{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T20:24:45Z","timestamp":1792095885531,"version":"4.4.0"},"reference-count":202,"publisher":"MDPI AG","issue":"11","license":[{"start":{"date-parts":[[2023,10,31]],"date-time":"2023-10-31T00:00:00Z","timestamp":1698710400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Antioxidants"],"abstract":"<jats:p>Mitochondria are specialized organelles, which serve as the \u201cPower House\u201d to generate energy for maintaining heart function. These organelles contain various enzymes for the oxidation of different substrates as well as the electron transport chain in the form of Complexes I to V for producing ATP through the process of oxidative phosphorylation (OXPHOS). Several studies have shown depressed OXPHOS activity due to defects in one or more components of the substrate oxidation and electron transport systems which leads to the depletion of myocardial high-energy phosphates (both creatine phosphate and ATP). Such changes in the mitochondria appear to be due to the development of oxidative stress, inflammation, and Ca2+-handling abnormalities in the failing heart. Although some investigations have failed to detect any changes in the OXPHOS activity in the failing heart, such results appear to be due to a loss of Ca2+ during the mitochondrial isolation procedure. There is ample evidence to suggest that mitochondrial Ca2+-overload occurs, which is associated with impaired mitochondrial OXPHOS activity in the failing heart. The depression in mitochondrial OXPHOS activity may also be due to the increased level of reactive oxygen species, which are formed as a consequence of defects in the electron transport complexes in the failing heart. Various metabolic interventions which promote the generation of ATP have been reported to be beneficial for the therapy of heart failure. Accordingly, it is suggested that depression in mitochondrial OXPHOS activity plays an important role in the development of heart failure.<\/jats:p>","DOI":"10.3390\/antiox12111941","type":"journal-article","created":{"date-parts":[[2023,10,31]],"date-time":"2023-10-31T12:44:03Z","timestamp":1698756243000},"page":"1941","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":55,"title":["Status of Mitochondrial Oxidative Phosphorylation during the Development of Heart Failure"],"prefix":"10.3390","volume":"12","author":[{"given":"Sukhwinder K.","family":"Bhullar","sequence":"first","affiliation":[{"name":"Institute of Cardiovascular Sciences, St. Boniface Hospital Albrechtsen Research Centre, Department of Physiology and Pathophysiology, Max Rady College of Medicine, University of Manitoba, Winnipeg, MB R2H 2A6, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Naranjan S.","family":"Dhalla","sequence":"additional","affiliation":[{"name":"Institute of Cardiovascular Sciences, St. Boniface Hospital Albrechtsen Research Centre, Department of Physiology and Pathophysiology, Max Rady College of Medicine, University of Manitoba, Winnipeg, MB R2H 2A6, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,10,31]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1124\/jpet.112.192104","article-title":"Mitochondrial Function and Dysfunction: An Update","volume":"342","author":"Davis","year":"2012","journal-title":"J. Pharmacol. Exp Ther."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1534\/genetics.117.300262","article-title":"Cell Biology of the Mitochondrion","volume":"207","author":"Sedensky","year":"2017","journal-title":"Genetics"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1960","DOI":"10.1161\/RES.0000000000000104","article-title":"Mitochondrial function, biology, and role in disease: A scientific statement from the American Heart Association","volume":"118","author":"Murphy","year":"2016","journal-title":"Circ. Res."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1198","DOI":"10.1161\/CIRCRESAHA.112.268946","article-title":"Mitochondrial Control of Cellular Life, Stress, and Death","volume":"111","author":"Galluzzi","year":"2012","journal-title":"Circ. Res."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1146\/annurev.ph.41.030179.002413","article-title":"Mitochondrial heart function","volume":"41","author":"Williamson","year":"1979","journal-title":"Ann. Rev. Physiol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1038\/s41580-018-0052-8","article-title":"The machineries, regulation and cellular functions of mitochondrial calcium","volume":"19","author":"Giorgi","year":"2018","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"342","DOI":"10.1038\/nrcardio.2017.23","article-title":"Sarcoplasmic reticulum\u2013mitochondria communication in cardiovascular pathophysiology","volume":"14","author":"Pennanen","year":"2017","journal-title":"Nat. Rev. Cardiol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"1812","DOI":"10.1161\/CIRCRESAHA.117.311082","article-title":"Autophagy and Mitophagy in Cardiovascular Disease","volume":"120","author":"Kroemer","year":"2017","journal-title":"Circ. Res."},{"key":"ref_9","doi-asserted-by":"crossref","unstructured":"Budde, H., Hassoun, R., Tangos, M., Zhazykbayeva, S., Herwig, M., Varatnitskaya, M., Sieme, M., Delalat, S., Sultana, I., and Kolijn, D. (2021). The Interplay between S-Glutathionylation and Phosphorylation of Cardiac Troponin I and Myosin Binding Protein C in End-Stage Human Failing Hearts. Antioxidants, 10.","DOI":"10.3390\/antiox10071134"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"8197","DOI":"10.1073\/pnas.0707723105","article-title":"Quantifying changes in the thiol redox proteome upon oxidative stress in vivo","volume":"105","author":"Leichert","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"412","DOI":"10.1038\/nrcardio.2017.35","article-title":"Myocardial stress and autophagy: Mechanisms and potential therapies","volume":"14","author":"Delbridge","year":"2017","journal-title":"Nat. Rev. Cardiol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"629","DOI":"10.1016\/S0092-8674(03)00926-7","article-title":"Integrated Analysis of Protein Composition, Tissue Diversity, and Gene Regulation in Mouse Mitochondria","volume":"115","author":"Mootha","year":"2003","journal-title":"Cell"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1616","DOI":"10.1093\/emboj\/21.7.1616","article-title":"Mitochondria are morphologically and functionally heterogeneous within cells","volume":"21","author":"Collins","year":"2002","journal-title":"EMBO J."},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"Glatz, J.F., Nabben, M., Young, M.E., Schulze, P.C., Taegtmeyer, H., and Luiken, J.J. (2020). Re-balancing cellular energy substrate metabolism to mend the failing heart. Biochim. Biophys. Acta (BBA)-Mol. Basis Dis., 1866.","DOI":"10.1016\/j.bbadis.2019.165579"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"1093","DOI":"10.1152\/physrev.00006.2004","article-title":"Myocardial Substrate Metabolism in the Normal and Failing Heart","volume":"85","author":"Stanley","year":"2005","journal-title":"Physiol. Rev."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1038\/nbt793","article-title":"Characterization of the human heart mitochondrial proteome","volume":"21","author":"Taylor","year":"2003","journal-title":"Nat. Biotechnol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"e012731","DOI":"10.1161\/JAHA.119.012731","article-title":"Complex Regulation of Mitochondrial Function During Cardiac Development","volume":"8","author":"Zhao","year":"2019","journal-title":"J. Am. Heart Assoc."