction assays. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Activating this pathway did not require complete separation of these proteins in the assay. organism: Human protein constructs in mammalian cell systems tissue_or_cell_type: KEAP1-CUL3-RBX1 control of Nrf2 experimental_model: Cell transfection, coimmunoprecipitation and ubiquitination assays limitations: The measured interaction is ubiquitin-ligase regulation; do not describe it as obligatory physical release of all bound Nrf2. exposure: Sulforaphane or quinone stress; C151S KEAP1 comparison evidence_span: {"source_cache": "artifacts/sulforaphane-research/15572695.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d120b0ea48a77a99b12e9147e4acb02fd63026ed729a37d5e2edf174c5674765", "start_char": 0, "end_char": 1484, "text_sha256": "d120b0ea48a77a99b12e9147e4acb02fd63026ed729a37d5e2edf174c5674765"} [sulforaphane-p15572695] Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex. (2004). https://pubmed.ncbi.nlm.nih.gov/15572695/ DOI: 10.1128/mcb.24.24.10941-10953.2004
Complete structured claim and evidence
KEAP1 C151S was markedly resistant to sulforaphane inhibition of its Nrf2-ubiquitination function.
Human KEAP1 C151S variant → KEAP1-dependent Nrf2 ubiquitination source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/sulforaphane-research/15572695.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d120b0ea48a77a99b12e9147e4acb02fd63026ed729a37d5e2edf174c5674765", "start_char": 0, "end_char": 1484, "text_sha256": "d120b0ea48a77a99b12e9147e4acb02fd63026ed729a37d5e2edf174c5674765"}
experimental_model
Cell transfection, coimmunoprecipitation and ubiquitination assays
exposure
Sulforaphane or quinone stress; C151S KEAP1 comparison
limitations
The measured interaction is ubiquitin-ligase regulation; do not describe it as obligatory physical release of all bound Nrf2.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human protein constructs in mammalian cell systems
plain_language
An altered sensor can block the response even when the compound is present.
primary_references
[sulforaphane-p15572695] Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex. (2004). https://pubmed.ncbi.nlm.nih.gov/15572695/ DOI: 10.1128/mcb.24.24.10941-10953.2004
tissue_or_cell_type
KEAP1-CUL3-RBX1 control of Nrf2
trigger_kind
machinery_impairment Imported condition classification; unverified.
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 502–513
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cell transfection, coimmunoprecipitation and ubiquitination assays · source_derived_draft · unverified_draft
### sulforaphane-c151s-response KEAP1 C151S was markedly resistant to sulforaphane inhibition of its Nrf2-ubiquitination function. Condition category: machinery_impairment nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: An altered sensor can block the response even when the compound is present. organism: Human protein constructs in mammalian cell systems tissue_or_cell_type: KEAP1-CUL3-RBX1 control of Nrf2 experimental_model: Cell transfection, coimmunoprecipitation and ubiquitination assays limitations: The measured interaction is ubiquitin-ligase regulation; do not describe it as obligatory physical release of all bound Nrf2. exposure: Sulforaphane or quinone stress; C151S KEAP1 comparison evidence_span: {"source_cache": "artifacts/sulforaphane-research/15572695.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d120b0ea48a77a99b12e9147e4acb02fd63026ed729a37d5e2edf174c5674765", "start_char": 0, "end_char": 1484, "text_sha256": "d120b0ea48a77a99b12e9147e4acb02fd63026ed729a37d5e2edf174c5674765"} [sulforaphane-p15572695] Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex. (2004). https://pubmed.ncbi.nlm.nih.gov/15572695/ DOI: 10.1128/mcb.24.24.10941-10953.2004
Complete structured claim and evidence
Sulforaphane enabled Nrf2 to escape KEAP1-dependent degradation and increased its stability.
Sulforaphane / SFN, stereochemistry specified per study → Nrf2 protein stability source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/14585973.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bc2e1304879d9bd3d1b4946981f93a78d3f604c580ea252af17f645e237cadd0", "start_char": 0, "end_char": 1647, "text_sha256": "bc2e1304879d9bd3d1b4946981f93a78d3f604c580ea252af17f645e237cadd0"}
experimental_model
KEAP1 mutagenesis and Nrf2 stability/localization assays
exposure
Sulforaphane or oxidative stress; C151/C273/C288 variants
limitations
Individual cysteines have different roles; activating Nrf2 does not establish prevention or treatment of cancer in humans.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human KEAP1 constructs in cellular experiments
plain_language
The cell keeps more of the regulator available.
primary_references
[sulforaphane-p14585973] Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress. (2003). https://pubmed.ncbi.nlm.nih.gov/14585973/ DOI: 10.1128/mcb.23.22.8137-8151.2003
tissue_or_cell_type
Ubiquitination, protein turnover and nuclear localization
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 515–526
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · KEAP1 mutagenesis and Nrf2 stability/localization assays · source_derived_draft · unverified_draft
### sulforaphane-nrf2-stability Sulforaphane enabled Nrf2 to escape KEAP1-dependent degradation and increased its stability. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The cell keeps more of the regulator available. organism: Human KEAP1 constructs in cellular experiments tissue_or_cell_type: Ubiquitination, protein turnover and nuclear localization experimental_model: KEAP1 mutagenesis and Nrf2 stability/localization assays limitations: Individual cysteines have different roles; activating Nrf2 does not establish prevention or treatment of cancer in humans. exposure: Sulforaphane or oxidative stress; C151/C273/C288 variants evidence_span: {"source_cache": "artifacts/sulforaphane-research/14585973.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bc2e1304879d9bd3d1b4946981f93a78d3f604c580ea252af17f645e237cadd0", "start_char": 0, "end_char": 1647, "text_sha256": "bc2e1304879d9bd3d1b4946981f93a78d3f604c580ea252af17f645e237cadd0"} [sulforaphane-p14585973] Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress. (2003). https://pubmed.ncbi.nlm.nih.gov/14585973/ DOI: 10.1128/mcb.23.22.8137-8151.2003
Complete structured claim and evidence
Sulforaphane induced Nrf2-dependent NQO1 expression in untransformed human CRL-1790 colon cells.
Sulforaphane / SFN, stereochemistry specified per study → Human NAD(P)H quinone dehydrogenase 1 / NQO1 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/27636860.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "38b05ba233878d75f74373f3093e4d51bbbbb417b59f06dec578f7c293e12793", "start_char": 0, "end_char": 1177, "text_sha256": "38b05ba233878d75f74373f3093e4d51bbbbb417b59f06dec578f7c293e12793"}
experimental_model
Gene and enzyme-response comparison
exposure
Sulforaphane exposure across three cell contexts
limitations
Cancer and untransformed cells regulated the pathway differently; no claim that all Nrf2 activation is desirable in established tumors.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human CRL-1790 untransformed colon cells, HT-29 and Caco-2 cancer cells
plain_language
One induced enzyme handles quinone chemistry.
primary_references
[sulforaphane-p27636860] Sulforaphane Regulates NFE2L2/Nrf2-Dependent Xenobiotic Metabolism Phase II and Phase III Enzymes Differently in Human Colorectal Cancer and Untransformed Epithelial Colon Cells. (2016). https://pubmed.ncbi.nlm.nih.gov/27636860/ DOI: 10.1080/01635581.2016.1224369
tissue_or_cell_type
Nrf2 targets and cell defense
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 541–552
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Gene and enzyme-response comparison · source_derived_draft · unverified_draft
### sulforaphane-nqo1-induction Sulforaphane induced Nrf2-dependent NQO1 expression in untransformed human CRL-1790 colon cells. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: One induced enzyme handles quinone chemistry. organism: Human CRL-1790 untransformed colon cells, HT-29 and Caco-2 cancer cells tissue_or_cell_type: Nrf2 targets and cell defense experimental_model: Gene and enzyme-response comparison limitations: Cancer and untransformed cells regulated the pathway differently; no claim that all Nrf2 activation is desirable in established tumors. exposure: Sulforaphane exposure across three cell contexts evidence_span: {"source_cache": "artifacts/sulforaphane-research/27636860.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "38b05ba233878d75f74373f3093e4d51bbbbb417b59f06dec578f7c293e12793", "start_char": 0, "end_char": 1177, "text_sha256": "38b05ba233878d75f74373f3093e4d51bbbbb417b59f06dec578f7c293e12793"} [sulforaphane-p27636860] Sulforaphane Regulates NFE2L2/Nrf2-Dependent Xenobiotic Metabolism Phase II and Phase III Enzymes Differently in Human Colorectal Cancer and Untransformed Epithelial Colon Cells. (2016). https://pubmed.ncbi.nlm.nih.gov/27636860/ DOI: 10.1080/01635581.2016.1224369
Complete structured claim and evidence
Sulforaphane induced Nrf2-dependent MRP1 expression in CRL-1790 cells.
Sulforaphane / SFN, stereochemistry specified per study → Human multidrug resistance-associated protein 1 / ABCC1 / MRP1 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/27636860.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "38b05ba233878d75f74373f3093e4d51bbbbb417b59f06dec578f7c293e12793", "start_char": 0, "end_char": 1177, "text_sha256": "38b05ba233878d75f74373f3093e4d51bbbbb417b59f06dec578f7c293e12793"}
experimental_model
Gene and enzyme-response comparison
exposure
Sulforaphane exposure across three cell contexts
limitations
Cancer and untransformed cells regulated the pathway differently; no claim that all Nrf2 activation is desirable in established tumors.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human CRL-1790 untransformed colon cells, HT-29 and Caco-2 cancer cells
plain_language
The response can increase an export transporter as well as enzymes.
primary_references
[sulforaphane-p27636860] Sulforaphane Regulates NFE2L2/Nrf2-Dependent Xenobiotic Metabolism Phase II and Phase III Enzymes Differently in Human Colorectal Cancer and Untransformed Epithelial Colon Cells. (2016). https://pubmed.ncbi.nlm.nih.gov/27636860/ DOI: 10.1080/01635581.2016.1224369
tissue_or_cell_type
Nrf2 targets and cell defense
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 554–565
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Gene and enzyme-response comparison · source_derived_draft · unverified_draft
### sulforaphane-mrp1-induction Sulforaphane induced Nrf2-dependent MRP1 expression in CRL-1790 cells. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The response can increase an export transporter as well as enzymes. organism: Human CRL-1790 untransformed colon cells, HT-29 and Caco-2 cancer cells tissue_or_cell_type: Nrf2 targets and cell defense experimental_model: Gene and enzyme-response comparison limitations: Cancer and untransformed cells regulated the pathway differently; no claim that all Nrf2 activation is desirable in established tumors. exposure: Sulforaphane exposure across three cell contexts evidence_span: {"source_cache": "artifacts/sulforaphane-research/27636860.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "38b05ba233878d75f74373f3093e4d51bbbbb417b59f06dec578f7c293e12793", "start_char": 0, "end_char": 1177, "text_sha256": "38b05ba233878d75f74373f3093e4d51bbbbb417b59f06dec578f7c293e12793"} [sulforaphane-p27636860] Sulforaphane Regulates NFE2L2/Nrf2-Dependent Xenobiotic Metabolism Phase II and Phase III Enzymes Differently in Human Colorectal Cancer and Untransformed Epithelial Colon Cells. (2016). https://pubmed.ncbi.nlm.nih.gov/27636860/ DOI: 10.1080/01635581.2016.1224369
Complete structured claim and evidence
SFN-Cys inhibited HDAC activity in vitro, whereas parent sulforaphane and SFN-GSH had little or no direct effect in the comparison.
Sulforaphane-cysteine conjugate / SFN-Cys → histone deacetylase activity source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/15313918.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9478957b1513e25cb47f13d6a1aca0df542fc851d8eb4b9c6394010e90dbe83e", "start_char": 0, "end_char": 1861, "text_sha256": "9478957b1513e25cb47f13d6a1aca0df542fc851d8eb4b9c6394010e90dbe83e"}
experimental_model
Cell exposure, enzyme assays, metabolites and chromatin immunoprecipitation
exposure
Parent SFN, SFN-GSH, SFN-Cys and SFN-NAC; GST inhibition
limitations
High-level HDAC activity was measured without establishing universal isoform inhibition; cell effects are not cancer-treatment outcomes.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human HEK293 and HCT116 cells
plain_language
A breakdown product had a different activity from the parent molecule.
primary_references
[sulforaphane-p15313918] A novel mechanism of chemoprotection by sulforaphane: inhibition of histone deacetylase. (2004). https://pubmed.ncbi.nlm.nih.gov/15313918/ DOI: 10.1158/0008-5472.can-04-1326
tissue_or_cell_type
Histone deacetylase activity and histone acetylation
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 567–578
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cell exposure, enzyme assays, metabolites and chromatin immunoprecipitation · source_derived_draft · unverified_draft
### sulforaphane-cys-hdac SFN-Cys inhibited HDAC activity in vitro, whereas parent sulforaphane and SFN-GSH had little or no direct effect in the comparison. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: A breakdown product had a different activity from the parent molecule. organism: Human HEK293 and HCT116 cells tissue_or_cell_type: Histone deacetylase activity and histone acetylation experimental_model: Cell exposure, enzyme assays, metabolites and chromatin immunoprecipitation limitations: High-level HDAC activity was measured without establishing universal isoform inhibition; cell effects are not cancer-treatment outcomes. exposure: Parent SFN, SFN-GSH, SFN-Cys and SFN-NAC; GST inhibition evidence_span: {"source_cache": "artifacts/sulforaphane-research/15313918.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9478957b1513e25cb47f13d6a1aca0df542fc851d8eb4b9c6394010e90dbe83e", "start_char": 0, "end_char": 1861, "text_sha256": "9478957b1513e25cb47f13d6a1aca0df542fc851d8eb4b9c6394010e90dbe83e"} [sulforaphane-p15313918] A novel mechanism of chemoprotection by sulforaphane: inhibition of histone deacetylase. (2004). https://pubmed.ncbi.nlm.nih.gov/15313918/ DOI: 10.1158/0008-5472.can-04-1326
Complete structured claim and evidence
SFN-NAC also inhibited HDAC activity in the in vitro comparison.
Sulforaphane-N-acetylcysteine conjugate / SFN-NAC → histone deacetylase activity source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/15313918.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9478957b1513e25cb47f13d6a1aca0df542fc851d8eb4b9c6394010e90dbe83e", "start_char": 0, "end_char": 1861, "text_sha256": "9478957b1513e25cb47f13d6a1aca0df542fc851d8eb4b9c6394010e90dbe83e"}
experimental_model
Cell exposure, enzyme assays, metabolites and chromatin immunoprecipitation
exposure
Parent SFN, SFN-GSH, SFN-Cys and SFN-NAC; GST inhibition
limitations
High-level HDAC activity was measured without establishing universal isoform inhibition; cell effects are not cancer-treatment outcomes.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human HEK293 and HCT116 cells
plain_language
Another separately tracked conjugate affected this enzyme readout.
primary_references
[sulforaphane-p15313918] A novel mechanism of chemoprotection by sulforaphane: inhibition of histone deacetylase. (2004). https://pubmed.ncbi.nlm.nih.gov/15313918/ DOI: 10.1158/0008-5472.can-04-1326
tissue_or_cell_type
Histone deacetylase activity and histone acetylation
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 580–591
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cell exposure, enzyme assays, metabolites and chromatin immunoprecipitation · source_derived_draft · unverified_draft
### sulforaphane-nac-hdac SFN-NAC also inhibited HDAC activity in the in vitro comparison. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Another separately tracked conjugate affected this enzyme readout. organism: Human HEK293 and HCT116 cells tissue_or_cell_type: Histone deacetylase activity and histone acetylation experimental_model: Cell exposure, enzyme assays, metabolites and chromatin immunoprecipitation limitations: High-level HDAC activity was measured without establishing universal isoform inhibition; cell effects are not cancer-treatment outcomes. exposure: Parent SFN, SFN-GSH, SFN-Cys and SFN-NAC; GST inhibition evidence_span: {"source_cache": "artifacts/sulforaphane-research/15313918.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9478957b1513e25cb47f13d6a1aca0df542fc851d8eb4b9c6394010e90dbe83e", "start_char": 0, "end_char": 1861, "text_sha256": "9478957b1513e25cb47f13d6a1aca0df542fc851d8eb4b9c6394010e90dbe83e"} [sulforaphane-p15313918] A novel mechanism of chemoprotection by sulforaphane: inhibition of histone deacetylase. (2004). https://pubmed.ncbi.nlm.nih.gov/15313918/ DOI: 10.1158/0008-5472.can-04-1326
Complete structured claim and evidence
Sulforaphane exposure increased acetylated histones in HEK293 and HCT116 experiments, including increased acetylated histones at the HCT116 P21 promoter.
Sulforaphane / SFN, stereochemistry specified per study → Core histone lysine acetylation source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/15313918.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9478957b1513e25cb47f13d6a1aca0df542fc851d8eb4b9c6394010e90dbe83e", "start_char": 0, "end_char": 1861, "text_sha256": "9478957b1513e25cb47f13d6a1aca0df542fc851d8eb4b9c6394010e90dbe83e"}
experimental_model
Cell exposure, enzyme assays, metabolites and chromatin immunoprecipitation
exposure
Parent SFN, SFN-GSH, SFN-Cys and SFN-NAC; GST inhibition
limitations
High-level HDAC activity was measured without establishing universal isoform inhibition; cell effects are not cancer-treatment outcomes.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human HEK293 and HCT116 cells
plain_language
The study measured a change to the chemical marks on DNA-packaging proteins.
primary_references
[sulforaphane-p15313918] A novel mechanism of chemoprotection by sulforaphane: inhibition of histone deacetylase. (2004). https://pubmed.ncbi.nlm.nih.gov/15313918/ DOI: 10.1158/0008-5472.can-04-1326
tissue_or_cell_type
Histone deacetylase activity and histone acetylation
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 593–604
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cell exposure, enzyme assays, metabolites and chromatin immunoprecipitation · source_derived_draft · unverified_draft
### sulforaphane-histone-acetylation-up Sulforaphane exposure increased acetylated histones in HEK293 and HCT116 experiments, including increased acetylated histones at the HCT116 P21 promoter. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The study measured a change to the chemical marks on DNA-packaging proteins. organism: Human HEK293 and HCT116 cells tissue_or_cell_type: Histone deacetylase activity and histone acetylation experimental_model: Cell exposure, enzyme assays, metabolites and chromatin immunoprecipitation limitations: High-level HDAC activity was measured without establishing universal isoform inhibition; cell effects are not cancer-treatment outcomes. exposure: Parent SFN, SFN-GSH, SFN-Cys and SFN-NAC; GST inhibition evidence_span: {"source_cache": "artifacts/sulforaphane-research/15313918.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9478957b1513e25cb47f13d6a1aca0df542fc851d8eb4b9c6394010e90dbe83e", "start_char": 0, "end_char": 1861, "text_sha256": "9478957b1513e25cb47f13d6a1aca0df542fc851d8eb4b9c6394010e90dbe83e"} [sulforaphane-p15313918] A novel mechanism of chemoprotection by sulforaphane: inhibition of histone deacetylase. (2004). https://pubmed.ncbi.nlm.nih.gov/15313918/ DOI: 10.1158/0008-5472.can-04-1326
Complete structured claim and evidence
Sulforaphane decreased acetylated histone H3, H4 and tubulin markers in the cell comparisons despite reduced HDAC protein levels.
Sulforaphane / SFN, stereochemistry specified per study → Core histone lysine acetylation source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/25307283.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "cc736d6c2f2dc6c4026bdad0a5835d69ed094775076a2c1606f47020e6783331", "start_char": 0, "end_char": 1504, "text_sha256": "cc736d6c2f2dc6c4026bdad0a5835d69ed094775076a2c1606f47020e6783331"}
experimental_model
Matched cell-type and time-course comparison
exposure
Sulforaphane exposure; serum and time-course comparisons
limitations
Activity assays, protein abundance and substrate acetylation are distinct endpoints; mechanism of their divergence was not established. Erratum PMID 27271518 adds an omitted funding acknowledgment without revising these results.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human HaCaT keratinocytes and HCT116 colon cancer cells
plain_language
Less enzyme protein did not produce the expected increase in acetylation.
primary_references
[sulforaphane-p25307283] The effect of sulforaphane on histone deacetylase activity in keratinocytes: Differences between in vitro and in vivo analyses. (2015). https://pubmed.ncbi.nlm.nih.gov/25307283/ DOI: 10.1002/mc.22224
tissue_or_cell_type
HDAC activity, protein levels and target acetylation
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 606–617
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Matched cell-type and time-course comparison · source_derived_draft · unverified_draft
### sulforaphane-histone-acetylation-down Sulforaphane decreased acetylated histone H3, H4 and tubulin markers in the cell comparisons despite reduced HDAC protein levels. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Less enzyme protein did not produce the expected increase in acetylation. organism: Human HaCaT keratinocytes and HCT116 colon cancer cells tissue_or_cell_type: HDAC activity, protein levels and target acetylation experimental_model: Matched cell-type and time-course comparison limitations: Activity assays, protein abundance and substrate acetylation are distinct endpoints; mechanism of their divergence was not established. Erratum PMID 27271518 adds an omitted funding acknowledgment without revising these results. exposure: Sulforaphane exposure; serum and time-course comparisons evidence_span: {"source_cache": "artifacts/sulforaphane-research/25307283.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "cc736d6c2f2dc6c4026bdad0a5835d69ed094775076a2c1606f47020e6783331", "start_char": 0, "end_char": 1504, "text_sha256": "cc736d6c2f2dc6c4026bdad0a5835d69ed094775076a2c1606f47020e6783331"} [sulforaphane-p25307283] The effect of sulforaphane on histone deacetylase activity in keratinocytes: Differences between in vitro and in vivo analyses. (2015). https://pubmed.ncbi.nlm.nih.gov/25307283/ DOI: 10.1002/mc.22224
Complete structured claim and evidence
HDAC6 protein decreased early during treatment and HDAC6 transcript was suppressed after 48 hours.
Sulforaphane / SFN, stereochemistry specified per study → Human histone deacetylase 6 / HDAC6 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/25307283.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "cc736d6c2f2dc6c4026bdad0a5835d69ed094775076a2c1606f47020e6783331", "start_char": 0, "end_char": 1504, "text_sha256": "cc736d6c2f2dc6c4026bdad0a5835d69ed094775076a2c1606f47020e6783331"}
experimental_model
Matched cell-type and time-course comparison
exposure
Sulforaphane exposure; serum and time-course comparisons
limitations
Activity assays, protein abundance and substrate acetylation are distinct endpoints; mechanism of their divergence was not established. Erratum PMID 27271518 adds an omitted funding acknowledgment without revising these results.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human HaCaT keratinocytes and HCT116 colon cancer cells
plain_language
Protein abundance and catalytic activity must be recorded separately.
primary_references
[sulforaphane-p25307283] The effect of sulforaphane on histone deacetylase activity in keratinocytes: Differences between in vitro and in vivo analyses. (2015). https://pubmed.ncbi.nlm.nih.gov/25307283/ DOI: 10.1002/mc.22224
tissue_or_cell_type
HDAC activity, protein levels and target acetylation
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 619–630
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Matched cell-type and time-course comparison · source_derived_draft · unverified_draft
### sulforaphane-hdac6-abundance HDAC6 protein decreased early during treatment and HDAC6 transcript was suppressed after 48 hours. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Protein abundance and catalytic activity must be recorded separately. organism: Human HaCaT keratinocytes and HCT116 colon cancer cells tissue_or_cell_type: HDAC activity, protein levels and target acetylation experimental_model: Matched cell-type and time-course comparison limitations: Activity assays, protein abundance and substrate acetylation are distinct endpoints; mechanism of their divergence was not established. Erratum PMID 27271518 adds an omitted funding acknowledgment without revising these results. exposure: Sulforaphane exposure; serum and time-course comparisons evidence_span: {"source_cache": "artifacts/sulforaphane-research/25307283.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "cc736d6c2f2dc6c4026bdad0a5835d69ed094775076a2c1606f47020e6783331", "start_char": 0, "end_char": 1504, "text_sha256": "cc736d6c2f2dc6c4026bdad0a5835d69ed094775076a2c1606f47020e6783331"} [sulforaphane-p25307283] The effect of sulforaphane on histone deacetylase activity in keratinocytes: Differences between in vitro and in vivo analyses. (2015). https://pubmed.ncbi.nlm.nih.gov/25307283/ DOI: 10.1002/mc.22224
Complete structured claim and evidence
Sulforaphane inhibited mTOR signaling in U2OS cells both with and without NRF2.
Sulforaphane / SFN, stereochemistry specified per study → mTOR signaling in human U2OS cells source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/31409554.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5486f97c1271a771620cdf2e6245a54ff63f3f56b3eb884f201fda9882ec947b", "start_char": 0, "end_char": 1778, "text_sha256": "5486f97c1271a771620cdf2e6245a54ff63f3f56b3eb884f201fda9882ec947b"}
experimental_model
Human cell experiments with CRISPR NRF2 deletion
exposure
Concentration- and time-dependent sulforaphane treatment
limitations
Preclinical cancer-cell signaling; AKT phosphorylation did not reliably represent catalytic output. Not a human longevity or autophagy trial.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human U2OS osteosarcoma cells and NRF2-knockout counterpart
plain_language
Some effects remain when the familiar NRF2 pathway is absent.
primary_references
[sulforaphane-p31409554] The isothiocyanate sulforaphane inhibits mTOR in an NRF2-independent manner. (2021). https://pubmed.ncbi.nlm.nih.gov/31409554/ DOI: 10.1016/j.phymed.2019.153062
tissue_or_cell_type
HDAC6, AKT and mTOR signaling
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 632–643
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human cell experiments with CRISPR NRF2 deletion · source_derived_draft · unverified_draft
### sulforaphane-mtor-independent Sulforaphane inhibited mTOR signaling in U2OS cells both with and without NRF2. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Some effects remain when the familiar NRF2 pathway is absent. organism: Human U2OS osteosarcoma cells and NRF2-knockout counterpart tissue_or_cell_type: HDAC6, AKT and mTOR signaling experimental_model: Human cell experiments with CRISPR NRF2 deletion limitations: Preclinical cancer-cell signaling; AKT phosphorylation did not reliably represent catalytic output. Not a human longevity or autophagy trial. exposure: Concentration- and time-dependent sulforaphane treatment evidence_span: {"source_cache": "artifacts/sulforaphane-research/31409554.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5486f97c1271a771620cdf2e6245a54ff63f3f56b3eb884f201fda9882ec947b", "start_char": 0, "end_char": 1778, "text_sha256": "5486f97c1271a771620cdf2e6245a54ff63f3f56b3eb884f201fda9882ec947b"} [sulforaphane-p31409554] The isothiocyanate sulforaphane inhibits mTOR in an NRF2-independent manner. (2021). https://pubmed.ncbi.nlm.nih.gov/31409554/ DOI: 10.1016/j.phymed.2019.153062
Complete structured claim and evidence
Sulforaphane inhibited cytoplasmic HDAC6 activity in the U2OS study.
Sulforaphane / SFN, stereochemistry specified per study → Human histone deacetylase 6 / HDAC6 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/31409554.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5486f97c1271a771620cdf2e6245a54ff63f3f56b3eb884f201fda9882ec947b", "start_char": 0, "end_char": 1778, "text_sha256": "5486f97c1271a771620cdf2e6245a54ff63f3f56b3eb884f201fda9882ec947b"}
experimental_model
Human cell experiments with CRISPR NRF2 deletion
exposure
Concentration- and time-dependent sulforaphane treatment
limitations
Preclinical cancer-cell signaling; AKT phosphorylation did not reliably represent catalytic output. Not a human longevity or autophagy trial.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human U2OS osteosarcoma cells and NRF2-knockout counterpart
plain_language
This experiment identifies a particular HDAC isoform.
primary_references
[sulforaphane-p31409554] The isothiocyanate sulforaphane inhibits mTOR in an NRF2-independent manner. (2021). https://pubmed.ncbi.nlm.nih.gov/31409554/ DOI: 10.1016/j.phymed.2019.153062
tissue_or_cell_type
HDAC6, AKT and mTOR signaling
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 645–656
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human cell experiments with CRISPR NRF2 deletion · source_derived_draft · unverified_draft
### sulforaphane-hdac6-activity Sulforaphane inhibited cytoplasmic HDAC6 activity in the U2OS study. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: This experiment identifies a particular HDAC isoform. organism: Human U2OS osteosarcoma cells and NRF2-knockout counterpart tissue_or_cell_type: HDAC6, AKT and mTOR signaling experimental_model: Human cell experiments with CRISPR NRF2 deletion limitations: Preclinical cancer-cell signaling; AKT phosphorylation did not reliably represent catalytic output. Not a human longevity or autophagy trial. exposure: Concentration- and time-dependent sulforaphane treatment evidence_span: {"source_cache": "artifacts/sulforaphane-research/31409554.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5486f97c1271a771620cdf2e6245a54ff63f3f56b3eb884f201fda9882ec947b", "start_char": 0, "end_char": 1778, "text_sha256": "5486f97c1271a771620cdf2e6245a54ff63f3f56b3eb884f201fda9882ec947b"} [sulforaphane-p31409554] The isothiocyanate sulforaphane inhibits mTOR in an NRF2-independent manner. (2021). https://pubmed.ncbi.nlm.nih.gov/31409554/ DOI: 10.1016/j.phymed.2019.153062
Complete structured claim and evidence
Reduced phosphorylation of the AKT substrate beta-catenin at S552 indicated lower AKT output despite increased AKT T308/S473 phosphorylation.
Sulforaphane / SFN, stereochemistry specified per study → AKT catalytic output in human U2OS cells source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/31409554.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5486f97c1271a771620cdf2e6245a54ff63f3f56b3eb884f201fda9882ec947b", "start_char": 0, "end_char": 1778, "text_sha256": "5486f97c1271a771620cdf2e6245a54ff63f3f56b3eb884f201fda9882ec947b"}
experimental_model
Human cell experiments with CRISPR NRF2 deletion
exposure
Concentration- and time-dependent sulforaphane treatment
limitations
Preclinical cancer-cell signaling; AKT phosphorylation did not reliably represent catalytic output. Not a human longevity or autophagy trial.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human U2OS osteosarcoma cells and NRF2-knockout counterpart
plain_language
An activation marker and the enzyme output moved in different directions.
primary_references
[sulforaphane-p31409554] The isothiocyanate sulforaphane inhibits mTOR in an NRF2-independent manner. (2021). https://pubmed.ncbi.nlm.nih.gov/31409554/ DOI: 10.1016/j.phymed.2019.153062
tissue_or_cell_type
HDAC6, AKT and mTOR signaling
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 658–669
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human cell experiments with CRISPR NRF2 deletion · source_derived_draft · unverified_draft
### sulforaphane-akt-output Reduced phosphorylation of the AKT substrate beta-catenin at S552 indicated lower AKT output despite increased AKT T308/S473 phosphorylation. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: An activation marker and the enzyme output moved in different directions. organism: Human U2OS osteosarcoma cells and NRF2-knockout counterpart tissue_or_cell_type: HDAC6, AKT and mTOR signaling experimental_model: Human cell experiments with CRISPR NRF2 deletion limitations: Preclinical cancer-cell signaling; AKT phosphorylation did not reliably represent catalytic output. Not a human longevity or autophagy trial. exposure: Concentration- and time-dependent sulforaphane treatment evidence_span: {"source_cache": "artifacts/sulforaphane-research/31409554.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5486f97c1271a771620cdf2e6245a54ff63f3f56b3eb884f201fda9882ec947b", "start_char": 0, "end_char": 1778, "text_sha256": "5486f97c1271a771620cdf2e6245a54ff63f3f56b3eb884f201fda9882ec947b"} [sulforaphane-p31409554] The isothiocyanate sulforaphane inhibits mTOR in an NRF2-independent manner. (2021). https://pubmed.ncbi.nlm.nih.gov/31409554/ DOI: 10.1016/j.phymed.2019.153062
Complete structured claim and evidence
