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.

Protein glycosylation is ubiquitous throughout biology. From bacteria to humans, this post translational modification with sophisticated carbohydrate structures plays a profound role in the interaction of proteins with cells and changes the physiochemical properties of …

2016年8月17日 · Significant development in the area of chemical O-glycosylation strategies is evident from the literature. These novel approaches offer a solid platform to deal with various complex oligosaccharides relevant for biological applications.

O -Glycosylation in general has impact on a diversity of biological processes covering cellular aspects (targeted transport of glycoproteins), molecular aspects (protein conformation, resistance to proteolysis), and aspects involved in cellular communication (cell …

This review provides insights on the molecular mechanism underlying O-glycan biosynthesis and modification, and highlights illustrative examples of diseases that are triggered or modulated by aberrant cellular O-glycosylation.

2024年8月5日 · O -glycosylation is mainly classified into two types: O -GlcNAcylation and O -GalNAcylation. Since the 2010s, the close connection between O -glycosylation and physiological processes such...

Mucin type O-glycosylation is one of the most diverse types of glycosylation, playing essential roles in tissue development and homeostasis. In complex organisms, O-GalNAc glycans comprise a substantial proportion of the glycocalyx, with defined …

Protein glycosylation is ubiquitous throughout biology. From bacteria to humans, this post translational modification with sophisticated carbohydrate structures plays a profound role in the interaction of proteins with cells and changes the physiochemical properties of …

O-linked glycosylation is a true post-translational event that occurs in the golgi, and no oligosaccharide precursor is required for protein transfer. The serine/threonine residues are modified directly by covalent addition of N-acetylgalactosamine residues. Initiation of mucin-type O-glycosylation is dependent upon polypeptide N ...

O-glycosylation is a process in which complex sugars, called glycans, are attached to the oxygen atom (O) of specific amino acids, typically serine or threonine, within proteins. This modification is essential for maintaining the stability, proper folding, and overall function of proteins.