Atomic-Resolution Three-Dimensional Structure of Amyloid β Fibrils Bearing the Osaka Mutation.

Autor:	Schütz, Anne K., Vagt, Toni, Huber, Matthias, Ovchinnikova, Oxana Y., Cadalbert, Riccardo, Wall, Joseph, Güntert, Peter, Böckmann, Anja, Glockshuber, Rudi, Meier, Beat H.
Předmět:	GENETICS of Alzheimer's disease NUCLEAR magnetic resonance AMYLOID beta-protein DELETION mutation NEURODEGENERATION GENETICS
Zdroj:	Angewandte Chemie International Edition; Jan2015, Vol. 54 Issue 1, p331-335, 5p
Abstrakt:	Despite its central importance for understanding the molecular basis of Alzheimer's disease (AD), high-resolution structural information on amyloid β-peptide (Aβ) fibrils, which are intimately linked with AD, is scarce. We report an atomic-resolution fibril structure of the Aβ1-40 peptide with the Osaka mutation (E22Δ), associated with early-onset AD. The structure, which differs substantially from all previously proposed models, is based on a large number of unambiguous intra- and intermolecular solid-state NMR distance restraints. [ABSTRACT FROM AUTHOR]
Databáze:	Complementary Index
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