Protein analysis under biological conditions is now regarded as indispensable for
understanding the structure and function of proteins, in addition to in vitro studies using …

Conspectus Oxidative post-translational modifications (OxiPTMs) of cysteine residues are
the molecular foundation of thiol-based redox regulation that modulates physiological …

Electrophilic small molecules that can reversibly modify proteins are of growing interest in
drug discovery. However, the ability to study reversible covalent probes in live cells can be …

Click chemistry has been established rapidly as one of the most valuable methods for the
chemical transformation of complex molecules. Due to the rapid rates, clean conversions to …

Although selenocysteine selenenic acids (Sec–SeOHs) have been recognized as key
intermediates in the catalytic cycle of glutathione peroxidase (GPx), examples of the direct …

Covalent inhibitors and other types of covalent modalities have seen a revival in the past two
decades, with a variety of new targeted covalent drugs having been approved in recent …

Sulfur-based functional groups are found in a broad range of natural products and
therapeutic compounds. The sulfoxide moiety is present in a significant portion of …

Living-cell imaging demands high specificity, sensitivity, and minimal background
interference to the targets of interest. However, developing a desirable imaging probe that …

Significance: The systematic investigation of oxidative modification of proteins by reactive
oxygen species started in 1980. Later, it was shown that reactive nitrogen species could also …

To understand oxidative stress, antioxidant defense, and redox signaling in health and
disease it is essential to assess protein thiol redox state. Protein thiol redox state is seldom …