Amyloid Fibrils
Amyloid Fibrils is a highly ordered, insoluble protein aggregate structure composed of misfolded polypeptides arranged in a cross-β-sheet conformation, distinguished from other protein aggregates by its characteristic fibrillar morphology, β-strand alignment perpendicular to the fibril axis, and resistance to proteolytic degradation.
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Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis
Rakez Kayed, Elizabeth Head, Jennifer L. Thompson et al. · Science · 2003 · 4.1K citations
Consort 2010 statement: extension to cluster randomised trials
Marion Campbell, Gilda Piaggio, Diana R Elbourne et al. · BMJ · 2012 · 3.6K citations · Full text
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University of California, Los Angeles, United States
84 publications · 18.7K citations
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University of Cambridge
Cambridge, United Kingdom
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Harvard University
Cambridge, United States
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806 publications
191.2K citations

Brigham and Women's Hospital
Boston, United States
87 h-index
506 publications
140K citations
University of California, Los Angeles
Los Angeles, United States
84 h-index
723 publications
122.5K citations
National Institutes of Health
Bethesda, United States
84 h-index
630 publications
105.5K citations
ETH Zurich
Zurich, Switzerland
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849 publications
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New York University
New York, United States
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Howard Hughes Medical Institute
Chevy Chase, United States
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480 publications
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PNAS · 409 publications · 107K citations
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JBC · 546 publications · 72.3K citations
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JACS · 291 publications · 29.4K citations
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JMB · 270 publications · 29.7K citations
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