Component

Ondansetron

Ondansetron. Species, exposure and limitations are retained in each linked claim.

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 acts on it

  1. CYP1A1 contributed to ondansetron metabolism in the studied human systems.

    Human cytochrome P450 1A1 → Ondansetron source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/dim-research/8591723.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "04a615c551d95089eb1a966d88d8be011687d658f383e81af5b651845427b66e", "start_char": 0, "end_char": 1460, "text_sha256": "04a615c551d95089eb1a966d88d8be011687d658f383e81af5b651845427b66e"}
    experimental_model
    Human microsomes and individually expressed enzymes
    exposure
    Enzyme-specific inhibitors and radiolabeled substrate
    limitations
    CYP3A is identified at subfamily level, without an exclusive isoform assignment. Multiple CYP pathways contribute; no DIM coadministration or clinically measured DIM effect.
    nutrient_topic
    Diindolylmethane (DIM) research collection; topical membership is not evidence of a direct dietary effect. · 3,3'-Diindolylmethane / DIM
    organism
    Human CYP systems
    plain_language
    A substrate list alone omits other routes that can limit a single-enzyme interaction.
    primary_references
    [dim-p8591723] Multiple forms of cytochrome P450 are involved in the metabolism of ondansetron in humans. (1995). https://pubmed.ncbi.nlm.nih.gov/8591723/ DOI: 10.1016/s0090-9556(25)06820-5
    tissue_or_cell_type
    Ondansetron oxidation

    Diindolylmethane (DIM): formation, receptor signaling, metabolism and drug interactions (2026-09-17) · lines 935–946

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human microsomes and individually expressed enzymes · source_derived_draft · unverified_draft

    ### dim-ondansetron-cyp1a1 CYP1A1 contributed to ondansetron metabolism in the studied human systems. Condition category: normal nutrient_topic: Diindolylmethane (DIM) research collection; topical membership is not evidence of a direct dietary effect. plain_language: A substrate list alone omits other routes that can limit a single-enzyme interaction. organism: Human CYP systems tissue_or_cell_type: Ondansetron oxidation experimental_model: Human microsomes and individually expressed enzymes limitations: CYP3A is identified at subfamily level, without an exclusive isoform assignment. Multiple CYP pathways contribute; no DIM coadministration or clinically measured DIM effect. exposure: Enzyme-specific inhibitors and radiolabeled substrate evidence_span: {"source_cache": "artifacts/dim-research/8591723.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "04a615c551d95089eb1a966d88d8be011687d658f383e81af5b651845427b66e", "start_char": 0, "end_char": 1460, "text_sha256": "04a615c551d95089eb1a966d88d8be011687d658f383e81af5b651845427b66e"} [dim-p8591723] Multiple forms of cytochrome P450 are involved in the metabolism of ondansetron in humans. (1995). https://pubmed.ncbi.nlm.nih.gov/8591723/ DOI: 10.1016/s0090-9556(25)06820-5
    Complete structured claim and evidence

  2. CYP1A2 contributed to ondansetron metabolism in the studied human systems.

    Human cytochrome P450 1A2 → Ondansetron source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/dim-research/8591723.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "04a615c551d95089eb1a966d88d8be011687d658f383e81af5b651845427b66e", "start_char": 0, "end_char": 1460, "text_sha256": "04a615c551d95089eb1a966d88d8be011687d658f383e81af5b651845427b66e"}
    experimental_model
    Human microsomes and individually expressed enzymes
    exposure
    Enzyme-specific inhibitors and radiolabeled substrate
    limitations
    CYP3A is identified at subfamily level, without an exclusive isoform assignment. Multiple CYP pathways contribute; no DIM coadministration or clinically measured DIM effect.
    nutrient_topic
    Diindolylmethane (DIM) research collection; topical membership is not evidence of a direct dietary effect. · 3,3'-Diindolylmethane / DIM
    organism
    Human CYP systems
    plain_language
    A substrate list alone omits other routes that can limit a single-enzyme interaction.
    primary_references
    [dim-p8591723] Multiple forms of cytochrome P450 are involved in the metabolism of ondansetron in humans. (1995). https://pubmed.ncbi.nlm.nih.gov/8591723/ DOI: 10.1016/s0090-9556(25)06820-5
    tissue_or_cell_type
    Ondansetron oxidation

    Diindolylmethane (DIM): formation, receptor signaling, metabolism and drug interactions (2026-09-17) · lines 948–959

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human microsomes and individually expressed enzymes · source_derived_draft · unverified_draft

    ### dim-ondansetron-cyp1a2 CYP1A2 contributed to ondansetron metabolism in the studied human systems. Condition category: normal nutrient_topic: Diindolylmethane (DIM) research collection; topical membership is not evidence of a direct dietary effect. plain_language: A substrate list alone omits other routes that can limit a single-enzyme interaction. organism: Human CYP systems tissue_or_cell_type: Ondansetron oxidation experimental_model: Human microsomes and individually expressed enzymes limitations: CYP3A is identified at subfamily level, without an exclusive isoform assignment. Multiple CYP pathways contribute; no DIM coadministration or clinically measured DIM effect. exposure: Enzyme-specific inhibitors and radiolabeled substrate evidence_span: {"source_cache": "artifacts/dim-research/8591723.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "04a615c551d95089eb1a966d88d8be011687d658f383e81af5b651845427b66e", "start_char": 0, "end_char": 1460, "text_sha256": "04a615c551d95089eb1a966d88d8be011687d658f383e81af5b651845427b66e"} [dim-p8591723] Multiple forms of cytochrome P450 are involved in the metabolism of ondansetron in humans. (1995). https://pubmed.ncbi.nlm.nih.gov/8591723/ DOI: 10.1016/s0090-9556(25)06820-5
    Complete structured claim and evidence

