期刊
CHEMISTRY & BIOLOGY
卷 17, 期 11, 页码 1250-1255出版社
CELL PRESS
DOI: 10.1016/j.chembiol.2010.09.014
关键词
-
资金
- Wellcome Trust
- Lister Institute for Preventive Medicine
- College of Life Sciences
- MRC [G0900138] Funding Source: UKRI
- Medical Research Council [G0900138] Funding Source: researchfish
Posttranslational modification of metazoan nucleocytoplasmic proteins with N-acetylglucosamine (O-GlcNAc) is essential, dynamic, and inducible and can compete with protein phosphorylation in signal transduction. Inhibitors of O-GlcNAcase, the enzyme removing O-GlcNAc, are useful tools for studying the role of O-GlcNAc in a range of cellular processes. We report the discovery of nanomolar OGA inhibitors that are up to 900,000-fold selective over the related lysosomal hexosaminidases. When applied at nanomolar concentrations on live cells, these cell-penetrant molecules shift the O-GlcNAc equilibrium toward hyper-O-GlcNAcylation with EC50 values down to 3 nM and are thus invaluable tools for the study of O-GlcNAc cell biology.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据