{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T12:04:35Z","timestamp":1790251475151,"version":"4.1.0"},"reference-count":171,"publisher":"MDPI AG","issue":"14","license":[{"start":{"date-parts":[[2021,7,8]],"date-time":"2021-07-08T00:00:00Z","timestamp":1625702400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100012190","name":"Ministry of Science and Higher Education of the Russian Federation","doi-asserted-by":"publisher","award":["Agreement No. 075-15-2020-901"],"award-info":[{"award-number":["Agreement No. 075-15-2020-901"]}],"id":[{"id":"10.13039\/501100012190","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Mitochondrial dysfunction is considered the major contributor to skeletal muscle wasting in different conditions. Genetically determined neuromuscular disorders occur as a result of mutations in the structural proteins of striated muscle cells and therefore are often combined with cardiac phenotype, which most often manifests as a cardiomyopathy. The specific roles played by mitochondria and mitochondrial energetic metabolism in skeletal muscle under muscle-wasting conditions in cardiomyopathies have not yet been investigated in detail, and this aspect of genetic muscle diseases remains poorly characterized. This review will highlight dysregulation of mitochondrial representation and bioenergetics in specific skeletal muscle disorders caused by mutations that disrupt the structural and functional integrity of muscle cells.<\/jats:p>","DOI":"10.3390\/ijms22147349","type":"journal-article","created":{"date-parts":[[2021,7,8]],"date-time":"2021-07-08T10:42:17Z","timestamp":1625740937000},"page":"7349","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":26,"title":["Skeletal Muscle Mitochondria Dysfunction in Genetic Neuromuscular Disorders with Cardiac Phenotype"],"prefix":"10.3390","volume":"22","author":[{"given":"Elena","family":"Ignatieva","sequence":"first","affiliation":[{"name":"Almazov National Medical Research Centre, 197341 St. Petersburg, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Natalia","family":"Smolina","sequence":"additional","affiliation":[{"name":"Almazov National Medical Research Centre, 197341 St. Petersburg, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9349-6257","authenticated-orcid":false,"given":"Anna","family":"Kostareva","sequence":"additional","affiliation":[{"name":"Almazov National Medical Research Centre, 197341 St. Petersburg, Russia"},{"name":"Department of Woman and Child Health, Karolinska Institute, 17177 Stockholm, Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3073-7914","authenticated-orcid":false,"given":"Renata","family":"Dmitrieva","sequence":"additional","affiliation":[{"name":"Almazov National Medical Research Centre, 197341 St. Petersburg, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,7,8]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"364","DOI":"10.7196\/SAMJ.2019.v109i6.14069","article-title":"An overview of the genetic basis of cardiovascular disease","volume":"109","author":"Laing","year":"2019","journal-title":"S. Afr. Med. J."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"325","DOI":"10.2741\/S375","article-title":"Genetic spectrum of cardiomyopathies with neuromuscular phenotype","volume":"5","author":"Kostareva","year":"2013","journal-title":"Front. Biosci."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"837","DOI":"10.2459\/JCM.0b013e3283641c69","article-title":"Skeletal muscle involvement in cardiomyopathies","volume":"14","author":"Limongelli","year":"2013","journal-title":"J. Cardiovasc. Med."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"608","DOI":"10.3389\/fgene.2019.00608","article-title":"Truncating variant in myof gene is associated with limb-girdle type muscular dystrophy and cardiomyopathy","volume":"10","author":"Kiselev","year":"2019","journal-title":"Front. Genet."},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Hyatt, H.W., and Powers, S.K. (2021). Mitochondrial dysfunction is a common denominator linking skeletal muscle wasting due to disease, aging, and prolonged inactivity. Antioxidants, 10.","DOI":"10.3390\/antiox10040588"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"102357","DOI":"10.1016\/j.ceca.2021.102357","article-title":"Skeletal muscle mitochondria in health and disease","volume":"94","author":"Gherardi","year":"2021","journal-title":"Cell Calcium"},{"key":"ref_7","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_8","doi-asserted-by":"crossref","first-page":"1021","DOI":"10.1016\/j.mehy.2015.08.015","article-title":"Revisiting the dystrophin-ATP connection: How half a century of research still implicates mitochondrial dysfunction in Duchenne Muscular Dystrophy aetiology","volume":"85","author":"Timpani","year":"2015","journal-title":"Med. Hypotheses"},{"key":"ref_9","doi-asserted-by":"crossref","unstructured":"Ferri, E., Marzetti, E., Calvani, R., Picca, A., Cesari, M., and Arosio, B. (2020). Role of Age-Related Mitochondrial Dysfunction in Sarcopenia. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21155236"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"1635","DOI":"10.1242\/jeb.01548","article-title":"Exercise-induced maximal metabolic rate scales with muscle aerobic capacity","volume":"208","author":"Weibel","year":"2005","journal-title":"J. Exp. Biol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"296","DOI":"10.3389\/fendo.2017.00296","article-title":"Functional Mitochondria in Health and Disease","volume":"8","author":"Herst","year":"2017","journal-title":"Front. Endocrinol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"2066","DOI":"10.1089\/ars.2018.7534","article-title":"Mitochondrial Morphofunction in Mammalian Cells","volume":"30","author":"Bulthuis","year":"2019","journal-title":"Antioxid. Redox Signal."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1016\/j.cell.2013.08.032","article-title":"Mitochondrial Cristae Shape Determines Respiratory Chain Supercomplexes Assembly and Respiratory Efficiency","volume":"155","author":"Cogliati","year":"2013","journal-title":"Cell"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1016\/0002-8703(75)90467-6","article-title":"Idiopathic cardiomyopathy and skeletal muscle abnormality","volume":"90","author":"Isaacs","year":"1975","journal-title":"Am. Heart J."