Receptor mapping found sulforaphane adducts at TLR4 C246 and C609 under non-reducing conditions.
Sulforaphane / SFN, stereochemistry specified per study → Human toll-like receptor 4 / TLR4 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/25284333.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0a293f12863f5cfc2d57d74f4acee8c62700e2744a5900643bc23eca85c62be5", "start_char": 0, "end_char": 1494, "text_sha256": "0a293f12863f5cfc2d57d74f4acee8c62700e2744a5900643bc23eca85c62be5"}
experimental_model
Recombinant receptor mapping, human cell exposure and ex vivo challenge
exposure
Sulforaphane under non-reducing conditions; LPS challenge after ITC exposure
limitations
Covalent mapping does not establish the sole cause of cytokine effects; not a chronic-disease outcome trial.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human TLR4, THP-1 monocytes and donor PBMCs
plain_language
The compound can interact with an inflammatory sensor as well as KEAP1.
primary_references
[sulforaphane-p25284333] Suppression of LPS-induced transcription and cytokine secretion by the dietary isothiocyanate sulforaphane. (2014). https://pubmed.ncbi.nlm.nih.gov/25284333/ DOI: 10.1002/mnfr.201400550
tissue_or_cell_type
LPS recognition and cytokine secretion
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 671–682
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant receptor mapping, human cell exposure and ex vivo challenge · source_derived_draft · unverified_draft
### sulforaphane-tlr4-adduct Receptor mapping found sulforaphane adducts at TLR4 C246 and C609 under non-reducing conditions. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The compound can interact with an inflammatory sensor as well as KEAP1. organism: Human TLR4, THP-1 monocytes and donor PBMCs tissue_or_cell_type: LPS recognition and cytokine secretion experimental_model: Recombinant receptor mapping, human cell exposure and ex vivo challenge limitations: Covalent mapping does not establish the sole cause of cytokine effects; not a chronic-disease outcome trial. exposure: Sulforaphane under non-reducing conditions; LPS challenge after ITC exposure evidence_span: {"source_cache": "artifacts/sulforaphane-research/25284333.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0a293f12863f5cfc2d57d74f4acee8c62700e2744a5900643bc23eca85c62be5", "start_char": 0, "end_char": 1494, "text_sha256": "0a293f12863f5cfc2d57d74f4acee8c62700e2744a5900643bc23eca85c62be5"} [sulforaphane-p25284333] Suppression of LPS-induced transcription and cytokine secretion by the dietary isothiocyanate sulforaphane. (2014). https://pubmed.ncbi.nlm.nih.gov/25284333/ DOI: 10.1002/mnfr.201400550
Complete structured claim and evidence
Sulforaphane suppressed LPS-induced cytokine secretion in THP-1 cells and human PBMC experiments.
Sulforaphane / SFN, stereochemistry specified per study → LPS-induced cytokine release in human monocytes or PBMCs source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/25284333.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0a293f12863f5cfc2d57d74f4acee8c62700e2744a5900643bc23eca85c62be5", "start_char": 0, "end_char": 1494, "text_sha256": "0a293f12863f5cfc2d57d74f4acee8c62700e2744a5900643bc23eca85c62be5"}
experimental_model
Recombinant receptor mapping, human cell exposure and ex vivo challenge
exposure
Sulforaphane under non-reducing conditions; LPS challenge after ITC exposure
limitations
Covalent mapping does not establish the sole cause of cytokine effects; not a chronic-disease outcome trial.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human TLR4, THP-1 monocytes and donor PBMCs
plain_language
An inflammatory challenge produced a smaller response in these systems.
primary_references
[sulforaphane-p25284333] Suppression of LPS-induced transcription and cytokine secretion by the dietary isothiocyanate sulforaphane. (2014). https://pubmed.ncbi.nlm.nih.gov/25284333/ DOI: 10.1002/mnfr.201400550
tissue_or_cell_type
LPS recognition and cytokine secretion
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 684–695
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant receptor mapping, human cell exposure and ex vivo challenge · source_derived_draft · unverified_draft
### sulforaphane-lps-response Sulforaphane suppressed LPS-induced cytokine secretion in THP-1 cells and human PBMC experiments. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: An inflammatory challenge produced a smaller response in these systems. organism: Human TLR4, THP-1 monocytes and donor PBMCs tissue_or_cell_type: LPS recognition and cytokine secretion experimental_model: Recombinant receptor mapping, human cell exposure and ex vivo challenge limitations: Covalent mapping does not establish the sole cause of cytokine effects; not a chronic-disease outcome trial. exposure: Sulforaphane under non-reducing conditions; LPS challenge after ITC exposure evidence_span: {"source_cache": "artifacts/sulforaphane-research/25284333.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0a293f12863f5cfc2d57d74f4acee8c62700e2744a5900643bc23eca85c62be5", "start_char": 0, "end_char": 1494, "text_sha256": "0a293f12863f5cfc2d57d74f4acee8c62700e2744a5900643bc23eca85c62be5"} [sulforaphane-p25284333] Suppression of LPS-induced transcription and cytokine secretion by the dietary isothiocyanate sulforaphane. (2014). https://pubmed.ncbi.nlm.nih.gov/25284333/ DOI: 10.1002/mnfr.201400550
Complete structured claim and evidence
Selenite delayed degradation of sulforaphane-induced TXNRD1 mRNA.
Selenite ion → Human TXNRD1 mRNA stability source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/12663510.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "95f1de031ede41aa12f975dff28193dcb426465d4bda94bb84d4e60ef6c292b9", "start_char": 0, "end_char": 1535, "text_sha256": "95f1de031ede41aa12f975dff28193dcb426465d4bda94bb84d4e60ef6c292b9"}
experimental_model
Transcription/translation and inhibitor experiments
exposure
Sulforaphane, sodium selenite, combined treatment and pathway inhibitors
limitations
Cell-culture synergy at specified exposures is not a clinical supplement recommendation; TXNRD1 and TXNRD2 were not interchangeable.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human HepG2 hepatoma cells
plain_language
The message could persist longer when both influences were present.
primary_references
[sulforaphane-p12663510] Synergy between sulforaphane and selenium in the induction of thioredoxin reductase 1 requires both transcriptional and translational modulation. (2003). https://pubmed.ncbi.nlm.nih.gov/12663510/ DOI: 10.1093/carcin/24.3.497
tissue_or_cell_type
Thioredoxin reductase regulation
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 723–734
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Transcription/translation and inhibitor experiments · source_derived_draft · unverified_draft
### sulforaphane-selenite-mrna-stability Selenite delayed degradation of sulforaphane-induced TXNRD1 mRNA. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The message could persist longer when both influences were present. organism: Human HepG2 hepatoma cells tissue_or_cell_type: Thioredoxin reductase regulation experimental_model: Transcription/translation and inhibitor experiments limitations: Cell-culture synergy at specified exposures is not a clinical supplement recommendation; TXNRD1 and TXNRD2 were not interchangeable. exposure: Sulforaphane, sodium selenite, combined treatment and pathway inhibitors evidence_span: {"source_cache": "artifacts/sulforaphane-research/12663510.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "95f1de031ede41aa12f975dff28193dcb426465d4bda94bb84d4e60ef6c292b9", "start_char": 0, "end_char": 1535, "text_sha256": "95f1de031ede41aa12f975dff28193dcb426465d4bda94bb84d4e60ef6c292b9"} [sulforaphane-p12663510] Synergy between sulforaphane and selenium in the induction of thioredoxin reductase 1 requires both transcriptional and translational modulation. (2003). https://pubmed.ncbi.nlm.nih.gov/12663510/ DOI: 10.1093/carcin/24.3.497
Complete structured claim and evidence
Combined sulforaphane and selenite protected HepG2 cells against paraquat-induced death, whereas either alone had little or no protection.
Sulforaphane plus selenite, study-specific combination → HepG2 survival after paraquat challenge source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/12663510.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "95f1de031ede41aa12f975dff28193dcb426465d4bda94bb84d4e60ef6c292b9", "start_char": 0, "end_char": 1535, "text_sha256": "95f1de031ede41aa12f975dff28193dcb426465d4bda94bb84d4e60ef6c292b9"}
experimental_model
Transcription/translation and inhibitor experiments
exposure
Sulforaphane, sodium selenite, combined treatment and pathway inhibitors
limitations
Cell-culture synergy at specified exposures is not a clinical supplement recommendation; TXNRD1 and TXNRD2 were not interchangeable.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human HepG2 hepatoma cells
plain_language
A measured combination effect occurred in this specific injury model.
primary_references
[sulforaphane-p12663510] Synergy between sulforaphane and selenium in the induction of thioredoxin reductase 1 requires both transcriptional and translational modulation. (2003). https://pubmed.ncbi.nlm.nih.gov/12663510/ DOI: 10.1093/carcin/24.3.497
tissue_or_cell_type
Thioredoxin reductase regulation
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 749–760
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Transcription/translation and inhibitor experiments · source_derived_draft · unverified_draft
### sulforaphane-paraquat-protection Combined sulforaphane and selenite protected HepG2 cells against paraquat-induced death, whereas either alone had little or no protection. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: A measured combination effect occurred in this specific injury model. organism: Human HepG2 hepatoma cells tissue_or_cell_type: Thioredoxin reductase regulation experimental_model: Transcription/translation and inhibitor experiments limitations: Cell-culture synergy at specified exposures is not a clinical supplement recommendation; TXNRD1 and TXNRD2 were not interchangeable. exposure: Sulforaphane, sodium selenite, combined treatment and pathway inhibitors evidence_span: {"source_cache": "artifacts/sulforaphane-research/12663510.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "95f1de031ede41aa12f975dff28193dcb426465d4bda94bb84d4e60ef6c292b9", "start_char": 0, "end_char": 1535, "text_sha256": "95f1de031ede41aa12f975dff28193dcb426465d4bda94bb84d4e60ef6c292b9"} [sulforaphane-p12663510] Synergy between sulforaphane and selenium in the induction of thioredoxin reductase 1 requires both transcriptional and translational modulation. (2003). https://pubmed.ncbi.nlm.nih.gov/12663510/ DOI: 10.1093/carcin/24.3.497
Complete structured claim and evidence
BSO pretreatment significantly reduced sulforaphane-induced TXNRD1 mRNA.
Pharmacological inhibition of glutathione synthesis by BSO → Human TXNRD1 mRNA abundance source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/sulforaphane-research/12663510.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "95f1de031ede41aa12f975dff28193dcb426465d4bda94bb84d4e60ef6c292b9", "start_char": 0, "end_char": 1535, "text_sha256": "95f1de031ede41aa12f975dff28193dcb426465d4bda94bb84d4e60ef6c292b9"}
experimental_model
Transcription/translation and inhibitor experiments
exposure
Sulforaphane, sodium selenite, combined treatment and pathway inhibitors
limitations
Cell-culture synergy at specified exposures is not a clinical supplement recommendation; TXNRD1 and TXNRD2 were not interchangeable.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human HepG2 hepatoma cells
plain_language
The signaling response depended on the surrounding glutathione system.
primary_references
[sulforaphane-p12663510] Synergy between sulforaphane and selenium in the induction of thioredoxin reductase 1 requires both transcriptional and translational modulation. (2003). https://pubmed.ncbi.nlm.nih.gov/12663510/ DOI: 10.1093/carcin/24.3.497
tissue_or_cell_type
Thioredoxin reductase regulation
trigger_kind
machinery_impairment Imported condition classification; unverified.
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 762–773
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Transcription/translation and inhibitor experiments · source_derived_draft · unverified_draft
### sulforaphane-gsh-gates-induction BSO pretreatment significantly reduced sulforaphane-induced TXNRD1 mRNA. Condition category: machinery_impairment nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The signaling response depended on the surrounding glutathione system. organism: Human HepG2 hepatoma cells tissue_or_cell_type: Thioredoxin reductase regulation experimental_model: Transcription/translation and inhibitor experiments limitations: Cell-culture synergy at specified exposures is not a clinical supplement recommendation; TXNRD1 and TXNRD2 were not interchangeable. exposure: Sulforaphane, sodium selenite, combined treatment and pathway inhibitors evidence_span: {"source_cache": "artifacts/sulforaphane-research/12663510.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "95f1de031ede41aa12f975dff28193dcb426465d4bda94bb84d4e60ef6c292b9", "start_char": 0, "end_char": 1535, "text_sha256": "95f1de031ede41aa12f975dff28193dcb426465d4bda94bb84d4e60ef6c292b9"} [sulforaphane-p12663510] Synergy between sulforaphane and selenium in the induction of thioredoxin reductase 1 requires both transcriptional and translational modulation. (2003). https://pubmed.ncbi.nlm.nih.gov/12663510/ DOI: 10.1093/carcin/24.3.497
Complete structured claim and evidence
TXNRD1 knockdown lowered survival under combined treatment from 82.4% to 66.5% in the peroxide-challenge assay.
Experimental human TXNRD1 knockdown → Survival after peroxide challenge, model specified source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/sulforaphane-research/26094214.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "de55004b06332873c312c03a18cec65eeb22c1bab6daddf5cde8a7977817567e", "start_char": 0, "end_char": 1568, "text_sha256": "de55004b06332873c312c03a18cec65eeb22c1bab6daddf5cde8a7977817567e"}
experimental_model
Combination treatment and siRNA loss-of-function
exposure
Sulforaphane plus selenium with Nrf2 or TXNRD1 knockdown
limitations
One cell model; survival percentages are assay-specific and not clinical benefit estimates.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human nontransformed CCD841 colonic cells
plain_language
Increasing the signal cannot replace the enzyme that carries out part of the response.
primary_references
[sulforaphane-p26094214] Synergy between sulforaphane and selenium in protection against oxidative damage in colonic CCD841 cells. (2015). https://pubmed.ncbi.nlm.nih.gov/26094214/ DOI: 10.1016/j.nutres.2015.05.011
tissue_or_cell_type
Nrf2/TXNRD1 and peroxide survival
trigger_kind
machinery_impairment Imported condition classification; unverified.
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 775–786
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Combination treatment and siRNA loss-of-function · source_derived_draft · unverified_draft
### sulforaphane-txnrd1-knockdown TXNRD1 knockdown lowered survival under combined treatment from 82.4% to 66.5% in the peroxide-challenge assay. Condition category: machinery_impairment nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Increasing the signal cannot replace the enzyme that carries out part of the response. organism: Human nontransformed CCD841 colonic cells tissue_or_cell_type: Nrf2/TXNRD1 and peroxide survival experimental_model: Combination treatment and siRNA loss-of-function limitations: One cell model; survival percentages are assay-specific and not clinical benefit estimates. exposure: Sulforaphane plus selenium with Nrf2 or TXNRD1 knockdown evidence_span: {"source_cache": "artifacts/sulforaphane-research/26094214.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "de55004b06332873c312c03a18cec65eeb22c1bab6daddf5cde8a7977817567e", "start_char": 0, "end_char": 1568, "text_sha256": "de55004b06332873c312c03a18cec65eeb22c1bab6daddf5cde8a7977817567e"} [sulforaphane-p26094214] Synergy between sulforaphane and selenium in protection against oxidative damage in colonic CCD841 cells. (2015). https://pubmed.ncbi.nlm.nih.gov/26094214/ DOI: 10.1016/j.nutres.2015.05.011
Complete structured claim and evidence
Nrf2 knockdown lowered survival under combined treatment from 82.4% to 51.1%.
Experimental human NFE2L2 knockdown → Survival after peroxide challenge, model specified source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_span
{"source_cache": "artifacts/sulforaphane-research/26094214.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "de55004b06332873c312c03a18cec65eeb22c1bab6daddf5cde8a7977817567e", "start_char": 0, "end_char": 1568, "text_sha256": "de55004b06332873c312c03a18cec65eeb22c1bab6daddf5cde8a7977817567e"}
experimental_model
Combination treatment and siRNA loss-of-function
exposure
Sulforaphane plus selenium with Nrf2 or TXNRD1 knockdown
limitations
One cell model; survival percentages are assay-specific and not clinical benefit estimates.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human nontransformed CCD841 colonic cells
plain_language
The regulator was necessary for much of the observed protection.
primary_references
[sulforaphane-p26094214] Synergy between sulforaphane and selenium in protection against oxidative damage in colonic CCD841 cells. (2015). https://pubmed.ncbi.nlm.nih.gov/26094214/ DOI: 10.1016/j.nutres.2015.05.011
tissue_or_cell_type
Nrf2/TXNRD1 and peroxide survival
trigger_kind
machinery_impairment Imported condition classification; unverified.
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 788–799
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Combination treatment and siRNA loss-of-function · source_derived_draft · unverified_draft
### sulforaphane-nrf2-knockdown Nrf2 knockdown lowered survival under combined treatment from 82.4% to 51.1%. Condition category: machinery_impairment nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The regulator was necessary for much of the observed protection. organism: Human nontransformed CCD841 colonic cells tissue_or_cell_type: Nrf2/TXNRD1 and peroxide survival experimental_model: Combination treatment and siRNA loss-of-function limitations: One cell model; survival percentages are assay-specific and not clinical benefit estimates. exposure: Sulforaphane plus selenium with Nrf2 or TXNRD1 knockdown evidence_span: {"source_cache": "artifacts/sulforaphane-research/26094214.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "de55004b06332873c312c03a18cec65eeb22c1bab6daddf5cde8a7977817567e", "start_char": 0, "end_char": 1568, "text_sha256": "de55004b06332873c312c03a18cec65eeb22c1bab6daddf5cde8a7977817567e"} [sulforaphane-p26094214] Synergy between sulforaphane and selenium in protection against oxidative damage in colonic CCD841 cells. (2015). https://pubmed.ncbi.nlm.nih.gov/26094214/ DOI: 10.1016/j.nutres.2015.05.011
Complete structured claim and evidence
The study reported sulforaphane cytotoxicity IC50 values of 25.1 micromolar in hepatocytes and 56.4 micromolar in HepG2 cells alongside lower-exposure protective experiments.
Sulforaphane / SFN, stereochemistry specified per study → Cultured human hepatocyte viability, preparation specified source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/25683399.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bfaef8428737a984f51d1c91e9f6dddaf1d40a19c8ced9ddd7f6a222a65e450e", "start_char": 0, "end_char": 1707, "text_sha256": "bfaef8428737a984f51d1c91e9f6dddaf1d40a19c8ced9ddd7f6a222a65e450e"}
experimental_model
Enzyme induction, viability and knockdown experiments
exposure
Sulforaphane with or without selenium; peroxide challenge
limitations
Model-specific cytotoxicity; no conversion of culture concentrations into a safe or toxic oral dose.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Immortalized human hepatocytes and HepG2 comparison
plain_language
Exposure and cell type can change whether the effect is protective or harmful.
primary_references
[sulforaphane-p25683399] Synergy between sulforaphane and selenium in the up-regulation of thioredoxin reductase and protection against hydrogen peroxide-induced cell death in human hepatocytes. (2012). https://pubmed.ncbi.nlm.nih.gov/25683399/ DOI: 10.1016/j.foodchem.2012.01.026
tissue_or_cell_type
TXNRD1 response and toxicity
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 801–812
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Enzyme induction, viability and knockdown experiments · source_derived_draft · unverified_draft
### sulforaphane-hepatocyte-toxicity The study reported sulforaphane cytotoxicity IC50 values of 25.1 micromolar in hepatocytes and 56.4 micromolar in HepG2 cells alongside lower-exposure protective experiments. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Exposure and cell type can change whether the effect is protective or harmful. organism: Immortalized human hepatocytes and HepG2 comparison tissue_or_cell_type: TXNRD1 response and toxicity experimental_model: Enzyme induction, viability and knockdown experiments limitations: Model-specific cytotoxicity; no conversion of culture concentrations into a safe or toxic oral dose. exposure: Sulforaphane with or without selenium; peroxide challenge evidence_span: {"source_cache": "artifacts/sulforaphane-research/25683399.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bfaef8428737a984f51d1c91e9f6dddaf1d40a19c8ced9ddd7f6a222a65e450e", "start_char": 0, "end_char": 1707, "text_sha256": "bfaef8428737a984f51d1c91e9f6dddaf1d40a19c8ced9ddd7f6a222a65e450e"} [sulforaphane-p25683399] Synergy between sulforaphane and selenium in the up-regulation of thioredoxin reductase and protection against hydrogen peroxide-induced cell death in human hepatocytes. (2012). https://pubmed.ncbi.nlm.nih.gov/25683399/ DOI: 10.1016/j.foodchem.2012.01.026
Complete structured claim and evidence
The human GCL holoenzyme was more active and less sensitive to glutathione inhibition than its catalytic subunit alone.
Human glutamate-cysteine ligase modifier subunit / GCLM → Human glutamate-cysteine ligase catalytic activity source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/9637733.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4e7a66b2c4a636f70f2a5954ff304e54d4ef0f00055e53bc32ba8ceb9772fbe2", "start_char": 0, "end_char": 1258, "text_sha256": "4e7a66b2c4a636f70f2a5954ff304e54d4ef0f00055e53bc32ba8ceb9772fbe2"}
experimental_model
Purified recombinant subunit/holoenzyme kinetics
exposure
Substrate comparisons and glutathione inhibition
limitations
Baseline enzymology, not a sulforaphane or nutrient-repletion trial.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human GCLC and GCLM expressed in insect cells
plain_language
The modifier subunit changes how the glutathione-building enzyme works.
primary_references
[sulforaphane-p9637733] Expression and characterization of human glutamate-cysteine ligase. (1998). https://pubmed.ncbi.nlm.nih.gov/9637733/ DOI: 10.1006/abbi.1998.0676
tissue_or_cell_type
Glutathione synthesis first-step enzyme
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 814–825
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified recombinant subunit/holoenzyme kinetics · source_derived_draft · unverified_draft
### sulforaphane-gclm-activity The human GCL holoenzyme was more active and less sensitive to glutathione inhibition than its catalytic subunit alone. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The modifier subunit changes how the glutathione-building enzyme works. organism: Human GCLC and GCLM expressed in insect cells tissue_or_cell_type: Glutathione synthesis first-step enzyme experimental_model: Purified recombinant subunit/holoenzyme kinetics limitations: Baseline enzymology, not a sulforaphane or nutrient-repletion trial. exposure: Substrate comparisons and glutathione inhibition evidence_span: {"source_cache": "artifacts/sulforaphane-research/9637733.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4e7a66b2c4a636f70f2a5954ff304e54d4ef0f00055e53bc32ba8ceb9772fbe2", "start_char": 0, "end_char": 1258, "text_sha256": "4e7a66b2c4a636f70f2a5954ff304e54d4ef0f00055e53bc32ba8ceb9772fbe2"} [sulforaphane-p9637733] Expression and characterization of human glutamate-cysteine ligase. (1998). https://pubmed.ncbi.nlm.nih.gov/9637733/ DOI: 10.1006/abbi.1998.0676
Complete structured claim and evidence
Glutathione inhibited both human GCLC and GCL holoenzyme, with greater sensitivity of GCLC alone.
GSH → Human glutamate-cysteine ligase catalytic activity source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/9637733.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4e7a66b2c4a636f70f2a5954ff304e54d4ef0f00055e53bc32ba8ceb9772fbe2", "start_char": 0, "end_char": 1258, "text_sha256": "4e7a66b2c4a636f70f2a5954ff304e54d4ef0f00055e53bc32ba8ceb9772fbe2"}
experimental_model
Purified recombinant subunit/holoenzyme kinetics
exposure
Substrate comparisons and glutathione inhibition
limitations
Baseline enzymology, not a sulforaphane or nutrient-repletion trial.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human GCLC and GCLM expressed in insect cells
plain_language
The product feeds back on the machinery that makes more of it.
primary_references
[sulforaphane-p9637733] Expression and characterization of human glutamate-cysteine ligase. (1998). https://pubmed.ncbi.nlm.nih.gov/9637733/ DOI: 10.1006/abbi.1998.0676
tissue_or_cell_type
Glutathione synthesis first-step enzyme
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 827–838
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified recombinant subunit/holoenzyme kinetics · source_derived_draft · unverified_draft
### sulforaphane-gsh-feedback Glutathione inhibited both human GCLC and GCL holoenzyme, with greater sensitivity of GCLC alone. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The product feeds back on the machinery that makes more of it. organism: Human GCLC and GCLM expressed in insect cells tissue_or_cell_type: Glutathione synthesis first-step enzyme experimental_model: Purified recombinant subunit/holoenzyme kinetics limitations: Baseline enzymology, not a sulforaphane or nutrient-repletion trial. exposure: Substrate comparisons and glutathione inhibition evidence_span: {"source_cache": "artifacts/sulforaphane-research/9637733.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4e7a66b2c4a636f70f2a5954ff304e54d4ef0f00055e53bc32ba8ceb9772fbe2", "start_char": 0, "end_char": 1258, "text_sha256": "4e7a66b2c4a636f70f2a5954ff304e54d4ef0f00055e53bc32ba8ceb9772fbe2"} [sulforaphane-p9637733] Expression and characterization of human glutamate-cysteine ligase. (1998). https://pubmed.ncbi.nlm.nih.gov/9637733/ DOI: 10.1006/abbi.1998.0676
Complete structured claim and evidence
Glutamate-cysteine ligase joins glutamate and cysteine to form gamma-glutamylcysteine in the first glutathione-synthesis step.
Human glutamate-cysteine ligase catalytic subunit / GCLC → Gamma-glutamylcysteine source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/30581542.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "77cf6674cf9b9bc140a228588a53c937966fd3a67397c1c4970221c5cc58a0b1", "start_char": 762, "end_char": 1092, "text_sha256": "927fa13b085700c20b578ecabc7c8c17a66ea4600b90809e3061d12bcaea3849"}
experimental_model
Human enzyme mutagenesis, kinetics and molecular dynamics
exposure
S-loop variants; established biosynthetic reactions described in the introduction
limitations
Reaction descriptions are background chemistry in a primary enzyme paper, not evidence that sulforaphane corrects inherited GSS deficiency.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human GSS
plain_language
The induced machinery still needs its amino-acid building blocks.
primary_references
[sulforaphane-p30581542] Genetic Mutations in the S-loop of Human Glutathione Synthetase: Links Between Substrate Binding, Active Site Structure and Allostery. (2019). https://pubmed.ncbi.nlm.nih.gov/30581542/ DOI: 10.1016/j.csbj.2018.11.008
tissue_or_cell_type
Glutathione synthesis and substrate binding
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 840–851
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human enzyme mutagenesis, kinetics and molecular dynamics · source_derived_draft · unverified_draft
### sulforaphane-gcl-first-step Glutamate-cysteine ligase joins glutamate and cysteine to form gamma-glutamylcysteine in the first glutathione-synthesis step. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The induced machinery still needs its amino-acid building blocks. organism: Human GSS tissue_or_cell_type: Glutathione synthesis and substrate binding experimental_model: Human enzyme mutagenesis, kinetics and molecular dynamics limitations: Reaction descriptions are background chemistry in a primary enzyme paper, not evidence that sulforaphane corrects inherited GSS deficiency. exposure: S-loop variants; established biosynthetic reactions described in the introduction evidence_span: {"source_cache": "artifacts/sulforaphane-research/30581542.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "77cf6674cf9b9bc140a228588a53c937966fd3a67397c1c4970221c5cc58a0b1", "start_char": 762, "end_char": 1092, "text_sha256": "927fa13b085700c20b578ecabc7c8c17a66ea4600b90809e3061d12bcaea3849"} [sulforaphane-p30581542] Genetic Mutations in the S-loop of Human Glutathione Synthetase: Links Between Substrate Binding, Active Site Structure and Allostery. (2019). https://pubmed.ncbi.nlm.nih.gov/30581542/ DOI: 10.1016/j.csbj.2018.11.008
Complete structured claim and evidence
Human GSS joins gamma-glutamylcysteine and glycine in an ATP-dependent reaction to form glutathione.
Human glutathione synthetase / GSS → GSH source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/30581542.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "77cf6674cf9b9bc140a228588a53c937966fd3a67397c1c4970221c5cc58a0b1", "start_char": 923, "end_char": 1092, "text_sha256": "bed9ef1323b513b1e31b65277f28b935ddf0c9b0c83cbe9ee9f827f97806846c"}
experimental_model
Human enzyme mutagenesis, kinetics and molecular dynamics
exposure
S-loop variants; established biosynthetic reactions described in the introduction
limitations
Reaction descriptions are background chemistry in a primary enzyme paper, not evidence that sulforaphane corrects inherited GSS deficiency.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human GSS
plain_language
A second enzyme, glycine and energy complete the molecule.
primary_references
[sulforaphane-p30581542] Genetic Mutations in the S-loop of Human Glutathione Synthetase: Links Between Substrate Binding, Active Site Structure and Allostery. (2019). https://pubmed.ncbi.nlm.nih.gov/30581542/ DOI: 10.1016/j.csbj.2018.11.008
tissue_or_cell_type
Glutathione synthesis and substrate binding
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 853–864
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human enzyme mutagenesis, kinetics and molecular dynamics · source_derived_draft · unverified_draft
### sulforaphane-gss-second-step Human GSS joins gamma-glutamylcysteine and glycine in an ATP-dependent reaction to form glutathione. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: A second enzyme, glycine and energy complete the molecule. organism: Human GSS tissue_or_cell_type: Glutathione synthesis and substrate binding experimental_model: Human enzyme mutagenesis, kinetics and molecular dynamics limitations: Reaction descriptions are background chemistry in a primary enzyme paper, not evidence that sulforaphane corrects inherited GSS deficiency. exposure: S-loop variants; established biosynthetic reactions described in the introduction evidence_span: {"source_cache": "artifacts/sulforaphane-research/30581542.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "77cf6674cf9b9bc140a228588a53c937966fd3a67397c1c4970221c5cc58a0b1", "start_char": 923, "end_char": 1092, "text_sha256": "bed9ef1323b513b1e31b65277f28b935ddf0c9b0c83cbe9ee9f827f97806846c"} [sulforaphane-p30581542] Genetic Mutations in the S-loop of Human Glutathione Synthetase: Links Between Substrate Binding, Active Site Structure and Allostery. (2019). https://pubmed.ncbi.nlm.nih.gov/30581542/ DOI: 10.1016/j.csbj.2018.11.008
Complete structured claim and evidence
The human GSS active sites bind ATP and associated magnesium for peptide-bond formation.
Mg2+ → Human glutathione synthetase / GSS source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/30581542.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "77cf6674cf9b9bc140a228588a53c937966fd3a67397c1c4970221c5cc58a0b1", "start_char": 1428, "end_char": 1604, "text_sha256": "a5d33b10162adea5e60fcff380eabf7e272963711914ea0e8e7091ad8c79df21"}
experimental_model
Human enzyme mutagenesis, kinetics and molecular dynamics
exposure
S-loop variants; established biosynthetic reactions described in the introduction
limitations
Reaction descriptions are background chemistry in a primary enzyme paper, not evidence that sulforaphane corrects inherited GSS deficiency.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human GSS
plain_language
The induced glutathione pathway still depends on ordinary enzyme cofactors.
primary_references
[sulforaphane-p30581542] Genetic Mutations in the S-loop of Human Glutathione Synthetase: Links Between Substrate Binding, Active Site Structure and Allostery. (2019). https://pubmed.ncbi.nlm.nih.gov/30581542/ DOI: 10.1016/j.csbj.2018.11.008
tissue_or_cell_type
Glutathione synthesis and substrate binding
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 866–877
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human enzyme mutagenesis, kinetics and molecular dynamics · source_derived_draft · unverified_draft
