The Roles of Coenzyme Q in Disease: Direct and Indirect Involvement in Cellular Functions
Open accessAbstract
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.
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Decreased CoQ10 levels disturb mitochondrial electron transport, resulting in limited ATP synthase activity and impaired energy metabolism and mitochondrial dysfunction.
“Decreased CoQ10 levels are considered to disturb the mitochondrial electron transport, resulting in a limited adenosine triphosphate (ATP) synthase activity and thus leading to an impaired energy metabolism and mitochondrial dysfunction.(16,18,19)”
From Effects of coenzyme Q10 supplementation on myopathy in statin-treated patients: a systematic review and meta-analysis (2025) · cites this paper as [16]
Section 2.1 (page unavailable) explains that CoQ carries electrons in the respiratory chain and that electron transfer generates the force used to synthesize ATP. Section 2.2 reports reduced respiratory-chain activity after CoQ10 depletion. The paper does not establish reduced ATP synthase activity specifically, and its Conclusions note that the causal direction between CoQ deficiency and mitochondrial dysfunction can be unclear. (LLM, conf=0.84)
Experimental — accuracy not yet measuredGeranylgeranyl pyrophosphate is essential for the endogenous synthesis of CoQ10.
“This isoprenoid is essential for the endogenous synthesis of CoQ10.(15)”
From Effects of coenzyme Q10 supplementation on myopathy in statin-treated patients: a systematic review and meta-analysis (2025) · cites this paper as [15]
Section 2 (Ubiquinone/Coenzyme Q Biosynthesis; page unavailable) says the isoprenoid chain is synthesized through the mevalonate pathway and identifies farnesyl pyrophosphate as a precursor of CoQ. It does not identify geranylgeranyl pyrophosphate or say that it is essential for endogenous CoQ10 synthesis (searched: “geranylgeranyl pyrophosphate” and “geranylgeranyl”). (LLM, conf=0.83)
Experimental — accuracy not yet measuredStatin intake can lead to reduced CoQ10 levels.
“As CoQ10 is only supplied in small quantities with food and is predominantly synthesised endogenously,(16,17) statin intake can lead to reduced CoQ10 levels.(17)”
From Effects of coenzyme Q10 supplementation on myopathy in statin-treated patients: a systematic review and meta-analysis (2025) · cites this paper as [16]
CoQ10 has structural and antioxidant properties and plays a central role as an electron transporter in the respiratory chain of mitochondria.
“In physiological conditions, CoQ10 has structural and antioxidant properties and plays a central role as an electron transporter in the respiratory chain of mitochondria.(16)”
From Effects of coenzyme Q10 supplementation on myopathy in statin-treated patients: a systematic review and meta-analysis (2025) · cites this paper as [16]
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Cites
Regulation of Ferroptotic Cancer Cell Death by GPX4
Yang, W. S., SriRamaratnam, R., Welsch, M. E., Shimada, K., Skouta, R., Viswanathan, V. S., Cheah, J. H., Clemons, P. A., Shamji, A. F., Clish, C. B., et al. (2014) · Cell · doi:10.1016/j.cell.2013.12.010 · Cited by 7,713 · see citing works
<i>SLCO1B1</i> Variants and Statin-Induced Myopathy — A Genomewide Study
(2008) · New England Journal of Medicine · doi:10.1056/nejmoa0801936 · Cited by 2,043 · see citing works
Metabolism and function of coenzyme Q
Turunen, M., Olsson, J., & Dallner, G. (2004) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2003.11.012 · Cited by 1,026 · see citing works
A Unifying Mechanism for Mitochondrial Superoxide Production during Ischemia-Reperfusion Injury
Chouchani, E. T., Pell, V. R., James, A. M., Work, L. M., Saeb-Parsy, K., Frezza, C., Krieg, T., & Murphy, M. P. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2015.12.009 · Cited by 752 · see citing works
Cardioprotection by S-nitrosation of a cysteine switch on mitochondrial complex I
Chouchani, E. T., Methner, C., Nadtochiy, S. M., Logan, A., Pell, V. R., Ding, S., James, A. M., Cochemé, H. M., Reinhold, J., Lilley, K. S., et al. (2013) · Nature Medicine · doi:10.1038/nm.3212 · Cited by 619 · cited 1× · see citing works
“RET was associated with an increased Reactive Oxygen Secies (ROS) production from Complex I, especially in conditions of ischemia-reperfusion injury [49,50].”
BackgroundShults, C. W., Haas, R. H., Passov, D., & Beal, M. F. (1997) · Annals of Neurology · doi:10.1002/ana.410420221 · Cited by 326 · see citing works
DE PINIEUX, G., CHARIOT, P., AMMI‐SAÏD, M., LOUARN, F., LEJONC, J. L., ASTIER, A., JACOTOT, B., & GHERARDI, R. (1996) · British Journal of Clinical Pharmacology · doi:10.1046/j.1365-2125.1996.04178.x · Cited by 262 · see citing works
Plasma coenzyme Q10 response to oral ingestion of coenzyme Q10 formulations
Bhagavan, H. N., & Chopra, R. K. (2007) · Mitochondrion · doi:10.1016/j.mito.2007.03.003 · Cited by 243 · see citing works
