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 ?
As discussed previously, Nrf1 is modified by N-linked glycosylation in the ER lumen.
The TML group has been studying glycosylation mechanisms to elucidate which mutations in patients affect the mechanisms of glycosylation.
To further verify the altered glycopatterns between DN and NDRD patients, lectin blotting was used to characterize the differences of glycosylation in protein level.
High-throughput ESI-MS/MS for glycopeptides, initially separated by LC, allows for the identification and quantification of all detectable features, which, in turn, provides a more detailed account of protein glycosylation patterns.
This suggests that EC-G (GlcNAc) and glucose are both involved in the proliferation/growth activity of the cells, whereas [sup.18]F-FDG is not in glycosylation process.
EGFR bears twelve N-linked glycosylation sites on the extracellular region (22) and is heavily glycosylated (23).
Services in Creative BioMart include: Annotate N-linked glycosylation, Annotate O-linked glycosylation, Annotate C-linked glycosylation, Annotate glycationn, Glycan staining or labeling, Glycoprotein purification or enrichment and Glycoproteome and Glycome Analysis by Mass Spectrometry.
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.
In the following, we will use the term "(NT-) proBNP" (NT-proBNP and/or proBNP) for better reading purposes, since the glycosylation positions are true for both peptides.
Although the early steps of glycosylation in the endoplasmic reticulum (ER) are very similar across eukaryotes, the structure of the final glycans is species specific due to differences in the oligosaccharide processing pathways [2, 3].

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