{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T14:27:24Z","timestamp":1791901644481,"version":"4.3.4"},"reference-count":249,"publisher":"MDPI AG","issue":"2","license":[{"start":{"date-parts":[[2026,2,14]],"date-time":"2026-02-14T00:00:00Z","timestamp":1771027200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biomolecules"],"abstract":"<jats:p>Coenzyme Q10 (CoQ10) is an essential lipid-soluble molecule that plays a central role in mitochondrial energy production as a mobile electron carrier. In addition to its bioenergetic function, CoQ10 participates in antioxidant defense, redox homeostasis, lipid and nucleotide metabolism, and mitochondrial quality control. Primary CoQ10 deficiencies are rare inherited mitochondrial disorders caused by pathogenic variants in nuclear genes involved in CoQ10 biosynthesis. These defects lead to reduced CoQ10 levels and impaired mitochondrial functions. Clinically, primary CoQ10 deficiencies display remarkable phenotypic heterogeneity, ranging from isolated organ involvement, notably renal or cerebellar disease, to severe multisystemic disorders affecting the nervous system, skeletal muscle, heart, and other organs. Disease onset spans from the antenatal period to adulthood, and clinical severity varies widely, even among patients carrying variants in the same gene. This diversity cannot be fully explained by defective ATP production alone. Growing evidence indicates that disruption of non-bioenergetic functions of CoQ10, including oxidative stress regulation and CoQ-dependent metabolic pathways, contributes significantly to disease pathophysiology and tissue vulnerability. In this review, we summarize current knowledge on CoQ10 biology, biosynthesis, and the clinical spectrum of primary CoQ10 deficiencies, and we discuss emerging mechanisms linking CoQ10 depletion to mitochondrial dysfunctions and human diseases.<\/jats:p>","DOI":"10.3390\/biom16020302","type":"journal-article","created":{"date-parts":[[2026,2,16]],"date-time":"2026-02-16T12:37:28Z","timestamp":1771245448000},"page":"302","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Mitochondrial Dysfunctions in Human Primary Coenzyme Q10 Deficiencies"],"prefix":"10.3390","volume":"16","author":[{"ORCID":"https:\/\/orcid.org\/0009-0004-1988-1925","authenticated-orcid":false,"given":"Fanny","family":"Fontaine","sequence":"first","affiliation":[{"name":"Department of Clinical Biochemistry, CHU Caen Normandie, CS 30001, 14033 Caen Cedex, France"},{"name":"UMRS 1237\u2014Physiopathologie et Imagerie des Troubles Neurologiques (PHIND), Universit\u00e9 de Caen Basse-Normandie, 14000 Caen, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0005-3320-7571","authenticated-orcid":false,"given":"Romain","family":"P\u00e9nicaud","sequence":"additional","affiliation":[{"name":"Department of Clinical Biochemistry, CHU Caen Normandie, CS 30001, 14033 Caen Cedex, France"},{"name":"UMRS 1237\u2014Physiopathologie et Imagerie des Troubles Neurologiques (PHIND), Universit\u00e9 de Caen Basse-Normandie, 14000 Caen, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3134-7501","authenticated-orcid":false,"given":"St\u00e9phane","family":"Allouche","sequence":"additional","affiliation":[{"name":"Department of Clinical Biochemistry, CHU Caen Normandie, CS 30001, 14033 Caen Cedex, France"},{"name":"UMRS 1237\u2014Physiopathologie et Imagerie des Troubles Neurologiques (PHIND), Universit\u00e9 de Caen Basse-Normandie, 14000 Caen, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,2,14]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"558","DOI":"10.1042\/bj0590558","article-title":"A constituent of the unsaponifiable portion of animal tissue lipids (lambda max. 272 m mu)","volume":"59","author":"Festenstein","year":"1955","journal-title":"Biochem. J."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1016\/0006-3002(57)90457-2","article-title":"Isolation of a quinone from beef heart mitochondria","volume":"25","author":"Crane","year":"1957","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"4751","DOI":"10.1021\/ja01550a095","article-title":"COENZYME Q: A NEW GROUP OF QUINONES1","volume":"80","author":"Lester","year":"1958","journal-title":"J. Am. Chem. Soc."