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"566","DOI":"10.7326\/0003-4819-85-5-566","article-title":"Voluntary Muscle Involvement in Hypertrophic Cardiomyopathy","volume":"85","author":"Smith","year":"1976","journal-title":"Ann. Intern. Med."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1464","DOI":"10.1016\/0735-1097(89)90383-5","article-title":"Type 1 fiber abnormalities in skeletal muscle of patients with hypertrophic and dilated cardiomyopathy: Evidence of subclinical myogenic myopathy","volume":"14","author":"Caforio","year":"1989","journal-title":"J. Am. Coll. Cardiol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"1856","DOI":"10.1002\/1097-4598(200012)23:12<1856::AID-MUS9>3.0.CO;2-T","article-title":"Electromyographic evidence of subclinical myopathy in hypertrophic cardiomyopathy","volume":"23","author":"Karandreas","year":"2000","journal-title":"Muscle Nerve"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1016\/0022-510X(72)90072-X","article-title":"Skeletal muscle in idiopathic cardiomyopathy","volume":"15","author":"Shafig","year":"1972","journal-title":"J. Neurol. Sci."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"296","DOI":"10.1016\/S0960-8966(98)00028-5","article-title":"Infantile fibre type disproportion, myofibrillar lysis and cardiomyopathy: A disorder in three unrelated Dutch families","volume":"8","author":"Barth","year":"1998","journal-title":"Neuromuscul. Disord."},{"key":"ref_20","first-page":"185","article-title":"Abnormalities of the skeletal muscle in hypertrophic cardiomyopathy. Spectroscopy using phosphorus-31 nuclear magnetic resonance","volume":"84","author":"Duboc","year":"1991","journal-title":"Arch. Mal. Coeur Vaiss."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1136\/hrt.78.2.177","article-title":"Abnormal skeletal muscle bioenergetics in familial hypertrophic cardiomyopathy","volume":"78","author":"Thompson","year":"1997","journal-title":"Heart"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"548","DOI":"10.1136\/hrt.80.6.548","article-title":"Coexistence of mitochondrial DNA and \u03b2 myosin heavy chain mutations in hypertrophic cardiomyopathy with late congestive heart failure","volume":"80","author":"Arbustini","year":"1998","journal-title":"Heart"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1007\/BF00666223","article-title":"Mitochondrial cardiomyopathy with involvement of skeletal muscles","volume":"399","author":"Grantzow","year":"1982","journal-title":"Virchows Arch."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"3993","DOI":"10.1073\/pnas.90.9.3993","article-title":"Missense mutations in the \u03b2-myosin heavy-chain gene cause central core disease in hypertrophic cardiomyopathy","volume":"90","author":"Fananapazir","year":"1993","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.1002\/cphy.c140048","article-title":"The dystrophin complex: Structure, function, and implications for therapy","volume":"5","author":"Gao","year":"2015","journal-title":"Compr. Physiol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"3710","DOI":"10.1073\/pnas.90.8.3710","article-title":"Dystrophin protects the sarcolemma from stresses developed during muscle contraction","volume":"90","author":"Petrof","year":"1993","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1575","DOI":"10.1002\/mus.1192","article-title":"The dystrophin-glycoprotein complex, cellular signaling, and the regulation of cell survival in the muscular dystrophies","volume":"24","author":"Rando","year":"2001","journal-title":"Muscle Nerve"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1161\/01.RES.0000126574.61061.25","article-title":"The Dystrophin Glycoprotein Complex: Signaling Strength and Integrity for the Sarcolemma","volume":"94","author":"Lapidos","year":"2004","journal-title":"Circ. Res."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"762","DOI":"10.1038\/nrm2024","article-title":"Molecular mechanisms of muscular dystrophies: Old and new players","volume":"7","author":"Davies","year":"2006","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1152\/physrev.00007.2015","article-title":"Absence of dystrophin disrupts skeletal muscle signaling: Roles of Ca2+, reactive oxygen species, and nitric oxide in the development of muscular dystrophy","volume":"96","author":"Allen","year":"2015","journal-title":"Physiol. Rev."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1016\/0002-9343(82)90184-X","article-title":"Cardiac function in Duchenne\u2019s muscular dystrophy. Results of 10-year follow-up study and noninvasive tests","volume":"73","author":"Hunsaker","year":"1982","journal-title":"Am. J. Med."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1161\/CIRCIMAGING.110.960740","article-title":"Cardiac involvement in patients with muscular dystrophies magnetic resonance imaging phenotype and genotypic considerations","volume":"4","author":"Verhaert","year":"2011","journal-title":"Circ. Cardiovasc. Imaging"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1189","DOI":"10.1073\/pnas.81.4.1189","article-title":"X chromosome-linked muscular dystrophy (mdx) in the mouse","volume":"81","author":"Bulfield","year":"1984","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"250","DOI":"10.1055\/s-2008-1062269","article-title":"Inherited Myopathies and Muscular Dystrophies","volume":"28","author":"Cardamone","year":"2008","journal-title":"Semin. Neurol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1146\/annurev.pathol.2.010506.091936","article-title":"Muscle Diseases: The Muscular Dystrophies","volume":"2","author":"McNally","year":"2007","journal-title":"Annu. Rev. Pathol. Mech. Dis."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"2533","DOI":"10.1016\/j.jacc.2016.02.081","article-title":"Dystrophin-Deficient Cardiomyopathy","volume":"67","author":"Kamdar","year":"2016","journal-title":"J. Am. Coll. Cardiol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1007\/BF00745010","article-title":"Experimental production of \u201csepta\u201d and apparent subdivision of muscle mitochondria","volume":"12","author":"Duncan","year":"1980","journal-title":"J. Bioenerg. Biomembr."