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首页> 外文期刊>Methods: A Companion to Methods in Enzymology >Characterization of histone post-translational modifications during virus infection using mass spectrometry-based proteomics
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Characterization of histone post-translational modifications during virus infection using mass spectrometry-based proteomics

机译:基于质谱型蛋白质组学的病毒感染期间组蛋白翻译后修饰的表征

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摘要

Viruses are obligate intracellular parasites that necessarily rely on hijacking cellular resources to produce viral progeny. The success of viral infection requires manipulation of host chromatin in order to activate genes useful for production of viral proteins as well as to suppress antiviral responses. Host chromatin manipulation on a global level is likely reliant on modulation of post-translational modifications (PTMs) on histone proteins. Mass spectrometry (MS) is a powerful tool to quantify and identify novel histone PTMs, beyond the limitations of site-specific antibodies. Here, we employ MS to investigate global changes in histone PTM relative abundance in human cells during infection with adenovirus. Our method reveals several changes in histone PTM patterns during infection. We propose that this method can be used to uncover global changes in histone PTM patterns that are universally modulated by viruses to take over the cell. (C) 2015 Elsevier Inc. All rights reserved.
机译:病毒迫使细胞内寄生虫,以依靠劫持细胞资源来产生病毒后代。 病毒感染的成功需要操纵宿主染色质,以激活可用于生产病毒蛋白的基因以及抑制抗病毒反应。 全球级别的宿主染色质操作可能依赖于组蛋白蛋白的翻译后修饰(PTMS)的调节。 质谱(MS)是一种能够量化和识别新型组蛋白PTM的强大工具,超出位点特异性抗体的局限性。 在这里,我们在用腺病毒感染期间雇用MS来研究人体细胞中组蛋白PTM相对丰度的全局变化。 我们的方法揭示了在感染期间组蛋白PTM模式的几种变化。 我们建议该方法可用于揭示由病毒普遍调制的组蛋白PTM模式的全局变化,以接管细胞。 (c)2015 Elsevier Inc.保留所有权利。

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