### sulforaphane-gss-magnesium The human GSS active sites bind ATP and associated magnesium for peptide-bond formation. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The induced glutathione pathway still depends on ordinary enzyme cofactors. organism: Human GSS tissue_or_cell_type: Glutathione synthesis and substrate binding experimental_model: Human enzyme mutagenesis, kinetics and molecular dynamics limitations: Reaction descriptions are background chemistry in a primary enzyme paper, not evidence that sulforaphane corrects inherited GSS deficiency. exposure: S-loop variants; established biosynthetic reactions described in the introduction evidence_span: {"source_cache": "artifacts/sulforaphane-research/30581542.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "77cf6674cf9b9bc140a228588a53c937966fd3a67397c1c4970221c5cc58a0b1", "start_char": 1428, "end_char": 1604, "text_sha256": "a5d33b10162adea5e60fcff380eabf7e272963711914ea0e8e7091ad8c79df21"} [sulforaphane-p30581542] Genetic Mutations in the S-loop of Human Glutathione Synthetase: Links Between Substrate Binding, Active Site Structure and Allostery. (2019). https://pubmed.ncbi.nlm.nih.gov/30581542/ DOI: 10.1016/j.csbj.2018.11.008
Complete structured claim and evidence
Sulforaphane increased G6PD expression in the fibroblast study.
Sulforaphane / SFN, stereochemistry specified per study → Glucose-6-phosphate dehydrogenase / G6PD source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/30595796.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "aa7d5e0ef15224906eb42eb49309439c966c30310740dbdea9553b76b2f91274", "start_char": 0, "end_char": 2097, "text_sha256": "aa7d5e0ef15224906eb42eb49309439c966c30310740dbdea9553b76b2f91274"}
experimental_model
Replicative culture and metabolic/gene-expression measurements
exposure
Sulforaphane treatment during serial culture
limitations
Cell-culture senescence is not human longevity; expression is not necessarily flux.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human MRC-5 and BJ fibroblasts
plain_language
The response includes machinery connected to the cellular reducing-power supply.
primary_references
[sulforaphane-p30595796] Sulforaphane Delays Fibroblast Senescence by Curbing Cellular Glucose Uptake, Increased Glycolysis, and Oxidative Damage. (2018). https://pubmed.ncbi.nlm.nih.gov/30595796/ DOI: 10.1155/2018/5642148
tissue_or_cell_type
Glucose handling, antioxidant response and senescence
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 879–890
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Replicative culture and metabolic/gene-expression measurements · source_derived_draft · unverified_draft
### sulforaphane-g6pd-expression Sulforaphane increased G6PD expression in the fibroblast study. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The response includes machinery connected to the cellular reducing-power supply. organism: Human MRC-5 and BJ fibroblasts tissue_or_cell_type: Glucose handling, antioxidant response and senescence experimental_model: Replicative culture and metabolic/gene-expression measurements limitations: Cell-culture senescence is not human longevity; expression is not necessarily flux. exposure: Sulforaphane treatment during serial culture evidence_span: {"source_cache": "artifacts/sulforaphane-research/30595796.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "aa7d5e0ef15224906eb42eb49309439c966c30310740dbdea9553b76b2f91274", "start_char": 0, "end_char": 2097, "text_sha256": "aa7d5e0ef15224906eb42eb49309439c966c30310740dbdea9553b76b2f91274"} [sulforaphane-p30595796] Sulforaphane Delays Fibroblast Senescence by Curbing Cellular Glucose Uptake, Increased Glycolysis, and Oxidative Damage. (2018). https://pubmed.ncbi.nlm.nih.gov/30595796/ DOI: 10.1155/2018/5642148
Complete structured claim and evidence
Sulforaphane increased TXNIP expression alongside reduced glucose entry in the studied fibroblasts.
Sulforaphane / SFN, stereochemistry specified per study → TXNIP source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/30595796.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "aa7d5e0ef15224906eb42eb49309439c966c30310740dbdea9553b76b2f91274", "start_char": 0, "end_char": 2097, "text_sha256": "aa7d5e0ef15224906eb42eb49309439c966c30310740dbdea9553b76b2f91274"}
experimental_model
Replicative culture and metabolic/gene-expression measurements
exposure
Sulforaphane treatment during serial culture
limitations
Cell-culture senescence is not human longevity; expression is not necessarily flux.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human MRC-5 and BJ fibroblasts
plain_language
A regulatory protein can change how much fuel enters the cell.
primary_references
[sulforaphane-p30595796] Sulforaphane Delays Fibroblast Senescence by Curbing Cellular Glucose Uptake, Increased Glycolysis, and Oxidative Damage. (2018). https://pubmed.ncbi.nlm.nih.gov/30595796/ DOI: 10.1155/2018/5642148
tissue_or_cell_type
Glucose handling, antioxidant response and senescence
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 892–903
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Replicative culture and metabolic/gene-expression measurements · source_derived_draft · unverified_draft
### sulforaphane-txnip-expression Sulforaphane increased TXNIP expression alongside reduced glucose entry in the studied fibroblasts. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: A regulatory protein can change how much fuel enters the cell. organism: Human MRC-5 and BJ fibroblasts tissue_or_cell_type: Glucose handling, antioxidant response and senescence experimental_model: Replicative culture and metabolic/gene-expression measurements limitations: Cell-culture senescence is not human longevity; expression is not necessarily flux. exposure: Sulforaphane treatment during serial culture evidence_span: {"source_cache": "artifacts/sulforaphane-research/30595796.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "aa7d5e0ef15224906eb42eb49309439c966c30310740dbdea9553b76b2f91274", "start_char": 0, "end_char": 2097, "text_sha256": "aa7d5e0ef15224906eb42eb49309439c966c30310740dbdea9553b76b2f91274"} [sulforaphane-p30595796] Sulforaphane Delays Fibroblast Senescence by Curbing Cellular Glucose Uptake, Increased Glycolysis, and Oxidative Damage. (2018). https://pubmed.ncbi.nlm.nih.gov/30595796/ DOI: 10.1155/2018/5642148
Complete structured claim and evidence
Sulforaphane lowered HK2 expression associated with reduced entry of glucose into glycolysis.
Sulforaphane / SFN, stereochemistry specified per study → Human hexokinase 2 / HK2 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/30595796.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "aa7d5e0ef15224906eb42eb49309439c966c30310740dbdea9553b76b2f91274", "start_char": 0, "end_char": 2097, "text_sha256": "aa7d5e0ef15224906eb42eb49309439c966c30310740dbdea9553b76b2f91274"}
experimental_model
Replicative culture and metabolic/gene-expression measurements
exposure
Sulforaphane treatment during serial culture
limitations
Cell-culture senescence is not human longevity; expression is not necessarily flux.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human MRC-5 and BJ fibroblasts
plain_language
The metabolic response included an early glucose-processing enzyme.
primary_references
[sulforaphane-p30595796] Sulforaphane Delays Fibroblast Senescence by Curbing Cellular Glucose Uptake, Increased Glycolysis, and Oxidative Damage. (2018). https://pubmed.ncbi.nlm.nih.gov/30595796/ DOI: 10.1155/2018/5642148
tissue_or_cell_type
Glucose handling, antioxidant response and senescence
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 905–916
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Replicative culture and metabolic/gene-expression measurements · source_derived_draft · unverified_draft
### sulforaphane-hk2-expression Sulforaphane lowered HK2 expression associated with reduced entry of glucose into glycolysis. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The metabolic response included an early glucose-processing enzyme. organism: Human MRC-5 and BJ fibroblasts tissue_or_cell_type: Glucose handling, antioxidant response and senescence experimental_model: Replicative culture and metabolic/gene-expression measurements limitations: Cell-culture senescence is not human longevity; expression is not necessarily flux. exposure: Sulforaphane treatment during serial culture evidence_span: {"source_cache": "artifacts/sulforaphane-research/30595796.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "aa7d5e0ef15224906eb42eb49309439c966c30310740dbdea9553b76b2f91274", "start_char": 0, "end_char": 2097, "text_sha256": "aa7d5e0ef15224906eb42eb49309439c966c30310740dbdea9553b76b2f91274"} [sulforaphane-p30595796] Sulforaphane Delays Fibroblast Senescence by Curbing Cellular Glucose Uptake, Increased Glycolysis, and Oxidative Damage. (2018). https://pubmed.ncbi.nlm.nih.gov/30595796/ DOI: 10.1155/2018/5642148
Complete structured claim and evidence
Sulforaphane delayed replicative senescence of cultured MRC-5 and BJ fibroblasts.
Sulforaphane / SFN, stereochemistry specified per study → Replicative senescence of cultured human fibroblasts source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/30595796.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "aa7d5e0ef15224906eb42eb49309439c966c30310740dbdea9553b76b2f91274", "start_char": 0, "end_char": 2097, "text_sha256": "aa7d5e0ef15224906eb42eb49309439c966c30310740dbdea9553b76b2f91274"}
experimental_model
Replicative culture and metabolic/gene-expression measurements
exposure
Sulforaphane treatment during serial culture
limitations
Cell-culture senescence is not human longevity; expression is not necessarily flux.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human MRC-5 and BJ fibroblasts
plain_language
The cells reached the study-defined senescent state later; human lifespan was not tested.
primary_references
[sulforaphane-p30595796] Sulforaphane Delays Fibroblast Senescence by Curbing Cellular Glucose Uptake, Increased Glycolysis, and Oxidative Damage. (2018). https://pubmed.ncbi.nlm.nih.gov/30595796/ DOI: 10.1155/2018/5642148
tissue_or_cell_type
Glucose handling, antioxidant response and senescence
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 918–929
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Replicative culture and metabolic/gene-expression measurements · source_derived_draft · unverified_draft
### sulforaphane-senescence-delay Sulforaphane delayed replicative senescence of cultured MRC-5 and BJ fibroblasts. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The cells reached the study-defined senescent state later; human lifespan was not tested. organism: Human MRC-5 and BJ fibroblasts tissue_or_cell_type: Glucose handling, antioxidant response and senescence experimental_model: Replicative culture and metabolic/gene-expression measurements limitations: Cell-culture senescence is not human longevity; expression is not necessarily flux. exposure: Sulforaphane treatment during serial culture evidence_span: {"source_cache": "artifacts/sulforaphane-research/30595796.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "aa7d5e0ef15224906eb42eb49309439c966c30310740dbdea9553b76b2f91274", "start_char": 0, "end_char": 2097, "text_sha256": "aa7d5e0ef15224906eb42eb49309439c966c30310740dbdea9553b76b2f91274"} [sulforaphane-p30595796] Sulforaphane Delays Fibroblast Senescence by Curbing Cellular Glucose Uptake, Increased Glycolysis, and Oxidative Damage. (2018). https://pubmed.ncbi.nlm.nih.gov/30595796/ DOI: 10.1155/2018/5642148
Complete structured claim and evidence
Sulforaphane increased GCLM gene expression in early-passage nonsenescent MRC-5 fibroblasts.
Sulforaphane / SFN, stereochemistry specified per study → Human glutamate-cysteine ligase modifier subunit / GCLM source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/30595796.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "13f25a5ca61ca9bdf80d4b24878682c90b414a5718a73b6a5b86ff20a9673279", "start_char": 14986, "end_char": 15205, "text_sha256": "c8a5b844826129e5cff61e4e19c0eb34f04a29a8feb8ced52a567eae1585d935"}
experimental_model
Replicative culture and metabolic/gene-expression measurements
exposure
Sulforaphane treatment during serial culture
limitations
Cell-culture senescence is not human longevity; expression is not necessarily flux.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human MRC-5 and BJ fibroblasts
plain_language
The response includes this separately identified defense-system protein.
primary_references
[sulforaphane-p30595796] Sulforaphane Delays Fibroblast Senescence by Curbing Cellular Glucose Uptake, Increased Glycolysis, and Oxidative Damage. (2018). https://pubmed.ncbi.nlm.nih.gov/30595796/ DOI: 10.1155/2018/5642148
tissue_or_cell_type
Glucose handling, antioxidant response and senescence
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 931–942
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Replicative culture and metabolic/gene-expression measurements · source_derived_draft · unverified_draft
### sulforaphane-gclm-induction Sulforaphane increased GCLM gene expression in early-passage nonsenescent MRC-5 fibroblasts. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The response includes this separately identified defense-system protein. organism: Human MRC-5 and BJ fibroblasts tissue_or_cell_type: Glucose handling, antioxidant response and senescence experimental_model: Replicative culture and metabolic/gene-expression measurements limitations: Cell-culture senescence is not human longevity; expression is not necessarily flux. exposure: Sulforaphane treatment during serial culture evidence_span: {"source_cache": "artifacts/sulforaphane-research/30595796.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "13f25a5ca61ca9bdf80d4b24878682c90b414a5718a73b6a5b86ff20a9673279", "start_char": 14986, "end_char": 15205, "text_sha256": "c8a5b844826129e5cff61e4e19c0eb34f04a29a8feb8ced52a567eae1585d935"} [sulforaphane-p30595796] Sulforaphane Delays Fibroblast Senescence by Curbing Cellular Glucose Uptake, Increased Glycolysis, and Oxidative Damage. (2018). https://pubmed.ncbi.nlm.nih.gov/30595796/ DOI: 10.1155/2018/5642148
Complete structured claim and evidence
Sulforaphane increased GSR gene expression in early-passage nonsenescent MRC-5 fibroblasts.
Sulforaphane / SFN, stereochemistry specified per study → Glutathione reductase / GSR source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/30595796.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "13f25a5ca61ca9bdf80d4b24878682c90b414a5718a73b6a5b86ff20a9673279", "start_char": 14986, "end_char": 15205, "text_sha256": "c8a5b844826129e5cff61e4e19c0eb34f04a29a8feb8ced52a567eae1585d935"}
experimental_model
Replicative culture and metabolic/gene-expression measurements
exposure
Sulforaphane treatment during serial culture
limitations
Cell-culture senescence is not human longevity; expression is not necessarily flux.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human MRC-5 and BJ fibroblasts
plain_language
The response includes this separately identified defense-system protein.
primary_references
[sulforaphane-p30595796] Sulforaphane Delays Fibroblast Senescence by Curbing Cellular Glucose Uptake, Increased Glycolysis, and Oxidative Damage. (2018). https://pubmed.ncbi.nlm.nih.gov/30595796/ DOI: 10.1155/2018/5642148
tissue_or_cell_type
Glucose handling, antioxidant response and senescence
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 944–955
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Replicative culture and metabolic/gene-expression measurements · source_derived_draft · unverified_draft
### sulforaphane-gsr-induction Sulforaphane increased GSR gene expression in early-passage nonsenescent MRC-5 fibroblasts. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The response includes this separately identified defense-system protein. organism: Human MRC-5 and BJ fibroblasts tissue_or_cell_type: Glucose handling, antioxidant response and senescence experimental_model: Replicative culture and metabolic/gene-expression measurements limitations: Cell-culture senescence is not human longevity; expression is not necessarily flux. exposure: Sulforaphane treatment during serial culture evidence_span: {"source_cache": "artifacts/sulforaphane-research/30595796.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "13f25a5ca61ca9bdf80d4b24878682c90b414a5718a73b6a5b86ff20a9673279", "start_char": 14986, "end_char": 15205, "text_sha256": "c8a5b844826129e5cff61e4e19c0eb34f04a29a8feb8ced52a567eae1585d935"} [sulforaphane-p30595796] Sulforaphane Delays Fibroblast Senescence by Curbing Cellular Glucose Uptake, Increased Glycolysis, and Oxidative Damage. (2018). https://pubmed.ncbi.nlm.nih.gov/30595796/ DOI: 10.1155/2018/5642148
Complete structured claim and evidence
Sulforaphane increased HMOX1 gene expression in early-passage nonsenescent MRC-5 fibroblasts.
Sulforaphane / SFN, stereochemistry specified per study → Human heme oxygenase 1 / HMOX1 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/30595796.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "13f25a5ca61ca9bdf80d4b24878682c90b414a5718a73b6a5b86ff20a9673279", "start_char": 14986, "end_char": 15205, "text_sha256": "c8a5b844826129e5cff61e4e19c0eb34f04a29a8feb8ced52a567eae1585d935"}
experimental_model
Replicative culture and metabolic/gene-expression measurements
exposure
Sulforaphane treatment during serial culture
limitations
Cell-culture senescence is not human longevity; expression is not necessarily flux.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human MRC-5 and BJ fibroblasts
plain_language
The response includes this separately identified defense-system protein.
primary_references
[sulforaphane-p30595796] Sulforaphane Delays Fibroblast Senescence by Curbing Cellular Glucose Uptake, Increased Glycolysis, and Oxidative Damage. (2018). https://pubmed.ncbi.nlm.nih.gov/30595796/ DOI: 10.1155/2018/5642148
tissue_or_cell_type
Glucose handling, antioxidant response and senescence
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 957–968
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Replicative culture and metabolic/gene-expression measurements · source_derived_draft · unverified_draft
### sulforaphane-hmox1-induction Sulforaphane increased HMOX1 gene expression in early-passage nonsenescent MRC-5 fibroblasts. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The response includes this separately identified defense-system protein. organism: Human MRC-5 and BJ fibroblasts tissue_or_cell_type: Glucose handling, antioxidant response and senescence experimental_model: Replicative culture and metabolic/gene-expression measurements limitations: Cell-culture senescence is not human longevity; expression is not necessarily flux. exposure: Sulforaphane treatment during serial culture evidence_span: {"source_cache": "artifacts/sulforaphane-research/30595796.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "13f25a5ca61ca9bdf80d4b24878682c90b414a5718a73b6a5b86ff20a9673279", "start_char": 14986, "end_char": 15205, "text_sha256": "c8a5b844826129e5cff61e4e19c0eb34f04a29a8feb8ced52a567eae1585d935"} [sulforaphane-p30595796] Sulforaphane Delays Fibroblast Senescence by Curbing Cellular Glucose Uptake, Increased Glycolysis, and Oxidative Damage. (2018). https://pubmed.ncbi.nlm.nih.gov/30595796/ DOI: 10.1155/2018/5642148
Complete structured claim and evidence
In the broccoli meal study, estimated sulforaphane bioavailability was 37% raw versus 3.4% cooked, with plasma peaks at 1.6 versus 6 hours.
Broccoli food preparation, cooking conditions specified per study → Systemic sulforaphane exposure measured by study-specific biomarkers source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/18950181.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ef43f16e111c240c46a1cc958ef8777a466694e04916e7c96ffe6bf7047c826c", "start_char": 0, "end_char": 937, "text_sha256": "ef43f16e111c240c46a1cc958ef8777a466694e04916e7c96ffe6bf7047c826c"}
experimental_model
Randomized open crossover food trial
exposure
200 g crushed raw versus cooked broccoli with a meal
limitations
Small food experiment; processing-specific exposure, not a long-term health outcome.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human, eight men
plain_language
The preparation changed both the amount and timing of exposure.
primary_references
[sulforaphane-p18950181] Bioavailability and kinetics of sulforaphane in humans after consumption of cooked versus raw broccoli. (2008). https://pubmed.ncbi.nlm.nih.gov/18950181/ DOI: 10.1021/jf801989e
tissue_or_cell_type
Blood and urinary exposure
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 970–981
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized open crossover food trial · source_derived_draft · unverified_draft
### sulforaphane-raw-cooked In the broccoli meal study, estimated sulforaphane bioavailability was 37% raw versus 3.4% cooked, with plasma peaks at 1.6 versus 6 hours. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The preparation changed both the amount and timing of exposure. organism: Human, eight men tissue_or_cell_type: Blood and urinary exposure experimental_model: Randomized open crossover food trial limitations: Small food experiment; processing-specific exposure, not a long-term health outcome. exposure: 200 g crushed raw versus cooked broccoli with a meal evidence_span: {"source_cache": "artifacts/sulforaphane-research/18950181.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ef43f16e111c240c46a1cc958ef8777a466694e04916e7c96ffe6bf7047c826c", "start_char": 0, "end_char": 937, "text_sha256": "ef43f16e111c240c46a1cc958ef8777a466694e04916e7c96ffe6bf7047c826c"} [sulforaphane-p18950181] Bioavailability and kinetics of sulforaphane in humans after consumption of cooked versus raw broccoli. (2008). https://pubmed.ncbi.nlm.nih.gov/18950181/ DOI: 10.1021/jf801989e
Complete structured claim and evidence
Adding mustard powder increased mean urinary SFN-NAC from 9.8 to 44.7 micromol per gram creatinine after cooked broccoli.
Mustard seed myrosinase preparation, study-specific → Urinary sulforaphane and conjugates, assay specified source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/29806738.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "f6b9a289e09015264ee781be4b765486c80783805e5fa5bdb23361e8740fdc01", "start_char": 0, "end_char": 1324, "text_sha256": "f6b9a289e09015264ee781be4b765486c80783805e5fa5bdb23361e8740fdc01"}
experimental_model
Randomized crossover meal study
exposure
200 g cooked broccoli with or without 1 g brown mustard powder
limitations
Urinary SFN-NAC is an exposure marker; study-specific meal is not a guaranteed product conversion factor.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human, 12 healthy adults
plain_language
Adding an active plant enzyme source increased measured exposure.
primary_references
[sulforaphane-p29806738] Supplementation of the Diet by Exogenous Myrosinase via Mustard Seeds to Increase the Bioavailability of Sulforaphane in Healthy Human Subjects after the Consumption of Cooked Broccoli. (2018). https://pubmed.ncbi.nlm.nih.gov/29806738/ DOI: 10.1002/mnfr.201700980
tissue_or_cell_type
Urinary SFN-NAC
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 983–994
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized crossover meal study · source_derived_draft · unverified_draft
### sulforaphane-mustard-food Adding mustard powder increased mean urinary SFN-NAC from 9.8 to 44.7 micromol per gram creatinine after cooked broccoli. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Adding an active plant enzyme source increased measured exposure. organism: Human, 12 healthy adults tissue_or_cell_type: Urinary SFN-NAC experimental_model: Randomized crossover meal study limitations: Urinary SFN-NAC is an exposure marker; study-specific meal is not a guaranteed product conversion factor. exposure: 200 g cooked broccoli with or without 1 g brown mustard powder evidence_span: {"source_cache": "artifacts/sulforaphane-research/29806738.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "f6b9a289e09015264ee781be4b765486c80783805e5fa5bdb23361e8740fdc01", "start_char": 0, "end_char": 1324, "text_sha256": "f6b9a289e09015264ee781be4b765486c80783805e5fa5bdb23361e8740fdc01"} [sulforaphane-p29806738] Supplementation of the Diet by Exogenous Myrosinase via Mustard Seeds to Increase the Bioavailability of Sulforaphane in Healthy Human Subjects after the Consumption of Cooked Broccoli. (2018). https://pubmed.ncbi.nlm.nih.gov/29806738/ DOI: 10.1002/mnfr.201700980
Complete structured claim and evidence
GSTP1-1 expression alone accelerated sulforaphane/conjugate accumulation and increased ARE reporter induction.
Human glutathione S-transferase P1 / GSTP1 → Intracellular sulforaphane plus glutathione-conjugate accumulation source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/18204073.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0fcd98974f9fe12b2ca7c4326f94eddf4f20de4ac2ae6fdebb64de0efb1d8be9", "start_char": 0, "end_char": 1894, "text_sha256": "0fcd98974f9fe12b2ca7c4326f94eddf4f20de4ac2ae6fdebb64de0efb1d8be9"}
experimental_model
Transgenic transporter/enzyme comparison
exposure
Sulforaphane; GSH depletion control
limitations
Engineered cancer cells; enzyme expression and efflux can have opposing effects without being a scientific contradiction.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human MCF7 cells with GSTP1 and/or MRP1
plain_language
Conjugation can initially retain the exposure inside cells.
primary_references
[sulforaphane-p18204073] Expression of MRP1 and GSTP1-1 modulate the acute cellular response to treatment with the chemopreventive isothiocyanate, sulforaphane. (2008). https://pubmed.ncbi.nlm.nih.gov/18204073/ DOI: 10.1093/carcin/bgn013
tissue_or_cell_type
Intracellular retention, ARE induction and Nrf2 persistence
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1009–1020
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Transgenic transporter/enzyme comparison · source_derived_draft · unverified_draft
### sulforaphane-gstp-retention GSTP1-1 expression alone accelerated sulforaphane/conjugate accumulation and increased ARE reporter induction. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Conjugation can initially retain the exposure inside cells. organism: Human MCF7 cells with GSTP1 and/or MRP1 tissue_or_cell_type: Intracellular retention, ARE induction and Nrf2 persistence experimental_model: Transgenic transporter/enzyme comparison limitations: Engineered cancer cells; enzyme expression and efflux can have opposing effects without being a scientific contradiction. exposure: Sulforaphane; GSH depletion control evidence_span: {"source_cache": "artifacts/sulforaphane-research/18204073.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0fcd98974f9fe12b2ca7c4326f94eddf4f20de4ac2ae6fdebb64de0efb1d8be9", "start_char": 0, "end_char": 1894, "text_sha256": "0fcd98974f9fe12b2ca7c4326f94eddf4f20de4ac2ae6fdebb64de0efb1d8be9"} [sulforaphane-p18204073] Expression of MRP1 and GSTP1-1 modulate the acute cellular response to treatment with the chemopreventive isothiocyanate, sulforaphane. (2008). https://pubmed.ncbi.nlm.nih.gov/18204073/ DOI: 10.1093/carcin/bgn013
Complete structured claim and evidence
MRP1 expression reduced intracellular sulforaphane/conjugate accumulation and attenuated ARE-dependent responses.
Human multidrug resistance-associated protein 1 / ABCC1 / MRP1 → Intracellular sulforaphane plus glutathione-conjugate accumulation source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/18204073.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0fcd98974f9fe12b2ca7c4326f94eddf4f20de4ac2ae6fdebb64de0efb1d8be9", "start_char": 0, "end_char": 1894, "text_sha256": "0fcd98974f9fe12b2ca7c4326f94eddf4f20de4ac2ae6fdebb64de0efb1d8be9"}
experimental_model
Transgenic transporter/enzyme comparison
exposure
Sulforaphane; GSH depletion control
limitations
Engineered cancer cells; enzyme expression and efflux can have opposing effects without being a scientific contradiction.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human MCF7 cells with GSTP1 and/or MRP1
plain_language
Export can counter the retention effect.
primary_references
[sulforaphane-p18204073] Expression of MRP1 and GSTP1-1 modulate the acute cellular response to treatment with the chemopreventive isothiocyanate, sulforaphane. (2008). https://pubmed.ncbi.nlm.nih.gov/18204073/ DOI: 10.1093/carcin/bgn013
tissue_or_cell_type
Intracellular retention, ARE induction and Nrf2 persistence
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1022–1033
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Transgenic transporter/enzyme comparison · source_derived_draft · unverified_draft
### sulforaphane-mrp-retention MRP1 expression reduced intracellular sulforaphane/conjugate accumulation and attenuated ARE-dependent responses. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Export can counter the retention effect. organism: Human MCF7 cells with GSTP1 and/or MRP1 tissue_or_cell_type: Intracellular retention, ARE induction and Nrf2 persistence experimental_model: Transgenic transporter/enzyme comparison limitations: Engineered cancer cells; enzyme expression and efflux can have opposing effects without being a scientific contradiction. exposure: Sulforaphane; GSH depletion control evidence_span: {"source_cache": "artifacts/sulforaphane-research/18204073.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0fcd98974f9fe12b2ca7c4326f94eddf4f20de4ac2ae6fdebb64de0efb1d8be9", "start_char": 0, "end_char": 1894, "text_sha256": "0fcd98974f9fe12b2ca7c4326f94eddf4f20de4ac2ae6fdebb64de0efb1d8be9"} [sulforaphane-p18204073] Expression of MRP1 and GSTP1-1 modulate the acute cellular response to treatment with the chemopreventive isothiocyanate, sulforaphane. (2008). https://pubmed.ncbi.nlm.nih.gov/18204073/ DOI: 10.1093/carcin/bgn013
Complete structured claim and evidence
The sulforaphane-induced Nrf2 increase was less sustained in MRP1-expressing cells, especially with GSTP1 coexpression.
Human multidrug resistance-associated protein 1 / ABCC1 / MRP1 → Persistence of induced nuclear Nrf2, assay specified source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/18204073.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0fcd98974f9fe12b2ca7c4326f94eddf4f20de4ac2ae6fdebb64de0efb1d8be9", "start_char": 0, "end_char": 1894, "text_sha256": "0fcd98974f9fe12b2ca7c4326f94eddf4f20de4ac2ae6fdebb64de0efb1d8be9"}
experimental_model
Transgenic transporter/enzyme comparison
exposure
Sulforaphane; GSH depletion control
limitations
Engineered cancer cells; enzyme expression and efflux can have opposing effects without being a scientific contradiction.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human MCF7 cells with GSTP1 and/or MRP1
plain_language
The duration of the response depends partly on how the compound is handled.
primary_references
[sulforaphane-p18204073] Expression of MRP1 and GSTP1-1 modulate the acute cellular response to treatment with the chemopreventive isothiocyanate, sulforaphane. (2008). https://pubmed.ncbi.nlm.nih.gov/18204073/ DOI: 10.1093/carcin/bgn013
tissue_or_cell_type
Intracellular retention, ARE induction and Nrf2 persistence
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1035–1046
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Transgenic transporter/enzyme comparison · source_derived_draft · unverified_draft
### sulforaphane-mrp-nrf2-duration The sulforaphane-induced Nrf2 increase was less sustained in MRP1-expressing cells, especially with GSTP1 coexpression. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The duration of the response depends partly on how the compound is handled. organism: Human MCF7 cells with GSTP1 and/or MRP1 tissue_or_cell_type: Intracellular retention, ARE induction and Nrf2 persistence experimental_model: Transgenic transporter/enzyme comparison limitations: Engineered cancer cells; enzyme expression and efflux can have opposing effects without being a scientific contradiction. exposure: Sulforaphane; GSH depletion control evidence_span: {"source_cache": "artifacts/sulforaphane-research/18204073.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0fcd98974f9fe12b2ca7c4326f94eddf4f20de4ac2ae6fdebb64de0efb1d8be9", "start_char": 0, "end_char": 1894, "text_sha256": "0fcd98974f9fe12b2ca7c4326f94eddf4f20de4ac2ae6fdebb64de0efb1d8be9"} [sulforaphane-p18204073] Expression of MRP1 and GSTP1-1 modulate the acute cellular response to treatment with the chemopreventive isothiocyanate, sulforaphane. (2008). https://pubmed.ncbi.nlm.nih.gov/18204073/ DOI: 10.1093/carcin/bgn013
Complete structured claim and evidence
The intervention increased urinary benzene-derived conjugate excretion by 61% compared with placebo.
Broccoli sprout preparation, composition specified per study → Urinary benzene-derived mercapturic acid source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/24913818.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "dabcc8a48260f668232ae3ab528fbf08e7b8b814ad9959d709fcd4702bbda7dd", "start_char": 0, "end_char": 1710, "text_sha256": "dabcc8a48260f668232ae3ab528fbf08e7b8b814ad9959d709fcd4702bbda7dd"}
experimental_model
Randomized placebo-controlled beverage trial
exposure
600 micromol glucoraphanin plus 40 micromol sulforaphane daily for 12 weeks
limitations
Urinary conjugate excretion is not proof of reduced cancer incidence, removal of every toxin or a clinical detoxification indication.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human, 291 recruited adults in Qidong
plain_language
A specific exposure-processing marker increased.
primary_references
[sulforaphane-p24913818] Rapid and sustainable detoxication of airborne pollutants by broccoli sprout beverage: results of a randomized clinical trial in China. (2014). https://pubmed.ncbi.nlm.nih.gov/24913818/ DOI: 10.1158/1940-6207.capr-14-0103
