glycosylation

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glycosylation

[glī‚käs·ə′lā·shən]
(biochemistry)
A chemical reaction in which glycosyl groups are added to a protein to produce a glycoprotein.
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References in periodicals archive ?
The TML group has been studying glycosylation mechanisms to elucidate which mutations in patients affect the mechanisms of glycosylation.
One of our strategic objectives is to combine the analysis of PTMs and intact proteins to develop novel personalized diagnostics, as we recently did for the intact glycoprotein transferrin that we apply to diagnose specific subtypes of congenital disorders of glycosylation."
Development of chemo-enzymatic glycosylations based on substrate design of glycosyl donors
In 1986, he moved to Tohoku University and joined the lab of Professor Shiro Kobayashi in the field of polymer synthesis, where he developed new chemo-enzymatic glycosylations by using glycosyl fluorides and sugar oxazolines as glycosyl donors.
His research interests include synthesis of carbohydrates, development of novel glycosylations, macromolecular architecture and precision synthesis of well-designed functional oligo- and polysaccharides.
The diseases in this pathway have collectively been referred to as congenital disorders of glycosylation (CDG).
This posttranslational modification is more analogous to phosphorylation than to classical complex O-glycosylation because it is a reversible process catalyzed by the enzymes O-GlcNAc transferase and O-GlcNAcase, respectively (12), and the "normal glycosylation machinery" is not implicated (12, 13).
N-linked glycosylation sites and Cys residues were found to be located in the same position in all species.
One of the hot topics in biopharm focuses on a better understanding of the glycosylation of biotherapeutics.
Food and Drug Administration (FDA), the European Medicines Agency (EMA) and other regulatory bodies are increasing pressure on manufacturers to analyze the glycosylation of therapeutics more fully, and to demonstrate how their processes can affect glycan composition," says StJean Skilton, Senior Manager, Late Stage Development, Waters Corp., Milford, Mass.
GLYCOSYLATION OF proBNP AT T71-RESIDUE CONTROLS THE LEVELS OF EXTRACELLULAR proBNP
2 and 3), we hypothesized that the glycosylation at the T71 residue also plays the key role in the secretion of glycosylated proBNP.

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