Component

Myricetin 3′-O-sulfate

Context-specific entity; species, compartment and exposure are stated on each claim.

10 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. The sulfate bound human serum albumin with high affinity and moderately displaced the Site I marker warfarin in vitro.

    Myricetin 3′-O-sulfate → Human serum albumin source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Albumin fluorescence and ultrafiltration assays.
    limitations
    Not demonstrated displacement toxicity or a change in patient anticoagulation.
    nutrient_topic
    Myricetin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Myricetin
    plain_language
    Carrier binding changes the freely available fraction.
    primary_references
    Interaction of myricetin, ampelopsin (dihydromyricetin), and their sulfate metabolites with serum albumin, cytochrome P450 (CYP2C9, 2C19, and 3A4) enzymes, and organic anion-transporting polypeptides (OATP1B1 and OATP2B1). · 2024 · https://pubmed.ncbi.nlm.nih.gov/39344282/ · DOI 10.1002/prp2.70021

    Myricetin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 172–178

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Albumin fluorescence and ultrafiltration assays. · source_derived_draft · unverified_draft

    ## myricetin-sulfate-albumin Carrier binding changes the freely available fraction. The sulfate bound human serum albumin with high affinity and moderately displaced the Site I marker warfarin in vitro. Model: Albumin fluorescence and ultrafiltration assays. Limitations: Not demonstrated displacement toxicity or a change in patient anticoagulation. Evidence access: Primary full text Interaction of myricetin, ampelopsin (dihydromyricetin), and their sulfate metabolites with serum albumin, cytochrome P450 (CYP2C9, 2C19, and 3A4) enzymes, and organic anion-transporting polypeptides (OATP1B1 and OATP2B1). · 2024 · https://pubmed.ncbi.nlm.nih.gov/39344282/ · DOI 10.1002/prp2.70021
    Complete structured claim and evidence

  2. At 20 micromolar, the sulfate did not significantly inhibit mephenytoin hydroxylation in the human CYP2C19 assay.

    Myricetin 3′-O-sulfate → Human cytochrome P450 2C19 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Recombinant human enzymes; 5 micromolar substrate.
    limitations
    Restricted substrate, concentration and preparation; earlier CYP2C9 assays gave different potency.
    nutrient_topic
    Myricetin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Myricetin
    plain_language
    A transporter interaction does not imply strong CYP inhibition.
    primary_references
    Interaction of myricetin, ampelopsin (dihydromyricetin), and their sulfate metabolites with serum albumin, cytochrome P450 (CYP2C9, 2C19, and 3A4) enzymes, and organic anion-transporting polypeptides (OATP1B1 and OATP2B1). · 2024 · https://pubmed.ncbi.nlm.nih.gov/39344282/ · DOI 10.1002/prp2.70021

    Myricetin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 188–194

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant human enzymes; 5 micromolar substrate. · source_derived_draft · unverified_draft

    ## myricetin-sulfate-cyp2c19 A transporter interaction does not imply strong CYP inhibition. At 20 micromolar, the sulfate did not significantly inhibit mephenytoin hydroxylation in the human CYP2C19 assay. Model: Recombinant human enzymes; 5 micromolar substrate. Limitations: Restricted substrate, concentration and preparation; earlier CYP2C9 assays gave different potency. Evidence access: Primary full text Interaction of myricetin, ampelopsin (dihydromyricetin), and their sulfate metabolites with serum albumin, cytochrome P450 (CYP2C9, 2C19, and 3A4) enzymes, and organic anion-transporting polypeptides (OATP1B1 and OATP2B1). · 2024 · https://pubmed.ncbi.nlm.nih.gov/39344282/ · DOI 10.1002/prp2.70021
    Complete structured claim and evidence

  3. At 20 micromolar, the sulfate did not inhibit diclofenac hydroxylation in the human CYP2C9 assay.

    Myricetin 3′-O-sulfate → Human cytochrome P450 2C9 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Recombinant human enzymes; 5 micromolar substrate.
    limitations
    Restricted substrate, concentration and preparation; earlier CYP2C9 assays gave different potency.
    nutrient_topic
    Myricetin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Myricetin
    plain_language
    A transporter interaction does not imply strong CYP inhibition.
    primary_references
    Interaction of myricetin, ampelopsin (dihydromyricetin), and their sulfate metabolites with serum albumin, cytochrome P450 (CYP2C9, 2C19, and 3A4) enzymes, and organic anion-transporting polypeptides (OATP1B1 and OATP2B1). · 2024 · https://pubmed.ncbi.nlm.nih.gov/39344282/ · DOI 10.1002/prp2.70021

