The researchers' next steps are to examine select proteins modified by O-GlcNAc and found at locations important for various steps in cell division to figure out why an imbalance of O-GlcNAc on the cells' proteins has such a dramatic effect on the process. The researchers were funded by the National Institute of Child Health and Human Development, the National Institute of Diabetes and Digestive and Kidney Diseases and the National Cancer Institute. Authors on the paper are Slawson, Natasha Zachara, Keith Vosseller, Win Den Cheung, Daniel Lane and Gerald Hart, all at Johns Hopkins while working on this project. Vosseller is now at Drexel University. O-GlcNAc modification of proteins is detected using an antibody developed at Johns Hopkins. Under a licensing agreement between Covance Research Products, Sigma Chemical Company and The Johns Hopkins University School of Medicine, Hart receives a percentage of royalties received by the university on sales of this antibody (CTD 110.6). The terms of this arrangement are being managed in accordance with the university's conflict of interest policy. 蛋白质的O位N-乙酰葡萄糖胺(O-GlcNAc)糖基化修饰是一种新近发现的广泛存在于细胞核蛋白与细胞浆蛋白的蛋白质翻译后修饰.其性质与经典的膜蛋白和分泌蛋白的糖基化修饰不同,而与蛋白质磷酸化修饰更相似。 (责任编辑:泉水) |