PrPc glycoform heterogeneity as a function of brain region: implications for selective targeting of neurons by prion strains.
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Microdissection: a method developed to investigate mechanisms involved in transmissible spongiform encephalopathy pathogenesisMultifaceted Role of Sialylation in Prion DiseasesSialylation of prion protein controls the rate of prion amplification, the cross-species barrier, the ratio of PrPSc glycoform and prion infectivityGlycosylation influences cross-species formation of protease-resistant prion protein.Pharmacological prion protein silencing accelerates central nervous system autoimmune disease via T cell receptor signallingHost PrP glycosylation: a major factor determining the outcome of prion infection.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 PrPScNovel antibody-lectin enzyme-linked immunosorbent assay that distinguishes prion proteins in sporadic and variant cases of Creutzfeldt-Jakob disease.Cerebral amyloidosis in prion diseases.N-glycans and glycosylphosphatidylinositol-anchor act on polarized sorting of mouse PrP(C) in Madin-Darby canine kidney cells.Scrapie strains maintain biological phenotypes on propagation in a cell line in culture.Pathogenesis of prion diseases: a progress report.What is the basis of transmissible spongiform encephalopathy induced neurodegeneration and can it be repaired?Chronic wasting disease prion trafficking via the autonomic nervous system.Abrogation of complex glycosylation by swainsonine results in strain- and cell-specific inhibition of prion replication.A new mechanism for transmissible prion diseasesSialylation of the prion protein glycans controls prion replication rate and glycoform ratioSelective amplification of classical and atypical prions using modified protein misfolding cyclic amplification.Prion strain discrimination in cell culture: the cell panel assayPrion diseases: from protein to cell pathology.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.Atypical and classical forms of the disease-associated state of the prion protein exhibit distinct neuronal tropism, deposition patterns, and lesion profiles.Prion disease: a tale of folds and strains.Cerebellar compartmentation of prion pathogenesis.Endoproteolytic processing of the mammalian prion glycoprotein family.Conversion of raft associated prion protein to the protease-resistant state requires insertion of PrP-res (PrP(Sc)) into contiguous membranes.Glycan-controlled epitopes of prion protein include a major determinant of susceptibility to sheep scrapie.Simulations of membrane-bound diglycosylated human prion protein reveal potential protective mechanisms against misfolding.Glycosylation deficiency at either one of the two glycan attachment sites of cellular prion protein preserves susceptibility to bovine spongiform encephalopathy and scrapie infections.Biochemical fingerprints of prion infection: accumulations of aberrant full-length and N-terminally truncated PrP species are common features in mouse prion disease.Distance of sequons to the C-terminus influences the cellular N-glycosylation of the prion protein.Molecular profiling of ovine prion diseases by using thermolysin-resistant PrPSc and endogenous C2 PrP fragmentsDeterminants of the in vivo folding of the prion protein. A bipartite function of helix 1 in folding and aggregation.Effect of glycosylphosphatidylinositol anchor-dependent and -independent prion protein association with model raft membranes on conversion to the protease-resistant isoform.Inhibition of complex glycosylation increases the formation of PrPsc.Altered glycosylated PrP proteins can have different neuronal trafficking in brain but do not acquire scrapie-like properties.Changes in the glycosylation pattern of prion protein in murine scrapie. Implications for the mechanism of neurodegeneration in prion diseases.Heterogeneity of normal prion protein in two- dimensional immunoblot: presence of various glycosylated and truncated forms.
P2860
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P2860
PrPc glycoform heterogeneity as a function of brain region: implications for selective targeting of neurons by prion strains.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
1999年论文
@zh
1999年论文
@zh-cn
name
PrPc glycoform heterogeneity a ...... g of neurons by prion strains.
@en
type
label
PrPc glycoform heterogeneity a ...... g of neurons by prion strains.
@en
prefLabel
PrPc glycoform heterogeneity a ...... g of neurons by prion strains.
@en
P2093
P1476
PrPc glycoform heterogeneity a ...... g of neurons by prion strains.
@en
P2093
P304
P356
10.1097/00005072-199909000-00010
P577
1999-09-01T00:00:00Z