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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >The γ_134.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1α to dephosphorylate the α subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated p
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The γ_134.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1α to dephosphorylate the α subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated p

机译:单纯疱疹病毒1的γ_134.5蛋白与蛋白磷酸酶1α结合,使真核翻译起始因子2的α亚基去磷酸化,并阻止双链RNA激活的p关闭蛋白合成

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摘要

In human cells infected with herpes simplex virus 1 the double-stranded RNA-dependent protein kinase (PKR) is activated but phosphorylation of the subunit of eukaryotic translation initiation factor 2 (eIF-2) and total shutoff of protein synthesis is observed only in cells infected with γ_1z34.5~ mutants. The carboxyl-terminal 64 aa of γ_134.5 protein are homologous to the corresponding domain of MyD116, the murine growth arrest and DNA damage gene 34 (GADD34) protein and the two domains are functionally interchangeable in infected cells.
机译:在感染单纯疱疹病毒1的人类细胞中,双链RNA依赖性蛋白激酶(PKR)被激活,但仅在细胞中观察到真核翻译起始因子2(eIF-2)亚基的磷酸化和蛋白质合成的完全关闭感染了γ_1z34.5〜突变体。 γ_134.5蛋白的羧基末端64aa与MyD116的相应结构域,鼠生长停滞和DNA损伤基因34(GADD34)蛋白同源,并且这两个结构域在感染细胞中在功能上可互换。

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