Amyloid Fibril Structure
Amyloid Fibril Structure is a structural biology construct that refers to the highly ordered, β-sheet-rich, filamentous protein aggregate morphology characterized by its insolubility, resistance to proteolysis, and specific cross-β architecture, distinguishing it from other protein folding states such as native globular or amorphous aggregates.
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Consort 2010 statement: extension to cluster randomised trials
Marion Campbell, Gilda Piaggio, Diana R Elbourne et al. · BMJ · 2012 · 3.6K citations · Full text
Atomic structures of amyloid cross-β spines reveal varied steric zippers
M.R. Sawaya, Shilpa Sambashivan, Rebecca A. Nelson et al. · Nature · 2007 · 2.3K citations
Structure of the cross-β spine of amyloid-like fibrils
Rebecca A. Nelson, M.R. Sawaya, Melinda Balbirnie et al. · Nature · 2005 · 2.2K citations · Full text
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National Institute of Diabetes and Digestive and Kidney Diseases, United States
39 publications · 13.2K citations
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University of Cambridge
Cambridge, United Kingdom
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359 publications
50.7K citations
National Institutes of Health
Bethesda, United States
51 h-index
255 publications
65K citations
ETH Zurich
Zurich, Switzerland
47 h-index
308 publications
36.1K citations

Centre National de la Recherche Scientifique
Paris, France
44 h-index
329 publications
21.4K citations
National Institute of Diabetes and Digestive and Kidney Diseases
Bethesda, United States
39 h-index
156 publications
63.1K citations

Howard Hughes Medical Institute
Chevy Chase, United States
39 h-index
204 publications
61K citations
Massachusetts Institute of Technology
Cambridge, United States
37 h-index
202 publications
33K citations
The University of Osaka
Osaka, Japan
34 h-index
211 publications
14.3K citations
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PNAS · 106 publications · 24.3K citations
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JMB · 120 publications · 13.3K citations
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JACS · 102 publications · 10.6K citations
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JBC · 123 publications · 10.6K citations
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