title: Biochemical methods for monitoring protein thiol redox states in biological systems.
abstract: Oxidative post-translational modifications of proteins resulting from events that increase cellular oxidant levels play important roles in physiological and pathophysiological processes. Evaluation of alterations to protein redox states is increasingly common place because of methodological advances that have enabled detection, quantification and identification of such changes in cells and tissues. This mini-review provides a synopsis of biochemical methods that can be utilized to monitor the array of different oxidative and electrophilic modifications that can occur to protein thiols and can be important in the regulatory or maladaptive impact oxidants can have on biological systems. Several of the methods discussed are valuable for monitoring the redox state of established redox sensing proteins such as Keap1.
authors.affiliation: King's College London, Cardiovascular Division, The British Heart Foundation Centre of Excellence, The Rayne Institute, St Thomas' Hospital, London SE1 7EH, UK.
authors.forename: Olena
authors.initials: O
authors.lastname: Rudyk
authors.affiliation: King's College London, Cardiovascular Division, The British Heart Foundation Centre of Excellence, The Rayne Institute, St Thomas' Hospital, London SE1 7EH, UK.
authors.forename: Philip
authors.initials: P
authors.lastname: Eaton
mesh_terms: D003545:Cysteine / Q000737:chemistry / Q000378:metabolism; D004220:Disulfides / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D015538:Nitrosation; D010084:Oxidation-Reduction; D011506:Proteins / Q000378:metabolism*; D013438:Sulfhydryl Compounds / Q000737:chemistry* / Q000378:metabolism
chemical_list: D004220:Disulfides; D011506:Proteins; D013438:Sulfhydryl Compounds; D003545:Cysteine
keywords: Disulfide; Hyperoxidation; Keap1; Methods; Redox state; S-nitrosation