An unanswered question in human health is whether antioxidation prevents or promotes
cancer. Antioxidation has historically been viewed as chemopreventive, but emerging …

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 …

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 …

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

NO is a versatile free radical that mediates numerous biological functions within every major
organ system. A molecular pathway by which NO accomplishes functional diversity is the …

It is widely accepted that the redox status of protein thiols is of central importance to protein
structure and folding and that glutathione is an important low-molecular-mass redox …

Protein S-glutathionylation, the reversible formation of mixed disulfides between glutathione
and low-pKa cysteinyl residues, not only is a cellular response to mild oxidative/nitrosative …

Cysteine occupies a unique place in protein chemistry. The nucleophilic thiol group allows
cysteine to undergo a broad range of redox modifications beyond classical thiol-disulfide …

By nature of the reversibility of the addition of glutathione to low pKa cysteine residues, the
post-translational modification of S-glutathionylation sanctions a cycle that can create a …

Inevitable byproducts of aerobic metabolism are free radicals and other highly reactive
oxidants and nitrosants that are continuously formed within cells. Most cells generally …