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Article

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

Proceedings of the National Academy of Sciences of the United States of America - 18 Aug 2009

Maynard Christa J, Böttcher Claudia, Ortega Zaira, Smith Ruben, Florea Bogdan I, Díaz-Hernández Miguel, Brundin Patrik, Overkleeft Hermen S, Li Jia-Yi, Lucas Jose J, Dantuma Nico P

Abstract excerpt

Aggregation-prone proteins have been suggested to overwhelm and impair the ubiquitin/proteasome system (UPS) in polyglutamine (polyQ) disorders, such as Huntington's disease (HD). Overexpression of an N-terminal fragment of mutant huntingtin (N-mutHtt), an aggregation-prone polyQ protein responsible for HD, obstructs the UPS in cellular models. Furthermore, based on the accumulation of polyubiquitin conjugates in...

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Identifiers

PMID: 19666572
DOI: 10.1073/pnas.0906463106
PMCID: PMC2729007

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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.

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