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1212\/WNL.28.5.439","article-title":"Intracellular calcium accumulation in Duchenne dystrophy and other myopathies: A study of 567,000 muscle fibers in 114 biopsies","volume":"28","author":"Bodensteiner","year":"1978","journal-title":"Neurology"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"10909","DOI":"10.1074\/jbc.270.18.10909","article-title":"Calpains are activated in necrotic fibers from mdx dystrophic mice","volume":"270","author":"Spencer","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/0014-4827(92)90045-A","article-title":"Calpain concentration is elevated although net calcium-dependent proteolysis is suppressed in dystrophin-deficient muscle","volume":"203","author":"Spencer","year":"1992","journal-title":"Exp. Cell Res."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"4647","DOI":"10.1074\/jbc.M006337200","article-title":"Alteration in calcium handling at the subcellular level in mdx myotubes","volume":"276","author":"Robert","year":"2001","journal-title":"J Biol. Chem."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"2229","DOI":"10.1016\/j.bbadis.2017.06.009","article-title":"ER stress disturbs SR\/ER-mitochondria Ca2+ transfer: Implications in Duchenne muscular dystrophy","volume":"1863","author":"Pauly","year":"2017","journal-title":"Biochim. Biophys. Acta Mol. Basis Dis."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1002\/mus.25199","article-title":"P2Y2 purinergic receptors are highly expressed in cardiac and diaphragm muscles of mdx mice, and their expression is decreased by suramin","volume":"55","author":"Neto","year":"2017","journal-title":"Muscle Nerve"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"670","DOI":"10.1038\/344670a0","article-title":"Calcium entry through stretch-inactivated ion channels in mdx myotubes","volume":"344","author":"Franco","year":"1990","journal-title":"Nature"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1113\/jphysiol.1994.sp020440","article-title":"Mechanosensitive ion channels in skeletal muscle from normal and dystrophic mice","volume":"481","author":"Lansman","year":"1994","journal-title":"J. Physiol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"19023","DOI":"10.1073\/pnas.0906591106","article-title":"Calcium influx is sufficient to induce muscular dystrophy through a TRPC-dependent mechanism","volume":"106","author":"Millay","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1038\/nm.1916","article-title":"Hypernitrosylated ryanodine receptor calcium release channels are leaky in dystrophic muscle","volume":"15","author":"Bellinger","year":"2009","journal-title":"Nat. Med."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"2198","DOI":"10.1073\/pnas.0711074105","article-title":"Remodeling of ryanodine receptor complex causes \u201cleaky\u201d channels: A molecular mechanism for decreased exercise capacity","volume":"105","author":"Bellinger","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1038\/cdd.2016.127","article-title":"Mitochondria mediate cell membrane repair and contribute to Duchenne muscular dystrophy","volume":"24","author":"Vila","year":"2017","journal-title":"Cell Death Differ."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"165674","DOI":"10.1016\/j.bbadis.2020.165674","article-title":"Duchenne muscular dystrophy is associated with the inhibition of calcium uniport in mitochondria and an increased sensitivity of the organelles to the calcium-induced permeability transition","volume":"1866","author":"Dubinin","year":"2020","journal-title":"Biochim. Biophys. Acta Mol. Basis Dis."},{"key":"ref_51","doi-asserted-by":"crossref","unstructured":"Dubinin, M.V., Talanov, E.Y., Tenkov, K.S., Starinets, V.S., Belosludtseva, N.V., and Belosludtsev, K.N. (2020). The Effect of Deflazacort Treatment on the Functioning of Skeletal Muscle Mitochondria in Duchenne Muscular Dystrophy. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21228763"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"148250","DOI":"10.1016\/j.bbabio.2020.148250","article-title":"Transport of Ca2+ and Ca2+-dependent permeability transition in heart mitochondria in the early stages of Duchenne muscular dystrophy","volume":"1861","author":"Dubinin","year":"2020","journal-title":"Biochim. Biophys. Acta Bioenerg."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1016\/j.bbrc.2009.06.053","article-title":"Mutation in dystrophin-encoding gene affects energy metabolism in mouse myoblasts","volume":"386","author":"Onopiuk","year":"2009","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1002\/jcsm.12405","article-title":"Early myopathy in Duchenne muscular dystrophy is associated with elevated mitochondrial H2O2 emission during impaired oxidative phosphorylation","volume":"10","author":"Hughes","year":"2019","journal-title":"J. Cachexia Sarcopenia Muscle"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1016\/S0140-6736(76)92781-1","article-title":"Mitochondrial calcium overload: A general mechanism for cell-necrosis in muscle diseases","volume":"307","author":"Wrogemann","year":"1976","journal-title":"Lancet"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1016\/j.phrs.2016.09.043","article-title":"Forty years later: Mitochondria as therapeutic targets in muscle diseases","volume":"113","author":"Zulian","year":"2016","journal-title":"Pharmacol. Res."},{"key":"ref_57","doi-asserted-by":"crossref","unstructured":"Heydemann, A. (2018). Skeletal muscle metabolism in duchenne and becker muscular dystrophy\u2014Implications for therapies. Nutrients, 10.","DOI":"10.3390\/nu10060796"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1016\/0306-9877(94)90112-0","article-title":"\u201cOil globules\u201d in Duchenne muscular dystrophy-History, demonstration, and metabolic significance","volume":"43","author":"Bonsett","year":"1994","journal-title":"Med. Hypotheses"},{"key":"ref_59","first-page":"5487","article-title":"Peroxisome proliferator-activated receptor \u03b3 coactivator 1-\u03b1 gene transfer restores mitochondrial biomass and improves mitochondrial calcium handling in post-necrotic mdx mouse skeletal muscle","volume":"590","author":"Godin","year":"2012","journal-title":"Authors. J. Physiol. C"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1186\/2044-5040-2-16","article-title":"Metabolic remodeling agents show beneficial effects in the dystrophin-deficient mdx mouse model","volume":"2","author":"Jahnke","year":"2012","journal-title":"Skelet. Muscle"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1093\/hmg\/dds415","article-title":"Defects in mitochondrial localization and ATP synthesis in the mdx mouse model of Duchenne muscular dystrophy are not alleviated by PDE5 inhibition","volume":"22","author":"Percival","year":"2013","journal-title":"Hum. Mol. Gen."