Component

Human estrogen receptor beta / ESR2

Human estrogen receptor beta / ESR2. 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. DIM activated ERbeta target transcription without detectable binding to ERbeta in the study.

    3,3'-Diindolylmethane / DIM → Human estrogen receptor beta / ESR2 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/dim-research/20160136.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "558ee877330aede2675ccccdef5e31debf9824e00a1eaaacb1e7fe385d45b8e5", "start_char": 0, "end_char": 1134, "text_sha256": "558ee877330aede2675ccccdef5e31debf9824e00a1eaaacb1e7fe385d45b8e5"}
    experimental_model
    Reporter, binding, chromatin and coactivator-silencing assays
    exposure
    DIM and SRC-2 silencing
    limitations
    Subtype-selective response in this system; other studies find ERalpha responses under other hormonal and concentration conditions.
    nutrient_topic
    Diindolylmethane (DIM) research collection; topical membership is not evidence of a direct dietary effect. · 3,3'-Diindolylmethane / DIM
    organism
    Human receptor-expressing cell systems
    plain_language
    Receptor-dependent signaling need not mean that DIM directly occupies the hormone-binding site.
    primary_references
    [dim-p20160136] Selective activation of estrogen receptor-beta target genes by 3,3'-diindolylmethane. (2010). https://pubmed.ncbi.nlm.nih.gov/20160136/ DOI: 10.1210/en.2009-1028
    tissue_or_cell_type
    ERbeta transcription

    Diindolylmethane (DIM): formation, receptor signaling, metabolism and drug interactions (2026-09-17) · lines 571–582

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Reporter, binding, chromatin and coactivator-silencing assays · source_derived_draft · unverified_draft

    ### dim-erbeta-activation DIM activated ERbeta target transcription without detectable binding to ERbeta in the study. Condition category: normal nutrient_topic: Diindolylmethane (DIM) research collection; topical membership is not evidence of a direct dietary effect. plain_language: Receptor-dependent signaling need not mean that DIM directly occupies the hormone-binding site. organism: Human receptor-expressing cell systems tissue_or_cell_type: ERbeta transcription experimental_model: Reporter, binding, chromatin and coactivator-silencing assays limitations: Subtype-selective response in this system; other studies find ERalpha responses under other hormonal and concentration conditions. exposure: DIM and SRC-2 silencing evidence_span: {"source_cache": "artifacts/dim-research/20160136.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "558ee877330aede2675ccccdef5e31debf9824e00a1eaaacb1e7fe385d45b8e5", "start_char": 0, "end_char": 1134, "text_sha256": "558ee877330aede2675ccccdef5e31debf9824e00a1eaaacb1e7fe385d45b8e5"} [dim-p20160136] Selective activation of estrogen receptor-beta target genes by 3,3'-diindolylmethane. (2010). https://pubmed.ncbi.nlm.nih.gov/20160136/ DOI: 10.1210/en.2009-1028
    Complete structured claim and evidence

  2. Resveratrol acted as an estrogen agonist in ERalpha/ERbeta reporter systems; selected ERE sequences also showed estradiol antagonism with ERalpha but not ERbeta.

    trans-Resveratrol → Human estrogen receptor beta / ESR2 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Transfected CHO-K1 reporter cells.
    limitations
    Normal experimental context dependence, not an unresolved contradiction.
    nutrient_topic
    Resveratrol collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Resveratrol
    plain_language
    Direction depends on receptor and gene-control sequence.
    primary_references
    Resveratrol acts as a mixed agonist/antagonist for estrogen receptors alpha and beta. · 2000 · https://pubmed.ncbi.nlm.nih.gov/11014220/ · DOI 10.1210/endo.141.10.7721

    Resveratrol: metabolites, target selectivity and cross-nutrient mechanisms (2026-09-19) · lines 406–412

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Transfected CHO-K1 reporter cells. · source_derived_draft · unverified_draft

    ## resveratrol-er-sequence Direction depends on receptor and gene-control sequence. Resveratrol acted as an estrogen agonist in ERalpha/ERbeta reporter systems; selected ERE sequences also showed estradiol antagonism with ERalpha but not ERbeta. Model: Transfected CHO-K1 reporter cells. Limitations: Normal experimental context dependence, not an unresolved contradiction. Evidence access: Primary abstract Resveratrol acts as a mixed agonist/antagonist for estrogen receptors alpha and beta. · 2000 · https://pubmed.ncbi.nlm.nih.gov/11014220/ · DOI 10.1210/endo.141.10.7721
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. DIM promoted ERbeta recruitment of SRC-2 at regulatory elements; SRC-2 silencing inhibited target-gene activation.

