{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,20]],"date-time":"2026-10-20T13:07:24Z","timestamp":1792501644577,"version":"4.5.0"},"reference-count":144,"publisher":"MDPI AG","issue":"4","license":[{"start":{"date-parts":[[2021,3,31]],"date-time":"2021-03-31T00:00:00Z","timestamp":1617148800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100007069","name":"Universit\u00e0 della Calabria","doi-asserted-by":"publisher","award":["Fondi di Ateneo 2019"],"award-info":[{"award-number":["Fondi di Ateneo 2019"]}],"id":[{"id":"10.13039\/501100007069","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biomolecules"],"abstract":"<jats:p>The SLC25A20 transporter, also known as carnitine acyl-carnitine carrier (CAC), catalyzes the transport of short, medium and long carbon chain acyl-carnitines across the mitochondrial inner membrane in exchange for carnitine. The 30-year story of the protein responsible for this function started with its purification from rat liver mitochondria. Even though its 3D structure is not yet available, CAC is one of the most deeply characterized transport proteins of the inner mitochondrial membrane. Other than functional, kinetic and mechanistic data, post-translational modifications regulating the transport activity of CAC have been revealed. CAC interactions with drugs or xenobiotics relevant to human health and toxicology and the response of the carrier function to dietary compounds have been discovered. Exploiting combined approaches of site-directed mutagenesis with chemical targeting and bioinformatics, a large set of data on structure\/function relationships have been obtained, giving novel information on the molecular mechanism of the transport catalyzed by this protein.<\/jats:p>","DOI":"10.3390\/biom11040521","type":"journal-article","created":{"date-parts":[[2021,3,31]],"date-time":"2021-03-31T05:57:18Z","timestamp":1617170238000},"page":"521","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":63,"title":["The Mitochondrial Carnitine Acyl-carnitine Carrier (SLC25A20): Molecular Mechanisms of Transport, Role in Redox Sensing and Interaction with Drugs"],"prefix":"10.3390","volume":"11","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-7635-521X","authenticated-orcid":false,"given":"Annamaria","family":"Tonazzi","sequence":"first","affiliation":[{"name":"Institute of Biomembranes, Bioenergetics and Molecular Biotechnologies (IBIOM), National Research Council, Via Orabona 4, 70126 Bari, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7151-0708","authenticated-orcid":false,"given":"Nicola","family":"Giangregorio","sequence":"additional","affiliation":[{"name":"Institute of Biomembranes, Bioenergetics and Molecular Biotechnologies (IBIOM), National Research Council, Via Orabona 4, 70126 Bari, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0238-0946","authenticated-orcid":false,"given":"Lara","family":"Console","sequence":"additional","affiliation":[{"name":"Unit of Biochemistry and Molecular Biotechnology, Department DiBEST (Biologia, Ecologia, Scienze della Terra), University of Calabria, Via P. Bucci 4C, 87036 Arcavacata di Rende, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ferdinando","family":"Palmieri","sequence":"additional","affiliation":[{"name":"Institute of Biomembranes, Bioenergetics and Molecular Biotechnologies (IBIOM), National Research Council, Via Orabona 4, 70126 Bari, Italy"},{"name":"Department of Biosciences, Biotechnologies and Biopharmaceutics, University of Bari, 70125 Bari, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9818-6621","authenticated-orcid":false,"given":"Cesare","family":"Indiveri","sequence":"additional","affiliation":[{"name":"Institute of Biomembranes, Bioenergetics and Molecular Biotechnologies (IBIOM), National Research Council, Via Orabona 4, 70126 Bari, Italy"},{"name":"Unit of Biochemistry and Molecular Biotechnology, Department DiBEST (Biologia, Ecologia, Scienze della Terra), University of Calabria, Via P. 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Biomolecules, 10.","DOI":"10.3390\/biom10040655"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1042\/BJ20111420","article-title":"The human gene SLC25A17 encodes a peroxisomal transporter of coenzyme A, FAD and NAD+","volume":"443","author":"Agrimi","year":"2012","journal-title":"Biochem. J."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1016\/j.cell.2018.11.025","article-title":"The Molecular Mechanism of Transport by the Mitochondrial ADP\/ATP Carrier","volume":"176","author":"Ruprecht","year":"2019","journal-title":"Cell"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"E426","DOI":"10.1073\/pnas.1320692111","article-title":"Structures of yeast mitochondrial ADP\/ATP carriers support a domain-based alternating-access transport mechanism","volume":"111","author":"Ruprecht","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_7","unstructured":"Stanley, C.A., Palmieri, F., and Bennett, M.J. (2013). Disorders of the mitochondrial carnitine shuttle. Online Metab. Mol. Bases Inherit. Dis."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"1185","DOI":"10.1016\/0026-0495(95)90013-6","article-title":"Effects of high-fat diet and fasting on levels of acyl-coenzyme A binding protein in liver, kidney, and heart of rat","volume":"44","author":"Bhuiyan","year":"1995","journal-title":"Metabolism"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1016\/j.mam.2011.10.008","article-title":"The mitochondrial carnitine\/acylcarnitine carrier: Function, structure and physiopathology","volume":"32","author":"Indiveri","year":"2011","journal-title":"Mol. Asp. Med."