    Myricetin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 180–186

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant human enzymes; 5 micromolar substrate. · source_derived_draft · unverified_draft

    ## myricetin-sulfate-cyp2c9 A transporter interaction does not imply strong CYP inhibition. At 20 micromolar, the sulfate did not inhibit diclofenac hydroxylation in the human CYP2C9 assay. Model: Recombinant human enzymes; 5 micromolar substrate. Limitations: Restricted substrate, concentration and preparation; earlier CYP2C9 assays gave different potency. Evidence access: Primary full text Interaction of myricetin, ampelopsin (dihydromyricetin), and their sulfate metabolites with serum albumin, cytochrome P450 (CYP2C9, 2C19, and 3A4) enzymes, and organic anion-transporting polypeptides (OATP1B1 and OATP2B1). · 2024 · https://pubmed.ncbi.nlm.nih.gov/39344282/ · DOI 10.1002/prp2.70021
    Complete structured claim and evidence

  4. At 20 micromolar, the sulfate reduced testosterone hydroxylation by less than 10% in the human CYP3A4 assay.

    Myricetin 3′-O-sulfate → Human cytochrome P450 3A4 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Recombinant human enzymes; 5 micromolar substrate.
    limitations
    Restricted substrate, concentration and preparation; earlier CYP2C9 assays gave different potency.
    nutrient_topic
    Myricetin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Myricetin
    plain_language
    A transporter interaction does not imply strong CYP inhibition.
    primary_references
    Interaction of myricetin, ampelopsin (dihydromyricetin), and their sulfate metabolites with serum albumin, cytochrome P450 (CYP2C9, 2C19, and 3A4) enzymes, and organic anion-transporting polypeptides (OATP1B1 and OATP2B1). · 2024 · https://pubmed.ncbi.nlm.nih.gov/39344282/ · DOI 10.1002/prp2.70021

    Myricetin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 196–202

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant human enzymes; 5 micromolar substrate. · source_derived_draft · unverified_draft

    ## myricetin-sulfate-cyp3a4 A transporter interaction does not imply strong CYP inhibition. At 20 micromolar, the sulfate reduced testosterone hydroxylation by less than 10% in the human CYP3A4 assay. Model: Recombinant human enzymes; 5 micromolar substrate. Limitations: Restricted substrate, concentration and preparation; earlier CYP2C9 assays gave different potency. Evidence access: Primary full text Interaction of myricetin, ampelopsin (dihydromyricetin), and their sulfate metabolites with serum albumin, cytochrome P450 (CYP2C9, 2C19, and 3A4) enzymes, and organic anion-transporting polypeptides (OATP1B1 and OATP2B1). · 2024 · https://pubmed.ncbi.nlm.nih.gov/39344282/ · DOI 10.1002/prp2.70021
    Complete structured claim and evidence

  5. The sulfate inhibited human SLCO1B1 transport in vitro, IC50 1.7 micromolar.

    Myricetin 3′-O-sulfate → Human OATP1B1 / SLCO1B1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Human transporter-overexpressing cells.
    limitations
    Probe-substrate potency is not a measured clinical drug interaction.
    nutrient_topic
    Myricetin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Myricetin
    plain_language
    Transport competition can depend on the metabolite.
    primary_references
    Interaction of myricetin, ampelopsin (dihydromyricetin), and their sulfate metabolites with serum albumin, cytochrome P450 (CYP2C9, 2C19, and 3A4) enzymes, and organic anion-transporting polypeptides (OATP1B1 and OATP2B1). · 2024 · https://pubmed.ncbi.nlm.nih.gov/39344282/ · DOI 10.1002/prp2.70021

    Myricetin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 156–162

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human transporter-overexpressing cells. · source_derived_draft · unverified_draft

    ## myricetin-sulfate-slco1b1 Transport competition can depend on the metabolite. The sulfate inhibited human SLCO1B1 transport in vitro, IC50 1.7 micromolar. Model: Human transporter-overexpressing cells. Limitations: Probe-substrate potency is not a measured clinical drug interaction. Evidence access: Primary full text Interaction of myricetin, ampelopsin (dihydromyricetin), and their sulfate metabolites with serum albumin, cytochrome P450 (CYP2C9, 2C19, and 3A4) enzymes, and organic anion-transporting polypeptides (OATP1B1 and OATP2B1). · 2024 · https://pubmed.ncbi.nlm.nih.gov/39344282/ · DOI 10.1002/prp2.70021
    Complete structured claim and evidence

