glycosylation

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glycosylation

 [gli-ko″-sĭ-la´shun]
the formation of linkages with glycosyl groups.

gly·co·sy·la·tion

(glī'kō-si-lā'shŭn),
Formation of linkages with glycosyl groups, as between d-glucose and the hemoglobin chain to form the fraction hemoglobin AIc, the level of which rises in association with the elevated concentration of d-glucose in blood concentration in poorly controlled or uncontrolled diabetes mellitus.
See also: glycosylated hemoglobin.

glycosylation

/gly·co·syl·a·tion/ (gli-ko″sĭ-la´shun) the formation of linkages with glycosyl groups.

glycosylation

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

gly·co′sy·late′ v.

glycosylation

[glīkə′səlā′shən]
the formation of linkages with glycosyl groups, covalently attaching a carbohydrate to another molecule.

gly·co·sy·la·tion

(glī'kō-si-lā'shŭn)
Formation of linkages with glycosyl groups, as between d-glucose and the hemoglobin chain to form the fraction hemoglobin AIc, the level of which rises in association with the raised blood d-glucose concentration in poorly controlled or uncontrolled diabetes mellitus.
See also: glycosylated hemoglobin

glycosylation

the addition of a CARBOHYDRATE to an organic molecule such as a PROTEIN.

glycosylation (glī·kōˈ·s·lāˑ·shn),

n process in which a carbohydrate is covalently attached to another molecule.

glycosylation

the formation of linkages with glycosyl groups.

N-linked glycosylation
attachment of oligosaccharides, synthesized on a dolichol-lipid platform to proteins through the amino acid asparagine spaced close to threonine or serine in the polypeptide sequence.
O-linked glycosylation
attachment of groups of oligosaccharides directly to proteins through the hydroxyl group of threonine.
References in periodicals archive ?
His research interests include synthesis of carbohydrates, development of novel glycosylations, macromolecular architecture and precision synthesis of well-designed functional oligo- and polysaccharides.
Elements of accelerators that can be used for glycosyl fluoride method (yellow shading) compared with accelerators that have been used for classical glycosylations (red shading).
Since 1976, I have consistently devoted my effort to finding new glycosylation reactions as basic and general tools for maintaining glyco-science.
Interestingly, in spite of the large bond-dissociation energy of the C-F bond, the desired glycosylation reaction proceeded smoothly with Sn[Cl.
In this glycosylation reaction, it is assumed that Sn[Cl.
As observed in patients with CDG-Ia and CDG-Ib, aberrant glycosylation results from insufficient availability of GDP-Man.
The tight regulation of the biosynthesis of nucleotide sugars means that alterations in a single nucleotide sugar can significantly impair glycosylation.
The nucleotide sugars are biosynthesized in the cytosol, and their monosaccharides must be translocated into the lumen of the ER and/or Golgi before they can be used for the glycosylation process.
As observed in the case of patients with CDG-IIc who have a deficient GDP-Fuc transporter (FUCT) (48) and in a patient with CDG-IIf who has a deficient CMP-NeuAc transporter (49), abnormal glycosylation results from diminished NST function.
Moreover, the T71A mutant, which ablates one of the O-glycosylation sites near the proBNP cleavage site (71TLRAPR [down arrow] S, with T71 glycosylation site and RXXR 2 [down arrow] protease recognition/cleavage sequence), resulted in severe reduction in the extracellular proBNP.
reported that deglycosylation of proBNP or disruption of the O-glycosylation at T71 were necessary for furin to process proBNP, suggesting that glycosylation of proBNP at T71 masks the furin recognition site (18).
As for the problem of glycosylation masking the convertase recognition site, the study by Seferian et al.

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