Role of the highly conserved middle region of prion protein (PrP) in PrP-lipid interaction
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Intraperitoneal Infection of Wild-Type Mice with Synthetically Generated Mammalian PrionPrion Protein Prolines 102 and 105 and the Surrounding Lysine Cluster Impede Amyloid Formation.Dissociation of infectivity from seeding ability in prions with alternate docking mechanism.Comparison of 2 synthetically generated recombinant prions.Lipopolysaccharide induced conversion of recombinant prion protein.A C-terminal membrane anchor affects the interactions of prion proteins with lipid membranes.Neutron reflectometry studies define prion protein N-terminal peptide membrane bindingCyclin-dependent kinase 5 phosphorylation of familial prion protein mutants exacerbates conversion into amyloid structure.PrP assemblies: spotting the responsible regions in prion propagation.A micellar on-pathway intermediate step explains the kinetics of prion amyloid formationContrasting Effects of Two Lipid Cofactors of Prion Replication on the Conformation of the Prion ProteinDetergents modify proteinase K resistance of PrP Sc in different transmissible spongiform encephalopathies (TSEs).Structural transitions in full-length human prion protein detected by xenon as probe and spin labeling of the N-terminal domain.Proline and lysine residues provide modulatory switches in amyloid formation: Insights from prion protein.De novo generation of infectious prions with bacterially expressed recombinant prion protein.Prion nucleation site unmasked by transient interaction with phospholipid cofactor.Role of lipid in forming an infectious prion?Melanin or a Melanin-Like Substance Interacts with the N-Terminal Portion of Prion Protein and Inhibits Abnormal Prion Protein Formation in Prion-Infected Cells.Unique structural properties associated with mouse prion Δ105-125 protein.Role of the central lysine cluster and scrapie templating in the transmissibility of synthetic prion protein aggregates.PrP P102L and nearby lysine mutations promote spontaneous in vitro formation of transmissible prions.Destabilizing polymorphism in cervid prion protein hydrophobic core determines prion conformation and conversion efficiency.Self-propagating, protease-resistant, recombinant prion protein conformers with or without in vivo pathogenicity.Simulations of membrane-bound diglycosylated human prion protein reveal potential protective mechanisms against misfolding.Cofactor molecules induce structural transformation during infectious prion formation.Effect of surfactant hydrophobicity on the pathway for unfolding of ubiquitin.Localization of A11-reactive oligomeric species in prion diseases.Prion protein inhibits fast axonal transport through a mechanism involving casein kinase 2.Interaction of Peptide Aptamers with Prion Protein Central Domain Promotes α-Cleavage of PrPC.Prion Diseases.
P2860
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P2860
Role of the highly conserved middle region of prion protein (PrP) in PrP-lipid interaction
description
2010 nî lūn-bûn
@nan
2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի սեպտեմբերին 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
Role of the highly conserved m ...... (PrP) in PrP-lipid interaction
@ast
Role of the highly conserved m ...... (PrP) in PrP-lipid interaction
@en
Role of the highly conserved middle region of prion protein
@nl
type
label
Role of the highly conserved m ...... (PrP) in PrP-lipid interaction
@ast
Role of the highly conserved m ...... (PrP) in PrP-lipid interaction
@en
Role of the highly conserved middle region of prion protein
@nl
prefLabel
Role of the highly conserved m ...... (PrP) in PrP-lipid interaction
@ast
Role of the highly conserved m ...... (PrP) in PrP-lipid interaction
@en
Role of the highly conserved middle region of prion protein
@nl
P2093
P2860
P356
P1433
P1476
Role of the highly conserved m ...... (PrP) in PrP-lipid interaction
@en
P2093
P2860
P304
P356
10.1021/BI101146V
P407
P577
2010-09-01T00:00:00Z