Structural Differences in Aβ Amyloid Protofibrils and Fibrils Mapped by Hydrogen Exchange – Mass Spectrometry with On-line Proteolytic Fragmentation
Authors:
- Maolian ChenMCMaolian Chen
- Kelsey D. CookKCKelsey D. Cook
- Ronald WetzelRWRonald Wetzel
- 1 August 2006
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 361 (4) , 785-795
Abstract
No abstract availableKeywords
Funding Information
- Louisiana Board of Regents
- National Science Foundation (EPS-0346411)
- National Institutes of Health (F32 AG05869, R01AG18927)
This publication has 61 references indexed in Scilit:
- Alanine Scanning Mutagenesis of Aβ(1-40) Amyloid Fibril StabilityJournal of Molecular Biology, 2006
- 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
- Structure of the cross-β spine of amyloid-like fibrilsNature, 2005
- Structural properties of Aβ protofibrils stabilized by a small moleculeProceedings of the National Academy of Sciences, 2005
- Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid FibrilsScience, 2005
- Mechanism of Prion Propagation: Amyloid Growth Occurs by Monomer AdditionPLOS Biology, 2004
- Mapping Aβ Amyloid Fibril Secondary Structure Using Scanning Proline MutagenesisJournal of Molecular Biology, 2004
- Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolutionJournal of Molecular Medicine, 2003
- Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseasesNature, 2002