Residues 17–20 and 30–35 of beta‐amyloid play critical roles in aggregation
Author:
Affiliation:
1. Department of Chemical and Materials Engineering, Arizona State University, Tempe, Arizona
2. Department of Microbiology, Arizona State University, Tempe, Arizona
Publisher
Wiley
Subject
Cellular and Molecular Neuroscience
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/jnr.10859
Reference67 articles.
1. Amyloid Fibril Formation by Aβ16-22, a Seven-Residue Fragment of the Alzheimer's β-Amyloid Peptide, and Structural Characterization by Solid State NMR
2. Solution Structures of β Peptide and Its Constituent Fragments: Relation to Amyloid Deposition
3. Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's disease
4. Assemblies of Alzheimer’s peptides Aβ25–35 and Aβ31–35: reverse-turn conformation and side-chain interactions revealed by X-ray diffraction
5. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
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