  3. CYP2D6 contributed to ondansetron metabolism in the studied human systems.

    Human cytochrome P450 2D6 → Ondansetron source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/dim-research/8591723.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "04a615c551d95089eb1a966d88d8be011687d658f383e81af5b651845427b66e", "start_char": 0, "end_char": 1460, "text_sha256": "04a615c551d95089eb1a966d88d8be011687d658f383e81af5b651845427b66e"}
    experimental_model
    Human microsomes and individually expressed enzymes
    exposure
    Enzyme-specific inhibitors and radiolabeled substrate
    limitations
    CYP3A is identified at subfamily level, without an exclusive isoform assignment. Multiple CYP pathways contribute; no DIM coadministration or clinically measured DIM effect.
    nutrient_topic
    Diindolylmethane (DIM) research collection; topical membership is not evidence of a direct dietary effect. · 3,3'-Diindolylmethane / DIM
    organism
    Human CYP systems
    plain_language
    A substrate list alone omits other routes that can limit a single-enzyme interaction.
    primary_references
    [dim-p8591723] Multiple forms of cytochrome P450 are involved in the metabolism of ondansetron in humans. (1995). https://pubmed.ncbi.nlm.nih.gov/8591723/ DOI: 10.1016/s0090-9556(25)06820-5
    tissue_or_cell_type
    Ondansetron oxidation

    Diindolylmethane (DIM): formation, receptor signaling, metabolism and drug interactions (2026-09-17) · lines 961–972

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human microsomes and individually expressed enzymes · source_derived_draft · unverified_draft

    ### dim-ondansetron-cyp2d6 CYP2D6 contributed to ondansetron metabolism in the studied human systems. Condition category: normal nutrient_topic: Diindolylmethane (DIM) research collection; topical membership is not evidence of a direct dietary effect. plain_language: A substrate list alone omits other routes that can limit a single-enzyme interaction. organism: Human CYP systems tissue_or_cell_type: Ondansetron oxidation experimental_model: Human microsomes and individually expressed enzymes limitations: CYP3A is identified at subfamily level, without an exclusive isoform assignment. Multiple CYP pathways contribute; no DIM coadministration or clinically measured DIM effect. exposure: Enzyme-specific inhibitors and radiolabeled substrate evidence_span: {"source_cache": "artifacts/dim-research/8591723.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "04a615c551d95089eb1a966d88d8be011687d658f383e81af5b651845427b66e", "start_char": 0, "end_char": 1460, "text_sha256": "04a615c551d95089eb1a966d88d8be011687d658f383e81af5b651845427b66e"} [dim-p8591723] Multiple forms of cytochrome P450 are involved in the metabolism of ondansetron in humans. (1995). https://pubmed.ncbi.nlm.nih.gov/8591723/ DOI: 10.1016/s0090-9556(25)06820-5
    Complete structured claim and evidence

  4. The CYP3A subfamily contributed to ondansetron metabolism in the studied human systems.

    Human CYP3A subfamily, isoform unresolved → Ondansetron source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/dim-research/8591723.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "04a615c551d95089eb1a966d88d8be011687d658f383e81af5b651845427b66e", "start_char": 0, "end_char": 1460, "text_sha256": "04a615c551d95089eb1a966d88d8be011687d658f383e81af5b651845427b66e"}
    experimental_model
    Human microsomes and individually expressed enzymes
    exposure
    Enzyme-specific inhibitors and radiolabeled substrate
    limitations
    CYP3A is identified at subfamily level, without an exclusive isoform assignment. Multiple CYP pathways contribute; no DIM coadministration or clinically measured DIM effect.
    nutrient_topic
    Diindolylmethane (DIM) research collection; topical membership is not evidence of a direct dietary effect. · 3,3'-Diindolylmethane / DIM
    organism
    Human CYP systems
    plain_language
    A substrate list alone omits other routes that can limit a single-enzyme interaction.
    primary_references
    [dim-p8591723] Multiple forms of cytochrome P450 are involved in the metabolism of ondansetron in humans. (1995). https://pubmed.ncbi.nlm.nih.gov/8591723/ DOI: 10.1016/s0090-9556(25)06820-5
    tissue_or_cell_type
    Ondansetron oxidation

    Diindolylmethane (DIM): formation, receptor signaling, metabolism and drug interactions (2026-09-17) · lines 974–985

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human microsomes and individually expressed enzymes · source_derived_draft · unverified_draft

    ### dim-ondansetron-cyp3a-subfamily The CYP3A subfamily contributed to ondansetron metabolism in the studied human systems. Condition category: normal nutrient_topic: Diindolylmethane (DIM) research collection; topical membership is not evidence of a direct dietary effect. plain_language: A substrate list alone omits other routes that can limit a single-enzyme interaction. organism: Human CYP systems tissue_or_cell_type: Ondansetron oxidation experimental_model: Human microsomes and individually expressed enzymes limitations: CYP3A is identified at subfamily level, without an exclusive isoform assignment. Multiple CYP pathways contribute; no DIM coadministration or clinically measured DIM effect. exposure: Enzyme-specific inhibitors and radiolabeled substrate evidence_span: {"source_cache": "artifacts/dim-research/8591723.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "04a615c551d95089eb1a966d88d8be011687d658f383e81af5b651845427b66e", "start_char": 0, "end_char": 1460, "text_sha256": "04a615c551d95089eb1a966d88d8be011687d658f383e81af5b651845427b66e"} [dim-p8591723] Multiple forms of cytochrome P450 are involved in the metabolism of ondansetron in humans. (1995). https://pubmed.ncbi.nlm.nih.gov/8591723/ DOI: 10.1016/s0090-9556(25)06820-5
    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