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"2615","DOI":"10.1101\/gad.229724.113","article-title":"Hallmarks of a new era in mitochondrial biochemistry","volume":"27","author":"Pagliarini","year":"2013","journal-title":"Genes Dev."},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Chandel, N.S. (2014). Mitochondria as signaling organelles. BMC Biol., 12.","DOI":"10.1186\/1741-7007-12-34"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1029","DOI":"10.1083\/jcb.200609074","article-title":"The Qo site of the mitochondrial complex III is required for the transduction of hypoxic signaling via reactive oxygen species production","volume":"177","author":"Bell","year":"2007","journal-title":"J. Cell Biol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1016\/j.tem.2012.06.005","article-title":"The dynamic regulation of NAD metabolism in mitochondria","volume":"23","author":"Stein","year":"2012","journal-title":"Trends Endocrinol. Metab."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.celrep.2014.02.046","article-title":"Inhibition of ATPIF1 Ameliorates Severe Mitochondrial Respiratory Chain Dysfunction in Mammalian Cells","volume":"7","author":"Chen","year":"2014","journal-title":"Cell Rep."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/0022-2828(78)90042-1","article-title":"Mitochondrial calcium overloading in cardiomyopathic hamsters","volume":"10","author":"Wrogemann","year":"1978","journal-title":"J. Mol. Cell. Cardiol."},{"key":"ref_24","unstructured":"Dhalla, N.S., Lee, S.-L., Shah, K.R., Elimban, V., Suzuki, S., and Jasmin, G. (1994). Cardiomyopathic Heart, New York Raven Press Ltd."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"256","DOI":"10.21037\/atm.2018.06.21","article-title":"Mitochondria and cardiovascular diseases\u2014From pathophysiology to treatment","volume":"6","author":"Siasos","year":"2018","journal-title":"Ann. Transl. Med."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"16330","DOI":"10.1016\/S0021-9258(17)46227-2","article-title":"The oxidative inactivation of mitochondrial electron transport chain components and ATPase","volume":"265","author":"Zhang","year":"1990","journal-title":"J. Biol. Chem."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1278","DOI":"10.1016\/j.freeradbiomed.2005.02.014","article-title":"Mitochondrial dysfunction in cardiovascular disease","volume":"38","author":"Ballinger","year":"2005","journal-title":"Free Radic. Biol. Med."},{"key":"ref_28","doi-asserted-by":"crossref","unstructured":"Yang, J., Guo, Q., Feng, X., Liu, Y., and Zhou, Y. (2022). Mitochondrial Dysfunction in Cardiovascular Diseases: Potential Targets for Treatment. Front. Cell Dev. Biol., 10.","DOI":"10.3389\/fcell.2022.841523"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1080\/07853890.2017.1417631","article-title":"The role of mitochondrial dysfunction in cardiovascular disease: A brief review","volume":"50","author":"Chistiakov","year":"2018","journal-title":"Ann. Med."},{"key":"ref_30","doi-asserted-by":"crossref","unstructured":"Calbet, J.A.L., Mart\u00edn-Rodr\u00edguez, S., Martin-Rincon, M., and Morales-Alamo, D. (2020). An integrative approach to the regulation of mitochondrial respiration during exercise: Focus on high-intensity exercise. Redox Biol., 35.","DOI":"10.1016\/j.redox.2020.101478"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1007\/s10741-012-9340-0","article-title":"Mitochondrial dysfunction in heart failure","volume":"18","author":"Rosca","year":"2013","journal-title":"Heart Fail. Rev."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"011","DOI":"10.1055\/s-0037-1615263","article-title":"Heart and Mitochondria: Pathophysiology and Implications for Cardiac Surgeons","volume":"66","author":"Schwarzer","year":"2018","journal-title":"Thorac. Cardiovasc. Surg."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1038\/s41569-018-0074-0","article-title":"Targeting mitochondria for cardiovascular disorders: Therapeutic potential and obstacles","volume":"16","author":"Bonora","year":"2019","journal-title":"Nat. Rev. Cardiol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1514","DOI":"10.3389\/fphys.2018.01514","article-title":"Diabetic Cardiomyopathy: Current and Future Therapies. Beyond Glycemic Control","volume":"9","author":"Borghetti","year":"2018","journal-title":"Front. Physiol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"21630","DOI":"10.1002\/jcp.28821","article-title":"Impact of different ectopic fat depots on cardiovascular and metabolic diseases","volume":"234","author":"Ferrara","year":"2019","journal-title":"J. Cell. Physiol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"1606","DOI":"10.3389\/fphar.2019.01606","article-title":"Secondary Prevention Medical Therapy and Outcomes in Patients with Myocardial Infarction with Non-Obstructive Coronary Artery Disease","volume":"10","author":"Paolisso","year":"2020","journal-title":"Front. Pharmacol."},{"key":"ref_37","first-page":"48","article-title":"Heart mitochondrial function in chronic experimental diabetes in rats","volume":"1","author":"Pierce","year":"1985","journal-title":"Can. J. Cardiol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1016\/j.freeradbiomed.2009.12.022","article-title":"Reactive oxygen species, cellular redox systems, and apoptosis","volume":"48","author":"Circu","year":"2010","journal-title":"Free Radic. Biol. Med."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"883","DOI":"10.1161\/CIRCULATIONAHA.116.022495","article-title":"Normalization of NAD+ Redox Balance as a Therapy for Heart Failure","volume":"134","author":"Lee","year":"2016","journal-title":"Circulation"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1038\/nature10992","article-title":"Mitochondrial DNA that escapes from autophagy causes inflammation and heart failure","volume":"485","author":"Oka","year":"2012","journal-title":"Nature"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1038\/ni.1980","article-title":"Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome","volume":"12","author":"Nakahira","year":"2011","journal-title":"Nat. Immunol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1038\/nature09663","article-title":"A role for mitochondria in NLRP3 inflammasome activation","volume":"469","author":"Zhou","year":"2011","journal-title":"Nature"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1007\/s10741-007-9079-1","article-title":"Mitochondrial centrality in heart failure","volume":"13","author":"Goldenthal","year":"2008","journal-title":"Heart Fail. Rev."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"3716","DOI":"10.1172\/JCI120849","article-title":"Mitochondrial dysfunction in pathophysiology of heart failure","volume":"128","author":"Zhou","year":"2018","journal-title":"J. Clin. Investig."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"1140","DOI":"10.1056\/NEJMra063052","article-title":"The failing heart-an engine out of fuel","volume":"356","author":"Neubauer","year":"2007","journal-title":"N. Engl. J. Med."