Component

SIRT1

Independent protein record; interpretation is limited by each linked claim and its study context.

11 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. Human SIRT1 removes acetylation from histone H4 Lys16 in an NAD+-dependent reaction.

    SIRT1 → Histone H4 acetylated at K16 source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Human enzyme assays and cultured-cell SIRT1 perturbation.
    limitations
    This reaction modifies lysine already in a protein. It does not show that extra oral lysine increases the reaction or improves a clinical outcome.
    organism
    Human
    plain_language
    A different enzyme removes a lysine modification using NAD+.
    primary_references
    [sirt1-2004] Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin (2004). https://pubmed.ncbi.nlm.nih.gov/15469825/ DOI: 10.1016/j.molcel.2004.08.031
    tissue_or_cell_type
    Not specified as a whole tissue; see experimental model.

    L-Lysine: mechanism-first literature curation (2026-09-17) · lines 537–545

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human enzyme assays and cultured-cell SIRT1 perturbation. · source_derived_draft · unverified_draft

    ### sirt1-h4k16-deacetylation Human SIRT1 removes acetylation from histone H4 Lys16 in an NAD+-dependent reaction. Plain language: A different enzyme removes a lysine modification using NAD+. Condition category: normal organism: Human tissue_or_cell_type: Not specified as a whole tissue; see experimental model. experimental_model: Human enzyme assays and cultured-cell SIRT1 perturbation. limitations: This reaction modifies lysine already in a protein. It does not show that extra oral lysine increases the reaction or improves a clinical outcome. [sirt1-2004] Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin (2004). https://pubmed.ncbi.nlm.nih.gov/15469825/ DOI: 10.1016/j.molcel.2004.08.031
    Complete structured claim and evidence

What acts on it

  1. Norathyriol increased SIRT1 protein expression in HepG2 cells.

    Norathyriol → SIRT1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/mangiferin-research/29563875.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1a48a1f92d67cd91638969bb1ec3cb9f18cb3cb4e29c7e5f2bacf627dda76415", "start_char": 35295, "end_char": 36269, "text_sha256": "4b69cb6e7f09043eda3312b226bc03bbf8e0cbf25a4f6b51505c0aebed3b7d04"}
    experimental_model
    KK-Ay mouse liver experiments and mechanistic HepG2 studies
    exposure
    Norathyriol in sodium-oleate lipid-loading model; micromolar range
    limitations
    Phosphorylation and expression are scoped to experiments; no established human fatty-liver therapy or direct SIRT1 ligand claim.
    nutrient_topic
    Mangiferin research collection; topical membership is not evidence of a direct dietary effect. · Mangiferin
    organism
    Homo sapiens for HepG2 experiments; mouse findings separately scoped
    plain_language
    The metabolite altered an NAD-dependent regulatory pathway.
    primary_references
    [mangiferin-p29563875] Mangiferin Improves Hepatic Lipid Metabolism Mainly Through Its Metabolite-Norathyriol by Modulating SIRT-1/AMPK/SREBP-1c Signaling. (2018). https://pubmed.ncbi.nlm.nih.gov/29563875/ DOI: 10.3389/fphar.2018.00201
    tissue_or_cell_type
    HepG2 cells

    Mangiferin: metabolism, signaling and nutrient connections (2026-09-17) · lines 445–456

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · KK-Ay mouse liver experiments and mechanistic HepG2 studies · source_derived_draft · unverified_draft

    ### mangiferin-sirt1-expression Norathyriol increased SIRT1 protein expression in HepG2 cells. Condition category: normal nutrient_topic: Mangiferin research collection; topical membership is not evidence of a direct dietary effect. plain_language: The metabolite altered an NAD-dependent regulatory pathway. organism: Homo sapiens for HepG2 experiments; mouse findings separately scoped tissue_or_cell_type: HepG2 cells experimental_model: KK-Ay mouse liver experiments and mechanistic HepG2 studies limitations: Phosphorylation and expression are scoped to experiments; no established human fatty-liver therapy or direct SIRT1 ligand claim. exposure: Norathyriol in sodium-oleate lipid-loading model; micromolar range evidence_span: {"source_cache": "artifacts/mangiferin-research/29563875.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1a48a1f92d67cd91638969bb1ec3cb9f18cb3cb4e29c7e5f2bacf627dda76415", "start_char": 35295, "end_char": 36269, "text_sha256": "4b69cb6e7f09043eda3312b226bc03bbf8e0cbf25a4f6b51505c0aebed3b7d04"} [mangiferin-p29563875] Mangiferin Improves Hepatic Lipid Metabolism Mainly Through Its Metabolite-Norathyriol by Modulating SIRT-1/AMPK/SREBP-1c Signaling. (2018). https://pubmed.ncbi.nlm.nih.gov/29563875/ DOI: 10.3389/fphar.2018.00201
    Complete structured claim and evidence

