Document Detail

A comparative analysis of the aggregation behavior of amyloid-β peptide variants.
MedLine Citation:
PMID:  23103738     Owner:  NLM     Status:  Publisher    
Aggregated forms of the amyloid-β peptide are hypothesized to act as the prime toxic agents in Alzheimer disease (AD). The in vivo amyloid-β peptide pool consists of both C- and N-terminally truncated or mutated peptides, and the composition thereof significantly determines AD risk. Other variations, such as biotinylation, are introduced as molecular tools to aid the understanding of disease mechanisms. Since these modifications have the potential to alter key aggregation properties of the amyloid-beta peptide, we present a comparative study of the aggregation of a substantial set of the most common in vivo identified and in vitro produced amyloid-beta peptides. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: Amyloid beta and Amyloid betabind by fluorescence technology (View Interaction: 1, 2, 3, 4, 5) Amyloid beta and Amyloid betabind by transmission electron microscopy (View Interaction: 1, 2) Amyloid beta and Amyloid betabind by filter binding (View Interaction: 1, 2, 3).
Annelies Vandersteen; Ellen Hubin; Rabia Sarroukh; Greet De Baets; Joost Schymkowitz; Frederic Rousseau; Vinod Subramaniam; Vincent Raussens; Holger Wenschuh; Dirk Wildemann; Kerensa Broersen
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-10-24
Journal Detail:
Title:  FEBS letters     Volume:  -     ISSN:  1873-3468     ISO Abbreviation:  FEBS Lett.     Publication Date:  2012 Oct 
Date Detail:
Created Date:  2012-10-29     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2012. Published by Elsevier B.V.
Nanobiophysics Group, MIRA Institute for Biomedical Technology and Technical Medicine, Faculty of Science and Technology, University of Twente, 7500 AE Enschede, The Netherlands; VIB Switch Laboratory, Department of Cellular and Molecular Medicine, Katholieke Universiteit Leuven (KUL), Herestraat 49 Box 802, 3000 Leuven, Belgium.
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