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1007\/BF00688245","article-title":"Ultrastructure of the skeletal muscle in the X chromosome-linked dystrophic (mdx) mouse-Comparison with Duchenne muscular dystrophy","volume":"77","author":"Cullen","year":"1988","journal-title":"Acta Neuropathol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1016\/j.ajpath.2012.04.004","article-title":"AMPK activation stimulates autophagy and ameliorates muscular dystrophy in the mdx mouse diaphragm","volume":"181","author":"Pauly","year":"2012","journal-title":"Am. J. Pathol."},{"key":"ref_64","doi-asserted-by":"crossref","unstructured":"Rybalka, E., Timpani, C.A., Cooke, M.B., Williams, A.D., and Hayes, A. (2014). Defects in mitochondrial ATP synthesis in dystrophin-deficient Mdx skeletal muscles may be caused by complex I insufficiency. PLoS ONE.","DOI":"10.1371\/journal.pone.0115763"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"690","DOI":"10.3389\/fphys.2020.00690","article-title":"Mitochondrial Dysfunction Is an Early Consequence of Partial or Complete Dystrophin Loss in mdx Mice","volume":"11","author":"Moore","year":"2020","journal-title":"Front. Physiol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"649","DOI":"10.1042\/bj3040649","article-title":"Defective regulation of energy metabolism in mdx-mouse skeletal muscles","volume":"304","author":"Even","year":"1994","journal-title":"Biochem. J."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1016\/0014-5793(95)01225-4","article-title":"Down-regulation of mitochondrial mRNAs in the mdx mouse model for Duchenne muscular dystrophy","volume":"375","author":"Chambon","year":"1995","journal-title":"FEBS Lett."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1023\/A:1006868130002","article-title":"Impaired mitochondrial oxidative phosphorylation in skeletal muscle of the dystrophin-deficient mdx mouse","volume":"183","author":"Kuznetsov","year":"1998","journal-title":"Mol. Cell. Biochem."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"1321","DOI":"10.1083\/jcb.151.6.1321","article-title":"Expression profiling in the muscular dystrophies: Identification of novel aspects of molecular pathophysiology","volume":"151","author":"Chen","year":"2000","journal-title":"J. Cell Biol."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/S0960-8966(01)00278-4","article-title":"A quantitative study of bioenergetics in skeletal muscle lacking utrophin and dystrophin","volume":"12","author":"Cole","year":"2002","journal-title":"Neuromuscul. Disord."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"1986","DOI":"10.1038\/s41598-019-38609-4","article-title":"Reduced mitochondrial respiration and increased calcium deposits in the EDL muscle, but not in soleus, from 12-week-old dystrophic mdx mice","volume":"9","author":"Gaglianone","year":"2019","journal-title":"Sci. Rep."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1016\/S0960-8966(01)00273-5","article-title":"Creatine supplementation reduces skeletal muscle degeneration and enhances mitochondrial function in mdx mice","volume":"12","author":"Passaquin","year":"2002","journal-title":"Neuromuscul. Disord."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1016\/0885-4505(86)90121-0","article-title":"Studies on mitochondria from dystrophic skeletal muscle of mice","volume":"36","author":"Liang","year":"1986","journal-title":"Biochem. Med. Metab. Biol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"712","DOI":"10.1152\/ajpregu.00229.2011","article-title":"Measuring mitochondrial respiration in intact single muscle fibers","volume":"302","author":"Schuh","year":"2012","journal-title":"Am. J. Physiol. Regul. Integr. Comp. Physiol."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"361ra139","DOI":"10.1126\/scitranslmed.aaf5504","article-title":"NAD+ repletion improves muscle function in muscular dystrophy and counters global parylation","volume":"8","author":"Ryu","year":"2016","journal-title":"Sci. Transl. Med."},{"key":"ref_76","doi-asserted-by":"crossref","unstructured":"Mohiuddin, M., Choi, J.J., Lee, N.H., Jeong, H., Anderson, S.E., Han, W.M., Aliya, B., Peykova, T.Z., Verma, S., and Garc\u00eda, A.J. (2020). Transplantation of Muscle Stem Cell Mitochondria Rejuvenates the Bioenergetic Function of Dystrophic Muscle. bioRxiv.","DOI":"10.1101\/2020.04.17.017822"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"442","DOI":"10.1038\/nm1736","article-title":"Genetic and pharmacologic inhibition of mitochondrial-dependent necrosis attenuates muscular dystrophy","volume":"14","author":"Millay","year":"2008","journal-title":"Nat. Med."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"574","DOI":"10.1038\/bjp.2008.285","article-title":"Investigation of Debio 025, a cyclophilin inhibitor, in the dystrophic mdx mouse, a model for Duchenne muscular dystrophy","volume":"155","author":"Reutenauer","year":"2008","journal-title":"Br. J. Pharmacol."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"1775","DOI":"10.1016\/j.bbabio.2010.07.002","article-title":"Mitochondrial Ca2+ transport and permeability transition in zebrafish (Danio rerio)","volume":"1797","author":"Azzolin","year":"2010","journal-title":"Biochim. Biophys. Acta Bioenerg."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1016\/j.phrs.2017.09.001","article-title":"Alisporivir rescues defective mitochondrial respiration in Duchenne muscular dystrophy","volume":"125","author":"Schiavone","year":"2017","journal-title":"Pharmacol. Res."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"1655","DOI":"10.1002\/cmdc.201500284","article-title":"Discovery, Synthesis, and Optimization of Diarylisoxazole-3-carboxamides as Potent Inhibitors of the Mitochondrial Permeability Transition Pore","volume":"10","author":"Roy","year":"2015","journal-title":"ChemMedChem"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"1771","DOI":"10.1002\/cmdc.201900376","article-title":"Second-Generation Inhibitors of the Mitochondrial Permeability Transition Pore with Improved Plasma Stability","volume":"14","author":"Devereaux","year":"2019","journal-title":"ChemMedChem"},{"key":"ref_83","doi-asserted-by":"crossref","unstructured":"Stocco, A., Smolina, N., Sabatelli, P., \u0160ileikyt\u0117, J., Artusi, E., Mouly, V., Cohen, M., Forte, M., Schiavone, M., and Bernardi, P. (2021). Treatment with a triazole inhibitor of the mitochondrial permeability transition pore fully corrects the pathology of sapje zebrafish lacking dystrophin. Pharmacol. Res., 165.","DOI":"10.1016\/j.phrs.2021.105421"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.yexcr.2004.08.004","article-title":"Desmin: A major intermediate filament protein essential for the structural integrity and function of muscle","volume":"301","author":"Paulin","year":"2004","journal-title":"Exp. Cell Res."