Glycosylation deficiency at either one of the two glycan attachment sites of cellular prion protein preserves susceptibility to bovine spongiform encephalopathy and scrapie infections.
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Insights into Mechanisms of Chronic NeurodegenerationGetting a grip on prions: oligomers, amyloids, and pathological membrane interactions.Early Delivery of Misfolded PrP from ER to Lysosomes by Autophagy.Host PrP glycosylation: a major factor determining the outcome of prion infection.Species and strain glycosylation patterns of PrPScPropagation of RML prions in mice expressing PrP devoid of GPI anchor leads to formation of a novel, stable prion strainGlycoform-selective prion formation in sporadic and familial forms of prion disease.Conserved roles of the prion protein domains on subcellular localization and cell-cell adhesionEffect 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 speciesIncreased infectivity of anchorless mouse scrapie prions in transgenic mice overexpressing human prion proteinCopper and Zinc Interactions with Cellular Prion Proteins Change Solubility of Full-Length Glycosylated Isoforms and Induce the Occurrence of Heterogeneous PhenotypesSialylation of the prion protein glycans controls prion replication rate and glycoform ratioPrion Infectivity Plateaus and Conversion to Symptomatic Disease Originate from Falling Precursor Levels and Increased Levels of Oligomeric PrPSc Species.Post-translational changes to PrP alter transmissible spongiform encephalopathy strain properties.The reconstitution of mammalian prion infectivity de novo.Retrotranslocation of prion proteins from the endoplasmic reticulum by preventing GPI signal transamidationDistinct structures of scrapie prion protein (PrPSc)-seeded versus spontaneous recombinant prion protein fibrils revealed by hydrogen/deuterium exchange.How independent are TSE agents from their hosts?Species-barrier phenomenon in prion transmissibility from a viewpoint of protein science.Altered prion protein glycosylation in the aging mouse brain.Lysosomal Quality Control in Prion Diseases.Implications of peptide assemblies in amyloid diseases.Prion propagation in cells expressing PrP glycosylation mutants.Conditional modulation of membrane protein expression in cultured cells mediated by prion protein recognition of short phosphorothioate oligodeoxynucleotides.Cell Biology Approaches to Studying Prion Diseases.Glycoform-independent prion conversion by highly efficient, cell-based, protein misfolding cyclic amplification.Separation of native prion protein (PrP) glycoforms by copper-binding using immobilized metal affinity chromatography (IMAC)Increased proportions of C1 truncated prion protein protect against cellular M1000 prion infection.Altered glycosylated PrP proteins can have different neuronal trafficking in brain but do not acquire scrapie-like properties.Prion Strains and Transmission Barrier Phenomena.Dimerization of the cellular prion protein inhibits propagation of scrapie prions.Structural and mechanistic aspects influencing the ADAM10-mediated shedding of the prion protein.
P2860
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P2860
Glycosylation deficiency at either one of the two glycan attachment sites of cellular prion protein preserves susceptibility to bovine spongiform encephalopathy and scrapie infections.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
Glycosylation deficiency at ei ...... opathy and scrapie infections.
@en
type
label
Glycosylation deficiency at ei ...... opathy and scrapie infections.
@en
prefLabel
Glycosylation deficiency at ei ...... opathy and scrapie infections.
@en
P2093
P2860
P356
P1476
Glycosylation deficiency at ei ...... lopathy and scrapie infections
@en
P2093
Artur Weber
Eberhardt Pfaff
Erdmute Neuendorf
Kurt Reifenberg
Martin Hermann Groschup
P2860
P304
53306-53316
P356
10.1074/JBC.M410796200
P407
P577
2004-09-23T00:00:00Z