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NADPH oxidases, superoxide dismutases, nitric oxide synthases, and others produce the redox active molecules superoxide, hydrogen peroxide, nitric oxide, and hydrogen sulfide. These react with target proteins inducing spatiotemporal modifications of cysteine residues within different signaling cascades. Thioredoxin family proteins are key regulators of the redox state of proteins. They regulate the formation and removal of oxidative modifications by specific thiol reduction and oxidation. All of these redox enzymes affect inflammatory processes and the innate and adaptive immune response. Interestingly, this regulation involves different mechanisms in different biological compartments and specialized cell types. The localization and activity of distinct proteins including, for instance, the transcription factor NF\n                    <jats:italic>\u03ba<\/jats:italic>\n                    B and the immune mediator HMGB1 are redox\u2010regulated. The transmembrane protein ADAM17 releases proinflammatory mediators, such as TNF\n                    <jats:italic>\u03b1<\/jats:italic>\n                    , and is itself regulated by a thiol switch. Moreover, extracellular redox enzymes were shown to modulate the activity and migration behavior of various types of immune cells by acting as cytokines and\/or chemokines. Within this review article, we will address the concept of redox signaling and the functions of both redox enzymes and redox active molecules in innate and adaptive immune responses.\n                  <\/jats:p>","DOI":"10.1155\/2017\/8459402","type":"journal-article","created":{"date-parts":[[2017,10,8]],"date-time":"2017-10-08T17:01:26Z","timestamp":1507482086000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":61,"title":["Redox Regulation of Inflammatory Processes Is Enzymatically 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