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- W63237210 endingPage "350" @default.
- W63237210 startingPage "315" @default.
- W63237210 abstract "Oligosaccharides based on GalNAcα–Ser/Thr linkages (mucin-type O-glycans) found on many glycoproteins are highly diverse in their structures with multiple potential biological functions. Mucins and mucin-like glycoproteins on cell surfaces, as well as mucins in secretions, are especially rich in these O-glycans. The ranges of O-glycans are often shifted in disease states, which indicates that the biosynthesis of O-glycans is also abnormal and the expression and activities of the enzymes involved (glycosyltransferases and sulfotransferases) may be affected. O-glycans are assembled by the stepwise addition of individual sugar residues by specific glycosyltransferases and sulfotransferases. The assembly is controlled by the activities of transferases in the Golgi, their localization in specific compartments, and interaction with cofactors and other components of Golgi membranes. Golgi transferases exist as families with the individual members having similar but distinct substrate specificities and often different tissue-specific expression patterns. Modeling and crystal structures help to elucidate the protein folding and catalytic mechanisms of glycosyltransferases. These studies shed light on the complex regulation of O-glycan biosynthesis and help to identify mechanisms of O-glycan changes in diseases." @default.
- W63237210 created "2016-06-24" @default.
- W63237210 creator A5061857544 @default.
- W63237210 date "2010-01-01" @default.
- W63237210 modified "2023-09-23" @default.
- W63237210 title "Biosynthesis of Complex Mucin-Type O-Glycans" @default.
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