CHIP Targets Toxic α-Synuclein Oligomers for Degradation
Open Access
- 1 June 2008
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 283 (26) , 17962-17968
- https://doi.org/10.1074/jbc.m802283200
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- U‐box protein carboxyl terminus of Hsc70‐interacting protein (CHIP) mediates poly‐ubiquitylation preferentially on four‐repeat Tau and is involved in neurodegeneration of tauopathyJournal of Neurochemistry, 2004
- Geldanamycin induces Hsp70 and prevents α-synuclein aggregation and toxicity in vitroPublished by Elsevier ,2004
- Hsp70 Reduces α-Synuclein Aggregation and ToxicityJournal of Biological Chemistry, 2004
- CHIP-Hsc70 Complex Ubiquitinates Phosphorylated Tau and Enhances Cell SurvivalJournal of Biological Chemistry, 2004
- CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregationHuman Molecular Genetics, 2004
- Zeroing in on the Pathogenic Form of α-Synuclein and Its Mechanism of Neurotoxicity in Parkinson's DiseaseBiochemistry, 2003
- Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysisNature Biotechnology, 2003
- The Formation of Highly Soluble Oligomers of α-Synuclein Is Regulated by Fatty Acids and Enhanced in Parkinson's DiseaseNeuron, 2003
- Vesicle Permeabilization by Protofibrillar α-Synuclein Is Sensitive to Parkinson's Disease-Linked Mutations and Occurs by a Pore-like MechanismBiochemistry, 2002
- Chaperone Suppression of α-Synuclein Toxicity in a Drosophila Model for Parkinson's DiseaseScience, 2002