Oligosaccharyltransferase: the central enzyme of N-linked protein glycosylation.
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Plant protein glycosylationGlycoprotein Quality Control and Endoplasmic Reticulum StressEndoplasmic reticulum-mediated protein quality control in ArabidopsisN-linked sugar-regulated protein folding and quality control in the ERCrystal structure of the C-terminal globular domain of the third paralog of the Archaeoglobus fulgidus oligosaccharyltransferasesSILAC-MS Based Characterization of LPS and Resveratrol Induced Changes in Adipocyte Proteomics - Resveratrol as Ameliorating Factor on LPS Induced ChangesOST4 is a subunit of the mammalian oligosaccharyltransferase required for efficient N-glycosylationQuantitative glycoproteomics analysis reveals changes in N-glycosylation level associated with pancreatic ductal adenocarcinoma.Two conserved oligosaccharyltransferase catalytic subunits required for N-glycosylation exist in Spartina alterniflora.N-linked glycosylation in Archaea: a structural, functional, and genetic analysis.Using pharmacological chaperones to restore proteostasisCharacterization of the structurally diverse N-linked glycans of Campylobacter species.Quantitative proteomics reveals the effect of protein glycosylation in soybean root under flooding stress.Synthesis, Processing, and Function of N-glycans in N-glycoproteins.Analysis of Sec61p and Ssh1p interactions in the ER membrane using the split-ubiquitin system.Mass spectrometry approach and ELISA reveal the effect of codon optimization on N-linked glycosylation of HIV-1 gp120N-glycosylation is required for secretion and mitosis in C. elegansGlucosidase II and MRH-domain containing proteins in the secretory pathway.Decreased TUSC3 Promotes Pancreatic Cancer Proliferation, Invasion and MetastasisTargeting the glycoproteomeThe Dependence of Carbohydrate-Aromatic Interaction Strengths on the Structure of the Carbohydrate.Molecular determinants of co- and post-translational N-glycosylation of type I transmembrane peptides.Integrative omics connects N-glycoproteome-wide alterations with pathways and regulatory events in induced pluripotent stem cells.Identification of GABA(C) receptor protein homeostasis network components from three tandem mass spectrometry proteomics approaches.ATP increases within the lumen of the endoplasmic reticulum upon intracellular Ca2+ release.Vertebrate protein glycosylation: diversity, synthesis and function.Glycoprotein folding and quality-control mechanisms in protein-folding diseasesSOX2 regulates multiple malignant processes of breast cancer development through the SOX2/miR-181a-5p, miR-30e-5p/TUSC3 axis.N-linked protein glycosylation in the endoplasmic reticulum.Protein transport into the human ER and related diseases, Sec61-channelopathies.Archaeal S-layer glycoproteins: post-translational modification in the face of extremesTUSC3 promotes colorectal cancer progression and epithelial-mesenchymal transition (EMT) through WNT/β-catenin and MAPK signalling.Cholinergic System and Post-translational Modifications: An Insight on the Role in Alzheimer's DiseaseTumor suppressor candidate 3 (TUSC3) prevents the epithelial-to-mesenchymal transition and inhibits tumor growth by modulating the endoplasmic reticulum stress response in ovarian cancer cells.TUSC3 loss alters the ER stress response and accelerates prostate cancer growth in vivo.Sequence-based protein stabilization in the absence of glycosylation.TUSC3: a novel tumour suppressor gene and its functional implications.N-Linked Glycosylation Is Required for Vacuolar H+ -ATPase (V-ATPase) a4 Subunit Stability, Assembly, and Cell Surface Expression.Protein Primary Structure of the Vaccinia Virion at Increased ResolutionDDOST mutations identified by whole-exome sequencing are implicated in congenital disorders of glycosylation.
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Oligosaccharyltransferase: the central enzyme of N-linked protein glycosylation.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 26 May 2011
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Oligosaccharyltransferase: the central enzyme of N-linked protein glycosylation.
@en
Oligosaccharyltransferase: the central enzyme of N-linked protein glycosylation.
@nl
type
label
Oligosaccharyltransferase: the central enzyme of N-linked protein glycosylation.
@en
Oligosaccharyltransferase: the central enzyme of N-linked protein glycosylation.
@nl
prefLabel
Oligosaccharyltransferase: the central enzyme of N-linked protein glycosylation.
@en
Oligosaccharyltransferase: the central enzyme of N-linked protein glycosylation.
@nl
P2093
P2860
P1476
Oligosaccharyltransferase: the central enzyme of N-linked protein glycosylation.
@en
P2093
Elisabeth Mohorko
Markus Aebi
Rudi Glockshuber
P2860
P2888
P304
P356
10.1007/S10545-011-9337-1
P577
2011-05-26T00:00:00Z