glycosylation

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glycosylation

[glī‚käs·ə′lā·shən]
(biochemistry)
A chemical reaction in which glycosyl groups are added to a protein to produce a glycoprotein.
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In addition to N-linked glycosylation, O-linked glycosylation is believed to be involved in Nrf1 transcription activity.
Glycosylation sites analysis showed that one N-linked glycosylation sites (N20) and eight O-linked glycosylation sites (T22, T24, T25, S33, S38, T41, T46 and S269) were found in the amino acid sequence according to NetNGlyc 1.0 Server and NetOGlyc 4.0 Server, respectively.
2-DG Interferes with N-Linked Glycosylation (NLG) and Induces Changes in the Metabolic Profile of Leukemic Cells In Vitro.
The N-linked glycosylation of [MSP1.sub.42]kDa protein was studied using NetNGlyc1.0 server of Technical University of Denmark (http://www.cbs.dtu.dk/services/NetNGlyc).
EX-CELL Glycosylation Adjust (Gal+) is an off-the-shelf protein quality supplement designed to achieve functionally relevant shifts in N-linked glycosylation quickly and efficiently, according to the company, and is highly concentrated, only requiring a small amount of product.
There are 12 potential N-linked glycosylation sites in the receptor, two in each of domains I and II and four in each of domains III and IV [14].
This insertion generates N-linked glycosylation. Interestingly, SAA4 is not completely glycosylated; two forms, glycosylated (G) and nonglycosylated (NG), are observed in plasma (Figure 1).
The eukaryotic N-linked glycosylation pathway is divided in two sequential stages: (a) synthesis in the rough endoplasmic reticulum (rER) of the dolichol-linked glycan precursor Dol-PP-GlcN[Ac.sub.2][Man.sub.3][Glc.sub.3] and its transfer to a nascent protein and (b) the N-linked glycan processing and maturation in the rER and Golgi (Figure 1).
The transmembrane domain of protein and N-linked glycosylation sites were analyzed using TMHMM Server v.2.0 (http://www.cbs.dtu.dk/services/TMHMM) and NetNGlyc 1.0 Server (http:// www.cbs.dtu.dk/services/NetNGlyc/), respectively.
The technology is said to genetically ligate an external amino acid domain to a therapeutic protein or peptide candidate which results in additional N-linked glycosylation.
Integrins, receptors and extracellular matrix (ECM) ligands display altered pattern of N-linked glycosylation in cells undergoing a malignant transformation (Janik et al.
Mobility shift caused by addition of tunicamyc in-a N-linked glycosylation inhibitor-to culture indicated the effect of glycosylation on the protein weight and SDS-PAGE protein band pattern.