{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,8]],"date-time":"2026-10-08T15:49:52Z","timestamp":1791474592795,"version":"4.3.4"},"reference-count":151,"publisher":"MDPI AG","issue":"1","license":[{"start":{"date-parts":[[2021,12,23]],"date-time":"2021-12-23T00:00:00Z","timestamp":1640217600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Coenzyme Q (CoQ) is a key component of the respiratory chain of all eukaryotic cells. Its function is closely related to mitochondrial respiration, where it acts as an electron transporter. However, the cellular functions of coenzyme Q are multiple: it is present in all cell membranes, limiting the toxic effect of free radicals, it is a component of LDL, it is involved in the aging process, and its deficiency is linked to several diseases. Recently, it has been proposed that coenzyme Q contributes to suppressing ferroptosis, a type of iron-dependent programmed cell death characterized by lipid peroxidation. In this review, we report the latest hypotheses and theories analyzing the multiple functions of coenzyme Q. The complete knowledge of the various cellular CoQ functions is essential to provide a rational basis for its possible therapeutic use, not only in diseases characterized by primary CoQ deficiency, but also in large number of diseases in which its secondary deficiency has been found.<\/jats:p>","DOI":"10.3390\/ijms23010128","type":"journal-article","created":{"date-parts":[[2021,12,23]],"date-time":"2021-12-23T10:16:18Z","timestamp":1640254578000},"page":"128","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":107,"title":["The Roles of Coenzyme Q in Disease: Direct and Indirect Involvement in Cellular Functions"],"prefix":"10.3390","volume":"23","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9946-8516","authenticated-orcid":false,"given":"Francesco","family":"Pallotti","sequence":"first","affiliation":[{"name":"Dipartimento di Medicina e Chirurgia, Universit\u00e0 Degli Studi dell\u2019Insubria, 21100 Varese, Italy"},{"name":"SSD Laboratorio Analisi-SMEL Specializzato in Citogenetica e Genetica Medica, ASST Settelaghi-Ospedale di Circolo-Fondazione Macchi, 21100 Varese, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4387-5117","authenticated-orcid":false,"given":"Christian","family":"Bergamini","sequence":"additional","affiliation":[{"name":"Dipartimento di Farmacia e Biotecnologie, FABIT, Universit\u00e0 Degli Studi di Bologna, 40126 Bologna, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Costanza","family":"Lamperti","sequence":"additional","affiliation":[{"name":"UO Genetica Medica e Neurogenetica Fondazione IRCCS Istituto Neurologico C. Besta, 20133 Milano, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8945-6826","authenticated-orcid":false,"given":"Romana","family":"Fato","sequence":"additional","affiliation":[{"name":"Dipartimento di Farmacia e Biotecnologie, FABIT, Universit\u00e0 Degli Studi di Bologna, 40126 Bologna, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,12,23]]},"reference":[{"key":"ref_1","unstructured":"Kofler, M. (1946). Ueber ein pflanzliches Chinon. Festschrift Emil Christoph Barell, Hoffmann Laroche."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1104\/pp.34.2.128","article-title":"Internal Distribution of Coenzyme Q in Higher Plants","volume":"34","author":"Crane","year":"1959","journal-title":"Plant Physiol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"546","DOI":"10.1104\/pp.34.5.546","article-title":"Isolation of Two Quinones with Coenzyme Q Activity from Alfalfa","volume":"34","author":"Crane","year":"1959","journal-title":"Plant Physiol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1016\/0003-9861(60)90160-0","article-title":"Quinones in electron transport. 1. Coenzymatic activity of plastoquinone, coenzyme Q and related natural quinones","volume":"87","author":"Crane","year":"1960","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"2169","DOI":"10.1016\/S0021-9258(18)69886-2","article-title":"The natural occurrence of coenzyme Q and related compounds","volume":"234","author":"Lester","year":"1959","journal-title":"J. Biol. Chem."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1016\/S0021-9258(18)70267-6","article-title":"Chromatography of the coenzyme Q family of compounds on silicone-impregnated paper","volume":"234","author":"Lester","year":"1959","journal-title":"J. Biol. Chem."},{"key":"ref_7","doi-asserted-by":"crossref","unstructured":"Crane, F.L. (1961). Isolation and characterization of the coenzyme Q group and plastoquinone. Ciba Foundation Symposium-Endocrinology of the Testis (Colloquia on Endocrinology), John Wiley & Sons, Ltd.","DOI":"10.1002\/9780470719213.ch3"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1038\/191144a0","article-title":"Coupling of Phosphorylation to Electron and Hydrogen Transfer by a Chemi-Osmotic type of Mechanism","volume":"191","author":"Mitchell","year":"1961","journal-title":"Nature"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1002\/bies.200900131","article-title":"How did LUCA make a living? Chemiosmosis in the origin of life","volume":"32","author":"Lane","year":"2010","journal-title":"Bioessays"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"982","DOI":"10.1016\/j.bbabio.2013.12.005","article-title":"Free energy conversion in the LUCA: Quo vadis?","volume":"1837","author":"Ducluzeau","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1002\/biof.156","article-title":"Non-mitochondrial coenzyme","volume":"37","year":"2011","journal-title":"Q. Biofactors."