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

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.

Proteins - 15 Feb 2010

Zhou Jinming, Liu Bing, Geng Guoyan, Wu Jian Hui

Abstract excerpt

Antiandrogen flutamide, an antagonist of the wild-type androgen receptor (AR), is used in the clinics for treating metastatic prostate cancer. However, the T877A mutated AR is paradoxically activated by hydroxyflutamide, an active form of flutamide. Despite of crystallographic studies, how the T8...

Read the complete abstract on PubMed

Topics

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

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

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ligands

Share to Molecular Dynamics Simulation

Share to Principal Component Analysis

Share to Protein Interaction Domains and Motifs

Share to Receptors, Androgen

Source

Identifiers

PMID: 19787772
DOI: 10.1002/prot.22592

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-19787772-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

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.PMID 19787772Read ↗

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 ↗

A Molecular Modeling Study of the Hydroxyflutamide Resistance Mechanism Induced by Androgen Receptor Mutations.Semantic proximity Read ↗

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

Analysis of the binding modes of the first- and second-generation antiandrogens with respect to F876L mutation.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 ↗

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

Molecular Dynamics Studies on the Enzalutamide Resistance Mechanisms Induced by Androgen Receptor MutationsSemantic proximity Read ↗

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

Modeling androgen receptor flexibility: a binding mode hypothesis of CYP17 inhibitors/antiandrogens for prostate cancer therapy.Semantic proximity Read ↗

Mutation of the androgen receptor at amino acid 708 (Gly-->Ala) abolishes partial agonist activity of steroidal antiandrogens.Semantic proximity Read ↗

Overcoming mutation-based resistance to antiandrogens with rational drug design.Semantic proximity Read ↗

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