glycosylation

(redirected from O-linked glycosylation)
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Related to O-linked glycosylation: N-linked glycosylation

gly·co·sy·la·tion

 (glī′kō-sĭ-lā′shən)
n.
The addition of saccharides to proteins or lipids to form a glycoprotein or glycolipid.

[glycose, a monosaccharide (variant of glucose) + -yl + -ation.]

gly·co′sy·late′ v.

glycosylation

(ˌɡlaɪkəʊsəˈleɪʃən)
n
(Biochemistry) the process by which sugars are chemically attached to proteins to form glycoproteins
[from glycosyl radical derived from glycose + -ation]
References in periodicals archive ?
Mutations in GALNT3, encoding a protein involved in O-linked glycosylation, cause familial tumoral calcinosis.
In addition to N-linked glycosylation, O-linked glycosylation is believed to be involved in Nrf1 transcription activity.
The synthesized UDP-GlcNAc is transported from ER to the Golgi apparatus via the UDP-GlcNAc transporters and is then utilized as a donor substrate for the N- and O-linked glycosylation of extracellular and membrane proteins [9, 10].
Glycosylation sites analysis was performed using NetNGlyc 1.0 (http://www.cbs.dtu.dk/services/NetNGlyc/) for N-linked glycosylation sites and NetOGlyc 4.0 (http://www.cbs.dtu.dk/services/NetOGlyc/) for O-linked glycosylation sites, respectively.
O-linked glycosylation in higher eukaryotes occurs through several different mechanisms.
Taylor-Papadimitriou, "O-linked glycosylation in the mammary gland: changes that occur during malignancy," Journal of Mammary Gland Biology and Neoplasia, vol.
The O-linked glycosylation (also known as mucin type) is initiated in the Golgi compartment of human cells by the transfer of monosaccharide N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the hydroxyl groups of Ser/Thr residues in core polypeptides by a large family (~20) of GalNAc-transferases (ppGalNac-Ts or GalNAc-Ts; E.C.
Opdenakker, "Concepts and principles of O-linked glycosylation," Critical Reviews in Biochemistry and Molecular Biology, vol.
In the precursor structure, the midregion (proBNP 36-71) contains 7 serine and threonine residues, where O-linked glycosylation occurs either fully or partially (Fig.