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1007\/s00441-014-2016-4","article-title":"Desmin in muscle and associated diseases: Beyond the structural function","volume":"360","author":"Hnia","year":"2015","journal-title":"Cell Tissue Res."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"983","DOI":"10.1007\/s12551-018-0429-0","article-title":"Molecular insights into cardiomyopathies associated with desmin (DES) mutations","volume":"10","author":"Brodehl","year":"2018","journal-title":"Biophys. Rev."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"1244","DOI":"10.1161\/CIRCULATIONAHA.106.646778","article-title":"Prevalence of desmin mutations in dilated cardiomyopathy","volume":"115","author":"Taylor","year":"2007","journal-title":"Circulation"},{"key":"ref_88","doi-asserted-by":"crossref","unstructured":"Schwarz, N., and Leube, R. (2016). Intermediate Filaments as Organizers of Cellular Space: How They Affect Mitochondrial Structure and Function. Cells, 5.","DOI":"10.3390\/cells5030030"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"1283","DOI":"10.1083\/jcb.150.6.1283","article-title":"Desmin cytoskeleton linked to muscle mitochondrial distribution and respiratory function","volume":"150","author":"Milner","year":"2000","journal-title":"J. Cell Biol."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"1255","DOI":"10.1083\/jcb.134.5.1255","article-title":"Disruption of muscle architecture and myocardial degeneration in mice lacking desmin","volume":"134","author":"Milner","year":"1996","journal-title":"J. Cell Biol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1083\/jcb.139.1.129","article-title":"Desmin is essential for the tensile strength and integrity of myofibrils but not for myogenic commitment, differentiation, and fusion of skeletal muscle","volume":"139","author":"Li","year":"1997","journal-title":"J. Cell Biol."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/S0005-2728(97)00071-6","article-title":"Study of regulation of mitochondrial respiration in vivo. An analysis of influence of ADP diffusion and possible role of cytoskeleton","volume":"1322","author":"Kay","year":"1997","journal-title":"Biochim. Biophys. Acta Bioenerg."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1016\/j.nmd.2005.05.006","article-title":"A novel desmin R355P mutation causes cardiac and skeletal myopathy","volume":"15","author":"Kotowicz","year":"2005","journal-title":"Neuromuscul. Disord."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1016\/j.nmd.2010.01.001","article-title":"Desmin myopathy with severe cardiomyopathy in a Uruguayan family due to a codon deletion in a new location within the desmin 1A rod domain","volume":"20","author":"Vernengo","year":"2010","journal-title":"Neuromuscul. Disord."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1093\/hmg\/ddg060","article-title":"On noxious desmin: Functional effects of a novel heterozygous desmin insertion mutation on the extrasarcomeric desmin cytoskeleton and mitochondria","volume":"12","author":"Goudeau","year":"2003","journal-title":"Hum. Mol. Genet."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"199","DOI":"10.3389\/fgene.2015.00199","article-title":"Desmin common mutation is associated with multi-systemic disease manifestations and depletion of mitochondria and mitochondrial DNA","volume":"6","author":"McCormick","year":"2015","journal-title":"Front. Genet."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1007\/s00401-016-1592-7","article-title":"Mutant desmin substantially perturbs mitochondrial morphology, function and maintenance in skeletal muscle tissue","volume":"132","author":"Winter","year":"2016","journal-title":"Acta Neuropathol."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"691","DOI":"10.1016\/j.nmd.2016.08.004","article-title":"Mitochondrial dysfunction in myofibrillar myopathy","volume":"26","author":"Vincent","year":"2016","journal-title":"Neuromuscul. Disord."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"15","DOI":"10.5414\/NP300969","article-title":"Mitochondrial proteomics reveal potential targets involved in mitochondrial abnormalities of desminopathy","volume":"36","author":"Chen","year":"2017","journal-title":"Clin. Neuropathol."},{"key":"ref_100","doi-asserted-by":"crossref","unstructured":"Kub\u00e1nek, M., Schimerov\u00e1, T., Piherov\u00e1, L., Brodehl, A., Krebsov\u00e1, A., Ratnavadivel, S., Stanasiuk, C., Hans\u00edkov\u00e1, H., Zeman, J., and Pale\u010dek, T. (2020). Desminopathy: Novel Desmin Variants, a New Cardiac Phenotype, and Further Evidence for Secondary Mitochondrial Dysfunction. J. Clin. Med., 9.","DOI":"10.3390\/jcm9040937"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1007\/s10974-008-9139-8","article-title":"Mice expressing L345P mutant desmin exhibit morphological and functional changes of skeletal and cardiac mitochondria","volume":"29","author":"Kostareva","year":"2008","journal-title":"J. Muscle Res. Cell Motil."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"165745","DOI":"10.1016\/j.bbadis.2020.165745","article-title":"Desmin mutations result in mitochondrial dysfunction regardless of their aggregation properties","volume":"1866","author":"Smolina","year":"2020","journal-title":"Biochim. Biophys. Acta Mol. Basis Dis."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1016\/j.ceca.2014.08.001","article-title":"Aggregate-prone desmin mutations impair mitochondrial calcium uptake in primary myotubes","volume":"56","author":"Smolina","year":"2014","journal-title":"Cell Calcium"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"656","DOI":"10.1016\/j.nmd.2008.06.367","article-title":"Electron microscopy in myofibrillar myopathies reveals clues to the mutated gene","volume":"18","author":"Claeys","year":"2008","journal-title":"Neuromuscul. Disord."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1186\/gb-2011-12-5-222","article-title":"The lamin protein family","volume":"12","author":"Dittmer","year":"2011","journal-title":"Genome Biol."