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

Specificity of ligand-dependent androgen receptor stabilization: receptor domain interactions influence ligand dissociation and receptor stability.

1 Feb 1995

Abstract excerpt

The molecular basis for the different physiological effects of testosterone (T) and dihydrotestosterone (DHT) was investigated using recombinantly expressed wild-type and mutant androgen receptor (AR). Rates of androgen dissociation from nuclear and cytoplasmic AR were compared with hormone- and concentration-dependent receptor degradation rates. T dissociates from AR 3 times faster than DHT or methyltrienolone...

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 Hormonal and reproductive studies
Share to Sexual Differentiation and Disorders

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

Source

Identifiers

PMID: 7776971
DOI: 10.1210/mend.9.2.7776971

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

Specificity of ligand-dependent androgen receptor stabilization: receptor domain interactions influence ligand dissociation and receptor stability.PMID 7776971Read ↗

Structure and function of the androgen receptor.Semantic proximity Read ↗

Minireview: The Contribution of Different Androgen Receptor Domains to Receptor Dimerization and SignalingSemantic proximity Read ↗

An examination of how different mutations at arginine 855 of the androgen receptor result in different androgen insensitivity phenotypes.Semantic proximity Read ↗

Ligand induced dissociation of the AR homodimer precedes AR monomer translocation to the nucleus.Semantic proximity Read ↗

The androgen receptor transactivation domain: the interplay between protein conformation and protein-protein interactions.Semantic proximity Read ↗

Intermolecular NH2-/Carboxyl-terminal Interactions in Androgen Receptor Dimerization Revealed by Mutations That Cause Androgen InsensitivitySemantic proximity Read ↗

The use of androgen receptor amino/carboxyl-terminal interaction assays to investigate androgen receptor gene mutations in subjects with varying degrees of androgen insensitivity.Semantic proximity Read ↗

Study of novel androgen receptor V770 variant in androgen insensitivity syndrome patients reveals the transitional state of the androgen receptor ligand binding domain homodimer.Semantic proximity Read ↗

Evolution of the Primate Androgen Receptor: A Structural Basis for DiseaseSemantic proximity Read ↗

A novel androgen receptor mutant, A748T, exhibits hormone concentration-dependent defects in nuclear accumulation and activity despite normal hormone-binding affinity.Semantic proximity Read ↗

Substitution of valine-865 by methionine or leucine in the human androgen receptor causes complete or partial androgen insensitivity, respectively with distinct androgen receptor phenotypes.Semantic proximity Read ↗

Structure of the homodimeric androgen receptor ligand-binding domainSemantic proximity Read ↗

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