{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,19]],"date-time":"2026-01-19T22:21:54Z","timestamp":1768861314043,"version":"3.49.0"},"reference-count":60,"publisher":"Elsevier BV","issue":"20","license":[{"start":{"date-parts":[[2018,5,1]],"date-time":"2018-05-01T00:00:00Z","timestamp":1525132800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,8,27]],"date-time":"2020-08-27T00:00:00Z","timestamp":1598486400000},"content-version":"vor","delay-in-days":849,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100004411","name":"Heart and Stroke Foundation of Canada (HSF)","doi-asserted-by":"publisher","award":["Grant-in-Aid"],"award-info":[{"award-number":["Grant-in-Aid"]}],"id":[{"id":"10.13039\/100004411","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100002651","name":"Barth Syndrome Foundation (BSF)","doi-asserted-by":"publisher","award":["Operating"],"award-info":[{"award-number":["Operating"]}],"id":[{"id":"10.13039\/100002651","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2018,5]]},"DOI":"10.1074\/jbc.ra117.001024","type":"journal-article","created":{"date-parts":[[2018,3,21]],"date-time":"2018-03-21T16:40:41Z","timestamp":1521650441000},"page":"7564-7577","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":32,"title":["Expression of human monolysocardiolipin acyltransferase-1 improves mitochondrial function in Barth syndrome lymphoblasts"],"prefix":"10.1016","volume":"293","author":[{"given":"Edgard M.","family":"Mejia","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hana","family":"Zegallai","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Eric D.","family":"Bouchard","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Versha","family":"Banerji","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Amir","family":"Ravandi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Grant M.","family":"Hatch","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.RA117.001024_bib1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0304-4157(85)90002-4","article-title":"Lipids of mitochondria","volume":"822","author":"Daum","year":"1985","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/jbc.RA117.001024_bib2","series-title":"Phospholipids","first-page":"215","article-title":"Polyglycerophospholipids: phosphatidylglycerol, diphosphatidylglycerol and bis(monoacylglycero)phosphate","author":"Hostetler","year":"1982"},{"key":"10.1074\/jbc.RA117.001024_bib3","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1139\/o03-074","article-title":"Cell biology of cardiac mitochondrial phospholipids","volume":"82","author":"Hatch","year":"2004","journal-title":"Biochem. Cell Biol"},{"key":"10.1074\/jbc.RA117.001024_bib4","doi-asserted-by":"crossref","first-page":"2133","DOI":"10.1016\/j.cub.2009.10.074","article-title":"Mitochondrial cardiolipin involved in outer-membrane protein biogenesis: implications for Barth syndrome","volume":"19","author":"Gebert","year":"2009","journal-title":"Curr. Biol"},{"key":"10.1074\/jbc.RA117.001024_bib5","doi-asserted-by":"crossref","first-page":"681","DOI":"10.1083\/jcb.200803129","article-title":"Cardiolipin provides an essential activating platform for caspase-8 on mitochondria","volume":"183","author":"Gonzalvez","year":"2008","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.RA117.001024_bib6","doi-asserted-by":"crossref","first-page":"1194","DOI":"10.1016\/j.bbadis.2013.03.005","article-title":"Barth syndrome: cellular compensation of mitochondrial dysfunction and apoptosis inhibition due to changes in cardiolipin remodeling linked to tafazzin (TAZ) gene mutation","volume":"1832","author":"Gonzalvez","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/jbc.RA117.001024_bib7","doi-asserted-by":"crossref","first-page":"754","DOI":"10.1038\/35036395","article-title":"Cardiolipin provides specificity for targeting of tBid to mitochondria","volume":"2","author":"Lutter","year":"2000","journal-title":"Nat. Cell