Reactive oxygen, nitrogen, and sulfur species, referred to as ROS, RNS, and RSS,
respectively, are produced during normal cell function and in response to various stimuli. An …

Significance: Protein S-nitrosylation, the oxidative modification of cysteine by nitric oxide
(NO) to form protein S-nitrosothiols (SNOs), mediates redox-based signaling that conveys, in …

Nuclear factor κB (NF-κB) is an antiapoptotic transcription factor. We show that the
antiapoptotic actions of NF-κB are mediated by hydrogen sulfide (H 2 S) synthesized by …

Cysteine residues in proteins are subject to diverse redox chemistry. Oxidation of cysteine to
S-nitrosocysteine, cysteine sulfenic and sulfinic acids, disulfides and persulfides are a few …

S-Nitrosylation is a redox-mediated posttranslational modification that regulates protein
function via covalent reaction of nitric oxide (NO)-related species with a cysteine thiol group …

STAT1 and STAT3 are nuclear transcription factors that regulate genes involved in cell
cycle, cell survival and immune response. The cross-talk between these signaling pathways …

Redox biochemistry is increasingly recognized as an integral component of cellular signal
processing and cell fate decision making. Unfortunately, our capabilities to observe and …

Post-translational S-glutathionylation occurs through the reversible addition of a proximal
donor of glutathione to thiolate anions of cysteines in target proteins, where the modification …

In the cardiovascular system, changes in oxidative balance can affect many aspects of
cellular physiology through redox-signaling. Depending on the magnitude, fluctuations in …

S-Nitrosylation, the redox-based modification of Cys thiol side chains by nitric oxide, is a
common mechanism in signal transduction. Dysregulated S-nitrosylation contributes to a …