More than one glycan is needed for ER glucosidase II to allow entry of glycoproteins into the calnexin/calreticulin cycle.
about
Mechanisms of pharmacological rescue of trafficking-defective hERG mutant channels in human long QT syndromePalmitoylated calnexin is a key component of the ribosome-translocon complex.Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoformsGetting in and out from calnexin/calreticulin cyclesGlycoprotein Quality Control and Endoplasmic Reticulum StressN-linked sugar-regulated protein folding and quality control in the ERFunction and structure studies of GH family 31 and 97 α-glycosidasesEncoding asymmetry of the N-glycosylation motif facilitates glycoprotein evolutionMalectin: A Novel Carbohydrate-binding Protein of the Endoplasmic Reticulum and a Candidate Player in the Early Steps of Protein N-GlycosylationThe presence of monoglucosylated N196-glycan is important for the structural stability of storage protein, arylphorinInteraction mode between catalytic and regulatory subunits in glucosidase II involved in ER glycoprotein quality controlYeast GTB1 encodes a subunit of glucosidase II required for glycoprotein processing in the endoplasmic reticulum.A novel role for Gtb1p in glucose trimming of N-linked glycans.N-Glycan-based ER Molecular Chaperone and Protein Quality Control System: The Calnexin Binding CycleN-glycan remodeling on glucagon receptor is an effector of nutrient sensing by the hexosamine biosynthesis pathwayUDP-GlC:glycoprotein glucosyltransferase-glucosidase II, the ying-yang of the ER quality controlMutations in GANAB, Encoding the Glucosidase IIα Subunit, Cause Autosomal-Dominant Polycystic Kidney and Liver DiseaseSynthesis, Processing, and Function of N-glycans in N-glycoproteins.Folding, quality control, and secretion of pancreatic ribonuclease in live cellsStructural insight into substrate recognition by the endoplasmic reticulum folding-sensor enzyme: crystal structure of third thioredoxin-like domain of UDP-glucose:glycoprotein glucosyltransferaseCalnexin-assisted biogenesis of the neuronal glycine transporter 2 (GlyT2).Role of malectin in Glc(2)Man(9)GlcNAc(2)-dependent quality control of α1-antitrypsinGlucosidase II and MRH-domain containing proteins in the secretory pathway.Cotranslational and posttranslocational N-glycosylation of proteins in the endoplasmic reticulum.The UDP-glucose: glycoprotein glucosyltransferase (UGGT), a key enzyme in ER quality control, plays a significant role in plant growth as well as biotic and abiotic stress in Arabidopsis thaliana.Tyrosinase maturation through the mammalian secretory pathway: bringing color to life.A Novel Interacting Protein SERP1 Regulates the N-Linked Glycosylation and Function of GLP-1 Receptor in the Liver.Stimulation of N-linked glycosylation and lipid-linked oligosaccharide synthesis by stress responses in metazoan cells.Structural basis for two-step glucose trimming by glucosidase II involved in ER glycoprotein quality controlN-linked glycan recognition and processing: the molecular basis of endoplasmic reticulum quality controlExtreme C-terminal sites are posttranslocationally glycosylated by the STT3B isoform of the OST.Glycoprotein folding and the role of EDEM1, EDEM2 and EDEM3 in degradation of folding-defective glycoproteins.Consequences of individual N-glycan deletions and of proteasomal inhibition on secretion of active BACE.How sugars convey information on protein conformation in the endoplasmic reticulumStructures of mammalian ER α-glucosidase II capture the binding modes of broad-spectrum iminosugar antivirals.Hepatic lipase maturation: a partial proteome of interacting factorsNovel types of Ca2+ release channels participate in the secretory cycle of Paramecium cells.Nephrin missense mutations: induction of endoplasmic reticulum stress and cell surface rescue by reduction in chaperone interactions.Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals.Lectin chaperones help direct the maturation of glycoproteins in the endoplasmic reticulum.
P2860
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P2860
More than one glycan is needed for ER glucosidase II to allow entry of glycoproteins into the calnexin/calreticulin cycle.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh-hant
name
More than one glycan is needed ...... e calnexin/calreticulin cycle.
@en
More than one glycan is needed ...... e calnexin/calreticulin cycle.
@nl
type
label
More than one glycan is needed ...... e calnexin/calreticulin cycle.
@en
More than one glycan is needed ...... e calnexin/calreticulin cycle.
@nl
prefLabel
More than one glycan is needed ...... e calnexin/calreticulin cycle.
@en
More than one glycan is needed ...... e calnexin/calreticulin cycle.
@nl
P2093
P1433
P1476
More than one glycan is needed ...... e calnexin/calreticulin cycle.
@en
P2093
Ari Helenius
Matthias Gautschi
Paola Deprez
P304
P356
10.1016/J.MOLCEL.2005.05.029
P577
2005-07-01T00:00:00Z