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 ?
Guanosine diphosphatase is required for protein and sphingolipid glycosylation in the Golgi lumen of Saccharomyces cerevisiae.
Factors controlling the glycosylation potential of the Golgi apparatus.
Trafficking and localization of resident Golgi glycosylation enzymes.
Role of glycosylation on the conformation and chain dimensions of O-linked glycoproteins: light-scattering studies of ovine submaxillary mucin.
Expression of human glycophorin A in wild type and glycosylation-deficient Chinese hamster ovary cells: role of N- and O-linked glycosylation in cell surface expression.
Serum "big insulin-like growth factor II" from patients with tumor hypoglycemia lacks normal E-domain O-linked glycosylation, a possible determinant of normal propeptide processing.
Mutations in GALNT3, encoding a protein involved in O-linked glycosylation, cause familial tumoral calcinosis.
Congenital muscular dystrophy with glycosylation defects of [alpha]-dystroglycan in Japan.
Mutations in the fukutin-related protein gene (FKRP) cause a form of congenital muscular dystrophy with secondary laminin [alpha]2 deficiency and abnormal glycosylation of [alpha]-dystroglycan.
Mutations in the human LARGE gene cause MDC1D, a novel form of congenital muscular dystrophy with severe mental retardation and abnormal glycosylation of [alpha]-dystroglycan.
The role of defective glycosylation in congenital muscular dystrophy.
LARGE can functionally bypass [alpha]-dystroglycan glycosylation defects in distinct congenital muscular dystrophies.

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