O-linked glycosylation - Wikipedia
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.
Glycosylation in health and disease - Nature Reviews Nephrology
2019年3月11日 · IgA1 has core 1 O-glycans (that is, GalNAc with β1,3-linked galactose), but in some diseases, including IgA nephropathy (IgAN), patients have elevated circulatory IgA1 with galactose-deficient O...
Current Methods for the Characterization of O-Glycans
2020年9月5日 · Synthetic O-glycopeptides were characterized by mass spectrometry. Released glycans were identical to those on the glycopeptide. O-Linked glycans from a range of glycoproteins of increasing complexity, namely, bovine serum fetuin, glycophorin A, and previously uncharacterized glycopeptides isolated from human salivary mucin Muc5B, were also ...
O-Glycans - Essentials of Glycobiology - NCBI Bookshelf
THE BIOSYNTHESIS AND BIOLOGY OF SERINE/THREONINE (O)-linked glycans (O-glycans) involving the GalNAc-peptide linkage are detailed in this chapter with an emphasis on vertebrate systems. Pathways involving the formation of the various O …
O-glycosylation and its role in therapeutic proteins - PMC
When the glycans are linked to Ser or Thr residues, they are known as O-linked glycans, as the glycosidic linkage is through oxygen. O-glycans are perhaps best known as part of the mucin proteins, however many soluble proteins carry these types of glycans, and that their roles in biology are still being discovered.
O-glycosylation and its role in therapeutic proteins
When the glycans are linked to Ser or Thr residues, they are known as O-linked glycans, as the glycosidic linkage is through oxygen. O-glycans are perhaps best known as part of the mucin proteins, however many soluble proteins carry these types of glycans, and that their roles in biology are still being discovered.
Global view of human protein glycosylation pathways and functions - Nature
2020年10月21日 · Glycans are attached to proteins in four different ways — N-linked to asparagine (Asn), O-linked to the hydroxyl groups of serine (Ser), threonine (Thr) or tyrosine (Tyr), C-linked to...
Review of O-Linked Glycoproteins - MilliporeSigma
O-Linked glycans are most commonly attached to the peptide chain through serine (Ser) or threonine (Thr) residues. While O-linkage does link primarily to peptide residues through a hydroxyl group, there is no consensus sequence required.
O-Linked Glycosylation - an overview | ScienceDirect Topics
O-glycosylation occurs in the periplasm and the O-linked glycan (in the case of B. fragilis) consists of nine sugars (with a molecular mass of 1550.6 Da) that are added to Ser and Thr residues within the three amino acid motif D(S,T)(A,L,V,I,M,T).
Concepts and principles of O-linked glycosylation - PubMed
The biosynthesis, structures, and functions of O-glycosylation, as a complex posttranslational event, is reviewed and compared for the various types of O-glycans. Mucin-type O-glycosylation is initiated by tissue-specific addition of a GalNAc-residue to …