about
PK-sensitive PrP is infectious and shares basic structural features with PK-resistant PrPUse of proteinase K nonspecific digestion for selective and comprehensive identification of interpeptide cross-links: application to prion proteins.Prion removal capacity of plasma protein manufacturing processes: a data collection from PPTA member companies.Neurodegeneration in humans caused by prionsDetection and analysis of animal materials in food and feed.Inactivation of prions by acidic sodium dodecyl sulfateEvaluation of a combinatorial approach to prion inactivation using an oxidizing agent, SDS, and proteinase K.Prion diseases: pathogenesis and public health concerns.Proteomics in neurodegenerative diseases: Methods for obtaining a closer look at the neuronal proteome.Spontaneous conversion of PrPC to PrPSc.Separation and properties of cellular and scrapie prion proteins.From slow virus to prion: a review of transmissible spongiform encephalopathies.Viroids and prions.Prions, proteinase K and infectivity.Molecular biology and pathology of scrapie and the prion diseases of humans.Molecular biology and transgenetics of prion diseases.Protease sensitivity and nuclease resistance of the scrapie agent propagated in vitro in neuroblastoma cellsBiogenesis and transmembrane orientation of the cellular isoform of the scrapie prion protein [published errratum appears in Mol Cell Biol 1987 May;7(5):2035]Detection and control of prion diseases in food animals.Has the virus of multiple sclerosis been isolated?The search for scrapie agent nucleic acidAnti-bovine prion protein RNA aptamer containing tandem GGA repeat interacts both with recombinant bovine prion protein and its beta isoform with high affinityPrion propagation: the role of protein dynamicsPrion liposomes.From prion diseases to prion-like propagation mechanisms of neurodegenerative diseases.Characterization and application of a novel RNA aptamer against the mouse prion protein.RNA aptamers specifically interact with the prion protein PrP.Bioassays and Inactivation of Prions.Structural Biology of PrP Prions.Misfolding pathways of the prion protein probed by molecular dynamics simulations.The genetics and transgenetics of human prion disease.Evidence suggesting that PrP is not the infectious agent in Creutzfeldt-Jakob disease.Inactivation of the scrapie agent by pronase.Protease-resistant and detergent-insoluble prion protein is not necessarily associated with prion infectivity.The prion diseases: Creutzfeldt-Jakob, Gerstmann-Sträussler-Scheinker, and related disorders.Ionic strength and transition metals control PrPSc protease resistance and conversion-inducing activity.Resistance of the scrapie agent to inactivation by psoralens.A Method to Perform Western Blots of Microscopic Areas of Histological Sections
P2860
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P2860
description
1981 nî lūn-bûn
@nan
1981年の論文
@ja
1981年学术文章
@wuu
1981年学术文章
@zh-cn
1981年学术文章
@zh-hans
1981年学术文章
@zh-my
1981年学术文章
@zh-sg
1981年學術文章
@yue
1981年學術文章
@zh
1981年學術文章
@zh-hant
name
Scrapie agent contains a hydrophobic protein
@ast
Scrapie agent contains a hydrophobic protein
@en
type
label
Scrapie agent contains a hydrophobic protein
@ast
Scrapie agent contains a hydrophobic protein
@en
prefLabel
Scrapie agent contains a hydrophobic protein
@ast
Scrapie agent contains a hydrophobic protein
@en
P2093
P2860
P356
P1476
Scrapie agent contains a hydrophobic protein
@en
P2093
F R Masiarz
K A Bowman
M P McKinley
S P Cochran
P2860
P304
P356
10.1073/PNAS.78.11.6675
P407
P577
1981-11-01T00:00:00Z