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"4752","DOI":"10.1021\/ja01550a096","article-title":"COENZYME Q. I. STRUCTURE STUDIES ON THE COENZYME Q GROUP","volume":"80","author":"Wolf","year":"1958","journal-title":"J. Am. Chem. Soc."},{"key":"ref_5","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":"Aberg","year":"1992","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_6","first-page":"380","article-title":"[Distribution of ubiquinones (coenzyme Q) in Gram negative bacillae]","volume":"169","author":"Denis","year":"1975","journal-title":"Comptes Rendus Seances Soc. Biol. Fil."},{"key":"ref_7","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_8","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":"2004","journal-title":"Biochim. Biophys. Acta (BBA)-Biomembr."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"2089","DOI":"10.1093\/jn\/126.9.2089","article-title":"Restricted uptake of dietary coenzyme Q is in contrast to the unrestricted uptake of alpha-tocopherol into rat organs and cells","volume":"126","author":"Zhang","year":"1996","journal-title":"J. Nutr."},{"key":"ref_10","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\/CoQ10 ratio as a possible marker of increased risk for atherosclerosis","volume":"9","author":"Tomasetti","year":"1999","journal-title":"BioFactors"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"504","DOI":"10.1139\/o92-078","article-title":"Localization and preferred orientations of ubiquinone homologs in model bilayers","volume":"70","author":"Lenaz","year":"1992","journal-title":"Biochem. Cell Biol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/j.chemphyslip.2004.04.007","article-title":"Active oxygen chemistry within the liposomal bilayer. Part III: Locating Vitamin E, ubiquinol and ubiquinone and their derivatives in the lipid bilayer","volume":"131","author":"Afri","year":"2004","journal-title":"Chem. Phys. Lipids"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"2116","DOI":"10.1016\/j.bbamem.2016.06.016","article-title":"Distribution and dynamics of quinones in the lipid bilayer mimicking the inner membrane of mitochondria","volume":"1858","author":"Kaurola","year":"2016","journal-title":"Biochim. Biophys. Acta (BBA)-Biomembr."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1560","DOI":"10.1016\/j.bbabio.2015.08.001","article-title":"Partition, orientation and mobility of ubiquinones in a lipid bilayer","volume":"1847","author":"Galassi","year":"2015","journal-title":"Biochim. Biophys. Acta (BBA)-Bioenerg."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"S103","DOI":"10.1016\/j.mito.2007.03.006","article-title":"Coenzyme Q, oxidative stress and aging","volume":"7","author":"Sohal","year":"2007","journal-title":"Mitochondrion"},{"key":"ref_16","doi-asserted-by":"crossref","unstructured":"Garrido-Maraver, J. (2014). Clinical applications of coenzyme Q10. Front. Biosci., 19.","DOI":"10.2741\/4231"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"S251","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_18","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1159\/000362390","article-title":"Biochemical diagnosis of coenzyme q10 deficiency","volume":"5","author":"Yubero","year":"2014","journal-title":"Mol. Syndromol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1080\/10715760600617843","article-title":"Coenzyme Q10: Absorption, tissue uptake, metabolism and pharmacokinetics","volume":"40","author":"Bhagavan","year":"2006","journal-title":"Free Radic. Res."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"S72","DOI":"10.1016\/j.mito.2007.02.012","article-title":"The uptake and distribution of coenzyme Q10","volume":"7","author":"Miles","year":"2007","journal-title":"Mitochondrion"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.yrtph.2006.07.001","article-title":"Study on safety and bioavailability of ubiquinol (Kaneka QH) after single and 4-week multiple oral administration to healthy volunteers","volume":"47","author":"Hosoe","year":"2007","journal-title":"Regul. Toxicol. Pharmacol. RTP"},{"key":"ref_22","first-page":"536","article-title":"Pharmacokinetic study of deuterium-labelled coenzyme Q10 in man","volume":"24","author":"Tomono","year":"1986","journal-title":"Int. J. Clin. Pharmacol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1002\/biof.5520090205","article-title":"Metabolism of coenzyme Q10: Biliary and urinary excretion study in guinea pigs","volume":"9","author":"Nakamura","year":"1999","journal-title":"BioFactors"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1016\/S0891-5849(02)01357-6","article-title":"Distribution and breakdown of labeled coenzyme Q10 in rat","volume":"34","author":"Bentinger","year":"2003","journal-title":"Free Radic. Biol. Med."