This type of O-glycosylation is one of the most abundant forms of glycosylation, and it is differentially regulated in cells by expression of a subset of homologous polypeptide GalNAc-transferases. Here, we have genetically engineered CHO cells to produce homogeneous truncated O-glycans, so-called...
Mucin-type O-glycosylation is initiated by a large family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-Ts) that target different proteins and are differentially expressed in cells and organs. Here, we investigated the expression patterns of all of the GalNAc-Ts in colon ...
COMMUNICATIONS | DOI: 10.1038/ncomms7937 Mucin-type (GalNAc-type) O-glycosylation is by far the most differentially and complex regulated type of protein glycosylation, and likely the most abundant with over 80% of all proteins passing through the secretory pathway that is predicted to be O-...
occurs on serine/Threonine (Ser/Thr) of peptide chain, and the sugar chain and Ser/Thr side chain hydroxyl generate O - Glycosidic bond under enzyme catalysis. A common type of O-glycosylation modification starts with GalNAc, forming O-GlacNAc bonds, known as mucin like O-glycosylation....
O-GalNAc glycosylation decorates over 80% of secretory and cell surface proteins3. It confers many critical biological functions ranging from structural roles to immune responses and cell-cell interactions. For example, mucin is a major part of the mucosal barrier on gastrointestinal, respiratory, ...
The initiation of mucin-type O-glycosylation is catalysed by a family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (EC 2.4.1.41). These enzymes are responsible for the transfer of N-acetylgalactosamine from the nucleotide sugar donor, UDP-GalNAc, to the hydroxyl group on specific ...
GalNAc-type (mucin-type) O-glycosylation (hereafter simply O-glycosylation) is arguably one of the most abundant and complex types of protein glycosylation, and it is predicted that over 80% of proteins passing through the secretory pathway are O-glycosylated (1). O-Glycosylation is initiated by...
Mucin type O-glycosylation is initiated by a large family of polypeptide GalNAc transferases (ppGalNAc Ts) that add 伪- GalNAc to the Ser and Thr residues of peptides. Of the 20 human isoforms, all but one are composed of two globular domains linked by a short flexible linker: a ...
The Initiation of Mucin Type O-glycosylation: Development of a Web-Based Tool for the Prediction of ppGalNAc T Isoform Specific O-Glycosylation 来自 ResearchGate 喜欢 0 阅读量: 21 作者:TA Gerken,G Cardenas,I Almeida,MY Leung 会议时间: 2011/11/01 ...
The glycosylation of serine and threonine residues during mucin-type O-linked protein glycosylation is catalyzed by a family of polypeptide GalNAc transferases (EC 2.4.1.41). Five distinct GalNAc-transferase genes termed GalNAc-T1, -T2, -T3, -T4 and -T5 have been cloned and characterized. Homa...