ライフサイエンスコーパス: normal prion protein

1 of PrP(Sc) misfolding at the expense of the normal prion protein.

2 ent evidence argues it is not due to loss of normal prion protein activity or direct toxic effects of

3 There is increasing evidence that the normal prion protein binds copper and the resulting comp

4 oid peptides with an elevated level of their normal prion protein dendritic receptor and of phospho-t

5 ormation than the reported structures of the normal prion protein determined in solution.

6 In addition to its role in the normal prion protein folding, this intermediate likely r

7 ain prion generation in vitro at expenses of normal prion proteins from various mammals and human, re

8 rative disorders caused by misfolding of the normal prion protein into an infectious cellular pathoge

9 n has identified two specific regions of the normal prion protein isoform that undergo a change in ch

10 A conformational variant of the normal prion protein PrP(C) is believed to be identical

11 How do the normal prion protein (PrP(C)) and infectious prion prote

12 by lipid interactions, given the location of normal prion protein (PrP(C)) in lipid rafts and lipid c

13 ated with the misfolding and accumulation of normal prion protein (PrP(C)) into its pathogenic scrapi

14 imals and that result from the conversion of normal prion protein (PrP(C)) into the misfolded prion p

15 in of infected individuals by converting the normal prion protein (PrP(C)) into the pathological isof

16 ent and the molecular mechanism by which the normal prion protein (PrP(C)) is converted into the abno

17 Converting normal prion protein (PrP(C)) to the pathogenic PrP(Sc)

18 Normal prion protein (PrP(c)), an essential substrate fo

19 ormational conversion and oligomerization of normal prion protein (PrP(C)).

20 ther proteins including a vast excess of the normal prion protein (PrP(C)).

21 d to a pathogenic conformer (PrP(Sc)) of the normal prion protein (PrP(C)).

22 rative disorders caused by misfolding of the normal prion protein (PrP) into a pathogenic "scrapie" c

23 The conversion of normal prion protein (PrP) into pathogenic PrP conformer

24 e transmissible spongiform encephalopathies, normal prion protein (PrP-sen) is converted to a proteas

25 strate that the amino-terminal domain of the normal prion protein, PrP(c), hinders seeded conversion

26 pathies is associated with the conversion of normal prion protein, PrP(C), into a misfolded, oligomer

27 ated with the conformational conversion of a normal prion protein, PrP(C), to a misfolded aggregated

28 ion disease, the templated misfolding of the normal prion protein, PrP(c), to a pathogenic, amyloid i

29 mmalian prion diseases involve conversion of normal prion protein, PrP(C), to a pathological aggregat

30 es are associated with the conversion of the normal prion protein, PrP(C), to the infectious disease

31 n replication involves the conversion of the normal prion protein (PrPC) into the misfolded isoform,

32 llmark of prion disease is the conversion of normal prion protein (PrPC) to an insoluble, proteinase

33 anti-scrapie activity and can interact with normal prion protein (PrPC).

34 However, there is also a normal prion protein that does not cause disease.

35 formers can self-propagate by converting the normal prion protein to the abnormal conformers that ind