{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T18:54:17Z","timestamp":1786992857342,"version":"build-2736575974"},"reference-count":68,"publisher":"Elsevier BV","issue":"13","license":[{"start":{"date-parts":[[2021,6,1]],"date-time":"2021-06-01T00:00:00Z","timestamp":1622505600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,6,1]],"date-time":"2021-06-01T00:00:00Z","timestamp":1622505600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2021,4,21]],"date-time":"2021-04-21T00:00:00Z","timestamp":1618963200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000038","name":"Natural Sciences and Engineering Research Council of Canada","doi-asserted-by":"publisher","award":["RGPIN-2015-06664"],"award-info":[{"award-number":["RGPIN-2015-06664"]}],"id":[{"id":"10.13039\/501100000038","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000024","name":"Canadian Institutes of Health Research","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000024","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Molecular Biology"],"published-print":{"date-parts":[[2021,6]]},"DOI":"10.1016\/j.jmb.2021.167010","type":"journal-article","created":{"date-parts":[[2021,4,24]],"date-time":"2021-04-24T01:50:12Z","timestamp":1619229012000},"page":"167010","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":10,"title":["Dilated Cardiomyopathy Mutations and Phosphorylation disrupt the Active Orientation of Cardiac Troponin C"],"prefix":"10.1016","volume":"433","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5336-9002","authenticated-orcid":false,"given":"Zabed","family":"Mahmud","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8490-4140","authenticated-orcid":false,"given":"Prabhpaul S.","family":"Dhami","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Caleb","family":"Rans","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5651-4017","authenticated-orcid":false,"given":"Philip B.","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter M.","family":"Hwang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jmb.2021.167010_b0005","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1186\/1471-2261-14-73","article-title":"Comorbidity profiles and inpatient outcomes during hospitalization for heart failure: an analysis of the U.S. Nationwide inpatient sample","volume":"14","author":"Lee","year":"2014","journal-title":"BMC Cardiovasc. Disord."},{"key":"10.1016\/j.jmb.2021.167010_b0010","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1172\/JCI62862","article-title":"Genetic mutations and mechanisms in dilated cardiomyopathy","volume":"123","author":"McNally","year":"2013","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.jmb.2021.167010_b0015","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1196\/annals.1302.018","article-title":"Molecular and cellular aspects of troponin cardiomyopathies","volume":"1015","author":"Gomes","year":"2004","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"10.1016\/j.jmb.2021.167010_b0020","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/j.bpj.2009.04.023","article-title":"Differences between cardiac and skeletal troponin interaction with the thin filament probed by troponin exchange in skeletal myofibrils","volume":"97","author":"Yang","year":"2009","journal-title":"Biophys. J."},{"key":"10.1016\/j.jmb.2021.167010_b0025","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1038\/203645a0","article-title":"A new protein factor promoting contraction of actomyosin","volume":"203","author":"Ebashi","year":"1964","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2021.167010_b0030","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1093\/oxfordjournals.jbchem.a128628","article-title":"Troponin as the Ca++-receptive protein in the contractile system","volume":"62","author":"Ebashi","year":"1967","journal-title":"J. Biochem."},{"key":"10.1016\/j.jmb.2021.167010_b0035","doi-asserted-by":"crossref","first-page":"2125","DOI":"10.1016\/S0021-9258(19)44195-1","article-title":"Purification and properties of the components from troponin","volume":"248","author":"Greaser","year":"1973","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2021.167010_b0040","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1038\/nature01780","article-title":"Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form","volume":"424","author":"Takeda","year":"2003","journal-title":"Nature"},{"issue":"Suppl 1","key":"10.1016\/j.jmb.2021.167010_b0045","doi-asserted-by":"crossref","first-page":"i35","DOI":"10.1093\/jmicro\/54.suppl_1.i35","article-title":"Crystal structure of troponin and the molecular mechanism of muscle regulation","volume":"54","author":"Takeda","year":"2005","journal-title":"J. Electron. Microsc. (Tokyo)"},{"key":"10.1016\/j.jmb.2021.167010_b0050","doi-asserted-by":"crossref","first-page":"18216","DOI":"10.1074\/jbc.272.29.18216","article-title":"Structure of cardiac muscle troponin C unexpectedly reveals a closed regulatory domain","volume":"272","author":"Sia","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2021.167010_b0055","doi-asserted-by":"crossref","first-page":"12138","DOI":"10.1021\/bi971223d","article-title":"Calcium-induced structural transition in the regulatory domain of human cardiac troponin C","volume":"36","author":"Spyracopoulos","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2021.167010_b0060","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1038\/s41467-019-14008-1","article-title":"Cardiac muscle thin filament structures reveal calcium regulatory mechanism","volume":"11","author":"Yamada","year":"2020","journal-title":"Nature Commun."