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

Structural basis for accommodation of nonsteroidal ligands in the androgen receptor.

The Journal of biological chemistry - 11 Nov 2005

Bohl Casey E, Miller Duane D, Chen Jiyun, Bell Charles E, Dalton James T

Abstract excerpt

The mechanism by which the androgen receptor (AR) distinguishes between agonist and antagonist ligands is poorly understood. AR antagonists are currently used to treat prostate cancer. However, mutations commonly develop in patients that convert these compounds to agonists. Recently, our laboratory discovered selective androgen receptor modulators, which structurally resemble the nonsteroidal AR antagonists...

Read the complete abstract on PubMed

Topics

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

Share to Androgen Receptor Antagonists
Share to Androgens
Share to Drug Design

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ligands

Share to Molecular Conformation

Share to Receptors, Androgen

Share to Structure-Activity Relationship

Share to Transcriptional Activation

Source

Open in PubMed Open full text

Identifiers

PMID: 16129672
DOI: 10.1074/jbc.M507464200
PMCID: PMC2072880

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural basis for accommodation of nonsteroidal ligands in the androgen receptor.PMID 16129672Read ↗

Molecular mechanism of R-bicalutamide switching from androgen receptor antagonist to agonist induced by amino acid mutations using molecular dynamics simulations and free energy calculation.Semantic proximity Read ↗

Molecular Basis of Bicalutamide Response Alteration of Androgen Receptor Caused by Single Nucleotide Polymorphisms: An In Silico Investigation.Semantic proximity Read ↗

Interaction mechanism exploration of R-bicalutamide/S-1 with WT/W741L AR using molecular dynamics simulations.Semantic proximity Read ↗

Molecular basis of agonicity and antagonicity in the androgen receptor studied by molecular dynamics simulations.Semantic proximity Read ↗

Structural insights into the mechanism of resistance to bicalutamide by the clinical mutations in androgen receptor in chemo-treatment resistant prostate cancer.Semantic proximity Read ↗

Study of the impact of the T877A mutation on ligand-induced helix-12 positioning of the androgen receptor resulted in design and synthesis of novel antiandrogens.Semantic proximity Read ↗

A partially open conformation of an androgen receptor ligand-binding domain with drug-resistance mutations.Semantic proximity Read ↗

Homology modeling using multiple molecular dynamics simulations and docking studies of the human androgen receptor ligand binding domain bound to testosterone and nonsteroidal ligands.Semantic proximity Read ↗

Learning from estrogen receptor antagonism: structure-based identification of novel antiandrogens effective against multiple clinically relevant androgen receptor mutants.Semantic proximity Read ↗

In silico comparison between the mutated and wild-type androgen receptors and their influence on the selection of optimum androgenic receptor blockers for the treatment of prostate cancerSemantic proximity Read ↗

The discovery of novel human androgen receptor antagonist chemotypes using a combined pharmacophore screening procedure.Semantic proximity Read ↗

Molecular dynamics simulations reveal the plausible agonism/antagonism mechanism by steroids on androgen receptor mutations.Semantic proximity Read ↗

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