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B19细小病毒非结构蛋白中一个假定的核苷三磷酸结合结构域是细胞毒性所必需的。

A putative nucleoside triphosphate-binding domain in the nonstructural protein of B19 parvovirus is required for cytotoxicity.

作者信息

Momoeda M, Wong S, Kawase M, Young N S, Kajigaya S

机构信息

Hematology Branch, National Heart, Lung, and Blood Institute, Bethesda, Maryland 20892.

出版信息

J Virol. 1994 Dec;68(12):8443-6. doi: 10.1128/JVI.68.12.8443-8446.1994.

Abstract

Cytotoxicity secondary to B19 parvovirus infection is due to expression of the viral nonstructural protein. Nonstructural proteins of many parvoviruses contain a well-conserved nucleoside triphosphate (NTP)-binding motif, which has been shown to be essential for a variety of protein functions. We show here that cytotoxicity of the B19 parvovirus nonstructural protein was abolished by single mutations of amino acids within the NTP-binding domain, especially within the A motif, implicating NTP-binding in virus-induced cell death.

摘要

继发于B19细小病毒感染的细胞毒性是由于病毒非结构蛋白的表达。许多细小病毒的非结构蛋白含有一个高度保守的核苷三磷酸(NTP)结合基序,已证明该基序对多种蛋白质功能至关重要。我们在此表明,NTP结合域内尤其是A基序内的氨基酸单点突变消除了B19细小病毒非结构蛋白的细胞毒性,这表明NTP结合与病毒诱导的细胞死亡有关。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b99d/237320/bfe04a62d09d/jvirol00021-0790-a.jpg

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