Hydrogen peroxide (H 2 O 2 ) is an important messenger molecule for diverse cellular
processes. H 2 O 2 oxidizes proteinaceous cysteinyl thiols to sulfenic acid, also known as S-…

Post-translational changes in the redox state of cysteine residues can rapidly and reversibly
alter protein functions, thereby modulating biological processes. The nematode C. elegans …

‘Turn-on’ fluorescence probes for detecting H 2 O 2 in cells are established, but equivalent
tools to monitor the products of its reaction with protein cysteines have not been reported. …

Proteasome inhibitors (PI) have evolved as the central backbone of treatment for multiple
myeloma (MM), with first-in-class bortezomib and second-and third-generation PI, carfilzomib …

Oxidation of a protein cysteinyl thiol (Cys‐SH) to S‐sulfenic acid (Cys‐SOH) by a reactive
oxygen species (eg, hydrogen peroxide), which is termed protein S‐sulfenylation, is a …

Background Oxidative stress contributes to thrombosis in atherosclerosis, inflammation,
infection, aging, and malignancy. Oxidant-induced cysteine modifications, including sulfenylation…

A novel approach to the asymmetric reduction of dihydro-β-carboline derivatives to the
corresponding tetrahydro-β-carbolines is described based on the supramolecular lyophilized …

Sulfur dioxide (SO 2 ) has emerged as a physiological relevant signaling molecule that
plays a prominent role in regulating vascular functions. However, molecular mechanisms …

Arterial thrombosis in the setting of dyslipidemia promotes clinically significant events, including
myocardial infarction and stroke. Oxidized lipids in low-density lipoproteins (oxLDL) are …

With an eye toward expanding chemistries used for covalent ligand discovery, we elaborated
an umpolung strategy that exploits the ‘polarity reversal’ of sulfur when cysteine is oxidized …