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1 e and proteinase K resistant particle of the scrapie prion.
2 interaction and assembly into the amyloid of scrapie prion.
3 isease when infected i.p. with mouse-adapted scrapie prions.
4 force-fed material infected with RML-strain scrapie prions.
5 P) mice were inoculated intracerebrally with scrapie prions.
6 dent brain are not altered by infection with scrapie prions.
7 ma cells that are persistently infected with scrapie prions.
8 in cultured cells persistently infected with scrapie prions.
9 ose seen in these mice injected with natural scrapie prions.
10 ffect on the survival of those infected with scrapie prions.
11 chronic wasting disease, and hamster-adapted scrapie prions.
12 uli beginning 49 days after inoculation with scrapie prions and reached a level 2.5 times normal by d
13 ified that can be persistently infected with scrapie prions, and none of these cells show cytopatholo
14 n formation when seeded by minute amounts of scrapie prions in vitro Surprisingly, combination of the
15 expression exposed to classical or atypical scrapie prion inocula showed a faster decrease in locomo
16 These data demonstrate that orally available scrapie prions may be a common feature in sheep incubati
17 s, a protease-resistant ordered aggregate of scrapie prion protein (PrP(Sc)) accumulates in affected
20 ave studied the modulation of the HSR by the scrapie prion protein (PrP(Sc)) and amyloid beta peptide
21 disease would show a phenotype including the scrapie prion protein (PrP(Sc)) features that differ fro
23 f either one of the two protease K-resistant scrapie prion protein (PrP(Sc)) types identified as 1 an
24 of a misfolded, beta-sheet-enriched isoform (scrapie prion protein (PrP(Sc))) of the cellular prion p
25 s often seen without obvious deposits of the scrapie prion protein (PrP(Sc)), the principal cause of
26 the molecular mass of the protease-resistant scrapie prion protein (PrP(Sc)), which can be type 1 or
30 ly, component of the infectious prion is the scrapie prion protein (PrPSc); the protease resistant co
34 n, PrP(c), to a pathogenic, amyloid isoform, scrapie prion protein, PrP(Sc) We examined the role of t
35 Molecular dynamics simulation produces a scrapie prion protein-like conformation enriched in beta
37 ction with any one of three strains of mouse scrapie prion (PrPSc), 139A, ME7, or 22L, results in the
39 la are susceptible to classical and atypical scrapie prion strains and highlight the utility of this
40 ce that were intracerebrally challenged with scrapie prions succumbed to disease with a mean incubati
41 ed no transmission barrier for Suffolk sheep scrapie prions, suggesting that cattle may be highly sus
42 prions were similar, the stability of sheep scrapie prions was higher than that found for the BSE pr
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