Glycosylation of PrPC determines timing of neuroinvasion and targeting in the brain following transmissible spongiform encephalopathy infection by a peripheral route.
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Insights into Mechanisms of Chronic NeurodegenerationPost-translational modifications in PrP expand the conformational diversity of prions in vivoSequence-dependent prion protein misfolding and neurotoxicity.Propagation of RML prions in mice expressing PrP devoid of GPI anchor leads to formation of a novel, stable prion strainCrucial role for prion protein membrane anchoring in the neuroinvasion and neural spread of prion infectionEffect 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.Stimulating the Release of Exosomes Increases the Intercellular Transfer of PrionsPost-translational changes to PrP alter transmissible spongiform encephalopathy strain properties.Defining the Microglia Response during the Time Course of Chronic NeurodegenerationAnalyses of protease resistance and aggregation state of abnormal prion protein across the spectrum of human prionsPrP Knockout Cells Expressing Transmembrane PrP Resist Prion InfectionThe Biological Function of the Prion Protein: A Cell Surface Scaffold of Signaling ModulesRole of proteomics in understanding prion infection.Prion propagation in cells expressing PrP glycosylation mutants.Prion pathogenesis is unaltered following down-regulation of SIGN-R1.PrP mRNA and protein expression in brain and PrP(c) in CSF in Creutzfeldt-Jakob disease MM1 and VV2.Glycosylation Significantly Inhibits the Aggregation of Human Prion Protein and Decreases Its Cytotoxicity
P2860
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P2860
Glycosylation of PrPC determines timing of neuroinvasion and targeting in the brain following transmissible spongiform encephalopathy infection by a peripheral route.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
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2010年论文
@zh-cn
name
Glycosylation of PrPC determin ...... fection by a peripheral route.
@en
Glycosylation of PrPC determin ...... fection by a peripheral route.
@nl
type
label
Glycosylation of PrPC determin ...... fection by a peripheral route.
@en
Glycosylation of PrPC determin ...... fection by a peripheral route.
@nl
prefLabel
Glycosylation of PrPC determin ...... fection by a peripheral route.
@en
Glycosylation of PrPC determin ...... fection by a peripheral route.
@nl
P2093
P2860
P50
P356
P1433
P1476
Glycosylation of PrPC determin ...... fection by a peripheral route.
@en
P2093
Debbie Brown
Dorothy Kisielewski
Enrico Cancellotti
Karen L Brown
Nadia L Tuzi
Pedro Piccardo
Raymond D Hickey
P2860
P304
P356
10.1128/JVI.02374-09
P407
P577
2010-01-27T00:00:00Z