Immobilized prion protein undergoes spontaneous rearrangement to a conformation having features in common with the infectious form.
about
S100B and S100A6 differentially modulate cell survival by interacting with distinct RAGE (receptor for advanced glycation end products) immunoglobulin domainsThe octarepeat region of the prion protein is conformationally altered in PrP(Sc)Tetracysteine-tagged prion protein allows discrimination between the native and converted formsEffects of beta-sheet breaker peptide polymers on scrapie-infected mouse neuroblastoma cells and their affinities to prion protein fragment PrP(81-145).Bovine PrPC directly interacts with alphaB-crystalline.Prion and doppel proteins bind to granule cells of the cerebellumQuaternary structure of pathological prion protein as a determining factor of strain-specific prion replication dynamics.Phosphorothioate oligonucleotides reduce PrP levels and prion infectivity in cultured cells.Mouse prion protein (PrP) segment 100 to 104 regulates conversion of PrP(C) to PrP(Sc) in prion-infected neuroblastoma cells.Role of ADAMs in the ectodomain shedding and conformational conversion of the prion protein.Different immunoreactivity against monoclonal antibodies between wild-type and mutant copper/zinc superoxide dismutase linked to amyotrophic lateral sclerosis.Dual mechanisms for shedding of the cellular prion protein.Vitamin D 2 interacts with Human PrP(c) (90-231) and breaks PrP(c) oligomerization in vitro.Polymorphisms at amino acid residues 141 and 154 influence conformational variation in ovine PrP.Green fluorescent protein as a reporter of prion protein folding.A nanoparticle-based immobilization assay for prion-kinetics study.Acidic pH and detergents enhance in vitro conversion of human brain PrPC to a PrPSc-like form.Proteinaceous infectious behavior in non-pathogenic proteins is controlled by molecular chaperones.Antibodies inhibit prion propagation and clear cell cultures of prion infectivity.Detection of prion epitopes on PrP and PrP of transmissible spongiform encephalopathies using specific monoclonal antibodies to PrP.A de novo designed template for generating conformation-specific antibodies that recognize alpha-helices in proteins.Probing the conformation of the prion protein within a single amyloid fibril using a novel immunoconformational assay.
P2860
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P2860
Immobilized prion protein undergoes spontaneous rearrangement to a conformation having features in common with the infectious form.
description
2001 nî lūn-bûn
@nan
2001 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Immobilized prion protein unde ...... ommon with the infectious form
@nl
Immobilized prion protein unde ...... mmon with the infectious form.
@ast
Immobilized prion protein unde ...... mmon with the infectious form.
@en
type
label
Immobilized prion protein unde ...... ommon with the infectious form
@nl
Immobilized prion protein unde ...... mmon with the infectious form.
@ast
Immobilized prion protein unde ...... mmon with the infectious form.
@en
prefLabel
Immobilized prion protein unde ...... ommon with the infectious form
@nl
Immobilized prion protein unde ...... mmon with the infectious form.
@ast
Immobilized prion protein unde ...... mmon with the infectious form.
@en
P2093
P2860
P356
P1433
P1476
Immobilized prion protein unde ...... mmon with the infectious form.
@en
P2093
D R Burton
R A Williamson
P2860
P304
P356
10.1093/EMBOJ/20.7.1547
P407
P577
2001-04-01T00:00:00Z