Overexpression of nonconvertible PrPc delta114-121 in scrapie-infected mouse neuroblastoma cells leads to trans-dominant inhibition of wild-type PrP(Sc) accumulation.
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Intracellular re-routing of prion protein prevents propagation of PrP(Sc) and delays onset of prion diseaseα-Cleavage of cellular prion proteinProbing the role of structural features of mouse PrP in yeast by expression as Sup35-PrP fusionsCritical significance of the region between Helix 1 and 2 for efficient dominant-negative inhibition by conversion-incompetent prion proteinEnhanced stability of human prion proteins with two disulfide bridges.Lethal recessive myelin toxicity of prion protein lacking its central domain.Mapping of possible prion protein self-interaction domains using peptide arraysDeletion of beta-strand and alpha-helix secondary structure in normal prion protein inhibits formation of its protease-resistant isoform.Multiple amino acid residues within the rabbit prion protein inhibit formation of its abnormal isoformA bovine cell line that can be infected by natural sheep scrapie prions.A naturally occurring C-terminal fragment of the prion protein (PrP) delays disease and acts as a dominant-negative inhibitor of PrPSc formation.Ion channels induced by the prion protein: mediators of neurotoxicity.Role of prion protein aggregation in neurotoxicity.Dodecylphosphocholine Micelles Induce Amyloid Formation of the PrP(110-136) Peptide via an α-Helical Metastable Conformation.Detection and partial discrimination of atypical and classical bovine spongiform encephalopathies in cattle and primates using real-time quaking-induced conversion assay.Nucleation-dependent conformational conversion of the Y145Stop variant of human prion protein: structural clues for prion propagation.Cellular prion protein: from physiology to pathology.Generating Bona Fide Mammalian Prions with Internal DeletionsThe region approximately between amino acids 81 and 137 of proteinase K-resistant PrPSc is critical for the infectivity of the Chandler prion strain.Pathogenic mutations within the hydrophobic domain of the prion protein lead to the formation of protease-sensitive prion species with increased lethality.The structure of human prions: from biology to structural models-considerations and pitfalls.The paraffin-embedded tissue blot detects PrP(Sc) early in the incubation time in prion diseases.Aberrant ERK 1/2 complex activation and localization in scrapie-infected GT1-1 cells.Stress-protective signalling of prion protein is corrupted by scrapie prions.The CNS glycoprotein Shadoo has PrP(C)-like protective properties and displays reduced levels in prion infections.Destabilizing polymorphism in cervid prion protein hydrophobic core determines prion conformation and conversion efficiency.Cofactor molecules induce structural transformation during infectious prion formation.Conserved amyloid core structure of stop mutants of the human prion protein.Burial of the polymorphic residue 129 in amyloid fibrils of prion stop mutantsPrion-like characteristics of the bacterial protein Microcin E492.Specific binding of normal prion protein to the scrapie form via a localized domain initiates its conversion to the protease-resistant state.Design of metastable β-sheet oligomers from natively unstructured peptide.PrPSc-like prion protein peptide inhibits the function of cellular prion protein.Interaction of Peptide Aptamers with Prion Protein Central Domain Promotes α-Cleavage of PrPC.
P2860
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P2860
Overexpression of nonconvertible PrPc delta114-121 in scrapie-infected mouse neuroblastoma cells leads to trans-dominant inhibition of wild-type PrP(Sc) accumulation.
description
1998 nî lūn-bûn
@nan
1998 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Overexpression of nonconvertib ...... nt inhibition of wild-type PrP
@nl
Overexpression of nonconvertib ...... ild-type PrP(Sc) accumulation.
@ast
Overexpression of nonconvertib ...... ild-type PrP(Sc) accumulation.
@en
type
label
Overexpression of nonconvertib ...... nt inhibition of wild-type PrP
@nl
Overexpression of nonconvertib ...... ild-type PrP(Sc) accumulation.
@ast
Overexpression of nonconvertib ...... ild-type PrP(Sc) accumulation.
@en
prefLabel
Overexpression of nonconvertib ...... nt inhibition of wild-type PrP
@nl
Overexpression of nonconvertib ...... ild-type PrP(Sc) accumulation.
@ast
Overexpression of nonconvertib ...... ild-type PrP(Sc) accumulation.
@en
P2093
P2860
P1433
P1476
Overexpression of nonconvertib ...... ild-type PrP(Sc) accumulation.
@en
P2093
P2860
P304
P407
P577
1998-02-01T00:00:00Z