Component

ADP-ribose

Free ADP-ribose; distinct from cyclic ADP-ribose and protein-bound ADP-ribose.

4 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. Intracellular free ADP-ribose gated calcium-permeable currents in HEK293 cells expressing human TRPM2/LTRPC2.

    ADP-ribose → Human TRPM2 source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    true
    evidence_span
    {"source_cache": "artifacts/niacin-consumption-sources/trpm2001.abstract.txt", "locator": "Indexed abstract", "start_char": 0, "end_char": 964, "file_sha256": "960106d86cb7e891772139bf3b6339a1e50129c93a9e3517ebc7b86d61b4178e", "text_sha256": "960106d86cb7e891772139bf3b6339a1e50129c93a9e3517ebc7b86d61b4178e"}
    experimental_model
    Whole-cell and single-channel electrophysiology
    exposure
    Intracellular free ADP-ribose
    limitations
    This establishes channel gating in the assay, not that all NAD cleavage causes calcium influx in vivo.
    nutrient_topic
    Niacin research collection; topical membership is not evidence of a direct dietary effect. · Niacin (vitamin B3)
    organism
    Human
    plain_language
    Free ADP-ribose can open a channel that conducts calcium.
    primary_references
    [b3-cons-trpm2001] ADP-ribose gating of the calcium-permeable LTRPC2 channel revealed by Nudix motif homology. (2001). https://pubmed.ncbi.nlm.nih.gov/11385575/ DOI: 10.1038/35079100
    tissue_or_cell_type
    HEK293 cells expressing recombinant TRPM2

    Niacin: NAD metabolism, deficiency and nutrient interactions (2026-09-17) · lines 621–633

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Whole-cell and single-channel electrophysiology · source_derived_draft · unverified_draft

    ### b3-cons-adpr-trpm2-gating Intracellular free ADP-ribose gated calcium-permeable currents in HEK293 cells expressing human TRPM2/LTRPC2. Condition category: normal nutrient_topic: Niacin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Free ADP-ribose can open a channel that conducts calcium. organism: Human tissue_or_cell_type: HEK293 cells expressing recombinant TRPM2 experimental_model: Whole-cell and single-channel electrophysiology limitations: This establishes channel gating in the assay, not that all NAD cleavage causes calcium influx in vivo. exposure: Intracellular free ADP-ribose cross_nutrient: true evidence_span: {"source_cache": "artifacts/niacin-consumption-sources/trpm2001.abstract.txt", "locator": "Indexed abstract", "start_char": 0, "end_char": 964, "file_sha256": "960106d86cb7e891772139bf3b6339a1e50129c93a9e3517ebc7b86d61b4178e", "text_sha256": "960106d86cb7e891772139bf3b6339a1e50129c93a9e3517ebc7b86d61b4178e"} [b3-cons-trpm2001] ADP-ribose gating of the calcium-permeable LTRPC2 channel revealed by Nudix motif homology. (2001). https://pubmed.ncbi.nlm.nih.gov/11385575/ DOI: 10.1038/35079100
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Human CD38 also hydrolyzes cyclic ADP-ribose to ADP-ribose.

    Human CD38 → Cyclic ADP-ribose source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    evidence_span
    {"source_cache": "artifacts/niacin-consumption-sources/cd381998.abstract.txt", "locator": "Indexed abstract", "start_char": 0, "end_char": 1755, "file_sha256": "39f90bb382ddfee34e808fc93c5a1afafc1d9638a9dc73f2770e815827b4f2ad", "text_sha256": "39f90bb382ddfee34e808fc93c5a1afafc1d9638a9dc73f2770e815827b4f2ad"}
    experimental_model
    Biochemical characterization of human CD38
    exposure
    Cyclic ADP-ribose substrate
    limitations
    Primary human enzyme study; source abstract used. Product proportions are assay-specific and do not establish tissue flux or supplementation outcomes.
    nutrient_topic
    Niacin research collection; topical membership is not evidence of a direct dietary effect. · Niacin (vitamin B3)
    organism
    Human
    plain_language
    CD38 also breaks down cyclic ADP-ribose.
    primary_references
    [b3-cons-cd381998] Human CD38 is an authentic NAD(P)+ glycohydrolase. (1998). https://pubmed.ncbi.nlm.nih.gov/9494110/ DOI: 10.1042/bj3301383
    tissue_or_cell_type
    Cell-free enzyme preparation

