Helices 2 and 3 are the initiation sites in the PrP(C) → PrP(SC) transition
about
The intrinsic helical propensities of the helical fragments in prion protein under neutral and low pH conditions: a replica exchange molecular dynamics study.Comparing the energy landscapes for native folding and aggregation of PrP.Caprine PrP variants harboring Asp-146, His-154 and Gln-211 alleles display reduced convertibility upon interaction with pathogenic murine prion protein in scrapie infected cells.Cofactor molecules induce structural transformation during infectious prion formation.In Vitro Approach To Identify Key Amino Acids in Low Susceptibility of Rabbit Prion Protein to Misfolding.Perturbations in inter-domain associations may trigger the onset of pathogenic transformations in PrP(C): insights from atomistic simulations.
P2860
Helices 2 and 3 are the initiation sites in the PrP(C) → PrP(SC) transition
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2012 nî lūn-bûn
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2012年の論文
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Helices 2 and 3 are the initiation sites in the PrP(C) → PrP(SC) transition
@ast
Helices 2 and 3 are the initiation sites in the PrP(C) → PrP(SC) transition
@en
type
label
Helices 2 and 3 are the initiation sites in the PrP(C) → PrP(SC) transition
@ast
Helices 2 and 3 are the initiation sites in the PrP(C) → PrP(SC) transition
@en
prefLabel
Helices 2 and 3 are the initiation sites in the PrP(C) → PrP(SC) transition
@ast
Helices 2 and 3 are the initiation sites in the PrP(C) → PrP(SC) transition
@en
P2860
P356
P1433
P1476
Helices 2 and 3 are the initiation sites in the PrP(C) → PrP(SC) transition
@en
P2093
D Thirumalai
P2860
P304
P356
10.1021/BI3005472
P407
P577
2012-12-31T00:00:00Z