    3,3'-Diindolylmethane / DIM → Nuclear receptor coactivator 2 / TIF2 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/dim-research/20160136.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "558ee877330aede2675ccccdef5e31debf9824e00a1eaaacb1e7fe385d45b8e5", "start_char": 0, "end_char": 1134, "text_sha256": "558ee877330aede2675ccccdef5e31debf9824e00a1eaaacb1e7fe385d45b8e5"}
    experimental_model
    Reporter, binding, chromatin and coactivator-silencing assays
    exposure
    DIM and SRC-2 silencing
    limitations
    Subtype-selective response in this system; other studies find ERalpha responses under other hormonal and concentration conditions.
    nutrient_topic
    Diindolylmethane (DIM) research collection; topical membership is not evidence of a direct dietary effect. · 3,3'-Diindolylmethane / DIM
    organism
    Human receptor-expressing cell systems
    plain_language
    A separate coactivator was required for the transcriptional response.
    primary_references
    [dim-p20160136] Selective activation of estrogen receptor-beta target genes by 3,3'-diindolylmethane. (2010). https://pubmed.ncbi.nlm.nih.gov/20160136/ DOI: 10.1210/en.2009-1028
    tissue_or_cell_type
    ERbeta transcription

    Diindolylmethane (DIM): formation, receptor signaling, metabolism and drug interactions (2026-09-17) · lines 584–595

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Reporter, binding, chromatin and coactivator-silencing assays · source_derived_draft · unverified_draft

    ### dim-src2-recruitment DIM promoted ERbeta recruitment of SRC-2 at regulatory elements; SRC-2 silencing inhibited target-gene activation. Condition category: normal nutrient_topic: Diindolylmethane (DIM) research collection; topical membership is not evidence of a direct dietary effect. plain_language: A separate coactivator was required for the transcriptional response. organism: Human receptor-expressing cell systems tissue_or_cell_type: ERbeta transcription experimental_model: Reporter, binding, chromatin and coactivator-silencing assays limitations: Subtype-selective response in this system; other studies find ERalpha responses under other hormonal and concentration conditions. exposure: DIM and SRC-2 silencing evidence_span: {"source_cache": "artifacts/dim-research/20160136.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "558ee877330aede2675ccccdef5e31debf9824e00a1eaaacb1e7fe385d45b8e5", "start_char": 0, "end_char": 1134, "text_sha256": "558ee877330aede2675ccccdef5e31debf9824e00a1eaaacb1e7fe385d45b8e5"} [dim-p20160136] Selective activation of estrogen receptor-beta target genes by 3,3'-diindolylmethane. (2010). https://pubmed.ncbi.nlm.nih.gov/20160136/ DOI: 10.1210/en.2009-1028
    Complete structured claim and evidence

  2. Resveratrol bound ERalpha and ERbeta with comparable affinity, approximately 7,000-fold weaker than estradiol in the reported assays.

    trans-Resveratrol → Human estrogen receptor alpha / ESR1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Receptor binding and CHO-K1 reporter experiments.
    limitations
    No demonstrated hormone normalization in humans.
    nutrient_topic
    Resveratrol collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Resveratrol
    plain_language
    It can interact with hormone receptors, but weak affinity matters.
    primary_references
    Resveratrol acts as a mixed agonist/antagonist for estrogen receptors alpha and beta. · 2000 · https://pubmed.ncbi.nlm.nih.gov/11014220/ · DOI 10.1210/endo.141.10.7721

    Resveratrol: metabolites, target selectivity and cross-nutrient mechanisms (2026-09-19) · lines 398–404

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Receptor binding and CHO-K1 reporter experiments. · source_derived_draft · unverified_draft

    ## resveratrol-er-binding It can interact with hormone receptors, but weak affinity matters. Resveratrol bound ERalpha and ERbeta with comparable affinity, approximately 7,000-fold weaker than estradiol in the reported assays. Model: Receptor binding and CHO-K1 reporter experiments. Limitations: No demonstrated hormone normalization in humans. Evidence access: Primary abstract Resveratrol acts as a mixed agonist/antagonist for estrogen receptors alpha and beta. · 2000 · https://pubmed.ncbi.nlm.nih.gov/11014220/ · DOI 10.1210/endo.141.10.7721
    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