    Niacin: NAD metabolism, deficiency and nutrient interactions (2026-09-17) · lines 593–605

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Biochemical characterization of human CD38 · source_derived_draft · unverified_draft

    ### b3-cons-cd38-cadpr-hydrolysis Human CD38 also hydrolyzes cyclic ADP-ribose to ADP-ribose. Condition category: normal nutrient_topic: Niacin research collection; topical membership is not evidence of a direct dietary effect. plain_language: CD38 also breaks down cyclic ADP-ribose. organism: Human tissue_or_cell_type: Cell-free enzyme preparation experimental_model: Biochemical characterization of human CD38 limitations: Primary human enzyme study; source abstract used. Product proportions are assay-specific and do not establish tissue flux or supplementation outcomes. exposure: Cyclic ADP-ribose substrate cross_nutrient: false evidence_span: {"source_cache": "artifacts/niacin-consumption-sources/cd381998.abstract.txt", "locator": "Indexed abstract", "start_char": 0, "end_char": 1755, "file_sha256": "39f90bb382ddfee34e808fc93c5a1afafc1d9638a9dc73f2770e815827b4f2ad", "text_sha256": "39f90bb382ddfee34e808fc93c5a1afafc1d9638a9dc73f2770e815827b4f2ad"} [b3-cons-cd381998] Human CD38 is an authentic NAD(P)+ glycohydrolase. (1998). https://pubmed.ncbi.nlm.nih.gov/9494110/ DOI: 10.1042/bj3301383
    Complete structured claim and evidence

  2. Human CD38 hydrolyzes NAD+ to free ADP-ribose and nicotinamide.

    Human CD38 → NAD+ source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    evidence_span
    {"source_cache": "artifacts/niacin-consumption-sources/cd381998.abstract.txt", "locator": "Indexed abstract", "start_char": 0, "end_char": 1755, "file_sha256": "39f90bb382ddfee34e808fc93c5a1afafc1d9638a9dc73f2770e815827b4f2ad", "text_sha256": "39f90bb382ddfee34e808fc93c5a1afafc1d9638a9dc73f2770e815827b4f2ad"}
    experimental_model
    Biochemical characterization of human CD38
    exposure
    NAD+ as substrate
    limitations
    Primary human enzyme study; source abstract used. Product proportions are assay-specific and do not establish tissue flux or supplementation outcomes.
    nutrient_topic
    Niacin research collection; topical membership is not evidence of a direct dietary effect. · Niacin (vitamin B3)
    organism
    Human
    plain_language
    CD38 can break NAD into ADP-ribose and nicotinamide.
    primary_references
    [b3-cons-cd381998] Human CD38 is an authentic NAD(P)+ glycohydrolase. (1998). https://pubmed.ncbi.nlm.nih.gov/9494110/ DOI: 10.1042/bj3301383
    tissue_or_cell_type
    Cell-free enzyme preparation

    Niacin: NAD metabolism, deficiency and nutrient interactions (2026-09-17) · lines 565–577

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Biochemical characterization of human CD38 · source_derived_draft · unverified_draft