  6. The sulfate inhibited human SLCO2B1 transport in vitro, IC50 0.3 micromolar.

    Myricetin 3′-O-sulfate → Human organic anion transporting polypeptide 2B1 / SLCO2B1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Human transporter-overexpressing cells.
    limitations
    Probe-substrate potency is not a measured clinical drug interaction.
    nutrient_topic
    Myricetin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Myricetin
    plain_language
    Transport competition can depend on the metabolite.
    primary_references
    Interaction of myricetin, ampelopsin (dihydromyricetin), and their sulfate metabolites with serum albumin, cytochrome P450 (CYP2C9, 2C19, and 3A4) enzymes, and organic anion-transporting polypeptides (OATP1B1 and OATP2B1). · 2024 · https://pubmed.ncbi.nlm.nih.gov/39344282/ · DOI 10.1002/prp2.70021

    Myricetin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 164–170

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human transporter-overexpressing cells. · source_derived_draft · unverified_draft

    ## myricetin-sulfate-slco2b1 Transport competition can depend on the metabolite. The sulfate inhibited human SLCO2B1 transport in vitro, IC50 0.3 micromolar. Model: Human transporter-overexpressing cells. Limitations: Probe-substrate potency is not a measured clinical drug interaction. Evidence access: Primary full text Interaction of myricetin, ampelopsin (dihydromyricetin), and their sulfate metabolites with serum albumin, cytochrome P450 (CYP2C9, 2C19, and 3A4) enzymes, and organic anion-transporting polypeptides (OATP1B1 and OATP2B1). · 2024 · https://pubmed.ncbi.nlm.nih.gov/39344282/ · DOI 10.1002/prp2.70021
    Complete structured claim and evidence

  7. Myricetin 3′-O-sulfate inhibited bovine-milk xanthine oxidase-mediated 6-mercaptopurine oxidation.

    Myricetin 3′-O-sulfate → Bovine xanthine oxidoreductase / XDH source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract and repository full-text methods
    experimental_model
    Purified bovine-milk enzyme, chromatographic product analysis.
    limitations
    Sulfate was more potent than parent in the study. Not demonstrated human urate lowering or thiopurine toxicity.
    nutrient_topic
    Myricetin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Myricetin
    plain_language
    One enzyme processes both a natural purine and a medication.
    primary_references
    Inhibition of xanthine oxidase-catalyzed xanthine and 6-mercaptopurine oxidation by luteolin, naringenin, myricetin, ampelopsin and their conjugated metabolites. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37734263/ · DOI 10.1016/j.biopha.2023.115548

    Myricetin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 412–418

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified bovine-milk enzyme, chromatographic product analysis. · source_derived_draft · unverified_draft

    ## myricetin-xo-sulfate-6-mercaptopurine One enzyme processes both a natural purine and a medication. Myricetin 3′-O-sulfate inhibited bovine-milk xanthine oxidase-mediated 6-mercaptopurine oxidation. Model: Purified bovine-milk enzyme, chromatographic product analysis. Limitations: Sulfate was more potent than parent in the study. Not demonstrated human urate lowering or thiopurine toxicity. Evidence access: Primary abstract and repository full-text methods Inhibition of xanthine oxidase-catalyzed xanthine and 6-mercaptopurine oxidation by luteolin, naringenin, myricetin, ampelopsin and their conjugated metabolites. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37734263/ · DOI 10.1016/j.biopha.2023.115548
    Complete structured claim and evidence

  8. Myricetin 3′-O-sulfate inhibited bovine-milk xanthine oxidase-mediated xanthine oxidation.

    Myricetin 3′-O-sulfate → Bovine xanthine oxidoreductase / XDH source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract and repository full-text methods
    experimental_model
    Purified bovine-milk enzyme, chromatographic product analysis.
    limitations
    Sulfate was more potent than parent in the study. Not demonstrated human urate lowering or thiopurine toxicity.
    nutrient_topic
    Myricetin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Myricetin
    plain_language
    One enzyme processes both a natural purine and a medication.
    primary_references
    Inhibition of xanthine oxidase-catalyzed xanthine and 6-mercaptopurine oxidation by luteolin, naringenin, myricetin, ampelopsin and their conjugated metabolites. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37734263/ · DOI 10.1016/j.biopha.2023.115548

    Myricetin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 404–410

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified bovine-milk enzyme, chromatographic product analysis. · source_derived_draft · unverified_draft

