{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,19]],"date-time":"2026-10-19T01:34:08Z","timestamp":1792373648407,"version":"4.4.0"},"reference-count":58,"publisher":"Elsevier BV","issue":"5","license":[{"start":{"date-parts":[[2020,5,1]],"date-time":"2020-05-01T00:00:00Z","timestamp":1588291200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,5,1]],"date-time":"2020-05-01T00:00:00Z","timestamp":1588291200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2021,5,1]],"date-time":"2021-05-01T00:00:00Z","timestamp":1619827200000},"content-version":"vor","delay-in-days":365,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100003593","name":"Conselho Nacional de Desenvolvimento Cient\u00edfico e Tecnol\u00f3gico","doi-asserted-by":"publisher","award":["425914\/2016-0"],"award-info":[{"award-number":["425914\/2016-0"]}],"id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004263","name":"Funda\u00e7\u00e3o de Amparo \u00e0 Pesquisa do Estado do Rio Grande do Sul","doi-asserted-by":"publisher","award":["17\/2551-0000\/800-6"],"award-info":[{"award-number":["17\/2551-0000\/800-6"]}],"id":[{"id":"10.13039\/501100004263","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100007395","name":"Instituto Nacional de Ci\u00eancia e Tecnologia para Excitotoxicidade e Neuroprote\u00e7\u00e3o","doi-asserted-by":"publisher","award":["573677\/2008-5"],"award-info":[{"award-number":["573677\/2008-5"]}],"id":[{"id":"10.13039\/501100007395","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001807","name":"Funda\u00e7\u00e3o de Amparo \u00e0 Pesquisa do Estado de S\u00e3o Paulo","doi-asserted-by":"publisher","award":["17\/17728-8"],"award-info":[{"award-number":["17\/17728-8"]}],"id":[{"id":"10.13039\/501100001807","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease"],"published-print":{"date-parts":[[2020,5]]},"DOI":"10.1016\/j.bbadis.2020.165682","type":"journal-article","created":{"date-parts":[[2020,1,10]],"date-time":"2020-01-10T11:51:43Z","timestamp":1578657103000},"page":"165682","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":26,"title":["Disturbance of bioenergetics and calcium homeostasis provoked by metabolites accumulating in propionic acidemia in heart mitochondria of developing rats"],"prefix":"10.1016","volume":"1866","author":[{"given":"Ana Cristina","family":"Roginski","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alessandro","family":"Wajner","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cristiane","family":"Cecatto","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Simone Magagnin","family":"Wajner","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Roger Frig\u00e9rio","family":"Castilho","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Moacir","family":"Wajner","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexandre Umpierrez","family":"Amaral","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbadis.2020.165682_bb0005","series-title":"The Online Metabolic & Molecular Bases of Inherited Disease","article-title":"Disorders of propionate and methylmalonate metabolism","author":"Fenton","year":"2001"},{"key":"10.1016\/j.bbadis.2020.165682_bb0010","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/j.ymgme.2017.10.002","article-title":"Propionyl-CoA carboxylase - a review","volume":"122","author":"Wongkittichote","year":"2017","journal-title":"Mol. Genet. Metab."},{"key":"10.1016\/j.bbadis.2020.165682_bb0015","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1111\/j.1651-2227.1976.tb04417.x","article-title":"A case of methylmalonic and propionic acidemia due to methulmalonyl-CoA carbonylmutase apoenzyme deficiency","volume":"65","author":"van den Berg","year":"1976","journal-title":"Acta Paediatr. Scand."},{"key":"10.1016\/j.bbadis.2020.165682_bb0020","doi-asserted-by":"crossref","first-page":"117","DOI":"10.3109\/00365518109092023","article-title":"Propionyl-CoA carboxylase deficiency: case report, effect of low-protein diet and identification of 3-oxo-2-methylvaleric acid 3-hydroxy-2-methylvaleric acid, and maleic acid in urine","volume":"41","author":"Bergstrom","year":"1981","journal-title":"Scand. J. Clin. Lab. Invest."