Amyloid Fibrillogenesis
Amyloid Fibrillogenesis is a biochemical process defined as the pathogenic self-assembly of misfolded proteins into highly ordered, insoluble fibrillar aggregates characterized by a cross-β sheet quaternary structure, distinct from other protein aggregation mechanisms by its specific structural morphology and resistance to degradation.
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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
Amyloid β-peptide is produced by cultured cells during normal metabolism
Christian Haass, Michael G. Schlossmacher, Albert Y. Hung et al. · Nature · 1992 · 1.9K citations
Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein
Bart De Strooper, Paul Säftig, Katleen Craessaerts et al. · Nature · 1998 · 1.8K citations
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Harvard University
Cambridge, United States
57 h-index
293 publications
95.5K citations
University of Cambridge
Cambridge, United Kingdom
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309 publications
44.3K citations
National Institutes of Health
Bethesda, United States
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217 publications
34.7K citations

Centre National de la Recherche Scientifique
Paris, France
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342 publications
18.2K citations

Brigham and Women's Hospital
Boston, United States
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152 publications
64.4K citations
New York University
New York, United States
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210 publications
29K citations
The University of Osaka
Osaka, Japan
39 h-index
309 publications
19.5K citations
University of Fukui
Fukui-shi, Japan
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JBC · 238 publications · 29.1K citations
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PNAS · 123 publications · 33.2K citations
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JMB · 141 publications · 14K citations
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BBRC · 103 publications · 8.7K citations
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