Journal
MOLECULAR & CELLULAR PROTEOMICS
Volume 17, Issue 1, Pages 2-17Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/mcp.MR117.000126
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Funding
- Hungarian Scientific Research Fund [105611]
- Economic Development and Innovation Operative Programmes from the Ministry for National Economy [GINOP-2.3.2-15-2016-00001, GINOP-2.3.2-15-2016-00020]
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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.
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