Title: A comparative analysis of the aggregation behavior of amyloid-β peptide variants
Authors: Vandersteen, Annelies
Hubin, Ellen
Sarroukh, Rabia
De Baets, Greet
Schymkowitz, Joost
Rousseau, Frederic
Subramaniam, Vinod
Raussens, Vincent
Wenschuh, Holger
Wildemann, Dirk
Broersen, Kerensa # ×
Issue Date: Oct-2012
Publisher: Elsevier on behalf of the Federation of European Biochemical Societies
Series Title: FEBS Letters vol:586 issue:23 pages:4088-4093
Article number: S0014-5793(12)00805-8
Abstract: 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).
ISSN: 0014-5793
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Switch Laboratory
× corresponding author
# (joint) last author

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