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1038\/s41569-018-0044-6","article-title":"Metabolic remodelling in heart failure","volume":"15","author":"Bertero","year":"2018","journal-title":"Nat. Rev. Cardiol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1016\/j.mito.2010.09.011","article-title":"Tissue-specific differences in mitochondrial activity and biogenesis","volume":"11","author":"Montoya","year":"2011","journal-title":"Mitochondrion"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1007\/s10863-009-9215-9","article-title":"New aspects of impaired mitochondrial function in heart failure","volume":"41","author":"Rosca","year":"2009","journal-title":"J. Bioenerg. Biomembr."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1093\/cvr\/cvq240","article-title":"Mitochondria in heart failure","volume":"88","author":"Rosca","year":"2010","journal-title":"Cardiovasc. Res."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"694","DOI":"10.1016\/j.yjmcc.2008.01.008","article-title":"Increased mitochondrial uncoupling proteins, respiratory uncoupling and decreased efficiency in the chronically infarcted rat heart","volume":"44","author":"Murray","year":"2008","journal-title":"J. Mol. Cell. Cardiol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"528","DOI":"10.1038\/s41556-018-0090-7","article-title":"Spatial orchestration of mitochondrial translation and OXPHOS complex assembly","volume":"20","author":"Stoldt","year":"2018","journal-title":"Nat. Cell Biol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"C1172","DOI":"10.1152\/ajpcell.00195.2006","article-title":"Physiological diversity of mitochondrial oxidative phosphorylation","volume":"291","author":"Benard","year":"2006","journal-title":"Am. J. Physiol. Physiol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"1266","DOI":"10.2174\/092986709787846578","article-title":"Mitochondrial Respiratory Complex I: Structure, Function and Implication in Human Diseases","volume":"16","author":"Sharma","year":"2009","journal-title":"Curr. Med. Chem."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1038\/nature11871","article-title":"Crystal structure of the entire respiratory complex I","volume":"494","author":"Baradaran","year":"2013","journal-title":"Nature"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1074\/jbc.RA118.006056","article-title":"Exploring the quinone\/inhibitor-binding pocket in mitochondrial respiratory complex I by chemical biology approaches","volume":"294","author":"Uno","year":"2019","journal-title":"J. Biol. Chem."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"29514","DOI":"10.1074\/jbc.M704519200","article-title":"Exploring the Ubiquinone Binding Cavity of Respiratory Complex I","volume":"282","author":"Tocilescu","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"1043","DOI":"10.1016\/j.cell.2005.05.025","article-title":"Crystal Structure of Mitochondrial Respiratory Membrane Protein Complex II","volume":"121","author":"Sun","year":"2005","journal-title":"Cell"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1016\/j.tibs.2017.01.003","article-title":"Mitochondrial Complex II: At the Crossroads","volume":"42","author":"Rohlena","year":"2017","journal-title":"Trends Biochem. Sci."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1007\/s13238-011-1079-1","article-title":"Thiabendazole inhibits ubiquinone reduction activity of mitochondrial respiratory complex II via a water molecule mediated binding feature","volume":"2","author":"Zhou","year":"2011","journal-title":"Protein Cell"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1598","DOI":"10.1016\/j.cell.2016.11.012","article-title":"Structure of mammalian respiratory supercomplex I1III2IV1","volume":"167","author":"Wu","year":"2016","journal-title":"Cell"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"590","DOI":"10.1128\/MMBR.00016-08","article-title":"ATP Synthase and the Actions of Inhibitors Utilized To Study Its Roles in Human Health, Disease, and Other Scientific Areas","volume":"72","author":"Hong","year":"2008","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"400","DOI":"10.1089\/ars.2012.4777","article-title":"Mitochondrial Dynamics in Cardiovascular Health and Disease","volume":"19","author":"Ong","year":"2013","journal-title":"Antioxid. Redox Signal."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1152\/physrev.00015.2009","article-title":"Myocardial fatty acid metabolism in health and disease","volume":"90","author":"Lopaschuk","year":"2010","journal-title":"Physiol. Rev."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"e84897","DOI":"10.1172\/jci.insight.84897","article-title":"Mitochondrial protein hyperacetylation in the failing heart","volume":"1","author":"Horton","year":"2016","journal-title":"JCI Insight"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"2052","DOI":"10.1161\/CIRCULATIONAHA.117.030486","article-title":"MicroRNA-195 Regulates Metabolism in Failing Myocardium Via Alterations in Sirtuin 3 Expression and Mitochondrial Protein Acetylation","volume":"137","author":"Zhang","year":"2018","journal-title":"Circulation"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"98","DOI":"10.2144\/000113610","article-title":"Mitochondrial membrane potential probes and the proton gradient: A practical usage guide","volume":"50","author":"Perry","year":"2011","journal-title":"BioTechniques"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1016\/j.cmet.2015.11.014","article-title":"Assessing the Mitochondrial Membrane Potential in Cells and In Vivo using Targeted Click Chemistry and Mass Spectrometry","volume":"23","author":"Logan","year":"2016","journal-title":"Cell Metab."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"1567","DOI":"10.1126\/science.1230381","article-title":"Supercomplex assembly determines electron flux in the mitochondrial electron transport chain","volume":"340","author":"Balsa","year":"2013","journal-title":"Science"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1007\/s00109-020-02004-8","article-title":"Mitochondrial respiratory supercomplexes in mammalian cells: Structural versus functional role","volume":"99","author":"Javadov","year":"2021","journal-title":"J. Mol. Med."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1016\/j.bbabio.2011.11.021","article-title":"Damage to mitochondrial complex I during cardiac ischemia reperfusion injury is reduced indirectly by anti-anginal drug ranolazine","volume":"1817","author":"Gadicherla","year":"2012","journal-title":"Biochim. Biophys. Acta (BBA)-Bioenerg."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"19565","DOI":"10.1073\/pnas.0810654106","article-title":"Opening and closing the metabolite gate","volume":"105","author":"Neutze","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/BJ20081386","article-title":"How mitochondria produce reactive oxygen species","volume":"417","author":"Murphy","year":"2009","journal-title":"Biochem. J."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"524","DOI":"10.1161\/CIRCRESAHA.114.300559","article-title":"Cardiac Mitochondria and Reactive Oxygen Species Generation","volume":"114","author":"Chen","year":"2014","journal-title":"Circ. Res."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1146\/annurev.bi.64.070195.000525","article-title":"Superoxide radical and superoxide dismutases","volume":"64","author":"Fridovich","year":"1995","journal-title":"Annu. Rev. Biochem."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"151","DOI":"10.3389\/fphar.2014.00151","article-title":"Glutathione and mitochondria","volume":"5","author":"Ribas","year":"2014","journal-title":"Front. Pharmacol."