Department of Biochemistry, Section on Molecular Medicine, Wake Forest School of Medicine, Winston-Salem, NC 27157, U.S.A.
Center for Redox Biology and Medicine, Section on Molecular Medicine, Wake Forest School of Medicine, Winston-Salem, NC 27157, U.S.A.
Essays Biochem. 2020 Feb 17;64(1):1-17. doi: 10.1042/EBC20190050.
Oxidative modifications of cysteine thiols in cellular proteins are pivotal to the way signal-stimulated reactive oxygen species are sensed and elicit appropriate or sometimes pathological responses, but the dynamic and often transitory nature of these modifications offer a challenge to the investigator trying to identify such sites and the responses they elicit. A number of reagents and workflows have been developed to identify proteins undergoing oxidation and to query the timing, extent and location of such modifications, as described in this minireview. While no approach is perfect to capture all the redox information in a functioning cell, best practices described herein can enable considerable insights into the "redox world" of cells and organisms.
细胞蛋白质中半胱氨酸巯基的氧化修饰对于感应信号刺激的活性氧并引发适当或有时病理性反应的方式至关重要,但这些修饰的动态性和短暂性常常给试图识别这些修饰位点及其引发的反应的研究人员带来挑战。本文综述描述了许多已经开发出来的用于识别发生氧化的蛋白质并查询这些修饰的时间、程度和位置的试剂和工作流程。虽然没有一种方法可以完美地捕获功能细胞中的所有氧化还原信息,但本文中描述的最佳实践可以使人们对细胞和生物体的“氧化还原世界”有更深入的了解。