Component

Human PARP1

Human poly(ADP-ribose) polymerase 1.

6 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. Silencing PARP1 abolished the one-hour NAD increase induced by low-dose resveratrol in human HeLa cells.

    Human PARP1 → NAD content in human 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
    siRNA experiments; 5 micromolar resveratrol.
    limitations
    Cell-model dependency, not a dietary resveratrol-deficiency state.
    nutrient_topic
    Resveratrol collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Resveratrol
    plain_language
    Removing a signaling component prevented the rebound.
    primary_references
    A human tRNA synthetase is a potent PARP1-activating effector target for resveratrol. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25533949/ · DOI 10.1038/nature14028
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Resveratrol: metabolites, target selectivity and cross-nutrient mechanisms (2026-09-19) · lines 326–332

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · siRNA experiments; 5 micromolar resveratrol. · source_derived_draft · unverified_draft

    ## resveratrol-parp-loss Removing a signaling component prevented the rebound. Silencing PARP1 abolished the one-hour NAD increase induced by low-dose resveratrol in human HeLa cells. Model: siRNA experiments; 5 micromolar resveratrol. Limitations: Cell-model dependency, not a dietary resveratrol-deficiency state. Evidence access: Primary full text A human tRNA synthetase is a potent PARP1-activating effector target for resveratrol. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25533949/ · DOI 10.1038/nature14028
    Complete structured claim and evidence

  2. The PARP inhibitor Tiq-A slowed early nuclear/cytoplasmic NAD+ depletion after NAMPT inhibition, with little effect on mitochondrial depletion.

    Human PARP1 → Nucleocytoplasmic NAD depletion during salvage blockade source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary full text
    experimental_model
    Cultured human cells; pharmacological PARP inhibition.
    limitations
    Tiq-A is not a PARP1-specific genetic experiment, and did not prevent eventual depletion in all compartments.
    nutrient_topic
    NAD+ collection; molecular form, preparation, species, exposure and manipulation remain explicit. · NAD+
    plain_language
    Consumption can determine how quickly a blocked supply becomes a shortage.
    primary_references
    Biosensor reveals multiple sources for mitochondrial NAD⁺. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27313049/ · DOI 10.1126/science.aad5168
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    NAD+: compartmental supply, consumption and cross-nutrient mechanisms (2026-09-19) · lines 28–34

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cultured human cells; pharmacological PARP inhibition. · source_derived_draft · unverified_draft

    ## nad-plus-parp-depletion-rate Consumption can determine how quickly a blocked supply becomes a shortage. The PARP inhibitor Tiq-A slowed early nuclear/cytoplasmic NAD+ depletion after NAMPT inhibition, with little effect on mitochondrial depletion. Model: Cultured human cells; pharmacological PARP inhibition. Limitations: Tiq-A is not a PARP1-specific genetic experiment, and did not prevent eventual depletion in all compartments. Evidence access: Primary full text Biosensor reveals multiple sources for mitochondrial NAD⁺. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27313049/ · DOI 10.1126/science.aad5168
    Complete structured claim and evidence

  3. 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

What acts on it

  1. In the resveratrol study, human TyrRS stimulated NAD-dependent PARP1 auto-poly-ADP-ribosylation in biochemical experiments.

    Human cytosolic tyrosyl-tRNA synthetase / YARS1 → Human PARP1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Purified-protein interaction/activation assays.
    limitations
    Greater PARylation need not imply greater net NAD stores.
    nutrient_topic
    Resveratrol collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Resveratrol
    plain_language
    This signaling step consumes a niacin-derived cofactor.
    primary_references
    A human tRNA synthetase is a potent PARP1-activating effector target for resveratrol. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25533949/ · DOI 10.1038/nature14028

    Resveratrol: metabolites, target selectivity and cross-nutrient mechanisms (2026-09-19) · lines 302–308

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified-protein interaction/activation assays. · source_derived_draft · unverified_draft

    ## resveratrol-tyrrs-parp This signaling step consumes a niacin-derived cofactor. In the resveratrol study, human TyrRS stimulated NAD-dependent PARP1 auto-poly-ADP-ribosylation in biochemical experiments. Model: Purified-protein interaction/activation assays. Limitations: Greater PARylation need not imply greater net NAD stores. Evidence access: Primary full text A human tRNA synthetase is a potent PARP1-activating effector target for resveratrol. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25533949/ · DOI 10.1038/nature14028
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Resveratrol promoted endogenous TyrRS nuclear translocation in human HeLa cells, coincident with PARP1 auto-PARylation.

    Resveratrol → Human cytosolic tyrosyl-tRNA synthetase / YARS1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    HeLa time-course and purified interaction experiments.
    limitations
    Compartment change is not general inhibition of protein synthesis in humans.
    nutrient_topic
    Resveratrol collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Resveratrol
    plain_language
    An amino-acid enzyme moves into a stress-signaling role.
    primary_references
    A human tRNA synthetase is a potent PARP1-activating effector target for resveratrol. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25533949/ · DOI 10.1038/nature14028

    Resveratrol: metabolites, target selectivity and cross-nutrient mechanisms (2026-09-19) · lines 294–300

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · HeLa time-course and purified interaction experiments. · source_derived_draft · unverified_draft

    ## resveratrol-tyrrs-nucleus An amino-acid enzyme moves into a stress-signaling role. Resveratrol promoted endogenous TyrRS nuclear translocation in human HeLa cells, coincident with PARP1 auto-PARylation. Model: HeLa time-course and purified interaction experiments. Limitations: Compartment change is not general inhibition of protein synthesis in humans. Evidence access: Primary full text A human tRNA synthetase is a potent PARP1-activating effector target for resveratrol. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25533949/ · DOI 10.1038/nature14028
    Complete structured claim and evidence

  2. FK866-mediated NAD depletion impaired DNA repair and damage-induced PARylation in the tested human cancer-cell experiments.

    Human nicotinamide phosphoribosyltransferase / NAMPT → DNA repair after NAD depletion in human MCF-7 cells source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary full text
    experimental_model
    Human MCF-7 cells, NAMPT inhibitor, genotoxins and CometChip/PAR assays.
    limitations
    Genotoxin and endpoint dependent; not proof that raising NAD prevents human cancer.
    nutrient_topic
    NAD+ collection; molecular form, preparation, species, exposure and manipulation remain explicit. · NAD+
    plain_language
    When salvage is blocked, repair enzymes can lose access to their substrate.
    primary_references
    Extracellular NAD+ enhances PARP-dependent DNA repair capacity independently of CD73 activity. · 2020 · https://pubmed.ncbi.nlm.nih.gov/31959836/ · DOI 10.1038/s41598-020-57506-9
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    NAD+: compartmental supply, consumption and cross-nutrient mechanisms (2026-09-19) · lines 252–258

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human MCF-7 cells, NAMPT inhibitor, genotoxins and CometChip/PAR assays. · source_derived_draft · unverified_draft

    ## nad-plus-repair-depletion When salvage is blocked, repair enzymes can lose access to their substrate. FK866-mediated NAD depletion impaired DNA repair and damage-induced PARylation in the tested human cancer-cell experiments. Model: Human MCF-7 cells, NAMPT inhibitor, genotoxins and CometChip/PAR assays. Limitations: Genotoxin and endpoint dependent; not proof that raising NAD prevents human cancer. Evidence access: Primary full text Extracellular NAD+ enhances PARP-dependent DNA repair capacity independently of CD73 activity. · 2020 · https://pubmed.ncbi.nlm.nih.gov/31959836/ · DOI 10.1038/s41598-020-57506-9
    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