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/S0005-2728(99)00049-3","article-title":"The plasma membrane NADH oxidase of HeLa cells has hydroquinone oxidase activity","volume":"1412","author":"Kishi","year":"1999","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1023\/A:1022462111175","article-title":"Antioxi-dant ascorbate is stabilized by NADH-coenzyme Q10 reductase in the plasma membrane","volume":"29","author":"Barroso","year":"1997","journal-title":"J. Bioenerg. Biomembr."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"28220","DOI":"10.1074\/jbc.M302297200","article-title":"Coenzyme q10 prevents apoptosis by inhibiting mitochondrial depolarization independently of its free radical scavenging property","volume":"278","author":"Papucci","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"628","DOI":"10.1080\/15216540701545991","article-title":"Functional connections and pathways of coenzyme Q10-inducible genes: An in-silico study","volume":"59","author":"Schmelzer","year":"2007","journal-title":"IUBMB Life"},{"key":"ref_16","unstructured":"Yagi, K. (1993). Lipid peroxidation in biological membranes: Mechanism and implications. Active Oxygens, Lipid Peroxides, and Antioxidants, CRC Press."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"S60","DOI":"10.1007\/BF00226842","article-title":"Ubiquinol: An endogenous antioxidant in aerobic organisms","volume":"71","author":"Ernster","year":"1993","journal-title":"Clin. Investig."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1002\/biof.5520080305","article-title":"Oxidative stress, antioxidant defences and aging","volume":"8","author":"Lenaz","year":"1998","journal-title":"BioFactors"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"S41","DOI":"10.1016\/j.mito.2007.02.006","article-title":"The antioxidant role of coenzyme Q","volume":"7","author":"Bentinger","year":"2007","journal-title":"Mitochondrion"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1111\/j.1749-6632.1999.tb07920.x","article-title":"Coenzyme Q10 can in some circumstances block apoptosis, and this effect is mediated through mitochondria","volume":"887","author":"Kagan","year":"1999","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/j.bbamem.2003.11.012","article-title":"Metabolism and function of coenzyme Q","volume":"1660","author":"Turunen","year":"2003","journal-title":"Biochim. Biophys. Acta (BBA)-Biomembr."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1016\/j.bbrc.2010.02.147","article-title":"Coenzyme Q--biosynthesis and functions","volume":"396","author":"Bentinger","year":"2010","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1007\/s10517-017-3633-1","article-title":"Impairment of Energy-Dependent Processes in the Muscle Tissue as a Pathogenetic Mechanism of Statin-Induced Myopathy","volume":"162","author":"Mikashinovich","year":"2017","journal-title":"Bull. Exp. Biol. Med."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.pharmthera.2017.02.029","article-title":"Myotoxicity of statins: Mechanism of action","volume":"175","author":"Roederer","year":"2017","journal-title":"Pharmacol Ther."},{"key":"ref_25","doi-asserted-by":"crossref","unstructured":"Ramachandran, R., and Wierzbicki, A.S. (2017). Statins, Muscle Disease and Mitochondria. J. Clin. Med., 6.","DOI":"10.3390\/jcm6080075"},{"key":"ref_26","doi-asserted-by":"crossref","unstructured":"Hayashi, K., Ogiyama, Y., Yokomi, K., Nakagawa, T., Kaino, T., and Kawamukai, M. (2014). Functional conservation of coen-zyme Q biosynthetic genes among yeasts, plants, and humans. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0099038"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"2773","DOI":"10.1681\/ASN.2006080833","article-title":"COQ2 nephropathy: A newly described inherited mitochondriopathy with primary renal involvement","volume":"18","author":"Santorelli","year":"2007","journal-title":"J. Am. Soc. Nephrol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1086\/500092","article-title":"A mutation in pa-ra-hydroxybenzoate-polyprenyl transferase (COQ2) causes primary coenzyme Q10 deficiency","volume":"78","author":"Quinzii","year":"2006","journal-title":"Am. J. Hum. Genet."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1172\/JCI29089","article-title":"Prenyldiphosphate synthase, subunit 1 (PDSS1) and OH-benzoate polyprenyltransferase (COQ2) mutations in ubiquinone deficiency and oxidative phosphorylation disorders","volume":"117","author":"Mollet","year":"2007","journal-title":"J. Clin. Investig."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"1125","DOI":"10.1086\/510023","article-title":"Leigh syndrome with nephropathy and CoQ10 deficiency due to decaprenyl diphosphate synthase subunit 2 (PDSS2) mutations","volume":"79","author":"Schuelke","year":"2006","journal-title":"Am. J. Hum. Genet."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1136\/jmedgenet-2011-100394","article-title":"Haploinsufficiency ofCOQ4causes coenzyme Q10deficiency","volume":"49","author":"Salviati","year":"2012","journal-title":"J. Med. Genet."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"2013","DOI":"10.1172\/JCI45693","article-title":"COQ6 mutations in human patients produce nephrotic syndrome with sensorineural deafness","volume":"121","author":"Heeringa","year":"2011","journal-title":"J. Clin. Investig."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1016\/j.ajhg.2007.12.024","article-title":"ADCK3, an Ancestral Kinase, Is Mutated in a Form of Recessive Ataxia Associated with Coenzyme Q10 Deficiency","volume":"82","author":"Tazir","year":"2008","journal-title":"Am. J. Hum. Genet."