PrP assemblies: spotting the responsible regions in prion propagation.
about
Techniques to elucidate the conformation of prionsIntegrity of helix 2-helix 3 domain of the PrP protein is not mandatory for prion replication.Polymorphism at 129 dictates metastable conformations of the human prion protein N-terminal β-sheet.The mechanism of monomer transfer between two structurally distinct PrP oligomersCaprine 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.The part of a long beta hairpin from the scrapie form of the human prion protein is reconstructed in the synthetic CC36 protein.Monitoring Conformational Landscape of Ovine Prion Protein Monomer Using Ion Mobility Coupled to Mass Spectrometry.In Vitro Approach To Identify Key Amino Acids in Low Susceptibility of Rabbit Prion Protein to Misfolding.
P2860
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P2860
PrP assemblies: spotting the responsible regions in prion propagation.
description
2011 nî lūn-bûn
@nan
2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
PrP assemblies: spotting the responsible regions in prion propagation.
@ast
PrP assemblies: spotting the responsible regions in prion propagation.
@en
type
label
PrP assemblies: spotting the responsible regions in prion propagation.
@ast
PrP assemblies: spotting the responsible regions in prion propagation.
@en
prefLabel
PrP assemblies: spotting the responsible regions in prion propagation.
@ast
PrP assemblies: spotting the responsible regions in prion propagation.
@en
P2860
P356
P1433
P1476
PrP assemblies: spotting the responsible regions in prion propagation.
@en
P2093
Human Rezaei
Stéphanie Prigent
P2860
P356
10.4161/PRI.5.2.16383
P577
2011-04-01T00:00:00Z