Cordero, M. D., De Miguel, M., Moreno Fernández, A. M., Carmona López, I. M., Garrido Maraver, J., Cotán, D., Gómez Izquierdo, L., Bonal, P., Campa, F., Bullon, P., et al. (2010) · Arthritis Research & Therapy · doi:10.1186/ar2918 · Cited by 165 · see citing works
Mitochondrial CoQ deficiency is a common driver of mitochondrial oxidants and insulin resistance
Fazakerley, D. J., Chaudhuri, R., Yang, P., Maghzal, G. J., Thomas, K. C., Krycer, J. R., Humphrey, S. J., Parker, B. L., Fisher-Wellman, K. H., Meoli, C. C., et al. (2018) · eLife · doi:10.7554/elife.32111 · Cited by 160 · see citing works
Lenaz, G., & Genova, M. L. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00263.2006 · Cited by 155 · see citing works
Orr, A. L., Ashok, D., Sarantos, M. R., Shi, T., Hughes, R. E., & Brand, M. D. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.08.170 · Cited by 80 · see citing works
Flagged first, then by citations
Research works printed but not linked: 137
- [2]Crane F.L. Internal Distribution of Coenzyme Q in Higher Plants Plant Physiol. 1959 34 128 131 10.1104/pp.34.2.128 16655188 PMC541159 · DOI
- [3]Crane F.L. Isolation of Two Quinones with Coenzyme Q Activity from Alfalfa Plant Physiol. 1959 34 546 551 10.1104/pp.34.5.546 16655271 PMC541250 · DOI
- [4]Crane F.L. Quinones in electron transport. 1. Coenzymatic activity of plastoquinone, coenzyme Q and related natural quinones Arch. Biochem. Biophys. 1960 87 198 202 10.1016/0003-9861(60)90160-0 13812647 · DOI
- [5]Lester R.L. Crane F.L. The natural occurrence of coenzyme Q and related compounds J. Biol. Chem. 1959 234 2169 2175 10.1016/S0021-9258(18)69886-2 13673033 · DOI
- [6]Lester R.L. Ramasarma T. Chromatography of the coenzyme Q family of compounds on silicone-impregnated paper J. Biol. Chem. 1959 234 672 676 10.1016/S0021-9258(18)70267-6 13641282 · DOI
- [7]Crane F.L. Isolation and characterization of the coenzyme Q group and plastoquinone Ciba Foundation Symposium-Endocrinology of the Testis (Colloquia on Endocrinology) John Wiley & Sons, Ltd. Chichester, UK 1961 36 78
- [8]Mitchell P. Coupling of Phosphorylation to Electron and Hydrogen Transfer by a Chemi-Osmotic type of Mechanism Nature 1961 191 144 148 10.1038/191144a0 13771349 · DOI · Paper page
- [9]Lane N. Allen J.F. Martin W. How did LUCA make a living? Chemiosmosis in the origin of life Bioessays 2010 32 271 280 10.1002/bies.200900131 20108228 · DOI · Paper page
- [10]Ducluzeau A.L. Schoepp-Cothenet B. Baymann F. Russell M.J. Nitschke W. Free energy conversion in the LUCA: Quo vadis? Biochim. Biophys. Acta 2014 1837 982 988 10.1016/j.bbabio.2013.12.005 24361840 · DOI · Paper page
- [11]Morré D.J. Morré D.M. Non-mitochondrial coenzyme Q. Biofactors. 2011 37 355 360 10.1002/biof.156 21674641 · DOI
- [12]Kishi T. Morré D.M. Morré D.J. The plasma membrane NADH oxidase of HeLa cells has hydroquinone oxidase activity Biochim. Biophys. Acta 1999 1412 66 77 10.1016/S0005-2728(99)00049-3 10354495 · DOI
- [13]Gómez-Díaz C. Rodríguez-Aguilera J.C. Barroso M.P. Villalba J.M. Navarro F. Crane F.L. Navas P. Antioxi-dant ascorbate is stabilized by NADH-coenzyme Q10 reductase in the plasma membrane J. Bioenerg. Biomembr. 1997 29 251 257 10.1023/A:1022410127104 9298710 · DOI
- [14]Papucci L. Schiavone N. Witort E. Donnini M. Lapucci A. Tempestini A. Formigli L. Zecchi-Orlandini S. Or-landini G. Carella G. Coenzyme q10 prevents apoptosis by inhibiting mitochondrial depolarization independently of its free radical scavenging property J. Biol. Chem. 2003 278 28220 28228 10.1074/jbc.M302297200 12736273 · DOI
- [15]Döring F. Schmelzer C. Lindner I. Vock C. Fujii K. Functional connections and pathways of coenzyme Q10-inducible genes: An in-silico study IUBMB Life 2007 59 628 633 10.1080/15216540701545991 17852568 · DOI
- [16]Ernster L. Lipid peroxidation in biological membranes: Mechanism and implications Active Oxygens, Lipid Peroxides, and Antioxidants Yagi K. CRC Press Tokyo, Japan 1993 1 38
- [17]Ernster L. Forsmark-Andrée P. Ubiquinol: An endogenous antioxidant in aerobic organisms Clin. Investig. 1993 71 S60 S65 10.1007/BF00226842 8241707 · DOI
- [18]Lenaz G. Cavazzoni M. Genova M.L. D’Aurelio M. Pich M.M. Pallotti F. Formiggini G. Marchetti M. Castelli G.P. Bovina C. Oxidative stress, antioxidant defences and aging BioFactors 1998 8 195 204 10.1002/biof.5520080305 9914819 · DOI
- [19]Bentinger M. Brismar K. Dallner G. The antioxidant role of coenzyme Q Mitochondrion 2007 7 S41 S50 10.1016/j.mito.2007.02.006 17482888 · DOI · Paper page
- [20]Kagan T. Davis C. Lin L. Zakeri Z. Coenzyme Q10 can in some circumstances block apoptosis, and this effect is mediated through mitochondria Ann. N. Y. Acad. Sci. 1999 887 31 47 10.1111/j.1749-6632.1999.tb07920.x 10668462 · DOI
- [22]Bentinger M. Tekle M. Dallner G. Coenzyme Q--biosynthesis and functions Biochem. Biophys. Res. Commun. 2010 396 74 79 10.1016/j.bbrc.2010.02.147 20494114 · DOI
- [23]Mikashinovich Z.I. Belousova E.S. Sarkisyan O.G. Impairment of Energy-Dependent Processes in the Muscle Tissue as a Pathogenetic Mechanism of Statin-Induced Myopathy Bull. Exp. Biol. Med. 2017 162 433 435 10.1007/s10517-017-3633-1 28239789 · DOI · Paper page
