Stoichiometric Thiol Redox Proteomics for Quantifying Cellular Responses to Perturbations.

Stoichiometric Thiol Redox Proteomics for Quantifying Cellular Responses to Perturbations.
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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:
Antioxidants (Basel, Switzerland)
影响因子:
--
通讯作者:
Qian WJ
Qian WJ
中科院分区:
其他
文献类型:
--
作者:
Day NJ;Gaffrey MJ;Qian WJ

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翻译后修饰可以调节蛋白质的结构和功能,从而导致不同途径的活性发生变化。这些修饰包括改变蛋白质半胱氨酸残基上硫醇基团的氧化还原状态,半胱氨酸残基对氧化环境敏感。虽然质谱学促进了蛋白质硫醇修饰的鉴定,并扩大了我们对氧化还原敏感途径的了解,但这项技术的定量方面对氧化还原蛋白质组学领域至关重要。在这篇综述中,我们描述了基于质谱学的氧化还原蛋白质组学如何使研究人员能够准确地定量蛋白质特定半胱氨酸残基上可逆氧化修饰的化学计量比。我们将描述允许硫醇修饰绝对定量的方法的进展,以及最近实施这一方法的报告。我们还将强调这种测量的意义和应用,以及为什么它们对氧化还原生物学领域具有信息性。
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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