M
Michael P. McKinley
Researcher at University of California, San Francisco
Publications - 54
Citations - 10880
Michael P. McKinley is an academic researcher from University of California, San Francisco. The author has contributed to research in topics: Scrapie & Amyloid. The author has an hindex of 35, co-authored 54 publications receiving 10713 citations.
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Journal ArticleDOI
A cellular gene encodes scrapie PrP 27-30 protein
Bruno Oesch,Bruno Oesch,David Westaway,Monika Wälchli,Monika Wälchli,Michael P. McKinley,Stephen B. H. Kent,Stephen B. H. Kent,Ruedi Aebersold,Ruedi Aebersold,Ronald A. Barry,Paul Tempst,Paul Tempst,David B. Teplow,David B. Teplow,Leroy Hood,Leroy Hood,Stanley B. Prusiner,Stanley B. Prusiner,Charles Weissmann,Charles Weissmann +20 more
TL;DR: A clone encoding PrP 27-30, the major protein in purified preparations of scrapie agent, was selected from a scrapie-infected hamster brain cDNA library by oligonucleotide probes corresponding to the N terminus of the protein.
Journal ArticleDOI
Identification of a protein that purifies with the scrapie prion.
TL;DR: Initial results suggest that the amount of this protein correlates with the titer of the agent, and the resistance of thisprotein to digestion by proteinase K distinguished it from proteins of similar molecular weight found in normal hamster brain.
Journal ArticleDOI
Scrapie prions aggregate to form amyloid-like birefringent rods
Stanley B. Prusiner,Michael P. McKinley,Karen A. Bowman,David C. Bolton,Paul E. Bendheim,Darlene Groth,George G. Glenner +6 more
TL;DR: The findings raise the possibility that the amyloid plaques observed in transmissible, degenerative neurological diseases might consist of prions, a polymeric form of the scrapie prion.
Journal ArticleDOI
A protease-resistant protein is a structural component of the Scrapie prion
TL;DR: Fractions purified from scrapie-infected hamster brain contain a unique protein, designated PrP, which is found to be directly proportional to the titer of the infectious prion.
Journal ArticleDOI
Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene
Konrad Basler,Bruno Oesch,Michael R. Scott,David Westaway,Monika Wälchli,Darlene Groth,Michael P. McKinley,Stanley B. Prusiner,Charles Weissmann +8 more
TL;DR: The primary structure of PrP encoded by the gene of a healthy animal does not differ from that encoded by a cDNA from a scrapie-infected animal, suggesting that the different properties ofPrP from normal and scrapie -infected brains are due to post-translational events.