Host PrP glycosylation: a major factor determining the outcome of prion infection.
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Conformational diversity in prion protein variants influences intermolecular beta-sheet formationInsights into Mechanisms of Chronic NeurodegenerationPrions in variably protease-sensitive prionopathy: an updateSialylation of prion protein controls the rate of prion amplification, the cross-species barrier, the ratio of PrPSc glycoform and prion infectivityDefining the conformational features of anchorless, poorly neuroinvasive prionsPost-translational modifications in PrP expand the conformational diversity of prions in vivoGetting a grip on prions: oligomers, amyloids, and pathological membrane interactions.Regulating factors of PrP glycosylation in Creutzfeldt-Jakob disease--implications for the dissemination and the diagnosis of human prion strains.Species and strain glycosylation patterns of PrPScFatal transmissible amyloid encephalopathy: a new type of prion disease associated with lack of prion protein membrane anchoringMammalian prions generated from bacterially expressed prion protein in the absence of any mammalian cofactorsGlycosylphosphatidylinositol anchor analogues sequester cholesterol and reduce prion formation.N-glycans and glycosylphosphatidylinositol-anchor act on polarized sorting of mouse PrP(C) in Madin-Darby canine kidney cells.Sequence-dependent prion protein misfolding and neurotoxicity.Small protease sensitive oligomers of PrPSc in distinct human prions determine conversion rate of PrP(C).Glycoform-selective prion formation in sporadic and familial forms of prion disease.Effect of glycans and the glycophosphatidylinositol anchor on strain dependent conformations of scrapie prion protein: improved purifications and infrared spectra.The glycosylation status of PrPC is a key factor in determining transmissible spongiform encephalopathy transmission between speciesPrions on the move.Increased infectivity of anchorless mouse scrapie prions in transgenic mice overexpressing human prion proteinSialylation of the prion protein glycans controls prion replication rate and glycoform ratioThe prion protein preference of sporadic Creutzfeldt-Jakob disease subtypes.Prion Infectivity Plateaus and Conversion to Symptomatic Disease Originate from Falling Precursor Levels and Increased Levels of Oligomeric PrPSc Species.Selective amplification of classical and atypical prions using modified protein misfolding cyclic amplification.Post-translational changes to PrP alter transmissible spongiform encephalopathy strain properties.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.Analyses of protease resistance and aggregation state of abnormal prion protein across the spectrum of human prionsSwitching in amyloid structure within individual fibrils: implication for strain adaptation, species barrier and strain classificationDistinct structures of scrapie prion protein (PrPSc)-seeded versus spontaneous recombinant prion protein fibrils revealed by hydrogen/deuterium exchange.Prion protein misfolding, strains, and neurotoxicity: an update from studies on Mammalian prions.Design and construction of diverse mammalian prion strainsHow independent are TSE agents from their hosts?PrP Knockout Cells Expressing Transmembrane PrP Resist Prion InfectionDivergent prion strain evolution driven by PrPC expression level in transgenic mice.Species-barrier phenomenon in prion transmissibility from a viewpoint of protein science.Prion Strain Characterization of a Novel Subtype of Creutzfeldt-Jakob Disease.Prion propagation in cells expressing PrP glycosylation mutants.Glycosylation of PrPC determines timing of neuroinvasion and targeting in the brain following transmissible spongiform encephalopathy infection by a peripheral route.Glycoform-independent prion conversion by highly efficient, cell-based, protein misfolding cyclic amplification.
P2860
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P2860
Host PrP glycosylation: a major factor determining the outcome of prion infection.
description
2008 nî lūn-bûn
@nan
2008 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Host PrP glycosylation: a major factor determining the outcome of prion infection.
@ast
Host PrP glycosylation: a major factor determining the outcome of prion infection.
@en
Host PrP glycosylation: a major factor determining the outcome of prion infection.
@nl
type
label
Host PrP glycosylation: a major factor determining the outcome of prion infection.
@ast
Host PrP glycosylation: a major factor determining the outcome of prion infection.
@en
Host PrP glycosylation: a major factor determining the outcome of prion infection.
@nl
prefLabel
Host PrP glycosylation: a major factor determining the outcome of prion infection.
@ast
Host PrP glycosylation: a major factor determining the outcome of prion infection.
@en
Host PrP glycosylation: a major factor determining the outcome of prion infection.
@nl
P2093
P2860
P50
P1433
P1476
Host PrP glycosylation: a major factor determining the outcome of prion infection.
@en
P2093
Anne Coghill
Chris Plinston
Enrico Cancellotti
Herbert Baybutt
Lorraine Blackford
Nadia L Tuzi
Pedro Piccardo
P2860
P356
10.1371/JOURNAL.PBIO.0060100
P407
P577
2008-04-01T00:00:00Z