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

Glucocorticoid modulation of androgen receptor nuclear aggregation and cellular toxicity is associated with distinct forms of soluble expanded polyglutamine protein.

Human molecular genetics - 15 Dec 2001

Welch W J, Diamond M I

Abstract excerpt

Spinobulbar muscular atrophy is a progressive motor neuron disease caused by abnormal polyglutamine tract expansion in the androgen receptor (AR) gene, and is part of a family of central nervous system (CNS) neurodegenerative diseases, including Huntington's disease (HD). Each pathologic protein is widely expressed, but the cause of neuronal degeneration within the CNS remains unknown. Many reports now link...

Read the complete abstract on PubMed

Topics

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

Share to 3T3 Cells
Share to Adrenal Cortex Hormones

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cell Nucleus

Share to Cell Survival

Share to Drug-Related Side Effects and Adverse Reactions

Share to Heat-Shock Proteins

Share to Peptides

Share to Receptors, Androgen

Source

Identifiers

PMID: 11751688
DOI: 10.1093/hmg/10.26.3063

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

Glucocorticoid modulation of androgen receptor nuclear aggregation and cellular toxicity is associated with distinct forms of soluble expanded polyglutamine protein.PMID 11751688Read ↗

Enhanced aggregation of androgen receptor in induced pluripotent stem cell-derived neurons from spinal and bulbar muscular atrophy.Semantic proximity Read ↗

Cytoplasmic retention of polyglutamine-expanded androgen receptor ameliorates disease via autophagy in a mouse model of spinal and bulbar muscular atrophySemantic proximity Read ↗

Subcellular Localization And Formation Of Huntingtin Aggregates Correlates With Symptom Onset And Progression In A Huntington’S Disease ModelSemantic proximity Read ↗

Specific N-terminal mutations in the human androgen receptor induce cytotoxicity.Semantic proximity Read ↗

Protein aggregation in motor neurone disorders.Semantic proximity Read ↗

Pathogenesis of polyglutamine disorders: aggregation revisitedSemantic proximity Read ↗

Targeting expression of expanded polyglutamine proteins to the endoplasmic reticulum or mitochondria prevents their aggregation.Semantic proximity Read ↗

Trinucleotide repeat disease. The androgen receptor in spinal and bulbar muscular atrophy.Semantic proximity Read ↗

Aggregation and proteasome: the case of elongated polyglutamine aggregation in spinal and bulbar muscular atrophy.Semantic proximity Read ↗

Small ubiquitin-like modifier (SUMO) modification of the androgen receptor attenuates polyglutamine-mediated aggregation.Semantic proximity Read ↗

Aggresomes protect cells by enhancing the degradation of toxic polyglutamine-containing protein.Semantic proximity Read ↗

An interdomain interaction of the androgen receptor is required for its aggregation and toxicity in spinal and bulbar muscular atrophy.Semantic proximity Read ↗

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