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In addition, glycosylation is often used by viruses to shield the underlying viral protein from immune recognition. A significant example is the dense glycan shield of the envelope spike of the human immunodeficiency virus. [8] Overall, glycosylation needs to be understood by the likely evolutionary selection pressures that have shaped it.
Glycosylation contributes to several concerted biological mechanisms essential to maintaining physiological function. The study of the glycosylation of proteins is important to understanding certain diseases, like cancer, because a connection between a change in glycosylation and these diseases has been discovered.
The process of glycosylation (binding a carbohydrate to a protein) is a post-translational modification, meaning it happens after the production of the protein. [3] Glycosylation is a process that roughly half of all human proteins undergo and heavily influences the properties and functions of the protein. [ 3 ]
In contrast with glycation, glycosylation is the enzyme-mediated ATP-dependent attachment of sugars to a protein or lipid. [1] Glycosylation occurs at defined sites on the target molecule. It is a common form of post-translational modification of proteins and is required for the functioning of the mature protein.
The spike protein is a trimeric structure, with each subunit containing 22 N-glycosylation sites, making it an attractive target for vaccine search. [ 3 ] [ 4 ] Glycosylation, i.e., the addition of glycans (a generic name for monosaccharides and oligosaccharides ) to a protein, is one of the major post-translational modification of proteins ...
The different types of lipid-linked oligosaccharide (LLO) precursor produced in different organisms.. N-linked glycosylation is the attachment of an oligosaccharide, a carbohydrate consisting of several sugar molecules, sometimes also referred to as glycan, to a nitrogen atom (the amide nitrogen of an asparagine (Asn) residue of a protein), in a process called N-glycosylation, studied in ...
Glycosylphosphatidylinositol (pronunciation ⓘ) or glycophosphatidylinositol (GPI) is a phosphoglyceride that can be attached to the C-terminus of a protein during posttranslational modification. The resulting GPI-anchored proteins play key roles in a wide variety of biological processes. [ 1 ]
O-linked glycosylation is the attachment of a sugar molecule to the oxygen atom of serine (Ser) or threonine (Thr) residues in a protein. O -glycosylation is a post-translational modification that occurs after the protein has been synthesised.