- [24]Du Souich P. Roederer G. Dufour R. Myotoxicity of statins: Mechanism of action Pharmacol Ther. 2017 175 1 16 10.1016/j.pharmthera.2017.02.029 28223230 · DOI
- [25]Ramachandran R. Wierzbicki A.S. Statins, Muscle Disease and Mitochondria J. Clin. Med. 2017 6 75 10.3390/jcm6080075 28757597 PMC5575577 · DOI
- [26]Hayashi K. Ogiyama Y. Yokomi K. Nakagawa T. Kaino T. Kawamukai M. Functional conservation of coen-zyme Q biosynthetic genes among yeasts, plants, and humans PLoS ONE 2014 9 e99038 10.1371/journal.pone.0099038 24911838 PMC4049637 · DOI
- [27]Diomedi-Camassei F. Di Giandomenico S. Santorelli F.M. Caridi G. Piemonte F. Montini G. Ghiggeri G.M. Murer L. Barisoni L. Pastore A. COQ2 nephropathy: A newly described inherited mitochondriopathy with primary renal involvement J. Am. Soc. Nephrol. 2007 18 2773 2780 10.1681/ASN.2006080833 17855635 · DOI
- [28]Quinzii C. Naini A. Salviati L. Trevisson E. Navas P. Dimauro S. Hirano M. A mutation in pa-ra-hydroxybenzoate-polyprenyl transferase (COQ2) causes primary coenzyme Q10 deficiency Am. J. Hum. Genet. 2006 78 345 349 10.1086/500092 16400613 PMC1380241 · DOI
- [29]Mollet J. Giurgea I. Schlemmer D. Dallner G. Chretien D. Delahodde A. Bacq D. De Lonlay P. Munnich A. Rotig A. Prenyldiphosphate synthase, subunit 1 (PDSS1) and OH-benzoate polyprenyltransferase (COQ2) mutations in ubiquinone deficiency and oxidative phosphorylation disorders J. Clin. Investig. 2007 117 765 772 10.1172/JCI29089 17332895 PMC1804361 · DOI
- [30]López L.C. Schuelke M. Quinzii C.M. Kanki T. Rodenburg R.J. Naini A. Dimauro S. Hirano M. Leigh syndrome with nephropathy and CoQ10 deficiency due to decaprenyl diphosphate synthase subunit 2 (PDSS2) mutations Am. J. Hum. Genet. 2006 79 1125 1129 10.1086/510023 17186472 PMC1698707 · DOI
- [31]Salviati L. Trevisson E. Hernandez M.A.R. Casarin A. Pertegato V. Doimo M. Cassina M. Agosto C. Desbats M.A. Sartori G. Haploinsufficiency ofCOQ4causes coenzyme Q10deficiency J. Med. Genet. 2012 49 187 191 10.1136/jmedgenet-2011-100394 22368301 PMC3983946 · DOI
- [32]Heeringa S.F. Chernin G. Chaki M. Zhou W. Sloan A.J. Ji Z. Xie L.X. Salviati L. Hurd T.W. Vega-Warner V. COQ6 mutations in human patients produce nephrotic syndrome with sensorineural deafness J. Clin. Investig. 2011 121 2013 2024 10.1172/JCI45693 21540551 PMC3083770 · DOI
- [33]Lagier-Tourenne C. Tazir M. López L.C. Quinzii C.M. Assoum M. Drouot N. Busso C. Makri S. Ali-Pacha L. Benhassine T. ADCK3, an Ancestral Kinase, Is Mutated in a Form of Recessive Ataxia Associated with Coenzyme Q10 Deficiency Am. J. Hum. Genet. 2008 82 661 672 10.1016/j.ajhg.2007.12.024 18319074 PMC2427193 · DOI
- [34]Mollet J. Delahodde A. Serre V. Chretien D. Schlemmer D. Lombes A. Boddaert N. Desguerre I. De Lonlay P. De Baulny H.O. CABC1 Gene Mutations Cause Ubiquinone Deficiency with Cerebellar Ataxia and Seizures Am. J. Hum. Genet. 2008 82 623 630 10.1016/j.ajhg.2007.12.022 18319072 PMC2427298 · DOI
- [35]Duncan A.J. Bitner-Glindzicz M. Meunier B. Costello H. Hargreaves I.P. López L.C. Hirano M. Quinzii C.M. Sadowski M.I. Hardy J. A nonsense mutation in COQ9 causes autoso-mal-recessive neonatal-onset primary coenzyme Q10 deficiency: A potentially treatable form of mitochondrial disease Am. J. Hum. Genet. 2009 84 558 566 10.1016/j.ajhg.2009.03.018 19375058 PMC2681001 · DOI
- [36]Liu S. Guo W. Han X. Dai W. Diao Z. Liu W. Role of UBIAD1 in Intracellular Cholesterol Metabolism and Vascular Cell Calcification PLoS ONE 2016 11 e0149639 10.1371/journal.pone.0149639 26890002 PMC4758632 · DOI
- [37]Kemmerer Z.A. Robinson K.P. Schmitz J.M. Manicki M. Paulson B.R. Jochem A. Hutchins P.D. Coon J.J. Pagliarini D.J. UbiB proteins regulate cellular CoQ distribution in Saccharomyces cerevisiae Nat. Commun. 2021 12 1 11 10.1038/s41467-021-25084-7 34362905 PMC8346625 · DOI
- [38]Green D.E. Tzagoloff A. The mitochondrial electron transfer chain Arch. Biochem. Biophys. 1966 116 293 304 10.1016/0003-9861(66)90036-1 4289862 · DOI
- [39]Kröger A. Klingenberg M. The Kinetics of the Redox Reactions of Ubiquinone Related to the Electron-Transport Activity in the Respiratory Chain JBIC J. Biol. Inorg. Chem. 1973 34 358 368 10.1111/j.1432-1033.1973.tb02767.x 4351161 · DOI
- [40]Hackenbrock C.R. Chazotte B. Gupte S.S. The random collision model and a critical assessment of diffusion and collision in mitochondrial electron transport J. Bioenerg. Biomembr. 1986 18 331 368 10.1007/BF00743010 3021714 · DOI
- [41]Schägger H. Pfeiffer K. Supercomplexes in the respiratory chains of yeast and mammalian mitochondria EMBO J. 2000 19 1777 1783 10.1093/emboj/19.8.1777 10775262 PMC302020 · DOI · Paper page
- [42]Schägger H. Pfeiffer K. The Ratio of Oxidative Phosphorylation Complexes I–V in Bovine Heart Mitochondria and the Composition of Respiratory Chain Supercomplexes J. Biol. Chem. 2001 276 37861 37867 10.1074/jbc.M106474200 11483615 · DOI
