Glycosylation influences cross-species formation of protease-resistant prion protein. - Wikidata - awgldk - TriplyDB

Glycosylation influences cross-species formation of protease-resistant prion protein.

Glycosylation influences cross-species formation of protease-resistant prion protein.

http://www.wikidata.org/entity/Q28365495

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Mapping of possible prion protein self-interaction domains using peptide arrays Species and strain glycosylation patterns of PrPSc Conservation of a glycine-rich region in the prion protein is required for uptake of prion infectivity Assessing proteinase K resistance of fish prion proteins in a scrapie-infected mouse neuroblastoma cell line.Glycosylphosphatidylinositol anchor-dependent stimulation pathway required for generation of baculovirus-derived recombinant scrapie prion protein.Experimental H-type bovine spongiform encephalopathy characterized by plaques and glial- and stellate-type prion protein deposits.The glycosylation status of PrPC is a key factor in determining transmissible spongiform encephalopathy transmission between species Increased infectivity of anchorless mouse scrapie prions in transgenic mice overexpressing human prion protein Folding and misfolding of the prion protein in the secretory pathway.Mouse prion protein (PrP) segment 100 to 104 regulates conversion of PrP(C) to PrP(Sc) in prion-infected neuroblastoma cells.Efficient in vitro amplification of chronic wasting disease PrPRES.Prion protein glycosylation.In vitro amplification of scrapie and chronic wasting disease PrP(res) using baculovirus-expressed recombinant PrP as substrate The prion protein preference of sporadic Creutzfeldt-Jakob disease subtypes.Octapeptide repeat insertions increase the rate of protease-resistant prion protein formation Cells expressing anchorless prion protein are resistant to scrapie infection.Identification of an intracellular site of prion conversion.Characterization of cell-surface prion protein relative to its recombinant analogue: insights from molecular dynamics simulations of diglycosylated, membrane-bound human prion protein.Prion protein glycosylation is not required for strain-specific neurotropism.Recombinant human prion protein inhibits prion propagation in vitro.PrP Knockout Cells Expressing Transmembrane PrP Resist Prion Infection Prion disease: a tale of folds and strains.Altered prion protein glycosylation in the aging mouse brain.N-glycoprotein macroheterogeneity: biological implications and proteomic characterization.Endoproteolytic processing of the mammalian prion glycoprotein family.Prion propagation in cells expressing PrP glycosylation mutants.Glycan-controlled epitopes of prion protein include a major determinant of susceptibility to sheep scrapie.PrioNet Canada: a network of centres of excellence for research on prion diseases--ongoing and future research directions.Simulations of membrane-bound diglycosylated human prion protein reveal potential protective mechanisms against misfolding.Glycosylation deficiency at either one of the two glycan attachment sites of cellular prion protein preserves susceptibility to bovine spongiform encephalopathy and scrapie infections.Separation of native prion protein (PrP) glycoforms by copper-binding using immobilized metal affinity chromatography (IMAC)Distance of sequons to the C-terminus influences the cellular N-glycosylation of the prion protein.Evidence for distinct chronic wasting disease (CWD) strains in experimental CWD in ferrets.Determinants of the in vivo folding of the prion protein. A bipartite function of helix 1 in folding and aggregation.Inhibition of complex glycosylation increases the formation of PrPsc.Altered glycosylated PrP proteins can have different neuronal trafficking in brain but do not acquire scrapie-like properties.Scientific Opinion on a request for a review of a scientific publication concerning the zoonotic potential of ovine scrapie prions Prion Strains and Transmission Barrier Phenomena.Prion Diseases.

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P2860

Glycosylation influences cross-species formation of protease-resistant prion protein.

http://www.wikidata.org/entity/Q28365495

description

2001 nî lūn-bûn

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2001 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

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2001 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2001年の論文

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2001年論文

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2001年論文

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2001年論文

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2001年論文

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2001年論文

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2001年论文

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name

Glycosylation influences cross-species formation of protease-resistant prion protein

@nl

Glycosylation influences cross-species formation of protease-resistant prion protein.

@ast

Glycosylation influences cross-species formation of protease-resistant prion protein.

@en

type

label

Glycosylation influences cross-species formation of protease-resistant prion protein

@nl

Glycosylation influences cross-species formation of protease-resistant prion protein.

@ast

Glycosylation influences cross-species formation of protease-resistant prion protein.

@en

prefLabel

Glycosylation influences cross-species formation of protease-resistant prion protein

@nl

Glycosylation influences cross-species formation of protease-resistant prion protein.

@ast

Glycosylation influences cross-species formation of protease-resistant prion protein.

@en

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The EMBO Journal

P1476

Glycosylation influences cross-species formation of protease-resistant prion protein.

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Lawson VA

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Priola SA

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P2860

Modulation of protein structure and function by asparagine-linked glycosylation.

Chaperone-supervised conversion of prion protein to its protease-resistant form.

Efficient conversion of normal prion protein (PrP) by abnormal hamster PrP is determined by homology at amino acid residue 155.

Acquisition of protease resistance by prion proteins in scrapie-infected cells does not require asparagine-linked glycosylation

A new variant of Creutzfeldt-Jakob disease in the UK.

Species specificity in the cell-free conversion of prion protein to protease-resistant forms: a model for the scrapie species barrier

Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD.

A cellular gene encodes scrapie PrP 27-30 protein.

Interactions between heterologous forms of prion protein: binding, inhibition of conversion, and species barriers

A single hamster PrP amino acid blocks conversion to protease-resistant PrP in scrapie-infected mouse neuroblastoma cells.

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6692-6699

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10.1093/EMBOJ/20.23.6692

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23

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20

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11726505

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Prion protein family

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125748

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