Component

Histone H3

Human histone H3 protein family; individual isoform not resolved by the selected assay.

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

Where it participates (unsigned role)

  1. The 2011 study reported natural biotinylation of less than 0.001% of human H3/H4 and argued for rare modification rather than a universal assay artifact.

    Biotin → Detection of biotin on human histones source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/biotin-research/21930408.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "51af2341c7be0cb58c57e09784ebb8daabdd98cc93f04be52bb7b04b496e0b91", "start_char": 0, "end_char": 1318, "text_sha256": "51af2341c7be0cb58c57e09784ebb8daabdd98cc93f04be52bb7b04b496e0b91"}
    experimental_model
    Multiple antibody, radiotracer and cell-line comparisons of human histone biotinylation
    exposure
    Assay comparisons responding to artifact criticism
    limitations
    Authors estimated extremely low abundance and proposed HLCS chromatin scaffolding as a working model; nutritional epigenetic benefit was not demonstrated.
    nutrient_topic
    Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin
    organism
    Homo sapiens
    plain_language
    Later work defended a very rare mark while questioning whether that tiny amount explains biological effects.
    primary_references
    [b7-p21930408] Biotinylation is a natural, albeit rare, modification of human histones. (2011). https://pubmed.ncbi.nlm.nih.gov/21930408/ DOI: 10.1016/j.ymgme.2011.08.030
    tissue_or_cell_type
    Human histones H3/H4 in cultured cells

    Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 1183–1194

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Multiple antibody, radiotracer and cell-line comparisons of human histone biotinylation · source_derived_draft · unverified_draft

    ### b7-histone-rare-report The 2011 study reported natural biotinylation of less than 0.001% of human H3/H4 and argued for rare modification rather than a universal assay artifact. Condition category: normal nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Later work defended a very rare mark while questioning whether that tiny amount explains biological effects. organism: Homo sapiens tissue_or_cell_type: Human histones H3/H4 in cultured cells experimental_model: Multiple antibody, radiotracer and cell-line comparisons of human histone biotinylation limitations: Authors estimated extremely low abundance and proposed HLCS chromatin scaffolding as a working model; nutritional epigenetic benefit was not demonstrated. exposure: Assay comparisons responding to artifact criticism evidence_span: {"source_cache": "artifacts/biotin-research/21930408.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "51af2341c7be0cb58c57e09784ebb8daabdd98cc93f04be52bb7b04b496e0b91", "start_char": 0, "end_char": 1318, "text_sha256": "51af2341c7be0cb58c57e09784ebb8daabdd98cc93f04be52bb7b04b496e0b91"} [b7-p21930408] Biotinylation is a natural, albeit rare, modification of human histones. (2011). https://pubmed.ncbi.nlm.nih.gov/21930408/ DOI: 10.1016/j.ymgme.2011.08.030
    Complete structured claim and evidence

  2. PARP1 with HPF1 and NAD+ ADP-ribosylated histone H3 at serines 10 and 28 in reconstituted assays.

    Human PARP1 → Histone H3 serine ADP-ribosylation source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    evidence_span
    {"source_cache": "artifacts/niacin-consumption-sources/parp2017.txt", "locator": "Full text, normalized paragraph 33", "start_char": 8991, "end_char": 10338, "file_sha256": "8195abaa884a41856a21fb1d4e7ee376ce80424f11f4625ca4d597a717cef30e", "text_sha256": "ce51127814506d2aa745261fa114922afd3585ee7a97be6fc1cf3914c6609789"}
    experimental_model
    Recombinant human PARP/HPF1 and histone substrate reconstitution with mass spectrometry
    exposure
    Activated DNA and NAD+; HPF1 addition
    limitations
    Direct in vitro modification; protein-bound serine is not a free dietary substrate. No vitamin intake or clinical benefit measured.
    nutrient_topic
    Niacin research collection; topical membership is not evidence of a direct dietary effect. · Niacin (vitamin B3)
    organism
    Human
    plain_language
    PARP1 uses NAD to add ADP-ribose to histone serines when HPF1 is present.
    primary_references
    [b3-cons-parp2017] Serine ADP-Ribosylation Depends on HPF1. (2017). https://pubmed.ncbi.nlm.nih.gov/28190768/ DOI: 10.1016/j.molcel.2017.01.003
    tissue_or_cell_type
    Cell-free histone assay

    Niacin: NAD metabolism, deficiency and nutrient interactions (2026-09-17) · lines 635–647

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human PARP/HPF1 and histone substrate reconstitution with mass spectrometry · source_derived_draft · unverified_draft

    ### b3-cons-parp1-h3-serine PARP1 with HPF1 and NAD+ ADP-ribosylated histone H3 at serines 10 and 28 in reconstituted assays. Condition category: normal nutrient_topic: Niacin research collection; topical membership is not evidence of a direct dietary effect. plain_language: PARP1 uses NAD to add ADP-ribose to histone serines when HPF1 is present. organism: Human tissue_or_cell_type: Cell-free histone assay experimental_model: Recombinant human PARP/HPF1 and histone substrate reconstitution with mass spectrometry limitations: Direct in vitro modification; protein-bound serine is not a free dietary substrate. No vitamin intake or clinical benefit measured. exposure: Activated DNA and NAD+; HPF1 addition cross_nutrient: false evidence_span: {"source_cache": "artifacts/niacin-consumption-sources/parp2017.txt", "locator": "Full text, normalized paragraph 33", "start_char": 8991, "end_char": 10338, "file_sha256": "8195abaa884a41856a21fb1d4e7ee376ce80424f11f4625ca4d597a717cef30e", "text_sha256": "ce51127814506d2aa745261fa114922afd3585ee7a97be6fc1cf3914c6609789"} [b3-cons-parp2017] Serine ADP-Ribosylation Depends on HPF1. (2017). https://pubmed.ncbi.nlm.nih.gov/28190768/ DOI: 10.1016/j.molcel.2017.01.003
    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