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

Ligand responsiveness in human prostate cancer: structural analysis of mutant androgen receptors from LNCaP and CWR22 tumors.

Cancer research - 1 May 2000

McDonald S, Brive L, Agus D B, Scher H I, Ely K R

Abstract excerpt

Androgen receptors (ARs) belong to the family of hormone receptors that are ligand-dependent transcription factors. Endocrine therapy provides effective treatment for prostate cancer until mutations arise that alter the ligand responsiveness of AR. In this study, structural models were developed for the functional domains of human AR by homology modeling from crystal structures of closely related nuclear...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Ligands
Share to Neoplasms, Hormone-Dependent

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

Share to Prostatic Neoplasms

Share to Receptors, Androgen

Share to Receptors, Progesterone

Share to Sequence Homology, Amino Acid

Share to Tumor Cells, Cultured

Source

Identifiers

PMID: 10811100

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

Ligand responsiveness in human prostate cancer: structural analysis of mutant androgen receptors from LNCaP and CWR22 tumors.PMID 10811100Read ↗

Structure and Function of the Nuclear Receptor Superfamily and Current Targeted Therapies of Prostate CancerSemantic proximity Read ↗

Broadened ligand responsiveness of androgen receptor mutants obtained by random amino acid substitution of H874 and mutation hot spot T877 in prostate cancer.Semantic proximity Read ↗

Mutations at the boundary of the hinge and ligand binding domain of the androgen receptor confer increased transactivation function.Semantic proximity Read ↗

The Androgen Receptor in Prostate Cancer: Effect of Structure, Ligands and Spliced Variants on TherapySemantic proximity Read ↗

Structural basis for androgen receptor interdomain and coactivator interactions suggests a transition in nuclear receptor activation function dominance.Semantic proximity Read ↗

Isolation and characterization of androgen receptor mutant, AR(M749L), with hypersensitivity to 17-beta estradiol treatment.Semantic proximity Read ↗

A mutation in the ligand binding domain of the androgen receptor of human LNCaP cells affects steroid binding characteristics and response to anti-androgens.Semantic proximity Read ↗

Targeting Alternative Sites on the Androgen Receptor to Treat Castration-Resistant Prostate CancerSemantic proximity Read ↗

Mechanisms of androgen receptor activation in advanced prostate cancer: differential co-activator recruitment and gene expression.Semantic proximity Read ↗

Analyzing the Androgen Receptor Interactome in Prostate Cancer: Implications for Therapeutic InterventionSemantic 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 ↗

A hotspot for posttranslational modifications on the androgen receptor dimer interface drives pathology and anti-androgen resistance.Semantic proximity Read ↗

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