Biol"},{"key":"10.1074\/jbc.RA117.001024_bib8","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1016\/S0092-8674(02)01036-X","article-title":"Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane","volume":"111","author":"Kuwana","year":"2002","journal-title":"Cell"},{"key":"10.1074\/jbc.RA117.001024_bib9","doi-asserted-by":"crossref","first-page":"52873","DOI":"10.1074\/jbc.M308366200","article-title":"Cardiolipin stabilizes respiratory chain supercomplexes","volume":"278","author":"Pfeiffer","year":"2003","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA117.001024_bib10","doi-asserted-by":"crossref","first-page":"43553","DOI":"10.1074\/jbc.C200551200","article-title":"Gluing the respiratory chain together. Cardiolipin is required for supercomplex formation in the inner mitochondrial membrane","volume":"277","author":"Zhang","year":"2002","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA117.001024_bib11","doi-asserted-by":"crossref","first-page":"806","DOI":"10.1016\/j.scr.2013.05.005","article-title":"Cardiolipin deficiency affects respiratory chain function and organization in an induced pluripotent stem cell model of Barth syndrome","volume":"11","author":"Dudek","year":"2013","journal-title":"Stem Cell Res"},{"key":"10.1074\/jbc.RA117.001024_bib12","doi-asserted-by":"crossref","first-page":"98","DOI":"10.2174\/1871529X14666140505123753","article-title":"Cardiolipin metabolism and the role it plays in heart failure and mitochondrial supercomplex formation","volume":"14","author":"Mejia","year":"2014","journal-title":"Cardiovasc. Hematol. Disord. Drug Targets"},{"key":"10.1074\/jbc.RA117.001024_bib13","doi-asserted-by":"crossref","first-page":"5047","DOI":"10.1091\/mbc.e08-05-0486","article-title":"Cardiolipin mediates cross-talk between mitochondria and the vacuole","volume":"19","author":"Chen","year":"2008","journal-title":"Mol. Biol. Cell"},{"key":"10.1074\/jbc.RA117.001024_bib14","doi-asserted-by":"crossref","first-page":"376","DOI":"10.4161\/auto.27191","article-title":"LC3 binds externalized cardiolipin on injured mitochondria to signal mitophagy in neurons: implications for Parkinson disease","volume":"10","author":"Chu","year":"2014","journal-title":"Autophagy"},{"key":"10.1074\/jbc.RA117.001024_bib15","doi-asserted-by":"crossref","first-page":"976","DOI":"10.1021\/bi00895a023","article-title":"On the structure of cardiolipin","volume":"3","author":"Lecocq","year":"1964","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA117.001024_bib16","doi-asserted-by":"crossref","first-page":"C33","DOI":"10.1152\/ajpcell.00243.2006","article-title":"Role of cardiolipin alterations in mitochondrial dysfunction and disease","volume":"292","author":"Chicco","year":"2007","journal-title":"Am. J. Physiol. Cell Physiol"},{"key":"10.1074\/jbc.RA117.001024_bib17","doi-asserted-by":"crossref","first-page":"1607","DOI":"10.1194\/jlr.R700018-JLR200","article-title":"Cardiolipin synthesis for the assembly of bacterial and mitochondrial membranes","volume":"49","author":"Schlame","year":"2008","journal-title":"J. Lipid Res"},{"key":"10.1074\/jbc.RA117.001024_bib18","doi-asserted-by":"crossref","first-page":"39217","DOI":"10.1074\/jbc.M606100200","article-title":"The enzymatic function of tafazzin","volume":"281","author":"Xu","year":"2006","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA117.001024_bib19","doi-asserted-by":"crossref","first-page":"634","DOI":"10.1002\/ana.10176","article-title":"Deficiency of tetralinoleoyl-cardiolipin in Barth syndrome","volume":"51","author":"Schlame","year":"2002","journal-title":"Ann. Neurol"},{"key":"10.1074\/jbc.RA117.001024_bib20","doi-asserted-by":"crossref","first-page":"5499","DOI":"10.1074\/jbc.M116.769182","article-title":"The basis for acyl specificity in the tafazzin reaction","volume":"292","author":"Schlame","year":"2017","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA117.001024_bib21","doi-asserted-by":"crossref","first-page":"15491","DOI":"10.1074\/jbc.M116.718510","article-title":"Mechanism for remodeling of the acyl chain