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

In vitro functional characterization of androgen receptor gene mutations at arginine p.856 of the ligand-binding-domain associated with androgen insensitivity syndrome.

The Journal of steroid biochemistry and molecular biology - 1 Apr 2021

Tajouri Asma, Kharrat Maher, Trabelsi Mediha, M'rad Ridha, Hiort Olaf, Werner Ralf

Abstract excerpt

Androgens are critical for male sex differentiation. Their actions are mediated by the androgen receptor (AR). Mutations disrupting AR function result in the androgen insensitivity syndrome (AIS). In this study, we identified in a patient with complete AIS, a novel AR mutation p.R856L. To investigate the functional properties of p.R856L, we performed functional studies. In comparison, we have characterized two...

Read the complete abstract on PubMed

Topics

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

Share to Androgen-Insensitivity Syndrome
Share to Androgens

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

Share to Arginine

Share to Cricetulus

Share to Ligands

Share to Protein Domains

Share to Receptors, Androgen

Share to Sex Differentiation

Source

Identifiers

PMID: 33548461
DOI: 10.1016/j.jsbmb.2021.105834

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

In vitro functional characterization of androgen receptor gene mutations at arginine p.856 of the ligand-binding-domain associated with androgen insensitivity syndrome.PMID 33548461Read ↗

Five novel androgen receptor gene mutations associated with complete androgen insensitivity syndrome.Semantic proximity Read ↗

Pathophysiology of androgen insensitivity syndromes: molecular and structural approaches of natural and engineered androgen receptor mutations at amino acid 743.Semantic proximity Read ↗

Preserved fertility in a patient with gynecomastia associated with the p.Pro695Ser mutation in the androgen receptor.Semantic proximity Read ↗

Disrupted Amino- and Carboxyl-Terminal Interactions of the Androgen Receptor Are Linked to Androgen InsensitivitySemantic proximity Read ↗

Functional characterisation of mutations in the ligand-binding domain of the androgen receptor gene in patients with androgen insensitivity syndrome.Semantic proximity Read ↗

A Novel Mutation in the Human Androgen Receptor Suggests a Regulatory Role for the Hinge Region in Amino-Terminal and Carboxy-Terminal InteractionsSemantic proximity Read ↗

In-vitro characterization of androgen receptor mutations associated with complete androgen insensitivity syndrome reveals distinct functional deficits.Semantic proximity Read ↗

Response to treatment in patients with partial androgen insensitivity due to mutations in the DNA-binding domain of the androgen receptor.Semantic proximity Read ↗

Androgen receptor abnormalities.Semantic proximity Read ↗

Androgen receptor gene mutations in androgen insensitivity syndrome cause distinct patterns of reduced activation of androgen-responsive promoter constructs.Semantic proximity Read ↗

Comparison of the molecular consequences of different mutations at residue 754 and 690 of the androgen receptor (AR) and androgen insensitivity syndrome (AIS) phenotype.Semantic proximity Read ↗

Functional Impact of Novel Androgen Receptor Mutations on the Clinical Manifestation of Androgen Insensitivity Syndrome.Semantic proximity Read ↗

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