Membrane topology influences N-glycosylation of the prion protein.
about
Glypican-1 mediates both prion protein lipid raft association and disease isoform formationMinimotif miner 2nd release: a database and web system for motif searchThe membrane-associated form of α(s1)-casein interacts with cholesterol-rich detergent-resistant microdomainsCellular prion protein regulates beta-secretase cleavage of the Alzheimer's amyloid precursor protein.The glycan role in the glycopeptide immunogenicity revealed by atomistic simulations and spectroscopic experiments on the multiple sclerosis biomarker CSF114(Glc)Effect of glycans and the glycophosphatidylinositol anchor on strain dependent conformations of scrapie prion protein: improved purifications and infrared spectra.Prion protein interacts with BACE1 protein and differentially regulates its activity toward wild type and Swedish mutant amyloid precursor protein.C-terminal hydrophobic region in human bone marrow stromal cell antigen 2 (BST-2)/tetherin protein functions as second transmembrane motif.Emerging therapeutic agents for transmissible spongiform encephalopathies: a review.Folding and misfolding of the prion protein in the secretory pathway.Prion protein glycosylation.PrP Knockout Cells Expressing Transmembrane PrP Resist Prion InfectionPrion protein "gamma-cleavage": characterizing a novel endoproteolytic processing event.CD39 reveals novel insights into the role of transmembrane domains in protein processing, apical targeting and activity.Prion propagation in cells expressing PrP glycosylation mutants.Role of ADAMs in the ectodomain shedding and conformational conversion of the prion protein.Dual mechanisms for shedding of the cellular prion protein.A point mutation in the juxtamembrane stalk of human angiotensin I-converting enzyme invokes the action of a distinct secretase.Efficient glycosylphosphatidylinositol (GPI) modification of membrane proteins requires a C-terminal anchoring signal of marginal hydrophobicityInterplays between covalent modifications in the endoplasmic reticulum increase conformational diversity in nascent prion protein.Distance of sequons to the C-terminus influences the cellular N-glycosylation of the prion protein.Determinants of the in vivo folding of the prion protein. A bipartite function of helix 1 in folding and aggregation.Tethering the N-terminus of the prion protein compromises the cellular response to oxidative stress.Post-translational import of the prion protein into the endoplasmic reticulum interferes with cell viability: a critical role for the putative transmembrane domain.Glycosylation and GPI anchorage of the prion protein.Emerging and potential therapies for Alzheimer's disease
P2860
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P2860
Membrane topology influences N-glycosylation of the prion protein.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
2001年论文
@zh
2001年论文
@zh-cn
name
Membrane topology influences N-glycosylation of the prion protein.
@en
Membrane topology influences N-glycosylation of the prion protein.
@en-gb
Membrane topology influences N-glycosylation of the prion protein.
@nl
type
label
Membrane topology influences N-glycosylation of the prion protein.
@en
Membrane topology influences N-glycosylation of the prion protein.
@en-gb
Membrane topology influences N-glycosylation of the prion protein.
@nl
prefLabel
Membrane topology influences N-glycosylation of the prion protein.
@en
Membrane topology influences N-glycosylation of the prion protein.
@en-gb
Membrane topology influences N-glycosylation of the prion protein.
@nl
P2860
P356
P1433
P1476
Membrane topology influences N-glycosylation of the prion protein.
@en
P2093
P2860
P304
P356
10.1093/EMBOJ/20.4.703
P407
P577
2001-02-01T00:00:00Z