- [44]Lapuente-Brun E. Moreno-Loshuertos R. Acín-Pérez R. Latorre-Pellicer A. Colás C. Balsa E. Per-ales-Clemente E. Quirós P.M. Calvo E. Rodríguez-Hernández M.A. Supercomplex as-sembly determines electron flux in the mitochondrial electron transport chain Science 2013 340 1567 1570 10.1126/science.1230381 23812712 · DOI · Paper page
- [45]Hinkle P.C. Butow R.A. Racker E. Chance B. 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 J. Biol. Chem. 1967 242 5169 5173 10.1016/S0021-9258(18)99410-X 4294331 · DOI
- [46]Murphy M.P. How mitochondria produce reactive oxygen species Biochem. J. 2009 417 1 13 10.1042/BJ20081386 19061483 PMC2605959 · DOI · Paper page
- [47]Fernández-Agüera M.C. Gao L. Gonzalez P. Pintado C.O. Arias-Mayenco I. García-Flores P. García-Pergañeda A. Pascual A. Ortega-Sáenz P. López-Barneo J. Oxygen Sensing by Arterial Chemoreceptors Depends on Mitochondrial Complex I Signaling Cell Metab. 2015 22 825 837 10.1016/j.cmet.2015.09.004 26437605 · DOI
- [51]Guarás A. Perales-Clemente E. Calvo E. Acín-Pérez R. Loureiro-Lopez M. Pujol C. Martínez-Carrascoso I. Nuñez E. García-Marqués F. Rodríguez-Hernández M.A. The CoQH2/CoQ Ratio Serves as a Sen-sor of Respiratory Chain Efficiency Cell Rep. 2016 15 197 209 10.1016/j.celrep.2016.03.009 27052170 · DOI
- [52]Burger N. Logan A. Prime T.A. Mottahedin A. Caldwell S. Krieg T. Hartley R. James A.M. Murphy M.P. A sensitive mass spectrometric assay for mitochondrial CoQ pool redox state in vivo Free Radic. Biol. Med. 2019 147 37 47 10.1016/j.freeradbiomed.2019.11.028 31811922 PMC6975167 · DOI
- [53]Rauchová H. Battino M. Fato R. Lenaz G. Drahota Z. Coenzyme Q-pool function in glycerol-3-phosphate oxidation in hamster brown adipose tissue mitochondria J. Bioenerg. Biomembr. 1992 24 235 241 10.1007/BF00762682 1326518 · DOI
- [54]Moxley M.A. Tanner J.J. Becker D.F. Steady-state kinetic mechanism of the proline:ubiquinone oxidoreductase activity of proline utilization A (PutA) from Escherichia coli Arch. Biochem. Biophys. 2011 516 113 120 10.1016/j.abb.2011.10.011 22040654 PMC3223275 · DOI
- [55]Barrett M.C. Dawson A.P. The reaction of choline dehydrogenase with some electron acceptors Biochem. J. 1975 151 677 683 10.1042/bj1510677 1218095 PMC1172417 · DOI
- [56]De Bari L. Moro L. Passarella S. Prostate cancer cells metabolize d-lactate inside mitochondria via a D-lactate dehydrogenase which is more active and highly expressed than in normal cells FEBS Lett. 2013 587 467 473 10.1016/j.febslet.2013.01.011 23333299 · DOI
- [57]De Bari L. Atlante A. Armeni T. Kalapos M.P. Synthesis and metabolism of methylglyoxal, S-D-lactoylglutathione and D-lactate in cancer and Alzheimer’s disease. Exploring the crossroad of eternal youth and premature aging Ageing Res. Rev. 2019 53 100915 10.1016/j.arr.2019.100915 31173890 · DOI
- [58]Maurino V.G. Welchen E. García L. Schmitz J. Fuchs P. Wagner S. Wienstroer J. Schertl P. Braun H.-P. Schwarzländer M. D-Lactate dehydrogenase links methylglyoxal degradation and electron transport through cytochrome C Plant Physiol. 2016 172 901 912 10.1104/pp.16.01174 27506242 PMC5047114 · DOI
- [59]Szibor M. Gainutdinov T. Fernandez-Vizarra E. Dufour E. Gizatullina Z. Debska-Vielhaber G. Heidler J. Wittig I. Viscomi C. Gellerich F. Bioenergetic consequences from xenotopic expression of a tuni-cate AOX in mouse mitochondria: Switch from RET and ROS to FET Biochim. Biophys Acta Bioenerg. 2020 1861 148137 10.1016/j.bbabio.2019.148137 31825809 · DOI
- [60]Ernster L. Dallner G. Biochemical, physiological and medical aspects of ubiquinone function Biochim. Biophys. Acta (BBA)-Mol. Basis Dis. 1995 1271 195 204 10.1016/0925-4439(95)00028-3 7599208 · DOI
- [61]Villalba J. Navarro F. Gómez-Díaz C. Arroyo A. Bello R. Navas P. Role of cytochrome b5 reductase on the antioxidant function of coenzyme Q in the plasma membrane Mol. Asp. Med. 1997 18 7 13 10.1016/S0098-2997(97)00015-0 9266501 · DOI
- [62]Ross D. Siegel D. The diverse functionality of NQO1 and its roles in redox control Redox Biol. 2021 41 101950 10.1016/j.redox.2021.101950 33774477 PMC8027776 · DOI · Paper page
- [63]Aguilera J.C.R. López-Lluch G. Ocaña C.S. Villalba J. Gómez-Díaz C. Navas P. Plasma membrane redox system protects cells against oxidative stress Redox Rep. 2000 5 148 150 10.1179/135100000101535528 10939299 · DOI
- [64]Liparulo I. Bergamini C. Bortolus M. Calonghi N. Gasparre G. Kurelac I. Masin L. Rizzardi N. Rugolo M. Wang W. Coenzyme Q biosynthesis inhibition induces HIF-1α stabilization and metabolic switch toward glycolysis FEBS J. 2020 288 1956 1974 10.1111/febs.15561 32898935 · DOI
- [65]Mitchell P. Protonmotive redox mechanism of the cytochrome b-c1 complex in the respiratory chain: Pro-tonmotive ubiquinone cycle FEBS Lett. 1975 56 1 6 10.1016/0014-5793(75)80098-6 239860 · DOI
- [67]Bersuker K. Hendricks J.M. Li Z. Magtanong L. Ford B. Tang P.H. Roberts M.A. Tong B. Maimone T.J. Zoncu R. The CoQ oxidoreductase FSP1 acts parallel to GPX4 to in-hibit ferroptosis Nature 2019 575 688 692 10.1038/s41586-019-1705-2 31634900 PMC6883167 · DOI · Paper page