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1016\/j.ajhg.2007.12.022","article-title":"CABC1 Gene Mutations Cause Ubiquinone Deficiency with Cerebellar Ataxia and Seizures","volume":"82","author":"Mollet","year":"2008","journal-title":"Am. J. Hum. Genet."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"558","DOI":"10.1016\/j.ajhg.2009.03.018","article-title":"A nonsense mutation in COQ9 causes autoso-mal-recessive neonatal-onset primary coenzyme Q10 deficiency: A potentially treatable form of mitochondrial disease","volume":"84","author":"Duncan","year":"2009","journal-title":"Am. J. Hum. Genet."},{"key":"ref_36","doi-asserted-by":"crossref","unstructured":"Liu, S., Guo, W., Han, X., Dai, W., Diao, Z., and Liu, W. (2016). Role of UBIAD1 in Intracellular Cholesterol Metabolism and Vascular Cell Calcification. PLoS ONE, 11.","DOI":"10.1371\/journal.pone.0149639"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41467-021-25084-7","article-title":"UbiB proteins regulate cellular CoQ distribution in Saccharomyces cerevisiae","volume":"12","author":"Kemmerer","year":"2021","journal-title":"Nat. Commun."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1016\/0003-9861(66)90036-1","article-title":"The mitochondrial electron transfer chain","volume":"116","author":"Green","year":"1966","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_39","first-page":"358","article-title":"The Kinetics of the Redox Reactions of Ubiquinone Related to the Electron-Transport Activity in the Respiratory Chain","volume":"34","author":"Klingenberg","year":"1973","journal-title":"JBIC J. Biol. Inorg. Chem."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1007\/BF00743010","article-title":"The random collision model and a critical assessment of diffusion and collision in mitochondrial electron transport","volume":"18","author":"Hackenbrock","year":"1986","journal-title":"J. Bioenerg. Biomembr."},{"key":"ref_41","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":"Pfeiffer","year":"2000","journal-title":"EMBO J."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"37861","DOI":"10.1074\/jbc.M106474200","article-title":"The Ratio of Oxidative Phosphorylation Complexes I\u2013V in Bovine Heart Mitochondria and the Composition of Respiratory Chain Supercomplexes","volume":"276","author":"Pfeiffer","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"C1221","DOI":"10.1152\/ajpcell.00263.2006","article-title":"Kinetics of integrated electron transfer in the mitochondrial respiratory chain: Random collisions vs. solid state electron channeling","volume":"292","author":"Lenaz","year":"2007","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1567","DOI":"10.1126\/science.1230381","article-title":"Supercomplex as-sembly determines electron flux in the mitochondrial electron transport chain","volume":"340","author":"Balsa","year":"2013","journal-title":"Science"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"5169","DOI":"10.1016\/S0021-9258(18)99410-X","article-title":"Partial resolution of the enzymes catalyzing oxidative phosphorylation. XV. Reverse electron transfer in the flavin-cytochrome beta region of the respiratory chain of beef heart submitochondrial particles","volume":"242","author":"Hinkle","year":"1967","journal-title":"J. Biol. Chem."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/BJ20081386","article-title":"How mitochondria produce reactive oxygen species","volume":"417","author":"Murphy","year":"2009","journal-title":"Biochem. J."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"825","DOI":"10.1016\/j.cmet.2015.09.004","article-title":"Oxygen Sensing by Arterial Chemoreceptors Depends on Mitochondrial Complex I Signaling","volume":"22","author":"Gao","year":"2015","journal-title":"Cell Metab."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"1047","DOI":"10.1016\/j.freeradbiomed.2013.08.170","article-title":"Inhibitors of ROS production by the ubiqui-none-binding site of mitochondrial complex I identified by chemical screening","volume":"65","author":"Orr","year":"2013","journal-title":"Free Radic. Biol. Med."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1016\/j.cmet.2015.12.009","article-title":"A Unifying Mechanism for Mitochondrial Superoxide Production during Ischemia-Reperfusion Injury","volume":"23","author":"Chouchani","year":"2016","journal-title":"Cell Metab."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"753","DOI":"10.1038\/nm.3212","article-title":"Cardioprotection by S-nitrosation of a cysteine switch on mitochondrial complex I","volume":"19","author":"Chouchani","year":"2013","journal-title":"Nat. Med."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/j.celrep.2016.03.009","article-title":"The CoQH2\/CoQ Ratio Serves as a Sen-sor of Respiratory Chain Efficiency","volume":"15","author":"Calvo","year":"2016","journal-title":"Cell Rep."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/j.freeradbiomed.2019.11.028","article-title":"A sensitive mass spectrometric assay for mitochondrial CoQ pool redox state in vivo","volume":"147","author":"Burger","year":"2019","journal-title":"Free Radic. Biol. Med."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1007\/BF00762682","article-title":"Coenzyme Q-pool function in glycerol-3-phosphate oxidation in hamster brown adipose tissue mitochondria","volume":"24","author":"Battino","year":"1992","journal-title":"J. Bioenerg. Biomembr."