},{"key":"10.1016\/j.bbadis.2020.165682_bb0025","doi-asserted-by":"crossref","first-page":"2807","DOI":"10.1073\/pnas.69.10.2807","article-title":"3-hydroxypropionate: significance of -oxidation of propionate in patients with propionic acidemia and methylmalonic acidemia","volume":"69","author":"Ando","year":"1972","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbadis.2020.165682_bb0030","doi-asserted-by":"crossref","first-page":"2200","DOI":"10.1016\/S0021-9258(19)45512-9","article-title":"Isolation and identification of methylcitrate, a major metabolic product of propionate in patients with propionic acidemia","volume":"247","author":"Ando","year":"1972","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2020.165682_bb0035","doi-asserted-by":"crossref","first-page":"E413","DOI":"10.1152\/ajpendo.00105.2017","article-title":"Interrelations between 3-hydroxypropionate and propionate metabolism in rat liver: relevance to disorders of propionyl-CoA metabolism","volume":"313","author":"Wilson","year":"2017","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"10.1016\/j.bbadis.2020.165682_bb0040","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1186\/s13023-014-0130-8","article-title":"Proposed guidelines for the diagnosis and management of methylmalonic and propionic acidemia","volume":"9","author":"Baumgartner","year":"2014","journal-title":"Orphanet J. Rare Dis."},{"key":"10.1016\/j.bbadis.2020.165682_bb0045","series-title":"GeneReviews(R), Seattle (WA), 2012- Updated","article-title":"Propionic acidemia","author":"Shchelochkov","year":"2016"},{"key":"10.1016\/j.bbadis.2020.165682_bb0050","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1016\/j.jpeds.2009.07.002","article-title":"Cardiomyopathies in propionic aciduria are reversible after liver transplantation","volume":"156","author":"Romano","year":"2010","journal-title":"J. Pediatr."},{"issue":"Suppl. 1","key":"10.1016\/j.bbadis.2020.165682_bb0055","doi-asserted-by":"crossref","first-page":"S97","DOI":"10.1007\/s10545-009-1084-1","article-title":"Unusual presentation of propionic acidaemia as isolated cardiomyopathy","volume":"32","author":"Lee","year":"2009","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.bbadis.2020.165682_bb0060","doi-asserted-by":"crossref","first-page":"971","DOI":"10.1007\/s00431-014-2359-6","article-title":"Propionic acidemia in a previously healthy adolescent with acute onset of dilated cardiomyopathy","volume":"173","author":"Laemmle","year":"2014","journal-title":"Eur. J. Pediatr."},{"key":"10.1016\/j.bbadis.2020.165682_bb0065","doi-asserted-by":"crossref","first-page":"682","DOI":"10.1097\/MOP.0000000000000422","article-title":"Methylmalonic and propionic acidemias: clinical management update","volume":"28","author":"Fraser","year":"2016","journal-title":"Curr. Opin. Pediatr."},{"key":"10.1016\/j.bbadis.2020.165682_bb0070","doi-asserted-by":"crossref","first-page":"S68","DOI":"10.1007\/BF02138781","article-title":"Propionic acidaemia: clinical, biochemical and therapeutic aspects. Experience in 30 patients","volume":"153","author":"Lehnert","year":"1994","journal-title":"Eur. J. Pediatr."},{"key":"10.1016\/j.bbadis.2020.165682_bb0075","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1038\/sj.ejhg.5200442","article-title":"Potential relationship between genotype and clinical outcome in propionic acidaemia patients","volume":"8","author":"Perez-Cerda","year":"2000","journal-title":"Eur. J. Hum. Genet."},{"key":"10.1016\/j.bbadis.2020.165682_bb0080","doi-asserted-by":"crossref","first-page":"866","DOI":"10.1016\/j.jpeds.2010.12.031","article-title":"Left ventricular assist device as bridge to liver transplantation in a patient with propionic acidemia and cardiogenic shock","volume":"158","author":"Ameloot","year":"2011","journal-title":"J. Pediatr."},{"key":"10.1016\/j.bbadis.2020.165682_bb0085","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1016\/j.mito.2014.07.001","article-title":"Successful reversal of propionic acidaemia associated cardiomyopathy: evidence for low myocardial coenzyme Q10 status and secondary mitochondrial dysfunction as an underlying pathophysiological mechanism","volume":"17","author":"Baruteau","year":"2014","journal-title":"Mitochondrion"},{"key":"10.1016\/j.bbadis.2020.165682_bb0090","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.freeradbiomed.2016.04.007","article-title":"In vivo evidence of mitochondrial dysfunction and altered redox homeostasis in a genetic mouse model of propionic acidemia: implications for the pathophysiology of this disorder","volume":"96","author":"Gallego-Villar","year":"2016","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.bbadis.2020.165682_bb0095","doi-asserted-by":"crossref","first-page":"1447","DOI":"10.1111\/tri.12677","article-title":"Reversal of cardiomyopathy in propionic acidemia after liver transplantation: a 10-year follow-up","volume":"28","author":"Arrizza","year":"2015","journal-title":"Transpl. Int."