- [68]Rizzardi N. Liparulo I. Antonelli G. Orsini F. Riva A. Bergamini C. Fato R. Coenzyme Q10 Phytosome Formulation Improves CoQ10 Bioavailability and Mitochondrial Functionality in Cultured Cells Antioxidants 2021 10 927 10.3390/antiox10060927 34200321 PMC8226950 · DOI
- [69]López-Lluch G. Coenzyme Q homeostasis in aging: Response to non-genetic interventions Free Radic. Biol. Med. 2021 164 285 302 10.1016/j.freeradbiomed.2021.01.024 33454314 · DOI
- [70]Stocker R. Bowry V.W. Frei B. Ubiquinol-10 protects human low density lipoprotein more efficiently against lipid peroxidation than does alpha-tocopherol Proc. Natl. Acad. Sci. USA 1991 88 1646 1650 10.1073/pnas.88.5.1646 2000375 PMC51081 · DOI
- [71]Tribble D.L. van den Berg J.J. Motchnik P.A. Ames B.N. Lewis D.M. Chait A. Krauss R.M. Oxidative susceptibil-ity of low density lipoprotein subfractions is related to their ubiquinol-10 and alpha-tocopherol content Proc. Natl. Acad. Sci. USA 1994 91 1183 1187 10.1073/pnas.91.3.1183 8302851 PMC521478 · DOI
- [72]Takahashi T. Mine Y. Okamoto T. Extracellular coenzyme Q10 (CoQ10) is reduced to ubiquinol-10 by intact Hep G2 cells independent of intracellular CoQ10 reduction Arch. Biochem. Biophys. 2019 672 108067 10.1016/j.abb.2019.108067 31400302 · DOI
- [73]Schneider D. Elstner E.F. Coenzyme Q10, Vitamin E, and Dihydrothioctic Acid Cooperatively Prevent Diene Conjugation in Isolated Low-Density Lipoprotein Antioxidants Redox Signal. 2000 2 327 333 10.1089/ars.2000.2.2-327 11229536 · DOI
- [76]Ristow M. Zarse K. How increased oxidative stress promotes longevity and metabolic health: The concept of mitochondrial hormesis (mitohormesis) Exp. Gerontol. 2010 45 410 418 10.1016/j.exger.2010.03.014 20350594 · DOI · Paper page
- [77]López-Lluch G. Hernández-Camacho J.D. Fernández-Ayala D.J.M. Navas P. Mitochondrial dysfunction in metabolism and ageing: Shared mechanisms and outcomes? Biogerontology 2018 19 461 480 10.1007/s10522-018-9768-2 30143941 · DOI
- [78]Pagano G. Pallardó F.V. Lyakhovich A. Tiano L. Fittipaldi M.R. Toscanesi M. Trifuoggi M. Aging-Related Disorders and Mitochondrial Dysfunction: A Critical Review for Prospect Mitoprotective Strategies Based on Mitochondrial Nutrient Mixtures Int. J. Mol. Sci. 2020 21 7060 10.3390/ijms21197060 PMC7582285 32992778 · DOI
- [79]Haas R.H. Mitochondrial Dysfunction in Aging and Diseases of Aging Biology 2019 8 48 10.3390/biology8020048 31213034 PMC6627182 · DOI
- [80]López-Lluch G. Rodríguez-Aguilera J.C. Santos-Ocaña C. Navas P. Is coenzyme Q a key factor in aging? Mech. Ageing Dev. 2010 131 225 235 10.1016/j.mad.2010.02.003 20193705 · DOI
- [81]Maroz A. Anderson R.F. Smith R.A. Murphy M.P. Reactivity of ubiquinone and ubiquinol with superoxide and the hydroperoxyl radical: Implications for in vivo antioxidant activity Free Radic. Biol. Med. 2009 46 105 109 10.1016/j.freeradbiomed.2008.09.033 18977291 · DOI
- [82]Groneberg D.A. Kindermann B. Althammer M. Klapper M. Vormann J. Littarru G.P. Döring F. Coenzyme Q10 affects expression of genes involved in cell signalling, metabolism and transport in human CaCo-2 cells Int. J. Biochem. Cell Biol. 2005 37 1208 1218 10.1016/j.biocel.2004.11.017 15778085 · DOI
- [83]Moreno Fernández-Ayala D.J. Navas P. López-Lluch G. Age-related mitochondrial dysfunction as a key factor in COVID-19 disease Exp. Gerontol. 2020 142 111147 10.1016/j.exger.2020.111147 33171276 PMC7648491 · DOI
- [84]Alcazar-Fabra M. Trevisson E. Brea-Calvo G. Clinical syndromes associated with Coenzyme Q10 deficiency Essays Biochem. 2018 62 377 398 10.1042/ebc20170107 30030365 · DOI
- [85]Quinzii C.M. Luna-Sanchez M. Ziosi M. Hidalgo-Gutierrez A. Kleiner G. Lopez L.C. The Role of Sulfide Oxidation Impairment in the Pathogenesis of Primary CoQ Deficiency Front Physiol. 2017 8 525 10.3389/fphys.2017.00525 28790927 PMC5525000 · DOI
- [86]Yang Q. He G.-W. Imbalance of Homocysteine and H2S: Significance, Mechanisms, and Therapeutic Promise in Vascular Injury Oxidative Med. Cell. Longev. 2019 2019 7629673 10.1155/2019/7629673 31885816 PMC6893243 · DOI
- [87]Wang C. Lv H. Xu X. Ma Y. Li Q. Clinical characteristics and gene mutation analysis of an adult patient with ETFDH-related multiple acyl-CoA dehydrogenase deficiency Mol. Med. Rep. 2020 22 4396 4402 10.3892/mmr.2020.11524 33000234 PMC7533516 · DOI
- [88]Schmelzer C. Lindner I. Rimbach G. Niklowitz P. Menke T. Döring F. Functions of coenzyme Q10 in inflammation and gene expression Biofactors 2008 32 179 183 10.1002/biof.5520320121 19096114 · DOI · Paper page
- [90]Cordero M.D. Díaz-Parrado E. Carrión A.M. Alfonsi S. Sánchez-Alcazar J.A. Bullón P. Battino M. de Miguel M. Is inflammation a mitochondrial dysfunction-dependent event in fibromyalgia? Antioxid Redox Signal. 2013 18 800 807 10.1089/ars.2012.4892 22938055 PMC3555092 · DOI