  2. The E230K substitution attenuated resveratrol activation of human SIRT1 with an AMC substrate and a natural-amino-acid substrate without abolishing basal catalytic activity.

    Human SIRT1 E230K activation-defective variant → SIRT1 source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary full text
    experimental_model
    Recombinant mutagenesis; 40 micromolar resveratrol in the illustrated AMC assay.
    limitations
    Other figures use synthetic STACs; those interventions are not silently attributed to resveratrol.
    nutrient_topic
    Resveratrol collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Resveratrol
    plain_language
    An enzyme residue contributes to selective activation.
    primary_references
    Evidence for a common mechanism of SIRT1 regulation by allosteric activators. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23471411/ · DOI 10.1126/science.1231097
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Resveratrol: metabolites, target selectivity and cross-nutrient mechanisms (2026-09-19) · lines 166–172

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant mutagenesis; 40 micromolar resveratrol in the illustrated AMC assay. · source_derived_draft · unverified_draft

    ## resveratrol-sirt1-e230 An enzyme residue contributes to selective activation. The E230K substitution attenuated resveratrol activation of human SIRT1 with an AMC substrate and a natural-amino-acid substrate without abolishing basal catalytic activity. Model: Recombinant mutagenesis; 40 micromolar resveratrol in the illustrated AMC assay. Limitations: Other figures use synthetic STACs; those interventions are not silently attributed to resveratrol. Evidence access: Primary full text Evidence for a common mechanism of SIRT1 regulation by allosteric activators. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23471411/ · DOI 10.1126/science.1231097
    Complete structured claim and evidence

  3. Resveratrol did not activate human SIRT1 on the tested unlabelled p53 peptide or full-length p53 and acetyl-CoA-synthetase substrates, while fluorophore-tagged peptide assays showed activation.

    Resveratrol → SIRT1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Biochemical comparison of labelled and native substrates.
    limitations
    This is a negative result for tested substrates, not proof that no native sequence can respond.
    nutrient_topic
    Resveratrol collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Resveratrol
    plain_language
    Some original activation assays depended on the artificial reporter.
    primary_references
    SRT1720, SRT2183, SRT1460, and resveratrol are not direct activators of SIRT1. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20061378/ · DOI 10.1074/jbc.M109.088682

    Resveratrol: metabolites, target selectivity and cross-nutrient mechanisms (2026-09-19) · lines 150–156

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Biochemical comparison of labelled and native substrates. · source_derived_draft · unverified_draft

    ## resveratrol-sirt1-native-null Some original activation assays depended on the artificial reporter. Resveratrol did not activate human SIRT1 on the tested unlabelled p53 peptide or full-length p53 and acetyl-CoA-synthetase substrates, while fluorophore-tagged peptide assays showed activation. Model: Biochemical comparison of labelled and native substrates. Limitations: This is a negative result for tested substrates, not proof that no native sequence can respond. Evidence access: Primary abstract SRT1720, SRT2183, SRT1460, and resveratrol are not direct activators of SIRT1. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20061378/ · DOI 10.1074/jbc.M109.088682
    Complete structured claim and evidence

  4. In a 6,802-site physiological acetyl-peptide screen, resveratrol stimulated SIRT1 deacetylation of a small subset, inhibited another subset and left most sites largely unchanged; solution assays confirmed selected categories.