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1016\/j.plipres.2015.11.004","article-title":"Carnitine palmitoyltransferase 1C: From cognition to cancer","volume":"61","author":"Casals","year":"2016","journal-title":"Prog. Lipid Res."},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"De Pinto, V. (2021). Renaissance of VDAC: New Insights on a Protein Family at the Interface between Mitochondria and Cytosol. Biomolecules, 11.","DOI":"10.3390\/biom11010107"},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"Console, L., Giangregorio, N., Indiveri, C., and Tonazzi, A. (2014). Carnitine\/acylcarnitine translocase and carnitine palmitoyltransferase 2 form a complex in the inner mitochondrial membrane. Mol. Cell Biochem.","DOI":"10.1007\/s11010-014-2098-z"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1369","DOI":"10.3945\/ajcn.2010.29885","article-title":"Specific metabolic rates of major organs and tissues across adulthood: Evaluation by mechanistic model of resting energy expenditure","volume":"92","author":"Wang","year":"2010","journal-title":"Am. J. Clin Nutr"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"794","DOI":"10.3389\/fphys.2020.00794","article-title":"The Link Between the Mitochondrial Fatty Acid Oxidation Derangement and Kidney Injury","volume":"11","author":"Console","year":"2020","journal-title":"Front. Physiol."},{"key":"ref_15","unstructured":"Talley, J.T., and Mohiuddin, S.S. (2020). Biochemistry, Fatty Acid Oxidation, StatPearls."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1016\/j.mam.2004.06.001","article-title":"Carnitine: Transport and physiological functions in the brain","volume":"25","author":"Miecz","year":"2004","journal-title":"Mol. Aspects Med."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"2535","DOI":"10.1007\/s11064-013-1168-z","article-title":"Localization of mitochondrial carnitine\/acylcarnitine translocase in sensory neurons from rat dorsal root Ganglia","volume":"38","author":"Tonazzi","year":"2013","journal-title":"Neurochem. Res."},{"key":"ref_18","first-page":"999","article-title":"Purification of carnitine carrier from rat brain mitochondria","volume":"29","author":"Kaminska","year":"1993","journal-title":"Biochem. Mol. Biol. Int."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1239","DOI":"10.1086\/301628","article-title":"Cloning of the human carnitine-acylcarnitine carrier cDNA and identification of the molecular defect in a patient","volume":"61","author":"Huizing","year":"1997","journal-title":"Am. J. Hum. Genet."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1007\/0-306-46818-2_40","article-title":"Identification of a missense mutation in a patient with lethal carnitine acyl-carnitine carrier deficiency","volume":"466","author":"IJlst","year":"1999","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1002\/ajmg.a.20573","article-title":"Response to therapy in carnitine\/acylcarnitine translocase (CACT) deficiency due to a novel missense mutation","volume":"126A","author":"Iacobazzi","year":"2004","journal-title":"Am. J. Med. Genet. A"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1002\/humu.20085","article-title":"Molecular and functional analysis of SLC25A20 mutations causing carnitine-acylcarnitine translocase deficiency","volume":"24","author":"Iacobazzi","year":"2004","journal-title":"Hum. Mutat."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1006\/mgme.2001.3235","article-title":"Aberrant mRNA splicing associated with coding region mutations in children with carnitine-acylcarnitine translocase deficiency","volume":"74","author":"Hsu","year":"2001","journal-title":"Mol. Genet. Metab."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1023\/A:1005324323401","article-title":"Carnitine-acylcarnitine carrier deficiency: Identification of the molecular defect in a patient","volume":"21","author":"Huizing","year":"1998","journal-title":"J. Inherit. Metab. Dis."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"583850","DOI":"10.3389\/fcell.2020.583850","article-title":"Carnitine Traffic in Cells. Link With Cancer","volume":"8","author":"Console","year":"2020","journal-title":"Front. Cell Dev. Biol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1186\/1750-1172-7-68","article-title":"Systemic primary carnitine deficiency: An overview of clinical manifestations, diagnosis, and management","volume":"7","author":"Magoulas","year":"2012","journal-title":"Orphanet. J. Rare Dis."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1002\/humu.21607","article-title":"Genotype-phenotype correlation in primary carnitine deficiency","volume":"33","author":"Rose","year":"2012","journal-title":"Hum. Mutat."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"3805","DOI":"10.2337\/db13-1677","article-title":"Downregulation of carnitine acyl-carnitine translocase by miRNAs 132 and 212 amplifies glucose-stimulated insulin secretion","volume":"63","author":"Soni","year":"2014","journal-title":"Diabetes"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"a109","DOI":"10.2741\/A745","article-title":"Decreased mitochondrial carnitine translocase in skeletal muscles impairs utilization of fatty acids in insulin-resistant patients","volume":"7","author":"Peluso","year":"2002","journal-title":"Front. Biosci. J. Virtual Libr."