A misfolded protein conformation is not a sufficient condition for in vivo glucosylation by the UDP-Glc:glycoprotein glucosyltransferase.
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Structure of the Lectin Mannose 6-Phosphate Receptor Homology (MRH) Domain of Glucosidase II, an Enzyme That Regulates Glycoprotein Folding Quality Control in the Endoplasmic ReticulumUDP-Glc:glycoprotein glucosyltransferase recognizes structured and solvent accessible hydrophobic patches in molten globule-like folding intermediatesImmunolocalization of UDP-glucose:glycoprotein glucosyltransferase indicates involvement of pre-Golgi intermediates in protein quality controlThe role of UDP-Glc:glycoprotein glucosyltransferase 1 in the maturation of an obligate substrate prosaposin.Role of N-oligosaccharide endoplasmic reticulum processing reactions in glycoprotein folding and degradationCharacterization of Schizosaccharomyces pombe ER alpha-mannosidase: a reevaluation of the role of the enzyme on ER-associated degradationGlycoprotein folding in the endoplasmic reticulum.Lectin-like proteins in model organisms: implications for evolution of carbohydrate-binding activity.Glucosidase II and N-glycan mannose content regulate the half-lives of monoglucosylated species in vivo.Reglucosylation by UDP-glucose:glycoprotein glucosyltransferase 1 delays glycoprotein secretion but not degradation.The annotation of the asparagine N-linked glycosylation pathway in the Reactome database.Conformational requirements for glycoprotein reglucosylation in the endoplasmic reticulum.A cell-based reglucosylation assay demonstrates the role of GT1 in the quality control of a maturing glycoproteinGlucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals.N-glycan trimming by glucosidase II is essential for Arabidopsis development.Genetic evidence for the heterodimeric structure of glucosidase II. The effect of disrupting the subunit-encoding genes on glycoprotein folding.Modification of the T cell antigen receptor (TCR) complex by UDP-glucose:glycoprotein glucosyltransferase. TCR folding is finalized convergent with formation of alpha beta delta epsilon gamma epsilon complexes.Trypanosoma brucei UDP-glucose:glycoprotein glucosyltransferase has unusual substrate specificity and protects the parasite from stress.The conundrum of UDP-Glc entrance into the yeast ER lumen.Nucleoside diphosphatase and glycosyltransferase activities can localize to different subcellular compartments in Schizosaccharomyces pombe.
P2860
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P2860
A misfolded protein conformation is not a sufficient condition for in vivo glucosylation by the UDP-Glc:glycoprotein glucosyltransferase.
description
1998 nî lūn-bûn
@nan
1998 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
A misfolded protein conformati ...... coprotein glucosyltransferase.
@ast
A misfolded protein conformati ...... coprotein glucosyltransferase.
@en
type
label
A misfolded protein conformati ...... coprotein glucosyltransferase.
@ast
A misfolded protein conformati ...... coprotein glucosyltransferase.
@en
prefLabel
A misfolded protein conformati ...... coprotein glucosyltransferase.
@ast
A misfolded protein conformati ...... coprotein glucosyltransferase.
@en
P2093
P2860
P356
P1433
P1476
A misfolded protein conformati ...... coprotein glucosyltransferase.
@en
P2093
A J Parodi
C D'Alessio
F Fernández
S Fanchiotti
P2860
P304
P356
10.1093/EMBOJ/17.20.5877
P407
P577
1998-10-01T00:00:00Z