composition of cardiolipin catalyzed by Saccharomyces cerevisiae tafazzin","volume":"291","author":"Abe","year":"2016","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA117.001024_bib22","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":"10.1074\/jbc.RA117.001024_bib23","doi-asserted-by":"crossref","first-page":"738","DOI":"10.1016\/S0022-3476(05)80289-6","article-title":"X-linked dilated cardiomyopathy with neutropenia, growth retardation, and 3-methylglutaconic aciduria","volume":"119","author":"Kelley","year":"1991","journal-title":"J. Pediatr"},{"key":"10.1074\/jbc.RA117.001024_bib24","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1006\/bbrc.2000.3952","article-title":"Defective remodeling of cardiolipin and phosphatidylglycerol in Barth syndrome","volume":"279","author":"Vreken","year":"2000","journal-title":"Biochem. Biophys. Res. Commun"},{"key":"10.1074\/jbc.RA117.001024_bib25","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1016\/j.plipres.2005.12.001","article-title":"Cardiolipin metabolism and Barth syndrome","volume":"45","author":"Hauff","year":"2006","journal-title":"Prog. Lipid Res"},{"key":"10.1074\/jbc.RA117.001024_bib26","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":"10.1074\/jbc.RA117.001024_bib27","doi-asserted-by":"crossref","first-page":"616","DOI":"10.1038\/nm.3545","article-title":"Modeling the mitochondrial cardiomyopathy of Barth syndrome with induced pluripotent stem cell and heart-on-chip technologies","volume":"20","author":"Wang","year":"2014","journal-title":"Nat. Med"},{"key":"10.1074\/jbc.RA117.001024_bib28","doi-asserted-by":"crossref","first-page":"462","DOI":"10.1016\/j.jmb.2006.06.057","article-title":"Mitochondrial respiratory chain supercomplexes are destabilized in Barth syndrome patients","volume":"361","author":"McKenzie","year":"2006","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.RA117.001024_bib29","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":"10.1074\/jbc.RA117.001024_bib30","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1042\/bj2720589","article-title":"Lysocardiolipin formation and reacylation in isolated rat liver mitochondria","volume":"272","author":"Schlame","year":"1990","journal-title":"Biochem. J"},{"key":"10.1074\/jbc.RA117.001024_bib31","doi-asserted-by":"crossref","first-page":"1837","DOI":"10.1016\/S0022-2275(20)34900-2","article-title":"Acylation of monolysocardiolipin in rat heart","volume":"40","author":"Ma","year":"1999","journal-title":"J. Lipid Res"},{"key":"10.1074\/jbc.RA117.001024_bib32","doi-asserted-by":"crossref","first-page":"12716","DOI":"10.1074\/jbc.M210329200","article-title":"Purification and characterization of monolysocardiolipin acyltransferase from pig liver mitochondria","volume":"278","author":"Taylor","year":"2003","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA117.001024_bib33","doi-asserted-by":"crossref","first-page":"30360","DOI":"10.1074\/jbc.M109.048322","article-title":"Identification of the human mitochondrial linoleoyl-coenzyme A monolysocardiolipin acyltransferase (MLCL AT-1)","volume":"284","author":"Taylor","year":"2009","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA117.001024_bib34","doi-asserted-by":"crossref","first-page":"1182","DOI":"10.1194\/jlr.M500056-JLR200","article-title":"Monolysocardiolipins accumulate in Barth syndrome but do not lead to enhanced apoptosis","volume":"46","author":"Valianpour","year":"2005","journal-title":"J. Lipid Res"},{"key":"10.1074\/jbc.RA117.001024_bib35","doi-asserted-by":"crossref","first-page":"2346","DOI":"10.1194\/jlr.D600024-JLR200","article-title":"Monolysocardiolipin in cultured fibroblasts is a sensitive and specific marker for Barth syndrome","volume":"47","author":"van Werkhoven","year":"2006","journal-title":"J. Lipid Res"},{"key":"10.1074\/jbc.RA117.001024_bib36","doi-asserted-by":"crossref","first-page":"e48628","DOI":"10.1371\/journal.pone.0048628","article-title":"Human trifunctional protein \u03b1 links cardiolipin remodeling