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"1883","DOI":"10.1089\/ars.2008.2114","article-title":"Regulation of reactive oxygen species and genomic stability in hematopoietic stem cells","volume":"10","author":"Naka","year":"2008","journal-title":"Antioxid. Redox Signal."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"2017","DOI":"10.1111\/bph.12468","article-title":"Targeting mitochondrial cardiolipin and the cytochrome c\/cardiolipin complex to promote electron transport and optimize mitochondrial ATP synthesis","volume":"171","author":"Birk","year":"2014","journal-title":"Br. J. Pharmacol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"1588","DOI":"10.1016\/j.bbabio.2012.04.015","article-title":"The stability and activity of respiratory Complex II is cardiolipin-dependent","volume":"1817","author":"Schwall","year":"2012","journal-title":"Biochim. Biophys Acta (BBA)-Bioenerg."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1016\/j.chemphyslip.2013.10.012","article-title":"Cardiolipin-dependent formation of mitochondrial respiratory supercomplexes","volume":"179","author":"Mileykovskaya","year":"2013","journal-title":"Chem. Phys. Lipids"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1074\/jbc.M112.425876","article-title":"Cardiolipin-dependent re-constitution of respiratory supercomplexes from purified Saccharomyces cerevisiae complexes III and IV","volume":"288","author":"Mileykovskaya","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"1799","DOI":"10.1016\/j.cmet.2023.07.015","article-title":"Preserved respiratory chain capacity and physiology in mice with profoundly reduced levels of mitochondrial respirasomes","volume":"35","author":"Milenkovic","year":"2023","journal-title":"Cell Metab."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"1757","DOI":"10.1006\/jmcc.1998.0739","article-title":"Abnormal Mitochondrial Function in Myocardium of Dogs with Chronic Heart Failure","volume":"30","author":"Sharov","year":"1998","journal-title":"J. Mol. Cell. Cardiol."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"2361","DOI":"10.1006\/jmcc.2000.1266","article-title":"Abnormal Mitochondrial Respiration in Failed Human Myocardium","volume":"32","author":"Sharov","year":"2000","journal-title":"J. Mol. Cell. Cardiol."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1161\/CIRCRESAHA.115.304384","article-title":"Super-suppression of mitochondrial reactive oxygen species signaling impairs compensatory autophagy in primary mitophagic cardiomyopathy","volume":"115","author":"Song","year":"2014","journal-title":"Circ. Res."},{"key":"ref_85","unstructured":"Ghadially, F. (1997). Ultrastructural Pathology of the Cell and Matrix, Butter-worth-Heinemann."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s12276-019-0355-7","article-title":"Mitochondrial dysfunction and oxidative stress in heart disease","volume":"51","author":"Peoples","year":"2019","journal-title":"Exp. Mol. Med."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"1327","DOI":"10.1161\/CIRCRESAHA.111.258723","article-title":"Mitochondrial Fusion is Essential for Organelle Function and Cardiac Homeostasis","volume":"109","author":"Chen","year":"2011","journal-title":"Circ. Res."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"1929","DOI":"10.1089\/ars.2010.3799","article-title":"Targeting Mitochondrial Dysfunction: Role for PINK1 and Parkin in Mitochondrial Quality Control","volume":"14","author":"Narendra","year":"2011","journal-title":"Antioxid. Redox Signal."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1007\/s10545-011-9382-9","article-title":"Mitochondrial ATP synthase: Architecture, function and pathology","volume":"35","author":"Jonckheere","year":"2012","journal-title":"J. Inherit. Metab. Dis."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1111\/j.1365-2796.2008.02058.x","article-title":"Mitochondrial medicine: Entering the era of treatment","volume":"265","author":"Koene","year":"2009","journal-title":"J. Intern. Med."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1016\/j.yjmcc.2006.09.013","article-title":"Cyclosporine A attenuates mitochondrial permeability transition and improves mitochondrial respiratory function in cardiomyocytes isolated from dogs with heart failure","volume":"42","author":"Sharov","year":"2007","journal-title":"J. Mol. Cell. Cardiol."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1007\/s10741-012-9346-7","article-title":"Alterations in mitochondrial function in cardiac hypertrophy and heart failure","volume":"18","author":"Osterholt","year":"2013","journal-title":"Heart Fail. Rev."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"1228","DOI":"10.1161\/CIRCRESAHA.114.303551","article-title":"Metabolic Flux as a Predictor of Heart Failure Prognosis","volume":"114","author":"Lygate","year":"2014","journal-title":"Circ. Res."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1146\/annurev.pharmtox.47.120505.105122","article-title":"Mitochondrial Oxidative Stress: Implications for Cell Death","volume":"47","author":"Orrenius","year":"2007","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"2256","DOI":"10.1161\/CIRCULATIONAHA.116.026099","article-title":"Nicotinamide Riboside Preserves Cardiac Function in a Mouse Model of Dilated Cardiomyopathy","volume":"137","author":"Diguet","year":"2018","journal-title":"Circulation"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"1629","DOI":"10.1161\/CIRCRESAHA.120.317046","article-title":"NAD + Repletion Reverses Heart Failure with Preserved Ejection Fraction","volume":"128","author":"Tong","year":"2021","journal-title":"Circ. Res."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"821","DOI":"10.1016\/j.yjmcc.2009.02.021","article-title":"What is the mitochondrial permeability transition pore?","volume":"46","author":"Halestrap","year":"2009","journal-title":"J. Mol. Cell. Cardiol."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1042\/bj3410233","article-title":"The mitochondrial permeability transition pore and its role in cell death","volume":"341","author":"Crompton","year":"1999","journal-title":"Biochem. J."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"1701","DOI":"10.1016\/j.bbamcr.2007.10.001","article-title":"Regulation of mitochondrial oxidative phosphorylation through cell signaling","volume":"1773","author":"Lee","year":"2007","journal-title":"Biochim. Biophys. Acta (BBA)-Mol. Cell Res."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"H623","DOI":"10.1152\/ajpheart.00493.2014","article-title":"Mitochondria-derived ROS bursts disturb Ca2+ cycling and induce abnormal automaticity in guinea pig cardiomyocytes: A theoretical study","volume":"308","author":"Li","year":"2015","journal-title":"Am. J. Physiol. Circ. Physiol."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1152\/physrev.00018.2001","article-title":"Free Radicals in the Physiological Control of Cell Function","volume":"82","year":"2002","journal-title":"Physiol. Rev."