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

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...

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Autores principales: Schütz, Anne K, Vagt, Toni, Huber, Matthias, Ovchinnikova, Oxana Y, Cadalbert, Riccardo, Wall, Joseph, Güntert, Peter, Böckmann, Anja, Glockshuber, Rudi, Meier, Beat H
Formato: Online Artículo Texto
Lenguaje:English
Publicado: WILEY-VCH Verlag 2015
Materias:
Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4502972/
https://www.ncbi.nlm.nih.gov/pubmed/25395337
http://dx.doi.org/10.1002/anie.201408598
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author Schütz, Anne K
Vagt, Toni
Huber, Matthias
Ovchinnikova, Oxana Y
Cadalbert, Riccardo
Wall, Joseph
Güntert, Peter
Böckmann, Anja
Glockshuber, Rudi
Meier, Beat H
author_facet Schütz, Anne K
Vagt, Toni
Huber, Matthias
Ovchinnikova, Oxana Y
Cadalbert, Riccardo
Wall, Joseph
Güntert, Peter
Böckmann, Anja
Glockshuber, Rudi
Meier, Beat H
author_sort Schütz, Anne K
collection PubMed
description 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.
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spelling pubmed-45029722015-07-22 Atomic-Resolution Three-Dimensional Structure of Amyloid β Fibrils Bearing the Osaka Mutation** Schütz, Anne K Vagt, Toni Huber, Matthias Ovchinnikova, Oxana Y Cadalbert, Riccardo Wall, Joseph Güntert, Peter Böckmann, Anja Glockshuber, Rudi Meier, Beat H Angew Chem Int Ed Engl Communications 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. WILEY-VCH Verlag 2015-01-02 2014-11-13 /pmc/articles/PMC4502972/ /pubmed/25395337 http://dx.doi.org/10.1002/anie.201408598 Text en © 2014 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. http://creativecommons.org/licenses/by/3.0/ This is an open access article under the terms of the Creative Commons Attribution Non-Commercial NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.
spellingShingle Communications
Schütz, Anne K
Vagt, Toni
Huber, Matthias
Ovchinnikova, Oxana Y
Cadalbert, Riccardo
Wall, Joseph
Güntert, Peter
Böckmann, Anja
Glockshuber, Rudi
Meier, Beat H
Atomic-Resolution Three-Dimensional Structure of Amyloid β Fibrils Bearing the Osaka Mutation**
title Atomic-Resolution Three-Dimensional Structure of Amyloid β Fibrils Bearing the Osaka Mutation**
title_full Atomic-Resolution Three-Dimensional Structure of Amyloid β Fibrils Bearing the Osaka Mutation**
title_fullStr Atomic-Resolution Three-Dimensional Structure of Amyloid β Fibrils Bearing the Osaka Mutation**
title_full_unstemmed Atomic-Resolution Three-Dimensional Structure of Amyloid β Fibrils Bearing the Osaka Mutation**
title_short Atomic-Resolution Three-Dimensional Structure of Amyloid β Fibrils Bearing the Osaka Mutation**
title_sort atomic-resolution three-dimensional structure of amyloid β fibrils bearing the osaka mutation**
topic Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4502972/
https://www.ncbi.nlm.nih.gov/pubmed/25395337
http://dx.doi.org/10.1002/anie.201408598
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