Document Detail


A comparative analysis of the aggregation behavior of amyloid-β peptide variants.
MedLine Citation:
PMID:  23103738     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
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).
Authors:
Annelies Vandersteen; Ellen Hubin; Rabia Sarroukh; Greet De Baets; Joost Schymkowitz; Frederic Rousseau; Vinod Subramaniam; Vincent Raussens; Holger Wenschuh; Dirk Wildemann; Kerensa Broersen
Related Documents :
20441878 - An oegylated thiol monolayer for the tethering of liposomes and the study of liposome i...
12133008 - Temporin l: antimicrobial, haemolytic and cytotoxic activities, and effects on membrane...
14757228 - Stabilisation of mixed peptide/lipid complexes in selective antifungal hexapeptides.
19124558 - Novel peptide ligand directs liposomes toward egf-r high-expressing cancer cells in vit...
12643528 - Peptide end sequencing by orthogonal maldi tandem mass spectrometry.
17450548 - Protein structure prediction aided by geometrical and probabilistic constraints.
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.
Affiliation:
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.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:

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


Previous Document:  Concise Clinical Review: High Altitude Medicine.
Next Document:  MiR-34a is involved in Tat-induced HIV-1 long terminal repeat (LTR) transactivation through the SIRT...