- [92]Shimizu M. Miyazaki T. Takagi A. Sugita Y. Yatsu S. Murata A. Kato T. Suda S. Ouchi S. Aikawa T. Low circulating coenzyme Q10 during acute phase is associated with inflammation, malnutrition, and in-hospital mortality in patients admitted to the coronary care unit Hear. Vessel. 2016 32 668 673 10.1007/s00380-016-0923-x 27942805 · DOI
- [93]Ogawa O. Zhu X. Perry G. Smith M.A. Mitochondrial abnormalities and oxidative imbalance in neuro-degenerative disease Sci. Aging Knowl. Environ. 2002 2002 e16 10.1126/sageke.2002.41.pe16 14603007 · DOI
- [94]Gvozdjakova A. Kucharska J. Sumbalova Z. Rausova Z. Chladekova A. Komlosi M. Szamosova M. Mojto V. The importance of coenzyme Q10 and its ratio to cholesterol in the progress of chronic kidney diseases linked to non- -communicable diseases Bratisl. Med. J. 2020 121 693 699 10.4149/BLL_2020_113 32955899 · DOI
- [95]Chen K. Chen X. Xue H. Zhang P. Fang W. Chen X. Ling W. Coenzyme Q10 attenuates high-fat di-et-induced non-alcoholic fatty liver disease through activation of the AMPK pathway Food Funct. 2019 10 814 823 10.1039/C8FO01236A 30675881 · DOI
- [96]Ferri E. Marzetti E. Calvani R. Picca A. Cesari M. Arosio B. Role of Age-Related Mitochondrial Dysfunction in Sarcopenia Int. J. Mol. Sci. 2020 21 5236 10.3390/ijms21155236 32718064 PMC7432902 · DOI · Paper page
- [97]Åberg F. Appelkvist E.-L. Dallner G. Ernster L. Distribution and redox state of ubiquinones in rat and human tissues Arch. Biochem. Biophys. 1992 295 230 234 10.1016/0003-9861(92)90511-T 1586151 · DOI
- [98]Yuan B. Liu C. Xu P. Lin L. Pan C. Wang L. Xu H. Validated HPLC method for the quantitative determination of CoQ10 in dog plasma and its application to a pharmacokinetic study Biomed. Chromatogr. 2010 25 1038 1044 10.1002/bmc.1567 21154890 · DOI
- [99]Niklowitz P. Onur S. Fischer A. Laudes M. Palussen M. Menke T. Döring F. Coenzyme Q10 serum concentration and redox status in European adults: Influence of age, sex, and lipoprotein concentration J. Clin. Biochem. Nutr. 2016 58 240 245 10.3164/jcbn.15-73 27257350 PMC4865593 · DOI
- [100]Finckh B. Kontush A. Commentz J. Hübner C. Burdelski M. Kohlschütter A. [31] High-performance liquid chromatography-coulometric electrochemical detection of ubiquinol 10, ubiquinone 10, carotenoids, and tocopherols in neonatal plasma Methods Enzymol. 1999 299 341 348 10.1016/s0076-6879(99)99034-1 9916213 · DOI
- [101]Tang P.H. Miles M.V. Degrauw A. Hershey A. Pesce A. HPLC Analysis of Reduced and Oxidized Coenzyme Q10 in Human Plasma Clin. Chem. 2001 47 256 265 10.1093/clinchem/47.2.256 11159774 · DOI
- [102]Barshop B.A. Gangoiti J.A. Analysis of coenzyme Q in human blood and tissues Mitochondrion 2007 7 S89 S93 10.1016/j.mito.2007.04.002 17485249 · DOI
- [103]Schou-Pedersen A.M.V. Schemeth D. Lykkesfeldt J. Determination of Reduced and Oxidized Coenzyme Q10 in Canine Plasma and Heart Tissue by HPLC-ECD: Comparison with LC-MS/MS Quantification Antioxidants 2019 8 253 10.3390/antiox8080253 PMC6720496 31366077 · DOI
- [104]Molyneux S.L. Young J.M. Florkowski C.M. Lever M. George P.M. Coenzyme Q10: Is There a Clini-cal Role and a Case for Measurement? Clin. Biochem. Rev. 2008 29 71 82 18787645 PMC2533152
- [105]Kaikkonen J. Nyyssonen K. Salonen J. Kaikkonen K.N.J. Measurement and stability of plasma reduced, oxidized and total coenzyme Q10 in humans Scand. J. Clin. Lab. Investig. 1999 59 457 466 10.1080/00365519950185481 10612557 · DOI
- [106]Okamoto T. Fukunaga Y. Ida Y. Kishi T. Determination of reduced and total ubiquinones in biological materials by liquid chromatography with electrochemical detection J. Chromatogr. B Biomed. Sci. Appl. 1988 430 11 19 10.1016/S0378-4347(00)83129-1 3215946 · DOI
- [107]Kaya Y. ÇEBİ A. Söylemez N. Demir H. Alp H.H. Bakan E. Correlations between Oxidative DNA Damage, Oxidative Stress and Coenzyme Q10 in Patients with Coronary Artery Disease Int. J. Med. Sci. 2012 9 621 626 10.7150/ijms.4768 23055813 PMC3465845 · DOI
- [108]Pastore A. Di Giovamberardino G. Petrillo S. Boenzi S. Bertini E. Dionisi-Vici C. Piemonte F. Pediatric reference intervals for muscle coenzyme Q10 Biomarkers 2012 17 764 766 10.3109/1354750X.2012.727029 23020092 · DOI
- [109]Weber C. Bysted A. Hølmer G. Coenzyme Q10 in the diet-daily intake and relative bioavailability Mol. Asp. Med. 1997 18 251 254 10.1016/S0098-2997(97)00003-4 9266531 · DOI
- [110]Vadhanavikit S. Sakamoto N. Ashida N. Kishi T. Folkers K. Quantitative determination of coenzyme Q10 in human blood for clinical studies Anal. Biochem. 1984 142 155 158 10.1016/0003-2697(84)90530-X 6517310 · DOI
- [111]Tang P.H. Miles M.V. Miles L. Quinlan J. Wong B. Wenisch A. Bove K. Measurement of reduced and oxidized coenzyme Q9 and coenzyme Q10 levels in mouse tissues by HPLC with coulometric detection Clin. Chim. Acta 2004 341 173 184 10.1016/j.cccn.2003.12.002 14967174 · DOI
- [112]Duncan A.J. Heales S.J. Mills K. Eaton S. Land J.M. Hargreaves I.P. Determination of Coenzyme Q10 Status in Blood Mononuclear Cells, Skeletal Muscle, and Plasma by HPLC with Di-Propoxy-Coenzyme Q10 as an Internal Standard Clin. Chem. 2005 51 2380 2382 10.1373/clinchem.2005.054643 16306103 · DOI