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1016\/B978-0-12-800223-0.00008-6","article-title":"Antiporters of the mitochondrial carrier family","volume":"73","author":"Monne","year":"2014","journal-title":"Curr. Top. Membr."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1016\/0005-2736(91)90110-T","article-title":"Characterization of the unidirectional transport of carnitine catalyzed by the reconstituted carnitine carrier from rat liver mitochondria","volume":"1069","author":"Indiveri","year":"1991","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/0005-2736(94)90281-X","article-title":"The reconstituted carnitine carrier from rat liver mitochondria: Evidence for a transport mechanism different from that of the other mitochondrial translocators","volume":"1189","author":"Indiveri","year":"1994","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"472","DOI":"10.1016\/S0014-5793(99)01555-0","article-title":"Identification of the mitochondrial carnitine carrier in Saccharomyces cerevisiae","volume":"462","author":"Palmieri","year":"1999","journal-title":"FEBS Lett."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1080\/09687680701697476","article-title":"Functional characterization of residues within the carnitine\/acylcarnitine translocase RX(2)PANAAXF distinct motif","volume":"25","author":"Indiveri","year":"2008","journal-title":"Mol. Membr. Biol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1111\/j.1574-6968.2001.tb10756.x","article-title":"The Aspergillus nidulans carnitine carrier encoded by the acuH gene is exclusively located in the mitochondria","volume":"201","author":"Martinez","year":"2001","journal-title":"FEMS Microbiol. Lett."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/S1087-1845(03)00049-5","article-title":"Functional analysis of mutations in the human carnitine\/acylcarnitine translocase in Aspergillus nidulans","volume":"39","author":"Perez","year":"2003","journal-title":"Fungal Genet. Biol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"1249","DOI":"10.1016\/j.bbabio.2006.05.023","article-title":"Identification of mitochondrial carriers in Saccharomyces cerevisiae by transport assay of reconstituted recombinant proteins","volume":"1757","author":"Palmieri","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"432","DOI":"10.1016\/j.plantsci.2018.06.020","article-title":"Physiology of L-carnitine in plants in light of the knowledge in animals and microorganisms","volume":"274","author":"Jacques","year":"2018","journal-title":"Plant. Sci."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"1249","DOI":"10.1016\/j.bbabio.2018.08.001","article-title":"Molecular identification and functional characterization of a novel glutamate transporter in yeast and plant mitochondria","volume":"1859","author":"Porcelli","year":"2018","journal-title":"Biochim. Biophys. Acta Bioenerg."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"165720","DOI":"10.1016\/j.bbadis.2020.165720","article-title":"Metabolic interactions between peroxisomes and mitochondria with a special focus on acylcarnitine metabolism","volume":"1866","author":"Houten","year":"2020","journal-title":"Biochim. Biophys. Acta Mol. Basis Dis."},{"key":"ref_41","doi-asserted-by":"crossref","unstructured":"Juraszek, B., and Na\u0142\u0119cz, K.A. (2019). SLC22A5 (OCTN2) Carnitine Transporter-Indispensable for Cell Metabolism, a Jekyll and Hyde of Human Cancer. Molecules, 25.","DOI":"10.3390\/molecules25010014"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"883","DOI":"10.1073\/pnas.72.3.883","article-title":"A mitochondrial carnitine acylcarnitine translocase system","volume":"72","author":"Pande","year":"1975","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1016\/S0022-2275(20)40302-5","article-title":"Long-Chain Carnitine Acyltransferase and the Role of Acylcarnitine Derivatives in the Catalytic Increase of Fatty Acid Oxidation Induced by Carnitine","volume":"4","author":"Fritz","year":"1963","journal-title":"J. Lipid Res."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/0014-5793(75)81059-3","article-title":"The mechanism of fatty acid uptake by heart mitochondria: An acylcarnitine-carnitine exchange","volume":"54","author":"Ramsay","year":"1975","journal-title":"FEBS Lett."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/0005-2728(90)90096-M","article-title":"Identification and purification of the carnitine carrier from rat liver mitochondria","volume":"1020","author":"Indiveri","year":"1990","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1016\/0005-2736(91)90235-Z","article-title":"Kinetic characterization of the reconstituted carnitine carrier from rat liver mitochondria","volume":"1065","author":"Indiveri","year":"1991","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/0005-2728(92)90019-X","article-title":"The mitochondrial carnitine carrier: Characterization of SH-groups relevant for its transport function","volume":"1140","author":"Indiveri","year":"1992","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1111\/j.1432-1033.1995.00271.x","article-title":"Probing the active site of the reconstituted carnitine carrier from rat liver mitochondria with sulfhydryl reagents. A cysteine residue is localized in or near the substrate binding site","volume":"228","author":"Indiveri","year":"1995","journal-title":"Eur. J. Biochem."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1042\/bj3210713","article-title":"The mitochondrial carnitine carrier protein: cDNA cloning, primary structure and comparison with other mitochondrial transport proteins","volume":"321 Pt 3","author":"Indiveri","year":"1997","journal-title":"Biochem. J."