Redox modifications of protein-thiols: emerging roles in cell signaling.

By S. Biswas, A. Chida, I. Rahman. Biochemical Pharmacology, 2006

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The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. (2007, background): “S-glutathiolation is a posttranslational modification of protein cysteines mediated by the interaction of peroxynitrite (derived from nitric oxide and superoxide) and glutathione, which ultimately leads to the formation of a reversible disulfide bond between the protein and glutathiolation (87).”
A novel and automated assay for thiol/disulphide homeostasis. (2014, background): “S, A novel and automated a 6 Dynamic thiol disulphide homeostasis status has critical roles in antioxidant protection, detoxification, signal transduction, apoptosis, regulation of enzymatic activity and transcription factors and cellular signalling mechanisms [5,6].”
The Response to Heat Shock and Oxidative Stress in Saccharomyces cerevisiae (2012, background): “Increasing evidence suggests that post-translational modification of glycolytic enzymes is a common response to oxidative stress causing rapid and reversible changes in enzyme activity (Biswas et al. 2006).”