Immunolocalization of UDP-glucose:glycoprotein glucosyltransferase indicates involvement of pre-Golgi intermediates in protein quality control
about
Identification of the neuroblastoma-amplified gene product as a component of the syntaxin 18 complex implicated in Golgi-to-endoplasmic reticulum retrograde transportNCB5OR is a novel soluble NAD(P)H reductase localized in the endoplasmic reticulumEDEM1 reveals a quality control vesicular transport pathway out of the endoplasmic reticulum not involving the COPII exit sitesAn HRD/DER-independent ER quality control mechanism involves Rsp5p-dependent ubiquitination and ER-Golgi transportN-Glycan-based ER Molecular Chaperone and Protein Quality Control System: The Calnexin Binding CycleCloning, expression, and functional characterization of a Ca(2+)-dependent endoplasmic reticulum nucleoside diphosphataseRab1 defines a novel pathway connecting the pre-Golgi intermediate compartment with the cell periphery.Rab2A is a pivotal switch protein that promotes either secretion or ER-associated degradation of (pro)insulin in insulin-secreting cells.TAPBPR bridges UDP-glucose:glycoprotein glucosyltransferase 1 onto MHC class I to provide quality control in the antigen presentation pathway.Probing for membrane domains in the endoplasmic reticulum: retention and degradation of unassembled MHC class I molecules.Organizational diversity among distinct glycoprotein endoplasmic reticulum-associated degradation programsUDP-GlC:glycoprotein glucosyltransferase-glucosidase II, the ying-yang of the ER quality controlCharacterization of Schizosaccharomyces pombe ER alpha-mannosidase: a reevaluation of the role of the enzyme on ER-associated degradationThe intrinsic and extrinsic effects of N-linked glycans on glycoproteostasis.Reglucosylation by UDP-glucose:glycoprotein glucosyltransferase 1 delays glycoprotein secretion but not degradation.A novel UGGT1 and p97-dependent checkpoint for native ectodomains with ionizable intramembrane residueGlucosidase II and MRH-domain containing proteins in the secretory pathway.Ca2+-activated nucleotidase 1, a novel target gene for the transcriptional repressor DREAM (downstream regulatory element antagonist modulator), is involved in protein folding and degradation.Applications of immunogold labeling in ultrastructural pathology.Protein quality control: the who's who, the where's and therapeutic escapes.A cell-based reglucosylation assay demonstrates the role of GT1 in the quality control of a maturing glycoproteinHow sugars convey information on protein conformation in the endoplasmic reticulumCalreticulin-dependent recycling in the early secretory pathway mediates optimal peptide loading of MHC class I molecules.Lectin chaperones help direct the maturation of glycoproteins in the endoplasmic reticulum.Sorting things out through endoplasmic reticulum quality control.Protein N-glycosylation, protein folding, and protein quality control.Endoplasmic reticulum-associated degradation of mammalian glycoproteins involves sugar chain trimming to Man6-5GlcNAc2.Quality control of glycoprotein folding and ERAD: the role of N-glycan handling, EDEM1 and OS-9.ERADication of EDEM1 occurs by selective autophagy and requires deglycosylation by cytoplasmic peptide N-glycanase.Immunoglobulin light chains dictate vesicular transport-dependent and -independent routes for IgM degradation by the ubiquitin-proteasome pathway.Endoplasmic reticulum quality control of unassembled iron transporter depends on Rer1p-mediated retrieval from the golgi.Endoplasmic reticulum-associated degradation of a degron-containing polytopic membrane protein.Aggregated myocilin induces russell bodies and causes apoptosis: implications for the pathogenesis of myocilin-caused primary open-angle glaucoma.ire-1-dependent transcriptional up-regulation of a lumenal uridine diphosphatase from Caenorhabditis elegans.Interdomain conformational flexibility underpins the activity of UGGT, the eukaryotic glycoprotein secretion checkpoint.Cell biology of protein glycosylation: a celebration of the career of Jürgen Roth on the occasion of his 70th birthday.Nucleoside diphosphatase and glycosyltransferase activities can localize to different subcellular compartments in Schizosaccharomyces pombe.Intermediate compartment (IC): from pre-Golgi vacuoles to a semi-autonomous membrane system
P2860
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P2860
Immunolocalization of UDP-glucose:glycoprotein glucosyltransferase indicates involvement of pre-Golgi intermediates in protein quality control
description
2001 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
article publié dans les Procee ...... f the United States of America
@fr
artículu científicu espublizáu en 2001
@ast
im September 2001 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2001/09/11)
@sk
vědecký článek publikovaný v roce 2001
@cs
wetenschappelijk artikel (gepubliceerd op 2001/09/11)
@nl
наукова стаття, опублікована у вересні 2001
@uk
name
Immunolocalization of UDP-gluc ...... tes in protein quality control
@ast
Immunolocalization of UDP-gluc ...... tes in protein quality control
@en
Immunolocalization of UDP-gluc ...... tes in protein quality control
@nl
type
label
Immunolocalization of UDP-gluc ...... tes in protein quality control
@ast
Immunolocalization of UDP-gluc ...... tes in protein quality control
@en
Immunolocalization of UDP-gluc ...... tes in protein quality control
@nl
prefLabel
Immunolocalization of UDP-gluc ...... tes in protein quality control
@ast
Immunolocalization of UDP-gluc ...... tes in protein quality control
@en
Immunolocalization of UDP-gluc ...... tes in protein quality control
@nl
P2093
P2860
P356
P1476
Immunolocalization of UDP-gluc ...... tes in protein quality control
@en
P2093
J. H. Fessler
P2860
P304
10710–10715
P356
10.1073/PNAS.191359198
P407
P577
2001-09-11T00:00:00Z