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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 in cultured cells persistently infected with scrapie prions.
8 ose seen in these mice injected with natural scrapie prions.
9 ma cells that are persistently infected with 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                 Similar effects were seen in scrapie prion-exposed ovine PrP Drosophila with modified
15 Sc in any of the WTD inoculated with classic scrapie prions from goats.
16 n formation when seeded by minute amounts of scrapie prions in vitro Surprisingly, combination of the
17  expression exposed to classical or atypical scrapie prion inocula showed a faster decrease in locomo
18 These data demonstrate that orally available scrapie prions may be a common feature in sheep incubati
19 s, a protease-resistant ordered aggregate of scrapie prion protein (PrP(Sc)) accumulates in affected
20                               The pattern of scrapie prion protein (PrP(Sc)) accumulation in the brai
21            The delay could relate to reduced scrapie prion protein (PrP(Sc)) accumulation on follicul
22 ave studied the modulation of the HSR by the scrapie prion protein (PrP(Sc)) and amyloid beta peptide
23 disease would show a phenotype including the scrapie prion protein (PrP(Sc)) features that differ fro
24              Because the insolubility of the scrapie prion protein (PrP(Sc)) has frustrated structura
25 f either one of the two protease K-resistant scrapie prion protein (PrP(Sc)) types identified as 1 an
26 of a misfolded, beta-sheet-enriched isoform (scrapie prion protein (PrP(Sc))) of the cellular prion p
27 s often seen without obvious deposits of the scrapie prion protein (PrP(Sc)), the principal cause of
28 the molecular mass of the protease-resistant scrapie prion protein (PrP(Sc)), which can be type 1 or
29 ive disorders characterized by deposition of scrapie prion protein (PrPSc) in the CNS.
30                                          The scrapie prion protein (PrPSc) is formed from the cellula
31                                          The scrapie prion protein (PrPSc) is the major, and possibly
32 ly, component of the infectious prion is the scrapie prion protein (PrPSc); the protease resistant co
33                                              Scrapie prion protein is a misfolded and aggregated form
34                                          The scrapie prion protein isoform, PrPSc, is a prion-associa
35 he infectious protease-resistant core of the scrapie prion protein PrPSc.
36 ally detect BSE, even within the presence of scrapie prion protein, are required.
37 n, PrP(c), to a pathogenic, amyloid isoform, scrapie prion protein, PrP(Sc) We examined the role of t
38     Molecular dynamics simulation produces a scrapie prion protein-like conformation enriched in beta
39 en 6 and 10 wk postinoculation (w.p.i.) with scrapie prion protein.
40            Limited proteolysis of infectious scrapie prions PrP(Sc) yields an N-truncated polypeptide
41 ction with any one of three strains of mouse scrapie prion (PrPSc), 139A, ME7, or 22L, results in the
42                  Tg(C1) mice inoculated with scrapie prions remain healthy and do not accumulate prot
43 la are susceptible to classical and atypical scrapie prion strains and highlight the utility of this
44 ral changes in PrP(D) from two mouse-adapted scrapie prion strains, 22L and 87V, influenced processin
45 ce that were intracerebrally challenged with scrapie prions succumbed to disease with a mean incubati
46 ed no transmission barrier for Suffolk sheep scrapie prions, suggesting that cattle may be highly sus
47 ice culture assay for sensitive detection of scrapie prions using ultrasensitive prion seeding.
48  prions were similar, the stability of sheep scrapie prions was higher than that found for the BSE pr
49 at found for the BSE prions but lower if the scrapie prions were passaged in Tg(BoPrP) mice.