tissue_or_cell_type
Urinary pollutant mercapturates
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1048–1059
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized placebo-controlled beverage trial · source_derived_draft · unverified_draft
### sulforaphane-benzene-excretion The intervention increased urinary benzene-derived conjugate excretion by 61% compared with placebo. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: A specific exposure-processing marker increased. organism: Human, 291 recruited adults in Qidong tissue_or_cell_type: Urinary pollutant mercapturates experimental_model: Randomized placebo-controlled beverage trial limitations: Urinary conjugate excretion is not proof of reduced cancer incidence, removal of every toxin or a clinical detoxification indication. exposure: 600 micromol glucoraphanin plus 40 micromol sulforaphane daily for 12 weeks evidence_span: {"source_cache": "artifacts/sulforaphane-research/24913818.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "dabcc8a48260f668232ae3ab528fbf08e7b8b814ad9959d709fcd4702bbda7dd", "start_char": 0, "end_char": 1710, "text_sha256": "dabcc8a48260f668232ae3ab528fbf08e7b8b814ad9959d709fcd4702bbda7dd"} [sulforaphane-p24913818] Rapid and sustainable detoxication of airborne pollutants by broccoli sprout beverage: results of a randomized clinical trial in China. (2014). https://pubmed.ncbi.nlm.nih.gov/24913818/ DOI: 10.1158/1940-6207.capr-14-0103
Complete structured claim and evidence
Urinary acrolein-derived conjugate excretion increased by 23%.
Broccoli sprout preparation, composition specified per study → Urinary acrolein-derived mercapturic acid source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/24913818.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "dabcc8a48260f668232ae3ab528fbf08e7b8b814ad9959d709fcd4702bbda7dd", "start_char": 0, "end_char": 1710, "text_sha256": "dabcc8a48260f668232ae3ab528fbf08e7b8b814ad9959d709fcd4702bbda7dd"}
experimental_model
Randomized placebo-controlled beverage trial
exposure
600 micromol glucoraphanin plus 40 micromol sulforaphane daily for 12 weeks
limitations
Urinary conjugate excretion is not proof of reduced cancer incidence, removal of every toxin or a clinical detoxification indication.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human, 291 recruited adults in Qidong
plain_language
The result extended to a second measured pollutant.
primary_references
[sulforaphane-p24913818] Rapid and sustainable detoxication of airborne pollutants by broccoli sprout beverage: results of a randomized clinical trial in China. (2014). https://pubmed.ncbi.nlm.nih.gov/24913818/ DOI: 10.1158/1940-6207.capr-14-0103
tissue_or_cell_type
Urinary pollutant mercapturates
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1061–1072
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized placebo-controlled beverage trial · source_derived_draft · unverified_draft
### sulforaphane-acrolein-excretion Urinary acrolein-derived conjugate excretion increased by 23%. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The result extended to a second measured pollutant. organism: Human, 291 recruited adults in Qidong tissue_or_cell_type: Urinary pollutant mercapturates experimental_model: Randomized placebo-controlled beverage trial limitations: Urinary conjugate excretion is not proof of reduced cancer incidence, removal of every toxin or a clinical detoxification indication. exposure: 600 micromol glucoraphanin plus 40 micromol sulforaphane daily for 12 weeks evidence_span: {"source_cache": "artifacts/sulforaphane-research/24913818.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "dabcc8a48260f668232ae3ab528fbf08e7b8b814ad9959d709fcd4702bbda7dd", "start_char": 0, "end_char": 1710, "text_sha256": "dabcc8a48260f668232ae3ab528fbf08e7b8b814ad9959d709fcd4702bbda7dd"} [sulforaphane-p24913818] Rapid and sustainable detoxication of airborne pollutants by broccoli sprout beverage: results of a randomized clinical trial in China. (2014). https://pubmed.ncbi.nlm.nih.gov/24913818/ DOI: 10.1158/1940-6207.capr-14-0103
Complete structured claim and evidence
Crotonaldehyde-derived conjugate excretion did not show the intervention increase observed for benzene and acrolein.
Broccoli sprout preparation, composition specified per study → Urinary crotonaldehyde-derived mercapturic acid source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/24913818.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "dabcc8a48260f668232ae3ab528fbf08e7b8b814ad9959d709fcd4702bbda7dd", "start_char": 0, "end_char": 1710, "text_sha256": "dabcc8a48260f668232ae3ab528fbf08e7b8b814ad9959d709fcd4702bbda7dd"}
experimental_model
Randomized placebo-controlled beverage trial
exposure
600 micromol glucoraphanin plus 40 micromol sulforaphane daily for 12 weeks
limitations
Urinary conjugate excretion is not proof of reduced cancer incidence, removal of every toxin or a clinical detoxification indication.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human, 291 recruited adults in Qidong
plain_language
The response was selective rather than a universal detoxification boost.
primary_references
[sulforaphane-p24913818] Rapid and sustainable detoxication of airborne pollutants by broccoli sprout beverage: results of a randomized clinical trial in China. (2014). https://pubmed.ncbi.nlm.nih.gov/24913818/ DOI: 10.1158/1940-6207.capr-14-0103
tissue_or_cell_type
Urinary pollutant mercapturates
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1074–1085
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized placebo-controlled beverage trial · source_derived_draft · unverified_draft
### sulforaphane-crotonaldehyde-null Crotonaldehyde-derived conjugate excretion did not show the intervention increase observed for benzene and acrolein. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The response was selective rather than a universal detoxification boost. organism: Human, 291 recruited adults in Qidong tissue_or_cell_type: Urinary pollutant mercapturates experimental_model: Randomized placebo-controlled beverage trial limitations: Urinary conjugate excretion is not proof of reduced cancer incidence, removal of every toxin or a clinical detoxification indication. exposure: 600 micromol glucoraphanin plus 40 micromol sulforaphane daily for 12 weeks evidence_span: {"source_cache": "artifacts/sulforaphane-research/24913818.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "dabcc8a48260f668232ae3ab528fbf08e7b8b814ad9959d709fcd4702bbda7dd", "start_char": 0, "end_char": 1710, "text_sha256": "dabcc8a48260f668232ae3ab528fbf08e7b8b814ad9959d709fcd4702bbda7dd"} [sulforaphane-p24913818] Rapid and sustainable detoxication of airborne pollutants by broccoli sprout beverage: results of a randomized clinical trial in China. (2014). https://pubmed.ncbi.nlm.nih.gov/24913818/ DOI: 10.1158/1940-6207.capr-14-0103
Complete structured claim and evidence
Inflammatory measures and pulmonary function did not differ among trial groups.
Sulforaphane / SFN, stereochemistry specified per study → Pulmonary function in COPD trial source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/27832073.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "cc345cf4434bd2d27451706ec614763c7be7562ac3e368f0e21b38c0f4d21003", "start_char": 0, "end_char": 1709, "text_sha256": "cc345cf4434bd2d27451706ec614763c7be7562ac3e368f0e21b38c0f4d21003"}
experimental_model
Randomized double-blind placebo-controlled phase 2 trial
exposure
25 or 150 micromol sulforaphane daily for four weeks
limitations
Absorption was documented; cell-based target engagement cannot be assumed after oral dosing in patients.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human, 89 COPD patients
plain_language
The short trial did not demonstrate a functional lung benefit.
primary_references
[sulforaphane-p27832073] Lack of Effect of Oral Sulforaphane Administration on Nrf2 Expression in COPD: A Randomized, Double-Blind, Placebo Controlled Trial. (2016). https://pubmed.ncbi.nlm.nih.gov/27832073/ DOI: 10.1371/journal.pone.0163716
tissue_or_cell_type
Alveolar macrophages, bronchial epithelium and pulmonary function
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1100–1111
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized double-blind placebo-controlled phase 2 trial · source_derived_draft · unverified_draft
### sulforaphane-copd-function-null Inflammatory measures and pulmonary function did not differ among trial groups. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The short trial did not demonstrate a functional lung benefit. organism: Human, 89 COPD patients tissue_or_cell_type: Alveolar macrophages, bronchial epithelium and pulmonary function experimental_model: Randomized double-blind placebo-controlled phase 2 trial limitations: Absorption was documented; cell-based target engagement cannot be assumed after oral dosing in patients. exposure: 25 or 150 micromol sulforaphane daily for four weeks evidence_span: {"source_cache": "artifacts/sulforaphane-research/27832073.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "cc345cf4434bd2d27451706ec614763c7be7562ac3e368f0e21b38c0f4d21003", "start_char": 0, "end_char": 1709, "text_sha256": "cc345cf4434bd2d27451706ec614763c7be7562ac3e368f0e21b38c0f4d21003"} [sulforaphane-p27832073] Lack of Effect of Oral Sulforaphane Administration on Nrf2 Expression in COPD: A Randomized, Double-Blind, Placebo Controlled Trial. (2016). https://pubmed.ncbi.nlm.nih.gov/27832073/ DOI: 10.1371/journal.pone.0163716
Complete structured claim and evidence
In the hepatic-cell experiments, sulforaphane promoted NRF2 nuclear translocation in the mechanism linked to reduced glucose production.
Sulforaphane / SFN, stereochemistry specified per study → Nrf2 nuclear localization in experimental hepatic cells source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/28615356.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "65f64f5fa5e84a03d3ba4b647ce94a815fd3bd345486b726e7a54f1a813cab0e", "start_char": 0, "end_char": 1106, "text_sha256": "65f64f5fa5e84a03d3ba4b647ce94a815fd3bd345486b726e7a54f1a813cab0e"}
experimental_model
Network-guided preclinical work with a human intervention
exposure
Sulforaphane in the preclinical hepatic-cell arm
limitations
Model-based mechanism and clinical subgroup outcomes are distinct; no equivalence to metformin in patients is claimed.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Experimental hepatic cells; distinct from the human intervention
plain_language
The glucose-production mechanism was studied in cells, separately from patient outcomes.
primary_references
[sulforaphane-p28615356] Sulforaphane reduces hepatic glucose production and improves glucose control in patients with type 2 diabetes. (2017). https://pubmed.ncbi.nlm.nih.gov/28615356/ DOI: 10.1126/scitranslmed.aah4477
tissue_or_cell_type
Hepatic-cell experiments
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1113–1124
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Network-guided preclinical work with a human intervention · source_derived_draft · unverified_draft
### sulforaphane-hepatic-nrf2 In the hepatic-cell experiments, sulforaphane promoted NRF2 nuclear translocation in the mechanism linked to reduced glucose production. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The glucose-production mechanism was studied in cells, separately from patient outcomes. organism: Experimental hepatic cells; distinct from the human intervention tissue_or_cell_type: Hepatic-cell experiments experimental_model: Network-guided preclinical work with a human intervention limitations: Model-based mechanism and clinical subgroup outcomes are distinct; no equivalence to metformin in patients is claimed. exposure: Sulforaphane in the preclinical hepatic-cell arm evidence_span: {"source_cache": "artifacts/sulforaphane-research/28615356.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "65f64f5fa5e84a03d3ba4b647ce94a815fd3bd345486b726e7a54f1a813cab0e", "start_char": 0, "end_char": 1106, "text_sha256": "65f64f5fa5e84a03d3ba4b647ce94a815fd3bd345486b726e7a54f1a813cab0e"} [sulforaphane-p28615356] Sulforaphane reduces hepatic glucose production and improves glucose control in patients with type 2 diabetes. (2017). https://pubmed.ncbi.nlm.nih.gov/28615356/ DOI: 10.1126/scitranslmed.aah4477
Complete structured claim and evidence
Sulforaphane lowered expression of key gluconeogenic enzymes in the hepatic-cell experiments.
Sulforaphane / SFN, stereochemistry specified per study → Gluconeogenic-enzyme expression in experimental hepatic cells source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/28615356.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "65f64f5fa5e84a03d3ba4b647ce94a815fd3bd345486b726e7a54f1a813cab0e", "start_char": 0, "end_char": 1106, "text_sha256": "65f64f5fa5e84a03d3ba4b647ce94a815fd3bd345486b726e7a54f1a813cab0e"}
experimental_model
Network-guided preclinical work with a human intervention
exposure
Sulforaphane in the preclinical hepatic-cell arm
limitations
Model-based mechanism and clinical subgroup outcomes are distinct; no equivalence to metformin in patients is claimed.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Experimental hepatic cells; distinct from the human intervention
plain_language
The machinery for making new glucose was reduced.
primary_references
[sulforaphane-p28615356] Sulforaphane reduces hepatic glucose production and improves glucose control in patients with type 2 diabetes. (2017). https://pubmed.ncbi.nlm.nih.gov/28615356/ DOI: 10.1126/scitranslmed.aah4477
tissue_or_cell_type
Hepatic-cell experiments
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1126–1137
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Network-guided preclinical work with a human intervention · source_derived_draft · unverified_draft
### sulforaphane-hepatic-enzymes Sulforaphane lowered expression of key gluconeogenic enzymes in the hepatic-cell experiments. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The machinery for making new glucose was reduced. organism: Experimental hepatic cells; distinct from the human intervention tissue_or_cell_type: Hepatic-cell experiments experimental_model: Network-guided preclinical work with a human intervention limitations: Model-based mechanism and clinical subgroup outcomes are distinct; no equivalence to metformin in patients is claimed. exposure: Sulforaphane in the preclinical hepatic-cell arm evidence_span: {"source_cache": "artifacts/sulforaphane-research/28615356.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "65f64f5fa5e84a03d3ba4b647ce94a815fd3bd345486b726e7a54f1a813cab0e", "start_char": 0, "end_char": 1106, "text_sha256": "65f64f5fa5e84a03d3ba4b647ce94a815fd3bd345486b726e7a54f1a813cab0e"} [sulforaphane-p28615356] Sulforaphane reduces hepatic glucose production and improves glucose control in patients with type 2 diabetes. (2017). https://pubmed.ncbi.nlm.nih.gov/28615356/ DOI: 10.1126/scitranslmed.aah4477
Complete structured claim and evidence
Sulforaphane suppressed glucose production from hepatic cells in the preclinical component of the study.
Sulforaphane / SFN, stereochemistry specified per study → Glucose production by experimental hepatic cells source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/28615356.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "65f64f5fa5e84a03d3ba4b647ce94a815fd3bd345486b726e7a54f1a813cab0e", "start_char": 0, "end_char": 1106, "text_sha256": "65f64f5fa5e84a03d3ba4b647ce94a815fd3bd345486b726e7a54f1a813cab0e"}
experimental_model
Network-guided preclinical work with a human intervention
exposure
Sulforaphane in the preclinical hepatic-cell arm
limitations
Model-based mechanism and clinical subgroup outcomes are distinct; no equivalence to metformin in patients is claimed.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Experimental hepatic cells; distinct from the human intervention
plain_language
This supplies a possible mechanism for the glucose-control research.
primary_references
[sulforaphane-p28615356] Sulforaphane reduces hepatic glucose production and improves glucose control in patients with type 2 diabetes. (2017). https://pubmed.ncbi.nlm.nih.gov/28615356/ DOI: 10.1126/scitranslmed.aah4477
tissue_or_cell_type
Hepatic-cell experiments
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1139–1150
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Network-guided preclinical work with a human intervention · source_derived_draft · unverified_draft
### sulforaphane-hepatic-glucose Sulforaphane suppressed glucose production from hepatic cells in the preclinical component of the study. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: This supplies a possible mechanism for the glucose-control research. organism: Experimental hepatic cells; distinct from the human intervention tissue_or_cell_type: Hepatic-cell experiments experimental_model: Network-guided preclinical work with a human intervention limitations: Model-based mechanism and clinical subgroup outcomes are distinct; no equivalence to metformin in patients is claimed. exposure: Sulforaphane in the preclinical hepatic-cell arm evidence_span: {"source_cache": "artifacts/sulforaphane-research/28615356.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "65f64f5fa5e84a03d3ba4b647ce94a815fd3bd345486b726e7a54f1a813cab0e", "start_char": 0, "end_char": 1106, "text_sha256": "65f64f5fa5e84a03d3ba4b647ce94a815fd3bd345486b726e7a54f1a813cab0e"} [sulforaphane-p28615356] Sulforaphane reduces hepatic glucose production and improves glucose control in patients with type 2 diabetes. (2017). https://pubmed.ncbi.nlm.nih.gov/28615356/ DOI: 10.1126/scitranslmed.aah4477
Complete structured claim and evidence
Concentrated broccoli sprout extract lowered fasting glucose in obese patients with dysregulated type 2 diabetes in the reported subgroup.
Broccoli sprout preparation, composition specified per study → Fasting plasma glucose source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/28615356.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "65f64f5fa5e84a03d3ba4b647ce94a815fd3bd345486b726e7a54f1a813cab0e", "start_char": 0, "end_char": 1106, "text_sha256": "65f64f5fa5e84a03d3ba4b647ce94a815fd3bd345486b726e7a54f1a813cab0e"}
experimental_model
Network-guided preclinical work with a human intervention
exposure
Concentrated broccoli sprout extract; obese dysregulated-diabetes subgroup
limitations
Model-based mechanism and clinical subgroup outcomes are distinct; no equivalence to metformin in patients is claimed.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Hepatic cell/animal models and humans with type 2 diabetes
plain_language
The clinical response depended on the studied metabolic population.
primary_references
[sulforaphane-p28615356] Sulforaphane reduces hepatic glucose production and improves glucose control in patients with type 2 diabetes. (2017). https://pubmed.ncbi.nlm.nih.gov/28615356/ DOI: 10.1126/scitranslmed.aah4477
tissue_or_cell_type
Glucose production and clinical glucose control
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1152–1163
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Network-guided preclinical work with a human intervention · source_derived_draft · unverified_draft
### sulforaphane-diabetes-glucose Concentrated broccoli sprout extract lowered fasting glucose in obese patients with dysregulated type 2 diabetes in the reported subgroup. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The clinical response depended on the studied metabolic population. organism: Hepatic cell/animal models and humans with type 2 diabetes tissue_or_cell_type: Glucose production and clinical glucose control experimental_model: Network-guided preclinical work with a human intervention limitations: Model-based mechanism and clinical subgroup outcomes are distinct; no equivalence to metformin in patients is claimed. exposure: Concentrated broccoli sprout extract; obese dysregulated-diabetes subgroup evidence_span: {"source_cache": "artifacts/sulforaphane-research/28615356.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "65f64f5fa5e84a03d3ba4b647ce94a815fd3bd345486b726e7a54f1a813cab0e", "start_char": 0, "end_char": 1106, "text_sha256": "65f64f5fa5e84a03d3ba4b647ce94a815fd3bd345486b726e7a54f1a813cab0e"} [sulforaphane-p28615356] Sulforaphane reduces hepatic glucose production and improves glucose control in patients with type 2 diabetes. (2017). https://pubmed.ncbi.nlm.nih.gov/28615356/ DOI: 10.1126/scitranslmed.aah4477
Complete structured claim and evidence
HbA1c decreased in the reported obese dysregulated-diabetes subgroup.
Broccoli sprout preparation, composition specified per study → Glycated hemoglobin / HbA1c concentration source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/28615356.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "65f64f5fa5e84a03d3ba4b647ce94a815fd3bd345486b726e7a54f1a813cab0e", "start_char": 0, "end_char": 1106, "text_sha256": "65f64f5fa5e84a03d3ba4b647ce94a815fd3bd345486b726e7a54f1a813cab0e"}
experimental_model
Network-guided preclinical work with a human intervention
exposure
Concentrated broccoli sprout extract; obese dysregulated-diabetes subgroup
limitations
Model-based mechanism and clinical subgroup outcomes are distinct; no equivalence to metformin in patients is claimed.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Hepatic cell/animal models and humans with type 2 diabetes
plain_language
A longer-term glucose marker also changed in that subgroup.
primary_references
[sulforaphane-p28615356] Sulforaphane reduces hepatic glucose production and improves glucose control in patients with type 2 diabetes. (2017). https://pubmed.ncbi.nlm.nih.gov/28615356/ DOI: 10.1126/scitranslmed.aah4477
tissue_or_cell_type
Glucose production and clinical glucose control
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1165–1176
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Network-guided preclinical work with a human intervention · source_derived_draft · unverified_draft
### sulforaphane-diabetes-hba1c HbA1c decreased in the reported obese dysregulated-diabetes subgroup. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: A longer-term glucose marker also changed in that subgroup. organism: Hepatic cell/animal models and humans with type 2 diabetes tissue_or_cell_type: Glucose production and clinical glucose control experimental_model: Network-guided preclinical work with a human intervention limitations: Model-based mechanism and clinical subgroup outcomes are distinct; no equivalence to metformin in patients is claimed. exposure: Concentrated broccoli sprout extract; obese dysregulated-diabetes subgroup evidence_span: {"source_cache": "artifacts/sulforaphane-research/28615356.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "65f64f5fa5e84a03d3ba4b647ce94a815fd3bd345486b726e7a54f1a813cab0e", "start_char": 0, "end_char": 1106, "text_sha256": "65f64f5fa5e84a03d3ba4b647ce94a815fd3bd345486b726e7a54f1a813cab0e"} [sulforaphane-p28615356] Sulforaphane reduces hepatic glucose production and improves glucose control in patients with type 2 diabetes. (2017). https://pubmed.ncbi.nlm.nih.gov/28615356/ DOI: 10.1126/scitranslmed.aah4477
Complete structured claim and evidence
The mean glucose reduction versus placebo was 0.2 mmol/L (95% CI -0.44 to -0.01; P=0.04), below the prespecified 0.3 mmol/L target.
Broccoli sprout preparation, composition specified per study → Fasting plasma glucose source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/39929977.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "525674c523bafc5e583bea8f2402f9e6dcf792c93b5af0c0f19d3aee15393a92", "start_char": 0, "end_char": 1849, "text_sha256": "525674c523bafc5e583bea8f2402f9e6dcf792c93b5af0c0f19d3aee15393a92"}
experimental_model
Randomized double-blind placebo-controlled trial with exploratory microbiome analysis
exposure
Daily broccoli sprout extract for 12 weeks
limitations
Primary target was 0.3 mmol/L; subgroup and microbiome results were exploratory and need confirmation.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human prediabetes; 35 extract and 39 placebo participants analyzed
plain_language
A small statistical signal did not meet the trial's planned target.
primary_references
[sulforaphane-p39929977] Effect of broccoli sprout extract and baseline gut microbiota on fasting blood glucose in prediabetes: a randomized, placebo-controlled trial. (2025). https://pubmed.ncbi.nlm.nih.gov/39929977/ DOI: 10.1038/s41564-025-01932-w
tissue_or_cell_type
Fasting glucose and serum exposure
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1178–1189
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized double-blind placebo-controlled trial with exploratory microbiome analysis · source_derived_draft · unverified_draft
### sulforaphane-prediabetes-primary The mean glucose reduction versus placebo was 0.2 mmol/L (95% CI -0.44 to -0.01; P=0.04), below the prespecified 0.3 mmol/L target. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: A small statistical signal did not meet the trial's planned target. organism: Human prediabetes; 35 extract and 39 placebo participants analyzed tissue_or_cell_type: Fasting glucose and serum exposure experimental_model: Randomized double-blind placebo-controlled trial with exploratory microbiome analysis limitations: Primary target was 0.3 mmol/L; subgroup and microbiome results were exploratory and need confirmation. exposure: Daily broccoli sprout extract for 12 weeks evidence_span: {"source_cache": "artifacts/sulforaphane-research/39929977.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "525674c523bafc5e583bea8f2402f9e6dcf792c93b5af0c0f19d3aee15393a92", "start_char": 0, "end_char": 1849, "text_sha256": "525674c523bafc5e583bea8f2402f9e6dcf792c93b5af0c0f19d3aee15393a92"} [sulforaphane-p39929977] Effect of broccoli sprout extract and baseline gut microbiota on fasting blood glucose in prediabetes: a randomized, placebo-controlled trial. (2025). https://pubmed.ncbi.nlm.nih.gov/39929977/ DOI: 10.1038/s41564-025-01932-w
Complete structured claim and evidence
Baseline abundance of the bacterial glucosinolate-conversion operon correlated with serum sulforaphane in exploratory analysis.
Baseline microbial glucosinolate-operon abundance → Systemic sulforaphane exposure measured by study-specific biomarkers source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/39929977.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "525674c523bafc5e583bea8f2402f9e6dcf792c93b5af0c0f19d3aee15393a92", "start_char": 0, "end_char": 1849, "text_sha256": "525674c523bafc5e583bea8f2402f9e6dcf792c93b5af0c0f19d3aee15393a92"}
experimental_model
Randomized double-blind placebo-controlled trial with exploratory microbiome analysis
exposure
Daily broccoli sprout extract for 12 weeks
limitations
Primary target was 0.3 mmol/L; subgroup and microbiome results were exploratory and need confirmation.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human prediabetes; 35 extract and 39 placebo participants analyzed
plain_language
Microbial conversion capacity may help explain exposure differences, but this was not a randomized microbial intervention.
primary_references
[sulforaphane-p39929977] Effect of broccoli sprout extract and baseline gut microbiota on fasting blood glucose in prediabetes: a randomized, placebo-controlled trial. (2025). https://pubmed.ncbi.nlm.nih.gov/39929977/ DOI: 10.1038/s41564-025-01932-w
tissue_or_cell_type
Fasting glucose and serum exposure
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1191–1202
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized double-blind placebo-controlled trial with exploratory microbiome analysis · source_derived_draft · unverified_draft
### sulforaphane-microbiome-response Baseline abundance of the bacterial glucosinolate-conversion operon correlated with serum sulforaphane in exploratory analysis. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Microbial conversion capacity may help explain exposure differences, but this was not a randomized microbial intervention. organism: Human prediabetes; 35 extract and 39 placebo participants analyzed tissue_or_cell_type: Fasting glucose and serum exposure experimental_model: Randomized double-blind placebo-controlled trial with exploratory microbiome analysis limitations: Primary target was 0.3 mmol/L; subgroup and microbiome results were exploratory and need confirmation. exposure: Daily broccoli sprout extract for 12 weeks evidence_span: {"source_cache": "artifacts/sulforaphane-research/39929977.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "525674c523bafc5e583bea8f2402f9e6dcf792c93b5af0c0f19d3aee15393a92", "start_char": 0, "end_char": 1849, "text_sha256": "525674c523bafc5e583bea8f2402f9e6dcf792c93b5af0c0f19d3aee15393a92"} [sulforaphane-p39929977] Effect of broccoli sprout extract and baseline gut microbiota on fasting blood glucose in prediabetes: a randomized, placebo-controlled trial. (2025). https://pubmed.ncbi.nlm.nih.gov/39929977/ DOI: 10.1038/s41564-025-01932-w
Complete structured claim and evidence
Gastrointestinal side effects occurred; no severe adverse events were reported in the trial.
Broccoli sprout preparation, composition specified per study → Gastrointestinal adverse events source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/39929977.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "525674c523bafc5e583bea8f2402f9e6dcf792c93b5af0c0f19d3aee15393a92", "start_char": 0, "end_char": 1849, "text_sha256": "525674c523bafc5e583bea8f2402f9e6dcf792c93b5af0c0f19d3aee15393a92"}
experimental_model
Randomized double-blind placebo-controlled trial with exploratory microbiome analysis
exposure
Daily broccoli sprout extract for 12 weeks
limitations
Primary target was 0.3 mmol/L; subgroup and microbiome results were exploratory and need confirmation.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human prediabetes; 35 extract and 39 placebo participants analyzed
plain_language
Tolerability and efficacy are separate outcomes.
primary_references
[sulforaphane-p39929977] Effect of broccoli sprout extract and baseline gut microbiota on fasting blood glucose in prediabetes: a randomized, placebo-controlled trial. (2025). https://pubmed.ncbi.nlm.nih.gov/39929977/ DOI: 10.1038/s41564-025-01932-w
tissue_or_cell_type
Fasting glucose and serum exposure
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1204–1215
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized double-blind placebo-controlled trial with exploratory microbiome analysis · source_derived_draft · unverified_draft
### sulforaphane-prediabetes-gi Gastrointestinal side effects occurred; no severe adverse events were reported in the trial. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Tolerability and efficacy are separate outcomes. organism: Human prediabetes; 35 extract and 39 placebo participants analyzed tissue_or_cell_type: Fasting glucose and serum exposure experimental_model: Randomized double-blind placebo-controlled trial with exploratory microbiome analysis limitations: Primary target was 0.3 mmol/L; subgroup and microbiome results were exploratory and need confirmation. exposure: Daily broccoli sprout extract for 12 weeks evidence_span: {"source_cache": "artifacts/sulforaphane-research/39929977.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "525674c523bafc5e583bea8f2402f9e6dcf792c93b5af0c0f19d3aee15393a92", "start_char": 0, "end_char": 1849, "text_sha256": "525674c523bafc5e583bea8f2402f9e6dcf792c93b5af0c0f19d3aee15393a92"} [sulforaphane-p39929977] Effect of broccoli sprout extract and baseline gut microbiota on fasting blood glucose in prediabetes: a randomized, placebo-controlled trial. (2025). https://pubmed.ncbi.nlm.nih.gov/39929977/ DOI: 10.1038/s41564-025-01932-w
Complete structured claim and evidence
TSH, free thyroxine, thyroglobulin and thyroid autoimmunity status were not affected in this 84-day analysis.
Broccoli sprout preparation, composition specified per study → Thyroid autoimmunity markers, trial specified source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/30735751.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0797bbf31c4a1fa8cf002b8752410e80a92e8a351c44273335bc52f19e66b2ea", "start_char": 0, "end_char": 1494, "text_sha256": "0797bbf31c4a1fa8cf002b8752410e80a92e8a351c44273335bc52f19e66b2ea"}
experimental_model
Thyroid safety analysis within a randomized beverage trial
exposure
Baseline and 84 days of glucoraphanin/sulforaphane-rich beverage
limitations
Subsample safety analysis; not all populations, iodine-deficient states, products, doses or lifelong exposure.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human, 45 women
plain_language
This preparation showed no thyroid signal under the conditions tested; that is not universal thyroid safety proof.
primary_references
[sulforaphane-p30735751] Broccoli sprout beverage is safe for thyroid hormonal and autoimmune status: Results of a 12-week randomized trial. (2019). https://pubmed.ncbi.nlm.nih.gov/30735751/ DOI: 10.1016/j.fct.2019.02.004
tissue_or_cell_type
Serum thyroid hormones, thyroglobulin and autoimmunity
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1217–1228
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Thyroid safety analysis within a randomized beverage trial · source_derived_draft · unverified_draft