to \u03b2-oxidation","volume":"7","author":"Taylor","year":"2012","journal-title":"PLoS One"},{"key":"10.1074\/jbc.RA117.001024_bib37","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1139\/O07-156","article-title":"Mitochondrial monolysocardiolipin acyltransferase is elevated in the surviving population of H9c2 cardiac myoblast cells exposed to 2-deoxyglucose-induced apoptosis","volume":"86","author":"Danos","year":"2008","journal-title":"Biochem. Cell Biol"},{"key":"10.1074\/jbc.RA117.001024_bib38","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1007\/BF02532585","article-title":"Turnover of fatty acids in rat liver cardiolipin: comparison with other mitochondrial phospholipids","volume":"11","author":"Landriscina","year":"1976","journal-title":"Lipids"},{"key":"10.1074\/jbc.RA117.001024_bib39","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/j.chemphyslip.2013.10.005","article-title":"The turnover of glycerol and acyl moieties of cardiolipin","volume":"179","author":"Xu","year":"2014","journal-title":"Chem. Phys. Lipids"},{"key":"10.1074\/jbc.RA117.001024_bib40","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. Invest"},{"key":"10.1074\/jbc.RA117.001024_bib41","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1016\/j.bbabio.2009.02.012","article-title":"Role of phospholipids in respiratory cytochrome bc1 complex catalysis and supercomplex formation","volume":"1787","author":"Wenz","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/jbc.RA117.001024_bib42","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":"2014","journal-title":"Chem. Phys. Lipids"},{"key":"10.1074\/jbc.RA117.001024_bib43","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":"10.1074\/jbc.RA117.001024_bib44","doi-asserted-by":"crossref","first-page":"1777","DOI":"10.1093\/emboj\/19.8.1777","article-title":"Supercomplexes in the respiratory chains of yeast and mammalian mitochondria","volume":"19","author":"Sch\u00e4gger","year":"2000","journal-title":"EMBO J"},{"key":"10.1074\/jbc.RA117.001024_bib45","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1042\/BJ20110162","article-title":"Assessing mitochondrial dysfunction in cells","volume":"435","author":"Brand","year":"2011","journal-title":"Biochem. J"},{"key":"10.1074\/jbc.RA117.001024_bib46","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1016\/j.bbabio.2009.11.005","article-title":"Regulation of vascular smooth muscle cell bioenergetic function by protein glutathiolation","volume":"1797","author":"Hill","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/jbc.RA117.001024_bib47","doi-asserted-by":"crossref","first-page":"2184","DOI":"10.1016\/j.bpj.2011.03.031","article-title":"Cardiolipin affects the supramolecular organization of ATP synthase in mitochondria","volume":"100","author":"Acehan","year":"2011","journal-title":"Biophys. J"},{"key":"10.1074\/jbc.RA117.001024_bib48","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1007\/s10545-012-9486-x","article-title":"Substrate metabolism during basal and hyperinsulinemic conditions in adolescents and young-adults with Barth syndrome","volume":"36","author":"Cade","year":"2013","journal-title":"J. Inherit. Metab. Dis"},{"key":"10.1074\/jbc.RA117.001024_bib49","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1128\/MCB.06051-11","article-title":"Cells lacking Rieske iron-sulfur protein have a reactive oxygen species-associated decrease in respiratory complexes I and IV","volume":"32","author":"Diaz","year":"2012","journal-title":"Mol. Cell. Biol"},{"key":"10.1074\/jbc.RA117.001024_bib50","doi-asserted-by":"crossref","first-page":"1469","DOI":"10.1089\/ars.2012.4845","article-title":"Mitochondrial respiratory supercomplex association limits production of reactive oxygen species from complex I","volume":"19","author":"Maranzana","year":"2013","journal-title":"Antioxid. Redox Signal"},{"key":"10.1074\/jbc.RA117.001024_bib51","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/S1567-7249(01)00011-3","article-title":"Reactive