    ### b3-cons-cd38-hydrolysis Human CD38 hydrolyzes NAD+ to free ADP-ribose and nicotinamide. Condition category: normal nutrient_topic: Niacin research collection; topical membership is not evidence of a direct dietary effect. plain_language: CD38 can break NAD into ADP-ribose and nicotinamide. organism: Human tissue_or_cell_type: Cell-free enzyme preparation experimental_model: Biochemical characterization of human CD38 limitations: Primary human enzyme study; source abstract used. Product proportions are assay-specific and do not establish tissue flux or supplementation outcomes. exposure: NAD+ as substrate cross_nutrient: false evidence_span: {"source_cache": "artifacts/niacin-consumption-sources/cd381998.abstract.txt", "locator": "Indexed abstract", "start_char": 0, "end_char": 1755, "file_sha256": "39f90bb382ddfee34e808fc93c5a1afafc1d9638a9dc73f2770e815827b4f2ad", "text_sha256": "39f90bb382ddfee34e808fc93c5a1afafc1d9638a9dc73f2770e815827b4f2ad"} [b3-cons-cd381998] Human CD38 is an authentic NAD(P)+ glycohydrolase. (1998). https://pubmed.ncbi.nlm.nih.gov/9494110/ DOI: 10.1042/bj3301383
    Complete structured claim and evidence

  3. Purified human SARM1 TIR domain cleaved NAD+, producing ADP-ribose and nicotinamide as major products.

    Human SARM1 TIR-domain construct → NAD+ source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    evidence_span
    {"source_cache": "artifacts/niacin-consumption-sources/sarm2017.txt", "locator": "Full text, normalized paragraph 24", "start_char": 15550, "end_char": 16946, "file_sha256": "fc30de231911f5c30425173d684495e62c725ba27c78d44592e6bc68433ef545", "text_sha256": "9a9b91a772186c34d8b6305a04bbcf6d3acc40b0448e6f478811527c5174981e"}
    experimental_model
    Purified human SARM1 TIR domain; HPLC and LC-MS/MS
    exposure
    NAD+ incubation
    limitations
    Purified engineered TIR fragment rather than basal activity of intact full-length SARM1; no dietary dose inference.
    nutrient_topic
    Niacin research collection; topical membership is not evidence of a direct dietary effect. · Niacin (vitamin B3)
    organism
    Human
    plain_language
    SARM1 contains a catalytic domain that breaks NAD.
    primary_references
    [b3-cons-sarm2017] The SARM1 Toll/Interleukin-1 Receptor Domain Possesses Intrinsic NAD+ Cleavage Activity that Promotes Pathological Axonal Degeneration. (2017). https://pubmed.ncbi.nlm.nih.gov/28334607/ DOI: 10.1016/j.neuron.2017.02.022
    tissue_or_cell_type
    Cell-free preparation

    Niacin: NAD metabolism, deficiency and nutrient interactions (2026-09-17) · lines 677–689

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human SARM1 TIR domain; HPLC and LC-MS/MS · source_derived_draft · unverified_draft

    ### b3-cons-sarm-adpr-nam Purified human SARM1 TIR domain cleaved NAD+, producing ADP-ribose and nicotinamide as major products. Condition category: normal nutrient_topic: Niacin research collection; topical membership is not evidence of a direct dietary effect. plain_language: SARM1 contains a catalytic domain that breaks NAD. organism: Human tissue_or_cell_type: Cell-free preparation experimental_model: Purified human SARM1 TIR domain; HPLC and LC-MS/MS limitations: Purified engineered TIR fragment rather than basal activity of intact full-length SARM1; no dietary dose inference. exposure: NAD+ incubation cross_nutrient: false evidence_span: {"source_cache": "artifacts/niacin-consumption-sources/sarm2017.txt", "locator": "Full text, normalized paragraph 24", "start_char": 15550, "end_char": 16946, "file_sha256": "fc30de231911f5c30425173d684495e62c725ba27c78d44592e6bc68433ef545", "text_sha256": "9a9b91a772186c34d8b6305a04bbcf6d3acc40b0448e6f478811527c5174981e"} [b3-cons-sarm2017] The SARM1 Toll/Interleukin-1 Receptor Domain Possesses Intrinsic NAD+ Cleavage Activity that Promotes Pathological Axonal Degeneration. (2017). https://pubmed.ncbi.nlm.nih.gov/28334607/ DOI: 10.1016/j.neuron.2017.02.022
    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