    Resveratrol → SIRT1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Peptide arrays and solution enzyme assays.
    limitations
    Peptides do not reproduce complete chromatin or whole-cell substrate competition.
    nutrient_topic
    Resveratrol collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Resveratrol
    plain_language
    SIRT1 is not a universal on/off switch for resveratrol.
    primary_references
    Sirt1 activation by resveratrol is substrate sequence-selective. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23524286/ · DOI 10.18632/aging.100542

    Resveratrol: metabolites, target selectivity and cross-nutrient mechanisms (2026-09-19) · lines 158–164

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Peptide arrays and solution enzyme assays. · source_derived_draft · unverified_draft

    ## resveratrol-sirt1-sequence-selectivity SIRT1 is not a universal on/off switch for resveratrol. In a 6,802-site physiological acetyl-peptide screen, resveratrol stimulated SIRT1 deacetylation of a small subset, inhibited another subset and left most sites largely unchanged; solution assays confirmed selected categories. Model: Peptide arrays and solution enzyme assays. Limitations: Peptides do not reproduce complete chromatin or whole-cell substrate competition. Evidence access: Primary full text Sirt1 activation by resveratrol is substrate sequence-selective. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23524286/ · DOI 10.18632/aging.100542
    Complete structured claim and evidence

  5. The THP-1 treatments increased SIRT1 and FOXO3a expression while suppressing high-glucose inflammatory responses.

    Fisetin → SIRT1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Fisetin, luteolin and combination conditions in human cells.
    limitations
    Expression is not proven direct SIRT1 activation or greater NAD availability.
    nutrient_topic
    Fisetin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Fisetin
    plain_language
    This branch connects to NAD-dependent cell regulation.
    primary_references
    Combination Treatments with Luteolin and Fisetin Enhance Anti-Inflammatory Effects in High Glucose-Treated THP-1 Cells Through Histone Acetyltransferase/Histone Deacetylase Regulation. · 2017 · https://pubmed.ncbi.nlm.nih.gov/28650731/ · DOI 10.1089/jmf.2017.3968

    Fisetin: metabolism, cell-state responses and cross-nutrient mechanisms (2026-09-19) · lines 456–462

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Fisetin, luteolin and combination conditions in human cells. · source_derived_draft · unverified_draft

    ## fisetin-sirt1-foxo-response This branch connects to NAD-dependent cell regulation. The THP-1 treatments increased SIRT1 and FOXO3a expression while suppressing high-glucose inflammatory responses. Model: Fisetin, luteolin and combination conditions in human cells. Limitations: Expression is not proven direct SIRT1 activation or greater NAD availability. Evidence access: Primary abstract Combination Treatments with Luteolin and Fisetin Enhance Anti-Inflammatory Effects in High Glucose-Treated THP-1 Cells Through Histone Acetyltransferase/Histone Deacetylase Regulation. · 2017 · https://pubmed.ncbi.nlm.nih.gov/28650731/ · DOI 10.1089/jmf.2017.3968
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Epac1 siRNA prevented the resveratrol-induced NAD increase and PGC-1alpha deacetylation in human HeLa experiments.

    Human Epac1 / RAPGEF3 → Resveratrol-associated NAD increase in HeLa cells source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary full text
    experimental_model
    Same cellular mechanism study.
    limitations
    NAD measurement and substrate deacetylation do not establish direct SIRT1 binding.
    nutrient_topic
    Resveratrol collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Resveratrol
    plain_language
    Calcium/cAMP signaling connects to NAD-dependent regulation.
    primary_references
    Resveratrol ameliorates aging-related metabolic phenotypes by inhibiting cAMP phosphodiesterases. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22304913/ · DOI 10.1016/j.cell.2012.01.017
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Resveratrol: metabolites, target selectivity and cross-nutrient mechanisms (2026-09-19) · lines 246–252

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Same cellular mechanism study. · source_derived_draft · unverified_draft

    ## resveratrol-epac-nad-loss Calcium/cAMP signaling connects to NAD-dependent regulation. Epac1 siRNA prevented the resveratrol-induced NAD increase and PGC-1alpha deacetylation in human HeLa experiments. Model: Same cellular mechanism study. Limitations: NAD measurement and substrate deacetylation do not establish direct SIRT1 binding. Evidence access: Primary full text Resveratrol ameliorates aging-related metabolic phenotypes by inhibiting cAMP phosphodiesterases. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22304913/ · DOI 10.1016/j.cell.2012.01.017
    Complete structured claim and evidence

  2. In 11 obese men, 150 mg/day resveratrol for 30 days increased muscle AMPK activation and SIRT1/PGC-1alpha protein, improved fatty-acid-supported mitochondrial respiration and reduced liver fat and selected metabolic markers.

