Component

Human acetyl-CoA carboxylase activity, isoform unresolved in assay

Human acetyl-CoA carboxylase activity, isoform unresolved in assay. Species, exposure and limitations are retained in each linked claim.

2 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 acts on it

  1. LKB1 knockdown prevented the norathyriol-associated increase in ACC phosphorylation.

    Experimental human STK11 / LKB1 siRNA knockdown → Human acetyl-CoA carboxylase activity, isoform unresolved in assay source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    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": 33073, "end_char": 35334, "text_sha256": "166efaa83fd229a3e036a60bf4e23173a7b50a3044686fe1a324d6dc604354a9"}
    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
    Removing an upstream component interrupted the response.
    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
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Mangiferin: metabolism, signaling and nutrient connections (2026-09-17) · lines 510–521

    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-lkb1-acc LKB1 knockdown prevented the norathyriol-associated increase in ACC phosphorylation. Condition category: machinery_impairment nutrient_topic: Mangiferin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Removing an upstream component interrupted the response. 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": 33073, "end_char": 35334, "text_sha256": "166efaa83fd229a3e036a60bf4e23173a7b50a3044686fe1a324d6dc604354a9"} [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. SAC treatment increased ACC phosphorylation in HepG2 cells.

    S-allyl-L-cysteine / SAC → Human acetyl-CoA carboxylase activity, isoform unresolved in assay 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
    The accessed abstract does not resolve the ACC isoform or phosphorylation site.
    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 lipid-synthesis enzyme had a separate measured modification.
    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 194–201

    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-acc A lipid-synthesis enzyme had a separate measured modification. SAC treatment increased ACC phosphorylation in HepG2 cells. Model: Free-fatty-acid-treated HepG2 cells Limitations: The accessed abstract does not resolve the ACC isoform or phosphorylation site. 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