Post-conversion sialylation of prions in lymphoid tissues.
about
Multifaceted Role of Sialylation in Prion DiseasesReversible off and on switching of prion infectivity via removing and reinstalling prion sialylation.PrPSc formation and clearance as determinants of prion tropism.Sialylation 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.How do PrPSc Prions Spread between Host Species, and within Hosts?Prion Strains and Transmission Barrier Phenomena.Complement Regulatory Protein Factor H Is a Soluble Prion Receptor That Potentiates Peripheral Prion Pathogenesis.Limited understanding of the functional diversity of N-linked glycans as a major gap of prion biology.Generation of novel neuroinvasive prions following intravenous challenge.Prolonged follicular helper T cell responses in ME7 scrapie-infected mice.
P2860
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P2860
Post-conversion sialylation of prions in lymphoid tissues.
description
2015 nî lūn-bûn
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2015年の論文
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2015年学术文章
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2015年学术文章
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2015年学术文章
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2015年学术文章
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2015年学术文章
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2015年學術文章
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2015年學術文章
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2015年學術文章
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name
Post-conversion sialylation of prions in lymphoid tissues.
@ast
Post-conversion sialylation of prions in lymphoid tissues.
@en
type
label
Post-conversion sialylation of prions in lymphoid tissues.
@ast
Post-conversion sialylation of prions in lymphoid tissues.
@en
prefLabel
Post-conversion sialylation of prions in lymphoid tissues.
@ast
Post-conversion sialylation of prions in lymphoid tissues.
@en
P2093
P2860
P356
P1476
Post-conversion sialylation of prions in lymphoid tissues.
@en
P2093
Elizaveta Katorcha
Ilia V Baskakov
Natallia Makarava
Regina Savtchenko
Reinhard Brossmer
Saurabh Srivastava
P2860
P304
P356
10.1073/PNAS.1517993112
P407
P577
2015-11-16T00:00:00Z