- [113]Edlund P.O. Determination of coenzyme Q10, α-tocopherol and cholesterol in biological samples by coupled-column liquid chromatography with coulometric and ultraviolet detection J. Chromatogr. B Biomed. Sci. Appl. 1988 425 87 97 10.1016/0378-4347(88)80009-4 3360880 · DOI
- [114]Miles M.V. Horn P.S. Tang P.H. Morrison J.A. Miles L. DeGrauw T. Pesce A.J. Age-related changes in plasma coenzyme Q10 concentrations and redox state in apparently healthy children and adults Clin. Chim. Acta 2004 347 139 144 10.1016/j.cccn.2004.04.003 15313151 · DOI
- [116]Yubero D. Allen G. Artuch R. Montero R. The Value of Coenzyme Q10 Determination in Mitochondrial Patients J. Clin. Med. 2017 6 37 10.3390/jcm6040037 28338638 PMC5406769 · DOI
- [117]Kalén A. Norling B. Appelkvist E. Dallner G. Ubiquinone biosynthesis by the microsomal fraction from rat liver Biochim. Biophys. Acta (BBA)-Gen. Subj. 1987 926 70 78 10.1016/0304-4165(87)90183-8 3651503 · DOI
- [118]Hargreaves I.P. Ubiquinone: Cholesterol’s reclusive cousin Ann. Clin. Biochem. Int. J. Lab. Med. 2003 40 207 218 10.1258/000456303321610493 12803831 · DOI
- [119]Karlsson J. Diamant B. Edlund P.O. Lund B. Folkers K. Theorell H. Plasma Ubiquinone, Al-pha-Tocopherol and Cholesterol in Man Int. J. Vitam. Nutr. Res. 1992 62 160 164 1517039
- [120]McDonnell M. Archbold G. Plasma ubiquinol/cholesterol ratios in patients with hyperlipidaemia, those with diabetes mellitus and in patients requiring dialysis Clin. Chim. Acta 1996 253 117 126 10.1016/0009-8981(96)06357-7 8879843 · DOI
- [121]Niklowitz P. Scherer J. Döring F. Paulussen M. Menke T. Oxidized proportion of muscle coenzyme Q10 increases with age in healthy children Pediatr. Res. 2015 78 365 370 10.1038/pr.2015.124 26107394 · DOI
- [122]Niklowitz P. Menke T. Andler W. Okun J.G. 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 Clin. Chim. Acta 2004 342 219 226 10.1016/j.cccn.2003.12.020 15026284 · DOI
- [123]Molyneux S.L. Florkowski C.M. Lever M. George P.M. Biological Variation of Coenzyme Q10 Clin. Chem. 2005 51 455 457 10.1373/clinchem.2004.043653 15681564 · DOI
- [124]Kaplan P. Sebestianová N. Turiaková J. Kucera I. Determination of coenzyme Q in human plasma Physiol. Res. 1996 45 39 46 8884922
- [125]Wahlqvist M.L. Wattanapenpaiboon N. Savige G.S. Kannar D. Bioavailability of Two Different For-mulations of Coenzyme Q10 in Healthy Subjects Asia Pac. J. Clin. Nutr. 1998 7 37 40 24394896
- [126]Miles M.V. Horn P.S. Morrison J.A. Tang P.H. DeGrauw T. Pesce A.J. Plasma coenzyme Q10 reference intervals, but not redox status, are affected by gender and race in self-reported healthy adults Clin. Chim. Acta 2003 332 123 132 10.1016/S0009-8981(03)00137-2 12763289 · DOI
- [127]Kontush A. Reich A. Baum K. Spranger T. Finckh B. Kohlschütter A. Beisiegel U. Plasma ubiquinol-10 is decreased in patients with hyperlipidaemia Atherosclerosis 1997 129 119 126 10.1016/S0021-9150(96)06021-2 9069526 · DOI
- [128]Tomasetti M. Alleva R. Solenghi M.D. Littarru G.P. Distribution of antioxidants among blood components and lipoproteins: Significance of lipids/CoQ10ratio as a possible marker of increased risk for atherosclerosis BioFactors 1999 9 231 240 10.1002/biof.5520090218 10416035 · DOI
- [129]Montero R. Yubero D. Salgado M.C. González M.J. Campistol J. O’Callaghan M.D.M. Pineda M. Delgadillo V. Maynou J. Fernandez G. Plasma coenzyme Q10 status is impaired in selected genetic conditions Sci. Rep. 2019 9 793 10.1038/s41598-018-37542-2 30692599 PMC6349877 · DOI
- [130]Artuch R. Vilaseca M.-A. Moreno J. Lambruschini N. Cambra F.J. Campistol J. Decreased serum ubiquinone-10 concentrations in phenylketonuria Am. J. Clin. Nutr. 1999 70 892 895 10.1093/ajcn/70.5.892 10539751 · DOI
- [131]Cooper J.M. Korlipara L.V.P. Hart P.E. Bradley J.L. Schapira A.H.V. Coenzyme Q10and vitamin E deficiency in Friedreich’s ataxia: Predictor of efficacy of vitamin E and coenzyme Q10therapy Eur. J. Neurol. 2008 15 1371 1379 10.1111/j.1468-1331.2008.02318.x 19049556 · DOI
- [132]Colomé C. Artuch R. Vilaseca M.A. Sierra C. Brandi N. Cambra F.J. Lambruschini N. Campistol J. Ubiquinone-10 content in lymphocytes of phenylketonuric patients Clin. Biochem. 2002 35 81 84 10.1016/S0009-9120(02)00278-3 11937084 · DOI
- [133]Steen G. Axelsson H. Bowallius M. Holthuis N. Molander B.-M. Isoprenoid biosynthesis in multiple sclerosis, II. A possible role of NADPH Acta Neurol. Scand. 1987 76 461 467 10.1111/j.1600-0404.1987.tb03603.x 2829495 · DOI
- [135]Miles M.V. Tang P.H. Miles L. Steele P.E. Moye M.J. Horn P.S. Validation and application of an HPLC-EC method for analysis of coenzyme Q10 in blood platelets Biomed. Chromatogr. 2008 22 1403 1408 10.1002/bmc.1072 18655217 · DOI
- [137]Crane F.L. Discovery of ubiquinone (coenzyme Q) and an overview of function Mitochondrion 2007 7 S2 S7 10.1016/j.mito.2007.02.011 17446142 · DOI
- [138]Ogasahara S. Engel A.G. Frens D. Mack D. Muscle coenzyme Q deficiency in familial mitochondrial encephalomyopathy Proc. Natl. Acad. Sci. USA 1989 86 2379 2382 10.1073/pnas.86.7.2379 2928337 PMC286916 · DOI