### sulforaphane-thyroid-markers TSH, free thyroxine, thyroglobulin and thyroid autoimmunity status were not affected in this 84-day analysis. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: This preparation showed no thyroid signal under the conditions tested; that is not universal thyroid safety proof. organism: Human, 45 women tissue_or_cell_type: Serum thyroid hormones, thyroglobulin and autoimmunity experimental_model: Thyroid safety analysis within a randomized beverage trial limitations: Subsample safety analysis; not all populations, iodine-deficient states, products, doses or lifelong exposure. exposure: Baseline and 84 days of glucoraphanin/sulforaphane-rich beverage evidence_span: {"source_cache": "artifacts/sulforaphane-research/30735751.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0797bbf31c4a1fa8cf002b8752410e80a92e8a351c44273335bc52f19e66b2ea", "start_char": 0, "end_char": 1494, "text_sha256": "0797bbf31c4a1fa8cf002b8752410e80a92e8a351c44273335bc52f19e66b2ea"} [sulforaphane-p30735751] Broccoli sprout beverage is safe for thyroid hormonal and autoimmune status: Results of a 12-week randomized trial. (2019). https://pubmed.ncbi.nlm.nih.gov/30735751/ DOI: 10.1016/j.fct.2019.02.004
Complete structured claim and evidence
Sulforaphane strongly reduced CYP3A4 mRNA in primary human hepatocytes without inducing GSTM1 or GSTT1 expression.
Sulforaphane / SFN, stereochemistry specified per study → Human cytochrome P450 3A4 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/20442190.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "130e0a3ab9cbabd496a64344ae8bfb9f98cccbf7521a64ec807f14b2259ceb69", "start_char": 0, "end_char": 1705, "text_sha256": "130e0a3ab9cbabd496a64344ae8bfb9f98cccbf7521a64ec807f14b2259ceb69"}
experimental_model
Primary human hepatocyte pretreatment and genotyping
exposure
Sulforaphane 10 or 50 micromolar for 48 hours before aflatoxin B1
limitations
Culture exposures are not ordinary plasma exposures; reduced CYP3A4 mRNA does not establish the direction of clinical drug interactions.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human hepatocyte cultures
plain_language
Suppressed activation machinery, rather than increased GST expression, accompanied the response.
primary_references
[sulforaphane-p20442190] Sulforaphane- and phenethyl isothiocyanate-induced inhibition of aflatoxin B1-mediated genotoxicity in human hepatocytes: role of GSTM1 genotype and CYP3A4 gene expression. (2010). https://pubmed.ncbi.nlm.nih.gov/20442190/ DOI: 10.1093/toxsci/kfq135
tissue_or_cell_type
Aflatoxin activation and DNA damage
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1230–1241
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Primary human hepatocyte pretreatment and genotyping · source_derived_draft · unverified_draft
### sulforaphane-cyp3a4-transcription Sulforaphane strongly reduced CYP3A4 mRNA in primary human hepatocytes without inducing GSTM1 or GSTT1 expression. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Suppressed activation machinery, rather than increased GST expression, accompanied the response. organism: Human hepatocyte cultures tissue_or_cell_type: Aflatoxin activation and DNA damage experimental_model: Primary human hepatocyte pretreatment and genotyping limitations: Culture exposures are not ordinary plasma exposures; reduced CYP3A4 mRNA does not establish the direction of clinical drug interactions. exposure: Sulforaphane 10 or 50 micromolar for 48 hours before aflatoxin B1 evidence_span: {"source_cache": "artifacts/sulforaphane-research/20442190.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "130e0a3ab9cbabd496a64344ae8bfb9f98cccbf7521a64ec807f14b2259ceb69", "start_char": 0, "end_char": 1705, "text_sha256": "130e0a3ab9cbabd496a64344ae8bfb9f98cccbf7521a64ec807f14b2259ceb69"} [sulforaphane-p20442190] Sulforaphane- and phenethyl isothiocyanate-induced inhibition of aflatoxin B1-mediated genotoxicity in human hepatocytes: role of GSTM1 genotype and CYP3A4 gene expression. (2010). https://pubmed.ncbi.nlm.nih.gov/20442190/ DOI: 10.1093/toxsci/kfq135
Complete structured claim and evidence
Pretreatment reduced aflatoxin-DNA adducts; simultaneous exposure without pretreatment did not.
Sulforaphane / SFN, stereochemistry specified per study → Aflatoxin B1-derived DNA adduct formation source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/20442190.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "130e0a3ab9cbabd496a64344ae8bfb9f98cccbf7521a64ec807f14b2259ceb69", "start_char": 0, "end_char": 1705, "text_sha256": "130e0a3ab9cbabd496a64344ae8bfb9f98cccbf7521a64ec807f14b2259ceb69"}
experimental_model
Primary human hepatocyte pretreatment and genotyping
exposure
Sulforaphane 10 or 50 micromolar for 48 hours before aflatoxin B1
limitations
Culture exposures are not ordinary plasma exposures; reduced CYP3A4 mRNA does not establish the direction of clinical drug interactions.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human hepatocyte cultures
plain_language
The time allowed for a cellular response mattered.
primary_references
[sulforaphane-p20442190] Sulforaphane- and phenethyl isothiocyanate-induced inhibition of aflatoxin B1-mediated genotoxicity in human hepatocytes: role of GSTM1 genotype and CYP3A4 gene expression. (2010). https://pubmed.ncbi.nlm.nih.gov/20442190/ DOI: 10.1093/toxsci/kfq135
tissue_or_cell_type
Aflatoxin activation and DNA damage
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1243–1254
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Primary human hepatocyte pretreatment and genotyping · source_derived_draft · unverified_draft
### sulforaphane-aflatoxin-pretreatment Pretreatment reduced aflatoxin-DNA adducts; simultaneous exposure without pretreatment did not. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The time allowed for a cellular response mattered. organism: Human hepatocyte cultures tissue_or_cell_type: Aflatoxin activation and DNA damage experimental_model: Primary human hepatocyte pretreatment and genotyping limitations: Culture exposures are not ordinary plasma exposures; reduced CYP3A4 mRNA does not establish the direction of clinical drug interactions. exposure: Sulforaphane 10 or 50 micromolar for 48 hours before aflatoxin B1 evidence_span: {"source_cache": "artifacts/sulforaphane-research/20442190.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "130e0a3ab9cbabd496a64344ae8bfb9f98cccbf7521a64ec807f14b2259ceb69", "start_char": 0, "end_char": 1705, "text_sha256": "130e0a3ab9cbabd496a64344ae8bfb9f98cccbf7521a64ec807f14b2259ceb69"} [sulforaphane-p20442190] Sulforaphane- and phenethyl isothiocyanate-induced inhibition of aflatoxin B1-mediated genotoxicity in human hepatocytes: role of GSTM1 genotype and CYP3A4 gene expression. (2010). https://pubmed.ncbi.nlm.nih.gov/20442190/ DOI: 10.1093/toxsci/kfq135
Complete structured claim and evidence
Coadministration did not prevent rifampicin-driven CYP3A induction; rifampicin alone lowered midazolam AUC by 70%.
Sulforaphane / SFN, stereochemistry specified per study → Human CYP3A4 activity, probe and compartment specified source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/23153560.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e13099fede346485f6e468497ff2a4754fcae4d0203dde7f54fc9643c0599fec", "start_char": 0, "end_char": 1664, "text_sha256": "e13099fede346485f6e468497ff2a4754fcae4d0203dde7f54fc9643c0599fec"}
experimental_model
Three-arm randomized crossover trial
exposure
Rifampicin 300 mg/day, with or without sulforaphane 450 micromol/day for seven days; sulforaphane alone
limitations
Average null result does not exclude individual or other-drug interactions; high-baseline subgroup finding is not a dosing rule.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human, 24 healthy adults; humanized-PXR mouse parallel study
plain_language
The proposed receptor-blocking effect from laboratory work did not carry through in the human trial.
primary_references
[sulforaphane-p23153560] Sulforaphane is not an effective antagonist of the human pregnane X-receptor in vivo. (2013). https://pubmed.ncbi.nlm.nih.gov/23153560/ DOI: 10.1016/j.taap.2012.10.029
tissue_or_cell_type
CYP3A phenotyping with midazolam
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1256–1267
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Three-arm randomized crossover trial · source_derived_draft · unverified_draft
### sulforaphane-cyp3a4-rifampicin-null Coadministration did not prevent rifampicin-driven CYP3A induction; rifampicin alone lowered midazolam AUC by 70%. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The proposed receptor-blocking effect from laboratory work did not carry through in the human trial. organism: Human, 24 healthy adults; humanized-PXR mouse parallel study tissue_or_cell_type: CYP3A phenotyping with midazolam experimental_model: Three-arm randomized crossover trial limitations: Average null result does not exclude individual or other-drug interactions; high-baseline subgroup finding is not a dosing rule. exposure: Rifampicin 300 mg/day, with or without sulforaphane 450 micromol/day for seven days; sulforaphane alone evidence_span: {"source_cache": "artifacts/sulforaphane-research/23153560.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e13099fede346485f6e468497ff2a4754fcae4d0203dde7f54fc9643c0599fec", "start_char": 0, "end_char": 1664, "text_sha256": "e13099fede346485f6e468497ff2a4754fcae4d0203dde7f54fc9643c0599fec"} [sulforaphane-p23153560] Sulforaphane is not an effective antagonist of the human pregnane X-receptor in vivo. (2013). https://pubmed.ncbi.nlm.nih.gov/23153560/ DOI: 10.1016/j.taap.2012.10.029
Complete structured claim and evidence
Sulforaphane alone did not change CYP3A activity in the cohort overall; a high-baseline subgroup showed increased midazolam exposure.
Sulforaphane / SFN, stereochemistry specified per study → Human CYP3A4 activity, probe and compartment specified source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/23153560.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e13099fede346485f6e468497ff2a4754fcae4d0203dde7f54fc9643c0599fec", "start_char": 0, "end_char": 1664, "text_sha256": "e13099fede346485f6e468497ff2a4754fcae4d0203dde7f54fc9643c0599fec"}
experimental_model
Three-arm randomized crossover trial
exposure
Rifampicin 300 mg/day, with or without sulforaphane 450 micromol/day for seven days; sulforaphane alone
limitations
Average null result does not exclude individual or other-drug interactions; high-baseline subgroup finding is not a dosing rule.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human, 24 healthy adults; humanized-PXR mouse parallel study
plain_language
An average null and an exploratory subgroup signal must both remain visible.
primary_references
[sulforaphane-p23153560] Sulforaphane is not an effective antagonist of the human pregnane X-receptor in vivo. (2013). https://pubmed.ncbi.nlm.nih.gov/23153560/ DOI: 10.1016/j.taap.2012.10.029
tissue_or_cell_type
CYP3A phenotyping with midazolam
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1269–1280
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Three-arm randomized crossover trial · source_derived_draft · unverified_draft
### sulforaphane-cyp3a4-alone-null Sulforaphane alone did not change CYP3A activity in the cohort overall; a high-baseline subgroup showed increased midazolam exposure. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: An average null and an exploratory subgroup signal must both remain visible. organism: Human, 24 healthy adults; humanized-PXR mouse parallel study tissue_or_cell_type: CYP3A phenotyping with midazolam experimental_model: Three-arm randomized crossover trial limitations: Average null result does not exclude individual or other-drug interactions; high-baseline subgroup finding is not a dosing rule. exposure: Rifampicin 300 mg/day, with or without sulforaphane 450 micromol/day for seven days; sulforaphane alone evidence_span: {"source_cache": "artifacts/sulforaphane-research/23153560.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e13099fede346485f6e468497ff2a4754fcae4d0203dde7f54fc9643c0599fec", "start_char": 0, "end_char": 1664, "text_sha256": "e13099fede346485f6e468497ff2a4754fcae4d0203dde7f54fc9643c0599fec"} [sulforaphane-p23153560] Sulforaphane is not an effective antagonist of the human pregnane X-receptor in vivo. (2013). https://pubmed.ncbi.nlm.nih.gov/23153560/ DOI: 10.1016/j.taap.2012.10.029
Complete structured claim and evidence
Sulforaphane caused time-dependent urease inactivation with spectroscopic evidence of cysteine-thiol adduct formation.
Sulforaphane / SFN, stereochemistry specified per study → Helicobacter pylori urease complex source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/23583386.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4542d001efffa337d1aae4de7767a914ed8cd951bc5e56ded5183046abe10577", "start_char": 0, "end_char": 1843, "text_sha256": "4542d001efffa337d1aae4de7767a914ed8cd951bc5e56ded5183046abe10577"}
experimental_model
Purified urease assays and bacterial comparisons
exposure
Sulforaphane and related isothiocyanates
limitations
Urease inactivation was not obligatory for bacterial killing; do not portray one target as the entire antibacterial mechanism.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
H. pylori and jack-bean urease experiments
plain_language
The compound can chemically inhibit a bacterial enzyme.
primary_references
[sulforaphane-p23583386] Urease from Helicobacter pylori is inactivated by sulforaphane and other isothiocyanates. (2013). https://pubmed.ncbi.nlm.nih.gov/23583386/ DOI: 10.1016/j.bbrc.2013.03.126
tissue_or_cell_type
Urease modification and bacterial killing
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1282–1293
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified urease assays and bacterial comparisons · source_derived_draft · unverified_draft
### sulforaphane-urease-inactivation Sulforaphane caused time-dependent urease inactivation with spectroscopic evidence of cysteine-thiol adduct formation. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The compound can chemically inhibit a bacterial enzyme. organism: H. pylori and jack-bean urease experiments tissue_or_cell_type: Urease modification and bacterial killing experimental_model: Purified urease assays and bacterial comparisons limitations: Urease inactivation was not obligatory for bacterial killing; do not portray one target as the entire antibacterial mechanism. exposure: Sulforaphane and related isothiocyanates evidence_span: {"source_cache": "artifacts/sulforaphane-research/23583386.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4542d001efffa337d1aae4de7767a914ed8cd951bc5e56ded5183046abe10577", "start_char": 0, "end_char": 1843, "text_sha256": "4542d001efffa337d1aae4de7767a914ed8cd951bc5e56ded5183046abe10577"} [sulforaphane-p23583386] Urease from Helicobacter pylori is inactivated by sulforaphane and other isothiocyanates. (2013). https://pubmed.ncbi.nlm.nih.gov/23583386/ DOI: 10.1016/j.bbrc.2013.03.126
Complete structured claim and evidence
Sulforaphane killed both urease-positive and urease-negative H. pylori strains.
Sulforaphane / SFN, stereochemistry specified per study → H. pylori viability in culture source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/23583386.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4542d001efffa337d1aae4de7767a914ed8cd951bc5e56ded5183046abe10577", "start_char": 0, "end_char": 1843, "text_sha256": "4542d001efffa337d1aae4de7767a914ed8cd951bc5e56ded5183046abe10577"}
experimental_model
Purified urease assays and bacterial comparisons
exposure
Sulforaphane and related isothiocyanates
limitations
Urease inactivation was not obligatory for bacterial killing; do not portray one target as the entire antibacterial mechanism.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
H. pylori and jack-bean urease experiments
plain_language
The antibacterial effect cannot be explained solely by blocking urease.
primary_references
[sulforaphane-p23583386] Urease from Helicobacter pylori is inactivated by sulforaphane and other isothiocyanates. (2013). https://pubmed.ncbi.nlm.nih.gov/23583386/ DOI: 10.1016/j.bbrc.2013.03.126
tissue_or_cell_type
Urease modification and bacterial killing
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1295–1306
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified urease assays and bacterial comparisons · source_derived_draft · unverified_draft
### sulforaphane-urease-independent-killing Sulforaphane killed both urease-positive and urease-negative H. pylori strains. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The antibacterial effect cannot be explained solely by blocking urease. organism: H. pylori and jack-bean urease experiments tissue_or_cell_type: Urease modification and bacterial killing experimental_model: Purified urease assays and bacterial comparisons limitations: Urease inactivation was not obligatory for bacterial killing; do not portray one target as the entire antibacterial mechanism. exposure: Sulforaphane and related isothiocyanates evidence_span: {"source_cache": "artifacts/sulforaphane-research/23583386.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4542d001efffa337d1aae4de7767a914ed8cd951bc5e56ded5183046abe10577", "start_char": 0, "end_char": 1843, "text_sha256": "4542d001efffa337d1aae4de7767a914ed8cd951bc5e56ded5183046abe10577"} [sulforaphane-p23583386] Urease from Helicobacter pylori is inactivated by sulforaphane and other isothiocyanates. (2013). https://pubmed.ncbi.nlm.nih.gov/23583386/ DOI: 10.1016/j.bbrc.2013.03.126
Complete structured claim and evidence
Urea breath-test and stool-antigen measures declined during broccoli sprout treatment and returned toward baseline after discontinuation.
Broccoli sprout preparation, composition specified per study → Urea breath test and stool H. pylori antigen source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/19349290.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d4d4cc51db00f336baa1c258bae013de96d52dfd8c2433096358bba600e6fbbd", "start_char": 0, "end_char": 1793, "text_sha256": "d4d4cc51db00f336baa1c258bae013de96d52dfd8c2433096358bba600e6fbbd"}
experimental_model
Randomized sprout intervention with a separate knockout-mouse experiment
exposure
70 g/day broccoli sprouts containing 420 micromol precursor versus alfalfa for eight weeks
limitations
Whole-food intervention; reduced biomarkers did not establish durable eradication or replace antibiotic therapy.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human, 48 H. pylori-infected participants; mouse study distinct
plain_language
The effect was temporary and was not proof of durable eradication.
primary_references
[sulforaphane-p19349290] Dietary sulforaphane-rich broccoli sprouts reduce colonization and attenuate gastritis in Helicobacter pylori-infected mice and humans. (2009). https://pubmed.ncbi.nlm.nih.gov/19349290/ DOI: 10.1158/1940-6207.capr-08-0192
tissue_or_cell_type
Colonization and inflammation biomarkers
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1308–1319
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized sprout intervention with a separate knockout-mouse experiment · source_derived_draft · unverified_draft
### sulforaphane-hpy-biomarkers Urea breath-test and stool-antigen measures declined during broccoli sprout treatment and returned toward baseline after discontinuation. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The effect was temporary and was not proof of durable eradication. organism: Human, 48 H. pylori-infected participants; mouse study distinct tissue_or_cell_type: Colonization and inflammation biomarkers experimental_model: Randomized sprout intervention with a separate knockout-mouse experiment limitations: Whole-food intervention; reduced biomarkers did not establish durable eradication or replace antibiotic therapy. exposure: 70 g/day broccoli sprouts containing 420 micromol precursor versus alfalfa for eight weeks evidence_span: {"source_cache": "artifacts/sulforaphane-research/19349290.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d4d4cc51db00f336baa1c258bae013de96d52dfd8c2433096358bba600e6fbbd", "start_char": 0, "end_char": 1793, "text_sha256": "d4d4cc51db00f336baa1c258bae013de96d52dfd8c2433096358bba600e6fbbd"} [sulforaphane-p19349290] Dietary sulforaphane-rich broccoli sprouts reduce colonization and attenuate gastritis in Helicobacter pylori-infected mice and humans. (2009). https://pubmed.ncbi.nlm.nih.gov/19349290/ DOI: 10.1158/1940-6207.capr-08-0192
Complete structured claim and evidence
Serum pepsinogens I and II declined during the human intervention and recovered after it ended.
Broccoli sprout preparation, composition specified per study → Serum pepsinogen I and II source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/19349290.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d4d4cc51db00f336baa1c258bae013de96d52dfd8c2433096358bba600e6fbbd", "start_char": 0, "end_char": 1793, "text_sha256": "d4d4cc51db00f336baa1c258bae013de96d52dfd8c2433096358bba600e6fbbd"}
experimental_model
Randomized sprout intervention with a separate knockout-mouse experiment
exposure
70 g/day broccoli sprouts containing 420 micromol precursor versus alfalfa for eight weeks
limitations
Whole-food intervention; reduced biomarkers did not establish durable eradication or replace antibiotic therapy.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human, 48 H. pylori-infected participants; mouse study distinct
plain_language
Inflammation-related markers changed alongside colonization markers.
primary_references
[sulforaphane-p19349290] Dietary sulforaphane-rich broccoli sprouts reduce colonization and attenuate gastritis in Helicobacter pylori-infected mice and humans. (2009). https://pubmed.ncbi.nlm.nih.gov/19349290/ DOI: 10.1158/1940-6207.capr-08-0192
tissue_or_cell_type
Colonization and inflammation biomarkers
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1321–1332
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized sprout intervention with a separate knockout-mouse experiment · source_derived_draft · unverified_draft
### sulforaphane-hpy-inflammation Serum pepsinogens I and II declined during the human intervention and recovered after it ended. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Inflammation-related markers changed alongside colonization markers. organism: Human, 48 H. pylori-infected participants; mouse study distinct tissue_or_cell_type: Colonization and inflammation biomarkers experimental_model: Randomized sprout intervention with a separate knockout-mouse experiment limitations: Whole-food intervention; reduced biomarkers did not establish durable eradication or replace antibiotic therapy. exposure: 70 g/day broccoli sprouts containing 420 micromol precursor versus alfalfa for eight weeks evidence_span: {"source_cache": "artifacts/sulforaphane-research/19349290.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d4d4cc51db00f336baa1c258bae013de96d52dfd8c2433096358bba600e6fbbd", "start_char": 0, "end_char": 1793, "text_sha256": "d4d4cc51db00f336baa1c258bae013de96d52dfd8c2433096358bba600e6fbbd"} [sulforaphane-p19349290] Dietary sulforaphane-rich broccoli sprouts reduce colonization and attenuate gastritis in Helicobacter pylori-infected mice and humans. (2009). https://pubmed.ncbi.nlm.nih.gov/19349290/ DOI: 10.1158/1940-6207.capr-08-0192
Complete structured claim and evidence
The active group showed a 34% ABC-score reduction at 18 weeks, with a significant between-treatment comparison.
Sulforaphane / SFN, stereochemistry specified per study → Aberrant Behavior Checklist score, population specified source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/25313065.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d6f39bcdb3d5d89fd9226e208c82da13d9f18fee2003a8c817c67da0e344fd44", "start_char": 0, "end_char": 1872, "text_sha256": "d6f39bcdb3d5d89fd9226e208c82da13d9f18fee2003a8c817c67da0e344fd44"}
experimental_model
Randomized double-blind placebo-controlled trial
exposure
Sulforaphane 50-150 micromol/day for 18 weeks, then four weeks off
limitations
Small male-only study; symptom-scale changes are not a cure and do not establish mechanism.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human, 44 males aged 13-27, 29 active and 15 placebo
plain_language
One early trial reported improvement in this symptom scale.
primary_references
[sulforaphane-p25313065] Sulforaphane treatment of autism spectrum disorder (ASD). (2014). https://pubmed.ncbi.nlm.nih.gov/25313065/ DOI: 10.1073/pnas.1416940111
tissue_or_cell_type
ABC and SRS behavioral ratings
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1334–1345
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized double-blind placebo-controlled trial · source_derived_draft · unverified_draft
### sulforaphane-autism-abc-early The active group showed a 34% ABC-score reduction at 18 weeks, with a significant between-treatment comparison. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: One early trial reported improvement in this symptom scale. organism: Human, 44 males aged 13-27, 29 active and 15 placebo tissue_or_cell_type: ABC and SRS behavioral ratings experimental_model: Randomized double-blind placebo-controlled trial limitations: Small male-only study; symptom-scale changes are not a cure and do not establish mechanism. exposure: Sulforaphane 50-150 micromol/day for 18 weeks, then four weeks off evidence_span: {"source_cache": "artifacts/sulforaphane-research/25313065.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d6f39bcdb3d5d89fd9226e208c82da13d9f18fee2003a8c817c67da0e344fd44", "start_char": 0, "end_char": 1872, "text_sha256": "d6f39bcdb3d5d89fd9226e208c82da13d9f18fee2003a8c817c67da0e344fd44"} [sulforaphane-p25313065] Sulforaphane treatment of autism spectrum disorder (ASD). (2014). https://pubmed.ncbi.nlm.nih.gov/25313065/ DOI: 10.1073/pnas.1416940111
Complete structured claim and evidence
SRS scores fell 17% in the active group; scores on the measured scales moved toward baseline after stopping treatment.
Sulforaphane / SFN, stereochemistry specified per study → Social Responsiveness Scale score, version specified source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/25313065.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d6f39bcdb3d5d89fd9226e208c82da13d9f18fee2003a8c817c67da0e344fd44", "start_char": 0, "end_char": 1872, "text_sha256": "d6f39bcdb3d5d89fd9226e208c82da13d9f18fee2003a8c817c67da0e344fd44"}
experimental_model
Randomized double-blind placebo-controlled trial
exposure
Sulforaphane 50-150 micromol/day for 18 weeks, then four weeks off
limitations
Small male-only study; symptom-scale changes are not a cure and do not establish mechanism.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human, 44 males aged 13-27, 29 active and 15 placebo
plain_language
The reported effect was not sustained unchanged after withdrawal.
primary_references
[sulforaphane-p25313065] Sulforaphane treatment of autism spectrum disorder (ASD). (2014). https://pubmed.ncbi.nlm.nih.gov/25313065/ DOI: 10.1073/pnas.1416940111
tissue_or_cell_type
ABC and SRS behavioral ratings
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1347–1358
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized double-blind placebo-controlled trial · source_derived_draft · unverified_draft
### sulforaphane-autism-srs-early SRS scores fell 17% in the active group; scores on the measured scales moved toward baseline after stopping treatment. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The reported effect was not sustained unchanged after withdrawal. organism: Human, 44 males aged 13-27, 29 active and 15 placebo tissue_or_cell_type: ABC and SRS behavioral ratings experimental_model: Randomized double-blind placebo-controlled trial limitations: Small male-only study; symptom-scale changes are not a cure and do not establish mechanism. exposure: Sulforaphane 50-150 micromol/day for 18 weeks, then four weeks off evidence_span: {"source_cache": "artifacts/sulforaphane-research/25313065.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d6f39bcdb3d5d89fd9226e208c82da13d9f18fee2003a8c817c67da0e344fd44", "start_char": 0, "end_char": 1872, "text_sha256": "d6f39bcdb3d5d89fd9226e208c82da13d9f18fee2003a8c817c67da0e344fd44"} [sulforaphane-p25313065] Sulforaphane treatment of autism spectrum disorder (ASD). (2014). https://pubmed.ncbi.nlm.nih.gov/25313065/ DOI: 10.1073/pnas.1416940111
Complete structured claim and evidence
The primary OACIS comparison did not significantly differ between active and placebo groups at seven or 15 weeks.
Glucoraphanin plus active myrosinase preparation → Ohio Autism Clinical Impressions Scale primary outcome source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/34034808.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1b60b5ce85bab14b43239e810410dd230703600eac55bc8960c621ae7de881a4", "start_char": 0, "end_char": 3223, "text_sha256": "1b60b5ce85bab14b43239e810410dd230703600eac55bc8960c621ae7de881a4"}
experimental_model
Randomized double-blind trial followed by open-label and withdrawal phases
exposure
Glucoraphanin plus active myrosinase tablets, not preformed sulforaphane; 15 weeks randomized, 15 weeks open-label, six weeks off
limitations
Primary endpoint was nonsignificant. The published correction (PMID 34134777, DOI 10.1186/s13229-021-00451-9) clarifies the preparation: 34 micromol glucoraphanin per tablet, calculated to yield about 15 micromol sulforaphane. Open-label analyses are nonrandomized.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human, 57 children aged 3-12 randomized; 45 analyzed
plain_language
The main outcome did not confirm the hoped-for benefit.
primary_references
[sulforaphane-p34034808] Randomized controlled trial of sulforaphane and metabolite discovery in children with Autism Spectrum Disorder. (2021). https://pubmed.ncbi.nlm.nih.gov/34034808/ DOI: 10.1186/s13229-021-00447-5
tissue_or_cell_type
Primary OACIS and secondary caregiver ratings
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1360–1371
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized double-blind trial followed by open-label and withdrawal phases · source_derived_draft · unverified_draft
### sulforaphane-autism-primary-null The primary OACIS comparison did not significantly differ between active and placebo groups at seven or 15 weeks. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The main outcome did not confirm the hoped-for benefit. organism: Human, 57 children aged 3-12 randomized; 45 analyzed tissue_or_cell_type: Primary OACIS and secondary caregiver ratings experimental_model: Randomized double-blind trial followed by open-label and withdrawal phases limitations: Primary endpoint was nonsignificant. The published correction (PMID 34134777, DOI 10.1186/s13229-021-00451-9) clarifies the preparation: 34 micromol glucoraphanin per tablet, calculated to yield about 15 micromol sulforaphane. Open-label analyses are nonrandomized. exposure: Glucoraphanin plus active myrosinase tablets, not preformed sulforaphane; 15 weeks randomized, 15 weeks open-label, six weeks off evidence_span: {"source_cache": "artifacts/sulforaphane-research/34034808.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1b60b5ce85bab14b43239e810410dd230703600eac55bc8960c621ae7de881a4", "start_char": 0, "end_char": 3223, "text_sha256": "1b60b5ce85bab14b43239e810410dd230703600eac55bc8960c621ae7de881a4"} [sulforaphane-p34034808] Randomized controlled trial of sulforaphane and metabolite discovery in children with Autism Spectrum Disorder. (2021). https://pubmed.ncbi.nlm.nih.gov/34034808/ DOI: 10.1186/s13229-021-00447-5
Complete structured claim and evidence
Caregiver ABC scores improved at 15 weeks, but SRS-2 did not significantly improve.
Glucoraphanin plus active myrosinase preparation → Aberrant Behavior Checklist score, population specified source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/34034808.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1b60b5ce85bab14b43239e810410dd230703600eac55bc8960c621ae7de881a4", "start_char": 0, "end_char": 3223, "text_sha256": "1b60b5ce85bab14b43239e810410dd230703600eac55bc8960c621ae7de881a4"}
experimental_model
Randomized double-blind trial followed by open-label and withdrawal phases
exposure
Glucoraphanin plus active myrosinase tablets, not preformed sulforaphane; 15 weeks randomized, 15 weeks open-label, six weeks off
limitations
Primary endpoint was nonsignificant. The published correction (PMID 34134777, DOI 10.1186/s13229-021-00451-9) clarifies the preparation: 34 micromol glucoraphanin per tablet, calculated to yield about 15 micromol sulforaphane. Open-label analyses are nonrandomized.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human, 57 children aged 3-12 randomized; 45 analyzed
plain_language
Different secondary measures gave different results.
primary_references
[sulforaphane-p34034808] Randomized controlled trial of sulforaphane and metabolite discovery in children with Autism Spectrum Disorder. (2021). https://pubmed.ncbi.nlm.nih.gov/34034808/ DOI: 10.1186/s13229-021-00447-5
tissue_or_cell_type
Primary OACIS and secondary caregiver ratings
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1373–1384
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized double-blind trial followed by open-label and withdrawal phases · source_derived_draft · unverified_draft
### sulforaphane-autism-secondary-abc Caregiver ABC scores improved at 15 weeks, but SRS-2 did not significantly improve. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Different secondary measures gave different results. organism: Human, 57 children aged 3-12 randomized; 45 analyzed tissue_or_cell_type: Primary OACIS and secondary caregiver ratings experimental_model: Randomized double-blind trial followed by open-label and withdrawal phases limitations: Primary endpoint was nonsignificant. The published correction (PMID 34134777, DOI 10.1186/s13229-021-00451-9) clarifies the preparation: 34 micromol glucoraphanin per tablet, calculated to yield about 15 micromol sulforaphane. Open-label analyses are nonrandomized. exposure: Glucoraphanin plus active myrosinase tablets, not preformed sulforaphane; 15 weeks randomized, 15 weeks open-label, six weeks off evidence_span: {"source_cache": "artifacts/sulforaphane-research/34034808.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1b60b5ce85bab14b43239e810410dd230703600eac55bc8960c621ae7de881a4", "start_char": 0, "end_char": 3223, "text_sha256": "1b60b5ce85bab14b43239e810410dd230703600eac55bc8960c621ae7de881a4"} [sulforaphane-p34034808] Randomized controlled trial of sulforaphane and metabolite discovery in children with Autism Spectrum Disorder. (2021). https://pubmed.ncbi.nlm.nih.gov/34034808/ DOI: 10.1186/s13229-021-00447-5
Complete structured claim and evidence
