title: Introduction to the thematic minireview series on redox-active protein modifications and signaling.
abstract: The dynamics of redox metabolism necessitate cellular strategies for sensing redox changes and for responding to them. A common mechanism for receiving and transmitting redox changes is via reversible modifications of protein cysteine residues. A plethora of cysteine modifications have been described, including sulfenylation, glutathionylation, and disulfide formation. These post-translational modifications have the potential to alter protein structure and/or function and to modulate cellular processes ranging from division to death and from circadian rhythms to secretion. The focus of this thematic minireview series is cysteine modifications in response to reactive oxygen and nitrogen species.
authors.affiliation: From the Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan 48109-0600.
authors.forename: Ruma
authors.initials: R
authors.lastname: Banerjee
mesh_terms: D000818:Animals; D003545:Cysteine / Q000378:metabolism*; D006801:Humans; D010084:Oxidation-Reduction; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000378:metabolism*; D026361:Reactive Nitrogen Species / Q000378:metabolism; D017382:Reactive Oxygen Species / Q000378:metabolism; D015398:Signal Transduction
chemical_list: D011506:Proteins; D026361:Reactive Nitrogen Species; D017382:Reactive Oxygen Species; D003545:Cysteine
keywords: Circadian Rhythms; Oxidation-Reduction; Peroxiredoxin; Redox; Redox Regulation; redox Signaling