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At the molecular level, redox regulation can directly modify the active sites of enzymes, although a growing number of examples indicate the importance of an additional underlying mechanism that involves conditionally disordered proteins. These proteins alter their functional behavior by undergoing a disorder\u2010to\u2010order transition in response to changing redox conditions. However, the extent to which this mechanism is used in various proteomes is currently unknown. Here, a recently developed sequence\u2010based prediction tool incorporated into the IUPred2A web server is used to estimate redox\u2010sensitive conditionally disordered regions at a large scale. It is shown that redox\u2010sensitive conditional disorder is fairly widespread in various proteomes and that its presence strongly correlates with the expansion of specific domains in multicellular organisms that largely rely on extra stability provided by disulfide bonds or zinc ion binding. The analyses of yeast redox proteomes and human disease data further underlie the significance of this phenomenon in the regulation of a wide range of biological processes, as well as its biomedical importance.<\/jats:p>","DOI":"10.1002\/pmic.201800070","type":"journal-article","created":{"date-parts":[[2019,1,10]],"date-time":"2019-01-10T01:44:21Z","timestamp":1547084661000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":35,"title":["Large\u2010Scale Analysis of Redox\u2010Sensitive Conditionally Disordered Protein Regions Reveals Their Widespread Nature and Key Roles in High\u2010Level Eukaryotic Processes"],"prefix":"10.1002","volume":"19","author":[{"given":"G\u00e1bor","family":"Erd\u0151s","sequence":"first","affiliation":[{"name":"MTA\u2010ELTE Lend\u00fclet Bioinformatics Research Group Department of Biochemistry E\u00f6tv\u00f6s Lor\u00e1nd University  Budapest H\u20101117 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