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Protein O-glycosylation analysis
bchm, 2012Abstract This review provides an overview on the methods available for analysis of O-glycosylation. Three major themes are addressed: analysis of released O-glycans including different O-glycan liberation, derivatization, and detection methods; analysis of formerly O-glycosylated peptides yielding information on O-glycan attachment sites;
Zauner, G. +5 more
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2003
Secreted as well as membrane-associated eukaryotic proteins are most commonly glycosylated. Saccharides are attached to proteins mainly through N-and O-glycosydic bonds or as part of the glycosylphosphatidyinositol-membrane anchor. In contrast to N-glycosylation, which involves the co-translational transfer in the endoplasmic reticulum (ER) of the ...
Juan J, Calvete, Libia, Sanz
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Secreted as well as membrane-associated eukaryotic proteins are most commonly glycosylated. Saccharides are attached to proteins mainly through N-and O-glycosydic bonds or as part of the glycosylphosphatidyinositol-membrane anchor. In contrast to N-glycosylation, which involves the co-translational transfer in the endoplasmic reticulum (ER) of the ...
Juan J, Calvete, Libia, Sanz
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One-pot synthesis of O-glycosyl triazoles by O-glycosylation–click reaction
Carbohydrate Research, 20132,3-Unsaturated-glycosyl triazoles were synthesized in a simple one-pot process under mild condition via tandem O-glycosylation using iodine promoter and a mild CuAAC reaction. Thirty examples of a variety of O-glycosyl triazoles were obtained in good to excellent yields and α-anomeric selectivity.
Wadchara, Mangsang +2 more
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O-Glycosylation of the Mucin Type
Biological Chemistry, 2001While only about ten percent of the databank entries are defined as glycoproteins, it has been estimated recently that more than half of all proteins are glycoproteins. Mucin-type O-glycosylation is a widespread post-translational modification of proteins found in the entire animal kingdom, but also in higher plants.
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Evidence for posttranslational O-glycosylation of fetuin
Biochemistry, 1986Fetuin, a major glycoprotein in the serum of fetal calves that contains three N-linked and three O-linked carbohydrate side chains, was found to be synthesized in the liver with an 18 amino acid signal peptide, Met-X-X-X-X-Leu-Leu-X-Cys-Leu-Ala-X-Leu-X-X-Cys-X-X, and to undergo cotranslational N-glycosylation.
W V, Johnson, E C, Heath
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Regulation of Notch Function by O-Glycosylation
2018The Notch receptor initiates a unique intercellular signaling pathway that is evolutionarily conserved across all metazoans and contributes to the development and maintenance of numerous tissues. Consequently, many diseases result from aberrant Notch signaling.
Beth M, Harvey, Robert S, Haltiwanger
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2009 Fifth International Conference on Intelligent Information Hiding and Multimedia Signal Processing, 2009
O-glycosylation of the mammalian protein is studied. It is serine or threonine specific, though any consensus sequence is still unknown. We have been applied support vector machines (SVM) for the prediction of O-glycosylation sites from various kinds of protein information, aiming to investigate a glycosylation condition and elucidate the mechanisms ...
Yukiko Nakajima +3 more
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O-glycosylation of the mammalian protein is studied. It is serine or threonine specific, though any consensus sequence is still unknown. We have been applied support vector machines (SVM) for the prediction of O-glycosylation sites from various kinds of protein information, aiming to investigate a glycosylation condition and elucidate the mechanisms ...
Yukiko Nakajima +3 more
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Use of O‐Glycosylation in Total Synthesis
ChemInform, 2005AbstractFor Abstract see ChemInform Abstract in Full Text.
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Methods in Enzymology: O‐Glycosylation of Proteins
2005Cell surface and extracellular proteins are O-glycosylated, where the most abundant type of O-glycosylation in proteins is the GalNAc attachment to serine (Ser) or threonine (Thr) in the protein chain by an a-glycosidic linkage. Most eukaryotic nuclear and cytoplasmic proteins modified by a-linked O-GlcNAc to Ser or Thr exhibit reciprocal O-GlcNAc ...
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Why are proteins O-glycosylated?
Trends in Biochemical Sciences, 1990The O-linked oligosaccharides of glycoproteins are usually clustered within heavily glycosylated regions of the peptide chain. Steric interactions between carbohydrate and peptide within these clusters induce the peptide core to adopt a stiff and extended conformation and this conformational effect appears to represent a major function of O ...
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