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1006\/bbrc.1998.9197","article-title":"Bacterial overexpression, purification, and reconstitution of the carnitine\/acylcarnitine carrier from rat liver mitochondria","volume":"249","author":"Indiveri","year":"1998","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1042\/bj2940293","article-title":"Abundant bacterial expression and reconstitution of an intrinsic membrane-transport protein from bovine mitochondria","volume":"294 Pt 1","author":"Fiermonte","year":"1993","journal-title":"Biochem. J."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"2362","DOI":"10.1016\/j.bbamcr.2016.03.007","article-title":"Discoveries, metabolic roles and diseases of mitochondrial carriers: A review","volume":"1863","author":"Palmieri","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"472","DOI":"10.3390\/pharmaceutics5030472","article-title":"Proteoliposomes as tool for assaying membrane transporter functions and interactions with xenobiotics","volume":"5","author":"Scalise","year":"2013","journal-title":"Pharmaceutics"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"3871","DOI":"10.2174\/1381612823666170616083705","article-title":"Studying Interactions of Drugs with Cell Membrane Nutrient Transporters: New Frontiers of Proteoliposome Nanotechnology","volume":"23","author":"Scalise","year":"2017","journal-title":"Curr. Pharm. Des."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"1276","DOI":"10.1021\/acscentsci.7b00420","article-title":"Chemical Proteomics Identifies SLC25A20 as a Functional Target of the Ingenol Class of Actinic Keratosis Drugs","volume":"3","author":"Parker","year":"2017","journal-title":"ACS Cent. Sci."},{"key":"ref_56","doi-asserted-by":"crossref","unstructured":"Tonazzi, A., Eberini, I., and Indiveri, C. (2013). Molecular mechanism of inhibition of the mitochondrial carnitine\/acylcarnitine transporter by omeprazole revealed by proteoliposome assay, mutagenesis and bioinformatics. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0082286"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/j.cbi.2008.03.003","article-title":"Interaction of beta-lactam antibiotics with the mitochondrial carnitine\/acylcarnitine transporter","volume":"173","author":"Pochini","year":"2008","journal-title":"Chem. Biol. Interact."},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"Bolognino, I., Giangregorio, N., Pisani, L., de Candia, M., Purgatorio, R., Tonazzi, A., Altomare, C.D., Cellamare, S., and Catto, M. (2019). A Prospective Repurposing of Dantrolene as a Multitarget Agent for Alzheimer\u2019s Disease. Molecules, 24.","DOI":"10.3390\/molecules24234298"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"1015","DOI":"10.1021\/acs.chemrestox.5b00050","article-title":"Mitochondrial carnitine\/acylcarnitine transporter, a novel target of mercury toxicity","volume":"28","author":"Tonazzi","year":"2015","journal-title":"Chem. Res. Toxicol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1007\/s11010-016-2881-0","article-title":"Post-translational modification by acetylation regulates the mitochondrial carnitine\/acylcarnitine transport protein","volume":"426","author":"Giangregorio","year":"2017","journal-title":"Mol. Cell Biochem."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1016\/j.bbagen.2015.10.005","article-title":"The mitochondrial carnitine\/acylcarnitine carrier is regulated by hydrogen sulfide via interaction with C136 and C155","volume":"1860","author":"Giangregorio","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1016\/j.bbabio.2017.04.002","article-title":"Nitric oxide inhibits the mitochondrial carnitine\/acylcarnitine carrier through reversible S-nitrosylation of cysteine 136","volume":"1858","author":"Tonazzi","year":"2017","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_63","doi-asserted-by":"crossref","unstructured":"Tonazzi, A., Console, L., and Indiveri, C. (2013). Inhibition of mitochondrial carnitine\/acylcarnitine transporter by H(2)O(2): Molecular mechanism and possible implication in pathophysiology. Chem. Biol. Interact.","DOI":"10.1016\/j.cbi.2013.01.006"},{"key":"ref_64","doi-asserted-by":"crossref","unstructured":"Giangregorio, N., Tonazzi, A., Console, L., Prejan\u00f2, M., Marino, T., Russo, N., and Indiveri, C. (2020). Effect of Copper on the Mitochondrial Carnitine\/Acylcarnitine Carrier Via Interaction with Cys136 and Cys155. Possible Implications in Pathophysiology. Molecules, 25.","DOI":"10.3390\/molecules25040820"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"9082","DOI":"10.1016\/S0021-9258(17)47268-1","article-title":"Mechanism of carnitine acylcarnitine translocase-catalyzed import of acylcarnitines into mitochondria","volume":"259","author":"Murthy","year":"1984","journal-title":"J. Biol. Chem."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1016\/j.bbabio.2012.02.007","article-title":"Identification by site-directed mutagenesis of a hydrophobic binding site of the mitochondrial carnitine\/acylcarnitine carrier involved in the interaction with acyl groups","volume":"1817","author":"Tonazzi","year":"2012","journal-title":"Biochim. Biophys. Acta Bioenerg."