Original paper
Role of the central lysine cluster and scrapie templating in the transmissibility of synthetic prion protein aggregates
Abstract
Mammalian prion structures and replication mechanisms are poorly understood. Most synthetic recombinant prion protein (rPrP) amyloids prepared without cofactors are non-infectious or much less infectious than bona fide tissue-derived PrPSc. This effect has been associated with differences in folding of the aggregates, manifested in part by reduced solvent exclusion and protease-resistance in rPrP amyloids, especially within residues ~90–160....
Paper Details
Title
Role of the central lysine cluster and scrapie templating in the transmissibility of synthetic prion protein aggregates
Published Date
Sep 14, 2017
Journal
Volume
13
Issue
9
Pages
e1006623 - e1006623
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Notes
History