glycan

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Related to Glycans: glycosylation, Glycosaminoglycans

glycan

[′glī‚kan]
(biochemistry)
References in periodicals archive ?
With the intention of optimize the glycoproteins synthesis process, which was hindered by the limitations from homogeneous glycans obtaining, production of the protein backbone, and linkage between glycan and protein backbone, scientists in Creative Biolabs summarize existing knowledge and technologies to propose enhanced glycoprotein synthesis approaches such as native chemical ligation, bacterial oligosaccharyltransferase, glycoprotein remodeling, and in vivo suppressor tRNA technology.
Gagneux and colleagues explained in their study that the uterine cells express a receptor that recognizes a glycan molecule on the surface of sperm cells.
Transferrin and its glycan isoform in cerebrospinal fluid (CSF)
Trainees will have access to leading-edge glycan research technologies at each of the participating institutions.
Glycobiology, which is the study of the structure, function and biology of carbohydrates, also called glycans, is a fast-growing and important field of study in life sciences.
Palo Alto, CA, July 13, 2018 --(PR.com)-- PREMIER Biosoft today announced that Jonathan Bones, Ph.D., has joined its Scientific Advisory Board (SAB) to assist the company in its efforts to offer solutions in glycan analysis for Bio-pharmaceuticals.
Dr Sharad Purohit, co-investigator and author, said, "Proteins determine cell function and about half the proteins we make are modified by glycans in a continuous and fundamental biochemical process".
Comparison of the methods for profiling glycoprotein glycans - HUPO Human Disease Glycomics/Proteome Initiative multi-institutional study.
N-Linked glycans are involved in many biological processes such as protein folding, cell-cell interaction, and immune response [1,2].
Glycans are a constituent of lipopolysaccharides, glycoproteins, and glycolipids, and being surface antigens in microorganisms and viruses, they play a key role in the immune recognition of self and foreign antigens.
Glycan microarray analysis showed that A/New York/108/2016 bound preferentially to [alpha]-2,3 avian-like receptors but also showed binding to the [alpha]-2,6 glycan with internal sialoside (LSTb, glycan #60), as well as to glycans with mixed [alpha]-2,3/[alpha]-2,6 receptors (Figure 1).
Sialylated glycans significantly changes during development depending on the manner of cell and tissue type (5).