AI Article Synopsis
- Cysteine's post-translational modifications are crucial for cells to manage oxidative stress, and studying these changes requires focused techniques like mass spectrometry for analysis.
- Recent advancements have been made in miniaturizing cysteine enrichment methods, investigating disulfide bonded structures, and measuring specific cysteine oxidation levels.
- The authors expect these improved methods to enhance the understanding of cysteine functions in various organisms, revealing new insights into how cysteines contribute to stress responses.
Article Abstract
The post-translational modification of cysteine to diverse oxidative states is understood as a critical cellular mechanism to combat oxidative stress. To study the role of cysteine oxidation, cysteine enrichments and subsequent analysis via mass spectrometry are necessary. As such, technologies and methods are rapidly developing for sensitive and efficient enrichments of cysteines to further explore its role in signaling pathways. In this review, we analyze recent developments in methods to miniaturize cysteine enrichments, analyze the underexplored disulfide bound redoxome, and quantify site-specific cysteine oxidation. We predict that further development of these methods will improve cysteine coverage across more diverse organisms than those previously studied and elicit novel roles cysteines play in stress response.
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| http://dx.doi.org/10.1016/j.cbpa.2023.102389 | DOI Listing |
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