Stoichiometric Thiol Redox Proteomics for Quantifying Cellular Responses to Perturbations.
Stoichiometric Thiol Redox Proteomics for Quantifying Cellular Responses to Perturbations.
复制标题
化学计量硫醇氧化还原蛋白质组学用于定量细胞对扰动的反应。
DOI:
10.3390/antiox10030499
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发表时间:
2021-03-23
期刊:
影响因子:
--
通讯作者:
Qian WJ
中科院分区:
文献类型:
--
作者:
Day NJ;Gaffrey MJ;Qian WJ
Post-translational modifications regulate the structure and function of proteins that can result in changes to the activity of different pathways. These include modifications altering the redox state of thiol groups on protein cysteine residues, which are sensitive to oxidative environments. While mass spectrometry has advanced the identification of protein thiol modifications and expanded our knowledge of redox-sensitive pathways, the quantitative aspect of this technique is critical for the field of redox proteomics. In this review, we describe how mass spectrometry-based redox proteomics has enabled researchers to accurately quantify the stoichiometry of reversible oxidative modifications on specific cysteine residues of proteins. We will describe advancements in the methodology that allow for the absolute quantitation of thiol modifications, as well as recent reports that have implemented this approach. We will also highlight the significance and application of such measurements and why they are informative for the field of redox biology.
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