Introduction of Laboratory

The nucleophilic thiol group allows cysteines to undergo a broad range of chemical modifications. Thiol-based protein oxidation (S-sulfenylation, S-sulfinylation, S-Glutathionylation, etc.) by exogenous and endogenous reactive oxygen species (ROS) is a crucial mechanism in cell signaling. To gain a better understanding of how these thiol modifications affect protein functions in normal or stressed biological systems, we should first know which cysteinyl thiols on a protein can be oxidized or modified. In other words, identification of protein targets of thiol oxidation is crucial to understanding of their roles in biology and disease. Our research programs develop two complementary site-centric chemoproteomic strategies to systematically quantify thiol reactivities and to globally map distinct types of thiol oxidation in native proteomes (Fig. 1). With these tools in hand, we redefine the hydrogen peroxide-dependent redoxome in human cells and generate the first site-centric S-sulfenylome and S-sulfinylome datasets. We also develop the first web