    Resveratrol → Metabolic response to resveratrol in obese men source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Randomized double-blind crossover; resVida preparation.
    limitations
    HOMA is not a clamp; no increase in mitochondrial content and no long-term disease outcome were demonstrated.
    nutrient_topic
    Resveratrol collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Resveratrol
    plain_language
    A small controlled human study found several metabolic changes.
    primary_references
    Calorie restriction-like effects of 30 days of resveratrol supplementation on energy metabolism and metabolic profile in obese humans. · 2011 · https://pubmed.ncbi.nlm.nih.gov/22055504/ · DOI 10.1016/j.cmet.2011.10.002

    Resveratrol: metabolites, target selectivity and cross-nutrient mechanisms (2026-09-19) · lines 454–460

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Randomized double-blind crossover; resVida preparation. · source_derived_draft · unverified_draft

    ## resveratrol-human-metabolic-positive A small controlled human study found several metabolic changes. In 11 obese men, 150 mg/day resveratrol for 30 days increased muscle AMPK activation and SIRT1/PGC-1alpha protein, improved fatty-acid-supported mitochondrial respiration and reduced liver fat and selected metabolic markers. Model: Randomized double-blind crossover; resVida preparation. Limitations: HOMA is not a clamp; no increase in mitochondrial content and no long-term disease outcome were demonstrated. Evidence access: Primary abstract Calorie restriction-like effects of 30 days of resveratrol supplementation on energy metabolism and metabolic profile in obese humans. · 2011 · https://pubmed.ncbi.nlm.nih.gov/22055504/ · DOI 10.1016/j.cmet.2011.10.002
    Complete structured claim and evidence

  3. In nonobese postmenopausal women with normal glucose tolerance, 75 mg/day resveratrol for 12 weeks did not improve liver, muscle or adipose insulin sensitivity or measured AMPK/SIRT1/NAMPT/PPARGC1A targets.

    Resveratrol → Metabolic outcomes in nonobese postmenopausal women source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Randomized double-blind placebo-controlled trial.
    limitations
    Null result is population- and regimen-specific.
    nutrient_topic
    Resveratrol collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Resveratrol
    plain_language
    Effects in metabolically abnormal models do not automatically transfer to healthy people.
    primary_references
    Resveratrol supplementation does not improve metabolic function in nonobese women with normal glucose tolerance. · 2012 · https://pubmed.ncbi.nlm.nih.gov/23102619/ · DOI 10.1016/j.cmet.2012.09.015

    Resveratrol: metabolites, target selectivity and cross-nutrient mechanisms (2026-09-19) · lines 470–476

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Randomized double-blind placebo-controlled trial. · source_derived_draft · unverified_draft

    ## resveratrol-human-women-null Effects in metabolically abnormal models do not automatically transfer to healthy people. In nonobese postmenopausal women with normal glucose tolerance, 75 mg/day resveratrol for 12 weeks did not improve liver, muscle or adipose insulin sensitivity or measured AMPK/SIRT1/NAMPT/PPARGC1A targets. Model: Randomized double-blind placebo-controlled trial. Limitations: Null result is population- and regimen-specific. Evidence access: Primary abstract Resveratrol supplementation does not improve metabolic function in nonobese women with normal glucose tolerance. · 2012 · https://pubmed.ncbi.nlm.nih.gov/23102619/ · DOI 10.1016/j.cmet.2012.09.015
    Complete structured claim and evidence

  4. SIRT1 siRNA diminished naringenin-associated improvements in endothelial senescence, oxidative stress and mitochondrial injury.

