Component

TXNRD1

Independent protein record for Thioredoxin reductase 1.

20 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

Read recorded mechanisms Open recursive mind map

How nutrients influence it

Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.

How nutrients reach it in more than one step

Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.

Tracing routes…

What it does

Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.

Recorded relationships

What it acts on

  1. Comparison with selenium-deprived and truncated mammalian TrxR forms showed selenium-dependent ubiquinone reduction.

    TXNRD1 → Ubiquinone-10 source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    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
    The chemistry depends on the enzyme being assembled correctly.
    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
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Coenzyme Q10: biosynthesis, electron transfer, antioxidant recycling and nutrient interactions (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 · Enzyme kinetics, mutants and overexpressing-cell homogenates · source_derived_draft · unverified_draft

    ### coq10-txnrd-selenium Comparison with selenium-deprived and truncated mammalian TrxR forms showed selenium-dependent ubiquinone reduction. Condition category: machinery_impairment nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The chemistry depends on the enzyme being assembled correctly. 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

  2. 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

  3. CRISPR–Cas9 silencing of TXNRD1 reduced IL-10-positive B-cell frequencies after CpGC stimulation.

    TXNRD1 → Human IL-10-positive regulatory B-cell differentiation source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary full text
    experimental_model
    Primary human B cells; 72-hour stimulation.
    limitations
    Supports machinery dependence, not selective drug targeting or evidence that a supplement causes autoimmunity.
    nutrient_topic
    Myricetin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Myricetin
    plain_language
    Removing one component weakens the same immune program.
    primary_references
    Thioredoxin is a metabolic rheostat controlling regulatory B cells. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38553615/ · DOI 10.1038/s41590-024-01798-w
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Myricetin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 300–306

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Primary human B cells; 72-hour stimulation. · source_derived_draft · unverified_draft

    ## myricetin-breg-silencing-txnrd1 Removing one component weakens the same immune program. CRISPR–Cas9 silencing of TXNRD1 reduced IL-10-positive B-cell frequencies after CpGC stimulation. Model: Primary human B cells; 72-hour stimulation. Limitations: Supports machinery dependence, not selective drug targeting or evidence that a supplement causes autoimmunity. Evidence access: Primary full text Thioredoxin is a metabolic rheostat controlling regulatory B cells. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38553615/ · DOI 10.1038/s41590-024-01798-w
    Complete structured claim and evidence

  4. The reconstituted TRP14 system used thioredoxin reductase 1 and NADPH to drive disulfide-reduction reactions.

    TXNRD1 → Human thioredoxin-related protein 14 / TXNDC17 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Purified enzyme systems, including human peroxiredoxin-2 decysteinylation.
    limitations
    This establishes a biochemical dependency; selenium or niacin depletion/repletion was not tested in this study.
    nutrient_topic
    L-Cysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Cysteine
    plain_language
    The sulfur-supply step depends on an electron supply and another enzyme.
    primary_references
    TRP14 is the rate-limiting enzyme for intracellular cystine reduction and regulates proteome cysteinylation. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38811853/ · DOI 10.1038/s44318-024-00117-1

    L-Cysteine: sulfur allocation, redox supply and cross-nutrient mechanisms (2026-09-19) · lines 68–74

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified enzyme systems, including human peroxiredoxin-2 decysteinylation. · source_derived_draft · unverified_draft

    ## l-cysteine-trp14-electron-supply The sulfur-supply step depends on an electron supply and another enzyme. The reconstituted TRP14 system used thioredoxin reductase 1 and NADPH to drive disulfide-reduction reactions. Model: Purified enzyme systems, including human peroxiredoxin-2 decysteinylation. Limitations: This establishes a biochemical dependency; selenium or niacin depletion/repletion was not tested in this study. Evidence access: Primary full text TRP14 is the rate-limiting enzyme for intracellular cystine reduction and regulates proteome cysteinylation. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38811853/ · DOI 10.1038/s44318-024-00117-1
    Complete structured claim and evidence

  5. Cytosolic TXNRD1 uses NADPH-derived reducing equivalents to reduce oxidized thioredoxin through its flavin and C-terminal redox centers.