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/j.abb.2011.10.011","article-title":"Steady-state kinetic mechanism of the proline:ubiquinone oxidoreductase activity of proline utilization A (PutA) from Escherichia coli","volume":"516","author":"Moxley","year":"2011","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"677","DOI":"10.1042\/bj1510677","article-title":"The reaction of choline dehydrogenase with some electron acceptors","volume":"151","author":"Barrett","year":"1975","journal-title":"Biochem. J."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1016\/j.febslet.2013.01.011","article-title":"Prostate cancer cells metabolize d-lactate inside mitochondria via a D-lactate dehydrogenase which is more active and highly expressed than in normal cells","volume":"587","author":"Moro","year":"2013","journal-title":"FEBS Lett."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"100915","DOI":"10.1016\/j.arr.2019.100915","article-title":"Synthesis and metabolism of methylglyoxal, S-D-lactoylglutathione and D-lactate in cancer and Alzheimer\u2019s disease. Exploring the crossroad of eternal youth and premature aging","volume":"53","author":"Atlante","year":"2019","journal-title":"Ageing Res. Rev."},{"key":"ref_58","first-page":"901","article-title":"D-Lactate dehydrogenase links methylglyoxal degradation and electron transport through cytochrome C","volume":"172","author":"Maurino","year":"2016","journal-title":"Plant Physiol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"148137","DOI":"10.1016\/j.bbabio.2019.148137","article-title":"Bioenergetic consequences from xenotopic expression of a tuni-cate AOX in mouse mitochondria: Switch from RET and ROS to FET","volume":"1861","author":"Szibor","year":"2020","journal-title":"Biochim. Biophys Acta Bioenerg."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1016\/0925-4439(95)00028-3","article-title":"Biochemical, physiological and medical aspects of ubiquinone function","volume":"1271","author":"Ernster","year":"1995","journal-title":"Biochim. Biophys. Acta (BBA)-Mol. Basis Dis."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/S0098-2997(97)00015-0","article-title":"Role of cytochrome b5 reductase on the antioxidant function of coenzyme Q in the plasma membrane","volume":"18","author":"Villalba","year":"1997","journal-title":"Mol. Asp. Med."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"101950","DOI":"10.1016\/j.redox.2021.101950","article-title":"The diverse functionality of NQO1 and its roles in redox control","volume":"41","author":"Ross","year":"2021","journal-title":"Redox Biol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1179\/135100000101535528","article-title":"Plasma membrane redox system protects cells against oxidative stress","volume":"5","author":"Aguilera","year":"2000","journal-title":"Redox Rep."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"1956","DOI":"10.1111\/febs.15561","article-title":"Coenzyme Q biosynthesis inhibition induces HIF-1\u03b1 stabilization and metabolic switch toward glycolysis","volume":"288","author":"Liparulo","year":"2020","journal-title":"FEBS J."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0014-5793(75)80098-6","article-title":"Protonmotive redox mechanism of the cytochrome b-c1 complex in the respiratory chain: Pro-tonmotive ubiquinone cycle","volume":"56","author":"Mitchell","year":"1975","journal-title":"FEBS Lett."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1016\/j.cell.2013.12.010","article-title":"Regulation of fer-roptotic cancer cell death by GPX4","volume":"156","author":"Yang","year":"2014","journal-title":"Cell"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"688","DOI":"10.1038\/s41586-019-1705-2","article-title":"The CoQ oxidoreductase FSP1 acts parallel to GPX4 to in-hibit ferroptosis","volume":"575","author":"Bersuker","year":"2019","journal-title":"Nature"},{"key":"ref_68","doi-asserted-by":"crossref","unstructured":"Rizzardi, N., Liparulo, I., Antonelli, G., Orsini, F., Riva, A., Bergamini, C., and Fato, R. (2021). Coenzyme Q10 Phytosome Formulation Improves CoQ10 Bioavailability and Mitochondrial Functionality in Cultured Cells. Antioxidants, 10.","DOI":"10.3390\/antiox10060927"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1016\/j.freeradbiomed.2021.01.024","article-title":"Coenzyme Q homeostasis in aging: Response to non-genetic interventions","volume":"164","year":"2021","journal-title":"Free Radic. Biol. Med."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"1646","DOI":"10.1073\/pnas.88.5.1646","article-title":"Ubiquinol-10 protects human low density lipoprotein more efficiently against lipid peroxidation than does alpha-tocopherol","volume":"88","author":"Stocker","year":"1991","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"1183","DOI":"10.1073\/pnas.91.3.1183","article-title":"Oxidative susceptibil-ity of low density lipoprotein subfractions is related to their ubiquinol-10 and alpha-tocopherol content","volume":"91","author":"Tribble","year":"1994","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"108067","DOI":"10.1016\/j.abb.2019.108067","article-title":"Extracellular coenzyme Q10 (CoQ10) is reduced to ubiquinol-10 by intact Hep G2 cells independent of intracellular CoQ10 reduction","volume":"672","author":"Takahashi","year":"2019","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1089\/ars.2000.2.2-327","article-title":"Coenzyme Q10, Vitamin E, and Dihydrothioctic Acid Cooperatively Prevent Diene Conjugation in Isolated Low-Density Lipoprotein","volume":"2","author":"Schneider","year":"2000","journal-title":"Antioxidants Redox Signal."