Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The hinge region of the human estrogen receptor determines functional synergy between AF-1 and AF-2 in the quantitative response to estradiol and tamoxifen

24 Mar 2010

Abstract excerpt

Human estrogen receptors alpha and beta (ERalpha and ERbeta) greatly differ in their target genes, transcriptional potency and cofactor-binding capacity, and are differentially expressed in various tissues. In classical estrogen response element (ERE)-mediated transactivation, ERbeta has a markedly reduced activation potential compared with ERalpha; the mechanism underlying this difference is unclear. Here, we...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Estrogen and related hormone effects
Share to Inflammatory mediators and NSAID effects
Share to Receptor Mechanisms and Signaling

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 20332105
DOI: 10.1242/jcs.061135

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The hinge region of the human estrogen receptor determines functional synergy between AF-1 and AF-2 in the quantitative response to estradiol and tamoxifenPMID 20332105Read ↗

The Estrogen Receptor β-Isoform (ERβ) of the Human Estrogen Receptor Modulates ERα Transcriptional Activity and Is a Key Regulator of the Cellular Response to Estrogens and Antiestrogens1Semantic proximity Read ↗

p300 mediates functional synergism between AF-1 and AF-2 of estrogen receptor alpha and beta by interacting directly with the N-terminal A/B domains.Semantic proximity Read ↗

The interaction between AF-1 and AF-2 in the two human estrogen receptorsSemantic proximity Read ↗

The estrogen receptor enhances AP-1 activity by two distinct mechanisms with different requirements for receptor transactivation functions.Semantic proximity Read ↗

The Estrogen Receptor -Isoform (ER ) of the Human Estrogen Receptor Modulates ER Transcriptional Activity and Is a Key Regulator of the Cellular Response to Estrogens and AntiestrogensSemantic proximity Read ↗

Synergism between ERalpha transactivation function 1 (AF-1) and AF-2 mediated by steroid receptor coactivator protein-1: requirement for the AF-1 alpha-helical core and for a direct interaction between the N- and C-terminal domains.Semantic proximity Read ↗

Estrogen Signaling: A Subtle Balance Between ER and ERSemantic proximity Read ↗

An antiestrogen-responsive estrogen receptor-alpha mutant (D351Y) shows weak AF-2 activity in the presence of tamoxifen.Semantic proximity Read ↗

Estrogen receptor (ER)-β isoforms: A key to understanding ER-β signalingSemantic proximity Read ↗

Identification of Regions within the F Domain of the Human Estrogen Receptor α that Are Important for Modulating Transactivation and Protein-Protein InteractionsSemantic proximity Read ↗

Estrogen receptor beta: an overview and update.Semantic proximity Read ↗

Enhancement of estrogen receptor transcriptional activity by the coactivator GRIP-1 highlights the role of activation function 2 in determining estrogen receptor pharmacology.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.