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"H2243","DOI":"10.1152\/ajpheart.00864.2003","article-title":"Myocardial carnitine palmitoyltransferase I expression and long-chain fatty acid oxidation in fetal and newborn lambs","volume":"286","author":"Bartelds","year":"2004","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/S0163-7827(01)00024-8","article-title":"Control of mitochondrial beta-oxidation flux","volume":"41","author":"Eaton","year":"2002","journal-title":"Prog. Lipid Res."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"2039","DOI":"10.1096\/fj.12-216689","article-title":"Carnitine palmitoyltransferase 2 and carnitine\/acylcarnitine translocase are involved in the mitochondrial synthesis and export of acylcarnitines","volume":"27","author":"Violante","year":"2013","journal-title":"FASEB J."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1002\/mrm.26492","article-title":"Acetate transport into mitochondria does not require a carnitine shuttle mechanism","volume":"77","author":"Arduini","year":"2017","journal-title":"Magn. Reson. Med."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1006\/abbi.1993.1216","article-title":"The carnitine acyltransferases and their role in modulating acyl-CoA pools","volume":"302","author":"Ramsay","year":"1993","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1016\/j.celrep.2015.12.030","article-title":"The Acetyl Group Buffering Action of Carnitine Acetyltransferase Offsets Macronutrient-Induced Lysine Acetylation of Mitochondrial Proteins","volume":"14","author":"Davies","year":"2016","journal-title":"Cell Rep."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/0005-2728(93)90095-W","article-title":"Reaction mechanism of the reconstituted tricarboxylate carrier from rat liver mitochondria","volume":"1142","author":"Bisaccia","year":"1993","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1016\/0968-0004(79)90215-9","article-title":"The ADP, ATP shuttle of the mitochondrion","volume":"4","author":"Klingenberg","year":"1979","journal-title":"Trends Biochem. Sci."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"1978","DOI":"10.1016\/j.bbamem.2008.04.011","article-title":"The ADP and ATP transport in mitochondria and its carrier","volume":"1778","author":"Klingenberg","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"2994","DOI":"10.1016\/S0021-9258(19)85841-6","article-title":"Carnitine-acylcarnitine translocase catalyzes an equilibrating unidirectional transport as well","volume":"255","author":"Pande","year":"1980","journal-title":"J. Biol. Chem."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1002\/ajmg.c.30087","article-title":"Disorders of carnitine transport and the carnitine cycle","volume":"142C","author":"Longo","year":"2006","journal-title":"Am. J. Med. Genet. C Semin Med. Genet."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1042\/bj3610417","article-title":"Carnitine biosynthesis in mammals","volume":"361","author":"Vaz","year":"2002","journal-title":"Biochem. J."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1177\/2472555218812821","article-title":"OCTN: A Small Transporter Subfamily with Great Relevance to Human Pathophysiology, Drug Discovery, and Diagnostics","volume":"24","author":"Pochini","year":"2019","journal-title":"SLAS Discov."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"22840","DOI":"10.1074\/jbc.M109.032888","article-title":"Carnitine insufficiency caused by aging and overnutrition compromises mitochondrial performance and metabolic control","volume":"284","author":"Noland","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_81","doi-asserted-by":"crossref","unstructured":"Almannai, M., Alfadhel, M., and El-Hattab, A.W. (2019). Carnitine Inborn Errors of Metabolism. Molecules, 24.","DOI":"10.3390\/molecules24183251"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/j.ymgme.2015.09.004","article-title":"Disorders of carnitine biosynthesis and transport","volume":"116","author":"Scaglia","year":"2015","journal-title":"Mol. Genet. Metab."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"6683","DOI":"10.1016\/S0021-9258(17)32999-X","article-title":"Characterization of carnitine acylcarnitine translocase system of heart mitochondria","volume":"251","author":"Pande","year":"1976","journal-title":"J. Biol. Chem."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/S0005-2736(03)00033-6","article-title":"Chemical modification of the mitochondrial ornithine\/citrulline carrier by SH reagents: Effects on the transport activity and transition from carrier to pore-like function","volume":"1611","author":"Tonazzi","year":"2003","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1113\/expphysiol.1998.sp004111","article-title":"Mitochondrial carrier proteins can reversibly change their transport mode: The cases of the aspartate\/glutamate and the phosphate carrier","volume":"83","year":"1998","journal-title":"Exp. Physiol."