报告摘要：The sulfur atom of cysteine exhibits distinct chemical properties, which can assume many different redox states. Redox changes on cysteine residues can reversibly alter protein functions, representing a crucial mechanism in cellular regulation and signaling. Dysregulation of cysteine-mediated redox network is believed to be associated with aging and diseases. However, efforts to understand their functional roles in physiology and pathophysiology have been hampered due to limitations of methods for globally analyzing site-specific protein targets and redox dynamics. We developed several site-centric quantitative chemoproteomic approaches to systematically profile three distinct types of cysteine redox forms (-SH, -SOH and SO2H) in complex proteomes. These analyses afford discovery of novel redox mechanisms of several proteins with key biological functions, and greatly expand the substrate spectrum of many functionally important reducing systems.