},{"key":"10.1016\/j.bbadis.2020.165682_bb0100","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/S0014-5793(03)00007-3","article-title":"Mitochondrial ATP-sensitive K+ channel opening decreases reactive oxygen species generation","volume":"536","author":"Ferranti","year":"2003","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbadis.2020.165682_bb0105","doi-asserted-by":"crossref","first-page":"4714","DOI":"10.1111\/febs.13526","volume":"282","author":"Cecatto","year":"2015","journal-title":"FEBS J."},{"key":"10.1016\/j.bbadis.2020.165682_bb0110","doi-asserted-by":"crossref","first-page":"1319","DOI":"10.3390\/biom5031319","article-title":"High-resolution respirometry for simultaneous measurement of oxygen and hydrogen peroxide fluxes in permeabilized cells, tissue homogenate and isolated mitochondria","volume":"5","author":"Makrecka-Kuka","year":"2015","journal-title":"Biomolecules"},{"key":"10.1016\/j.bbadis.2020.165682_bb0115","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/S0021-9258(19)52451-6","article-title":"Protein measurement with the Folin phenol reagent","volume":"193","author":"Lowry","year":"1951","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2020.165682_bb0120","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1016\/j.bbamcr.2014.11.015","article-title":"H9c2 and HL-1 cells demonstrate distinct features of energy metabolism, mitochondrial function and sensitivity to hypoxia-reoxygenation","volume":"1853","author":"Kuznetsov","year":"2015","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbadis.2020.165682_bb0125","doi-asserted-by":"crossref","first-page":"1837","DOI":"10.1016\/j.biocel.2009.03.013","article-title":"Capacity of oxidative phosphorylation in human skeletal muscle: new perspectives of mitochondrial physiology","volume":"41","author":"Gnaiger","year":"2009","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.bbadis.2020.165682_bb0130","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.tiv.2016.06.007","article-title":"Disturbance of mitochondrial functions provoked by the major long-chain 3-hydroxylated fatty acids accumulating in MTP and LCHAD deficiencies in skeletal muscle","volume":"36","author":"Cecatto","year":"2016","journal-title":"Toxicol. in Vitro"},{"key":"10.1016\/j.bbadis.2020.165682_bb0135","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1007\/s10545-007-0798-1","article-title":"Methylmalonate inhibits succinate-supported oxygen consumption by interfering with mitochondrial succinate uptake","volume":"31","author":"Mirandola","year":"2008","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.bbadis.2020.165682_bb0140","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/j.plipres.2005.04.001","article-title":"Coenzyme A: back in action","volume":"44","author":"Leonardi","year":"2005","journal-title":"Prog. Lipid Res."},{"key":"10.1016\/j.bbadis.2020.165682_bb0145","doi-asserted-by":"crossref","first-page":"18426","DOI":"10.1016\/S0021-9258(18)51483-6","article-title":"Dependence of mitochondrial coenzyme A uptake on the membrane electrical gradient","volume":"264","author":"Tahiliani","year":"1989","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2020.165682_bb0150","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/0005-2736(91)90022-Z","article-title":"Evidence for net uptake and efflux of mitochondrial coenzyme A","volume":"1067","author":"Tahiliani","year":"1991","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbadis.2020.165682_bb0155","doi-asserted-by":"crossref","first-page":"1437","DOI":"10.1111\/febs.14419","article-title":"Metabolite accumulation in VLCAD deficiency markedly disrupts mitochondrial bioenergetics and Ca(2+) homeostasis in the heart","volume":"285","author":"Cecatto","year":"2018","journal-title":"FEBS J."},{"key":"10.1016\/j.bbadis.2020.165682_bb0160","doi-asserted-by":"crossref","first-page":"8972","DOI":"10.1523\/JNEUROSCI.20-24-08972.2000","article-title":"Inhibition of Krebs cycle enzymes by hydrogen peroxide: a key role of [alpha]-ketoglutarate dehydrogenase in limiting NADH production under oxidative stress","volume":"20","author":"Tretter","year":"2000","journal-title":"J. Neurosci."