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"566","DOI":"10.1038\/nrm3412","article-title":"Mitochondria as sensors and regulators of calcium signalling","volume":"13","author":"Rizzuto","year":"2012","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"H1986","DOI":"10.1152\/ajpheart.01214.2006","article-title":"Role of oxidative stress in alterations of mitochondrial function in ischemic-reperfused hearts","volume":"292","author":"Makazan","year":"2007","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"789","DOI":"10.1139\/Y09-050","article-title":"Mitochondrial oxidative phosphorylation in hearts subjected to Ca2+ depletion and Ca2+ repletion","volume":"87","author":"Makazan","year":"2009","journal-title":"Can. J. Physiol. Pharmacol."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"632","DOI":"10.1016\/j.yjmcc.2011.05.007","article-title":"Dynamic modulation of Ca2+ sparks by mitochondrial oscillations in isolated guinea pig cardiomyocytes under oxidative stress","volume":"51","author":"Zhou","year":"2011","journal-title":"J. Mol. Cell. Cardiol."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1038\/nrcardio.2014.189","article-title":"Mitochondrial dysfunction and oxidative stress in CHF","volume":"12","author":"Okonko","year":"2015","journal-title":"Nat. Rev. Cardiol."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1161\/01.RES.85.4.357","article-title":"Mitochondrial Electron Transport Complex I Is a Potential Source of Oxygen Free Radicals in the Failing Myocardium","volume":"85","author":"Ide","year":"1999","journal-title":"Circ. Res."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1146\/annurev-pharmtox-010715-103335","article-title":"Mitochondrial Dysfunction and Myocardial Ischemia-Reperfusion: Implications for Novel Therapies","volume":"57","author":"Lesnefsky","year":"2017","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1089\/ars.2016.6635","article-title":"Elucidating Mitochondrial Electron Transport Chain Supercomplexes in the Heart During Ischemia\u2013Reperfusion","volume":"27","author":"Jang","year":"2017","journal-title":"Antioxid. Redox Signal."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"374","DOI":"10.1093\/cvr\/cvv279","article-title":"Succinate dehydrogenase inhibition with malonate during reperfusion reduces infarct size by preventing mitochondrial permeability transition","volume":"109","author":"Barba","year":"2016","journal-title":"Cardiovasc. Res."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"700","DOI":"10.1016\/j.mito.2011.06.001","article-title":"The role of mitochondrial membrane potential in ischemic heart failure","volume":"11","author":"Kadenbach","year":"2011","journal-title":"Mitochondrion"},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"686","DOI":"10.1038\/cdd.2008.13","article-title":"Role of hypoxia-inducible factor in cell survival during myocardial ischemia\u2013reperfusion","volume":"15","author":"Loor","year":"2008","journal-title":"Cell Death Differ."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"H541","DOI":"10.1152\/ajpheart.01142.2002","article-title":"Oxidative capacity in failing hearts","volume":"285","author":"Gong","year":"2003","journal-title":"Am. J. Physiol. Circ. Physiol."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"1729","DOI":"10.1016\/j.biocel.2011.08.008","article-title":"Mitochondrial respiratory control and early defects of oxidative phosphorylation in the failing human heart","volume":"43","author":"Lemieux","year":"2011","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"1205893","DOI":"10.3389\/fcvm.2023.1205893","article-title":"Myocardial capacity of mitochondrial oxidative phosphorylation in response to prolonged electromagnetic stress","volume":"10","author":"Savchenko","year":"2023","journal-title":"Front. Cardiovasc. Med."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"e002206","DOI":"10.1161\/CIRCHEARTFAILURE.115.002206","article-title":"Chronic Therapy with Elamipretide (MTP-131), a Novel Mitochondria-Targeting Peptide, Improves Left Ventricular and Mitochondrial Function in Dogs with Advanced Heart Failure","volume":"9","author":"Sabbah","year":"2016","journal-title":"Circ. Heart Fail."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1089\/ars.2009.2788","article-title":"Potential Therapeutic Benefits of Strategies Directed to Mitochondria","volume":"13","author":"Lesnefsky","year":"2010","journal-title":"Antioxid. Redox Signal."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"e2203628119","DOI":"10.1073\/pnas.2203628119","article-title":"Succinyl-CoA-based energy metabolism dysfunction in chronic heart failure","volume":"119","author":"Takada","year":"2022","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1016\/j.yjmcc.2019.11.159","article-title":"Defining decreased protein succinylation of failing human cardiac myofibrils in ischemic cardiomyopathy","volume":"138","author":"Ali","year":"2020","journal-title":"J. Mol. Cell. Cardiol."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"958","DOI":"10.1161\/CIRCRESAHA.117.311578","article-title":"Lack of Remuscularization Following Transplantation of Human Embryonic Stem Cell-Derived Cardiovascular Progenitor Cells in Infarcted Nonhuman Primates","volume":"122","author":"Zhu","year":"2018","journal-title":"Circ. Res."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"2007","DOI":"10.1161\/CIRCULATIONAHA.120.050812","article-title":"LARP7 Protects Against Heart Failure by Enhancing Mitochondrial Biogenesis","volume":"143","author":"Yu","year":"2021","journal-title":"Circulation"},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1007\/s10557-018-6805-y","article-title":"Abnormalities of Mitochondrial Dynamics in the Failing Heart: Normalization Following Long-Term Therapy with Elamipretide","volume":"32","author":"Sabbah","year":"2018","journal-title":"Cardiovasc. Drugs Ther."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"829","DOI":"10.1161\/CIRCULATIONAHA.121.055727","article-title":"DYRK1B-STAT3 drives cardiac hypertrophy and heart failure by impairing mito-chondrial bioenergetics","volume":"145","author":"Zhuang","year":"2022","journal-title":"Circulation"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1161\/CIRCULATIONAHA.120.050498","article-title":"Myocardial Gene Expression Signatures in Human Heart Failure with Preserved Ejection Fraction","volume":"143","author":"Hahn","year":"2021","journal-title":"Circulation"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"e13378","DOI":"10.1111\/apha.13378","article-title":"Disturbed cardiac mitochondrial and cytosolic calcium handling in a metabolic risk-related rat model of heart failure with preserved ejection fraction","volume":"228","author":"Kuster","year":"2020","journal-title":"Acta Physiol."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"810","DOI":"10.1016\/j.bbadis.2018.08.025","article-title":"The role of mitochondrial cardiolipin in heart function and its implication in cardiac disease","volume":"1865","author":"Dudek","year":"2019","journal-title":"Biochim. Biophys. Acta Mol. Basis Dis."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"1196","DOI":"10.1016\/j.jacc.2010.02.075","article-title":"Coenzyme Q10, Rosuvastatin, and Clinical Outcomes in Heart Failure: A Pre-Specified Substudy of CORONA (Controlled Rosuvastatin Multinational Study in Heart Failure)","volume":"56","author":"McMurray","year":"2010","journal-title":"J. Am. Coll. Cardiol."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1186\/s12964-019-0445-0","article-title":"Linoleic acid improves assembly of the CII subunit and CIII2\/CIV complex of the mitochondrial oxidative phosphorylation system in heart failure","volume":"17","author":"Maekawa","year":"2019","journal-title":"Cell Commun. Signal."