| Literature DB >> 29162637 |
Zsuzsanna Darula1, Katalin F Medzihradszky2,3.
Abstract
Glycosylation is perhaps the most common post-translational modification. Recently there has been growing interest in cataloging the glycan structures, glycoproteins, and specific sites modified and deciphering the biological functions of glycosylation. Although the results are piling up for N-glycosylation, O-glycosylation is seriously trailing behind. In our review we reiterate the difficulties researchers have to overcome in order to characterize O-glycosylation. We describe how an ingenious cell engineering method delivered exciting results, and what could we gain from "wild-type" samples. Although we refer to the biological role(s) of O-glycosylation, we do not provide a complete inventory on this topic.Entities:
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Year: 2017 PMID: 29162637 PMCID: PMC5750848 DOI: 10.1074/mcp.MR117.000126
Source DB: PubMed Journal: Mol Cell Proteomics ISSN: 1535-9476 Impact factor: 5.911