    TXNRD1 → TXN1 source_derived_draftliterature_reviewed:direct_experimental
    Experimental context and source evidence
    experimental_model
    Purified rat liver cytosolic thioredoxin reductase and recombinant active-site variants.
    limitations
    This experiment-specific relationship does not establish a human dietary-deficiency threshold or supplementation benefit.
    organism
    Rat protein and recombinant enzyme assays

    Selenium: literature corrections and mechanism additions · lines 965–974

    Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually · supports · Purified rat liver cytosolic thioredoxin reductase and recombinant active-site variants. · secondary_verified · secondary_verified

    ## txnrd1-reduces-txn1 TXNRD1 recharges thioredoxin so it can reduce other proteins. Cytosolic TXNRD1 uses NADPH-derived reducing equivalents to reduce oxidized thioredoxin through its flavin and C-terminal redox centers. Experimental model: Purified rat liver cytosolic thioredoxin reductase and recombinant active-site variants. Organism: Rat protein and recombinant enzyme assays Limitations: This experiment-specific relationship does not establish a human dietary-deficiency threshold or supplementation benefit. Primary reference: [Mammalian thioredoxin reductase: C-terminal redox center and selenium-to-sulfur substitution](https://pmc.ncbi.nlm.nih.gov/articles/PMC15961/)
    Complete structured claim and evidence

What acts on it

  1. Messenger RNA for heme oxygenase-1, manganese superoxide dismutase and cytoplasmic thioredoxin reductase 1 rose three- to six-fold nine hours after exposure, with heme oxygenase-1 rising a few hours before manganese superoxide dismutase, while catalase, copper-zinc superoxide dismutase, glutathione reductase, glutathione peroxidase and thioredoxin did not change.

    Hyperbaric oxygen therapy → TXNRD1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/hbot-research/15642322.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e3bc035a17e4e19dd92d4fadb1a79f8e3801619dac24fb91dcf985728afaf995", "start_char": 0, "end_char": 2646, "text_sha256": "e3bc035a17e4e19dd92d4fadb1a79f8e3801619dac24fb91dcf985728afaf995"}
    experimental_model
    Cultured human lens epithelial cells exposed to extreme hyperbaric oxygen with enzyme assays and real-time PCR
    exposure
    99% oxygen at 50 atmospheres for 3 hours, then normal culture for up to 11 days
    limitations
    Fifty atmospheres is an extreme experimental exposure far above therapy, chosen to probe which defences matter. The selenoenzyme result is the informative part; the pressure is not clinically relevant.
    nutrient_topic
    Hyperbaric oxygen research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. · Hyperbaric oxygen therapy
    organism
    Human cells
    plain_language
    The cell rebuilt exactly three proteins: the heme enzyme, the manganese enzyme and the selenium enzyme.
    primary_references
    [hbot-p15642322] Thioredoxin reductase may be essential for the normal growth of hyperbaric oxygen-treated human lens epithelial cells. (2004). https://pubmed.ncbi.nlm.nih.gov/15642322/ DOI: 10.1016/j.exer.2004.07.001
    tissue_or_cell_type
    Lens epithelium

    Hyperbaric oxygen: the exposure, its reactive species, the signals they carry, and the nutrient-dependent enzymes that handle them (2026-09-19) · lines 426–437

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cultured human lens epithelial cells exposed to extreme hyperbaric oxygen with enzyme assays and real-time PCR · source_derived_draft · unverified_draft