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1080\/19491034.2016.1183848","article-title":"The nuclear lamina in health and disease","volume":"7","author":"Dobrzynska","year":"2016","journal-title":"Nucleus"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"970","DOI":"10.1016\/j.bbadis.2012.01.014","article-title":"Protein profiling reveals energy metabolism and cytoskeletal protein alterations in LMNA mutation carriers","volume":"1822","author":"Magagnotti","year":"2012","journal-title":"Biochim. Biophys. Acta Mol. Basis Dis."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"1759","DOI":"10.1038\/sj.cdd.4402197","article-title":"Human lipodystrophies linked to mutations in A-type lamins and to HIV protease inhibitor therapy are both associated with prelamin A accumulation, oxidative stress and premature cellular senescence","volume":"14","author":"Caron","year":"2007","journal-title":"Cell Death Differ."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1080\/19491034.2015.1050568","article-title":"Sustained accumulation of prelamin A and depletion of lamin A\/C both cause oxidative stress and mitochondrial dysfunction but induce different cell fates","volume":"6","author":"Sieprath","year":"2015","journal-title":"Nucleus"},{"key":"ref_110","doi-asserted-by":"crossref","unstructured":"Maggi, L., Carboni, N., and Bernasconi, P. (2016). Skeletal Muscle Laminopathies: A Review of Clinical and Molecular Features. Cells, 5.","DOI":"10.3390\/cells5030033"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"1634","DOI":"10.1210\/jc.2009-1293","article-title":"LMNA mutations, skeletal muscle lipid metabolism, and insulin resistance","volume":"95","author":"Boschmann","year":"2010","journal-title":"J. Clin. Endocrinol. Metab."},{"key":"ref_112","doi-asserted-by":"crossref","unstructured":"Ignatieva, E.V., Ivanova, O.A., Komarova, M.Y., Khromova, N.V., Polev, D.E., Kostareva, A.A., Sergushichev, A., and Dmitrieva, R.I. (2020). LMNA Mutations G232E and R482L Cause Dysregulation of Skeletal Muscle Differentiation, Bioenergetics, and Metabolic Gene Expression Profile. Genes, 11.","DOI":"10.3390\/genes11091057"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"594","DOI":"10.1016\/j.bbadis.2014.05.019","article-title":"Myotonic dystrophies: An update on clinical aspects, genetic, pathology, and molecular pathomechanisms","volume":"1852","author":"Meola","year":"2015","journal-title":"Biochim. Biophys. Acta Mol. Basis Dis."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"368","DOI":"10.3389\/fneur.2018.00368","article-title":"Abnormalities in skeletal muscle myogenesis, growth, and regeneration in myotonic dystrophy","volume":"9","author":"Ausems","year":"2018","journal-title":"Front. Neurol."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"2167","DOI":"10.1093\/hmg\/9.14.2167","article-title":"Characterization of a monoclonal antibody panel shows that the myotonic dystrophy protein kinase, DMPK, is expressed almost exclusively in muscle and heart","volume":"9","author":"Lam","year":"2000","journal-title":"Hum. Mol. Genet."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1016\/j.bbadis.2006.05.013","article-title":"Myotonic dystrophy: Emerging mechanisms for DM1 and DM2","volume":"1772","author":"Cho","year":"2007","journal-title":"Biochim. Biophys. Acta Mol. Basis Dis."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"40296","DOI":"10.1074\/jbc.M111.241455","article-title":"Myotonic dystrophy protein kinase is critical for nuclear envelope integrity","volume":"286","author":"Harmon","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"1402","DOI":"10.1128\/MCB.25.4.1402-1414.2005","article-title":"Divergent Mitochondrial and Endoplasmic Reticulum Association of DMPK Splice Isoforms Depends on Unique Sequence Arrangements in Tail Anchors","volume":"25","author":"Oude","year":"2005","journal-title":"Mol. Cell. Biol."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1038\/ng0796-325","article-title":"Mice lacking the myotonic dystrophy protein kinase develop a late onset progressive myopathy","volume":"13","author":"Reddy","year":"1996","journal-title":"Nat. Genet."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1016\/S0022-510X(98)00290-1","article-title":"Decreased expression of myotonic dystrophy protein kinase and disorganization of sarcoplasmic reticulum in skeletal muscle of myotonic dystrophy","volume":"162","author":"Ueda","year":"1999","journal-title":"J. Neurol. Sci."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/S0022-510X(99)00306-8","article-title":"Detection of DNA fragmentation of myonuclei in myotonic dystrophy by double staining with anti-emerin antibody and by nick end-labeling","volume":"173","author":"Yamada","year":"2000","journal-title":"J. Neurol. Sci."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"1315","DOI":"10.1038\/cdd.2010.33","article-title":"Normal myogenesis and increased apoptosis in myotonic dystrophy type-1 muscle cells","volume":"17","author":"Loro","year":"2010","journal-title":"Cell Death Differ."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"S979","DOI":"10.1007\/s100720070014","article-title":"Potential involvement of ubiquinone in myotonic dystrophy pathophysiology: New diagnostic approaches for new rationale therapeutics","volume":"21","author":"Tedeschi","year":"2000","journal-title":"Neurol. Sci."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1016\/S0361-9230(01)00653-0","article-title":"Coenzyme Q10, exercise lactate and CTG trinucleotide expansion in myotonic dystrophy","volume":"56","author":"Siciliano","year":"2001","journal-title":"Brain Res. Bull."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1016\/j.nmd.2017.10.007","article-title":"Mitochondrial dysfunction in myotonic dystrophy type 1","volume":"28","author":"Gramegna","year":"2018","journal-title":"Neuromuscul. Disord."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"e858","DOI":"10.1038\/cddis.2013.385","article-title":"Myotonic dystrophy protein kinase (DMPK) prevents ROS-induced cell death by assembling a hexokinase II-Src complex on the mitochondrial surface","volume":"4","author":"Pantic","year":"2013","journal-title":"Cell Death Dis."