ライフサイエンスコーパス: normal prion protein

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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