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| Content Provider | Royal Society of Chemistry (RSC) |
|---|---|
| Author | Duan, Jicheng Gaffrey, Matthew J. Qian, Wei-Jun |
| Copyright Year | 2017 |
| Abstract | Protein thiols play a crucial role in redox signaling, in the regulation of enzymatic activity and protein function, and in maintaining redox homeostasis in living systems. The unique chemical reactivity of the thiol group makes protein cysteines susceptible to reactions with reactive oxygen and nitrogen species that form various reversible and irreversible post-translational modifications (PTMs). The reversible PTMs in particular are major components of redox signaling and are involved in the regulation of various cellular processes under physiological and pathological conditions. The biological significance of these redox PTMs in both healthy and disease states has been increasingly recognized. Herein, we review recent advances in quantitative proteomic approaches for investigating redox PTMs in complex biological systems, including general considerations of sample processing, chemical or affinity enrichment strategies, and quantitative approaches. We also highlight a number of redox proteomic approaches that enable effective profiling of redox PTMs for specific biological applications. Although technical limitations remain, redox proteomics is paving the way to a better understanding of redox signaling and regulation in both healthy and disease states. |
| Starting Page | 816 |
| Ending Page | 829 |
| Page Count | 14 |
| File Format | HTM / HTML PDF |
| ISSN | 1742206X |
| Volume Number | 13 |
| Issue Number | 5 |
| Journal | Molecular BioSystems |
| DOI | 10.1039/c6mb00861e |
| Language | English |
| Publisher | Royal Society of Chemistry |
| Access Restriction | Open |
| Subject Keyword | Thiol Reactive oxygen species Proteomics Antioxidants & Redox Signaling Redox Homeostasis Nitrogen Protein |
| Content Type | Text |
| Resource Type | Article |
| Subject | Molecular Biology Biotechnology |
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