A misfolded protein conformation is not a sufficient condition for in vivo glucosylation by the UDP-Glc:glycoprotein glucosyltransferase. - Wikidata - wikimedia - TriplyDB

A misfolded protein conformation is not a sufficient condition for in vivo glucosylation by the UDP-Glc:glycoprotein glucosyltransferase.

A misfolded protein conformation is not a sufficient condition for in vivo glucosylation by the UDP-Glc:glycoprotein glucosyltransferase.

http://www.wikidata.org/entity/Q33889672

about

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 Reticulum UDP-Glc:glycoprotein glucosyltransferase recognizes structured and solvent accessible hydrophobic patches in molten globule-like folding intermediates Immunolocalization of UDP-glucose:glycoprotein glucosyltransferase indicates involvement of pre-Golgi intermediates in protein quality control The 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 degradation Characterization of Schizosaccharomyces pombe ER alpha-mannosidase: a reevaluation of the role of the enzyme on ER-associated degradation Glycoprotein 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 glycoprotein Glucosidase 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.

http://www.wikidata.org/entity/Q33889672

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.

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A misfolded protein conformati ...... coprotein glucosyltransferase.

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type

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A misfolded protein conformati ...... coprotein glucosyltransferase.

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prefLabel

A misfolded protein conformati ...... coprotein glucosyltransferase.

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A misfolded protein conformati ...... coprotein glucosyltransferase.

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The EMBO Journal

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A misfolded protein conformati ...... coprotein glucosyltransferase.

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P2093

A J Parodi

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C D'Alessio

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F Fernández

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S Fanchiotti

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P2860

X-ray crystal structure of the soybean agglutinin cross-linked with a biantennary analog of the blood group I carbohydrate antigen

Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functions as a constituent of the ER quality control apparatus.

BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast

A mutation that prevents glucosylation of the lipid-linked oligosaccharide precursor leads to underglycosylation of secreted yeast invertase

Vacuolar protein sorting in fission yeast: cloning, biosynthesis, transport, and processing of carboxypeptidase Y from Schizosaccharomyces pombe.

A new stress protein: synthesis of Schizosaccharomyces pombe UDP--Glc:glycoprotein glucosyltransferase mRNA is induced by stress conditions but the enzyme is not essential for cell viability.

Selective retention of monoglucosylated high mannose oligosaccharides by a class of mutant vesicular stomatitis virus G proteins

Retention of glucose units added by the UDP-GLC:glycoprotein glucosyltransferase delays exit of glycoproteins from the endoplasmic reticulum.

Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum.

Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries.

P304

5877-5886

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scholarly article

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10.1093/EMBOJ/17.20.5877

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20

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17

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1998-10-01T00:00:00Z

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13512532

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9774332

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1170915

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