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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Yang, Jing Carroll, Kate S. Liebler, Daniel C. |
| Description | Author Affiliation: Yang J ( From the National Center for Protein Sciences · Beijing, Beijing, 102206, China); Carroll KS ( ¶Department of Chemistry, The Scripps Research Institute, Jupiter, Florida 33458); Liebler DC ( âDepartment of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232 yangjing54@hotmail.com Daniel.liebler@vanderbilt.edu.) |
| Abstract | Cysteine occupies a unique place in protein chemistry. The nucleophilic thiol group allows cysteine to undergo a broad range of redox modifications beyond classical thiol-disulfide redox equilibria, including S-sulfenylation (-SOH), S-sulfinylation (-SO(2)H), S-sulfonylation (-SO(3)H), S-nitrosylation (-SNO), S-sulfhydration (-SSH), S-glutathionylation (-SSG), and others. Emerging evidence suggests that these post-translational modifications (PTM) are important in cellular redox regulation and protection against oxidative damage. Identification of protein targets of thiol redox modifications is crucial to understanding their roles in biology and disease. However, analysis of these highly labile and dynamic modifications poses challenges. Recent advances in the design of probes for thiol redox forms, together with innovative mass spectrometry based chemoproteomics methods make it possible to perform global, site-specific, and quantitative analyses of thiol redox modifications in complex proteomes. Here, we review chemical proteomic strategies used to expand the landscape of thiol redox modifications. |
| File Format | HTM / HTML |
| ISSN | 15359476 |
| e-ISSN | 15359484 |
| Journal | Molecular & Cellular Proteomics |
| Issue Number | 1 |
| Volume Number | 15 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology |
| Publisher Date | 2016-01-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Discipline Proteomics Protein Processing, Post-translational Proteome Metabolism Proteomics Sulfhydryl Compounds Animals Cysteine Mass Spectrometry Oxidation-reduction Reproducibility Of Results Research Support, N.i.h., Extramural Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Analytical Chemistry Molecular Biology Biochemistry |
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