},{"key":"10.1016\/j.jmb.2021.167010_b0065","doi-asserted-by":"crossref","first-page":"16681","DOI":"10.1074\/jbc.274.24.16681","article-title":"Effects of troponin I phosphorylation on conformational exchange in the regulatory domain of cardiac troponin C","volume":"274","author":"Gaponenko","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2021.167010_b0070","doi-asserted-by":"crossref","first-page":"14412","DOI":"10.1073\/pnas.1410775111","article-title":"The cardiac-specific N-terminal region of troponin I positions the regulatory domain of troponin C","volume":"111","author":"Hwang","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2021.167010_b0075","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1016\/S0014-5793(00)01881-0","article-title":"Systematic mapping of regions of human cardiac troponin I involved in binding to cardiac troponin C: N- and C-terminal low affinity contributing regions","volume":"479","author":"Ferrieres","year":"2000","journal-title":"FEBS Letters"},{"key":"10.1016\/j.jmb.2021.167010_b0080","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1016\/j.bbrc.2015.01.018","article-title":"General order parameter based correlation analysis of protein backbone motions between experimental NMR relaxation measurements and molecular dynamics simulations","volume":"457","author":"Liu","year":"2015","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.jmb.2021.167010_b0085","doi-asserted-by":"crossref","first-page":"2429","DOI":"10.1126\/science.291.5512.2429","article-title":"Two-state allosteric behavior in a single-domain signaling protein","volume":"291","author":"Volkman","year":"2001","journal-title":"Science"},{"key":"10.1016\/j.jmb.2021.167010_b0090","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1006\/jmbi.1998.1723","article-title":"Backbone and methyl dynamics of the regulatory domain of troponin C: anisotropic rotational diffusion and contribution of conformational entropy to calcium affinity","volume":"278","author":"Gagne","year":"1998","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2021.167010_b0095","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1007\/s00424-011-0960-3","article-title":"Diastolic myofilament dysfunction in the failing human heart","volume":"462","author":"van der Velden","year":"2011","journal-title":"Pflugers Arch."},{"key":"10.1016\/j.jmb.2021.167010_b0100","doi-asserted-by":"crossref","first-page":"810","DOI":"10.1016\/j.yjmcc.2010.02.014","article-title":"Why does troponin I have so many phosphorylation sites? Fact and fancy","volume":"48","author":"Solaro","year":"2010","journal-title":"J. Mol. Cell. Cardiol."},{"key":"10.1016\/j.jmb.2021.167010_b0105","doi-asserted-by":"crossref","first-page":"4054","DOI":"10.1021\/pr200258m","article-title":"Top-down quantitative proteomics identified phosphorylation of cardiac troponin I as a candidate biomarker for chronic heart failure","volume":"10","author":"Zhang","year":"2011","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.jmb.2021.167010_b0110","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.abb.2019.01.025","article-title":"Troponin I modulation of cardiac performance: plasticity in the survival switch","volume":"664","author":"Biesiadecki","year":"2019","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.jmb.2021.167010_b0115","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/j.yjmcc.2014.09.013","article-title":"Cardiac troponin I tyrosine 26 phosphorylation decreases myofilament Ca2+ sensitivity and accelerates deactivation","volume":"76","author":"Salhi","year":"2014","journal-title":"J. Mol. Cell. Cardiol."},{"key":"10.1016\/j.jmb.2021.167010_b0120","doi-asserted-by":"crossref","first-page":"1170","DOI":"10.1161\/01.RES.0000105088.06696.17","article-title":"Modulation of thin filament activation by breakdown or isoform switching of thin filament proteins: physiological and pathological implications","volume":"93","author":"Marston","year":"2003","journal-title":"Circ. Res."},{"key":"10.1016\/j.jmb.2021.167010_b0125","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1016\/j.cardiores.2004.12.022","article-title":"Regulation of cardiac contractile function by troponin I phosphorylation","volume":"66","author":"Layland","year":"2005","journal-title":"Cardiovasc. Res."