中文摘要：

半胱氨酸的巯基具有很高的反应活性,作为亲核、氧化还原催化反应、金属结合及变构调节位点等在蛋白质的结构和功能中发挥着非常重要的作用,且容易发生多种翻译后修饰,调控亦或损伤蛋白功能,与人类许多重要疾病关系密切,因此,定性与定量分析蛋白质半胱氨酸上的翻译后修饰组对理解其生物学功能具有重要意义。本文综述了近年来蛋白质半胱氨酸上常见的翻译后修饰组的质谱和蛋白质组学分析方法进展。

英文摘要：

Cysteine thiols have high reaction activity and play significant roles in protein structures and functions as the sites of nucleophilic,redox catalysis,metal binding and allosteric regulation. Due to the reactivity of the thiol group,cysteine residues are very prone to post-translational modifications（PTMs）such as oxidation,lipidation,and so on,which can regulate / damage protein functions and are associated with many diseases. Thus,it is very important to qualitatively and quantitatively analyze PTMs in the cysteine residues for further understanding its biological functions. This review mainly focuses on the development of mass spectrometric and high-throughput proteomic approaches for investigating some commoncysteine posttranslational modifications.