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

Role for Hsp90-associated cochaperone p23 in estrogen receptor signal transduction.

Molecular and cellular biology - 1 May 1999

Knoblauch R, Garabedian M J

Abstract excerpt

The mechanism of signal transduction by the estrogen receptor (ER) is complex and not fully understood. In addition to the ER, a number of accessory proteins are apparently required to efficiently transduce the steroid hormone signal. In the absence of estradiol, the ER, like other steroid receptors, is complexed with Hsp90 and other molecular chaperone components, including an immunophilin, and p23. This...

Read the complete abstract on PubMed

Topics

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

Share to Estradiol
Share to Fluorescent Antibody Technique
Share to HSP90 Heat-Shock Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Luminescent Proteins

Share to Molecular Chaperones

Share to Receptors, Estrogen

Share to Suppression, Genetic

Share to Transcriptional Activation

Source

Open in PubMed Open full text

Identifiers

PMID: 10207098
DOI: 10.1128/MCB.19.5.3748
PMCID: PMC84199

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Role for Hsp90-associated cochaperone p23 in estrogen receptor signal transduction.PMID 10207098Read ↗

Genetic dissection of p23, an Hsp90 cochaperone, reveals a distinct surface involved in estrogen receptor signaling.Semantic proximity Read ↗

Genetic and biochemical analysis of p23 and ansamycin antibiotics in the function of Hsp90-dependent signaling proteins.Semantic proximity Read ↗

Cooperation of heat shock protein 90 and p23 in aryl hydrocarbon receptor signaling.Semantic proximity Read ↗

Estrogen receptor variants ERdelta5 and ERdelta7 down-regulate wild-type estrogen receptor activity.Semantic proximity Read ↗

Coupling endoplasmic reticulum stress to the cell-death program: a novel HSP90-independent role for the small chaperone protein p23.Semantic proximity Read ↗

High level expression of biologically active estrogen receptor in Saccharomyces cerevisiae.Semantic proximity Read ↗

Functional analysis of the human estrogen receptor using a phenotypic transactivation assay in yeast.Semantic proximity Read ↗

A role for the Hsp40 Ydj1 in repression of basal steroid receptor activity in yeast.Semantic proximity Read ↗

Non-canonical role of wild-type SEC23B in the cellular stress response pathway.Semantic proximity Read ↗

Targeted protein destabilization reveals an estrogen-mediated ER stress responseSemantic proximity Read ↗

Helix 12 in the human estrogen receptor (hER) is essential for the hER function by overcoming nucleosome repression in yeast.Semantic proximity Read ↗

Probing the structure and function of the estrogen receptor ligand binding domain by analysis of mutants with altered transactivation characteristics.Semantic proximity Read ↗

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