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/0005-2736(93)90022-R","article-title":"Functional properties of the reconstituted phosphate carrier from bovine heart mitochondria: Evidence for asymmetric orientation and characterization of three different transport modes","volume":"1149","author":"Stappen","year":"1993","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1016\/j.bbabio.2010.03.017","article-title":"Site-directed mutagenesis of charged amino acids of the human mitochondrial carnitine\/acylcarnitine carrier: Insight into the molecular mechanism of transport","volume":"1797","author":"Giangregorio","year":"2010","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"8649","DOI":"10.1021\/bi012183n","article-title":"Site-directed mutagenesis and chemical modification of the six native cysteine residues of the rat mitochondrial carnitine carrier: Implications for the role of cysteine-136","volume":"41","author":"Indiveri","year":"2002","journal-title":"Biochemistry"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"1331","DOI":"10.1016\/j.bbabio.2007.08.010","article-title":"Conformation-dependent accessibility of Cys-136 and Cys-155 of the mitochondrial rat carnitine\/acylcarnitine carrier to membrane-impermeable SH reagents","volume":"1767","author":"Giangregorio","year":"2007","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"22782","DOI":"10.1074\/jbc.273.35.22782","article-title":"Expression in Escherichia coli, functional characterization, and tissue distribution of isoforms A and B of the phosphate carrier from bovine mitochondria","volume":"273","author":"Fiermonte","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"18152","DOI":"10.1074\/jbc.M109.014118","article-title":"A novel member of solute carrier family 25 (SLC25A42) is a transporter of coenzyme A and adenosine 3\u2032,5\u2032-diphosphate in human mitochondria","volume":"284","author":"Fiermonte","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"13374","DOI":"10.1074\/jbc.M114.547448","article-title":"The human gene SLC25A29, of solute carrier family 25, encodes a mitochondrial transporter of basic amino acids","volume":"289","author":"Porcelli","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"33137","DOI":"10.1074\/jbc.M114.610808","article-title":"The human SLC25A33 and SLC25A36 genes of solute carrier family 25 encode two mitochondrial pyrimidine nucleotide transporters","volume":"289","author":"Todisco","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"eaav1850","DOI":"10.1126\/sciadv.aav1850","article-title":"How cardiolipin modulates the dynamics of respiratory complex I","volume":"5","author":"Jussupow","year":"2019","journal-title":"Sci. Adv."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"2048","DOI":"10.1016\/j.bbamem.2009.06.007","article-title":"Cardiolipin and mitochondrial carriers","volume":"1788","author":"Klingenberg","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1016\/j.bbabio.2010.12.005","article-title":"Functional and structural role of amino acid residues in the matrix alpha-helices, termini and cytosolic loops of the bovine mitochondrial oxoglutarate carrier","volume":"1807","author":"Miniero","year":"2011","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/j.jmb.2006.08.041","article-title":"Functional and structural role of amino acid residues in the even-numbered transmembrane alpha-helices of the bovine mitochondrial oxoglutarate carrier","volume":"363","author":"Cappello","year":"2006","journal-title":"J. Mol. Biol."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"400","DOI":"10.1016\/j.jmb.2007.03.048","article-title":"Functional and structural role of amino acid residues in the odd-numbered transmembrane alpha-helices of the bovine mitochondrial oxoglutarate carrier","volume":"369","author":"Cappello","year":"2007","journal-title":"J. Mol. Biol."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1038\/nature02056","article-title":"Structure of mitochondrial ADP\/ATP carrier in complex with carboxyatractyloside","volume":"426","author":"Kahn","year":"2003","journal-title":"Nature"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"2617","DOI":"10.1073\/pnas.0509994103","article-title":"Mitochondrial carriers in the cytoplasmic state have a common substrate binding site","volume":"103","author":"Robinson","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"1237","DOI":"10.1016\/j.bbabio.2006.03.021","article-title":"The conserved substrate binding site of mitochondrial carriers","volume":"1757","author":"Kunji","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1038\/s41439-020-0098-y","article-title":"A novel homozygous missense SLC25A20 mutation in three CACT-deficient patients: Clinical and autopsy data","volume":"7","author":"Chinen","year":"2020","journal-title":"Human Genome Var."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"1009","DOI":"10.1016\/j.bbabio.2009.02.026","article-title":"Site-directed mutagenesis of the His residues of the rat mitochondrial carnitine\/acylcarnitine carrier: Implications for the role of His-29 in the transport pathway","volume":"1787","author":"Tonazzi","year":"2009","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1016\/j.tibs.2019.11.001","article-title":"The SLC25 Mitochondrial Carrier Family: Structure and Mechanism","volume":"45","author":"Ruprecht","year":"2020","journal-title":"Trends Biochem. Sci."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1016\/j.sbi.2019.03.029","article-title":"Structural changes in the transport cycle of the mitochondrial ADP\/ATP carrier","volume":"57","author":"Ruprecht","year":"2019","journal-title":"Curr. Opin. Struct. Biol."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"17766","DOI":"10.1073\/pnas.0809580105","article-title":"The mechanism of transport by mitochondrial carriers based on analysis of symmetry","volume":"105","author":"Robinson","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"1931","DOI":"10.1016\/j.febslet.2009.10.063","article-title":"Structure and function of mitochondrial carriers-role of the transmembrane helix P and G residues in the gating and transport mechanism","volume":"584","author":"Palmieri","year":"2010","journal-title":"FEBS Lett."