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

Josephin domain of ataxin-3 contains two distinct ubiquitin-binding sites.

Biopolymers - 1 Dec 2009

Nicastro Giuseppe, Masino Laura, Esposito Veronica, Menon Rajesh P, De Simone Alfonso, Fraternali Franca, Pastore Annalisa

Abstract excerpt

Joseph-Machado is an incurable neurodegenerative disease caused by toxic aggregation of ataxin-3, a ubiquitin-specific cysteine protease, involved in the ubiquitin-proteasome pathway and known to bind poly-ubiquitin chains of four or more subunits. The enzymatic site resides in the N-terminal josephin domain of ataxin-3. We have characterized the ubiquitin-binding properties of josephin and showed that,...

Read the complete abstract on PubMed

Topics

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

Share to Ataxin-3
Share to Computer Simulation
Share to Kinetics

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Magnetic Resonance Spectroscopy

Share to Nerve Tissue Proteins

Share to Protein Structure, Secondary

Share to Repressor Proteins

Share to Ubiquitin

Source

Identifiers

PMID: 19382171
DOI: 10.1002/bip.21210

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

Josephin domain of ataxin-3 contains two distinct ubiquitin-binding sites.PMID 19382171Read ↗

Functional interactions as a survival strategy against abnormal aggregation.Semantic proximity Read ↗

Capturing the Conformational Ensemble of the Mixed Folded Polyglutamine Protein Ataxin-3.Semantic proximity Read ↗

Machado–Joseph disease/spinocerebellar ataxia type 3: lessons from disease pathogenesis and clues into therapySemantic proximity Read ↗

Ubiquitin-mediated sequestration of normal cellular proteins into polyglutamine aggregates.Semantic proximity Read ↗

Enhanced molecular mobility of ordinarily structured regions drives polyglutamine disease.Semantic proximity Read ↗

Interaction between the AAA+ ATPase p97 and its cofactor ataxin3 in health and disease: Nucleotide-induced conformational changes regulate cofactor binding.Semantic proximity Read ↗

Toward understanding Machado-Joseph disease.Semantic proximity Read ↗

Destabilization of a non-pathological variant of ataxin-3 results in fibrillogenesis via a partially folded intermediate: a model for misfolding in polyglutamine disease.Semantic proximity Read ↗

Flanking domain stability modulates the aggregation kinetics of a polyglutamine disease protein.Semantic proximity Read ↗

Polyglutamine diseases: The special case of ataxin-3 and Machado–Joseph diseaseSemantic proximity Read ↗

N-terminal ataxin-3 causes neurological symptoms with inclusions, endoplasmic reticulum stress and ribosomal dislocation.Semantic proximity Read ↗

An arginine/lysine-rich motif is crucial for VCP/p97-mediated modulation of ataxin-3 fibrillogenesis.Semantic proximity Read ↗

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