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1046\/j.1365-2125.1996.04178.x","article-title":"Lipid-lowering drugs and mitochondrial function: Effects of HMG-CoA reductase inhibitors on serum ubiquinone and blood lactate\/pyruvate ratio","volume":"42","author":"Chariot","year":"1996","journal-title":"Br. J. Clin. Pharmacol."},{"key":"ref_75","doi-asserted-by":"crossref","unstructured":"SEARCH Collaborative Group, Link, E., Parish, S., Armitage, J., Bowman, L., Heath, S., Matsuda, F., Gut, I., Lathrop, M., and Collins, R. (2008). SLCO1B1 variants and statin-induced myopathy\u2014A genomewide study. N. Engl. J. Med., 359, 789\u2013799.","DOI":"10.1056\/NEJMoa0801936"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"410","DOI":"10.1016\/j.exger.2010.03.014","article-title":"How increased oxidative stress promotes longevity and metabolic health: The concept of mitochondrial hormesis (mitohormesis)","volume":"45","author":"Ristow","year":"2010","journal-title":"Exp. Gerontol."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1007\/s10522-018-9768-2","article-title":"Mitochondrial dysfunction in metabolism and ageing: Shared mechanisms and outcomes?","volume":"19","author":"Navas","year":"2018","journal-title":"Biogerontology"},{"key":"ref_78","doi-asserted-by":"crossref","unstructured":"Pagano, G., Pallard\u00f3, F.V., Lyakhovich, A., Tiano, L., Fittipaldi, M.R., Toscanesi, M., and Trifuoggi, M. (2020). Aging-Related Disorders and Mitochondrial Dysfunction: A Critical Review for Prospect Mitoprotective Strategies Based on Mitochondrial Nutrient Mixtures. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21197060"},{"key":"ref_79","doi-asserted-by":"crossref","unstructured":"Haas, R.H. (2019). Mitochondrial Dysfunction in Aging and Diseases of Aging. Biology, 8.","DOI":"10.3390\/biology8020048"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1016\/j.mad.2010.02.003","article-title":"Is coenzyme Q a key factor in aging?","volume":"131","author":"Navas","year":"2010","journal-title":"Mech. Ageing Dev."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/j.freeradbiomed.2008.09.033","article-title":"Reactivity of ubiquinone and ubiquinol with superoxide and the hydroperoxyl radical: Implications for in vivo antioxidant activity","volume":"46","author":"Maroz","year":"2009","journal-title":"Free Radic. Biol. Med."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"1208","DOI":"10.1016\/j.biocel.2004.11.017","article-title":"Coenzyme Q10 affects expression of genes involved in cell signalling, metabolism and transport in human CaCo-2 cells","volume":"37","author":"Groneberg","year":"2005","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"111147","DOI":"10.1016\/j.exger.2020.111147","article-title":"Age-related mitochondrial dysfunction as a key factor in COVID-19 disease","volume":"142","author":"Navas","year":"2020","journal-title":"Exp. Gerontol."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1042\/EBC20170107","article-title":"Clinical syndromes associated with Coenzyme Q10 deficiency","volume":"62","author":"Trevisson","year":"2018","journal-title":"Essays Biochem."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"525","DOI":"10.3389\/fphys.2017.00525","article-title":"The Role of Sulfide Oxidation Impairment in the Pathogenesis of Primary CoQ Deficiency","volume":"8","author":"Quinzii","year":"2017","journal-title":"Front Physiol."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"7629673","DOI":"10.1155\/2019\/7629673","article-title":"Imbalance of Homocysteine and H2S: Significance, Mechanisms, and Therapeutic Promise in Vascular Injury","volume":"2019","author":"Yang","year":"2019","journal-title":"Oxidative Med. Cell. Longev."},{"key":"ref_87","first-page":"4396","article-title":"Clinical characteristics and gene mutation analysis of an adult patient with ETFDH-related multiple acyl-CoA dehydrogenase deficiency","volume":"22","author":"Wang","year":"2020","journal-title":"Mol. Med. Rep."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1002\/biof.5520320121","article-title":"Functions of coenzyme Q10 in inflammation and gene expression","volume":"32","author":"Schmelzer","year":"2008","journal-title":"Biofactors"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"R17","DOI":"10.1186\/ar2918","article-title":"Mitochondrial dysfunction and mitophagy activation in blood mononuclear cells of fibromyalgia patients: Implications in the patho-genesis of the disease","volume":"12","author":"Cordero","year":"2010","journal-title":"Arthritis Res. Ther."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"800","DOI":"10.1089\/ars.2012.4892","article-title":"Is inflammation a mitochondrial dysfunction-dependent event in fibromyalgia?","volume":"18","author":"Cordero","year":"2013","journal-title":"Antioxid Redox Signal."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"e32111","DOI":"10.7554\/eLife.32111","article-title":"Mito-chondrial CoQ deficiency is a common driver of mitochondrial oxidants and insulin resistance","volume":"7","author":"Fazakerley","year":"2018","journal-title":"Elife"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"668","DOI":"10.1007\/s00380-016-0923-x","article-title":"Low circulating coenzyme Q10 during acute phase is associated with inflammation, malnutrition, and in-hospital mortality in patients admitted to the coronary care unit","volume":"32","author":"Shimizu","year":"2016","journal-title":"Hear. Vessel."