Interaction of the Molecular Chaperone αB-Crystallin with α-Synuclein: Effects on Amyloid Fibril Formation and Chaperone Activity
- 15 June 2004
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 340 (5), 1167-1183
- https://doi.org/10.1016/j.jmb.2004.05.054
Abstract
No abstract availableKeywords
This publication has 66 references indexed in Scilit:
- Intracellular Protein Unfolding and Aggregation: The Role of Small Heat-Shock Chaperone ProteinsAustralian Journal of Chemistry, 2003
- TorsinA and heat shock proteins act as molecular chaperones: suppression of α‐synuclein aggregationJournal of Neurochemistry, 2002
- Clusterin/apolipoprotein J is associated with cortical Lewy bodies: immunohistochemical study in cases with α-synucleinopathiesActa Neuropathologica, 2002
- Structure and function of the small heat shock protein/α-crystallin family of molecular chaperonesAdvances in protein chemistry, 2001
- Fatal attractions: abnormal protein aggregation and neuron death in Parkinson's disease and Lewy body dementiaCell Death & Differentiation, 1998
- Filamentous nerve cell inclusions in neurodegenerative diseasesCurrent Opinion in Neurobiology, 1998
- Familial parkinsonism and dementia with ballooned neurons, argyrophilic neuronal inclusions, atypical neurofibrillary tangles, tau-negative astrocytic fibrillary tangles, and Lewy bodiesActa Neuropathologica, 1998
- The Interaction of the Molecular Chaperone, α-Crystallin, with Molten Globule States of Bovine α-LactalbuminJournal of Biological Chemistry, 1997
- α-Synuclein in Lewy bodiesNature, 1997
- Dementia with β-amyloid deposition: involvement of αB-crystallin supports two main diseasesThe Lancet, 1990