Cysteine is one of the least abundant amino acids, yet it is frequently found as a highly
conserved residue within functional (regulatory, catalytic, or binding) sites in proteins. It is …

Many cellular functions involve cysteine chemistry via thiol–disulfide exchange pathways.
The nucleophilic cysteines of the enzymes involved are activated as thiolate. A thiolate is …

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 …

The thiol functional group of the amino acid cysteine can undergo a wide array of oxidative
modifications and perform a countless number of physiological functions. In addition to …

The perception of reactive oxygen species has evolved over the past decade from agents of
cellular damage to secondary messengers which modify signaling proteins in physiology …

The sulfur biochemistry of the thiol group endows cysteines with a number of highly
specialized and unique features that enable them to serve a variety of different functions in …

Cysteine plays structural roles in proteins and can also participate in electron transfer
reactions, when some structural folds provide appropriated environments for stabilization of …

Thiol groups in protein cysteine (Cys) residues can undergo one-and two-electron oxidation
reactions leading to the formation of thiyl radicals or sulfenic acids, respectively. In this mini …

A well-regulated redox state is essential for normal physiological function and cellular
metabolism. In most eukaryotic cells, protein cysteine thiols are most sensitive to fluctuations …

Cysteine residues in proteins and enzymes often fulfill rather important roles, particularly in
the context of cellular signaling, protein–protein interactions, substrate and metal binding …