    ### hbot-trxr-mrna-response Messenger RNA for heme oxygenase-1, manganese superoxide dismutase and cytoplasmic thioredoxin reductase 1 rose three- to six-fold nine hours after exposure, with heme oxygenase-1 rising a few hours before manganese superoxide dismutase, while catalase, copper-zinc superoxide dismutase, glutathione reductase, glutathione peroxidase and thioredoxin did not change. Condition category: normal nutrient_topic: Hyperbaric oxygen research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. plain_language: The cell rebuilt exactly three proteins: the heme enzyme, the manganese enzyme and the selenium enzyme. organism: Human cells tissue_or_cell_type: Lens epithelium experimental_model: Cultured human lens epithelial cells exposed to extreme hyperbaric oxygen with enzyme assays and real-time PCR limitations: Fifty atmospheres is an extreme experimental exposure far above therapy, chosen to probe which defences matter. The selenoenzyme result is the informative part; the pressure is not clinically relevant. exposure: 99% oxygen at 50 atmospheres for 3 hours, then normal culture for up to 11 days evidence_span: {"source_cache": "artifacts/hbot-research/15642322.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e3bc035a17e4e19dd92d4fadb1a79f8e3801619dac24fb91dcf985728afaf995", "start_char": 0, "end_char": 2646, "text_sha256": "e3bc035a17e4e19dd92d4fadb1a79f8e3801619dac24fb91dcf985728afaf995"} [hbot-p15642322] Thioredoxin reductase may be essential for the normal growth of hyperbaric oxygen-treated human lens epithelial cells. (2004). https://pubmed.ncbi.nlm.nih.gov/15642322/ DOI: 10.1016/j.exer.2004.07.001
    Complete structured claim and evidence

  2. Mammalian thioredoxin reductase carries an essential selenocysteine in the conserved C-terminal sequence Gly-Cys-SeCys-Gly, forming a selenenylsulfide between Cys497 and SeCys498 that becomes a selenolthiol on reduction, alongside a separate Cys59-Cys64 disulfide identical to the glutathione reductase active site.

    Sec → TXNRD1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/hbot-research/10801974.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1627b8b48962b6d2b9bead351b64b71fb60b9681378b44f77a3fc288d35119e3", "start_char": 0, "end_char": 1719, "text_sha256": "1627b8b48962b6d2b9bead351b64b71fb60b9681378b44f77a3fc288d35119e3"}
    experimental_model
    Chemical modification, peptide sequencing, mass spectrometry and redox titration of mammalian thioredoxin reductase
    exposure
    Oxidised and NADPH-reduced enzyme states
    limitations
    Enzyme chemistry on purified protein. It establishes the selenium-containing active site; it is not a statement about selenium intake.
    nutrient_topic
    Hyperbaric oxygen research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. · Hyperbaric oxygen therapy
    organism
    Rat and human enzyme
    plain_language
    The enzyme’s working end is built from a selenium amino acid paired with a cysteine.
    primary_references
    [hbot-p10801974] Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence. (2000). https://pubmed.ncbi.nlm.nih.gov/10801974/ DOI: 10.1073/pnas.100114897
    tissue_or_cell_type
    Purified enzyme

    Hyperbaric oxygen: the exposure, its reactive species, the signals they carry, and the nutrient-dependent enzymes that handle them (2026-09-19) · lines 452–463

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Chemical modification, peptide sequencing, mass spectrometry and redox titration of mammalian thioredoxin reductase · source_derived_draft · unverified_draft

    ### hbot-trxr-selenocysteine-site Mammalian thioredoxin reductase carries an essential selenocysteine in the conserved C-terminal sequence Gly-Cys-SeCys-Gly, forming a selenenylsulfide between Cys497 and SeCys498 that becomes a selenolthiol on reduction, alongside a separate Cys59-Cys64 disulfide identical to the glutathione reductase active site. Condition category: normal nutrient_topic: Hyperbaric oxygen research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. plain_language: The enzyme’s working end is built from a selenium amino acid paired with a cysteine. organism: Rat and human enzyme tissue_or_cell_type: Purified enzyme experimental_model: Chemical modification, peptide sequencing, mass spectrometry and redox titration of mammalian thioredoxin reductase limitations: Enzyme chemistry on purified protein. It establishes the selenium-containing active site; it is not a statement about selenium intake. exposure: Oxidised and NADPH-reduced enzyme states evidence_span: {"source_cache": "artifacts/hbot-research/10801974.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1627b8b48962b6d2b9bead351b64b71fb60b9681378b44f77a3fc288d35119e3", "start_char": 0, "end_char": 1719, "text_sha256": "1627b8b48962b6d2b9bead351b64b71fb60b9681378b44f77a3fc288d35119e3"} [hbot-p10801974] Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence. (2000). https://pubmed.ncbi.nlm.nih.gov/10801974/ DOI: 10.1073/pnas.100114897
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Selenite treatment increased cytosolic TrxR activity together with ubiquinone reduction in the tested cell homogenates.