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"e16","DOI":"10.1126\/sageke.2002.41.pe16","article-title":"Mitochondrial abnormalities and oxidative imbalance in neuro-degenerative disease","volume":"2002","author":"Ogawa","year":"2002","journal-title":"Sci. Aging Knowl. Environ."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"693","DOI":"10.4149\/BLL_2020_113","article-title":"The importance of coenzyme Q10 and its ratio to cholesterol in the progress of chronic kidney diseases linked to non- -communicable diseases","volume":"121","author":"Gvozdjakova","year":"2020","journal-title":"Bratisl. Med. J."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"814","DOI":"10.1039\/C8FO01236A","article-title":"Coenzyme Q10 attenuates high-fat di-et-induced non-alcoholic fatty liver disease through activation of the AMPK pathway","volume":"10","author":"Chen","year":"2019","journal-title":"Food Funct."},{"key":"ref_96","doi-asserted-by":"crossref","unstructured":"Ferri, E., Marzetti, E., Calvani, R., Picca, A., Cesari, M., and Arosio, B. (2020). Role of Age-Related Mitochondrial Dysfunction in Sarcopenia. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21155236"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1016\/0003-9861(92)90511-T","article-title":"Distribution and redox state of ubiquinones in rat and human tissues","volume":"295","author":"Appelkvist","year":"1992","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"1038","DOI":"10.1002\/bmc.1567","article-title":"Validated HPLC method for the quantitative determination of CoQ10 in dog plasma and its application to a pharmacokinetic study","volume":"25","author":"Yuan","year":"2010","journal-title":"Biomed. Chromatogr."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"240","DOI":"10.3164\/jcbn.15-73","article-title":"Coenzyme Q10 serum concentration and redox status in European adults: Influence of age, sex, and lipoprotein concentration","volume":"58","author":"Niklowitz","year":"2016","journal-title":"J. Clin. Biochem. Nutr."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1016\/S0076-6879(99)99034-1","article-title":"[31] High-performance liquid chromatography-coulometric electrochemical detection of ubiquinol 10, ubiquinone 10, carotenoids, and tocopherols in neonatal plasma","volume":"299","author":"Finckh","year":"1999","journal-title":"Methods Enzymol."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"256","DOI":"10.1093\/clinchem\/47.2.256","article-title":"HPLC Analysis of Reduced and Oxidized Coenzyme Q10 in Human Plasma","volume":"47","author":"Tang","year":"2001","journal-title":"Clin. Chem."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"S89","DOI":"10.1016\/j.mito.2007.04.002","article-title":"Analysis of coenzyme Q in human blood and tissues","volume":"7","author":"Barshop","year":"2007","journal-title":"Mitochondrion"},{"key":"ref_103","doi-asserted-by":"crossref","unstructured":"Schou-Pedersen, A.M.V., Schemeth, D., and Lykkesfeldt, J. (2019). Determination of Reduced and Oxidized Coenzyme Q10 in Canine Plasma and Heart Tissue by HPLC-ECD: Comparison with LC-MS\/MS Quantification. Antioxidants, 8.","DOI":"10.3390\/antiox8080253"},{"key":"ref_104","first-page":"71","article-title":"Coenzyme Q10: Is There a Clini-cal Role and a Case for Measurement?","volume":"29","author":"Molyneux","year":"2008","journal-title":"Clin. Biochem. Rev."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1080\/00365519950185481","article-title":"Measurement and stability of plasma reduced, oxidized and total coenzyme Q10 in humans","volume":"59","author":"Kaikkonen","year":"1999","journal-title":"Scand. J. Clin. Lab. Investig."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/S0378-4347(00)83129-1","article-title":"Determination of reduced and total ubiquinones in biological materials by liquid chromatography with electrochemical detection","volume":"430","author":"Okamoto","year":"1988","journal-title":"J. Chromatogr. B Biomed. Sci. Appl."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"621","DOI":"10.7150\/ijms.4768","article-title":"Correlations between Oxidative DNA Damage, Oxidative Stress and Coenzyme Q10 in Patients with Coronary Artery Disease","volume":"9","author":"Kaya","year":"2012","journal-title":"Int. J. Med. Sci."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"764","DOI":"10.3109\/1354750X.2012.727029","article-title":"Pediatric reference intervals for muscle coenzyme Q10","volume":"17","author":"Pastore","year":"2012","journal-title":"Biomarkers"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1016\/S0098-2997(97)00003-4","article-title":"Coenzyme Q10 in the diet-daily intake and relative bioavailability","volume":"18","author":"Weber","year":"1997","journal-title":"Mol. Asp. Med."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/0003-2697(84)90530-X","article-title":"Quantitative determination of coenzyme Q10 in human blood for clinical studies","volume":"142","author":"Vadhanavikit","year":"1984","journal-title":"Anal. Biochem."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/j.cccn.2003.12.002","article-title":"Measurement of reduced and oxidized coenzyme Q9 and coenzyme Q10 levels in mouse tissues by HPLC with coulometric detection","volume":"341","author":"Tang","year":"2004","journal-title":"Clin. Chim. Acta"},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"2380","DOI":"10.1373\/clinchem.2005.054643","article-title":"Determination of Coenzyme Q10 Status in Blood Mononuclear Cells, Skeletal Muscle, and Plasma by HPLC with Di-Propoxy-Coenzyme Q10 as an Internal Standard","volume":"51","author":"Duncan","year":"2005","journal-title":"Clin. Chem."