Atomic‐Resolution Three‐Dimensional Structure of Amyloid β Fibrils Bearing the Osaka Mutation-Reference-Cited by-同舟云学术

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

Published:2014-11-13 Issue:1 Volume:54 Page:331-335
ISSN:1433-7851
Container-title:Angewandte Chemie International Edition
language:en
Short-container-title:Angew. Chem. Int. Ed.

Author:

Schütz Anne K.¹,Vagt Toni²,Huber Matthias¹,Ovchinnikova Oxana Y.²,Cadalbert Riccardo¹,Wall Joseph³,Güntert Peter⁴,Böckmann Anja⁵,Glockshuber Rudi²,Meier Beat H.¹

Affiliation:

1. Physical Chemistry, ETH Zürich, Vladimir‐Prelog‐Weg 2, 8093 Zurich (Switzerland)

2. Institute of Molecular Biology and Biophysics, ETH Zurich, Otto‐Stern‐Weg 5, 8093 Zurich (Switzerland)

3. Brookhaven National Laboratory, 50 Bell Avenue, Building 463,Upton, NY 11973‐5000 (USA)

4. Institute of Biophysical Chemistry, Center for Biomolecular Magnetic Resonance and Frankfurt Institute for Advanced Studies, Goethe University, Frankfurt am Main (Germany)

5. Institut de Biologie et Chimie des Protéines, Bases Moléculaires et Structurales des Systèmes Infectieux, Labex Ecofect, UMR 5086 CNRS, Université de Lyon, 7 passage du Vercors, 69367 Lyon (France)

Publisher

Wiley

Subject

General Chemistry,Catalysis

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/anie.201408598

Reference35 articles.

1. The Amyloid Hypothesis of Alzheimer's Disease: Progress and Problems on the Road to Therapeutics

2. Alzheimer's Disease: The Amyloid Cascade Hypothesis

3. Amyloid Fibrils of the HET-s(218–289) Prion Form a β Solenoid with a Triangular Hydrophobic Core

4. Atomic-Resolution Three-Dimensional Structure of HET-s(218−289) Amyloid Fibrils by Solid-State NMR Spectroscopy

5. Atomic structure and hierarchical assembly of a cross- amyloid fibril

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