Structural highlights
Publication Abstract from PubMed
O-GlcNAc transferase (OGT) glycosylates numerous proteins and is implicated in many diseases. To date, most OGT inhibitors lack either sufficient potency or characterized specificity in cells. We report the first targeted covalent inhibitor that predominantly reacts with OGT but does not affect other functionally similar enzymes. This study provides a new strategy to interrogate cellular OGT functions and to investigate other glycosyltransferases.
Targeted covalent inhibition of O-GlcNAc transferase in cells.,Worth M, Hu CW, Li H, Fan D, Estevez A, Zhu D, Wang A, Jiang J Chem Commun (Camb). 2019 Oct 31;55(88):13291-13294. doi: 10.1039/c9cc04560k. PMID:31626249[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Worth M, Hu CW, Li H, Fan D, Estevez A, Zhu D, Wang A, Jiang J. Targeted covalent inhibition of O-GlcNAc transferase in cells. Chem Commun (Camb). 2019 Oct 31;55(88):13291-13294. doi: 10.1039/c9cc04560k. PMID:31626249 doi:http://dx.doi.org/10.1039/c9cc04560k