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1016\/0378-4347(88)80009-4","article-title":"Determination of coenzyme Q10, \u03b1-tocopherol and cholesterol in biological samples by coupled-column liquid chromatography with coulometric and ultraviolet detection","volume":"425","author":"Edlund","year":"1988","journal-title":"J. Chromatogr. B Biomed. Sci. Appl."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/j.cccn.2004.04.003","article-title":"Age-related changes in plasma coenzyme Q10 concentrations and redox state in apparently healthy children and adults","volume":"347","author":"Miles","year":"2004","journal-title":"Clin. Chim. Acta"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"S78","DOI":"10.1016\/j.mito.2007.03.003","article-title":"Plasma coenzyme Q10 response to oral ingestion of coenzyme Q10 formulations","volume":"7","author":"Bhagavan","year":"2007","journal-title":"Mitochondrion"},{"key":"ref_116","doi-asserted-by":"crossref","unstructured":"Yubero, D., Allen, G., Artuch, R., and Montero, R. (2017). The Value of Coenzyme Q10 Determination in Mitochondrial Patients. J. Clin. Med., 6.","DOI":"10.3390\/jcm6040037"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/0304-4165(87)90183-8","article-title":"Ubiquinone biosynthesis by the microsomal fraction from rat liver","volume":"926","author":"Norling","year":"1987","journal-title":"Biochim. Biophys. Acta (BBA)-Gen. Subj."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1258\/000456303321610493","article-title":"Ubiquinone: Cholesterol\u2019s reclusive cousin","volume":"40","author":"Hargreaves","year":"2003","journal-title":"Ann. Clin. Biochem. Int. J. Lab. Med."},{"key":"ref_119","first-page":"160","article-title":"Plasma Ubiquinone, Al-pha-Tocopherol and Cholesterol in Man","volume":"62","author":"Karlsson","year":"1992","journal-title":"Int. J. Vitam. Nutr. Res."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/0009-8981(96)06357-7","article-title":"Plasma ubiquinol\/cholesterol ratios in patients with hyperlipidaemia, those with diabetes mellitus and in patients requiring dialysis","volume":"253","author":"McDonnell","year":"1996","journal-title":"Clin. Chim. Acta"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1038\/pr.2015.124","article-title":"Oxidized proportion of muscle coenzyme Q10 increases with age in healthy children","volume":"78","author":"Niklowitz","year":"2015","journal-title":"Pediatr. Res."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1016\/j.cccn.2003.12.020","article-title":"Simultaneous analysis of coenzyme Q10 in plasma, erythrocytes and platelets: Comparison of the antioxidant level in blood cells and their environment in healthy children and after oral supplementation in adults","volume":"342","author":"Niklowitz","year":"2004","journal-title":"Clin. Chim. Acta"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1373\/clinchem.2004.043653","article-title":"Biological Variation of Coenzyme Q10","volume":"51","author":"Molyneux","year":"2005","journal-title":"Clin. Chem."},{"key":"ref_124","first-page":"39","article-title":"Determination of coenzyme Q in human plasma","volume":"45","author":"Kaplan","year":"1996","journal-title":"Physiol. Res."},{"key":"ref_125","first-page":"37","article-title":"Bioavailability of Two Different For-mulations of Coenzyme Q10 in Healthy Subjects","volume":"7","author":"Wahlqvist","year":"1998","journal-title":"Asia Pac. J. Clin. Nutr."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/S0009-8981(03)00137-2","article-title":"Plasma coenzyme Q10 reference intervals, but not redox status, are affected by gender and race in self-reported healthy adults","volume":"332","author":"Miles","year":"2003","journal-title":"Clin. Chim. Acta"},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/S0021-9150(96)06021-2","article-title":"Plasma ubiquinol-10 is decreased in patients with hyperlipidaemia","volume":"129","author":"Kontush","year":"1997","journal-title":"Atherosclerosis"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1002\/biof.5520090218","article-title":"Distribution of antioxidants among blood components and lipoproteins: Significance of lipids\/CoQ10ratio as a possible marker of increased risk for atherosclerosis","volume":"9","author":"Tomasetti","year":"1999","journal-title":"BioFactors"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"793","DOI":"10.1038\/s41598-018-37542-2","article-title":"Plasma coenzyme Q10 status is impaired in selected genetic conditions","volume":"9","author":"Montero","year":"2019","journal-title":"Sci. Rep."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"892","DOI":"10.1093\/ajcn\/70.5.892","article-title":"Decreased serum ubiquinone-10 concentrations in phenylketonuria","volume":"70","author":"Artuch","year":"1999","journal-title":"Am. J. Clin. Nutr."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"1371","DOI":"10.1111\/j.1468-1331.2008.02318.x","article-title":"Coenzyme Q10and vitamin E deficiency in Friedreich\u2019s ataxia: Predictor of efficacy of vitamin E and coenzyme Q10therapy","volume":"15","author":"Cooper","year":"2008","journal-title":"Eur. J. Neurol."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/S0009-9120(02)00278-3","article-title":"Ubiquinone-10 content in lymphocytes of phenylketonuric patients","volume":"35","author":"Artuch","year":"2002","journal-title":"Clin. Biochem."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1111\/j.1600-0404.1987.tb03603.x","article-title":"Isoprenoid biosynthesis in multiple sclerosis, II. A possible role of NADPH","volume":"76","author":"Steen","year":"1987","journal-title":"Acta Neurol. Scand."