Component

Human KEAP1

Human KEAP1. Species, exposure and limitations are retained in each linked claim.

10 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. 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

What acts on it

  1. 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

  2. A cellular thermal-shift assay supported engagement of KEAP1 by SAC in human colonic epithelial cells.

    S-allyl-L-cysteine / SAC → Human KEAP1 source_derived_draftungraded
    Experimental context and source evidence
    acting_entity
    s-allylcysteine
    dose
    Not specified in accessed abstract
    duration
    Not specified in accessed abstract
    evidence_access
    Primary abstract
    experimental_comparison
    SAC with PhIP challenge and corresponding cell controls
    experimental_model
    Normal human colonic mucosal epithelial cells exposed to PhIP
    interpretation_status
    Source-derived research curation; not independent primary verification
    limitations
    Thermal stabilization does not alone identify a binding site, affinity, covalent adduct or purified-protein mechanism.
    nutrient_topic
    S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC
    organism
    Homo sapiens
    plain_language
    A target-engagement assay gives a more direct molecular lead.
    primary_references
    [35753083] S-Allylcysteine Potently Protects against PhIP-Induced DNA Damage via Nrf2/AhR Signaling Pathway Modulation in Normal Human Colonic Mucosal Epithelial Cells. · 2022 · https://pubmed.ncbi.nlm.nih.gov/35753083/ · DOI 10.1002/mnfr.202101141
    route
    Cell culture
    tissue_or_cell_type
    Normal human colonic mucosal epithelial cells exposed to PhIP

    S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 149–156

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Normal human colonic mucosal epithelial cells exposed to PhIP · source_derived_draft · unverified_draft

    ## s-allylcysteine-keap1-cetsa A target-engagement assay gives a more direct molecular lead. A cellular thermal-shift assay supported engagement of KEAP1 by SAC in human colonic epithelial cells. Model: Normal human colonic mucosal epithelial cells exposed to PhIP Limitations: Thermal stabilization does not alone identify a binding site, affinity, covalent adduct or purified-protein mechanism. Evidence access: Primary abstract [35753083] S-Allylcysteine Potently Protects against PhIP-Induced DNA Damage via Nrf2/AhR Signaling Pathway Modulation in Normal Human Colonic Mucosal Epithelial Cells. · 2022 · https://pubmed.ncbi.nlm.nih.gov/35753083/ · DOI 10.1002/mnfr.202101141 Structured context: {"organism": "Homo sapiens", "tissue_or_cell_type": "Normal human colonic mucosal epithelial cells exposed to PhIP", "dose": "Not specified in accessed abstract", "duration": "Not specified in accessed abstract", "route": "Cell culture", "experimental_comparison": "SAC with PhIP challenge and corresponding cell controls", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. 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

  2. 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

  3. 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

  4. 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

  5. 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

  6. 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

  7. Lipoic-acid exposure increased nuclear Nrf2 and reduced KEAP1 protein in HL-60 cells.

    Lipoic acid → Human HL-60 Nrf2 nuclear accumulation source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/ala-research/18813798.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bcc2d2fa7c8f550c53af52dfcd88a1e84bee38f98b85cb72e723eba495b01814", "start_char": 0, "end_char": 1245, "text_sha256": "bcc2d2fa7c8f550c53af52dfcd88a1e84bee38f98b85cb72e723eba495b01814"}
    experimental_model
    Human HL-60 leukemia cell biochemical study
    exposure
    Alpha-lipoic-acid exposure
    limitations
    Association of Nrf2/KEAP1 changes with NQO1 induction does not by itself establish genetic dependency or clinical cancer benefit.
    nutrient_topic
    Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. · Lipoic acid
    organism
    Human cell line
    plain_language
    A cellular stress-response regulator changed location while its inhibitor decreased.
    primary_references
    [ala-p18813798] Control of cellular redox status and upregulation of quinone reductase NQO1 via Nrf2 activation by alpha-lipoic acid in human leukemia HL-60 cells. (2008). https://pubmed.ncbi.nlm.nih.gov/18813798/ DOI: 10.3892/ijo_00000071
    tissue_or_cell_type
    HL-60 cells

    Alpha-lipoic acid: cofactor assembly, redox signaling and nutrient interactions (2026-09-17) · lines 871–882

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human HL-60 leukemia cell biochemical study · source_derived_draft · unverified_draft

    ### ala-hl60-nrf2-keap1 Lipoic-acid exposure increased nuclear Nrf2 and reduced KEAP1 protein in HL-60 cells. Condition category: normal nutrient_topic: Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: A cellular stress-response regulator changed location while its inhibitor decreased. organism: Human cell line tissue_or_cell_type: HL-60 cells experimental_model: Human HL-60 leukemia cell biochemical study limitations: Association of Nrf2/KEAP1 changes with NQO1 induction does not by itself establish genetic dependency or clinical cancer benefit. exposure: Alpha-lipoic-acid exposure evidence_span: {"source_cache": "artifacts/ala-research/18813798.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bcc2d2fa7c8f550c53af52dfcd88a1e84bee38f98b85cb72e723eba495b01814", "start_char": 0, "end_char": 1245, "text_sha256": "bcc2d2fa7c8f550c53af52dfcd88a1e84bee38f98b85cb72e723eba495b01814"} [ala-p18813798] Control of cellular redox status and upregulation of quinone reductase NQO1 via Nrf2 activation by alpha-lipoic acid in human leukemia HL-60 cells. (2008). https://pubmed.ncbi.nlm.nih.gov/18813798/ DOI: 10.3892/ijo_00000071
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    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