Sialylation of prion protein controls the rate of prion amplification, the cross-species barrier, the ratio of PrPSc glycoform and prion infectivity
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Multifaceted Role of Sialylation in Prion DiseasesLoss of Cellular Sialidases Does Not Affect the Sialylation Status of the Prion Protein but Increases the Amounts of Its Proteolytic Fragment C1Reversible off and on switching of prion infectivity via removing and reinstalling prion sialylation.Two alternative pathways for generating transmissible prion disease de novo.Sialylation of the prion protein glycans controls prion replication rate and glycoform ratioPost-conversion sialylation of prions in lymphoid tissues.Live-Cell Labeling of Specific Protein Glycoforms by Proximity-Enhanced Bioorthogonal LigationPrion infection impairs lysosomal degradation capacity by interfering with rab7 membrane attachment in neuronal cellsSialylation of Glycosylphosphatidylinositol (GPI) Anchors of Mammalian Prions Is Regulated in a Host-, Tissue-, and Cell-specific MannerAnalyses of N-linked glycans of PrPSc revealed predominantly 2,6-linked sialic acid residues.Sialylation Controls Prion Fate in Vivo.Protein Misfolding Cyclic Amplification Cross-Species Products of Mouse-Adapted Scrapie Strain 139A and Hamster-Adapted Scrapie Strain 263K with Brain and Muscle Tissues of Opposite Animals Generate Infectious Prions.Semisynthetic prion protein (PrP) variants carrying glycan mimics at position 181 and 197 do not form fibrils.Prion Strains and Transmission Barrier Phenomena.Complement Regulatory Protein Factor H Is a Soluble Prion Receptor That Potentiates Peripheral Prion Pathogenesis.Silver nanoparticle plasmonic enhanced förster resonance energy transfer (FRET) imaging of protein-specific sialylation on the cell surface.Limited understanding of the functional diversity of N-linked glycans as a major gap of prion biology.Structural and mechanistic aspects influencing the ADAM10-mediated shedding of the prion protein.Prion replication environment defines the fate of prion strain adaptation.Direct observation of murine prion protein replication in vitroIndependent amplification of co-infected long incubation period low conversion efficiency prion strainsGlycosylation Significantly Inhibits the Aggregation of Human Prion Protein and Decreases Its CytotoxicityPreserving prion strain identity upon replication of prions in vitro using recombinant prion protein
P2860
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P2860
Sialylation of prion protein controls the rate of prion amplification, the cross-species barrier, the ratio of PrPSc glycoform and prion infectivity
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2014 nî lūn-bûn
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2014 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
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2014 թվականի սեպտեմբերին հրատարակված գիտական հոդված
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2014年の論文
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2014年論文
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2014年論文
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2014年論文
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2014年論文
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2014年論文
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2014年论文
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Sialylation of prion protein c ...... lycoform and prion infectivity
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Sialylation of prion protein c ...... lycoform and prion infectivity
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Sialylation of prion protein c ...... lycoform and prion infectivity
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type
label
Sialylation of prion protein c ...... lycoform and prion infectivity
@ast
Sialylation of prion protein c ...... lycoform and prion infectivity
@en
Sialylation of prion protein c ...... lycoform and prion infectivity
@nl
prefLabel
Sialylation of prion protein c ...... lycoform and prion infectivity
@ast
Sialylation of prion protein c ...... lycoform and prion infectivity
@en
Sialylation of prion protein c ...... lycoform and prion infectivity
@nl
P2093
P2860
P3181
P1433
P1476
Sialylation of prion protein c ...... lycoform and prion infectivity
@en
P2093
Alessandra D'Azzo
Elizaveta Katorcha
Ilia V Baskakov
Natallia Makarava
Regina Savtchenko
P2860
P304
P3181
P356
10.1371/JOURNAL.PPAT.1004366
P407
P577
2014-09-01T00:00:00Z