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1002\/ana.410420221","article-title":"Coenzyme Q10 levels correlate with the activities of complexes I and II\/III in mitochondria from parkinsonian and nonparkinsonian subjects","volume":"42","author":"Shults","year":"1997","journal-title":"Ann. Neurol."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"1403","DOI":"10.1002\/bmc.1072","article-title":"Validation and application of an HPLC-EC method for analysis of coenzyme Q10 in blood platelets","volume":"22","author":"Miles","year":"2008","journal-title":"Biomed. Chromatogr."},{"key":"ref_136","unstructured":"Mortensen, S., Heidt, P., and Sehested, J. (1998). Clinical Perspectives in Treatment of Cardiovascular Diseases with Coenzyme Q 10. Highlights in Ubiquinone Research, Taylor and Francis."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"S2","DOI":"10.1016\/j.mito.2007.02.011","article-title":"Discovery of ubiquinone (coenzyme Q) and an overview of function","volume":"7","author":"Crane","year":"2007","journal-title":"Mitochondrion"},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"2379","DOI":"10.1073\/pnas.86.7.2379","article-title":"Muscle coenzyme Q deficiency in familial mitochondrial encephalomyopathy","volume":"86","author":"Ogasahara","year":"1989","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1002\/biof.5520250112","article-title":"Muscle coenzyme Q10 concentrations in patients with probable and definite diagnosis of respiratory chain disorders","volume":"25","author":"Montero","year":"2005","journal-title":"BioFactors"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1016\/j.mito.2008.01.003","article-title":"Systematic evaluation of muscle coenzyme Q10 content in children with mitochondrial respiratory chain enzyme deficiencies","volume":"8","author":"Miles","year":"2008","journal-title":"Mitochondrion"},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1016\/j.ymgme.2018.02.015","article-title":"The dilemma of diagnosing coenzyme Q10 deficiency in muscle","volume":"125","author":"Louw","year":"2018","journal-title":"Mol. Genet. Metab."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"619","DOI":"10.2741\/4231","article-title":"Clinical applications of coenzyme Q10","volume":"19","author":"Vega","year":"2014","journal-title":"Front Biosci"},{"key":"ref_143","doi-asserted-by":"crossref","unstructured":"Neergheen, V., Chalasani, A., Wainwright, L., Yubero, D., Montero, R., Artuch, R., and Hargreaves, I. (2017). Coenzyme Q10 in the Treatment of Mitochondrial Disease. J. Inborn Errors Metab. Screen., 5.","DOI":"10.1177\/2326409817707771"},{"key":"ref_144","doi-asserted-by":"crossref","unstructured":"Gutierrez-Mariscal, F.M., Larriva, A.P.A.-D., Limia-Perez, L., Romero-Cabrera, J.L., Yubero-Serrano, E.M., and L\u00f3pez-Miranda, J. (2020). Coenzyme Q10 Supplementation for the Reduction of Oxidative Stress: Clinical Implications in the Treatment of Chronic Diseases. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21217870"},{"key":"ref_145","doi-asserted-by":"crossref","unstructured":"Pravst, I., Rodriguez Aguilera, J.C., Cortes Rodriguez, A.B., Jazbar, J., Locatelli, I., Hristov, H., and \u017dmitek, K. (2020). Comparative Bioavailability of Different Coenzyme Q10 Formulations in Healthy Elderly Individuals. Nutrients, 12.","DOI":"10.3390\/nu12030784"},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"797","DOI":"10.1016\/j.sjbs.2015.10.025","article-title":"Preparation and quality evaluation of coenzyme Q10 long-circulating liposomes","volume":"24","author":"Li","year":"2015","journal-title":"Saudi J. Biol. Sci."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"793879","DOI":"10.1155\/2014\/793879","article-title":"Novel Lipid-Free Nanoformulation for Improving Oral Bioavailability of Coenzyme Q10","volume":"2014","author":"Zhou","year":"2014","journal-title":"BioMed Res. Int."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.ijpharm.2018.12.003","article-title":"High-dose coenzyme Q10-loaded oleogels for oral therapeutic supplementation","volume":"556","author":"Masotta","year":"2018","journal-title":"Int. J. Pharm."},{"key":"ref_149","first-page":"671","article-title":"Inclusion of coenzyme Q10 with beta-cyclodextrin studied by polarography","volume":"41","author":"Yang","year":"2006","journal-title":"Yao Xue Xue Bao"},{"key":"ref_150","doi-asserted-by":"crossref","unstructured":"Manzar, H., Abdulhussein, D., Yap, T., and Cordeiro, M. (2020). Cellular Consequences of Coenzyme Q10 Deficiency in Neurodegeneration of the Retina and Brain. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21239299"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"1834","DOI":"10.1016\/j.biocel.2012.06.032","article-title":"Putting together a plasma membrane NADH oxidase: A tale of three labor-atories","volume":"44","author":"Crane","year":"2012","journal-title":"Int. J. Biochem. Cell Biol."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/23\/1\/128\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T07:52:18Z","timestamp":1760169138000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/23\/1\/128"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,12,23]]},"references-count":151,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2022,1]]}},"alternative-id":["ijms23010128"],"URL":"https:\/\/doi.org\/10.3390\/ijms23010128","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,12,23]]}}}