title: Oxidant sensing by reversible disulfide bond formation.
abstract: Maintenance of the cellular redox balance is crucial for cell survival. An increase in reactive oxygen, nitrogen, or chlorine species can lead to oxidative stress conditions, potentially damaging DNA, lipids, and proteins. Proteins are very sensitive to oxidative modifications, particularly methionine and cysteine residues. The reversibility of some of these oxidative protein modifications makes them ideally suited to take on regulatory roles in protein function. This is especially true for disulfide bond formation, which has the potential to mediate extensive yet fully reversible structural and functional changes, rapidly adjusting the protein's activity to the prevailing oxidant levels.
authors.affiliation: From the Departments of Molecular, Cellular, and Developmental Biology and.
authors.forename: Claudia M
authors.initials: CM
authors.lastname: Cremers
authors.forename: Ursula
authors.initials: U
authors.lastname: Jakob
mesh_terms: D000818:Animals; D000975:Antioxidants / Q000378:metabolism; D003545:Cysteine / Q000737:chemistry*; D004220:Disulfides / Q000737:chemistry*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D016877:Oxidants / Q000737:chemistry*; D010084:Oxidation-Reduction; D018384:Oxidative Stress; D010544:Peroxidases / Q000378:metabolism; D010545:Peroxides / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D017382:Reactive Oxygen Species / Q000737:chemistry; D013438:Sulfhydryl Compounds / Q000737:chemistry
chemical_list: D000975:Antioxidants; D004220:Disulfides; D016877:Oxidants; D010545:Peroxides; D011506:Proteins; D017382:Reactive Oxygen Species; D013438:Sulfhydryl Compounds; D010544:Peroxidases; D003545:Cysteine
keywords: Antioxidants; Oxidative Stress; Reactive Oxygen Species (ROS); Redox Signaling; Stress Response