Mechanism of Formation of Amyloid Protofibrils of Barstar from Soluble Oligomers: Evidence for Multiple Steps and Lateral Association Coupled to Conformational Conversion
- 20 January 2007
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 367 (4) , 1186-1204
- https://doi.org/10.1016/j.jmb.2007.01.039
Abstract
No abstract availableKeywords
This publication has 69 references indexed in Scilit:
- 3D structure of Alzheimer's amyloid-β(1–42) fibrilsProceedings of the National Academy of Sciences, 2005
- Molecular recycling within amyloid fibrilsNature, 2005
- Structure of the cross-β spine of amyloid-like fibrilsNature, 2005
- Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid FibrilsScience, 2005
- Core and Heterogeneity of β2-Microglobulin Amyloid Fibrils as Revealed by H/D ExchangeJournal of Molecular Biology, 2004
- Progress towards a molecular-level structural understanding of amyloid fibrilsCurrent Opinion in Structural Biology, 2004
- Aβ Protofibrils Possess a Stable Core Structure Resistant to Hydrogen ExchangeBiochemistry, 2003
- Amyloid as a natural productThe Journal of cell biology, 2003
- Mapping the core of the β2-microglobulin amyloid fibril by H/D exchangeNature Structural & Molecular Biology, 2002
- Common core structure of amyloid fibrils by synchrotron X-ray diffraction 1 1Edited by F. E. CohenJournal of Molecular Biology, 1997