The Role of Protein Composition in Specifying Nuclear Inclusion Formation in Polyglutamine Disease
Open Access
- 1 November 2001
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 276 (48), 44889-44897
- https://doi.org/10.1074/jbc.m106575200
Abstract
No abstract availableKeywords
This publication has 54 references indexed in Scilit:
- Impairment of the Ubiquitin-Proteasome System by Protein AggregationScience, 2001
- Glutamine Repeats and NeurodegenerationAnnual Review of Neuroscience, 2000
- Nuclear Targeting of Mutant Huntingtin Increases ToxicityMolecular and Cellular Neuroscience, 1999
- Protein Fate in Neurodegenerative Proteinopathies: Polyglutamine Diseases Join the (Mis)FoldAmerican Journal of Human Genetics, 1999
- Aggresomes: A Cellular Response to Misfolded ProteinsThe Journal of cell biology, 1998
- Recruitment and the Role of Nuclear Localization in Polyglutamine-mediated AggregationThe Journal of cell biology, 1998
- Structure, Organization, and Dynamics of Promyelocytic Leukemia Protein Nuclear BodiesAmerican Journal of Human Genetics, 1998
- Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tractNature Genetics, 1996
- Expanded polyglutamine in the Machado–Joseph disease protein induces cell death in vitro and in vivoNature Genetics, 1996
- Polyglutamine expansion as a pathological epitope in Huntington's disease and four dominant cerebellar ataxiasNature, 1995