    Selenite ion → TrxR1-associated ubiquinone reductase activity 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
    Cell-culture exposure; no clinical supplement ratio or systemic outcome was tested.
    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 cell experiment connected selenium supply with CoQ recycling capacity.
    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 788–799

    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-selenite-cell-recycling Selenite treatment increased cytosolic TrxR activity together with ubiquinone reduction in the tested cell homogenates. Condition category: normal nutrient_topic: Coenzyme Q10 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A cell experiment connected selenium supply with CoQ recycling capacity. organism: Mammalian TrxR1 and human HEK293 cells tissue_or_cell_type: Ubiquinone reduction experimental_model: Enzyme kinetics, mutants and overexpressing-cell homogenates limitations: Cell-culture exposure; no clinical supplement ratio or systemic outcome was tested. 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

  2. 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

  3. 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

  4. 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

  5. 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

  6. 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

  7. 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

  8. 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

  9. 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

  10. Thioredoxin reductase activity fell by 51% after the 3-hour oxygen exposure, while cellular glutathione and the activities of several other antioxidant enzymes, including glyceraldehyde-3-phosphate dehydrogenase, showed no immediate effect.

    Hyperbaric oxygen therapy → Thioredoxin reductase catalytic activity source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/hbot-research/15642322.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e3bc035a17e4e19dd92d4fadb1a79f8e3801619dac24fb91dcf985728afaf995", "start_char": 0, "end_char": 2646, "text_sha256": "e3bc035a17e4e19dd92d4fadb1a79f8e3801619dac24fb91dcf985728afaf995"}
    experimental_model
    Cultured human lens epithelial cells exposed to extreme hyperbaric oxygen with enzyme assays and real-time PCR
    exposure
    99% oxygen at 50 atmospheres for 3 hours, then normal culture for up to 11 days
    limitations
    Fifty atmospheres is an extreme experimental exposure far above therapy, chosen to probe which defences matter. The selenoenzyme result is the informative part; the pressure is not clinically relevant.
    nutrient_topic
    Hyperbaric oxygen research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. · Hyperbaric oxygen therapy
    organism
    Human cells
    plain_language
    Of all the defences measured, the selenium enzyme was the one that was knocked down.
    primary_references
    [hbot-p15642322] Thioredoxin reductase may be essential for the normal growth of hyperbaric oxygen-treated human lens epithelial cells. (2004). https://pubmed.ncbi.nlm.nih.gov/15642322/ DOI: 10.1016/j.exer.2004.07.001
    tissue_or_cell_type
    Lens epithelium

    Hyperbaric oxygen: the exposure, its reactive species, the signals they carry, and the nutrient-dependent enzymes that handle them (2026-09-19) · lines 387–398

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cultured human lens epithelial cells exposed to extreme hyperbaric oxygen with enzyme assays and real-time PCR · source_derived_draft · unverified_draft

