Citation: ZHANG Xiao-Qin, CHEN Chuan, FANG Cai-Yun, LU Hao-Jie. Progress of Analytical Methods for Protein Cysteine Post-translational Modifications[J]. Chinese Journal of Analytical Chemistry, ;2016, 44(11): 1771-1779. doi: 10.11895/j.issn.0253-3820.160626 shu

Progress of Analytical Methods for Protein Cysteine Post-translational Modifications

Department of Chemistry and Institutes of Biomedical Sciences, Fudan University, Shanghai 200433, China

Received Date: 23 August 2016
Revised Date: 26 September 2016

Fund Project: This work was supported by the National Natural Science Foundation of China (Nos. 21205018, 21335002)

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 post-translational modifications.
- Cysteine,
- Post-translational modifications,
- Mass spectrometry,
- Proteomics,
- Review
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