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

SUMO-1 interacts with mutant ataxin-1 and colocalizes to its aggregates in Purkinje cells of SCA1 transgenic mice.

Archives italiennes de biologie - 1 Dec 2010

Kang Seongman, Hong Sunghoi

Abstract excerpt

Spinocerebellar ataxia type 1 (SCA1) is one of several progressive neurodegenerative diseases caused by the expanded polyglutamine tract in ataxin-1, the SCA1 gene product. In SCA1 patients and transgenic mice, the affected neuronal cells contain a large ubiquitin-positive aggregate which is derived from the mutant ataxin-1. Small ubiquitin-like modifier-1 (SUMO-1) is one of the most intriguing ubiquitin-like...

Read the complete abstract on PubMed

Topics

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

Share to Ataxin-1
Share to Ataxins
Share to Cell Line, Transformed

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Purkinje Cells

Share to Spinocerebellar Ataxias

Share to SUMO-1 Protein

Share to Two-Hybrid System Techniques

Share to Ubiquitin

Source

Identifiers

PMID: 21308649
DOI: 10.4449/aib.v148i4.1201

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

SUMO-1 interacts with mutant ataxin-1 and colocalizes to its aggregates in Purkinje cells of SCA1 transgenic mice.PMID 21308649Read ↗

USP7, a ubiquitin-specific protease, interacts with ataxin-1, the SCA1 gene product.Semantic proximity Read ↗

Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamine-induced pathology in SCA1 mice.Semantic proximity Read ↗

Identification of genes that modify ataxin-1-induced neurodegeneration.Semantic proximity Read ↗

SUMO-1 immunoreactivity co-localizes with phospho-Tau in APP transgenic mice but not in mutant Tau transgenic mice.Semantic proximity Read ↗

Identification of the ataxin-1 interaction network and its impact on spinocerebellar ataxia type 1Semantic proximity Read ↗

Amino acids in a region of ataxin-1 outside of the polyglutamine tract influence the course of disease in SCA1 transgenic mice.Semantic proximity Read ↗

Regulation of ALS-Associated SOD1 Mutant SUMOylation and Aggregation by SENP and PIAS Family Proteins.Semantic proximity Read ↗

PIAS1 S510G variant acts as a genetic modifier of spinocerebellar ataxia type 3 by selectively impairing mutant ataxin-3 proteostasis.Semantic proximity Read ↗

SUMO-1 modification increases human SOD1 stability and aggregation.Semantic proximity Read ↗

Ataxin 1, a SCA1 neurodegenerative disorder protein, is functionally linked to the silencing mediator of retinoid and thyroid hormone receptors.Semantic proximity Read ↗

SUMO-1 modification on K166 of polyQ-expanded ataxin-3 strengthens its stability and increases its cytotoxicity.Semantic proximity Read ↗

SUMO modification of Huntingtin and Huntington's disease pathology.Semantic proximity Read ↗

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