Publication | Open Access
Control of Amyloid β‐Peptide Protofibril Formation by a Designed Template Assembly
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Citations
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2006
Year
Insight into amyloids: Four identical segments of the amyloid β-peptide, which is associated with Alzheimer's disease by fibril formation, were successfully attached to a cyclic decapeptide template. The assembly forms soluble protofibrils (see picture) that reveal a cross-β-sheet structure, with fast controllable kinetics and without a lag phase. Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2002/2006/z600395_s.pdf or from the author. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
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A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR Aneta T. Petkova, Yoshitaka Ishii, John J. Balbach, Proceedings of the National Academy of Sciences Biophysical ModelingProtein AssemblyMolecular Biology40-Residue Beta-amyloid PeptideExperimental Constraints | 2002 | 1.8K |
1999 | 1.4K | |
2005 | 1K | |
1994 | 402 | |
1999 | 342 | |
1995 | 339 | |
1995 | 116 | |
2003 | 114 |
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