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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 [29,8286]

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A narrative review on financial challenges and health care costs associated with traumatic brain injury in the United States

Initial propeptide removal precedes precise catalytic domain cleavage into heavy and light chains, culminating in fully active tetramer assembly