Proteomic approaches to the characterization of protein thiol modification.

Proteomic approaches to the characterization of protein thiol modification.
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DOI:
10.1016/j.cbpa.2010.11.003
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发表时间:
2011-02
影响因子:
7.8
通讯作者:
Murphy, Michael P.
Murphy, Michael P.
中科院分区:
生物学2区
文献类型:
--
作者:
Chouchani, Edward T.;James, Andrew M.;Fearnley, Ian M.;Lilley, Kathryn S.;Murphy, Michael P.

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蛋白质半胱氨酸残基是氧化还原信号传导的中心,并通过与活性氧和氮物种以及亲电体的相互作用来保护免受氧化损伤。虽然有相当多的证据表明半胱氨酸修饰的功能作用,大多数蛋白质巯基改变的身份和生理意义是未知的。鉴定参与这些过程的候选蛋白质的一种方法是利用近年来开发的蛋白质组学方法,用于鉴定响应氧化还原信号或氧化损伤而经历半胱氨酸修饰的蛋白质。这些工具已被证明在发现氧化还原修饰的新蛋白质靶点方面是有效的,并且是重要的第一步,可以更好地理解反应性分子如何有助于信号传导和损伤。在这里,我们讨论了一些这些方法和它们的应用程序来识别各种半胱氨酸为中心的氧化还原修饰。
Protein cysteine residues are central to redox signaling and to protection against oxidative damage through their interactions with reactive oxygen and nitrogen species, and electrophiles. Although there is considerable evidence for a functional role for cysteine modifications, the identity and physiological significance of most protein thiol alterations are unknown. One way to identify candidate proteins involved in these processes is to utilize the proteomic methodologies that have been developed in recent years for the identification of proteins that undergo cysteine modification in response to redox signals or oxidative damage. These tools have proven effective in uncovering novel protein targets of redox modification and are important first steps that allow for a better understanding of how reactive molecules may contribute to signaling and damage. Here, we discuss a number of these approaches and their application to the identification of a variety of cysteine-centered redox modifications.
DOI: 10.1042/bj20100633
发表时间: 2010-08-15
期刊: The Biochemical journal
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Chouchani ET;Hurd TR;Nadtochiy SM;Brookes PS;Fearnley IM;Lilley KS;Smith RA;Murphy MP
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