Low density subcellular fractions enhance disease-specific prion protein misfolding.
about
Is tau ready for admission to the prion club?Complex folding and misfolding effects of deer-specific amino acid substitutions in the β2-α2 loop of murine prion protein.In vitro amplification of misfolded prion protein using lysate of cultured cells.Dissociation of infectivity from seeding ability in prions with alternate docking mechanism.Defining sporadic Creutzfeldt-Jakob disease strains and their transmission properties.Na+/K+-ATPase is present in scrapie-associated fibrils, modulates PrP misfolding in vitro and links PrP function and dysfunction.Monoacylated cellular prion protein modifies cell membranes, inhibits cell signaling, and reduces prion formation.The glycosylation status of PrPC is a key factor in determining transmissible spongiform encephalopathy transmission between speciesPrP aggregation can be seeded by pre-formed recombinant PrP amyloid fibrils without the replication of infectious prionsStructural requirements for efficient prion protein conversion: cofactors may promote a conversion-competent structure for PrP(C).The cellular prion protein with a monoacylated glycosylphosphatidylinositol anchor modifies cell membranes, inhibits cell signaling and reduces prion formation.Complement protein C1q forms a complex with cytotoxic prion protein oligomers
P2860
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P2860
Low density subcellular fractions enhance disease-specific prion protein misfolding.
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Low density subcellular fractions enhance disease-specific prion protein misfolding.
@ast
Low density subcellular fractions enhance disease-specific prion protein misfolding.
@en
type
label
Low density subcellular fractions enhance disease-specific prion protein misfolding.
@ast
Low density subcellular fractions enhance disease-specific prion protein misfolding.
@en
prefLabel
Low density subcellular fractions enhance disease-specific prion protein misfolding.
@ast
Low density subcellular fractions enhance disease-specific prion protein misfolding.
@en
P2093
P2860
P356
P1476
Low density subcellular fractions enhance disease-specific prion protein misfolding.
@en
P2093
Andrew C Gill
Dominic Kurian
James F Graham
Louise Kirby
Sonya Agarwal
Teresa J T Pinheiro
P2860
P304
P356
10.1074/JBC.M109.093484
P407
P577
2010-01-27T00:00:00Z