    ### hbot-trxr-activity-loss Thioredoxin reductase activity fell by 51% after the 3-hour oxygen exposure, while cellular glutathione and the activities of several other antioxidant enzymes, including glyceraldehyde-3-phosphate dehydrogenase, showed no immediate effect. Condition category: normal nutrient_topic: Hyperbaric oxygen research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. plain_language: Of all the defences measured, the selenium enzyme was the one that was knocked down. organism: Human cells tissue_or_cell_type: Lens epithelium experimental_model: Cultured human lens epithelial cells exposed to extreme hyperbaric oxygen with enzyme assays and real-time PCR limitations: Fifty atmospheres is an extreme experimental exposure far above therapy, chosen to probe which defences matter. The selenoenzyme result is the informative part; the pressure is not clinically relevant. exposure: 99% oxygen at 50 atmospheres for 3 hours, then normal culture for up to 11 days evidence_span: {"source_cache": "artifacts/hbot-research/15642322.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e3bc035a17e4e19dd92d4fadb1a79f8e3801619dac24fb91dcf985728afaf995", "start_char": 0, "end_char": 2646, "text_sha256": "e3bc035a17e4e19dd92d4fadb1a79f8e3801619dac24fb91dcf985728afaf995"} [hbot-p15642322] Thioredoxin reductase may be essential for the normal growth of hyperbaric oxygen-treated human lens epithelial cells. (2004). https://pubmed.ncbi.nlm.nih.gov/15642322/ DOI: 10.1016/j.exer.2004.07.001
    Complete structured claim and evidence

  11. Recovery of thioredoxin reductase activity over four days paralleled the return of the cells to a normal rate of growth, and the authors conclude that full activity of TrxR1, required for production of deoxyribonucleotides for DNA synthesis, is essential for normal growth of oxygen-challenged cells.

    Thioredoxin reductase catalytic activity → Human lens epithelial cell growth source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/hbot-research/15642322.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e3bc035a17e4e19dd92d4fadb1a79f8e3801619dac24fb91dcf985728afaf995", "start_char": 0, "end_char": 2646, "text_sha256": "e3bc035a17e4e19dd92d4fadb1a79f8e3801619dac24fb91dcf985728afaf995"}
    experimental_model
    Cultured human lens epithelial cells exposed to extreme hyperbaric oxygen with enzyme assays and real-time PCR
    exposure
    99% oxygen at 50 atmospheres for 3 hours, then normal culture for up to 11 days
    limitations
    Fifty atmospheres is an extreme experimental exposure far above therapy, chosen to probe which defences matter. The selenoenzyme result is the informative part; the pressure is not clinically relevant.
    nutrient_topic
    Hyperbaric oxygen research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. · Hyperbaric oxygen therapy
    organism
    Human cells
    plain_language
    The cells could not start dividing again until that enzyme came back.
    primary_references
    [hbot-p15642322] Thioredoxin reductase may be essential for the normal growth of hyperbaric oxygen-treated human lens epithelial cells. (2004). https://pubmed.ncbi.nlm.nih.gov/15642322/ DOI: 10.1016/j.exer.2004.07.001
    tissue_or_cell_type
    Lens epithelium
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Hyperbaric oxygen: the exposure, its reactive species, the signals they carry, and the nutrient-dependent enzymes that handle them (2026-09-19) · lines 400–411

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cultured human lens epithelial cells exposed to extreme hyperbaric oxygen with enzyme assays and real-time PCR · source_derived_draft · unverified_draft

    ### hbot-trxr-growth-requirement Recovery of thioredoxin reductase activity over four days paralleled the return of the cells to a normal rate of growth, and the authors conclude that full activity of TrxR1, required for production of deoxyribonucleotides for DNA synthesis, is essential for normal growth of oxygen-challenged cells. Condition category: machinery_impairment nutrient_topic: Hyperbaric oxygen research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. plain_language: The cells could not start dividing again until that enzyme came back. organism: Human cells tissue_or_cell_type: Lens epithelium experimental_model: Cultured human lens epithelial cells exposed to extreme hyperbaric oxygen with enzyme assays and real-time PCR limitations: Fifty atmospheres is an extreme experimental exposure far above therapy, chosen to probe which defences matter. The selenoenzyme result is the informative part; the pressure is not clinically relevant. exposure: 99% oxygen at 50 atmospheres for 3 hours, then normal culture for up to 11 days evidence_span: {"source_cache": "artifacts/hbot-research/15642322.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e3bc035a17e4e19dd92d4fadb1a79f8e3801619dac24fb91dcf985728afaf995", "start_char": 0, "end_char": 2646, "text_sha256": "e3bc035a17e4e19dd92d4fadb1a79f8e3801619dac24fb91dcf985728afaf995"} [hbot-p15642322] Thioredoxin reductase may be essential for the normal growth of hyperbaric oxygen-treated human lens epithelial cells. (2004). https://pubmed.ncbi.nlm.nih.gov/15642322/ DOI: 10.1016/j.exer.2004.07.001
    Complete structured claim and evidence

  12. TRP14 removed cysteinyl mixed-disulfide modifications from human peroxiredoxin 2 and restored its peroxide-reducing activity in vitro.

