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Mass spectrometry (MS) is an analytical technique used to improve the study of these proteins on the proteome level. 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 ...
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 ]
O-GlcNAc differs from other forms of protein glycosylation: (i) O-GlcNAc is not elongated or modified to form more complex glycan structures, (ii) O-GlcNAc is almost exclusively found on nuclear and cytoplasmic proteins rather than membrane proteins and secretory proteins, and (iii) O-GlcNAc is a highly dynamic modification that turns over more ...
O-GlcNAc modifications were only recently discovered, but the number of proteins with known O-GlcNAc modifications is increasing rapidly. [7] It is the first example of glycosylation that does not occur on secretory proteins. O-GlcNAc is added to the protein by O-GlcNAc transferase and is removed by O-GlcNAcase in a continuous cycle.
A mass spectrometer used for high throughput protein analysis. Protein mass spectrometry refers to the application of mass spectrometry to the study of proteins.Mass spectrometry is an important method for the accurate mass determination and characterization of proteins, and a variety of methods and instrumentations have been developed for its many uses.
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.
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 ...
Recently, paucimannosylation was reported to form an unconventional type of protein N-glycosylation in vertebrates. [3] It has been proposed that "higher" species including humans, rodents and other mammals use paucimannosylation in a more tissue- and context-restricted manner in pathophysiological conditions including cancer, [ 14 ] pathogen ...