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单纯疱疹病毒1型UL13蛋白激酶直接磷酸化的蛋白质的鉴定

Identification of proteins directly phosphorylated by UL13 protein kinase from herpes simplex virus 1.

作者信息

Asai Risa, Ohno Takashi, Kato Akihisa, Kawaguchi Yasushi

机构信息

Division of Viral Infection, Department of Infectious Disease Control, International Research Center for Infectious Diseases, The Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.

出版信息

Microbes Infect. 2007 Oct;9(12-13):1434-8. doi: 10.1016/j.micinf.2007.07.008. Epub 2007 Jul 31.

Abstract

Herpes simplex virus 1 (HSV-1) UL13 is a viral protein kinase that regulates optimal viral replication in cell cultures. Identification of substrates of protein kinases is a crucial step to elucidate the mechanism by which they function. Using our developed system to analyze the specific protein kinase activity of UL13, we have shown that UL13 protein kinase directly phosphorylates the viral proteins ICP22 and UL49 previously reported to be putative substrates. We also identified UL41 as a previously unreported and novel substrate of UL13. These data will serve as a basis to clarify the mechanism by which UL13 influences viral replication.

摘要

单纯疱疹病毒1型(HSV-1)UL13是一种病毒蛋白激酶,可调节细胞培养中病毒的最佳复制。鉴定蛋白激酶的底物是阐明其作用机制的关键步骤。利用我们开发的系统分析UL13的特异性蛋白激酶活性,我们发现UL13蛋白激酶可直接磷酸化先前报道的假定底物——病毒蛋白ICP22和UL49。我们还鉴定出UL41是UL13先前未报道的新底物。这些数据将为阐明UL13影响病毒复制的机制奠定基础。

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