    Experimental SIRT1 siRNA suppression → Naringenin response in oxidatively stressed endothelial cells source_derived_draftungraded
    Experimental context and source evidence
    dose
    Naringenin with SIRT1 siRNA
    duration
    Cell experiment accompanying three-month mouse dosing
    evidence_access
    Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    evidence_scope
    literature_reviewed; model-specific source-derived curation
    experimental_model
    Hydrogen-peroxide-stressed endothelial cells; aged ApoE-null mouse arm
    limitations
    SIRT1 involvement in a cell model does not establish direct SIRT1 binding or human atherosclerosis treatment.
    nutrient_topic
    Naringenin chapter; interacting nutrients, drugs, peptides and proteins retain their experimental settings. · Naringenin
    organism
    Hydrogen-peroxide-stressed endothelial cells; aged ApoE-null mouse arm
    plain_language
    SIRT1 siRNA diminished naringenin-associated improvements in endothelial senescence, oxidative stress and mitochondrial injury.
    primary_references
    Naringenin ameliorates vascular senescence and atherosclerosis involving SIRT1 activation. (2023). https://pubmed.ncbi.nlm.nih.gov/37343148/ DOI: 10.1093/jpp/rgad053
    route
    In vitro perturbation
    tissue
    SIRT1, FOXO3a/PGC1alpha and senescence measures

    Naringenin: mechanism of action and interactions (2026-09-20) · lines 143–152

    Original AI-assisted source-specific curation with primary-study citations, model, exposure, route, duration, negative findings and limitations preserved. Not publisher full text. · supports · Hydrogen-peroxide-stressed endothelial cells; aged ApoE-null mouse arm · source_derived_draft · unverified_draft

    ## naringenin-sirt1-silencing SIRT1 siRNA diminished naringenin-associated improvements in endothelial senescence, oxidative stress and mitochondrial injury. Model/species: Hydrogen-peroxide-stressed endothelial cells; aged ApoE-null mouse arm Tissue/system: SIRT1, FOXO3a/PGC1alpha and senescence measures Exposure: Naringenin with SIRT1 siRNA Route: In vitro perturbation Duration: Cell experiment accompanying three-month mouse dosing Limits: SIRT1 involvement in a cell model does not establish direct SIRT1 binding or human atherosclerosis treatment. Primary reference: Naringenin ameliorates vascular senescence and atherosclerosis involving SIRT1 activation. (2023). https://pubmed.ncbi.nlm.nih.gov/37343148/ DOI: 10.1093/jpp/rgad053 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    Complete structured claim and evidence

  5. Pharmacological inhibitor experiments implicated CaMKK and SIRT1 in SAC-associated AMPK signaling.

    S-allyl-L-cysteine / SAC → CaMKK/SIRT1-sensitive SAC signaling in HepG2 cells 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 addition; pathway inhibitor comparisons
    experimental_model
    Free-fatty-acid-treated HepG2 cells
    interpretation_status
    Source-derived research curation; not independent primary verification
    limitations
    Abstract does not specify CaMKK isoform, inhibitor selectivity or direct SIRT1 activation. No NAD or calcium depletion is demonstrated.
    nutrient_topic
    S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC
    organism
    Homo sapiens
    plain_language
    Upstream pathway perturbations identify dependencies to investigate.
    primary_references
    [23465592] S-allyl cysteine attenuates free fatty acid-induced lipogenesis in human HepG2 cells through activation of the AMP-activated protein kinase-dependent pathway. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23465592/ · DOI 10.1016/j.jnutbio.2012.12.006
    route
    Cell culture
    tissue_or_cell_type
    Free-fatty-acid-treated HepG2 cells

    S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 212–219

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Free-fatty-acid-treated HepG2 cells · source_derived_draft · unverified_draft

    ## s-allylcysteine-upstream-kinase Upstream pathway perturbations identify dependencies to investigate. Pharmacological inhibitor experiments implicated CaMKK and SIRT1 in SAC-associated AMPK signaling. Model: Free-fatty-acid-treated HepG2 cells Limitations: Abstract does not specify CaMKK isoform, inhibitor selectivity or direct SIRT1 activation. No NAD or calcium depletion is demonstrated. Evidence access: Primary abstract [23465592] S-allyl cysteine attenuates free fatty acid-induced lipogenesis in human HepG2 cells through activation of the AMP-activated protein kinase-dependent pathway. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23465592/ · DOI 10.1016/j.jnutbio.2012.12.006 Structured context: {"organism": "Homo sapiens", "tissue_or_cell_type": "Free-fatty-acid-treated HepG2 cells", "dose": "Not specified in accessed abstract", "duration": "Not specified in accessed abstract", "route": "Cell culture", "experimental_comparison": "SAC addition; pathway inhibitor comparisons", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}
    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