Original paper

Role of the central lysine cluster and scrapie templating in the transmissibility of synthetic prion protein aggregates

Volume: 13, Issue: 9, Pages: e1006623 - e1006623
Published: Sep 14, 2017
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
Volume
13
Issue
9
Pages
e1006623 - e1006623
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