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"2161","DOI":"10.1021\/pr1008042","article-title":"Characterization of the Human Myocardial Proteome in Inflammatory Dilated Cardiomyopathy by Label-free Quantitative Shotgun Proteomics of Heart Biopsies","volume":"10","author":"Hammer","year":"2011","journal-title":"J. Proteome Res."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"860","DOI":"10.1016\/S0008-6363(99)00388-0","article-title":"Mitochondrial function in heart muscle from patients with idiopathic dilated cardiomyopathy","volume":"45","author":"Jarreta","year":"2000","journal-title":"Cardiovasc. Res."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1093\/oxfordjournals.eurheartj.a059743","article-title":"Alterations of the mitochondrial respiratory chain in human dilated cardiomyopathy","volume":"11","author":"Buchwald","year":"1990","journal-title":"Eur. Heart J."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1093\/cvr\/cvr015","article-title":"Mitochondrial adaptations to physiological vs. pathological cardiac hypertrophy","volume":"90","author":"Abel","year":"2011","journal-title":"Cardiovasc. Res."},{"key":"ref_133","doi-asserted-by":"crossref","unstructured":"Bragoszewski, P., Turek, M., and Chacinska, A. (2017). Control of mitochondrial biogenesis and function by the ubiquitin-proteasome system. Open Biol., 7.","DOI":"10.1098\/rsob.170007"},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1089\/ars.2017.7415","article-title":"Mitochondrial NAD+\/NADH redox state and diabetic cardiomyopathy","volume":"30","author":"Berthiaume","year":"2019","journal-title":"Antioxid. Redox Signal."},{"key":"ref_135","doi-asserted-by":"crossref","unstructured":"Mongirdien\u0117, A., Liuiz\u0117, A., Kar\u010diauskait\u0117, D., Mazgelyt\u0117, E., Liekis, A., and Sadauskien\u0117, I. (2023). Relationship between Oxidative Stress and Left Ventricle Markers in Patients with Chronic Heart Failure. Cells, 12.","DOI":"10.3390\/cells12050803"},{"key":"ref_136","doi-asserted-by":"crossref","unstructured":"Shah, A.K., Bhullar, S.K., Elimban, V., and Dhalla, N.S. (2021). Oxidative Stress as A Mechanism for Functional Alterations in Cardiac Hypertrophy and Heart Failure. Antioxidants, 10.","DOI":"10.3390\/antiox10060931"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"2492","DOI":"10.1161\/hc4501.098944","article-title":"Mitochondrial Abnormalities in Tumor Necrosis Factor-\u03b1\u2013Induced Heart Failure Are Associated with Impaired DNA Repair Activity","volume":"104","author":"Li","year":"2001","journal-title":"Circulation"},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"1161","DOI":"10.1016\/S0022-2828(03)00204-9","article-title":"Mitochondrial tolerance to stress impaired in failing heart","volume":"35","author":"Ozcan","year":"2003","journal-title":"J. Mol. Cell. Cardiol."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"1333","DOI":"10.1016\/0022-2828(92)93098-5","article-title":"Mitochondrial abnormalities in myocardium of dogs with chronic heart failure","volume":"24","author":"Sabbah","year":"1992","journal-title":"J. Mol. Cell. Cardiol."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1161\/01.RES.88.5.529","article-title":"Mitochondrial DNA Damage and Dysfunction Associated with Oxidative Stress in Failing Hearts After Myocardial Infarction","volume":"88","author":"Ide","year":"2001","journal-title":"Circ. Res."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1161\/01.RES.21.3.355","article-title":"Normal oxidative phosphorylation in mitochondria from the failing heart","volume":"21","author":"Sobel","year":"1967","journal-title":"Circ. Res."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"998","DOI":"10.1016\/j.yjmcc.2006.08.117","article-title":"Compensated volume overload increases the vulnerability of heart mitochondria without affecting their functions in the absence of stress","volume":"41","author":"Marcil","year":"2006","journal-title":"J. Mol. Cell. Cardiol."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1152\/ajplegacy.1973.224.3.497","article-title":"Mitochondria and sarcoplasmic reticulum function in cardiac hypertrophy and failure","volume":"224","author":"Sordahl","year":"1973","journal-title":"Am. J. Physiol. Content"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"2837","DOI":"10.1161\/01.CIR.94.11.2837","article-title":"Fatty Acid Oxidation Enzyme Gene Expression Is Downregulated in the Failing Heart","volume":"94","author":"Sack","year":"1996","journal-title":"Circulation"},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1161\/CIRCRESAHA.118.312708","article-title":"Mitochondrial ROS drive sudden cardiac death and chronic proteome remodeling in heart failure","volume":"123","author":"Dey","year":"2018","journal-title":"Circ. Res."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"909","DOI":"10.1152\/physrev.00026.2013","article-title":"Mitochondrial Reactive Oxygen Species (ROS) and ROS-Induced ROS Release","volume":"94","author":"Zorov","year":"2014","journal-title":"Physiol. Rev."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"1373","DOI":"10.1089\/ars.2008.2331","article-title":"Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function","volume":"11","author":"Stowe","year":"2009","journal-title":"Antioxid. Redox Signal."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"2685","DOI":"10.1089\/ars.2009.2695","article-title":"Mitochondrial glutathione, a key survival anti-oxidant","volume":"11","author":"Morales","year":"2009","journal-title":"Antioxid. Redox Signal."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"1595","DOI":"10.1038\/s41467-023-37291-5","article-title":"A defect in mitochondrial protein translation influences mitonuclear communication in the heart","volume":"14","author":"Gao","year":"2023","journal-title":"Nat. Commun."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"243","DOI":"10.4161\/auto.7.2.14332","article-title":"PINK1-parkin-dependent mitophagy involves ubiquitination of mitofusins 1 and 2: Implications for Parkinson disease pathogenesis","volume":"7","author":"Gegg","year":"2011","journal-title":"Autophagy"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1038\/cdd.2012.81","article-title":"The pathways of mitophagy for quality control and clearance of mitochondria","volume":"20","author":"Ashrafi","year":"2013","journal-title":"Cell Death Differ."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1016\/j.ejphar.2015.04.056","article-title":"Mitochondrial fusion and fission proteins as novel therapeutic targets for treating cardiovascular disease","volume":"763","author":"Ong","year":"2015","journal-title":"Eur. J. Pharmacol."},{"key":"ref_153","doi-asserted-by":"crossref","unstructured":"M\u00fcller, M., Donhauser, E., Maske, T., Bischof, C., Dumitrescu, D., Rudolph, V., and Klinke, A. (2023). Mitochondrial Integrity Is Critical in Right Heart Failure Development. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms241311108"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1161\/CIRCRESAHA.110.236745","article-title":"MARF and Opa1 control mitochondrial and cardiac function in Drosophila","volume":"108","author":"Dorn","year":"2011","journal-title":"Circ. Res."