Structural Differences between Aβ(1-40) Intermediate Oligomers and Fibrils Elucidated by Proteolytic Fragmentation and Hydrogen/Deuterium Exchange
- 1 February 2009
- journal article
- Published by Elsevier in Biophysical Journal
- Vol. 96 (3), 1091-1104
- https://doi.org/10.1016/j.bpj.2008.10.022
Abstract
No abstract availableKeywords
Funding Information
- National Institutes of Health
This publication has 56 references indexed in Scilit:
- Annular Structures as Intermediates in Fibril Formation of Alzheimer Aβ17−42The Journal of Physical Chemistry B, 2008
- Simultaneous monitoring of peptide aggregate distributions, structure, and kinetics using amide hydrogen exchange: Application to Aβ(1‐40) fibrillogenesisBiotechnology & Bioengineering, 2008
- Amide solvent protection analysis demonstrates that amyloid-β(1–40) and amyloid-β(1–42) form different fibrillar structures under identical conditionsBiochemical Journal, 2007
- Role of aggregation conditions in structure, stability, and toxicity of intermediates in the Aβ fibril formation pathwayProtein Science, 2007
- Monomer adds to preformed structured oligomers of Aβ-peptides by a two-stage dock–lock mechanismProceedings of the National Academy of Sciences, 2007
- Experimental Constraints on Quaternary Structure in Alzheimer's β-Amyloid FibrilsBiochemistry, 2005
- 3D structure of Alzheimer's amyloid-β(1–42) fibrilsProceedings of the National Academy of Sciences, 2005
- Structural properties of Aβ protofibrils stabilized by a small moleculeProceedings of the National Academy of Sciences, 2005
- Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of PathogenesisScience, 2003
- Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseasesNature, 2002