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"772","DOI":"10.1016\/j.bbabio.2016.02.006","article-title":"The switching mechanism of the mitochondrial ADP\/ATP carrier explored by free-energy landscapes","volume":"1857","author":"Pietropaolo","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"6924","DOI":"10.1021\/bi5009112","article-title":"Identification of amino acid residues underlying the antiport mechanism of the mitochondrial carnitine\/acylcarnitine carrier by site-directed mutagenesis and chemical labeling","volume":"53","author":"Giangregorio","year":"2014","journal-title":"Biochemistry"},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"708","DOI":"10.1016\/j.bbabio.2019.07.006","article-title":"Tryptophan 224 of the rat mitochondrial carnitine\/acylcarnitine carrier is crucial for the antiport mechanism","volume":"1860","author":"Giangregorio","year":"2019","journal-title":"Biochim. Biophys. Acta Bioenerg."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"7925","DOI":"10.1074\/jbc.M111.324855","article-title":"Substrate specificity of the two mitochondrial ornithine carriers can be swapped by single mutation in substrate binding site","volume":"287","author":"Miniero","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"19607","DOI":"10.1074\/jbc.M411181200","article-title":"Identification by site-directed mutagenesis and chemical modification of three vicinal cysteine residues in rat mitochondrial carnitine\/acylcarnitine transporter","volume":"280","author":"Tonazzi","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1007\/s10059-011-0276-3","article-title":"Regulation of reactive oxygen species generation in cell signaling","volume":"32","author":"Bae","year":"2011","journal-title":"Mol. Cells"},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1089\/ars.2006.8.243","article-title":"Hydrogen peroxide: A signaling messenger","volume":"8","author":"Stone","year":"2006","journal-title":"Antioxid. Redox Signal."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.molcel.2007.03.016","article-title":"Hydrogen peroxide sensing and signaling","volume":"26","author":"Veal","year":"2007","journal-title":"Mol. Cell"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/j.coph.2007.12.012","article-title":"Hydrogen peroxide as an endogenous mediator and exogenous tool in cardiovascular research: Issues and considerations","volume":"8","author":"Schroder","year":"2008","journal-title":"Curr. Opin. Pharmacol."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1002\/cbf.2816","article-title":"Human OCTN2 (SLC22A5) is down-regulated in virus- and nonvirus-mediated cancer","volume":"30","author":"Scalise","year":"2012","journal-title":"Cell Biochem. Funct."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"5299","DOI":"10.1016\/j.bbagen.2013.08.003","article-title":"Glutathione controls the redox state of the mitochondrial carnitine\/acylcarnitine carrier Cys residues by glutathionylation","volume":"1830","author":"Giangregorio","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"2027","DOI":"10.1089\/ars.2007.1642","article-title":"What is the functional significance of the unique location of glutaredoxin 1 (GRx1) in the intermembrane space of mitochondria?","volume":"9","author":"Pai","year":"2007","journal-title":"Antioxid. Redox Signal."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1042\/BJ20112131","article-title":"The biological roles of glutaredoxins","volume":"446","author":"Stroher","year":"2012","journal-title":"Biochem. J."},{"key":"ref_121","doi-asserted-by":"crossref","unstructured":"Fernando, V., Zheng, X., Walia, Y., Sharma, V., Letson, J., and Furuta, S. (2019). S-Nitrosylation: An Emerging Paradigm of Redox Signaling. Antioxidants, 8.","DOI":"10.3390\/antiox8090404"},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"712","DOI":"10.1016\/j.bbagen.2011.03.008","article-title":"Regulation of mitochondrial processes by protein S-nitrosylation","volume":"1820","author":"Piantadosi","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"rs1","DOI":"10.1126\/scisignal.2003252","article-title":"Nitric oxide regulates mitochondrial fatty acid metabolism through reversible protein S-nitrosylation","volume":"6","author":"Doulias","year":"2013","journal-title":"Sci. Signal."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"7631","DOI":"10.1073\/pnas.95.13.7631","article-title":"Persistent inhibition of cell respiration by nitric oxide: Crucial role of S-nitrosylation of mitochondrial complex I and protective action of glutathione","volume":"95","author":"Clementi","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"702","DOI":"10.3389\/fphar.2020.00702","article-title":"Hydrogen Sulfide and Endoplasmic Reticulum Stress: A Potential Therapeutic Target for Central Nervous System Degeneration Diseases","volume":"11","author":"Zhong","year":"2020","journal-title":"Front. Pharmacol."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"492","DOI":"10.1016\/j.neuint.2013.09.003","article-title":"Physiological role of hydrogen sulfide and polysulfide in the central nervous system","volume":"63","author":"Kimura","year":"2013","journal-title":"Neurochem. Int."