- [139]Montero R. Artuch R. Briones P. Nascimento A. García-Cazorla A. Vilaseca M. Śnchez-Alćzar J. Navas P. Montoya J. Pineda M. Muscle coenzyme Q10 concentrations in patients with probable and definite diagnosis of respiratory chain disorders BioFactors 2005 25 109 115 10.1002/biof.5520250112 16873935 · DOI
- [140]Miles M.V. Miles L. Tang P.H. Horn P.S. Steele P.E. DeGrauw A.J. Wong B.L. Bove K.E. Systematic evaluation of muscle coenzyme Q10 content in children with mitochondrial respiratory chain enzyme deficiencies Mitochondrion 2008 8 170 180 10.1016/j.mito.2008.01.003 18313367 · DOI
- [141]Louw R. Smuts I. Wilsenach K.-L. Jonck L.-M. Schoonen M. van der Westhuizen F. The dilemma of diagnosing coenzyme Q10 deficiency in muscle Mol. Genet. Metab. 2018 125 38 43 10.1016/j.ymgme.2018.02.015 29530532 · DOI
- [142]Vega A.F. de la Mata M. Pavon A.D. Alcocer-Gomez E. Calero C.P. Paz M.V. Alanis M. de Lavera I. Clinical applications of coenzyme Q10 Front Biosci 2014 19 619 633 24389208
- [143]Neergheen V. Chalasani A. Wainwright L. Yubero D. Montero R. Artuch R. Hargreaves I. Coenzyme Q10 in the Treatment of Mitochondrial Disease J. Inborn Errors Metab. Screen. 2017 5 10.1177/2326409817707771 · DOI
- [144]Gutierrez-Mariscal F.M. Larriva A.P.A.-D. Limia-Perez L. Romero-Cabrera J.L. Yubero-Serrano E.M. López-Miranda J. Coenzyme Q10 Supplementation for the Reduction of Oxidative Stress: Clinical Implications in the Treatment of Chronic Diseases Int. J. Mol. Sci. 2020 21 7870 10.3390/ijms21217870 33114148 PMC7660335 · DOI · Paper page
- [145]Pravst I. Rodriguez Aguilera J.C. Cortes Rodriguez A.B. Jazbar J. Locatelli I. Hristov H. Žmitek K. Comparative Bioavailability of Different Coenzyme Q10 Formulations in Healthy Elderly Individuals Nutrients 2020 12 784 10.3390/nu12030784 PMC7146408 32188111 · DOI
- [146]Li H. Chen F. Preparation and quality evaluation of coenzyme Q10 long-circulating liposomes Saudi J. Biol. Sci. 2015 24 797 802 10.1016/j.sjbs.2015.10.025 28490948 PMC5415142 · DOI
- [147]Zhou H. Liu G. Zhang J. Sun N. Duan M. Yan Z. Xia Q. Novel Lipid-Free Nanoformulation for Improving Oral Bioavailability of Coenzyme Q10 BioMed Res. Int. 2014 2014 793879 10.1155/2014/793879 24995328 PMC4068099 · DOI
- [148]Masotta N.E. Martinefski M.R. Lucangioli S. Rojas A.M. Tripodi V.P. High-dose coenzyme Q10-loaded oleogels for oral therapeutic supplementation Int. J. Pharm. 2018 556 9 20 10.1016/j.ijpharm.2018.12.003 30529659 · DOI
- [149]Yang H. Song J. Inclusion of coenzyme Q10 with beta-cyclodextrin studied by polarography Yao Xue Xue Bao 2006 41 671 674 17007363
- [150]Manzar H. Abdulhussein D. Yap T. Cordeiro M. Cellular Consequences of Coenzyme Q10 Deficiency in Neurodegeneration of the Retina and Brain Int. J. Mol. Sci. 2020 21 9299 10.3390/ijms21239299 PMC7730520 33291255 · DOI
- [151]Löw H. Crane F.L. Morré D.J. Putting together a plasma membrane NADH oxidase: A tale of three labor-atories Int. J. Biochem. Cell Biol. 2012 44 1834 1838 10.1016/j.biocel.2012.06.032 22750028 · DOI
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Kovacic, S., Habicht, S. D., & Eckert, G. P. (2025) · Journal of Nutritional Science · doi:10.1017/jns.2025.10043 · Cited by 4 · see citing works
“(16,18,19) Mitochondrial dysfunction in muscle cells can lead to altered biochemical parameters such as a higher lactate to pyruvate ratio (L/P ratio), but also to development of myopathic symptoms.”
- Authors
- Pallotti, F., Bergamini, C., Lamperti, C., & Fato, R.
- Affiliations
- University of Insubria (IT)
- University of Bologna (IT)
- Fondazione IRCCS Istituto Neurologico Carlo Besta (IT)
- Corresponding author
- Pallotti, Francesco
- Bergamini, Christian
- Venue
- International Journal of Molecular Sciences
- Publisher
- MDPI AG
- Published
- 2021-12-23
- Volume
- 23
- Issue
- 1
- Pages
- 128
- ISSN
- 1422-0067 (ISSN-L)
- PMC
- PMC8745647
- OpenAlex
- W4200403055
- Cited by
- 109
- References
- 12
- Citations by year
- 2026: 18 · 2025: 33 · 2024: 26 · 2023: 25 · 2022: 7
- FWCI
- 1.52
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- International Journal of Molecular Sciences (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Archivio istituzionale della ricerca (Alma Mater Studiorum Università di Bologna) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- IrInSubria (University of Insubria) (submittedVersion, cc-by)
- Funders
- Ministero della Salute
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Coenzyme Q10 studies and effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Keywords
- coenzyme Q10, mitochondrial respiration, electron transport chain, electron transport, ferroptosis, lipid peroxidation, free radicals, aging, low-density lipoprotein, disease, therapeutic applications
- MeSH terms
- Animals, Ataxia, Cell Membrane, Humans, Mitochondria, Ubiquinone, Lipid Peroxidation, Muscle Weakness, Cell Respiration, Mitochondrial Diseases
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