Document Detail

Neurotoxic protein oligomers--what you see is not always what you get.
MedLine Citation:
PMID:  16011984     Owner:  NLM     Status:  MEDLINE    
An increasing body of evidence suggests that soluble assemblies of amyloid proteins are the predominant neurotoxic species in many amyloid-related diseases. Consequently, the focus of research on pathologic mechanisms underlying amyloidoses has shifted from amyloid fibrils to oligomers. Biophysical characterization of oligomers is difficult due to their metastable nature. The most popular experimental method for detection of oligomers has been SDS-PAGE. However, we provide experimental evidence that SDS-PAGE is not a reliable method for characterization of amyloid protein oligomers and discuss alternative approaches. In addition, we discuss how inconsistent nomenclature has obfuscated our understanding of the process and products of protein assembly. The goals of this paper are to identify pitfalls associated with the methods and language used to study protein oligomers and to provide alternatives, thereby facilitating successful elucidation of the mechanisms controlling amyloid protein oligomer assembly and toxicity.
Gal Bitan; Erica A Fradinger; Sean M Spring; David B Teplow
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis     Volume:  12     ISSN:  1350-6129     ISO Abbreviation:  Amyloid     Publication Date:  2005 Jun 
Date Detail:
Created Date:  2005-07-13     Completed Date:  2005-11-07     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  9433802     Medline TA:  Amyloid     Country:  United States    
Other Details:
Languages:  eng     Pagination:  88-95     Citation Subset:  IM    
Department of Neurology, David Geffen School of Medicine at UCLA, 90095-7334, USA.
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MeSH Terms
Biopolymers / chemistry,  toxicity*
Chromatography, Gel
Electrophoresis, Polyacrylamide Gel
Molecular Weight
Nervous System / drug effects*
Proteins / chemistry,  toxicity*
Terminology as Topic
Grant Support
Reg. No./Substance:
0/Biopolymers; 0/Proteins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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