},{"key":"ref_25","doi-asserted-by":"crossref","unstructured":"Paredes-Fuentes, A.J., Montero, R., Codina, A., Jou, C., Fern\u00e1ndez, G., Maynou, J., Santos-Oca\u00f1a, C., Riera, J., Navas, P., and Drobnic, F. (2020). Coenzyme Q10 Treatment Monitoring in Different Human Biological Samples. Antioxidants, 9.","DOI":"10.3390\/antiox9100979"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1016\/S0140-6736(00)02531-9","article-title":"Quinone-responsive multiple respiratory-chain dysfunction due to widespread coenzyme Q10 deficiency","volume":"356","author":"Appelkvist","year":"2000","journal-title":"Lancet"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"824","DOI":"10.1016\/j.tibs.2017.06.008","article-title":"Biochemistry of Mitochondrial Coenzyme Q Biosynthesis","volume":"42","author":"Stefely","year":"2017","journal-title":"Trends Biochem. Sci."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1038\/s41929-023-01087-z","article-title":"In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis","volume":"7","author":"Nicoll","year":"2024","journal-title":"Nat. Catal."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"3775","DOI":"10.1016\/j.molcel.2021.08.030","article-title":"Metabolic channeling: Predictions, deductions, and evidence","volume":"81","author":"Pareek","year":"2021","journal-title":"Mol. Cell"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1146\/annurev.biochem.76.052705.163409","article-title":"Translocation of proteins into mitochondria","volume":"76","author":"Neupert","year":"2007","journal-title":"Annu. Rev. Biochem."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1016\/j.tibs.2022.12.006","article-title":"Coenzyme Q biochemistry and biosynthesis","volume":"48","author":"Guerra","year":"2023","journal-title":"Trends Biochem. Sci."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"1004","DOI":"10.1016\/j.bbabio.2014.01.015","article-title":"Biosynthesis and physiology of coenzyme Q in bacteria","volume":"1837","author":"Aussel","year":"2014","journal-title":"Biochim. Biophys. Acta (BBA)-Bioenerg."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1042\/EBC20170106","article-title":"Coenzyme Q10 deficiencies: Pathways in yeast and humans","volume":"62","author":"Awad","year":"2018","journal-title":"Essays Biochem."},{"key":"ref_34","doi-asserted-by":"crossref","unstructured":"Fern\u00e1ndez-Del-R\u00edo, L., and Clarke, C.F. (2021). Coenzyme Q Biosynthesis: An Update on the Origins of the Benzenoid Ring and Discovery of New Ring Precursors. Metabolites, 11.","DOI":"10.3390\/metabo11060385"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1038\/s41586-021-03865-w","article-title":"The polar oxy-metabolome reveals the 4-hydroxymandelate CoQ10 synthesis pathway","volume":"597","author":"Banh","year":"2021","journal-title":"Nature"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"1191","DOI":"10.1038\/nbt.3683","article-title":"Mitochondrial protein functions elucidated by multi-omic mass spectrometry profiling","volume":"34","author":"Stefely","year":"2016","journal-title":"Nat. Biotechnol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"909","DOI":"10.1194\/jlr.M057919","article-title":"Resveratrol and para-coumarate serve as ring precursors for coenzyme Q biosynthesis","volume":"56","author":"Xie","year":"2015","journal-title":"J. Lipid Res."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1016\/j.freeradbiomed.2017.06.006","article-title":"Kaempferol increases levels of coenzyme Q in kidney cells and serves as a biosynthetic ring precursor","volume":"110","author":"Nag","year":"2017","journal-title":"Free Radic. Biol. Med."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"16067","DOI":"10.3390\/ijms160716067","article-title":"Mevalonate Pathway Blockade, Mitochondrial Dysfunction and Autophagy: A Possible Link","volume":"16","author":"Tricarico","year":"2015","journal-title":"Int. J. Mol. Sci."