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

Proteasome impairment does not contribute to pathogenesis in R6/2 Huntington's disease mice: exclusion of proteasome activator REGgamma as a therapeutic target.

Human molecular genetics - 1 Jan 2006

Bett John S, Goellner Geoffrey M, Woodman Ben, Pratt Gregory, Rechsteiner Martin, Bates Gillian P

Abstract excerpt

Huntington's disease (HD) is one of a group of neurodegenerative disorders caused by the pathological expansion of a glutamine tract. A hallmark of these so-called polyglutamine diseases is the presence of ubiquitylated inclusion bodies, which sequester various components of the 19S and 20S proteasomes. In addition, the ubiquitin-proteasome system (UPS) has been shown to be severely impaired in vitro in cells...

Read the complete abstract on PubMed

Topics

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

Share to Autoantigens
Share to Exploratory Behavior

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Huntington Disease

Share to Inclusion Bodies

Share to Mice, Mutant Strains

Share to Peptides

Share to Proteasome Endopeptidase Complex

Share to Rotarod Performance Test

Source

Identifiers

PMID: 16311253
DOI: 10.1093/hmg/ddi423

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

Proteasome impairment does not contribute to pathogenesis in R6/2 Huntington's disease mice: exclusion of proteasome activator REGgamma as a therapeutic target.PMID 16311253Read ↗

Accumulation of ubiquitin conjugates in a polyglutamine disease model occurs without global ubiquitin/proteasome system impairment.Semantic proximity Read ↗

Genetic knock-down of HDAC3 does not modify disease-related phenotypes in a mouse model of Huntington's disease.Semantic proximity Read ↗

Indirect inhibition of 26S proteasome activity in a cellular model of Huntington's disease.Semantic proximity Read ↗

Genetic knock-down of HDAC7 does not ameliorate disease pathogenesis in the R6/2 mouse model of Huntington's disease.Semantic proximity Read ↗

Hsp27 overexpression in the R6/2 mouse model of Huntington's disease: chronic neurodegeneration does not induce Hsp27 activation.Semantic proximity Read ↗

Tissue transglutaminase overexpression does not modify the disease phenotype of the R6/2 mouse model of Huntington's disease.Semantic proximity Read ↗

SIRT2 ablation has no effect on tubulin acetylation in brain, cholesterol biosynthesis or the progression of Huntington's disease phenotypes in vivo.Semantic proximity Read ↗

Tissue transglutaminase contributes to disease progression in the R6/2 Huntington's disease mouse model via aggregate‐independent mechanismsSemantic proximity Read ↗

Genetic deletion of transglutaminase 2 does not rescue the phenotypic deficits observed in R6/2 and zQ175 mouse models of Huntington's disease.Semantic proximity Read ↗

Genetic deletion of S6k1 does not rescue the phenotypic deficits observed in the R6/2 mouse model of Huntington's disease.Semantic proximity Read ↗

Capucin does not modify the toxicity of a mutant Huntingtin fragment in vivo.Semantic proximity Read ↗

Temporal separation of aggregation and ubiquitination during early inclusion formation in transgenic mice carrying the Huntington's disease mutation.Semantic proximity Read ↗

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