},{"key":"10.1016\/j.bbadis.2020.165682_bb0165","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1016\/0076-6879(69)13023-2","article-title":"Intra- and extramitochondrial malate dehydrogenase from chicken and tuna heart","volume":"13","author":"Kitto","year":"1969","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.bbadis.2020.165682_bb0170","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/0076-6879(69)13005-0","article-title":"Citrate synthase","volume":"13","author":"Srere","year":"1969","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.bbadis.2020.165682_bb0175","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1111\/j.1432-1033.1976.tb10625.x","article-title":"Continuous measurement and rapid kinetics of ATP synthesis in rat liver mitochondria, mitoplasts and inner membrane vesicles determined by firefly-luciferase luminescence","volume":"67","author":"Lemasters","year":"1976","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bbadis.2020.165682_bb0180","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/0014-5793(76)80434-6","article-title":"Safranine as a probe of the mitochondrial membrane potential","volume":"68","author":"Akerman","year":"1976","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbadis.2020.165682_bb0185","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1007\/978-1-61779-382-0_7","article-title":"Safranine as a fluorescent probe for the evaluation of mitochondrial membrane potential in isolated organelles and permeabilized cells","volume":"810","author":"Figueira","year":"2012","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.bbadis.2020.165682_bb0190","doi-asserted-by":"crossref","first-page":"1667","DOI":"10.1007\/s11064-010-0228-x","article-title":"Inhibitory effects of adenine nucleotides on brain mitochondrial permeability transition","volume":"35","author":"Saito","year":"2010","journal-title":"Neurochem. Res."},{"key":"10.1016\/j.bbadis.2020.165682_bb0195","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1007\/s10545-013-9600-8","article-title":"Current concepts in organic acidurias: understanding intra- and extracerebral disease manifestation","volume":"36","author":"Kolker","year":"2013","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1016\/j.bbadis.2020.165682_bb0200","doi-asserted-by":"crossref","first-page":"286","DOI":"10.1016\/j.ymgme.2005.04.004","article-title":"Clinical, pathological, and biochemical studies in a patient with propionic acidemia and fatal cardiomyopathy","volume":"85","author":"Mardach","year":"2005","journal-title":"Mol. Genet. Metab."},{"key":"10.1016\/j.bbadis.2020.165682_bb0205","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1203\/PDR.0b013e3181a7c270","article-title":"Multiple OXPHOS deficiency in the liver, kidney, heart, and skeletal muscle of patients with methylmalonic aciduria and propionic aciduria","volume":"66","author":"de Keyzer","year":"2009","journal-title":"Pediatr. Res."},{"key":"10.1016\/j.bbadis.2020.165682_bb0210","doi-asserted-by":"crossref","first-page":"13035","DOI":"10.1016\/S0021-9258(18)43001-3","article-title":"Effects of maleate on the content of CoA and its derivatives in rat kidney mitochondria","volume":"256","author":"Pacanis","year":"1981","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2020.165682_bb0215","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1007\/s11010-019-03534-7","article-title":"Experimental evidence that maleic acid markedly compromises glutamate oxidation through inhibition of glutamate dehydrogenase and alpha-ketoglutarate dehydrogenase activities in kidney of developing rats","volume":"458","author":"Roginski","year":"2019","journal-title":"Mol. Cell. Biochem."},{"key":"10.1016\/j.bbadis.2020.165682_bb0220","doi-asserted-by":"crossref","first-page":"E622","DOI":"10.1152\/ajpendo.00081.2018","article-title":"Propionate-induced changes in cardiac metabolism, notably CoA trapping, are not altered by l-carnitine","volume":"315","author":"Wang","year":"2018","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"10.1016\/j.bbadis.2020.165682_bb0225","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1016\/j.arcmed.2012.06.010","article-title":"Calcium-induced cardiac mitochondrial dysfunction is predominantly mediated by cyclosporine A-dependent mitochondrial permeability transition pore","volume":"43","author":"Yarana","year":"2012","journal-title":"Arch. Med. Res."},{"key":"10.1016\/j.bbadis.2020.165682_bb0230","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1016\/j.ceca.2011.04.007","article-title":"Mitochondrial permeability transition in Ca(2+)-dependent apoptosis and necrosis","volume":"50","author":"Rasola","year":"2011","journal-title":"Cell Calcium"},{"key":"10.1016\/j.bbadis.2020.165682_bb0235","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.freeradbiomed.2018.08.034","article-title":"Mitochondrial calcium transport and the redox nature of the calcium-induced membrane permeability transition","volume":"129","author":"Vercesi","year":"2018","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.bbadis.2020.165682_bb0240","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1039\/C7TX00234C","article-title":"Mitochondrial toxicity of organic arsenicals: membrane permeability transition pore opening and respiratory dysfunction","volume":"7","author":"Fan","year":"2018","journal-title":"Toxicol. Res. (Camb)"},{"key":"10.1016\/j.bbadis.2020.165682_bb0245","doi-asserted-by":"crossref","first-page":"1025","DOI":"10.1111\/j.1471-4159.2004.02565.x","article-title":"Mitochondrial permeability transition in neuronal damage promoted by Ca2+ and respiratory chain complex II inhibition","volume":"90","author":"Maciel","year":"2004","journal-title":"J. Neurochem."