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"13157","DOI":"10.1016\/S0021-9258(19)38280-8","article-title":"Elucidation of the deficiency in two yeast coenzyme Q mutants. Characterization of the structural gene encoding hexaprenyl pyrophosphate synthetase","volume":"265","author":"Ashby","year":"1990","journal-title":"J. Biol. Chem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"5606","DOI":"10.1111\/j.1742-4658.2005.04956.x","article-title":"Characterization of solanesyl and decaprenyl diphosphate synthases in mice and humans","volume":"272","author":"Saiki","year":"2005","journal-title":"FEBS J."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"4128","DOI":"10.1016\/S0021-9258(19)50638-X","article-title":"COQ2 is a candidate for the structural gene encoding para-hydroxybenzoate:polyprenyltransferase","volume":"267","author":"Ashby","year":"1992","journal-title":"J. Biol. Chem."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1042\/BJ20040261","article-title":"Isolation and functional expression of human COQ2, a gene encoding a polyprenyl transferase involved in the synthesis of CoQ","volume":"382","author":"Forsgren","year":"2004","journal-title":"Biochem. J."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"4256","DOI":"10.1093\/hmg\/ddw257","article-title":"The COQ2 genotype predicts the severity of coenzyme Q10 deficiency","volume":"25","author":"Desbats","year":"2016","journal-title":"Hum. Mol. Genet."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"902","DOI":"10.1002\/acn3.486","article-title":"4-Hydroxybenzoic acid restores CoQ10 biosynthesis in human COQ2 deficiency","volume":"4","author":"Herebian","year":"2017","journal-title":"Ann. Clin. Transl. Neurol."},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Pierrel, F. (2017). Impact of Chemical Analogs of 4-Hydroxybenzoic Acid on Coenzyme Q Biosynthesis: From Inhibition to Bypass of Coenzyme Q Deficiency. Front. Physiol., 8.","DOI":"10.3389\/fphys.2017.00436"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0304-4165(67)90239-5","article-title":"Methionine as the source of methyl groups for ubiquinone and vitamin K: A study using nuclear magnetic resonance and mass spectrometry","volume":"141","author":"Jackman","year":"1967","journal-title":"Biochim. Biophys. Acta (BBA)-Gen. Subj."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"4745","DOI":"10.1021\/bi00615a023","article-title":"Three hydroxylations incorporating molecular oxygen in the aerobic biosynthesis of ubiquinone in Escherichia coli","volume":"17","author":"Alexander","year":"1978","journal-title":"Biochemistry"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"25308","DOI":"10.1074\/jbc.M303234200","article-title":"The Saccharomyces cerevisiae COQ6 gene encodes a mitochondrial flavin-dependent monooxygenase required for coenzyme Q biosynthesis","volume":"278","author":"Gin","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"981","DOI":"10.1016\/j.molcel.2024.01.003","article-title":"COQ4 is required for the oxidative decarboxylation of the C1 carbon of coenzyme Q in eukaryotic cells","volume":"84","author":"Pelosi","year":"2024","journal-title":"Mol. Cell"},{"key":"ref_51","first-page":"69","article-title":"The yeast Coq4 polypeptide organizes a mitochondrial protein complex essential for coenzyme Q biosynthesis","volume":"1791","author":"Marbois","year":"2009","journal-title":"Biochim. Biophys. Acta (BBA)-Mol. Cell Biol. Lipids"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1016\/j.bbrc.2008.04.172","article-title":"Functional characterization of human COQ4, a gene required for Coenzyme Q10 biosynthesis","volume":"372","author":"Casarin","year":"2008","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_53","first-page":"3904905","article-title":"Vanillic Acid Restores Coenzyme Q Biosynthesis and ATP Production in Human Cells Lacking COQ6","volume":"2019","author":"Trevisson","year":"2019","journal-title":"Oxidative Med. Cell. Longev."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"2995","DOI":"10.1074\/jbc.271.6.2995","article-title":"The COQ7 gene encodes a protein in saccharomyces cerevisiae necessary for ubiquinone biosynthesis","volume":"271","author":"Marbois","year":"1996","journal-title":"J. Biol. Chem."