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Conformational diseases: structural studies of aggregation of polyglutamine proteins.
MedLine Citation:
PMID:  20807186     Owner:  NLM     Status:  In-Process    
Abstract/OtherAbstract:
Protein misfolding and aggregation into insoluble amyloid deposits are often associated with neurodegenerative disorders. In particular, the polyglutamine (polyQ) diseases are inherited disorders triggered by the expansion of the polyQ tract over its physiological length in the involved protein. The molecular mechanism of aggregation from the native protein into amyloids involves several steps including protein misfolding, aggregation into oligomers, which seems to be the most toxic species, and, finally rearrangements into mature fibrils. In the present contribution, we review studies, integrating computational and experimental approaches, of polyQ proteins, as well as of the details of the complicate aggregation mechanisms in which aberrant form of polyQ proteins are involved. These aspects are of crucial relevance for a complete understanding of the onset of polyQ conformational diseases and can also shed light on putative therapeutic targets and future development of aggregation inhibitors.
Authors:
Elena Papaleo; Gaetano Invernizzi
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Current computer-aided drug design     Volume:  7     ISSN:  1875-6697     ISO Abbreviation:  Curr Comput Aided Drug Des     Publication Date:  2011 Mar 
Date Detail:
Created Date:  2010-11-08     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101265750     Medline TA:  Curr Comput Aided Drug Des     Country:  United Arab Emirates    
Other Details:
Languages:  eng     Pagination:  23-43     Citation Subset:  IM    
Affiliation:
Department of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza 2, 20126 Milan, Italy. elena.papaleo@unimib.it
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