about
Microdissection: a method developed to investigate mechanisms involved in transmissible spongiform encephalopathy pathogenesisMultifaceted Role of Sialylation in Prion DiseasesSialylation of prion protein controls the rate of prion amplification, the cross-species barrier, the ratio of PrPSc glycoform and prion infectivityDistinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy.Glycosylation differences between the normal and pathogenic prion protein isoformsPrions adhere to soil minerals and remain infectiousTwo alleles of a neural protein gene linked to scrapie in sheep.In vitro expression in eukaryotic cells of a prion protein gene cloned from scrapie-infected mouse brain.Attempts to convert the cellular prion protein into the scrapie isoform in cell-free systems.Sparse PrP(Sc) accumulation in the placentas of goats with naturally acquired scrapie.The molecular mechanisms of scrapie encephalopathy and relevance to human neurodegenerative disease.NMR structure of the bovine prion protein isolated from healthy calf brains.Tubulofilaments in negatively stained scrapie-infected brains: relationship to scrapie-associated fibrils.Purified prion proteins and scrapie infectivity copartition into liposomes.Initial fate of prions upon peripheral infection: half-life, distribution, clearance, and tissue uptake.Infectious prion protein alters manganese transport and neurotoxicity in a cell culture model of prion disease.A 54-kDa normal cellular protein may be the precursor of the scrapie agent protease-resistant protein.Separation and properties of cellular and scrapie prion proteins.Etiology and pathogenesis of prion diseases.Scrapie prion proteins are synthesized in neuronsThe N-terminal, polybasic region of PrP(C) dictates the efficiency of prion propagation by binding to PrP(Sc).Scrapie and cellular prion proteins differ in their kinetics of synthesis and topology in cultured cellsPurification and properties of the cellular prion protein from Syrian hamster brain.Protease resistance of infectious prions is suppressed by removal of a single atom in the cellular prion protein.Molecular location of a species-specific epitope on the hamster scrapie agent protein.Prion protein biosynthesis in scrapie-infected and uninfected neuroblastoma cells.Normal and scrapie-associated forms of prion protein differ in their sensitivities to phospholipase and proteases in intact neuroblastoma cells.N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): implications regarding the site of conversion of PrP to the protease-resistant state.Biogenesis and transmembrane orientation of the cellular isoform of the scrapie prion protein [published errratum appears in Mol Cell Biol 1987 May;7(5):2035]Immunological comparison of scrapie-associated fibrils isolated from animals infected with four different scrapie strains.Antisera to scrapie-associated fibril protein and prion protein decorate scrapie-associated fibrilsPurified scrapie prions resist inactivation by UV irradiationCharacterization of major peptides in Creutzfeldt-Jakob disease and scrapieMolecular cloning and complete sequence of prion protein cDNA from mouse brain infected with the scrapie agent.Isolation of a cDNA clone encoding the leader peptide of prion protein and expression of the homologous gene in various tissues.Prion liposomes.Fate of prions in soil: a review.Analyses of N-linked glycans of PrPSc revealed predominantly 2,6-linked sialic acid residues.Sialylation Controls Prion Fate in Vivo.Evidence suggesting that PrP is not the infectious agent in Creutzfeldt-Jakob disease.
P2860
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P2860
description
1985 nî lūn-bûn
@nan
1985年の論文
@ja
1985年論文
@yue
1985年論文
@zh-hant
1985年論文
@zh-hk
1985年論文
@zh-mo
1985年論文
@zh-tw
1985年论文
@wuu
1985年论文
@zh
1985年论文
@zh-cn
name
Scrapie PrP 27-30 is a sialoglycoprotein.
@en
type
label
Scrapie PrP 27-30 is a sialoglycoprotein.
@en
prefLabel
Scrapie PrP 27-30 is a sialoglycoprotein.
@en
P2860
P1433
P1476
Scrapie PrP 27-30 is a sialoglycoprotein.
@en
P2093
P2860
P304
P407
P577
1985-02-01T00:00:00Z