Defining the S-Glutathionylation Proteome by Biochemical and Mass Spectrometric Approaches.

Defining the S-Glutathionylation Proteome by Biochemical and Mass Spectrometric Approaches.
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DOI:
10.3390/antiox11112272
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发表时间:
2022-11-17
期刊:
影响因子:
7
通讯作者:
Qian, Wei-Jun
Qian, Wei-Jun
中科院分区:
医学2区
文献类型:
--
作者:
Li, Xiaolu;Zhang, Tong;Day, Nicholas J. J.;Feng, Song;Gaffrey, Matthew J. J.;Qian, Wei-Jun

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Protein S-glutathionylation (SSG) is a reversible post-translational modification (PTM) featuring the conjugation of glutathione to a protein cysteine thiol. SSG can alter protein structure, activity, subcellular localization, and interaction with small molecules and other proteins. Thus, it plays a critical role in redox signaling and regulation in various physiological activities and pathological events. In this review, we summarize current biochemical and analytical approaches for characterizing SSG at both the proteome level and at individual protein levels. To illustrate the mechanism underlying SSG-mediated redox regulation, we highlight recent examples of functional and structural consequences of SSG modifications. Finally, we discuss the analytical challenges in characterizing SSG and the thiol PTM landscape, future directions for understanding of the role of SSG in redox signaling and regulation and its interplay with other PTMs, and the potential role of computational approaches to accelerate functional discovery.
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