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人呼吸道合胞病毒P蛋白的C末端磷酸化主要发生在丝氨酸残基232处。

C-terminal phosphorylation of human respiratory syncytial virus P protein occurs mainly at serine residue 232.

作者信息

Sánchez-Seco M P, Navarro J, Martínez R, Villanueva N

机构信息

Servicio de Viroloía, Centro Nacional de Microbiología, Virología e Inmunología Sanitarias, Instituto de Salud Carlos III, Madrid, Spain.

出版信息

J Gen Virol. 1995 Feb;76 ( Pt 2):425-30. doi: 10.1099/0022-1317-76-2-425.

Abstract

To determine which human respiratory syncytial virus (HRSV) P protein serine residues are modified by cellular protein kinase(s), several mutated versions of P protein were expressed in the absence of other viral proteins. Mutations at serines 232 or 232 and 237 drastically reduced the extent of phosphorylation P protein in vivo. Serine 232 is the main site of modification and is also essential for in vitro phosphorylation by casein kinase II. Additional in vivo phosphorylation was also detected in the region containing serines 116, 117 and 119.

摘要

为了确定细胞蛋白激酶修饰的人呼吸道合胞病毒(HRSV)P蛋白丝氨酸残基,在没有其他病毒蛋白的情况下表达了几种P蛋白的突变体。丝氨酸232或丝氨酸232和237处的突变显著降低了体内P蛋白的磷酸化程度。丝氨酸232是主要修饰位点,对于酪蛋白激酶II的体外磷酸化也是必需的。在包含丝氨酸116、117和119的区域也检测到额外的体内磷酸化。

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