A 7-kDa prion protein (PrP) fragment, an integral component of the PrP region required for infectivity, is the major amyloid protein in Gerstmann-Sträussler-Scheinker disease A117V.
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Gerstmann-Sträussler-Scheinker disease amyloid protein polymerizes according to the "dock-and-lock" modelTransmissibility of atypical scrapie in ovine transgenic mice: major effects of host prion protein expression and donor prion genotypeSmall ruminant nor98 prions share biochemical features with human gerstmann-sträussler-scheinker disease and variably protease-sensitive prionopathyA Drosophila model of GSS syndrome suggests defects in active zones are responsible for pathogenesis of GSS syndrome.Tetracyclines affect prion infectivity.The expanding universe of prion diseases.Diversity in neuroanatomical distribution of abnormal prion protein in atypical scrapieEvidence for a pathogenic role of different mutations at codon 188 of PRNPImmunopurification of pathological prion protein aggregatesLive cell fluorescence resonance energy transfer predicts an altered molecular association of heterologous PrPSc with PrPC.Atypical scrapie isolates involve a uniform prion species with a complex molecular signature.Metabolism of minor isoforms of prion proteins: Cytosolic prion protein and transmembrane prion proteinMolecular pathology of human prion disease.Review: contribution of transgenic models to understanding human prion disease.Comparative Study of Prions in Iatrogenic and Sporadic Creutzfeldt-Jakob Disease.Inherited prion disease A117V is not simply a proteinopathy but produces prions transmissible to transgenic mice expressing homologous prion protein.Familial prion disease with Alzheimer disease-like tau pathology and clinical phenotype.A case of Gerstmann-Sträussler-Scheinker disease with a novel six octapeptide repeat insertion.Prion (PrPres) allotypes profiling: a new perspectives from mass spectrometry.Nucleation-dependent conformational conversion of the Y145Stop variant of human prion protein: structural clues for prion propagation.Molecular conformation and dynamics of the Y145Stop variant of human prion protein in amyloid fibrilsProtease-sensitive prions with 144-bp insertion mutationsH-type bovine spongiform encephalopathy: complex molecular features and similarities with human prion diseasesA novel PRNP-P105S mutation associated with atypical prion disease and a rare PrPSc conformationSimilar biochemical signatures and prion protein genotypes in atypical scrapie and Nor98 cases, France and NorwayA New Transgenic Mouse Model of Gerstmann-Straussler-Scheinker Syndrome Caused by the A117V Mutation of PRNP.Prion protein misfolding, strains, and neurotoxicity: an update from studies on Mammalian prions.Amyloid fibrils from the N-terminal prion protein fragment are infectious.Mechanism of PrP-amyloid formation in mice without transmissible spongiform encephalopathy.Generation of a new infectious recombinant prion: a model to understand Gerstmann-Sträussler-Scheinker syndrome.Prion peptide induces neuronal cell death through a pathway involving glycogen synthase kinase 3Prion proteins with different conformations accumulate in Gerstmann-Sträussler-Scheinker disease caused by A117V and F198S mutations.Fate of pathological prion (PrP(sc)92-138) in soil and water: prion-clay nanoparticle molecular dynamics.Identification of novel proteinase K-resistant C-terminal fragments of PrP in Creutzfeldt-Jakob disease.Translational Research in Alzheimer's and Prion Diseases.Structural properties of Gerstmann-Straussler-Scheinker disease amyloid protein.Methods for Molecular Diagnosis of Human Prion Disease.Recombinant PrPSc shares structural features with brain-derived PrPSc: Insights from limited proteolysis.A novel Gerstmann-Sträussler-Scheinker disease mutation defines a precursor for amyloidogenic 8 kDa PrP fragments and reveals N-terminal structural changes shared by other GSS alleles.Flexible N-terminal region of prion protein influences conformation of protease-resistant prion protein isoforms associated with cross-species scrapie infection in vivo and in vitro.
P2860
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P2860
A 7-kDa prion protein (PrP) fragment, an integral component of the PrP region required for infectivity, is the major amyloid protein in Gerstmann-Sträussler-Scheinker disease A117V.
description
2000 nî lūn-bûn
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2000年の論文
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2000年学术文章
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2000年学术文章
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2000年学术文章
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name
A 7-kDa prion protein (PrP) fr ...... ssler-Scheinker disease A117V.
@en
A 7-kDa prion protein (PrP) fr ...... ssler-Scheinker disease A117V.
@nl
type
label
A 7-kDa prion protein (PrP) fr ...... ssler-Scheinker disease A117V.
@en
A 7-kDa prion protein (PrP) fr ...... ssler-Scheinker disease A117V.
@nl
prefLabel
A 7-kDa prion protein (PrP) fr ...... ssler-Scheinker disease A117V.
@en
A 7-kDa prion protein (PrP) fr ...... ssler-Scheinker disease A117V.
@nl
P2093
P2860
P356
P1476
A 7-kDa prion protein (PrP) fr ...... ssler-Scheinker disease A117V.
@en
P2093
B Frangione
C Tranchant
F Tagliavini
G Giaccone
J M Warter
P2860
P304
P356
10.1074/JBC.M007062200
P407
P577
2000-11-21T00:00:00Z