The study found no significant clinical improvement on ADOS-2, ABC or SRS-2 in the younger-child cohort.
Sulforaphane / SFN, stereochemistry specified per study → ADOS-2 assessment score source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/36771424.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "b571349cae03a080b09b387fa132d9f534133caef7a187be028370a9db48636e", "start_char": 0, "end_char": 1410, "text_sha256": "b571349cae03a080b09b387fa132d9f534133caef7a187be028370a9db48636e"}
experimental_model
Prospective randomized double-blind placebo-controlled study
exposure
Assessments at baseline, 18 and 36 weeks
limitations
Small sample with attrition; different age/formulation/endpoint context is retained rather than automatically classified as a contradiction.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human, children aged 3-7; 40 randomized and 28 completed
plain_language
Later testing did not reproduce a clear benefit in this population.
primary_references
[sulforaphane-p36771424] Sulforaphane Treatment in Children with Autism: A Prospective Randomized Double-Blind Study. (2023). https://pubmed.ncbi.nlm.nih.gov/36771424/ DOI: 10.3390/nu15030718
tissue_or_cell_type
ABC, SRS-2 and ADOS-2
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1386–1397
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Prospective randomized double-blind placebo-controlled study · source_derived_draft · unverified_draft
### sulforaphane-autism-younger-null The study found no significant clinical improvement on ADOS-2, ABC or SRS-2 in the younger-child cohort. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Later testing did not reproduce a clear benefit in this population. organism: Human, children aged 3-7; 40 randomized and 28 completed tissue_or_cell_type: ABC, SRS-2 and ADOS-2 experimental_model: Prospective randomized double-blind placebo-controlled study limitations: Small sample with attrition; different age/formulation/endpoint context is retained rather than automatically classified as a contradiction. exposure: Assessments at baseline, 18 and 36 weeks evidence_span: {"source_cache": "artifacts/sulforaphane-research/36771424.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "b571349cae03a080b09b387fa132d9f534133caef7a187be028370a9db48636e", "start_char": 0, "end_char": 1410, "text_sha256": "b571349cae03a080b09b387fa132d9f534133caef7a187be028370a9db48636e"} [sulforaphane-p36771424] Sulforaphane Treatment in Children with Autism: A Prospective Randomized Double-Blind Study. (2023). https://pubmed.ncbi.nlm.nih.gov/36771424/ DOI: 10.3390/nu15030718
Complete structured claim and evidence
Clinician-rated scales improved, whereas caregiver-rated scales did not significantly differ from placebo.
Sulforaphane / SFN, stereochemistry specified per study → Clinician-rated autism trial outcomes source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/sulforaphane-research/36427174.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "82957fc566b0bccc87dd6f53d6ad61edfa3d5b0b99ba6f557628c68f53faf1cc", "start_char": 0, "end_char": 826, "text_sha256": "82957fc566b0bccc87dd6f53d6ad61edfa3d5b0b99ba6f557628c68f53faf1cc"}
experimental_model
Randomized double-blind multicenter trial
exposure
Twelve-week treatment comparison
limitations
Rater-dependent results need replication; do not select only the favorable scale.
nutrient_topic
Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
organism
Human, 108 participants with ASD in China
plain_language
The trial did not give one consistent result across observers.
primary_references
[sulforaphane-p36427174] Efficacy of Sulforaphane in Treatment of Children with Autism Spectrum Disorder: A Randomized Double-Blind Placebo-Controlled Multi-center Trial. (2024). https://pubmed.ncbi.nlm.nih.gov/36427174/ DOI: 10.1007/s10803-022-05784-9
tissue_or_cell_type
Caregiver versus clinician outcome ratings
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 1399–1410
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Randomized double-blind multicenter trial · source_derived_draft · unverified_draft
### sulforaphane-autism-rater-difference Clinician-rated scales improved, whereas caregiver-rated scales did not significantly differ from placebo. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The trial did not give one consistent result across observers. organism: Human, 108 participants with ASD in China tissue_or_cell_type: Caregiver versus clinician outcome ratings experimental_model: Randomized double-blind multicenter trial limitations: Rater-dependent results need replication; do not select only the favorable scale. exposure: Twelve-week treatment comparison evidence_span: {"source_cache": "artifacts/sulforaphane-research/36427174.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "82957fc566b0bccc87dd6f53d6ad61edfa3d5b0b99ba6f557628c68f53faf1cc", "start_char": 0, "end_char": 826, "text_sha256": "82957fc566b0bccc87dd6f53d6ad61edfa3d5b0b99ba6f557628c68f53faf1cc"} [sulforaphane-p36427174] Efficacy of Sulforaphane in Treatment of Children with Autism Spectrum Disorder: A Randomized Double-Blind Placebo-Controlled Multi-center Trial. (2024). https://pubmed.ncbi.nlm.nih.gov/36427174/ DOI: 10.1007/s10803-022-05784-9
Complete structured claim and evidence
GSR reduces one glutathione-disulfide molecule to two reduced glutathione molecules using the NADPH/FAD catalytic relay.
Glutathione reductase / GSR → GSSG source_derived_draftungraded
Experimental context and source evidence
cross_nutrient
B2-FAD supports GSH recycling; selenium-dependent GPX use of GSH is a separate reaction.
evidence_location
Results: NADPH binding; Fig 1 consensus cycle; GSH/GSSG complexes
experimental_model
Purified human glutathione reductase crystals with natural substrates, 0.95-1.1-A resolution, chemically reduced controls.
exposure
Purified-enzyme assay
limitations
GSR is not glutathione peroxidase; this record does not show that B2 improves selenium repletion.
nutrient_topic
Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
organism
Homo sapiens
plain_language
This enzyme recycles glutathione after oxidation.
primary_references
[berkholz2008] Catalytic cycle of human glutathione reductase near 1 A resolution. (2008). https://pubmed.ncbi.nlm.nih.gov/18638483/ DOI: 10.1016/j.jmb.2008.06.083
tissue_or_cell_type
Purified human GSR
Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1332–1344
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human glutathione reductase crystals with natural substrates, 0.95-1.1-A resolution, chemically reduced controls. · source_derived_draft · unverified_draft
### b2-gsr-gssg-to-gsh GSR reduces one glutathione-disulfide molecule to two reduced glutathione molecules using the NADPH/FAD catalytic relay. Condition category: normal nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: This enzyme recycles glutathione after oxidation. organism: Homo sapiens tissue_or_cell_type: Purified human GSR experimental_model: Purified human glutathione reductase crystals with natural substrates, 0.95-1.1-A resolution, chemically reduced controls. limitations: GSR is not glutathione peroxidase; this record does not show that B2 improves selenium repletion. exposure: Purified-enzyme assay cross_nutrient: B2-FAD supports GSH recycling; selenium-dependent GPX use of GSH is a separate reaction. evidence_location: Results: NADPH binding; Fig 1 consensus cycle; GSH/GSSG complexes [berkholz2008] Catalytic cycle of human glutathione reductase near 1 A resolution. (2008). https://pubmed.ncbi.nlm.nih.gov/18638483/ DOI: 10.1016/j.jmb.2008.06.083
Complete structured claim and evidence
Human GSR substrate structures place NADPH for hydride transfer to bound FAD, the first redox step in glutathione recycling.
NADPH → FAD source_derived_draftungraded
Experimental context and source evidence
cross_nutrient
Nicotinamide-containing NADPH and B2-derived FAD perform distinct functions.
evidence_location
Results: NADPH binding; Fig 1 consensus cycle; GSH/GSSG complexes
experimental_model
Purified human glutathione reductase crystals with natural substrates, 0.95-1.1-A resolution, chemically reduced controls.
exposure
Purified-enzyme assay
limitations
Structural support for the established catalytic cycle; radiation reduction must be distinguished from natural catalysis.
nutrient_topic
Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
organism
Homo sapiens
plain_language
NADPH supplies electrons to the B2-derived cofactor.
primary_references
[berkholz2008] Catalytic cycle of human glutathione reductase near 1 A resolution. (2008). https://pubmed.ncbi.nlm.nih.gov/18638483/ DOI: 10.1016/j.jmb.2008.06.083
tissue_or_cell_type
Purified human erythrocyte-type GSR crystals
Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1304–1316
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human glutathione reductase crystals with natural substrates, 0.95-1.1-A resolution, chemically reduced controls. · source_derived_draft · unverified_draft
### b2-gsr-nadph-to-fad Human GSR substrate structures place NADPH for hydride transfer to bound FAD, the first redox step in glutathione recycling. Condition category: normal nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: NADPH supplies electrons to the B2-derived cofactor. organism: Homo sapiens tissue_or_cell_type: Purified human erythrocyte-type GSR crystals experimental_model: Purified human glutathione reductase crystals with natural substrates, 0.95-1.1-A resolution, chemically reduced controls. limitations: Structural support for the established catalytic cycle; radiation reduction must be distinguished from natural catalysis. exposure: Purified-enzyme assay cross_nutrient: Nicotinamide-containing NADPH and B2-derived FAD perform distinct functions. evidence_location: Results: NADPH binding; Fig 1 consensus cycle; GSH/GSSG complexes [berkholz2008] Catalytic cycle of human glutathione reductase near 1 A resolution. (2008). https://pubmed.ncbi.nlm.nih.gov/18638483/ DOI: 10.1016/j.jmb.2008.06.083
Complete structured claim and evidence
Human CTH cleaves cystathionine to cysteine, 2-oxobutanoate and ammonia in a PLP-dependent reaction.
Human cystathionine gamma-lyase / CTH → Cystathionine source_derived_draftungraded
Experimental context and source evidence
cross_nutrient
B6-dependent sulfur transfer supplies cysteine; glutathione synthesis requires additional enzymes.
experimental_model
Purified human CTH apo/holo crystal structures and assays
limitations
Purified-enzyme evidence does not define dietary requirements or cellular PLP thresholds.
nutrient_topic
Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B6
organism
Homo sapiens
plain_language
This step releases cysteine for downstream metabolism.
primary_references
[b6-cth-structure-2009] Structural Basis for the Inhibition Mechanism of Human Cystathionine gamma-Lyase, an Enzyme Responsible for the Production of H2S (2009). https://doi.org/10.1074/jbc.M805459200 DOI: 10.1074/jbc.M805459200
tissue_or_cell_type
Purified recombinant protein; no intact tissue
Vitamin B6: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 554–564
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human CTH apo/holo crystal structures and assays · source_derived_draft · unverified_draft
### b6-met-cth-cleavage Human CTH cleaves cystathionine to cysteine, 2-oxobutanoate and ammonia in a PLP-dependent reaction. Condition category: normal nutrient_topic: Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. plain_language: This step releases cysteine for downstream metabolism. organism: Homo sapiens tissue_or_cell_type: Purified recombinant protein; no intact tissue experimental_model: Purified human CTH apo/holo crystal structures and assays limitations: Purified-enzyme evidence does not define dietary requirements or cellular PLP thresholds. cross_nutrient: B6-dependent sulfur transfer supplies cysteine; glutathione synthesis requires additional enzymes. [b6-cth-structure-2009] Structural Basis for the Inhibition Mechanism of Human Cystathionine gamma-Lyase, an Enzyme Responsible for the Production of H2S (2009). https://doi.org/10.1074/jbc.M805459200 DOI: 10.1074/jbc.M805459200
Complete structured claim and evidence
Tracing in a cultured human hepatoma cell line estimated that transsulfuration supplied homocysteine-derived sulfur to approximately half of the intracellular glutathione pool.
Homocysteine → GSH source_derived_draftungraded
Experimental context and source evidence
cross_nutrient
B6-dependent transsulfuration connects methionine/homocysteine to the cysteine supply for glutathione.
experimental_model
Cultured human hepatoma cell line; metabolic sulfur tracing
limitations
Fraction is culture-specific and traces sulfur, not all glutathione atoms; this experiment did not measure dietary B6 depletion.
nutrient_topic
Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B6
organism
Homo sapiens
plain_language
In this cell system, sulfur routed through B6-dependent enzymes helped supply glutathione.
primary_references
[b6-glutathione-2000] The quantitatively important relationship between homocysteine metabolism and glutathione synthesis by the transsulfuration pathway and its regulation by redox changes (2000). https://pubmed.ncbi.nlm.nih.gov/11041866/ DOI: 10.1021/bi001088w
tissue_or_cell_type
Cultured human hepatoma cell line
Vitamin B6: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 590–600
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cultured human hepatoma cell line; metabolic sulfur tracing · source_derived_draft · unverified_draft
### b6-met-transsulfuration-glutathione Tracing in a cultured human hepatoma cell line estimated that transsulfuration supplied homocysteine-derived sulfur to approximately half of the intracellular glutathione pool. Condition category: normal nutrient_topic: Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. plain_language: In this cell system, sulfur routed through B6-dependent enzymes helped supply glutathione. organism: Homo sapiens tissue_or_cell_type: Cultured human hepatoma cell line experimental_model: Cultured human hepatoma cell line; metabolic sulfur tracing limitations: Fraction is culture-specific and traces sulfur, not all glutathione atoms; this experiment did not measure dietary B6 depletion. cross_nutrient: B6-dependent transsulfuration connects methionine/homocysteine to the cysteine supply for glutathione. [b6-glutathione-2000] The quantitatively important relationship between homocysteine metabolism and glutathione synthesis by the transsulfuration pathway and its regulation by redox changes (2000). https://pubmed.ncbi.nlm.nih.gov/11041866/ DOI: 10.1021/bi001088w
Complete structured claim and evidence
Mammalian TrxR1 reduced ubiquinone-10 to ubiquinol-10.
TXNRD1 → Ubiquinone-10 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/coq10-research/12435734.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "929e8de2bc15ea62eb4a3814995fd289de759d721f16b848174ad65f95847c55", "start_char": 0, "end_char": 1340, "text_sha256": "929e8de2bc15ea62eb4a3814995fd289de759d721f16b848174ad65f95847c55"}
experimental_model
Enzyme kinetics, mutants and overexpressing-cell homogenates
exposure
NADPH or NADH; selenite and selenium-deprived enzyme variants
limitations
Biochemical selenium dependence; not proof that all CoQ recycling stops with low selenium or that combined supplements are synergistic clinically.
nutrient_topic
Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. · Coenzyme Q10 / CoQ10 redox system
organism
Mammalian TrxR1 and human HEK293 cells
plain_language
A selenium-dependent enzyme can regenerate the antioxidant form of CoQ.
primary_references
[coq10-p12435734] The mammalian cytosolic selenoenzyme thioredoxin reductase reduces ubiquinone. A novel mechanism for defense against oxidative stress. (2003). https://pubmed.ncbi.nlm.nih.gov/12435734/ DOI: 10.1074/jbc.m210456200
tissue_or_cell_type
Ubiquinone reduction
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17) · lines 762–773
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Enzyme kinetics, mutants and overexpressing-cell homogenates · source_derived_draft · unverified_draft
### coq10-txnrd1-coq Mammalian TrxR1 reduced ubiquinone-10 to ubiquinol-10. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A selenium-dependent enzyme can regenerate the antioxidant form of CoQ. organism: Mammalian TrxR1 and human HEK293 cells tissue_or_cell_type: Ubiquinone reduction experimental_model: Enzyme kinetics, mutants and overexpressing-cell homogenates limitations: Biochemical selenium dependence; not proof that all CoQ recycling stops with low selenium or that combined supplements are synergistic clinically. exposure: NADPH or NADH; selenite and selenium-deprived enzyme variants evidence_span: {"source_cache": "artifacts/coq10-research/12435734.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "929e8de2bc15ea62eb4a3814995fd289de759d721f16b848174ad65f95847c55", "start_char": 0, "end_char": 1340, "text_sha256": "929e8de2bc15ea62eb4a3814995fd289de759d721f16b848174ad65f95847c55"} [coq10-p12435734] The mammalian cytosolic selenoenzyme thioredoxin reductase reduces ubiquinone. A novel mechanism for defense against oxidative stress. (2003). https://pubmed.ncbi.nlm.nih.gov/12435734/ DOI: 10.1074/jbc.m210456200
Complete structured claim and evidence
Increased extracellular cysteine supported cellular uptake and glutathione synthesis, bypassing dependence on cystine transport in the studied cells.
Cellular cysteine uptake → Cellular reduced-glutathione pool source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/ala-research/9288403.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6a14c857d89c580ffe8866d7e5f06658dcc806429ae3a4b8ad4bd096f664a2e2", "start_char": 0, "end_char": 1497, "text_sha256": "6a14c857d89c580ffe8866d7e5f06658dcc806429ae3a4b8ad4bd096f664a2e2"}
experimental_model
Cell-culture thiol transport and glutathione experiments
exposure
Lipoic acid/DHLA treatment and extracellular thiol measurements
limitations
Cell-type and extracellular-substrate dependence; no demonstration of general methylation-vitamin depletion.
nutrient_topic
Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. · Lipoic acid
organism
Human, rat and mouse cells as specified
plain_language
The cells could import ready-to-use cysteine instead of relying on cystine uptake.
primary_references
[ala-p9288403] Lipoic acid increases de novo synthesis of cellular glutathione by improving cystine utilization. (1997). https://pubmed.ncbi.nlm.nih.gov/9288403/ DOI: 10.1002/biof.5520060303
tissue_or_cell_type
Human lymphocytes, Jurkat cells and erythrocytes; rat C6 and mouse NB41A3 cells
Alpha-lipoic acid: cofactor assembly, redox signaling and nutrient interactions (2026-09-17) · lines 806–817
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cell-culture thiol transport and glutathione experiments · source_derived_draft · unverified_draft
### ala-cysteine-gsh-route Increased extracellular cysteine supported cellular uptake and glutathione synthesis, bypassing dependence on cystine transport in the studied cells. Condition category: normal nutrient_topic: Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: The cells could import ready-to-use cysteine instead of relying on cystine uptake. organism: Human, rat and mouse cells as specified tissue_or_cell_type: Human lymphocytes, Jurkat cells and erythrocytes; rat C6 and mouse NB41A3 cells experimental_model: Cell-culture thiol transport and glutathione experiments limitations: Cell-type and extracellular-substrate dependence; no demonstration of general methylation-vitamin depletion. exposure: Lipoic acid/DHLA treatment and extracellular thiol measurements evidence_span: {"source_cache": "artifacts/ala-research/9288403.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6a14c857d89c580ffe8866d7e5f06658dcc806429ae3a4b8ad4bd096f664a2e2", "start_char": 0, "end_char": 1497, "text_sha256": "6a14c857d89c580ffe8866d7e5f06658dcc806429ae3a4b8ad4bd096f664a2e2"} [ala-p9288403] Lipoic acid increases de novo synthesis of cellular glutathione by improving cystine utilization. (1997). https://pubmed.ncbi.nlm.nih.gov/9288403/ DOI: 10.1002/biof.5520060303
Complete structured claim and evidence
In the human MMACHC dealkylation study, cysteine and homocysteine did not substitute for glutathione as the thiol co-substrate.
GSH → MMACHC-catalyzed alkylcobalamin dealkylation source_derived_draftungraded
Experimental context and source evidence
cross_nutrient
true
evidence_location
Primary abstract; indexed article Introduction/Figure 1
experimental_model
Purified human MMACHC thiol substitution assays
exposure
GSH versus cysteine or homocysteine
limitations
No implication that cysteine availability is irrelevant to cellular GSH synthesis; that upstream pathway was not tested here.
nutrient_topic
Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B12 (cobalamins)
organism
Homo sapiens
plain_language
Having a thiol group was not enough; the enzyme required glutathione in these assays.
primary_references
[kim-2009-gsh-dealkylation] A human vitamin B12 trafficking protein uses glutathione transferase activity for processing alkylcobalamins (2009). https://pubmed.ncbi.nlm.nih.gov/19801555/ DOI: 10.1074/jbc.M109.057877
tissue_or_cell_type
Cell-free assay
Vitamin B12: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 739–751
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human MMACHC thiol substitution assays · source_derived_draft · unverified_draft
### b12-mmachc-thiol-specificity In the human MMACHC dealkylation study, cysteine and homocysteine did not substitute for glutathione as the thiol co-substrate. Condition category: normal nutrient_topic: Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Having a thiol group was not enough; the enzyme required glutathione in these assays. organism: Homo sapiens tissue_or_cell_type: Cell-free assay experimental_model: Purified human MMACHC thiol substitution assays limitations: No implication that cysteine availability is irrelevant to cellular GSH synthesis; that upstream pathway was not tested here. exposure: GSH versus cysteine or homocysteine cross_nutrient: true evidence_location: Primary abstract; indexed article Introduction/Figure 1 [kim-2009-gsh-dealkylation] A human vitamin B12 trafficking protein uses glutathione transferase activity for processing alkylcobalamins (2009). https://pubmed.ncbi.nlm.nih.gov/19801555/ DOI: 10.1074/jbc.M109.057877
Complete structured claim and evidence
Apo-10-prime-lycopenoic acid induced NQO1 in BEAS-2B cells.
Apo-10-prime-lycopenoic acid → Human NAD(P)H quinone dehydrogenase 1 / NQO1 source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/lycopene-research/18566994.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e34a21bb159c3e48372fd5cb104bfa50572903a5ef168b10100976a718b7b534", "start_char": 0, "end_char": 1416, "text_sha256": "e34a21bb159c3e48372fd5cb104bfa50572903a5ef168b10100976a718b7b534"}
experimental_model
Metabolite exposure and gene/protein/redox measurements
exposure
Time- and dose-dependent apo-10-prime-lycopenoid exposure
limitations
Cell-culture metabolite results do not prove oral lycopene reaches equivalent tissue concentrations or prevents human cancer.
nutrient_topic
Lycopene research collection; topical membership is not evidence of a direct dietary effect. · Lycopene
organism
Human BEAS-2B bronchial epithelial cells
plain_language
This shares a protective enzyme node with other compounds already in the ledger.
primary_references
[lycopene-p18566994] Enzymatic metabolites of lycopene induce Nrf2-mediated expression of phase II detoxifying/antioxidant enzymes in human bronchial epithelial cells. (2008). https://pubmed.ncbi.nlm.nih.gov/18566994/ DOI: 10.1002/ijc.23696
tissue_or_cell_type
Nucleus, antioxidant enzymes and intracellular glutathione
Lycopene: absorption, metabolism, nutrient connections and human outcomes (2026-09-17) · lines 520–531
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Metabolite exposure and gene/protein/redox measurements · source_derived_draft · unverified_draft
### lycopene-apo-nqo1 Apo-10-prime-lycopenoic acid induced NQO1 in BEAS-2B cells. Condition category: normal nutrient_topic: Lycopene research collection; topical membership is not evidence of a direct dietary effect. plain_language: This shares a protective enzyme node with other compounds already in the ledger. organism: Human BEAS-2B bronchial epithelial cells tissue_or_cell_type: Nucleus, antioxidant enzymes and intracellular glutathione experimental_model: Metabolite exposure and gene/protein/redox measurements limitations: Cell-culture metabolite results do not prove oral lycopene reaches equivalent tissue concentrations or prevents human cancer. exposure: Time- and dose-dependent apo-10-prime-lycopenoid exposure evidence_span: {"source_cache": "artifacts/lycopene-research/18566994.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e34a21bb159c3e48372fd5cb104bfa50572903a5ef168b10100976a718b7b534", "start_char": 0, "end_char": 1416, "text_sha256": "e34a21bb159c3e48372fd5cb104bfa50572903a5ef168b10100976a718b7b534"} [lycopene-p18566994] Enzymatic metabolites of lycopene induce Nrf2-mediated expression of phase II detoxifying/antioxidant enzymes in human bronchial epithelial cells. (2008). https://pubmed.ncbi.nlm.nih.gov/18566994/ DOI: 10.1002/ijc.23696
Complete structured claim and evidence
Sulforaphane-affinity beads captured APT2 from Huh-7 or transfected HEK293 lysates; C56S mutation attenuated binding in the reported assays.
Sulforaphane / SFN, stereochemistry specified per study → LYPLA2 source_derived_draftungraded
Experimental context and source evidence
evidence_cache
artifacts/discovery-research/round6-sources/sulforaphane-apt2.pdf; SHA256 31e2993f88fe05eec199b9013173b29379b3346b9696ac766771173ddd0f181a
experimental_model
Human Huh-7 and HEK293 cell lysates; endogenous or FLAG-tagged human APT2
exposure
Bead pulldown; free-sulforaphane competition at 100 micromolar for 30 minutes at 4 C. C56S and C2S constructs compared.
limitations
These are separate experimental observations, not a demonstrated sulforaphane-GPX4-ZDHHC6 pathway. Sulforaphane-driven APT2 relocalization is not equivalent to genetic depletion or general catalytic inhibition. No dietary, clinical or selenium-repletion effect is inferred. Protein stability, palmitoylation and substrate output remain different measurements. Mutagenesis supports C56-dependent engagement; no binding affinity or substrate-specific catalytic inhibition constant was established.
organism
Human experimental cells; construct species unresolved where stated for discussion-only nulls
primary_locator
Figures 1 and 3, Results 3.1 and 3.3
primary_references
https://doi.org/10.1016/j.bbrc.2024.150244
source_access
Full six-page primary PDF, methods and discussion read; Figure 4 visually inspected. No raw-data reanalysis.
APT2: sulforaphane engagement, GPX4 stability and ZDHHC6 turnover · lines 8–16
Targeted primary-literature curation from recursive ZDHHC6 exploration, 2026-09-20. · supports · Human Huh-7 and HEK293 cell lysates; endogenous or FLAG-tagged human APT2 · source_derived_draft · unverified_draft
Sulforaphane-affinity beads captured APT2 from Huh-7 or transfected HEK293 lysates; C56S mutation attenuated binding in the reported assays. primary_references: https://doi.org/10.1016/j.bbrc.2024.150244 primary_locator: Figures 1 and 3, Results 3.1 and 3.3 source_access: Full six-page primary PDF, methods and discussion read; Figure 4 visually inspected. No raw-data reanalysis. evidence_cache: artifacts/discovery-research/round6-sources/sulforaphane-apt2.pdf; SHA256 31e2993f88fe05eec199b9013173b29379b3346b9696ac766771173ddd0f181a experimental_model: Human Huh-7 and HEK293 cell lysates; endogenous or FLAG-tagged human APT2 organism: Human experimental cells; construct species unresolved where stated for discussion-only nulls exposure: Bead pulldown; free-sulforaphane competition at 100 micromolar for 30 minutes at 4 C. C56S and C2S constructs compared. limitations: These are separate experimental observations, not a demonstrated sulforaphane-GPX4-ZDHHC6 pathway. Sulforaphane-driven APT2 relocalization is not equivalent to genetic depletion or general catalytic inhibition. No dietary, clinical or selenium-repletion effect is inferred. Protein stability, palmitoylation and substrate output remain different measurements. Mutagenesis supports C56-dependent engagement; no binding affinity or substrate-specific catalytic inhibition constant was established.
Complete structured claim and evidence
Sulforaphane reduced Alk14 labeling of immunoprecipitated APT2 in transfected HEK293 cells.
Sulforaphane / SFN, stereochemistry specified per study → Human APT2 palmitoylation readout source_derived_draftungraded
Experimental context and source evidence
evidence_cache
artifacts/discovery-research/round6-sources/sulforaphane-apt2.pdf; SHA256 31e2993f88fe05eec199b9013173b29379b3346b9696ac766771173ddd0f181a
experimental_model
Human HEK293 expressing FLAG-tagged human APT2
exposure
100 micromolar sulforaphane for 3 hours followed by 50 micromolar Alk14 for 5 hours; hydroxylamine control; three separate experiments.
limitations
These are separate experimental observations, not a demonstrated sulforaphane-GPX4-ZDHHC6 pathway. Sulforaphane-driven APT2 relocalization is not equivalent to genetic depletion or general catalytic inhibition. No dietary, clinical or selenium-repletion effect is inferred. Protein stability, palmitoylation and substrate output remain different measurements. The authors could not distinguish reduced palmitoylation from enhanced depalmitoylation. This assay does not measure GPX4 or ZDHHC6.
organism
Human experimental cells; construct species unresolved where stated for discussion-only nulls
primary_locator
Figure 4B; Methods 2.8
primary_references
https://doi.org/10.1016/j.bbrc.2024.150244
source_access
Full six-page primary PDF, methods and discussion read; Figure 4 visually inspected. No raw-data reanalysis.
APT2: sulforaphane engagement, GPX4 stability and ZDHHC6 turnover · lines 19–27
Targeted primary-literature curation from recursive ZDHHC6 exploration, 2026-09-20. · supports · Human HEK293 expressing FLAG-tagged human APT2 · source_derived_draft · unverified_draft
Sulforaphane reduced Alk14 labeling of immunoprecipitated APT2 in transfected HEK293 cells. primary_references: https://doi.org/10.1016/j.bbrc.2024.150244 primary_locator: Figure 4B; Methods 2.8 source_access: Full six-page primary PDF, methods and discussion read; Figure 4 visually inspected. No raw-data reanalysis. evidence_cache: artifacts/discovery-research/round6-sources/sulforaphane-apt2.pdf; SHA256 31e2993f88fe05eec199b9013173b29379b3346b9696ac766771173ddd0f181a experimental_model: Human HEK293 expressing FLAG-tagged human APT2 organism: Human experimental cells; construct species unresolved where stated for discussion-only nulls exposure: 100 micromolar sulforaphane for 3 hours followed by 50 micromolar Alk14 for 5 hours; hydroxylamine control; three separate experiments. limitations: These are separate experimental observations, not a demonstrated sulforaphane-GPX4-ZDHHC6 pathway. Sulforaphane-driven APT2 relocalization is not equivalent to genetic depletion or general catalytic inhibition. No dietary, clinical or selenium-repletion effect is inferred. Protein stability, palmitoylation and substrate output remain different measurements. The authors could not distinguish reduced palmitoylation from enhanced depalmitoylation. This assay does not measure GPX4 or ZDHHC6.
Complete structured claim and evidence
Sulforaphane reduced the membrane-to-cytosol ratio of FLAG-tagged APT2 in HEK293 fractionation experiments.
Sulforaphane / SFN, stereochemistry specified per study → Membrane-to-cytosol APT2 ratio in human cells source_derived_draftungraded
Experimental context and source evidence
evidence_cache
artifacts/discovery-research/round6-sources/sulforaphane-apt2.pdf; SHA256 31e2993f88fe05eec199b9013173b29379b3346b9696ac766771173ddd0f181a
experimental_model
Human HEK293 expressing FLAG-tagged human APT2
exposure
100 micromolar sulforaphane for 3 hours; membrane and cytosol fractions with pan-cadherin and alpha-tubulin markers; three separate experiments.
limitations
These are separate experimental observations, not a demonstrated sulforaphane-GPX4-ZDHHC6 pathway. Sulforaphane-driven APT2 relocalization is not equivalent to genetic depletion or general catalytic inhibition. No dietary, clinical or selenium-repletion effect is inferred. Protein stability, palmitoylation and substrate output remain different measurements. The authors describe plasma-membrane localization, but fractionation is not an ER-specific or organelle-resolved measurement.
organism
Human experimental cells; construct species unresolved where stated for discussion-only nulls
primary_locator
Figure 4A; Results 3.4 and Methods 2.9
primary_references
https://doi.org/10.1016/j.bbrc.2024.150244
source_access
Full six-page primary PDF, methods and discussion read; Figure 4 visually inspected. No raw-data reanalysis.
APT2: sulforaphane engagement, GPX4 stability and ZDHHC6 turnover · lines 30–38
Targeted primary-literature curation from recursive ZDHHC6 exploration, 2026-09-20. · supports · Human HEK293 expressing FLAG-tagged human APT2 · source_derived_draft · unverified_draft