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"1012","DOI":"10.1161\/CIRCRESAHA.112.274142","article-title":"Mitofusins 1 and 2 Are Essential for Postnatal Metabolic Remodeling in Heart","volume":"111","author":"Papanicolaou","year":"2012","journal-title":"Circ. Res."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1093\/cvr\/cvp181","article-title":"Mitochondrial OPA1, apoptosis, and heart failure","volume":"84","author":"Chen","year":"2009","journal-title":"Cardiovasc. Res."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"8122","DOI":"10.1002\/jcp.27597","article-title":"Mitochondrial quality control in cardiac cells: Mechanisms and role in cardiac cell injury and disease","volume":"234","author":"Tahrir","year":"2019","journal-title":"J. Cell. Physiol."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"863","DOI":"10.1161\/CIRCRESAHA.112.266585","article-title":"Mitofusin 2-containing mitochondrial-reticular microdomains direct rapid cardiomyocyte bioenergetic responses via interorganelle Ca2+ crosstalk","volume":"111","author":"Chen","year":"2012","journal-title":"Circ. Res."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"1309","DOI":"10.1128\/MCB.00911-10","article-title":"Mitofusin-2 Maintains Mitochondrial Structure and Contributes to Stress-Induced Permeability Transition in Cardiac Myocytes","volume":"31","author":"Papanicolaou","year":"2011","journal-title":"Mol. Cell. Biol."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1016\/j.cmet.2014.12.011","article-title":"Mitochondrial Fission and Fusion Factors Reciprocally Orchestrate Mitophagic Culling in Mouse Hearts and Cultured Fibroblasts","volume":"21","author":"Song","year":"2015","journal-title":"Cell Metab."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"402","DOI":"10.15252\/embj.201592789","article-title":"Bax assembles into large ring-like structures re-modeling the mitochondrial outer membrane in apoptosis","volume":"35","author":"Wurm","year":"2016","journal-title":"EMBO J."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1016\/j.yjmcc.2014.09.019","article-title":"Molecular mechanisms mediating mitochondrial dynamics and mitophagy and their functional roles in the cardiovascular system","volume":"78","author":"Ikeda","year":"2015","journal-title":"J. Mol. Cell. Cardiol."},{"key":"ref_163","first-page":"236","article-title":"Impairment of mitochondrial and sarcoplasmic reticular functions during the development of heart failure in cardiomyopathic (UM-X7. 1) hamsters","volume":"2","author":"Panagia","year":"1986","journal-title":"Can. J. Cardiol."},{"key":"ref_164","first-page":"51","article-title":"Improvement of cardiac function and myocardial energy metabolism of rats with chronic heart failure by long-term coenzyme Q10 treatment","volume":"269","author":"Sanbe","year":"1994","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"ref_165","unstructured":"Pierce, G.N., Tuana, B.S., Moffat, M.P., Singal, P.K., Panagia, V., and Dhalla, N.S. (1984). Functional Aspects of the Normal, Hypertrophied, and Failing Heart, Springer."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/j.freeradbiomed.2021.07.040","article-title":"Prognostic value of oxidative stress in patients with acute myocardial infarction complicated by cardiogenic shock: A prospective cohort study","volume":"174","author":"Tomandlova","year":"2021","journal-title":"Free Radic. Biol. Med."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"494","DOI":"10.1177\/2047487319870344","article-title":"Oxidative stress and inflammation in the evolution of heart failure: From pathophysiology to therapeutic strategies","volume":"27","author":"Aimo","year":"2020","journal-title":"Eur. J. Prev. Cardiol."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1007\/s10545-010-9162-y","article-title":"Metabolic manipulators: A well founded strategy to combat mitochondrial dysfunction","volume":"34","author":"Koene","year":"2011","journal-title":"J. Inherit. Metab. Dis."},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1038\/nrd3403","article-title":"Combating oxidative stress in vascular disease: NADPH oxidases as therapeutic targets","volume":"10","author":"Drummond","year":"2011","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"9572","DOI":"10.1073\/pnas.1106291108","article-title":"PTEN-inducible kinase 1 (PINK1)\/Park6 is indispensable for normal heart function","volume":"108","author":"Billia","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"1860","DOI":"10.1016\/j.ijcard.2012.04.156","article-title":"Cardiovascular mortality and N-terminal-proBNP reduced after combined selenium and coenzyme Q10 supplementation: A 5-year prospective randomized double-blind placebo-controlled trial among elderly Swedish citizens","volume":"167","author":"Alehagen","year":"2013","journal-title":"Int. J. Cardiol."},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"2656","DOI":"10.1056\/NEJMra022567","article-title":"Mitochondrial Respiratory-Chain Diseases","volume":"348","author":"DiMauro","year":"2003","journal-title":"N. Engl. J. Med."},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"326rv3","DOI":"10.1126\/scitranslmed.aac7410","article-title":"Novel targets for mitochondrial medicine","volume":"8","author":"Wang","year":"2016","journal-title":"Sci. Transl. Med."},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1007\/164_2017_1","article-title":"The mitochondrial Ca2+ uniporter: Structure, function, and pharmacology","volume":"Volume 240","author":"Singh","year":"2017","journal-title":"Pharmacology of Mitochondria"},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"106038","DOI":"10.1016\/j.phrs.2021.106038","article-title":"Mitochondrial dysfunction and mitochondrial therapies in heart failure","volume":"175","author":"Wu","year":"2022","journal-title":"Pharmacol. Res."},{"key":"ref_176","doi-asserted-by":"crossref","unstructured":"Zanini, G., Selleri, V., Malerba, M., Solodka, K., Sinigaglia, G., Nasi, M., Mattioli, A.V., and Pinti, M. (2023). The Role of Lonp1 on Mitochondrial Functions during Cardiovascular and Muscular Diseases. Antioxidants, 12.","DOI":"10.3390\/antiox12030598"},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"7623","DOI":"10.1038\/s41598-019-43761-y","article-title":"Mitochondrial Oxidative Phosphorylation defect in the Heart of Subjects with Coronary Artery Disease","volume":"9","author":"Blaszak","year":"2019","journal-title":"Sci. Rep."},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"859253","DOI":"10.3389\/fcvm.2022.859253","article-title":"Direct Cardiac Actions of Sodium-Glucose Cotransporter 2 Inhibition Improve Mitochondrial Function and Attenuate Oxidative Stress in Pressure Overload-Induced Heart Failure","volume":"9","author":"Li","year":"2022","journal-title":"Front. Cardiovasc. Med."},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1016\/j.jacbts.2017.07.003","article-title":"Empagliflozin Prevents Worsening of Cardiac Function in an Experimental Model of Pressure Overload-Induced Heart Failure","volume":"2","author":"Byrne","year":"2017","journal-title":"JACC Basic Transl. Sci."},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"e018298","DOI":"10.1161\/JAHA.120.018298","article-title":"Direct cardiac actions of the sodium glucose co-transporter 2 inhibitor empagliflozin im-prove myocardial oxidative phosphorylation and attenuate pressure-overload heart failure","volume":"10","author":"Li","year":"2021","journal-title":"J. Am. Heart Assoc."