In vivo suppression of polyglutamine neurotoxicity by C-terminus of Hsp70-interacting protein (CHIP) supports an aggregation model of pathogenesis
- 8 November 2008
- journal article
- Published by Elsevier in Neurobiology of Disease
- Vol. 33 (3) , 342-353
- https://doi.org/10.1016/j.nbd.2008.10.016
Abstract
No abstract availableKeywords
Funding Information
- National Institutes of Health (NS056609, NS38712)
This publication has 57 references indexed in Scilit:
- Cellular Turnover of the Polyglutamine Disease Protein Ataxin-3 Is Regulated by Its Catalytic ActivityPublished by Elsevier ,2007
- Overexpression of the Cochaperone CHIP Enhances Hsp70-Dependent Folding Activity in Mammalian CellsMolecular and Cellular Biology, 2003
- Aggregate formation inhibits proteasomal degradation of polyglutamine proteinsHuman Molecular Genetics, 2002
- Huntington's disease age-of-onset linked to polyglutamine aggregation nucleationProceedings of the National Academy of Sciences, 2002
- CHIP Is Associated with Parkin, a Gene Responsible for Familial Parkinson's Disease, and Enhances Its Ubiquitin Ligase ActivityMolecular Cell, 2002
- Toxic Proteins in Neurodegenerative DiseaseScience, 2002
- Impairment of the Ubiquitin-Proteasome System by Protein AggregationScience, 2001
- The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteinsNature Cell Biology, 2000
- The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradationNature Cell Biology, 2000
- Cardiac Hypertrophy Is Not a Required Compensatory Response to Short-Term Pressure OverloadCirculation, 2000