Perpustakaan Digital ITB

Oxidative post-translational modifications (OxiPTMs) of cysteine residues are the molecular foundation of thiol-based redox regulation that modulates physiological events such as cell proliferation, differentiation, and migration and, when dysregulated, can lead to biomolecule damage and cell death. Common OxiPTMs of cysteine thiols (?SH) include reversible modifications such as S-sulfenylation (?SOH), S-glutathionylation (?SSG), disulfide formation (?SSR), S-nitrosylation (?SNO), and S-sulfhydration (?SSH) as well as more biologically stable modifications like S-sulfinylation (?SO2H) and S-sulfonylation (?SO3H). In the past decade, our laboratory has developed first-in-class chemistry-based tools and proteomic methods to advance the field of thiol-based redox biology and oxidative stress. In this Account, we take the reader through the historical aspects of probe development and application in our laboratory, highlighting key advances in our understanding of sulfur chemistry, in the test tube and in living systems.