Sulforaphane reduced the membrane-to-cytosol ratio of FLAG-tagged APT2 in HEK293 fractionation experiments. primary_references: https://doi.org/10.1016/j.bbrc.2024.150244 primary_locator: Figure 4A; Results 3.4 and Methods 2.9 source_access: Full six-page primary PDF, methods and discussion read; Figure 4 visually inspected. No raw-data reanalysis. evidence_cache: artifacts/discovery-research/round6-sources/sulforaphane-apt2.pdf; SHA256 31e2993f88fe05eec199b9013173b29379b3346b9696ac766771173ddd0f181a experimental_model: Human HEK293 expressing FLAG-tagged human APT2 organism: Human experimental cells; construct species unresolved where stated for discussion-only nulls exposure: 100 micromolar sulforaphane for 3 hours; membrane and cytosol fractions with pan-cadherin and alpha-tubulin markers; three separate experiments. limitations: These are separate experimental observations, not a demonstrated sulforaphane-GPX4-ZDHHC6 pathway. Sulforaphane-driven APT2 relocalization is not equivalent to genetic depletion or general catalytic inhibition. No dietary, clinical or selenium-repletion effect is inferred. Protein stability, palmitoylation and substrate output remain different measurements. The authors describe plasma-membrane localization, but fractionation is not an ER-specific or organelle-resolved measurement.
Complete structured claim and evidence
Sulforaphane did not significantly attenuate Alk14 labeling of APT2-C56S under the conditions that reduced labeling of wild-type APT2.
Human APT2-C56S expressed in HEK293 with sulforaphane exposure → Human APT2 palmitoylation readout source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
evidence_cache
artifacts/discovery-research/round6-sources/sulforaphane-apt2.pdf; SHA256 31e2993f88fe05eec199b9013173b29379b3346b9696ac766771173ddd0f181a
experimental_model
Human HEK293 expressing FLAG-tagged APT2-C56S
exposure
100 micromolar sulforaphane for 3 hours followed by 50 micromolar Alk14 for 5 hours; three separate experiments.
limitations
These are separate experimental observations, not a demonstrated sulforaphane-GPX4-ZDHHC6 pathway. Sulforaphane-driven APT2 relocalization is not equivalent to genetic depletion or general catalytic inhibition. No dietary, clinical or selenium-repletion effect is inferred. Protein stability, palmitoylation and substrate output remain different measurements. C56S is a mutant-plus-exposure actor. Its baseline function must be assessed before using it as a selective pharmacological rescue.
organism
Human experimental cells; construct species unresolved where stated for discussion-only nulls
primary_locator
Figure 4C
primary_references
https://doi.org/10.1016/j.bbrc.2024.150244
source_access
Full six-page primary PDF, methods and discussion read; Figure 4 visually inspected. No raw-data reanalysis.
trigger_kind
machinery_impairment Imported condition classification; unverified.
APT2: sulforaphane engagement, GPX4 stability and ZDHHC6 turnover · lines 41–49
Targeted primary-literature curation from recursive ZDHHC6 exploration, 2026-09-20. · supports · Human HEK293 expressing FLAG-tagged APT2-C56S · source_derived_draft · unverified_draft
Sulforaphane did not significantly attenuate Alk14 labeling of APT2-C56S under the conditions that reduced labeling of wild-type APT2. primary_references: https://doi.org/10.1016/j.bbrc.2024.150244 primary_locator: Figure 4C source_access: Full six-page primary PDF, methods and discussion read; Figure 4 visually inspected. No raw-data reanalysis. evidence_cache: artifacts/discovery-research/round6-sources/sulforaphane-apt2.pdf; SHA256 31e2993f88fe05eec199b9013173b29379b3346b9696ac766771173ddd0f181a experimental_model: Human HEK293 expressing FLAG-tagged APT2-C56S organism: Human experimental cells; construct species unresolved where stated for discussion-only nulls exposure: 100 micromolar sulforaphane for 3 hours followed by 50 micromolar Alk14 for 5 hours; three separate experiments. limitations: These are separate experimental observations, not a demonstrated sulforaphane-GPX4-ZDHHC6 pathway. Sulforaphane-driven APT2 relocalization is not equivalent to genetic depletion or general catalytic inhibition. No dietary, clinical or selenium-repletion effect is inferred. Protein stability, palmitoylation and substrate output remain different measurements. C56S is a mutant-plus-exposure actor. Its baseline function must be assessed before using it as a selective pharmacological rescue.
Complete structured claim and evidence
The sulforaphane study reports no significant change in GAP-43 palmitoylation in the presence of sulforaphane.
Sulforaphane / SFN, stereochemistry specified per study → GAP-43 palmitoylation in the sulforaphane null-result report source_derived_draftungraded
Experimental context and source evidence
evidence_cache
artifacts/discovery-research/round6-sources/sulforaphane-apt2.pdf; SHA256 31e2993f88fe05eec199b9013173b29379b3346b9696ac766771173ddd0f181a
experimental_model
Cell model and construct species not specified for this discussion-only result
exposure
Dose, timing and assay details for this null result are not separately reported.
limitations
These are separate experimental observations, not a demonstrated sulforaphane-GPX4-ZDHHC6 pathway. Sulforaphane-driven APT2 relocalization is not equivalent to genetic depletion or general catalytic inhibition. No dietary, clinical or selenium-repletion effect is inferred. Protein stability, palmitoylation and substrate output remain different measurements. No plotted experiment or effect-size interval is provided. Preserve this author-reported null; it is not proof of equivalence.
organism
Human experimental cells; construct species unresolved where stated for discussion-only nulls
primary_locator
Discussion, page 6
primary_references
https://doi.org/10.1016/j.bbrc.2024.150244
source_access
Full six-page primary PDF, methods and discussion read; Figure 4 visually inspected. No raw-data reanalysis.
APT2: sulforaphane engagement, GPX4 stability and ZDHHC6 turnover · lines 52–60
Targeted primary-literature curation from recursive ZDHHC6 exploration, 2026-09-20. · supports · Cell model and construct species not specified for this discussion-only result · source_derived_draft · unverified_draft
The sulforaphane study reports no significant change in GAP-43 palmitoylation in the presence of sulforaphane. primary_references: https://doi.org/10.1016/j.bbrc.2024.150244 primary_locator: Discussion, page 6 source_access: Full six-page primary PDF, methods and discussion read; Figure 4 visually inspected. No raw-data reanalysis. evidence_cache: artifacts/discovery-research/round6-sources/sulforaphane-apt2.pdf; SHA256 31e2993f88fe05eec199b9013173b29379b3346b9696ac766771173ddd0f181a experimental_model: Cell model and construct species not specified for this discussion-only result organism: Human experimental cells; construct species unresolved where stated for discussion-only nulls exposure: Dose, timing and assay details for this null result are not separately reported. limitations: These are separate experimental observations, not a demonstrated sulforaphane-GPX4-ZDHHC6 pathway. Sulforaphane-driven APT2 relocalization is not equivalent to genetic depletion or general catalytic inhibition. No dietary, clinical or selenium-repletion effect is inferred. Protein stability, palmitoylation and substrate output remain different measurements. No plotted experiment or effect-size interval is provided. Preserve this author-reported null; it is not proof of equivalence.
Complete structured claim and evidence
The sulforaphane study reports no significant change in H-Ras palmitoylation in the presence of sulforaphane.
Sulforaphane / SFN, stereochemistry specified per study → H-Ras palmitoylation in the sulforaphane null-result report source_derived_draftungraded
Experimental context and source evidence
evidence_cache
artifacts/discovery-research/round6-sources/sulforaphane-apt2.pdf; SHA256 31e2993f88fe05eec199b9013173b29379b3346b9696ac766771173ddd0f181a
experimental_model
Cell model and construct species not specified for this discussion-only result
exposure
Dose, timing and assay details for this null result are not separately reported.
limitations
These are separate experimental observations, not a demonstrated sulforaphane-GPX4-ZDHHC6 pathway. Sulforaphane-driven APT2 relocalization is not equivalent to genetic depletion or general catalytic inhibition. No dietary, clinical or selenium-repletion effect is inferred. Protein stability, palmitoylation and substrate output remain different measurements. No plotted experiment or effect-size interval is provided. This limits a universal APT2-substrate prediction.
organism
Human experimental cells; construct species unresolved where stated for discussion-only nulls
primary_locator
Discussion, page 6
primary_references
https://doi.org/10.1016/j.bbrc.2024.150244
source_access
Full six-page primary PDF, methods and discussion read; Figure 4 visually inspected. No raw-data reanalysis.
APT2: sulforaphane engagement, GPX4 stability and ZDHHC6 turnover · lines 63–71
Targeted primary-literature curation from recursive ZDHHC6 exploration, 2026-09-20. · supports · Cell model and construct species not specified for this discussion-only result · source_derived_draft · unverified_draft
The sulforaphane study reports no significant change in H-Ras palmitoylation in the presence of sulforaphane. primary_references: https://doi.org/10.1016/j.bbrc.2024.150244 primary_locator: Discussion, page 6 source_access: Full six-page primary PDF, methods and discussion read; Figure 4 visually inspected. No raw-data reanalysis. evidence_cache: artifacts/discovery-research/round6-sources/sulforaphane-apt2.pdf; SHA256 31e2993f88fe05eec199b9013173b29379b3346b9696ac766771173ddd0f181a experimental_model: Cell model and construct species not specified for this discussion-only result organism: Human experimental cells; construct species unresolved where stated for discussion-only nulls exposure: Dose, timing and assay details for this null result are not separately reported. limitations: These are separate experimental observations, not a demonstrated sulforaphane-GPX4-ZDHHC6 pathway. Sulforaphane-driven APT2 relocalization is not equivalent to genetic depletion or general catalytic inhibition. No dietary, clinical or selenium-repletion effect is inferred. Protein stability, palmitoylation and substrate output remain different measurements. No plotted experiment or effect-size interval is provided. This limits a universal APT2-substrate prediction.
Complete structured claim and evidence
ML349 increased STAT3 palmitoylation in the reported reconstituted HEK293T experiment.
ML349, experimental APT2 inhibitor → STAT3 palmitoylation in human cells source_derived_draftungraded
Experimental context and source evidence
experimental_model
Human HEK293T; DHHC7 knockout reconstituted with HA-DHHC7 and Flag-STAT3; DHHC construct species is not established as human for this figure.
exposure
20 micromolar ML349 for 36 hours before Alk14 labeling; labeling methods specify 50 micromolar Alk14 for 5 hours.
limitations
Reported cellular result, not a GPX4 time-course experiment. Overexpressed DHHC constructs in much of the study are mouse proteins; human constructs are explicitly identified only where confirmed. APT2 depletion, selective inhibitor exposure and sulforaphane are different interventions.
organism
Human
primary_locator
Figure 2f; Extended Data 7d; APT2 depalmitoylates p-STAT3.
primary_references
https://doi.org/10.1038/s41586-020-2799-2
APT2-STAT3 cycling and a competing sulforaphane target route · lines 6–12
Selected primary observations: 10.1038/s41586-020-2799-2 and 10.1038/s41388-020-1335-z. · supports · Human HEK293T; DHHC7 knockout reconstituted with HA-DHHC7 and Flag-STAT3; DHHC construct species is not established as human for this figure. · source_derived_draft · unverified_draft
ML349 increased STAT3 palmitoylation in the reported reconstituted HEK293T experiment. primary_references: https://doi.org/10.1038/s41586-020-2799-2 primary_locator: Figure 2f; Extended Data 7d; APT2 depalmitoylates p-STAT3. organism: Human experimental_model: Human HEK293T; DHHC7 knockout reconstituted with HA-DHHC7 and Flag-STAT3; DHHC construct species is not established as human for this figure. exposure: 20 micromolar ML349 for 36 hours before Alk14 labeling; labeling methods specify 50 micromolar Alk14 for 5 hours. limitations: Reported cellular result, not a GPX4 time-course experiment. Overexpressed DHHC constructs in much of the study are mouse proteins; human constructs are explicitly identified only where confirmed. APT2 depletion, selective inhibitor exposure and sulforaphane are different interventions.
Complete structured claim and evidence
LYPLA2 siRNA increased STAT3 palmitoylation in the reported reconstituted HEK293T experiment.
Human APT2/LYPLA2 knockdown in HEK293T → STAT3 palmitoylation in human cells source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
experimental_model
Human HEK293T; DHHC7 knockout reconstituted with HA-DHHC7 and Flag-STAT3; DHHC construct species is not established as human for this figure.
exposure
LYPLA2 siRNA before Alk14 labeling; Figure 2f states 36 hours before labeling; exact siRNA amount unresolved.
limitations
Reported cellular result, not a GPX4 time-course experiment. Overexpressed DHHC constructs in much of the study are mouse proteins; human constructs are explicitly identified only where confirmed. APT2 depletion, selective inhibitor exposure and sulforaphane are different interventions.
organism
Human
primary_locator
Figure 2f; Extended Data 7d.
primary_references
https://doi.org/10.1038/s41586-020-2799-2
trigger_kind
machinery_impairment Imported condition classification; unverified.
APT2-STAT3 cycling and a competing sulforaphane target route · lines 15–21
Selected primary observations: 10.1038/s41586-020-2799-2 and 10.1038/s41388-020-1335-z. · supports · Human HEK293T; DHHC7 knockout reconstituted with HA-DHHC7 and Flag-STAT3; DHHC construct species is not established as human for this figure. · source_derived_draft · unverified_draft
LYPLA2 siRNA increased STAT3 palmitoylation in the reported reconstituted HEK293T experiment. primary_references: https://doi.org/10.1038/s41586-020-2799-2 primary_locator: Figure 2f; Extended Data 7d. organism: Human experimental_model: Human HEK293T; DHHC7 knockout reconstituted with HA-DHHC7 and Flag-STAT3; DHHC construct species is not established as human for this figure. exposure: LYPLA2 siRNA before Alk14 labeling; Figure 2f states 36 hours before labeling; exact siRNA amount unresolved. limitations: Reported cellular result, not a GPX4 time-course experiment. Overexpressed DHHC constructs in much of the study are mouse proteins; human constructs are explicitly identified only where confirmed. APT2 depletion, selective inhibitor exposure and sulforaphane are different interventions.
Complete structured claim and evidence
APT2 knockdown reduced nuclear p-STAT3 in the HEK293T fractionation experiment.
Human APT2/LYPLA2 knockdown in HEK293T → Nuclear phosphorylated STAT3 abundance in human cells source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
experimental_model
Human HEK293T subcellular fractionation
exposure
LYPLA2 siRNA; exact dose/duration for this panel unresolved.
limitations
Reported cellular result, not a GPX4 time-course experiment. Overexpressed DHHC constructs in much of the study are mouse proteins; human constructs are explicitly identified only where confirmed. APT2 depletion, selective inhibitor exposure and sulforaphane are different interventions.
organism
Human
primary_locator
Figure 2g; APT2 depalmitoylates p-STAT3.
primary_references
https://doi.org/10.1038/s41586-020-2799-2
trigger_kind
machinery_impairment Imported condition classification; unverified.
APT2-STAT3 cycling and a competing sulforaphane target route · lines 24–30
Selected primary observations: 10.1038/s41586-020-2799-2 and 10.1038/s41388-020-1335-z. · supports · Human HEK293T subcellular fractionation · source_derived_draft · unverified_draft
APT2 knockdown reduced nuclear p-STAT3 in the HEK293T fractionation experiment. primary_references: https://doi.org/10.1038/s41586-020-2799-2 primary_locator: Figure 2g; APT2 depalmitoylates p-STAT3. organism: Human experimental_model: Human HEK293T subcellular fractionation exposure: LYPLA2 siRNA; exact dose/duration for this panel unresolved. limitations: Reported cellular result, not a GPX4 time-course experiment. Overexpressed DHHC constructs in much of the study are mouse proteins; human constructs are explicitly identified only where confirmed. APT2 depletion, selective inhibitor exposure and sulforaphane are different interventions.
Complete structured claim and evidence
APT2 knockdown reduced STAT3 transcriptional activity in the reported HEK293T experiments.
Human APT2/LYPLA2 knockdown in HEK293T → STAT3-dependent transcriptional output in human cells source_derived_draftungraded
Experimental context and source evidence
availability_state
machinery_impairment Imported condition classification; unverified.
experimental_model
Human HEK293T
exposure
LYPLA2 siRNA; exact exposure unresolved.
limitations
Reported cellular result, not a GPX4 time-course experiment. Overexpressed DHHC constructs in much of the study are mouse proteins; human constructs are explicitly identified only where confirmed. APT2 depletion, selective inhibitor exposure and sulforaphane are different interventions.
organism
Human
primary_locator
Extended Data 7e-f and Results: APT2 depalmitoylates p-STAT3.
primary_references
https://doi.org/10.1038/s41586-020-2799-2
trigger_kind
machinery_impairment Imported condition classification; unverified.
APT2-STAT3 cycling and a competing sulforaphane target route · lines 33–39
Selected primary observations: 10.1038/s41586-020-2799-2 and 10.1038/s41388-020-1335-z. · supports · Human HEK293T · source_derived_draft · unverified_draft
APT2 knockdown reduced STAT3 transcriptional activity in the reported HEK293T experiments. primary_references: https://doi.org/10.1038/s41586-020-2799-2 primary_locator: Extended Data 7e-f and Results: APT2 depalmitoylates p-STAT3. organism: Human experimental_model: Human HEK293T exposure: LYPLA2 siRNA; exact exposure unresolved. limitations: Reported cellular result, not a GPX4 time-course experiment. Overexpressed DHHC constructs in much of the study are mouse proteins; human constructs are explicitly identified only where confirmed. APT2 depletion, selective inhibitor exposure and sulforaphane are different interventions.
Complete structured claim and evidence
Wild-type APT2 expression reduced STAT3 palmitoylation.
Human APT2 WT expression in HEK293T → STAT3 palmitoylation in human cells source_derived_draftungraded
Experimental context and source evidence
experimental_model
Human HEK293T with expressed APT2 and Flag-STAT3
exposure
Expression constructs; 50 micromolar Alk14 labeling for 5 hours; expression duration unresolved.
limitations
C2S disrupts the APT2 palmitoylation site; S122A alters its catalytic site. They are not interchangeable controls. Null results do not establish equivalence. GPX4 was not an endpoint.
organism
Human
primary_locator
Figure 2d; Extended Data 7b-c.
primary_references
https://doi.org/10.1038/s41586-020-2799-2
APT2-STAT3 cycling and a competing sulforaphane target route · lines 42–48
Selected primary observations: 10.1038/s41586-020-2799-2 and 10.1038/s41388-020-1335-z. · supports · Human HEK293T with expressed APT2 and Flag-STAT3 · source_derived_draft · unverified_draft
Wild-type APT2 expression reduced STAT3 palmitoylation. primary_references: https://doi.org/10.1038/s41586-020-2799-2 primary_locator: Figure 2d; Extended Data 7b-c. organism: Human experimental_model: Human HEK293T with expressed APT2 and Flag-STAT3 exposure: Expression constructs; 50 micromolar Alk14 labeling for 5 hours; expression duration unresolved. limitations: C2S disrupts the APT2 palmitoylation site; S122A alters its catalytic site. They are not interchangeable controls. Null results do not establish equivalence. GPX4 was not an endpoint.
Complete structured claim and evidence
APT2-C2S expression did not reproduce the wild-type reduction in STAT3 palmitoylation.
Human APT2 C2S expression in HEK293T → STAT3 palmitoylation in human cells source_derived_draftungraded
Experimental context and source evidence
experimental_model
Human HEK293T with expressed APT2 and Flag-STAT3
exposure
Expression constructs; 50 micromolar Alk14 labeling for 5 hours; expression duration unresolved.
limitations
C2S disrupts the APT2 palmitoylation site; S122A alters its catalytic site. They are not interchangeable controls. Null results do not establish equivalence. GPX4 was not an endpoint.
organism
Human
primary_locator
Figure 2d; Extended Data 7b-c.
primary_references
https://doi.org/10.1038/s41586-020-2799-2
APT2-STAT3 cycling and a competing sulforaphane target route · lines 51–57
Selected primary observations: 10.1038/s41586-020-2799-2 and 10.1038/s41388-020-1335-z. · supports · Human HEK293T with expressed APT2 and Flag-STAT3 · source_derived_draft · unverified_draft
APT2-C2S expression did not reproduce the wild-type reduction in STAT3 palmitoylation. primary_references: https://doi.org/10.1038/s41586-020-2799-2 primary_locator: Figure 2d; Extended Data 7b-c. organism: Human experimental_model: Human HEK293T with expressed APT2 and Flag-STAT3 exposure: Expression constructs; 50 micromolar Alk14 labeling for 5 hours; expression duration unresolved. limitations: C2S disrupts the APT2 palmitoylation site; S122A alters its catalytic site. They are not interchangeable controls. Null results do not establish equivalence. GPX4 was not an endpoint.
Complete structured claim and evidence
APT2-S122A expression did not reproduce the wild-type reduction in STAT3 palmitoylation.
Human APT2 S122A expression in HEK293T → STAT3 palmitoylation in human cells source_derived_draftungraded
Experimental context and source evidence
experimental_model
Human HEK293T with expressed APT2 and Flag-STAT3
exposure
Expression constructs; 50 micromolar Alk14 labeling for 5 hours; expression duration unresolved.
limitations
C2S disrupts the APT2 palmitoylation site; S122A alters its catalytic site. They are not interchangeable controls. Null results do not establish equivalence. GPX4 was not an endpoint.
organism
Human
primary_locator
Figure 2d; Extended Data 7b-c.
primary_references
https://doi.org/10.1038/s41586-020-2799-2
APT2-STAT3 cycling and a competing sulforaphane target route · lines 60–66
Selected primary observations: 10.1038/s41586-020-2799-2 and 10.1038/s41388-020-1335-z. · supports · Human HEK293T with expressed APT2 and Flag-STAT3 · source_derived_draft · unverified_draft
APT2-S122A expression did not reproduce the wild-type reduction in STAT3 palmitoylation. primary_references: https://doi.org/10.1038/s41586-020-2799-2 primary_locator: Figure 2d; Extended Data 7b-c. organism: Human experimental_model: Human HEK293T with expressed APT2 and Flag-STAT3 exposure: Expression constructs; 50 micromolar Alk14 labeling for 5 hours; expression duration unresolved. limitations: C2S disrupts the APT2 palmitoylation site; S122A alters its catalytic site. They are not interchangeable controls. Null results do not establish equivalence. GPX4 was not an endpoint.
Complete structured claim and evidence
Human ZDHHC7 expression increased STAT3 palmitoylation in the human-construct confirmation experiment.
Human ZDHHC7 expression in HEK293T → STAT3 palmitoylation in human cells source_derived_draftungraded
Experimental context and source evidence
experimental_model
Human HEK293T expressing human DHHC proteins
exposure
Comparison of Flag-tagged human DHHC3, DHHC7 and DHHC19 with HA-STAT3; Alk14 assay.
limitations
Human-construct confirmation is separate from the mouse-DHHC screening experiments. Selected result/legend reviewed; raw gel intensities not reanalyzed.
organism
Human
primary_locator
Extended Data Figure 2f; Results: STAT3 is palmitoylated by DHHC7.
primary_references
https://doi.org/10.1038/s41586-020-2799-2
APT2-STAT3 cycling and a competing sulforaphane target route · lines 69–75
Selected primary observations: 10.1038/s41586-020-2799-2 and 10.1038/s41388-020-1335-z. · supports · Human HEK293T expressing human DHHC proteins · source_derived_draft · unverified_draft
Human ZDHHC7 expression increased STAT3 palmitoylation in the human-construct confirmation experiment. primary_references: https://doi.org/10.1038/s41586-020-2799-2 primary_locator: Extended Data Figure 2f; Results: STAT3 is palmitoylated by DHHC7. organism: Human experimental_model: Human HEK293T expressing human DHHC proteins exposure: Comparison of Flag-tagged human DHHC3, DHHC7 and DHHC19 with HA-STAT3; Alk14 assay. limitations: Human-construct confirmation is separate from the mouse-DHHC screening experiments. Selected result/legend reviewed; raw gel intensities not reanalyzed.
Complete structured claim and evidence
The sulforaphane-derived activity-based probe captured STAT3 from HBCX34 cells.
Sulforaphane-derived activity-based probe → STAT3 source_derived_draftungraded
Experimental context and source evidence
experimental_model
Human HBCx34 breast cancer patient-derived xenograft tumor cells
exposure
5 micromolar SFN-ABP for 30 minutes at 37 C in serum-free DMEM; click chemistry and avidin enrichment followed by anti-STAT3 immunoblot.
limitations
The chemical probe and stabilized formulation are separate experimental actors. Capture supports engagement but does not identify the modified STAT3 cysteine or demonstrate that APT2 mediates the effect. No GPX4 time-course endpoint. Primary cell/PDX studies are not evidence of benefit from dietary broccoli.
organism
Human
primary_locator
Figure 4c; Supplementary Methods: Affinity pull-down assays.
primary_references
https://doi.org/10.1038/s41388-020-1335-z
APT2-STAT3 cycling and a competing sulforaphane target route · lines 78–84
Selected primary observations: 10.1038/s41586-020-2799-2 and 10.1038/s41388-020-1335-z. · supports · Human HBCx34 breast cancer patient-derived xenograft tumor cells · source_derived_draft · unverified_draft
The sulforaphane-derived activity-based probe captured STAT3 from HBCX34 cells. primary_references: https://doi.org/10.1038/s41388-020-1335-z primary_locator: Figure 4c; Supplementary Methods: Affinity pull-down assays. organism: Human experimental_model: Human HBCx34 breast cancer patient-derived xenograft tumor cells exposure: 5 micromolar SFN-ABP for 30 minutes at 37 C in serum-free DMEM; click chemistry and avidin enrichment followed by anti-STAT3 immunoblot. limitations: The chemical probe and stabilized formulation are separate experimental actors. Capture supports engagement but does not identify the modified STAT3 cysteine or demonstrate that APT2 mediates the effect. No GPX4 time-course endpoint. Primary cell/PDX studies are not evidence of benefit from dietary broccoli.
Complete structured claim and evidence
The sulforaphane-derived activity-based probe captured STAT3 from BB3RC61 cells.
Sulforaphane-derived activity-based probe → STAT3 source_derived_draftungraded
Experimental context and source evidence
experimental_model
Human antiestrogen-resistant metastatic breast cancer sample BB3RC61
exposure
5 micromolar SFN-ABP for 30 minutes at 37 C in serum-free DMEM; click chemistry and avidin enrichment followed by anti-STAT3 immunoblot.
limitations
The chemical probe and stabilized formulation are separate experimental actors. Capture supports engagement but does not identify the modified STAT3 cysteine or demonstrate that APT2 mediates the effect. No GPX4 time-course endpoint. Primary cell/PDX studies are not evidence of benefit from dietary broccoli.
organism
Human
primary_locator
Figure 4e; Supplementary Methods: Affinity pull-down assays.
primary_references
https://doi.org/10.1038/s41388-020-1335-z
APT2-STAT3 cycling and a competing sulforaphane target route · lines 87–93
Selected primary observations: 10.1038/s41586-020-2799-2 and 10.1038/s41388-020-1335-z. · supports · Human antiestrogen-resistant metastatic breast cancer sample BB3RC61 · source_derived_draft · unverified_draft
The sulforaphane-derived activity-based probe captured STAT3 from BB3RC61 cells. primary_references: https://doi.org/10.1038/s41388-020-1335-z primary_locator: Figure 4e; Supplementary Methods: Affinity pull-down assays. organism: Human experimental_model: Human antiestrogen-resistant metastatic breast cancer sample BB3RC61 exposure: 5 micromolar SFN-ABP for 30 minutes at 37 C in serum-free DMEM; click chemistry and avidin enrichment followed by anti-STAT3 immunoblot. limitations: The chemical probe and stabilized formulation are separate experimental actors. Capture supports engagement but does not identify the modified STAT3 cysteine or demonstrate that APT2 mediates the effect. No GPX4 time-course endpoint. Primary cell/PDX studies are not evidence of benefit from dietary broccoli.
Complete structured claim and evidence
SFX-01 reduced phosphorylated STAT3 relative to antiestrogen-only treatments in BB3RC61 cells.
SFX-01, sulforaphane stabilized in an alpha-cyclodextrin complex → Whole-cell phosphorylated STAT3 abundance in human cells source_derived_draftungraded
Experimental context and source evidence
experimental_model
Human antiestrogen-resistant metastatic breast cancer sample BB3RC61
exposure
72-hour treatment. Supplementary reagent protocol uses 5 micromolar SFX-01, 1 micromolar 4-OH-tamoxifen or 0.1 micromolar fulvestrant; these concentrations are explicitly stated for cell lines, and patient-specific dosing is not independently confirmed here.
limitations
The chemical probe and stabilized formulation are separate experimental actors. Capture supports engagement but does not identify the modified STAT3 cysteine or demonstrate that APT2 mediates the effect. No GPX4 time-course endpoint. Primary cell/PDX studies are not evidence of benefit from dietary broccoli.
organism
Human
primary_locator
Figure 4d; Results: SFX-01 targets STAT3 signaling.
primary_references
https://doi.org/10.1038/s41388-020-1335-z
APT2-STAT3 cycling and a competing sulforaphane target route · lines 96–102
Selected primary observations: 10.1038/s41586-020-2799-2 and 10.1038/s41388-020-1335-z. · supports · Human antiestrogen-resistant metastatic breast cancer sample BB3RC61 · source_derived_draft · unverified_draft
SFX-01 reduced phosphorylated STAT3 relative to antiestrogen-only treatments in BB3RC61 cells. primary_references: https://doi.org/10.1038/s41388-020-1335-z primary_locator: Figure 4d; Results: SFX-01 targets STAT3 signaling. organism: Human experimental_model: Human antiestrogen-resistant metastatic breast cancer sample BB3RC61 exposure: 72-hour treatment. Supplementary reagent protocol uses 5 micromolar SFX-01, 1 micromolar 4-OH-tamoxifen or 0.1 micromolar fulvestrant; these concentrations are explicitly stated for cell lines, and patient-specific dosing is not independently confirmed here. limitations: The chemical probe and stabilized formulation are separate experimental actors. Capture supports engagement but does not identify the modified STAT3 cysteine or demonstrate that APT2 mediates the effect. No GPX4 time-course endpoint. Primary cell/PDX studies are not evidence of benefit from dietary broccoli.
Complete structured claim and evidence
SFX-01 did not repress STAT3 activity in the reported previously SFX-01-treated, resistant BB7121 sample.
SFX-01, sulforaphane stabilized in an alpha-cyclodextrin complex → Whole-cell phosphorylated STAT3 abundance in human cells source_derived_draftungraded
Experimental context and source evidence
experimental_model
Human metastatic breast cancer patient-derived sample BB7121
exposure
Prior clinical SFX-01 exposure with progression; ex vivo STAT3 assay. Exact panel exposure unresolved.
limitations
The chemical probe and stabilized formulation are separate experimental actors. Capture supports engagement but does not identify the modified STAT3 cysteine or demonstrate that APT2 mediates the effect. No GPX4 time-course endpoint. Primary cell/PDX studies are not evidence of benefit from dietary broccoli. A single resistant sample does not determine the mechanism of resistance. Supplementary legend/main-text result reviewed; raw image not quantitatively reanalyzed.
organism
Human
primary_locator
Results: SFX-01 targets STAT3 signaling; Supplementary Figure S4c.
primary_references
https://doi.org/10.1038/s41388-020-1335-z
APT2-STAT3 cycling and a competing sulforaphane target route · lines 105–111
Selected primary observations: 10.1038/s41586-020-2799-2 and 10.1038/s41388-020-1335-z. · supports · Human metastatic breast cancer patient-derived sample BB7121 · source_derived_draft · unverified_draft
SFX-01 did not repress STAT3 activity in the reported previously SFX-01-treated, resistant BB7121 sample. primary_references: https://doi.org/10.1038/s41388-020-1335-z primary_locator: Results: SFX-01 targets STAT3 signaling; Supplementary Figure S4c. organism: Human experimental_model: Human metastatic breast cancer patient-derived sample BB7121 exposure: Prior clinical SFX-01 exposure with progression; ex vivo STAT3 assay. Exact panel exposure unresolved. limitations: The chemical probe and stabilized formulation are separate experimental actors. Capture supports engagement but does not identify the modified STAT3 cysteine or demonstrate that APT2 mediates the effect. No GPX4 time-course endpoint. Primary cell/PDX studies are not evidence of benefit from dietary broccoli. A single resistant sample does not determine the mechanism of resistance. Supplementary legend/main-text result reviewed; raw image not quantitatively reanalyzed.
Complete structured claim and evidence

