Component

Human SGLT2-MAP17 transporter complex

Species, preparation, dose and limitations are retained on linked claims.

1 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

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. Cryo-EM placed phlorizin in an inward-facing human SGLT2-MAP17 complex, and biphasic kinetics suggested access from extracellular and intracellular sides.

    Phlorizin → Human SGLT2-MAP17 transporter complex source_derived_draftungraded
    Experimental context and source evidence
    dose
    Phlorizin and comparator synthetic inhibitors
    duration
    Acute
    evidence_access
    Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    evidence_scope
    literature_reviewed; model-specific source-derived curation
    experimental_model
    Purified human SGLT2-MAP17 complex
    limitations
    A bound structure explains inhibition but does not establish human pharmacokinetics; synthetic inhibitors used different outward-facing poses.
    nutrient_topic
    Phlorizin chapter; interacting nutrients, drugs, peptides and proteins retain their experimental settings. · Phlorizin
    organism
    Purified human SGLT2-MAP17 complex
    plain_language
    Cryo-EM placed phlorizin in an inward-facing human SGLT2-MAP17 complex, and biphasic kinetics suggested access from extracellular and intracellular sides.
    primary_references
    Transport and inhibition mechanism of the human SGLT2-MAP17 glucose transporter. (2024). https://pubmed.ncbi.nlm.nih.gov/38057552/ DOI: 10.1038/s41594-023-01134-0
    route
    Cell-free structural and transport analysis
    tissue
    Cryo-EM structures and inhibitor kinetics

    Phlorizin: mechanism of action and interactions (2026-09-20) · lines 33–42

    Original AI-assisted source-specific curation with primary-study citations, model, exposure, route, duration, negative findings and limitations preserved. Not publisher full text. · supports · Purified human SGLT2-MAP17 complex · source_derived_draft · unverified_draft

    ## phlorizin-sglt2-structure Cryo-EM placed phlorizin in an inward-facing human SGLT2-MAP17 complex, and biphasic kinetics suggested access from extracellular and intracellular sides. Model/species: Purified human SGLT2-MAP17 complex Tissue/system: Cryo-EM structures and inhibitor kinetics Exposure: Phlorizin and comparator synthetic inhibitors Route: Cell-free structural and transport analysis Duration: Acute Limits: A bound structure explains inhibition but does not establish human pharmacokinetics; synthetic inhibitors used different outward-facing poses. Primary reference: Transport and inhibition mechanism of the human SGLT2-MAP17 glucose transporter. (2024). https://pubmed.ncbi.nlm.nih.gov/38057552/ DOI: 10.1038/s41594-023-01134-0 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    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