Search results
Results from the WOW.Com Content Network
The function of protein paucimannosylation remains largely unexplored in vertebrates. Recent literature however has emerged demonstrating that paucimannosylation play roles in mediating pathophysiological processes such as in inflammation, pathogen infection, cancer and in the development of stem cells and in normal homeostasis.
O-GlcNAc transferase is a part of a host of biological functions within the human body. OGT is involved in the resistance of insulin in muscle cells and adipocytes by inhibiting the Threonine 308 phosphorylation of AKT1, increasing the rate of IRS1 phosphorylation (at serine 307 and serine 632/635), reducing insulin signaling, and glycosylating ...
The best characterised O-mannosylated human protein is α-dystroglycan. [16] O-Man sugars separate two domains of the protein, required to connect the extracellular and intracellular regions to anchor the cell in position. [18] Ribitol, xylose and glucuronic acid can be added to this structure in a complex modification that forms a long sugar ...
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]
There are over 100 different glycosyltransferases involved in the synthesis of protein-bound and lipid-bound oligosaccharides. UDP-N-acetylglucosamine:alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I is a medial-Golgi enzyme essential for the synthesis of hybrid and complex N-glycans. The protein, encoded by a single exon, shows ...
These can be divided into four groups: disorders of protein N-glycosylation, disorders of protein O-glycosylation, disorders of lipid glycosylation and disorders of other glycosylation pathways and of multiple glycosylation pathways. No effective treatment is known for any of these disorders. 80% of these affect the nervous system.
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 ...
Glycoproteomics is a branch of proteomics that identifies, catalogs, and characterizes proteins containing carbohydrates as a result of post-translational modifications. [1] Glycosylation is the most common post-translational modification of proteins, but continues to be the least studied on the proteome level. [2]