},{"key":"10.1016\/j.jmb.2021.167010_b0130","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1161\/CIRCRESAHA.112.268672","article-title":"Integration of troponin I phosphorylation with cardiac regulatory networks","volume":"112","author":"Solaro","year":"2013","journal-title":"Circ. Res."},{"key":"10.1016\/j.jmb.2021.167010_b0135","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1016\/S0021-9258(19)68355-9","article-title":"The effect of troponin I phosphorylation on the Ca2+-binding properties of the Ca2+-regulatory site of bovine cardiac troponin","volume":"257","author":"Robertson","year":"1982","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2021.167010_b0140","doi-asserted-by":"crossref","first-page":"33384","DOI":"10.1074\/jbc.M803302200","article-title":"Removal of the N-terminal extension of cardiac troponin I as a functional compensation for impaired myocardial beta-adrenergic signaling","volume":"283","author":"Feng","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2021.167010_b0145","doi-asserted-by":"crossref","first-page":"30773","DOI":"10.1074\/jbc.270.51.30773","article-title":"Phosphorylation of both serine residues in cardiac troponin I is required to decrease the Ca2+ affinity of cardiac troponin C","volume":"270","author":"Zhang","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2021.167010_b0150","first-page":"H385","article-title":"Troponin I phosphorylation and myofilament calcium sensitivity during decompensated cardiac hypertrophy","volume":"274","author":"McConnell","year":"1998","journal-title":"Am. J. Physiol."},{"key":"10.1016\/j.jmb.2021.167010_b0155","doi-asserted-by":"crossref","first-page":"15753","DOI":"10.1074\/jbc.M011048200","article-title":"A proteolytic NH2-terminal truncation of cardiac troponin I that is up-regulated in simulated microgravity","volume":"276","author":"Yu","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2021.167010_b0160","doi-asserted-by":"crossref","first-page":"6602","DOI":"10.1074\/jbc.M408525200","article-title":"Proteolytic N-terminal truncation of cardiac troponin I enhances ventricular diastolic function","volume":"280","author":"Barbato","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2021.167010_b0165","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1042\/bj2490709","article-title":"Phosphorylation of C-protein, troponin I and phospholamban in isolated rabbit hearts","volume":"249","author":"Garvey","year":"1988","journal-title":"Biochem. J."},{"key":"10.1016\/j.jmb.2021.167010_b0170","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1042\/bj1600295","article-title":"Studies on the phosphorylation of the inhibitory subunit of troponin during modification of contraction in perfused rat heart","volume":"160","author":"England","year":"1976","journal-title":"Biochem. J."},{"key":"10.1016\/j.jmb.2021.167010_b0175","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1085\/jgp.75.3.271","article-title":"Calcium sensitivity of the contractile system and phosphorylation of troponin in hyperpermeable cardiac cells","volume":"75","author":"Mope","year":"1980","journal-title":"J. Gen. Physiol."},{"key":"10.1016\/j.jmb.2021.167010_b0180","doi-asserted-by":"crossref","first-page":"718","DOI":"10.1161\/01.RES.74.4.718","article-title":"Effects of phosphorylation of troponin I and C protein on isometric tension and velocity of unloaded shortening in skinned single cardiac myocytes from rats","volume":"74","author":"Hofmann","year":"1994","journal-title":"Circ. Res."},{"key":"10.1016\/j.jmb.2021.167010_b0185","doi-asserted-by":"crossref","first-page":"1028","DOI":"10.1161\/01.RES.76.6.1028","article-title":"Cardiac troponin I phosphorylation increases the rate of cardiac muscle relaxation","volume":"76","author":"Zhang","year":"1995","journal-title":"Circ. Res."},{"key":"10.1016\/j.jmb.2021.167010_b0190","doi-asserted-by":"crossref","first-page":"1828","DOI":"10.1161\/CIRCULATIONAHA.112.096388","article-title":"Multiple reaction monitoring to identify site-specific troponin I phosphorylated residues in the failing human heart","volume":"126","author":"Zhang","year":"2012","journal-title":"Circulation"},{"key":"10.1016\/j.jmb.2021.167010_b0195","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1006\/jmcc.1993.1007","article-title":"Protein kinase C phosphorylation of cardiac troponin I and troponin T inhibits Ca(2+)-stimulated MgATPase activity in reconstituted actomyosin and isolated myofibrils, and decreases actin-myosin interactions","volume":"25","author":"Noland","year":"1993","journal-title":"J. Mol. Cell. Cardiol."