F
Frederick Cohen
Researcher at Genentech
Publications - 106
Citations - 7715
Frederick Cohen is an academic researcher from Genentech. The author has contributed to research in topics: Protein structure & Scrapie. The author has an hindex of 42, co-authored 104 publications receiving 7355 citations. Previous affiliations of Frederick Cohen include University of California, Irvine & National Institutes of Health.
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Journal ArticleDOI
Structural studies of the scrapie prion protein by electron crystallography
Holger Wille,Melissa D. Michelitsch,Vincent Guénebaut,Surachai Supattapone,Ana Serban,Frederick Cohen,David A. Agard,Stanley B. Prusiner +7 more
TL;DR: In this paper, the structure of two infectious variants of the scrapie prion protein (PrP(Sc)) was characterized using electron crystallography. But the results were limited to 7 A resolution.
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Pathway complexity of prion protein assembly into amyloid.
TL;DR: To study the kinetic pathways of amyloid formation in vitro, unglycosylated recombinant PrP corresponding to the proteinase K-resistant core of PrPSc is used and it is found that it can adopt two non-native abnormal isoforms, a β-oligomer and anAmyloid fibril.
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Predicted alpha-helical regions of the prion protein when synthesized as peptides form amyloid.
María Gasset,Michael A. Baldwin,David H. Lloyd,Jean-Marc Gabriel,David M. Holtzman,Frederick Cohen,Robert J. Fletterick,Stanley B. Prusiner +7 more
TL;DR: The findings suggest the possibility that the conversion of the cellular isoform of PrP to the scrapie iso Form involves the transition of one or more putative PrP alpha-helices into beta-sheets and that prion diseases are disorders of protein conformation.
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Identification of the Cu2+ Binding Sites in the N-Terminal Domain of the Prion Protein by EPR and CD Spectroscopy
Eliah Aronoff-Spencer,Colin S. Burns,Nikolai I. Avdievich,Gary J. Gerfen,Jack Peisach,William E. Antholine,Haydn L. Ball,Frederick Cohen,Stanley B. Prusiner,Glenn L. Millhauser +9 more
TL;DR: A model consistent with these data is proposed in which Cu(2+) is bound to the nitrogen of the histidine imidazole side chain and to two nitrogens from sequential glycine backbone amides.
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Elimination of prions by branched polyamines and implications for therapeutics
Surachai Supattapone,Hoang-Oanh B. Nguyen,Frederick Cohen,Stanley B. Prusiner,Michael R. Scott +4 more
TL;DR: Branched polyamines, including polyamidoamide dendimers, polypropyleneimine, and polyethyleneimine are able to purge PrP(Sc), the protease-resistant isoform of the prion protein, from scrapie-infected neuroblastoma (ScN2a) cells in culture.