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Interaction of the molecular chaperone alphaB-crystallin with alpha-synuclein: effects on amyloid fibril formation and chaperone activity.

Abstract:

alpha-Synuclein is a pre-synaptic protein, the function of which is not completely understood, but its pathological form is involved in neurodegenerative diseases. In vitro, alpha-synuclein spontaneously forms amyloid fibrils. Here, we report that alphaB-crystallin, a molecular chaperone found in Lewy bodies that are characteristic of Parkinson's disease (PD), is a potent in vitro inhibitor of alpha-synuclein fibrillization, both of wild-type and the two mutant forms (A30P and A53T) that caus...

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Publisher copy:
10.1016/j.jmb.2004.05.054

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Journal:
Journal of molecular biology
Volume:
340
Issue:
5
Pages:
1167-1183
Publication date:
2004-07-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:10c0116f-9c35-445c-a614-fad87a7abf7b
Source identifiers:
60300
Local pid:
pubs:60300

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