title: The redox proteome.
abstract: The redox proteome consists of reversible and irreversible covalent modifications that link redox metabolism to biologic structure and function. These modifications, especially of Cys, function at the molecular level in protein folding and maturation, catalytic activity, signaling, and macromolecular interactions and at the macroscopic level in control of secretion and cell shape. Interaction of the redox proteome with redox-active chemicals is central to macromolecular structure, regulation, and signaling during the life cycle and has a central role in the tolerance and adaptability to diet and environmental challenges.
authors.affiliation: From the Division of Pulmonary, Allergy, and Critical Care Medicine, Department of Medicine, Emory University, Atlanta, Georgia 30322.
authors.forename: Young-Mi
authors.initials: YM
authors.lastname: Go
authors.forename: Dean P
authors.initials: DP
authors.lastname: Jones
mesh_terms: D000199:Actins / Q000737:chemistry; D000818:Animals; D003545:Cysteine / Q000737:chemistry*; D005978:Glutathione / Q000737:chemistry; D006801:Humans; D046911:Macromolecular Substances / Q000737:chemistry; D055442:Metabolome; D010084:Oxidation-Reduction; D020543:Proteome; D040901:Proteomics / Q000379:methods*; D015398:Signal Transduction; D013438:Sulfhydryl Compounds / Q000737:chemistry; D013879:Thioredoxins / Q000737:chemistry
chemical_list: D000199:Actins; D046911:Macromolecular Substances; D020543:Proteome; D013438:Sulfhydryl Compounds; D013879:Thioredoxins; D005978:Glutathione; D003545:Cysteine
keywords: Glutathione; Redox Regulation; Systems Biology; Thiol; Thioredoxin