Distance of sequons to the C-terminus influences the cellular N-glycosylation of the prion protein.
about
N-glycosylation is required for efficient secretion of a novel human secreted glycoprotein, hPAP21Subtle evolutionary changes in the distribution of N-glycosylation sequons in the HIV-1 envelope glycoprotein 120Prion protein glycosylation.N-linked protein glycosylation in the endoplasmic reticulum.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.Hypoxia induces expression of a GPI-anchorless splice variant of the prion protein.Interplays between covalent modifications in the endoplasmic reticulum increase conformational diversity in nascent prion protein.Construction and analysis of a novel peptide tag containing an unnatural N-glycosylation site.Glycosylation and GPI anchorage of the prion protein.
P2860
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P2860
Distance of sequons to the C-terminus influences the cellular N-glycosylation of the prion protein.
description
2003 nî lūn-bûn
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2003年の論文
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2003年論文
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2003年論文
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2003年論文
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name
Distance of sequons to the C-t ...... sylation of the prion protein.
@en
Distance of sequons to the C-t ...... sylation of the prion protein.
@en-gb
type
label
Distance of sequons to the C-t ...... sylation of the prion protein.
@en
Distance of sequons to the C-t ...... sylation of the prion protein.
@en-gb
prefLabel
Distance of sequons to the C-t ...... sylation of the prion protein.
@en
Distance of sequons to the C-t ...... sylation of the prion protein.
@en-gb
P2860
P356
P1433
P1476
Distance of sequons to the C-t ...... sylation of the prion protein.
@en
P2093
Adrian R Walmsley
P2860
P304
P356
10.1042/BJ20021303
P407
P577
2003-02-01T00:00:00Z