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1016\/j.cca.2014.10.037","article-title":"Hydrogen sulfide in signaling pathways","volume":"439","author":"Olas","year":"2015","journal-title":"Clin. Chim. Acta"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1038\/nrd4433","article-title":"Hydrogen sulfide-based therapeutics: Exploiting a unique but ubiquitous gasotransmitter","volume":"14","author":"Wallace","year":"2015","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"6290931","DOI":"10.1155\/2018\/6290931","article-title":"Hydrogen Sulfide Biochemistry and Interplay with Other Gaseous Mediators in Mammalian Physiology","volume":"2018","author":"Giuffre","year":"2018","journal-title":"Oxid. Med. Cell Longev."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"7606","DOI":"10.1073\/pnas.1321232111","article-title":"Reactive cysteine persulfides and S-polythiolation regulate oxidative stress and redox signaling","volume":"111","author":"Ida","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1016\/j.bbabio.2015.04.009","article-title":"Acetylation of human mitochondrial citrate carrier modulates mitochondrial citrate\/malate exchange activity to sustain NADPH production during macrophage activation","volume":"1847","author":"Palmieri","year":"2015","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1016\/j.cmet.2015.05.014","article-title":"Acetyl coenzyme A: A central metabolite and second messenger","volume":"21","author":"Pietrocola","year":"2015","journal-title":"Cell Metab."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"770","DOI":"10.1006\/bbrc.1998.9738","article-title":"The structure and organization of the human carnitine\/acylcarnitine translocase (CACT1) gene","volume":"252","author":"Iacobazzi","year":"1998","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1159\/000134684","article-title":"Assignment of the carnitine\/acylcarnitine translocase gene (CACT) to human chromosome band 3p21.31 by in situ hybridization","volume":"79","author":"Viggiano","year":"1997","journal-title":"Cytogenet. Cell Genet."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1023\/A:1020501021222","article-title":"Human mitochondrial transmembrane metabolite carriers: Tissue distribution and its implication for mitochondrial disorders","volume":"30","author":"Huizing","year":"1998","journal-title":"J. Bioenerg. Biomembr."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1016\/j.bbrc.2009.09.018","article-title":"Regulation of the human SLC25A20 expression by peroxisome proliferator-activated receptor alpha in human hepatoblastoma cells","volume":"389","author":"Tachibana","year":"2009","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"284","DOI":"10.3390\/biology2010284","article-title":"Transcriptional Regulation of the Mitochondrial Citrate and Carnitine\/Acylcarnitine Transporters: Two Genes Involved in Fatty Acid Biosynthesis and \u03b2-oxidation","volume":"2","author":"Iacobazzi","year":"2013","journal-title":"Biology"},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1016\/j.bbrc.2009.08.008","article-title":"Statins, fibrates and retinoic acid upregulate mitochondrial acylcarnitine carrier gene expression","volume":"388","author":"Iacobazzi","year":"2009","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/j.cbi.2019.05.006","article-title":"Human mitochondrial carnitine acylcarnitine carrier: Molecular target of dietary bioactive polyphenols from sweet cherry (Prunus avium L.)","volume":"307","author":"Console","year":"2019","journal-title":"Chem. Biol. Interact."},{"key":"ref_140","first-page":"873","article-title":"Toxicity of cephaloridine to carnitine transport and fatty acid metabolism in rabbit renal cortical mitochondria: Structure-activity relationships","volume":"270","author":"Tune","year":"1994","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"396","DOI":"10.2174\/138955751505150408142032","article-title":"Mitochondrial carnitine\/acylcarnitine translocase: Insights in structure\/ function relationships. Basis for drug therapy and side effects prediction","volume":"15","author":"Tonazzi","year":"2015","journal-title":"Mini Rev. Med. Chem."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1002\/jbt.20208","article-title":"Interaction of mildronate with the mitochondrial carnitine\/acylcarnitine transport protein","volume":"22","author":"Oppedisano","year":"2008","journal-title":"J. Biochem. Mol. Toxicol."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/j.freeradbiomed.2014.04.030","article-title":"Mitochondrial thioredoxin reductase inhibition, selenium status, and Nrf-2 activation are determinant factors modulating the toxicity of mercury compounds","volume":"73","author":"Branco","year":"2014","journal-title":"Free Radic. Biol. Med."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"1435","DOI":"10.1289\/ehp.10056","article-title":"A biomonitoring study of lead, cadmium, and mercury in the blood of New York city adults","volume":"115","author":"McKelvey","year":"2007","journal-title":"Environ. Health Perspect."}],"container-title":["Biomolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2218-273X\/11\/4\/521\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,13]],"date-time":"2025-10-13T13:33:14Z","timestamp":1760362394000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2218-273X\/11\/4\/521"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,3,31]]},"references-count":144,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2021,4]]}},"alternative-id":["biom11040521"],"URL":"https:\/\/doi.org\/10.3390\/biom11040521","relation":{},"ISSN":["2218-273X"],"issn-type":[{"value":"2218-273X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,3,31]]}}}