    Human thioredoxin-related protein 14 / TXNDC17 → Human peroxiredoxin 2 / PRDX2 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Recombinant human Prx2; cysteinylation and hydrogen-peroxide reduction assays.
    limitations
    TRP14 repairs this modification; it is not being assigned the ordinary catalytic peroxide-reduction cycle of thioredoxin.
    nutrient_topic
    L-Cysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Cysteine
    plain_language
    A cysteine modification can temporarily obstruct another antioxidant enzyme.
    primary_references
    TRP14 is the rate-limiting enzyme for intracellular cystine reduction and regulates proteome cysteinylation. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38811853/ · DOI 10.1038/s44318-024-00117-1

    L-Cysteine: sulfur allocation, redox supply and cross-nutrient mechanisms (2026-09-19) · lines 84–90

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant human Prx2; cysteinylation and hydrogen-peroxide reduction assays. · source_derived_draft · unverified_draft

    ## l-cysteine-protein-decysteinylation A cysteine modification can temporarily obstruct another antioxidant enzyme. TRP14 removed cysteinyl mixed-disulfide modifications from human peroxiredoxin 2 and restored its peroxide-reducing activity in vitro. Model: Recombinant human Prx2; cysteinylation and hydrogen-peroxide reduction assays. Limitations: TRP14 repairs this modification; it is not being assigned the ordinary catalytic peroxide-reduction cycle of thioredoxin. Evidence access: Primary full text TRP14 is the rate-limiting enzyme for intracellular cystine reduction and regulates proteome cysteinylation. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38811853/ · DOI 10.1038/s44318-024-00117-1
    Complete structured claim and evidence

  13. TXNDC17 knockout in human HEK293 cells markedly reduced intracellular cystine reduction; wild-type TRP14 re-expression restored activity whereas its active-site mutant did not.

    Human thioredoxin-related protein 14 / TXNDC17 → L-Cysteine source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary full text
    experimental_model
    Human HEK293 knockout/rescue; fluorescent cystine-reduction assays.
    limitations
    The paper identifies a major rate-limiting route in tested systems, not the only possible reductase in every tissue.
    nutrient_topic
    L-Cysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Cysteine
    plain_language
    Importing oxidized cysteine is not enough: the cell must reduce it to use it.
    primary_references
    TRP14 is the rate-limiting enzyme for intracellular cystine reduction and regulates proteome cysteinylation. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38811853/ · DOI 10.1038/s44318-024-00117-1
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Cysteine: sulfur allocation, redox supply and cross-nutrient mechanisms (2026-09-19) · lines 60–66

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human HEK293 knockout/rescue; fluorescent cystine-reduction assays. · source_derived_draft · unverified_draft

    ## l-cysteine-trp14-cystine-reduction Importing oxidized cysteine is not enough: the cell must reduce it to use it. TXNDC17 knockout in human HEK293 cells markedly reduced intracellular cystine reduction; wild-type TRP14 re-expression restored activity whereas its active-site mutant did not. Model: Human HEK293 knockout/rescue; fluorescent cystine-reduction assays. Limitations: The paper identifies a major rate-limiting route in tested systems, not the only possible reductase in every tissue. Evidence access: Primary full text TRP14 is the rate-limiting enzyme for intracellular cystine reduction and regulates proteome cysteinylation. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38811853/ · DOI 10.1038/s44318-024-00117-1
    Complete structured claim and evidence

In the sources

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    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards