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IndexCopernicus Journal Abstract
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The review of O-GlcNAc modification [ O-GlcNAc修饰研究进展 ] Huadong Liu, Yongxiang Chen, Yanmei Li SciencePaper Online 2007; 2(8):543-549 ICID: 878691 |
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| Article type: Editorial | ||
| IC™ Value: 2.40 | ||
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| A hallmark of signal transduction is the dynamic and inducible post-translational modification of proteins. In addition to the well characterized phosphorylation of proteins, many nuclear and cytoplasmic proteins are covalently modified by the linkage of monosaccharide N-acetylglucosamine (GlcNAc) to serine or threonine, a reaction catalyzed by O-GlcNAc transferase (OGT). More and more evidences have indicated that the O-GlcNAc modification has the yin–yang relationship with phosphorylation. Herein, newly results about enzymes and substrate were reviewed. | ||
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: O-GlcNAc糖基化修饰作为一种特殊的蛋白质翻译后修饰形式，动态调节细胞信号传导途径中很多酶的功能，与磷酸修饰有“阴阳调节”关系，正在成为研究的热点。本文综述了近年来O-GlcNAc糖基化修饰酶及其供体底物的研究进展。 |
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ICID 878691 |
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