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"33297","DOI":"10.1074\/jbc.C100346200","article-title":"A new member of the family of di-iron carboxylate proteins. Coq7 (clk-1), a membrane-bound hydroxylase involved in ubiquinone biosynthesis","volume":"276","author":"Stenmark","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"2329","DOI":"10.1111\/jcmm.13154","article-title":"Pathogenicity of two COQ7 mutations and responses to 2,4-dihydroxybenzoate bypass treatment","volume":"21","author":"Wang","year":"2017","journal-title":"J. Cell. Mol. Med."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"3470","DOI":"10.1093\/brain\/awac453","article-title":"Homozygous COQ7 mutation: A new cause of potentially treatable distal hereditary motor neuropathy","volume":"146","author":"Jacquier","year":"2023","journal-title":"Brain"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"16636","DOI":"10.1016\/S0021-9258(18)55349-7","article-title":"Ubiquinone biosynthesis in Saccharomyces cerevisiae. Isolation and sequence of COQ3, the 3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase gene","volume":"266","author":"Clarke","year":"1991","journal-title":"J. Biol. Chem."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"12381","DOI":"10.1074\/jbc.275.17.12381","article-title":"Isolation and functional expression of human COQ3, a gene encoding a methyltransferase required for ubiquinone biosynthesis","volume":"275","author":"Jonassen","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_60","first-page":"1628","article-title":"Molecular characterization of the human COQ5 C-methyltransferase in coenzyme Q10 biosynthesis","volume":"1841","author":"Nguyen","year":"2014","journal-title":"Biochim. Biophys. Acta (BBA)-Mol. Cell Biol. Lipids"},{"key":"ref_61","first-page":"630","article-title":"Coenzyme Q supplementation or over-expression of the yeast Coq8 putative kinase stabilizes multi-subunit Coq polypeptide complexes in yeast coq null mutants","volume":"1841","author":"He","year":"2014","journal-title":"Biochim. Biophys. Acta (BBA)-Mol. Cell Biol. Lipids"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"148192","DOI":"10.1016\/j.bbabio.2020.148192","article-title":"Characterization of human mitochondrial PDSS and COQ proteins and their roles in maintaining coenzyme Q10 levels and each other\u2019s stability","volume":"1861","author":"Yen","year":"2020","journal-title":"Biochim. Biophys. Acta (BBA)-Bioenerg."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"1864","DOI":"10.1016\/j.bbagen.2016.05.005","article-title":"Disruption of the human COQ5-containing protein complex is associated with diminished coenzyme Q10 levels under two different conditions of mitochondrial energy deficiency","volume":"1860","author":"Yen","year":"2016","journal-title":"Biochim. Biophys. Acta (BBA)-Gen. Subj."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1016\/j.chembiol.2017.11.001","article-title":"Conserved Lipid and Small-Molecule Modulation of COQ8 Reveals Regulation of the Ancient Kinase-like UbiB Family","volume":"25","author":"Reidenbach","year":"2018","journal-title":"Cell Chem. Biol."},{"key":"ref_65","doi-asserted-by":"crossref","unstructured":"V\u00e1zquez-Fonseca, L., Schaefer, J., Navas-Enamorado, I., Santos-Oca\u00f1a, C., Hern\u00e1ndez-Camacho, J.D., Guerra, I., Cascajo, M.V., S\u00e1nchez-Cuesta, A., Horvath, Z., and Siendones, E. (2019). ADCK2 Haploinsufficiency Reduces Mitochondrial Lipid Oxidation and Causes Myopathy Associated with CoQ Deficiency. J. Clin. Med., 8.","DOI":"10.20944\/preprints201908.0069.v1"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"E4697","DOI":"10.1073\/pnas.1413128111","article-title":"Mitochondrial COQ9 is a lipid-binding protein that associates with COQ7 to enable coenzyme Q biosynthesis","volume":"111","author":"Lohman","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"4307","DOI":"10.1016\/j.molcel.2022.10.003","article-title":"Structure and functionality of a multimeric human COQ7:COQ9 complex","volume":"82","author":"Manicki","year":"2022","journal-title":"Mol. Cell"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"997","DOI":"10.1038\/s41431-025-01895-w","article-title":"Homozygous COQ9 mutation: A new cause of potentially treatable hereditary spastic paraplegia","volume":"33","author":"Fontaine","year":"2025","journal-title":"Eur. J. Hum. Genet. EJHG"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"1293","DOI":"10.1194\/jlr.M093534","article-title":"Human COQ10A and COQ10B are distinct lipid-binding START domain proteins required for coenzyme Q function","volume":"60","author":"Tsui","year":"2019","journal-title":"J. Lipid Res."