    ## myricetin-xo-sulfate-xanthine One enzyme processes both a natural purine and a medication. Myricetin 3′-O-sulfate inhibited bovine-milk xanthine oxidase-mediated xanthine oxidation. Model: Purified bovine-milk enzyme, chromatographic product analysis. Limitations: Sulfate was more potent than parent in the study. Not demonstrated human urate lowering or thiopurine toxicity. Evidence access: Primary abstract and repository full-text methods Inhibition of xanthine oxidase-catalyzed xanthine and 6-mercaptopurine oxidation by luteolin, naringenin, myricetin, ampelopsin and their conjugated metabolites. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37734263/ · DOI 10.1016/j.biopha.2023.115548
    Complete structured claim and evidence

What acts on it

  1. Myricetin 3′-O-sulfate was a substrate of human SLCO1B1.

    Human OATP1B1 / SLCO1B1 → Myricetin 3′-O-sulfate source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Overexpressing-cell uptake with flavonoid fluorescence method.
    limitations
    Not a quantified human tissue delivery rate.
    nutrient_topic
    Myricetin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Myricetin
    plain_language
    The sulfate is transported, not simply inactive waste.
    primary_references
    Interaction of myricetin, ampelopsin (dihydromyricetin), and their sulfate metabolites with serum albumin, cytochrome P450 (CYP2C9, 2C19, and 3A4) enzymes, and organic anion-transporting polypeptides (OATP1B1 and OATP2B1). · 2024 · https://pubmed.ncbi.nlm.nih.gov/39344282/ · DOI 10.1002/prp2.70021
    transport_effect
    raises Recorded as a substrate in the OATP1B1 uptake assay.
    transport_pool
    the hepatocyte-model cell in the uptake assay Recorded as a substrate in the OATP1B1 uptake assay.

    Myricetin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 204–210

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Overexpressing-cell uptake with flavonoid fluorescence method. · source_derived_draft · unverified_draft

    ## myricetin-sulfate-uptake-slco1b1 The sulfate is transported, not simply inactive waste. Myricetin 3′-O-sulfate was a substrate of human SLCO1B1. Model: Overexpressing-cell uptake with flavonoid fluorescence method. Limitations: Not a quantified human tissue delivery rate. Evidence access: Primary full text Interaction of myricetin, ampelopsin (dihydromyricetin), and their sulfate metabolites with serum albumin, cytochrome P450 (CYP2C9, 2C19, and 3A4) enzymes, and organic anion-transporting polypeptides (OATP1B1 and OATP2B1). · 2024 · https://pubmed.ncbi.nlm.nih.gov/39344282/ · DOI 10.1002/prp2.70021
    Complete structured claim and evidence

  2. Myricetin 3′-O-sulfate was a substrate of human SLCO2B1.

    Human organic anion transporting polypeptide 2B1 / SLCO2B1 → Myricetin 3′-O-sulfate source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Overexpressing-cell uptake with flavonoid fluorescence method.
    limitations
    Not a quantified human tissue delivery rate.
    nutrient_topic
    Myricetin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Myricetin
    plain_language
    The sulfate is transported, not simply inactive waste.
    primary_references
    Interaction of myricetin, ampelopsin (dihydromyricetin), and their sulfate metabolites with serum albumin, cytochrome P450 (CYP2C9, 2C19, and 3A4) enzymes, and organic anion-transporting polypeptides (OATP1B1 and OATP2B1). · 2024 · https://pubmed.ncbi.nlm.nih.gov/39344282/ · DOI 10.1002/prp2.70021
    transport_effect
    raises Recorded as a substrate in the OATP2B1 uptake assay.
    transport_pool
    the expressing cell Recorded as a substrate in the OATP2B1 uptake assay.

    Myricetin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 212–218

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Overexpressing-cell uptake with flavonoid fluorescence method. · source_derived_draft · unverified_draft

    ## myricetin-sulfate-uptake-slco2b1 The sulfate is transported, not simply inactive waste. Myricetin 3′-O-sulfate was a substrate of human SLCO2B1. Model: Overexpressing-cell uptake with flavonoid fluorescence method. Limitations: Not a quantified human tissue delivery rate. Evidence access: Primary full text Interaction of myricetin, ampelopsin (dihydromyricetin), and their sulfate metabolites with serum albumin, cytochrome P450 (CYP2C9, 2C19, and 3A4) enzymes, and organic anion-transporting polypeptides (OATP1B1 and OATP2B1). · 2024 · https://pubmed.ncbi.nlm.nih.gov/39344282/ · DOI 10.1002/prp2.70021
    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