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Quantitative mass spectrometry-based redox proteomic techniques have contributed to the identification of a large number of pro- and eukaryotic proteins that harbor redox-sensitive cysteine residues, which form sulfenic acid intermediates, disulfide bonds, or become S -glutathionylated, S -nitrosylated or persulfidated in response to endogenous and exogenous stimuli [29,82–86]

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