Availability and dependencies

Each situation shows the normal role first, then what the sources report under a specific condition. A shortfall in the diet, a fault in the machinery, and a low blood reading are kept separate because they are not the same thing.

When processing reduces formation

Condition: machinery_impairment · The studied florets were heated to at least 70 degrees C.

Normal role: Active plant enzymes convert the precursor after tissue disruption.

Recorded consequence: Both sulforaphane and its nitrile product decreased; sprouts behaved differently.

Scope: Food-processing experiment; low formation is not a human sulforaphane-deficiency syndrome.

Sulforaphane did not significantly attenuate Alk14 labeling of APT2-C56S under the conditions that reduced labeling of wild-type APT2.

Condition: machinery_impairment · 100 micromolar sulforaphane for 3 hours followed by 50 micromolar Alk14 for 5 hours; three separate experiments.

Normal role: APT2 regulates substrate depalmitoylation; relevant selenium-pathway proteins are separate actors. This scenario describes experimental machinery, not nutrient shortage.

Recorded consequence: Sulforaphane did not significantly attenuate Alk14 labeling of APT2-C56S under the conditions that reduced labeling of wild-type APT2.

Scope: Human HEK293 expressing FLAG-tagged APT2-C56S

When microbial conversion machinery is missing

Condition: machinery_impairment · Monoassociation with the experimental BT2157-mutant bacterium.

Normal role: Some gut bacteria activate glucosinolates through a multi-enzyme pathway.

Recorded consequence: Less gastrointestinal isothiocyanate production.

Scope: Gnotobiotic mouse experiment; not a validated human microbiome diagnosis.

When the electrophile sensor cannot respond normally

Condition: machinery_impairment · Experimental KEAP1 C151S substitution.

Normal role: Sulforaphane inhibits KEAP1-dependent Nrf2 ubiquitination.

Recorded consequence: The ligase regulation became resistant to sulforaphane.

Scope: Engineered protein/cell systems; not a demonstrated dietary deficiency or patient screening rule.

When glutathione synthesis is blocked

Condition: machinery_impairment · BSO inhibition of glutathione synthesis.

Normal role: Sulforaphane can induce TXNRD1 mRNA in HepG2 cells.

Recorded consequence: The sulforaphane-induced TXNRD1 mRNA response was reduced.

Scope: Pharmacological cell model; not a universal dietary cysteine or glycine threshold.

When the induced defense machinery is depleted

Condition: machinery_impairment · Nrf2 or TXNRD1 siRNA knockdown.

Normal role: Combined exposure improved peroxide-challenged cell survival.

Recorded consequence: Much of the observed protection was lost.

Scope: Human colonic cell line, not a nutrient-depletion trial.

The sources

Every document behind this chapter is preserved word for word. Open one to read it in full with its recorded conflicts marked in place.

APT2-STAT3 cycling and a competing sulforaphane target routeSelected primary observations: 10.1038/s41586-020-2799-2 and 10.1038/s41388-020-1335-z. · unverified_draftRead preserved source
APT2: sulforaphane engagement, GPX4 stability and ZDHHC6 turnoverTargeted primary-literature curation from recursive ZDHHC6 exploration, 2026-09-20. · unverified_draftRead preserved source
Alpha-lipoic acid: cofactor assembly, redox signaling and nutrient interactions (2026-09-17)AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · unverified_draftRead preserved source
Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (2026-09-17)AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · unverified_draftRead preserved source
Lycopene: absorption, metabolism, nutrient connections and human outcomes (2026-09-17)AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · unverified_draftRead preserved source
Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17)AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · unverified_draftRead preserved source
Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17)AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · unverified_draftRead preserved source
Vitamin B12: mechanisms, deficiency and nutrient interactions (2026-09-17)AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · unverified_draftRead preserved source
Vitamin B6: mechanisms, deficiency and nutrient interactions (2026-09-17)AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · unverified_draftRead preserved source

Recorded disagreements

Where two sources say different things, both are kept and the difference is explained. You can discuss a disagreement or propose a mechanism that might account for it.

Histone acetylation after sulforaphane: increased in one study, decreased in anotherThe 2004 study reported increased histone acetylation in HEK293 and HCT116 cells; the 2014-online/2015-print HCT116/HaCaT comparison reported decreased H3/H4 acetylation despite lower HDAC protein. HCT116 occurs in both studies. Exposure time, serum, metabolite formation, cell state and assay endpoints differ and may help explain the opposing directions, but none is established here as the resolution. The HaCaT HDAC-activity null alone is not the disagreement.Read the recorded disagreement

Open questions in this collection

Questions the curators could not answer from the sources in front of them, kept here with the reason each one is still open. These are gaps in this collection, not findings or proof that no one has studied them.

Which human peptidases and acetyltransferases dominate each sulforaphane-conjugate conversion in each tissue?Metabolite measurements establish the species but do not by themselves prove isoform-specific GGT, dipeptidase or NAT8 flux; those links are not invented.
Can vitamin C status predict an individual response to a glucoraphanin product?Plant myrosinase cofactor chemistry and trials containing ascorbic acid do not isolate the effect of human vitamin C status.
What is the long-term net benefit of a particular sulforaphane formulation for a particular condition?Exposure, age, baseline disease and endpoints differ. Preliminary or biomarker findings do not establish broad preventive or therapeutic efficacy.
Is there a human sulforaphane deficiency syndrome or validated target blood concentration?This nonessential food-derived bioactive has no established dietary-deficiency syndrome in this collection. Low exposure, altered metabolism and failed target engagement are recorded separately.
Which medicines have clinically important interactions with sulforaphane products?One CYP3A phenotyping trial and high-concentration hepatocyte findings cannot establish a universal drug list, direction or dose adjustment.
Which substrate or cofactor limits an individual response to induced antioxidant enzymes?Cysteine, glycine, ATP, NADPH, FAD and selenium have distinct biochemical roles; the selected experiments do not provide universal human deficiency cutoffs or prove benefit from adding all of them.
Does increased use of glutathione for sulforaphane conjugation impair B12 processing or other glutathione-dependent functions in people?A shared substrate is a testable connection, not proof of clinically important competition. No such patient outcome is established here.
When does NRF2 activation protect normal tissue versus support survival or drug export in an established tumor?Cell state and genetic background change the meaning of the same pathway. This collection does not justify using a supplement to treat cancer.

Chapters are assembled from supplied drafts and curated literature summaries. Statements remain unverified against the primary studies, and the ledger is not medical advice.

Evidence, AI assistance and curation standards

Sulforaphane / SFN, stereochemistry specified per study

The mechanisms

Myrosinase hydrolysis of glucoraphanin after broccoli tissue disruption enabled sulforaphane formation.

Ascorbate accelerated hydrolysis of the glycosyl-enzyme intermediate and occupied a position supporting its role as the catalytic base.

Recombinant broccoli ESP redirected myrosinase-dependent glucoraphanin hydrolysis toward sulforaphane nitrile rather than sulforaphane.

Myrosinase increased mean urinary-metabolite-based recovery from 18.6% to 39.8%, and early conversion during the first eight hours from 8.0% to 25.4%.

Revised mass spectrometry detected sulforaphane modification of at least four KEAP1 cysteines, including readily modified C151.

Sulforaphane inhibited KEAP1-dependent ubiquitination of Nrf2.

Sulforaphane increased nuclear localization of stabilized Nrf2 and Nrf2-dependent gene activation.

GSTP1-1 catalyzed sulforaphane conjugation with glutathione in the human enzyme comparison.

Sulforaphane increased TXNRD1 mRNA up to fourfold; TXNRD2 mRNA did not show this induction.

Selenite increased TXNRD1 protein 2.1-fold and activity 4.8-fold without increasing its mRNA.

Combined treatment increased TXNRD1 protein 5.5-fold, activity 13-fold and mRNA 6.5-fold in HepG2 cells.

Neither oral dose consistently induced the measured Nrf2 target genes despite detectable plasma metabolites.

Heating to 60 degrees C before homogenization reduced ESP activity and nitrile formation while increasing sulforaphane yield.

Heating broccoli florets to 70 degrees C or above decreased formation of both measured products; the same reduction did not occur in sprouts.

In vitro isothiocyanate formation required BT2158 together with either BT2156 or BT2157.

BT2156 supported glucosinolate activation when combined with BT2158 in the biochemical reconstitution.

BT2157 supported glucosinolate activation when combined with BT2158 in vitro.

Mice monoassociated with the BT2157-mutant strain had lower gastrointestinal isothiocyanate production.

GSTM1-1 was among the efficient tested human GST catalysts for isothiocyanate conjugation.

Sulforaphane underwent both nonenzymatic and GST-catalyzed conjugation with glutathione.

GSTs also catalyzed reverse cleavage of isothiocyanate-GSH conjugates; those reactions were slow and inhibited by high GSH.

MRP1-overexpressing human cells supported rapid export of accumulated sulforaphane, mainly as its glutathione conjugate.

P-glycoprotein overexpression also implicated ABCB1 in export of intracellular sulforaphane/conjugate pools.

Sulforaphane-glutathione was separately quantified in human urine after broccoli sprout exposure.

Sulforaphane-cysteinylglycine was separately quantified in human urine after broccoli sprout exposure.

Sulforaphane-cysteine was separately quantified in human urine after broccoli sprout exposure.

Sulforaphane-N-acetylcysteine was separately quantified in human urine after broccoli sprout exposure.

Interindividual precursor conversion varied over 100-fold in the studied intervention samples despite equivalent administered preparation.

Human jejunal perfusion detected sulforaphane-GSH returned into the lumen after uptake.

Parallel differentiated Caco-2 experiments assigned GSTA1 induction to sulforaphane; perfusion with mixed extract increased GSTA1 mRNA 2.0-fold.

Iodoacetamide-based sample preparation caused loss of reversible sulforaphane adducts at reactive KEAP1 cysteines including C151.

KEAP1 acted as a substrate adaptor in a functional CUL3-RBX1 ubiquitin-ligase complex.

The KEAP1-CUL3-RBX1 complex targeted multiple lysines in the Nrf2 Neh2 domain for ubiquitination.

Sulforaphane did not disrupt the KEAP1-Nrf2 association in the tested interaction assays.

KEAP1 C151S was markedly resistant to sulforaphane inhibition of its Nrf2-ubiquitination function.

Sulforaphane enabled Nrf2 to escape KEAP1-dependent degradation and increased its stability.

Sulforaphane induced Nrf2-dependent NQO1 expression in untransformed human CRL-1790 colon cells.

Sulforaphane induced Nrf2-dependent MRP1 expression in CRL-1790 cells.

SFN-Cys inhibited HDAC activity in vitro, whereas parent sulforaphane and SFN-GSH had little or no direct effect in the comparison.

SFN-NAC also inhibited HDAC activity in the in vitro comparison.

Sulforaphane exposure increased acetylated histones in HEK293 and HCT116 experiments, including increased acetylated histones at the HCT116 P21 promoter.

Sulforaphane decreased acetylated histone H3, H4 and tubulin markers in the cell comparisons despite reduced HDAC protein levels.

HDAC6 protein decreased early during treatment and HDAC6 transcript was suppressed after 48 hours.

Sulforaphane inhibited mTOR signaling in U2OS cells both with and without NRF2.

Sulforaphane inhibited cytoplasmic HDAC6 activity in the U2OS study.

Reduced phosphorylation of the AKT substrate beta-catenin at S552 indicated lower AKT output despite increased AKT T308/S473 phosphorylation.

Receptor mapping found sulforaphane adducts at TLR4 C246 and C609 under non-reducing conditions.

Sulforaphane suppressed LPS-induced cytokine secretion in THP-1 cells and human PBMC experiments.

Selenite delayed degradation of sulforaphane-induced TXNRD1 mRNA.

Combined sulforaphane and selenite protected HepG2 cells against paraquat-induced death, whereas either alone had little or no protection.

BSO pretreatment significantly reduced sulforaphane-induced TXNRD1 mRNA.

TXNRD1 knockdown lowered survival under combined treatment from 82.4% to 66.5% in the peroxide-challenge assay.

Nrf2 knockdown lowered survival under combined treatment from 82.4% to 51.1%.

The study reported sulforaphane cytotoxicity IC50 values of 25.1 micromolar in hepatocytes and 56.4 micromolar in HepG2 cells alongside lower-exposure protective experiments.

The human GCL holoenzyme was more active and less sensitive to glutathione inhibition than its catalytic subunit alone.

Glutathione inhibited both human GCLC and GCL holoenzyme, with greater sensitivity of GCLC alone.

Glutamate-cysteine ligase joins glutamate and cysteine to form gamma-glutamylcysteine in the first glutathione-synthesis step.

Human GSS joins gamma-glutamylcysteine and glycine in an ATP-dependent reaction to form glutathione.

The human GSS active sites bind ATP and associated magnesium for peptide-bond formation.

Sulforaphane increased G6PD expression in the fibroblast study.

Sulforaphane increased TXNIP expression alongside reduced glucose entry in the studied fibroblasts.

Sulforaphane lowered HK2 expression associated with reduced entry of glucose into glycolysis.

Sulforaphane delayed replicative senescence of cultured MRC-5 and BJ fibroblasts.

Sulforaphane increased GCLM gene expression in early-passage nonsenescent MRC-5 fibroblasts.

Sulforaphane increased GSR gene expression in early-passage nonsenescent MRC-5 fibroblasts.

Sulforaphane increased HMOX1 gene expression in early-passage nonsenescent MRC-5 fibroblasts.

In the broccoli meal study, estimated sulforaphane bioavailability was 37% raw versus 3.4% cooked, with plasma peaks at 1.6 versus 6 hours.

Adding mustard powder increased mean urinary SFN-NAC from 9.8 to 44.7 micromol per gram creatinine after cooked broccoli.

GSTP1-1 expression alone accelerated sulforaphane/conjugate accumulation and increased ARE reporter induction.

MRP1 expression reduced intracellular sulforaphane/conjugate accumulation and attenuated ARE-dependent responses.

The sulforaphane-induced Nrf2 increase was less sustained in MRP1-expressing cells, especially with GSTP1 coexpression.

The intervention increased urinary benzene-derived conjugate excretion by 61% compared with placebo.

Urinary acrolein-derived conjugate excretion increased by 23%.

Crotonaldehyde-derived conjugate excretion did not show the intervention increase observed for benzene and acrolein.

Inflammatory measures and pulmonary function did not differ among trial groups.

In the hepatic-cell experiments, sulforaphane promoted NRF2 nuclear translocation in the mechanism linked to reduced glucose production.

Sulforaphane lowered expression of key gluconeogenic enzymes in the hepatic-cell experiments.

Sulforaphane suppressed glucose production from hepatic cells in the preclinical component of the study.