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• W2895048867 abstract "The wide reactivity of the thiol group enables the formation of a variety of reversible, covalent modifications on cysteine residues. S-nitrosylation, like many other post-translational modifications, is site selective, reversible, and necessary for a wide variety of fundamental cellular processes. The overall abundance of S-nitrosylated proteins and reactivity of the nitrosyl group necessitates an enrichment strategy for accurate detection with adequate depth. Herein, a method is presented for the enrichment and detection of endogenous protein S-nitrosylation from complex mixtures of cell or tissue lysate utilizing organomercury resin. Minimal adaptations to the method also support the detection of either S-glutathionylation or S-acylation using the same enrichment platform. When coupled with high accuracy mass spectrometry, these methods enable a site-specific level of analysis, facilitating the curation comparable datasets of three separate cysteine post-translational modifications. © 2018 by John Wiley & Sons, Inc." @default.
• W2895048867 created "2018-10-12" @default.
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• W2895048867 date "2018-10-03" @default.
• W2895048867 modified "2023-10-16" @default.
• W2895048867 title "Analysis of Cysteine Post Translational Modifications Using Organic Mercury Resin" @default.
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• W2895048867 doi "https://doi.org/10.1002/cpps.69" @default.
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