},{"key":"10.1016\/j.jmb.2021.167010_b0200","doi-asserted-by":"crossref","first-page":"14923","DOI":"10.1021\/bi9616357","article-title":"Differential regulation of cardiac actomyosin S-1 MgATPase by protein kinase C isozyme-specific phosphorylation of specific sites in cardiac troponin I and its phosphorylation site mutants","volume":"35","author":"Noland","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2021.167010_b0205","doi-asserted-by":"crossref","first-page":"11265","DOI":"10.1074\/jbc.M210712200","article-title":"Phosphorylation or glutamic acid substitution at protein kinase C sites on cardiac troponin I differentially depress myofilament tension and shortening velocity","volume":"278","author":"Burkart","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2021.167010_b0210","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.abb.2014.04.017","article-title":"Phosphorylation of protein kinase C sites Ser42\/44 decreases Ca(2+)-sensitivity and blunts enhanced length-dependent activation in response to protein kinase A in human cardiomyocytes","volume":"554","author":"Wijnker","year":"2014","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.jmb.2021.167010_b0215","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1161\/CIRCRESAHA.109.196055","article-title":"Identification and functional characterization of cardiac troponin I as a novel disease gene in autosomal dominant dilated cardiomyopathy","volume":"105","author":"Carballo","year":"2009","journal-title":"Circ. Res."},{"key":"10.1016\/j.jmb.2021.167010_b0220","doi-asserted-by":"crossref","first-page":"3577","DOI":"10.1529\/biophysj.107.112896","article-title":"A novel mutant cardiac troponin C disrupts molecular motions critical for calcium binding affinity and cardiomyocyte contractility","volume":"94","author":"Lim","year":"2008","journal-title":"Biophys. J."},{"key":"10.1016\/j.jmb.2021.167010_b0225","doi-asserted-by":"crossref","first-page":"2033","DOI":"10.1016\/j.jacc.2004.08.027","article-title":"Severe disease expression of cardiac troponin C and T mutations in patients with idiopathic dilated cardiomyopathy","volume":"44","author":"Mogensen","year":"2004","journal-title":"J. Am. Coll. Cardiol."},{"key":"10.1016\/j.jmb.2021.167010_b0230","doi-asserted-by":"crossref","first-page":"771","DOI":"10.1007\/s00424-006-0161-7","article-title":"Functional effects of the DCM mutant Gly159Asp troponin C in skinned muscle fibres","volume":"453","author":"Preston","year":"2007","journal-title":"Pflugers Arch."},{"key":"10.1016\/j.jmb.2021.167010_b0235","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.bbrc.2007.05.221","article-title":"DCM troponin C mutant Gly159Asp blunts the response to troponin phosphorylation","volume":"360","author":"Preston","year":"2007","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.jmb.2021.167010_b0240","doi-asserted-by":"crossref","first-page":"1486","DOI":"10.1161\/01.RES.0000267744.92677.7f","article-title":"The troponin C G159D mutation blunts myofilament desensitization induced by troponin I Ser23\/24 phosphorylation","volume":"100","author":"Biesiadecki","year":"2007","journal-title":"Circ. Res."},{"key":"10.1016\/j.jmb.2021.167010_b0245","doi-asserted-by":"crossref","first-page":"3424","DOI":"10.1074\/jbc.M703822200","article-title":"Structural kinetics of cardiac troponin C mutants linked to familial hypertrophic and dilated cardiomyopathy in troponin complexes","volume":"283","author":"Dong","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2021.167010_b0250","doi-asserted-by":"crossref","first-page":"20054","DOI":"10.1074\/jbc.RA119.011177","article-title":"The intrinsically disordered C terminus of troponin T binds to troponin C to modulate myocardial force generation","volume":"294","author":"Johnston","year":"2019","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2021.167010_b0255","doi-asserted-by":"crossref","first-page":"624","DOI":"10.1074\/jbc.275.1.624","article-title":"Altered regulation of cardiac muscle contraction by troponin T mutations that cause familial hypertrophic cardiomyopathy","volume":"275","author":"Szczesna","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2021.167010_b0260","doi-asserted-by":"crossref","first-page":"1058","DOI":"10.1056\/NEJM199504203321603","article-title":"Mutations in the genes for cardiac troponin T and alpha-tropomyosin in hypertrophic cardiomyopathy","volume":"332","author":"Watkins","year":"1995","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.jmb.2021.167010_b0265","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1271\/bbb.90586","article-title":"Defective dynamic properties of human cardiac troponin mutations","volume":"74","author":"Lassalle","year":"2010","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"10.1016\/j.jmb.2021.167010_b0270","first-page":"909","article-title":"Novel mutations of cardiac troponin T in Chinese patients with hypertrophic cardiomyopathy","volume":"39","author":"Yang","year":"2011","journal-title":"Zhonghua Xin Xue Guan Bing Za Zhi."