},{"key":"ref_127","doi-asserted-by":"crossref","unstructured":"Ophuis, R.J.A.O., Wijers, M., Bennink, M.B., van de Loo, F.A.J., Fransen, J.A.M., Wieringa, B., and Wansink, D.G. (2009). A tail-anchored myotonic dystrophy protein kinase isoform induces perinuclear clustering of mitochondria, autophagy and apoptosis. PLoS ONE, 4.","DOI":"10.1371\/journal.pone.0008024"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1016\/0022-510X(83)90209-5","article-title":"An X-linked mitochondrial disease affecting cardiac muscle, skeletal muscle and neutrophil leucocytes","volume":"62","author":"Barth","year":"1983","journal-title":"J. Neurol. Sci."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1038\/ng0496-385","article-title":"A novel X-linked gene, G4.5. is responsible for Barth syndrome","volume":"12","author":"Bione","year":"1996","journal-title":"Nat. Genet."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"862","DOI":"10.1086\/514886","article-title":"The x-linked gene G4.5 is responsible for different infantile dilated cardiomyopathies","volume":"61","author":"Gedeon","year":"1997","journal-title":"Am. J. Hum. Genet."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"R462","DOI":"10.1016\/S0960-9822(06)00237-5","article-title":"Barth syndrome may be due to an acyltransferase deficiency","volume":"7","author":"Neuwald","year":"1997","journal-title":"Curr. Biol."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"1156","DOI":"10.1016\/j.bbamem.2017.03.013","article-title":"Cardiolipin and mitochondrial cristae organization","volume":"1859","author":"Ikon","year":"2017","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"43553","DOI":"10.1074\/jbc.C200551200","article-title":"Gluing the respiratory chain together: Cardiolipin is required for super complex formation in the inner mitochondrial membrane","volume":"277","author":"Zhang","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"462","DOI":"10.1016\/j.jmb.2006.06.057","article-title":"Mitochondrial Respiratory Chain Super complexes Are Destabilized in Barth Syndrome Patients","volume":"361","author":"McKenzie","year":"2006","journal-title":"J. Mol. Biol."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1038\/labinvest.3780427","article-title":"Infantile dilated X-linked cardiomyopathy, G4.5 mutations, altered lipids, and ultrastructural malformations of mitochondria in heart, liver, and skeletal muscle","volume":"82","author":"Bissler","year":"2002","journal-title":"Lab. Investig."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1038\/labinvest.3700480","article-title":"Comparison of lymphoblast mitochondria from normal subjects and patients with Barth syndrome using electron microscopic tomography","volume":"87","author":"Acehan","year":"2007","journal-title":"Lab. Investig."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"165744","DOI":"10.1016\/j.bbadis.2020.165744","article-title":"Mitochondrial dysfunction in metabolic and cardiovascular diseases associated with cardiolipin remodeling","volume":"1866","author":"Correa","year":"2020","journal-title":"Biochim. Biophys. Acta Mol. Basis Dis."},{"key":"ref_138","doi-asserted-by":"crossref","unstructured":"Paradies, G., Paradies, V., Ruggiero, F.M., and Petrosillo, G. (2019). Role of Cardiolipin in Mitochondrial Function and Dynamics in Health and Disease: Molecular and Pharmacological Aspects. Cells, 8.","DOI":"10.3390\/cells8070728"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1002\/ajmg.a.20660","article-title":"X-Linked Cardioskeletal Myopathy and Neutropenia (Barth Syndrome): An Update","volume":"126","author":"Barth","year":"2004","journal-title":"Am. J. Med. Genet."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"5202","DOI":"10.1091\/mbc.e05-03-0256","article-title":"Taz1, an outer mitochondrial membrane protein, affects stability and assembly of inner membrane protein complexes: Implications for Barth syndrome","volume":"16","author":"Brandner","year":"2005","journal-title":"Mol. Biol. Cell"},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"1061","DOI":"10.1111\/j.1365-2958.2008.06216.x","article-title":"Loss of tafazzin in yeast leads to increased oxidative stress during respiratory growth","volume":"68","author":"Chen","year":"2008","journal-title":"Mol. Microbiol."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1042\/bj3640317","article-title":"Cardiolipin prevents rate-dependent uncoupling and provides osmotic stability in yeast mitochondria","volume":"364","author":"Koshkin","year":"2002","journal-title":"Biochem. J."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"2916","DOI":"10.1074\/jbc.M116.753574","article-title":"Cardiolipin regulates mitophagy through the protein kinase C pathway","volume":"292","author":"Shen","year":"2017","journal-title":"J. Biol. Chem."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"11584","DOI":"10.1073\/pnas.0603242103","article-title":"A Drosophila model of Barth syndrome","volume":"103","author":"Xu","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1161\/01.RES.0000233378.95325.ce","article-title":"A zebrafish model of human barth syndrome reveals the essential role of tafazzin in cardiac development and function","volume":"99","author":"Khuchua","year":"2006","journal-title":"Circ. Res."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"899","DOI":"10.1074\/jbc.M110.171439","article-title":"Cardiac and skeletal muscle defects in a mouse model of human Barth syndrome","volume":"286","author":"Acehan","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"865","DOI":"10.1089\/hum.2010.199","article-title":"Characterization of a transgenic short hairpin RNA-induced murine model of tafazzin deficiency","volume":"22","author":"Soustek","year":"2011","journal-title":"Hum. Gene Ther."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"1312","DOI":"10.1194\/jlr.M034728","article-title":"Dysfunctional cardiac mitochondrial bioenergetic, lipidomic, and signaling in a murine model of Barth syndrome","volume":"54","author":"Kiebish","year":"2013","journal-title":"J. Lipid Res."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"139","DOI":"10.15252\/emmm.201505644","article-title":"Cardiac-specific succinate dehydrogenase deficiency in Barth syndrome","volume":"8","author":"Dudek","year":"2016","journal-title":"EMBO Mol. Med."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"12485","DOI":"10.1074\/jbc.RA119.011229","article-title":"Tafazzin deficiency impairs CoA-dependent oxidative metabolism in cardiac mitochondria","volume":"295","author":"Le","year":"2020","journal-title":"J. Biol. Chem."