},{"key":"10.1016\/j.bbadis.2020.165682_bb0250","doi-asserted-by":"crossref","first-page":"6746","DOI":"10.1074\/jbc.271.12.6746","article-title":"Modulation of the mitochondrial permeability transition pore by pyridine nucleotides and dithiol oxidation at two separate sites","volume":"271","author":"Costantini","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2020.165682_bb0255","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/0003-9861(87)90021-X","article-title":"The participation of NADP, the transmembrane potential and the energy-linked NAD(P) transhydrogenase in the process of Ca2+ efflux from rat liver mitochondria","volume":"252","author":"Vercesi","year":"1987","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.bbadis.2020.165682_bb0260","doi-asserted-by":"crossref","first-page":"12986","DOI":"10.1073\/pnas.1210718109","article-title":"Mitochondrial Ca2+ uptake contributes to buffering cytoplasmic Ca2+ peaks in cardiomyocytes","volume":"109","author":"Drago","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbadis.2020.165682_bb0265","doi-asserted-by":"crossref","first-page":"581","DOI":"10.1152\/physrev.00024.2007","article-title":"Mechanisms underlying acute protection from cardiac ischemia-reperfusion injury","volume":"88","author":"Murphy","year":"2008","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.bbadis.2020.165682_bb0270","doi-asserted-by":"crossref","first-page":"690","DOI":"10.1161\/CIRCRESAHA.113.301651","article-title":"Mechanisms of altered Ca(2)(+) handling in heart failure","volume":"113","author":"Luo","year":"2013","journal-title":"Circ. Res."},{"key":"10.1016\/j.bbadis.2020.165682_bb0275","doi-asserted-by":"crossref","first-page":"2443","DOI":"10.1111\/j.1582-4934.2010.01235.x","article-title":"Mitochondrial cyclophilin-D as a potential therapeutic target for post-myocardial infarction heart failure","volume":"15","author":"Lim","year":"2011","journal-title":"J. Cell. Mol. Med."},{"key":"10.1016\/j.bbadis.2020.165682_bb0280","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0128770","article-title":"Maleic acid\u2014but not structurally related methylmalonic acid\u2014interrupts energy metabolism by impaired calcium homeostasis","volume":"10","author":"Tuncel","year":"2015","journal-title":"PLoS One"},{"key":"10.1016\/j.bbadis.2020.165682_bb0285","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1203\/00006450-196811000-00010","article-title":"Propionicacidemia, a new inborn error of metabolism","volume":"2","author":"Hommes","year":"1968","journal-title":"Pediatr. Res."},{"key":"10.1016\/j.bbadis.2020.165682_bb0290","doi-asserted-by":"crossref","first-page":"1140","DOI":"10.1016\/S0140-6736(70)91216-X","article-title":"Localisation of enzymic defect in propionicacidaemia","volume":"1","author":"Gompertz","year":"1970","journal-title":"Lancet"}],"container-title":["Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0925443920300211?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0925443920300211?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,14]],"date-time":"2025-10-14T04:52:35Z","timestamp":1760417555000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0925443920300211"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,5]]},"references-count":58,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2020,5]]}},"alternative-id":["S0925443920300211"],"URL":"https:\/\/doi.org\/10.1016\/j.bbadis.2020.165682","relation":{},"ISSN":["0925-4439"],"issn-type":[{"value":"0925-4439","type":"print"}],"subject":[],"published":{"date-parts":[[2020,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Disturbance of bioenergetics and calcium homeostasis provoked by metabolites accumulating in propionic acidemia in heart mitochondria of developing rats","name":"articletitle","label":"Article Title"},{"value":"Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbadis.2020.165682","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"165682"}}