Atomic-resolution 3D structure of amyloid β fibrils: The Osaka mutation
Abstract
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 Aβ 1-40 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
- Authors:
-
- ETH Zurich, Wolfgang-Pauli-Strasse. Zurich (Switzerland)
- Brookhaven National Lab. (BNL), Upton, NY (United States)
- ETH Zurich, Zurich (Switzerland)
- Goethe Univ., Frankfurt (Germany)
- Univ. de Lyon, Lyon (France)
- Publication Date:
- Research Org.:
- Brookhaven National Laboratory (BNL), Upton, NY (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Biological and Environmental Research (BER)
- OSTI Identifier:
- 1183283
- Report Number(s):
- BNL-107758-2015-JA
Journal ID: ISSN 1433-7851; R&D Project: BO-108; KP1501010
- Grant/Contract Number:
- SC00112704
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Angewandte Chemie (International Edition)
- Additional Journal Information:
- Journal Name: Angewandte Chemie (International Edition); Journal Volume: 54; Journal Issue: 1; Journal ID: ISSN 1433-7851
- Publisher:
- Wiley
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES
Citation Formats
Schutz, Anne K., Wall, Joseph, Vagt, Toni, Huber, Matthias, Ovchinnikova, Oxana Y., Cadalbert, Riccardo, Guntert, Peter, Bockmann, Anja, Glockshuber, Rudi, and Meier, Beat H. Atomic-resolution 3D structure of amyloid β fibrils: The Osaka mutation. United States: N. p., 2014.
Web. doi:10.1002/anie.201408598.
Schutz, Anne K., Wall, Joseph, Vagt, Toni, Huber, Matthias, Ovchinnikova, Oxana Y., Cadalbert, Riccardo, Guntert, Peter, Bockmann, Anja, Glockshuber, Rudi, & Meier, Beat H. Atomic-resolution 3D structure of amyloid β fibrils: The Osaka mutation. United States. https://doi.org/10.1002/anie.201408598
Schutz, Anne K., Wall, Joseph, Vagt, Toni, Huber, Matthias, Ovchinnikova, Oxana Y., Cadalbert, Riccardo, Guntert, Peter, Bockmann, Anja, Glockshuber, Rudi, and Meier, Beat H. Thu .
"Atomic-resolution 3D structure of amyloid β fibrils: The Osaka mutation". United States. https://doi.org/10.1002/anie.201408598. https://www.osti.gov/servlets/purl/1183283.
@article{osti_1183283,
title = {Atomic-resolution 3D structure of amyloid β fibrils: The Osaka mutation},
author = {Schutz, Anne K. and Wall, Joseph and Vagt, Toni and Huber, Matthias and Ovchinnikova, Oxana Y. and Cadalbert, Riccardo and Guntert, Peter and Bockmann, Anja and Glockshuber, Rudi and Meier, Beat H.},
abstractNote = {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 Aβ 1-40 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},
doi = {10.1002/anie.201408598},
journal = {Angewandte Chemie (International Edition)},
number = 1,
volume = 54,
place = {United States},
year = {Thu Nov 13 00:00:00 EST 2014},
month = {Thu Nov 13 00:00:00 EST 2014}
}
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