oxygen species generated by the mitochondrial respiratory chain affect the complex III activity via cardiolipin peroxidation in beef-heart submitochondrial particles","volume":"1","author":"Paradies","year":"2001","journal-title":"Mitochondrion"},{"key":"10.1074\/jbc.RA117.001024_bib52","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1016\/S0378-1119(01)00814-9","article-title":"Reactive oxygen species affect mitochondrial electron transport complex I activity through oxidative cardiolipin damage","volume":"286","author":"Paradies","year":"2002","journal-title":"Gene"},{"key":"10.1074\/jbc.RA117.001024_bib53","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1016\/j.freeradbiomed.2004.10.016","article-title":"Mitochondrial H+ leak and ROS generation: an odd couple","volume":"38","author":"Brookes","year":"2005","journal-title":"Free Radic. Biol. Med"},{"key":"10.1074\/jbc.RA117.001024_bib54","doi-asserted-by":"crossref","first-page":"4338","DOI":"10.1002\/pmic.200500081","article-title":"Advantages and limitations of clear-native PAGE","volume":"5","author":"Wittig","year":"2005","journal-title":"Proteomics"},{"key":"10.1074\/jbc.RA117.001024_bib55","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1006\/meth.2001.1262","article-title":"Analysis of relative gene expression data using real-time quantitative PCR and the 2\u2212\u0394\u0394C(T) method","volume":"25","author":"Livak","year":"2001","journal-title":"Methods"},{"key":"10.1074\/jbc.RA117.001024_bib56","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Anal. Biochem"},{"key":"10.1074\/jbc.RA117.001024_bib57","doi-asserted-by":"crossref","first-page":"25810","DOI":"10.1074\/jbc.271.42.25810","article-title":"Regulation of cardiolipin biosynthesis in H9c2 cardiac myoblasts by cytidine 5\u2032-triphosphate","volume":"271","author":"Hatch","year":"1996","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA117.001024_bib58","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1007\/BF02668129","article-title":"Quantitative analysis of phospholipids by thin-layer chromatography and phosphorus analysis of spots","volume":"1","author":"Rouser","year":"1966","journal-title":"Lipids"},{"key":"10.1074\/jbc.RA117.001024_bib59","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1007\/s11010-017-3104-z","article-title":"\u03b1 linolenic acid decreases apoptosis and oxidized phospholipids in cardiomyocytes during ischemia\/reperfusion","volume":"437","author":"Ganguly","year":"2018","journal-title":"Mol. Cell. Biochem"},{"key":"10.1074\/jbc.RA117.001024_bib60","doi-asserted-by":"crossref","first-page":"2295","DOI":"10.1038\/nprot.2007.327","article-title":"Simultaneous detection of apoptosis and mitochondrial superoxide production in live cells by flow cytometry and confocal microscopy","volume":"2","author":"Mukhopadhyay","year":"2007","journal-title":"Nat. Protoc"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S002192582036957X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S002192582036957X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.RA117.001024","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,1,4]],"date-time":"2022-01-04T08:25:45Z","timestamp":1641284745000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S002192582036957X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,5]]},"references-count":60,"journal-issue":{"issue":"20","published-print":{"date-parts":[[2018,5]]}},"alternative-id":["S002192582036957X"],"URL":"https:\/\/doi.org\/10.1074\/jbc.ra117.001024","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2018,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Expression of human monolysocardiolipin acyltransferase-1 improves mitochondrial function in Barth syndrome lymphoblasts","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.RA117.001024","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2018 by The American Society for Biochemistry and Molecular Biology, Inc.","name":"copyright","label":"Copyright"}]}}