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"H2255","DOI":"10.1152\/ajpheart.00873.2020","article-title":"Barth Syndrome-Related Cardiomyopathy is Associated with a Reduction in Myocardial Glucose Oxidation","volume":"320","author":"Greenwell","year":"2021","journal-title":"Am. J. Physiol. Circ. Physiol."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1002\/1873-3468.13973","article-title":"Cardiolipin deficiency in Barth syndrome is not associated with increased superoxide\/H2O2 production in heart and skeletal muscle mitochondria","volume":"595","author":"Goncalves","year":"2021","journal-title":"FEBS Lett."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"16383","DOI":"10.1073\/pnas.2000640117","article-title":"An essential role for cardiolipin in the stability and function of the mitochondrial calcium uniporter","volume":"117","author":"Ghosh","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"1894","DOI":"10.1161\/CIRCULATIONAHA.120.048698","article-title":"Increased Reactive Oxygen Species-Mediated Ca2+\/Calmodulin-Dependent Protein Kinase II Activation Contributes to Calcium Handling Abnormalities and Impaired Contraction in Barth Syndrome","volume":"143","author":"Liu","year":"2021","journal-title":"Circulation"},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"1024","DOI":"10.1161\/CIRCRESAHA.119.315956","article-title":"AAV gene therapy prevents and reverses heart failure in a murine knockout model of barth syndrome","volume":"126","author":"Wang","year":"2020","journal-title":"Circ. Res."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"1767","DOI":"10.1113\/EP088812","article-title":"Mitochondrial dysfunction in skeletal muscle of fukutin-deficient mice is resistant to exercise- and 5-aminoimidazole-4-carboxamide ribonucleotide-induced rescue","volume":"105","author":"Southern","year":"2020","journal-title":"Exp. Physiol."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"3010","DOI":"10.1016\/j.celrep.2016.11.044","article-title":"Reversal of Defective Mitochondrial Biogenesis in Limb-Girdle Muscular Dystrophy 2D by Independent Modulation of Histone and PGC-1\u03b1 Acetylation","volume":"17","author":"Pambianco","year":"2016","journal-title":"Cell Rep."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"45272","DOI":"10.1038\/srep45272","article-title":"Bioenergetic Impairment in Congenital Muscular Dystrophy Type 1A and Leigh Syndrome Muscle Cells","volume":"7","author":"Steinz","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1016\/j.bbrc.2017.02.072","article-title":"The Caveolin-3 P104L mutation of LGMD-1C leads to disordered glucose metabolism in muscle cells","volume":"486","author":"Deng","year":"2017","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1186\/s13395-018-0173-y","article-title":"Biochemical and pathological changes result from mutatedcaveolin-3 in muscle","volume":"8","author":"Weis","year":"2018","journal-title":"Skelet. Muscle"},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"838","DOI":"10.1002\/jcsm.12541","article-title":"Caveolin-3 deficiency associated with the dystrophy P104L mutation impairs skeletal muscle mitochondrial form and function","volume":"11","author":"Shah","year":"2020","journal-title":"J. Cachexia Sarcopenia Muscle"},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"350","DOI":"10.4103\/0377-4929.81636","article-title":"Dysferlinopathy: Spectrum of pathological changes in skeletal muscle tissue","volume":"54","author":"Gayathri","year":"2011","journal-title":"Indian J. Pathol. Microbiol."},{"key":"ref_163","first-page":"499","article-title":"Dysferlinopathy: Mitochondrial abnormalities in human skeletal muscle","volume":"126","author":"Liu","year":"2016","journal-title":"Int. J. Neurosci."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"782","DOI":"10.1016\/j.nmd.2016.08.008","article-title":"Dysferlin mutations and mitochondrial dysfunction","volume":"26","author":"Vincent","year":"2016","journal-title":"Neuromuscul. Disord."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"1377","DOI":"10.1113\/JP277306","article-title":"Impairments in left ventricular mitochondrial bioenergetics precede overt cardiac dysfunction and remodelling in Duchenne muscular dystrophy","volume":"598","author":"Hughes","year":"2020","journal-title":"J. Physiol."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"6632","DOI":"10.1038\/s41598-020-63563-x","article-title":"RNA Sequence Analyses throughout the Course of Mouse Cardiac Laminopathy Identify Differentially Expressed Genes for Cell Cycle Control and Mitochondrial Function","volume":"10","author":"Shao","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1007\/s00401-014-1363-2","article-title":"The toxic effect of R350P mutant desmin in striated muscle of man and mouse","volume":"129","author":"Clemen","year":"2015","journal-title":"Acta Neuropathol."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1016\/j.yjmcc.2004.12.008","article-title":"Alterations in the heart mitochondrial proteome in a desmin null heart failure model","volume":"38","author":"Fountoulakis","year":"2005","journal-title":"J. Mol. Cell Cardiol."},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"436","DOI":"10.1073\/pnas.0908099107","article-title":"NCLX Is an Essential Component of Mitochondrial Na+\/Ca2+ Exchange","volume":"107","author":"Palty","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1016\/j.molcel.2016.10.001","article-title":"A MICU1 Splice Variant Confers High Sensitivity to the Mitochondrial Ca2+ Uptake Machinery of Skeletal Muscle","volume":"64","author":"Vallese","year":"2016","journal-title":"Mol. Cell"},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"3152","DOI":"10.1096\/fj.201801402R","article-title":"Slow-twitch skeletal muscle defects accompany cardiac dysfunction in transgenic mice with a mutation in the myosin regulatory light chain","volume":"33","author":"Kazmierczak","year":"2019","journal-title":"FASEB J."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/22\/14\/7349\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T06:27:47Z","timestamp":1760164067000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/22\/14\/7349"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,7,8]]},"references-count":171,"journal-issue":{"issue":"14","published-online":{"date-parts":[[2021,7]]}},"alternative-id":["ijms22147349"],"URL":"https:\/\/doi.org\/10.3390\/ijms22147349","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,7,8]]}}}