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

(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.

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.
References in periodicals archive ?
The N-linked glycosylation study of [MSP1.sub.42]kDa protein sequence revealed the presence of two N-linked glycosylation points at amino acid position 281(NISQ) and 326(NPTC) as seen in figure 4.
The Asn residues targeted for N-linked glycosylation are located, with rare exceptions, within the consensus sequence Asn-X-Ser/Thr (where X is any amino acid except proline) [12].
Because there is no N-linked glycosylation site in preproBNP, our data indicate that secreted HMW proBNP is O-glycosylated (Fig.
The enzymes involved in modification of N-linked glycosylation of glycoproteins are found in the ER and the Golgi (Fig.) (6).
N-linked glycosylation was demonstrated by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF Ms), and attractiveness was verified in the T-maze assay.
The EAG channels also undergo N-linked glycosylation before its insertion into plasma membrane [38].
For influenza A viruses, modifications of N-linked glycosylation sites in the globular head of the hemagglutinin protein have been linked to changes in virulence, antigenicity, receptor-binding preference, fusion activity, and immune evasion (4).
Multiple sequence alignment revealed conserved leader sequence of 24 amino acids and a potential N-linked glycosylation site, that is, Asn-Thr-Thr at positions 64-66.
The consensus sequence for N-linked glycosylation is Asn-X-Ser or Asn-X-Thr, where X can be any amino acid but Pro (31).
The glycosylation tripeptide (N-Y-S) at residues [E.sub.154-156], which allows N-linked glycosylation at a conserved site on the E protein, domain I, and is associated with virulence in most WNV strains (23), was present in [WNV.sub.NSW2011]; its presence is consistent with the mAb recognition profile.
As a group, integrins are highly N-glycosylated, with some dimers, e.g., [alpha]5[beta]1 and [alpha]3[beta]1, possessing a total of 26 potential N-linked glycosylation sites (62).