},{"key":"10.1016\/j.jmb.2021.167010_b0275","doi-asserted-by":"crossref","first-page":"4189","DOI":"10.1021\/acs.biochem.0c00499","article-title":"The positively charged C-terminal region of human skeletal troponin T retards activation and decreases calcium sensitivity","volume":"59","author":"Lopez Davila","year":"2020","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2021.167010_b0280","doi-asserted-by":"crossref","first-page":"8782","DOI":"10.1021\/bi000473i","article-title":"Interaction of cardiac troponin C with Ca(2+) sensitizer EMD 57033 and cardiac troponin I inhibitory peptide","volume":"39","author":"Li","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2021.167010_b0285","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1016\/j.yjmcc.2016.10.016","article-title":"Structures reveal details of small molecule binding to cardiac troponin","volume":"101","author":"Cai","year":"2016","journal-title":"J. Mol. Cell. Cardiol."},{"key":"10.1016\/j.jmb.2021.167010_b0290","first-page":"145","article-title":"The calcium sensitizer drug MCI-154 binds the structural C-terminal domain of cardiac troponin C","volume":"16","author":"Li","year":"2018","journal-title":"Biochem. Biophys. Rep."},{"key":"10.1016\/j.jmb.2021.167010_b0295","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1085\/jgp.201812131","article-title":"3-Chlorodiphenylamine activates cardiac troponin by a mechanism distinct from bepridil or TFP","volume":"151","author":"Tikunova","year":"2019","journal-title":"J. Gen. Physiol."},{"key":"10.1016\/j.jmb.2021.167010_b0300","doi-asserted-by":"crossref","first-page":"1969","DOI":"10.1016\/j.bpj.2011.02.061","article-title":"A new state of cardiac myosin with very slow ATP turnover: a potential cardioprotective mechanism in the heart","volume":"100","author":"Hooijman","year":"2011","journal-title":"Biophys. J."},{"key":"10.1016\/j.jmb.2021.167010_b0305","doi-asserted-by":"crossref","first-page":"943","DOI":"10.1016\/j.jmb.2011.06.051","article-title":"Slow myosin ATP turnover in the super-relaxed state in tarantula muscle","volume":"411","author":"Naber","year":"2011","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2021.167010_b0310","doi-asserted-by":"crossref","first-page":"430","DOI":"10.1073\/pnas.0909468107","article-title":"Myosin ATP turnover rate is a mechanism involved in thermogenesis in resting skeletal muscle fibers","volume":"107","author":"Stewart","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2021.167010_b0315","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/j.pep.2015.08.018","article-title":"Combining a PagP fusion protein system with nickel ion-catalyzed cleavage to produce intrinsically disordered proteins in E. coli","volume":"116","author":"Zahran","year":"2015","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.jmb.2021.167010_b0320","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/j.febslet.2013.09.028","article-title":"Targeted expression, purification, and cleavage of fusion proteins from inclusion bodies in Escherichia coli","volume":"588","author":"Hwang","year":"2014","journal-title":"FEBS Letters"},{"key":"10.1016\/j.jmb.2021.167010_b0325","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1016\/j.pep.2012.07.007","article-title":"A PagP fusion protein system for the expression of intrinsically disordered proteins in Escherichia coli","volume":"85","author":"Hwang","year":"2012","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.jmb.2021.167010_b0330","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1007\/978-1-4939-6887-9_14","article-title":"Removal of affinity tags with TEV protease","volume":"1586","author":"Raran-Kurussi","year":"2017","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.jmb.2021.167010_b0335","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1007\/BF00197809","article-title":"NMRPipe: a multidimensional spectral processing system based on UNIX pipes","volume":"6","author":"Delaglio","year":"1995","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/j.jmb.2021.167010_b0340","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1007\/s10858-012-9626-5","article-title":"Measurement of (1)(5)N relaxation rates in perdeuterated proteins by TROSY-based methods","volume":"53","author":"Lakomek","year":"2012","journal-title":"J. Biomol. NMR"}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283621002114?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283621002114?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,19]],"date-time":"2025-09-19T21:43:05Z","timestamp":1758318185000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022283621002114"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,6]]},"references-count":68,"journal-issue":{"issue":"13","published-print":{"date-parts":[[2021,6]]}},"alternative-id":["S0022283621002114"],"URL":"https:\/\/doi.org\/10.1016\/j.jmb.2021.167010","relation":{},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[2021,6]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Dilated Cardiomyopathy Mutations and Phosphorylation disrupt the Active Orientation of Cardiac Troponin C","name":"articletitle","label":"Article Title"},{"value":"Journal of Molecular Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jmb.2021.167010","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2021 The Author(s). Published by Elsevier Ltd.","name":"copyright","label":"Copyright"}],"article-number":"167010"}}