Heat Shock Protein 70 Inhibits α-Synuclein Fibril Formation via Interactions with Diverse Intermediates
- 1 December 2006
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 364 (3) , 323-336
- https://doi.org/10.1016/j.jmb.2006.08.062
Abstract
No abstract availableKeywords
Funding Information
- Ministry of Science and Technology of the People's Republic of China (2006CB806508)
- National Natural Science Foundation of China (30470363)
- Chinese Academy of Sciences (KSCX2-SW214-2)
This publication has 49 references indexed in Scilit:
- Amyloid Fibril Formation of α-Synuclein Is Accelerated by Preformed Amyloid Seeds of Other ProteinsPublished by Elsevier ,2005
- Role of the C‐terminal region of mouse inducible Hsp72 in the recognition of peptide substrate for chaperone activityFEBS Letters, 2004
- Interaction of the Molecular Chaperone αB-Crystallin with α-Synuclein: Effects on Amyloid Fibril Formation and Chaperone ActivityJournal of Molecular Biology, 2004
- The new mutation, E46K, of α‐synuclein causes parkinson and Lewy body dementiaAnnals of Neurology, 2003
- Dependence of α-Synuclein Aggregate Morphology on Solution ConditionsPublished by Elsevier ,2002
- Vesicle Permeabilization by Protofibrillar α-Synuclein: Implications for the Pathogenesis and Treatment of Parkinson's DiseaseBiochemistry, 2001
- Dopaminergic Loss and Inclusion Body Formation in α-Synuclein Mice: Implications for Neurodegenerative DisordersScience, 2000
- AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's diseaseNature Genetics, 1998
- Mutation in the α-Synuclein Gene Identified in Families with Parkinson's DiseaseScience, 1997
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976