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1038\/clpt.2014.174","article-title":"Serendipity and the discovery of novel compounds that restore mitochondrial plasticity","volume":"96","author":"Szeto","year":"2014","journal-title":"Clin. Pharmacol. Ther."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1016\/j.bbabio.2015.03.007","article-title":"Cardiolipin is a key determinant for mtDNA stability and segregation during mitochondrial stress","volume":"1847","author":"Forni","year":"2015","journal-title":"Biochim. Biophys. Acta (BBA)-Bioenerg."},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"68","DOI":"10.3389\/fcvm.2018.00068","article-title":"Loss of Metabolic Flexibility in the Failing Heart","volume":"5","author":"Karwi","year":"2018","journal-title":"Front. Cardiovasc. Med."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"11684","DOI":"10.1038\/s41598-022-15743-0","article-title":"PFKM inhibits doxorubicin-induced cardiotoxicity by enhancing oxidative phosphorylation and glycolysis","volume":"12","author":"Zhou","year":"2022","journal-title":"Sci. Rep."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"422","DOI":"10.1016\/j.jacc.2019.11.031","article-title":"Mechanisms of cardiorenal effects of sodium-glucose cotransporter 2 inhibitors: JACC state-of-the-art review","volume":"75","author":"Zelniker","year":"2020","journal-title":"J. Am. Coll. Cardiol."},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"191","DOI":"10.3389\/fendo.2020.00191","article-title":"Metformin and Its Benefits for Various Diseases","volume":"11","author":"Lv","year":"2020","journal-title":"Front. Endocrinol."},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"388","DOI":"10.14740\/jocmr2922e","article-title":"Effect of Metformin on Different Non-Diabetes Related Conditions, a Special Focus on Malignant Conditions: Review of Literature","volume":"9","author":"Abdelgadir","year":"2017","journal-title":"J. Clin. Med. Res."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1016\/S2213-8587(13)70152-9","article-title":"Metformin for non-diabetic patients with coronary heart disease (the CAMERA study): A randomised controlled trial","volume":"2","author":"Preiss","year":"2014","journal-title":"Lancet Diabetes Endocrinol."},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1016\/j.jchf.2014.06.008","article-title":"The effect of coenzyme Q10 on morbidity and mortality in chronic heart failure: Results from Q-SYMBIO: A randomized double-blind trial","volume":"2","author":"Mortensen","year":"2014","journal-title":"JACC Heart Fail."},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1016\/0006-3002(57)90457-2","article-title":"Isolation of a quinone from beef heart mitochondria","volume":"25","author":"FL","year":"1957","journal-title":"Biochim. Biophys. Acta."},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1016\/S0140-6736(00)02531-9","article-title":"Quinone-responsive multiple respiratory-chain dysfunction due to widespread coenzyme Q10 deficiency","volume":"356","author":"Appelkvist","year":"2000","journal-title":"Lancet"},{"key":"ref_192","doi-asserted-by":"crossref","unstructured":"Gutierrez-Mariscal, F.M., Larriva, A.P.A.-D., Limia-Perez, L., Romero-Cabrera, J.L., Yubero-Serrano, E.M., and L\u00f3pez-Miranda, J. (2020). Coenzyme Q10 Supplementation for the Reduction of Oxidative Stress: Clinical Implications in the Treatment of Chronic Diseases. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21217870"},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"s287","DOI":"10.1016\/0098-2997(94)90040-X","article-title":"Italian multicenter study on the safety and efficacy of coenzyme Q10 as adjunctive therapy in heart failure","volume":"15","author":"Baggio","year":"1994","journal-title":"Mol. Asp. Med."},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"eabb1929","DOI":"10.1126\/sciadv.abb1929","article-title":"Translatable mitochondria-targeted protection against programmed cardiovascular dysfunction","volume":"6","author":"Botting","year":"2020","journal-title":"Sci. Adv."},{"key":"ref_195","doi-asserted-by":"crossref","unstructured":"Goh, K.Y., He, L., Song, J., Jinno, M., Rogers, A.J., Sethu, P., Halade, G.V., Rajasekaran, N.S., Liu, X., and Prabhu, S.D. (2019). Mitoquinone ameliorates pressure overload-induced cardiac fibrosis and left ventricular dysfunction in mice. Redox Biol., 21.","DOI":"10.1016\/j.redox.2019.101100"},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1016\/j.redox.2016.12.022","article-title":"The mitochondria-targeted antioxidant MitoQ ameliorated tubular injury mediated by mitophagy in diabetic kidney disease via Nrf2\/PINK1","volume":"11","author":"Xiao","year":"2017","journal-title":"Redox Biol."},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"1701024","DOI":"10.1183\/13993003.01024-2017","article-title":"Impact of the mitochondria-targeted antioxidant MitoQ on hypoxia-induced pulmonary hypertension","volume":"51","author":"Pak","year":"2018","journal-title":"Eur. Respir. J."},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"H682","DOI":"10.1152\/ajpheart.00617.2019","article-title":"MitoQ regulates redox-related noncoding RNAs to preserve mitochondrial network integrity in pressure-overload heart failure","volume":"318","author":"Kim","year":"2020","journal-title":"Am. J. Physiol. Circ. Physiol."},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"316","DOI":"10.1096\/fj.12-226225","article-title":"Dynamin-related protein 1 (Drp1)-mediated diastolic dysfunction in myocardial ischemia-reperfusion injury: Therapeutic benefits of Drp1 inhibition to reduce mitochondrial fission","volume":"28","author":"Sharp","year":"2013","journal-title":"FASEB J."},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"e38","DOI":"10.1097\/CCM.0000000000000817","article-title":"Inhibition of the mitochondrial fission protein Drp1 improves survival in a murine cardiac arrest model","volume":"43","author":"Sharp","year":"2015","journal-title":"Crit. Care Med."},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1007\/s00109-017-1522-8","article-title":"Ischemia-induced Drp1 and Fis1-mediated mitochondrial fission and right ventricular dysfunction in pulmonary hypertension","volume":"95","author":"Tian","year":"2017","journal-title":"J. Mol. Med."},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"e000461","DOI":"10.1161\/JAHA.113.000461","article-title":"Acute Inhibition of Excessive Mitochondrial Fission After Myocardial Infarction Prevents Long-term Cardiac Dysfunction","volume":"2","author":"Disatnik","year":"2013","journal-title":"J. Am. Heart Assoc."}],"container-title":["Antioxidants"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2076-3921\/12\/11\/1941\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T21:14:43Z","timestamp":1760130883000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2076-3921\/12\/11\/1941"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,10,31]]},"references-count":202,"journal-issue":{"issue":"11","published-online":{"date-parts":[[2023,11]]}},"alternative-id":["antiox12111941"],"URL":"https:\/\/doi.org\/10.3390\/antiox12111941","relation":{},"ISSN":["2076-3921"],"issn-type":[{"value":"2076-3921","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,10,31]]}}}