{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,26]],"date-time":"2026-09-26T22:23:27Z","timestamp":1790461407786,"version":"4.1.0"},"reference-count":268,"publisher":"Walter de Gruyter GmbH","issue":"8","license":[{"start":{"date-parts":[[2016,8,1]],"date-time":"2016-08-01T00:00:00Z","timestamp":1470009600000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/3.0"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2016,8,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Cardiac troponin is a dynamic complex of troponin C, troponin I, and troponin T (TnC, TnI, and TnT, respectively) found in the myocyte thin filament where it plays an essential role in cardiac muscle contraction. Mutations in troponin subunits are found in inherited cardiomyopathies, such as hypertrophic cardiomyopathy (HCM) and dilated cardiomyopathy (DCM). The highly dynamic nature of human cardiac troponin and presence of numerous flexible linkers in its subunits suggest that understanding of structural and functional properties of this important complex can benefit from the consideration of the protein intrinsic disorder phenomenon. We show here that mutations causing decrease in the disorder score in TnI and TnT are significantly more abundant in HCM and DCM than mutations leading to the increase in the disorder score. Identification and annotation of intrinsically disordered regions in each of the troponin subunits conducted in this study can help in better understanding of the roles of intrinsic disorder in regulation of interactomes and posttranslational modifications of these proteins. These observations suggest that disease-causing mutations leading to a decrease in the local flexibility of troponins can trigger a whole plethora of functional changes in the heart.<\/jats:p>","DOI":"10.1515\/hsz-2015-0303","type":"journal-article","created":{"date-parts":[[2016,4,13]],"date-time":"2016-04-13T19:14:47Z","timestamp":1460574887000},"page":"731-751","source":"Crossref","is-referenced-by-count":24,"title":["Troponins, intrinsic disorder, and cardiomyopathy"],"prefix":"10.1515","volume":"397","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4507-5789","authenticated-orcid":false,"given":"Insung","family":"Na","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Min J.","family":"Kong","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shelby","family":"Straight","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jose R.","family":"Pinto","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vladimir N.","family":"Uversky","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"374","reference":[{"key":"ref691","doi-asserted-by":"crossref","first-page":"2041","DOI":"10.1016\/j.febslet.2006.03.003","article-title":"Disordered domains and high surface charge confer hubs with the ability to interact with multiple proteins in interaction networks","volume":"580","year":"2006","journal-title":"FEBS Lett."},{"key":"ref91","doi-asserted-by":"crossref","first-page":"3433","DOI":"10.1093\/bioinformatics\/bti541","article-title":"IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content","volume":"21","year":"2005","journal-title":"Bioinformatics"},{"key":"ref801","doi-asserted-by":"crossref","first-page":"1217","DOI":"10.1542\/peds.2008-0708","article-title":"Sudden unexpected death in young athletes: reconsidering \u201chypertrophic cardiomyopathy\u201d","volume":"123","year":"2009","journal-title":"Pediatrics"},{"key":"ref2301","doi-asserted-by":"crossref","first-page":"484","DOI":"10.1016\/j.tibs.2005.07.008","article-title":"Structural disorder throws new light on moonlighting","volume":"30","year":"2005","journal-title":"Trends Biochem. 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