The GalNAc-type O-Glycoproteome of CHO cells characterized by the SimpleCell strategy
about
Multiple enzyme approach for the characterization of glycan modifications on the C-terminus of the intestinal MUC2mucin.Proteomic approaches for site-specific O-GlcNAcylation analysis.A strategy for O-glycoproteomics of enveloped viruses--the O-glycoproteome of herpes simplex virus type 1Probing the O-glycoproteome of gastric cancer cell lines for biomarker discovery.Fast and sensitive detection of indels induced by precise gene targeting.Deconstruction of O-glycosylation--GalNAc-T isoforms direct distinct subsets of the O-glycoproteome.Molecular basis of antibody binding to mucin glycopeptides in lung cancerO-glycosylation sites identified from mucin core-1 type glycopeptides from human serumOptimizing eukaryotic cell hosts for protein production through systems biotechnology and genome-scale modeling.New Mammalian Expression Systems.Genetic engineering of CHO cells for viral resistance to minute virus of mice.Chemical Glycoproteomics.Characterizing Glycoproteins by Mass Spectrometry in Campylobacter jejuni.A theoretical estimate for nucleotide sugar demand towards Chinese Hamster Ovary cellular glycosylation.A novel monoclonal antibody to a defined peptide epitope in MUC16.Cryptosporidium parvum vaccine candidates are incompletely modified with O-linked-N-acetylgalactosamine or contain N-terminal N-myristate and S-palmitateAnalysis of mammalian O-glycopeptides - we have made a good start, but there is a long way to go.The Role of Electron Transfer Dissociation in Modern Proteomics.CHO-Omics Review: The Impact of Current and Emerging Technologies on Chinese Hamster Ovary Based Bioproduction.Recent advances in methods for the analysis of protein o-glycosylation at proteome level.Conformational characterization of nerve growth factor-β reveals that its regulatory pro-part domain stabilizes three loop regions in its mature part.Site-specific O-glycosylation of members of the low-density lipoprotein receptor superfamily enhances ligand interactions.
P2860
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P2860
The GalNAc-type O-Glycoproteome of CHO cells characterized by the SimpleCell strategy
description
2014 nî lūn-bûn
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2014 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2014年の論文
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2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
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name
The GalNAc-type O-Glycoproteome of CHO cells characterized by the SimpleCell strategy
@ast
The GalNAc-type O-Glycoproteome of CHO cells characterized by the SimpleCell strategy
@en
The GalNAc-type O-Glycoproteome of CHO cells characterized by the SimpleCell strategy
@nl
type
label
The GalNAc-type O-Glycoproteome of CHO cells characterized by the SimpleCell strategy
@ast
The GalNAc-type O-Glycoproteome of CHO cells characterized by the SimpleCell strategy
@en
The GalNAc-type O-Glycoproteome of CHO cells characterized by the SimpleCell strategy
@nl
prefLabel
The GalNAc-type O-Glycoproteome of CHO cells characterized by the SimpleCell strategy
@ast
The GalNAc-type O-Glycoproteome of CHO cells characterized by the SimpleCell strategy
@en
The GalNAc-type O-Glycoproteome of CHO cells characterized by the SimpleCell strategy
@nl
P2093
P2860
P50
P356
P1476
The GalNAc-type O-Glycoproteome of CHO cells characterized by the SimpleCell strategy
@en
P2093
Eric Paul Bennett
Henrik Clausen
Hiren Jitendra Joshi
Katrine Ter-Borch Gram Schjoldager
Kevin J Kayser
Morten Alder Schulz
Natalie R Sealover
Sergey Y Vakhrushev
Steven B Levery
P2860
P304
P356
10.1074/MCP.M114.041541
P577
2014-08-04T00:00:00Z