Component

Formaldehyde

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

3 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. Only Adh3-null mice had a significantly reduced formaldehyde LD50, and Adh3 played no role with ethanol or retinol.

    Experimental Adh3-null mouse genotype → Formaldehyde source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/alcohol-research/10358022.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c1e4e6f0703d814d36609e71a38be53f7c36bebcfdcd3a60c52ea49625369305", "start_char": 0, "end_char": 1272, "text_sha256": "c1e4e6f0703d814d36609e71a38be53f7c36bebcfdcd3a60c52ea49625369305"}
    experimental_model
    Adh1, Adh3 and Adh4 null mutant mice with ethanol, formaldehyde and retinol challenges
    exposure
    Intoxicating ethanol dose, formaldehyde LD50, and retinol administration
    limitations
    A clean three-gene dissection showing which enzyme does which job. It is a mouse gene family that does not map one-to-one onto the human one.
    nutrient_topic
    Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol
    organism
    Mouse
    plain_language
    The third enzyme has a different job entirely.
    primary_references
    [alcohol-p10358022] Metabolic deficiencies in alcohol dehydrogenase Adh1, Adh3, and Adh4 null mutant mice. Overlapping roles of Adh1 and Adh4 in ethanol clearance and metabolism of retinol to retinoic acid. (1999). https://pubmed.ncbi.nlm.nih.gov/10358022/ DOI: 10.1074/jbc.274.24.16796
    tissue_or_cell_type
    Liver and embryo
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 254–265

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Adh1, Adh3 and Adh4 null mutant mice with ethanol, formaldehyde and retinol challenges · source_derived_draft · unverified_draft

    ### alcohol-adh3-formaldehyde Only Adh3-null mice had a significantly reduced formaldehyde LD50, and Adh3 played no role with ethanol or retinol. Condition category: machinery_impairment nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: The third enzyme has a different job entirely. organism: Mouse tissue_or_cell_type: Liver and embryo experimental_model: Adh1, Adh3 and Adh4 null mutant mice with ethanol, formaldehyde and retinol challenges limitations: A clean three-gene dissection showing which enzyme does which job. It is a mouse gene family that does not map one-to-one onto the human one. exposure: Intoxicating ethanol dose, formaldehyde LD50, and retinol administration evidence_span: {"source_cache": "artifacts/alcohol-research/10358022.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c1e4e6f0703d814d36609e71a38be53f7c36bebcfdcd3a60c52ea49625369305", "start_char": 0, "end_char": 1272, "text_sha256": "c1e4e6f0703d814d36609e71a38be53f7c36bebcfdcd3a60c52ea49625369305"} [alcohol-p10358022] Metabolic deficiencies in alcohol dehydrogenase Adh1, Adh3, and Adh4 null mutant mice. Overlapping roles of Adh1 and Adh4 in ethanol clearance and metabolism of retinol to retinoic acid. (1999). https://pubmed.ncbi.nlm.nih.gov/10358022/ DOI: 10.1074/jbc.274.24.16796
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. KDM1A/LSD1 oxidatively removes a methyl group from H3K4me2 through a flavin-dependent reaction.

    KDM1A → Histone H3 dimethylated at K4 source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Purified LSD1 enzyme / histone assays and cellular RNA interference.
    limitations
    Do not extend this specific activity to trimethyllysine or every histone site. 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
    Some lysine methyl marks can be erased by a flavin enzyme.
    primary_references
    [lsd1-2004] Histone demethylation mediated by the nuclear amine oxidase homolog LSD1 (2004). https://pubmed.ncbi.nlm.nih.gov/15620353/ DOI: 10.1016/j.cell.2004.12.012
    tissue_or_cell_type
    Not specified as a whole tissue; see experimental model.

    L-Lysine: mechanism-first literature curation (2026-09-17) · lines 557–565

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified LSD1 enzyme / histone assays and cellular RNA interference. · source_derived_draft · unverified_draft

    ### kdm1a-h3k4-demethylation KDM1A/LSD1 oxidatively removes a methyl group from H3K4me2 through a flavin-dependent reaction. Plain language: Some lysine methyl marks can be erased by a flavin enzyme. Condition category: normal organism: Human tissue_or_cell_type: Not specified as a whole tissue; see experimental model. experimental_model: Purified LSD1 enzyme / histone assays and cellular RNA interference. limitations: Do not extend this specific activity to trimethyllysine or every histone site. This reaction modifies lysine already in a protein. It does not show that extra oral lysine increases the reaction or improves a clinical outcome. [lsd1-2004] Histone demethylation mediated by the nuclear amine oxidase homolog LSD1 (2004). https://pubmed.ncbi.nlm.nih.gov/15620353/ DOI: 10.1016/j.cell.2004.12.012
    Complete structured claim and evidence

  2. KDM4A/JMJD2A can convert H3K9me3 to H3K9me2 using Fe(II), oxygen and 2-oxoglutarate.

    KDM4A → Histone H3 trimethylated at K9 source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Human JMJD2A catalytic-domain structures and methylated peptide assays.
    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
    An iron-dependent enzyme erases a different class of methyl mark.
    primary_references
    [kdm4a-2006] Structural insights into histone demethylation by JMJD2 family members (2006). https://pubmed.ncbi.nlm.nih.gov/16677698/ DOI: 10.1016/j.cell.2006.04.024 [kdm4a-specificity-2007] Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase (2007). https://pubmed.ncbi.nlm.nih.gov/17589523/ DOI: 10.1038/nsmb1273
    tissue_or_cell_type
    Not specified as a whole tissue; see experimental model.

    L-Lysine: mechanism-first literature curation (2026-09-17) · lines 567–576

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human JMJD2A catalytic-domain structures and methylated peptide assays. · source_derived_draft · unverified_draft

    ### kdm4a-h3k9-demethylation KDM4A/JMJD2A can convert H3K9me3 to H3K9me2 using Fe(II), oxygen and 2-oxoglutarate. Plain language: An iron-dependent enzyme erases a different class of methyl mark. Condition category: normal organism: Human tissue_or_cell_type: Not specified as a whole tissue; see experimental model. experimental_model: Human JMJD2A catalytic-domain structures and methylated peptide assays. 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. [kdm4a-2006] Structural insights into histone demethylation by JMJD2 family members (2006). https://pubmed.ncbi.nlm.nih.gov/16677698/ DOI: 10.1016/j.cell.2006.04.024 [kdm4a-specificity-2007] Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase (2007). https://pubmed.ncbi.nlm.nih.gov/17589523/ DOI: 10.1038/nsmb1273
    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