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"350","DOI":"10.1016\/j.jnutbio.2008.04.005","article-title":"Characterization of cellular uptake and distribution of coenzyme Q10 and vitamin E in PC12 cells","volume":"20","author":"Saito","year":"2009","journal-title":"J. Nutr. Biochem."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"85","DOI":"10.3164\/jcbn.13-106","article-title":"Prosaposin regulates coenzyme Q10 levels in HepG2 cells, especially those in mitochondria","volume":"55","author":"Kashiba","year":"2014","journal-title":"J. Clin. Biochem. Nutr."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"504","DOI":"10.1016\/j.cell.2013.01.013","article-title":"Ubiad1 Is an Antioxidant Enzyme that Regulates eNOS Activity by CoQ10 Synthesis","volume":"152","author":"Mugoni","year":"2013","journal-title":"Cell"},{"key":"ref_73","first-page":"246","article-title":"Mitochondria regulate intracellular coenzyme Q transport and ferroptotic resistance via STARD7","volume":"25","author":"Deshwal","year":"2023","journal-title":"Nat. Cell Biol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"e70378","DOI":"10.1111\/cns.70378","article-title":"Mitochondria-Associated Membranes: A Key Point of Neurodegenerative Diseases","volume":"31","author":"Zhang","year":"2025","journal-title":"CNS Neurosci. Ther."},{"key":"ref_75","first-page":"428","article-title":"Prenatal Diagnosis of Lissencephaly Associated with Biallelic Pathologic Variants in the COQ2 Gene","volume":"36","author":"Rodrigues","year":"2023","journal-title":"Acta Med. Port."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1136\/jmedgenet-2015-103140","article-title":"Mutations in COQ4, an essential component of coenzyme Q biosynthesis, cause lethal neonatal mitochondrial encephalomyopathy","volume":"52","author":"Chung","year":"2015","journal-title":"J. Med. Genet."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"1047","DOI":"10.1002\/jimd.12776","article-title":"New variants expand the neurological phenotype of COQ7 deficiency","volume":"47","author":"Fabra","year":"2024","journal-title":"J. Inherit. Metab. Dis."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"938","DOI":"10.1038\/s41431-024-01615-w","article-title":"COQ7 defect causes prenatal onset of mitochondrial CoQ10 deficiency with cardiomyopathy and gastrointestinal obstruction","volume":"32","author":"Pettenuzzo","year":"2024","journal-title":"Eur. J. Hum. Genet."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"719","DOI":"10.1007\/s10545-017-0122-7","article-title":"A family segregating lethal neonatal coenzyme Q10 deficiency caused by mutations in COQ9","volume":"41","author":"Smith","year":"2018","journal-title":"J. Inherit. Metab. Dis."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/j.jns.2013.01.004","article-title":"A novel mutation in COQ2 leading to fatal infantile multisystem disease","volume":"326","author":"Jakobs","year":"2013","journal-title":"J. Neurol. Sci."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1016\/j.ejpn.2013.05.013","article-title":"Early myoclonic epilepsy, hypertrophic cardiomyopathy and subsequently a nephrotic syndrome in a patient with CoQ10 deficiency caused by mutations in para-hydroxybenzoate-polyprenyl transferase (COQ2)","volume":"17","author":"Scalais","year":"2013","journal-title":"Eur. J. Paediatr. Neurol."},{"key":"ref_82","doi-asserted-by":"crossref","unstructured":"Pan, P., Zhou, N., Sun, Y., Chen, Z., Han, J., and Zhou, W. (2024). The Spectrum of clinical manifestations in newborns with the COQ4 mutation: Case series and literature review. Front. Pediatr., 12.","DOI":"10.3389\/fped.2024.1410133"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1016\/j.ajhg.2014.12.023","article-title":"COQ4 Mutations Cause a Broad Spectrum of Mitochondrial Disorders Associated with CoQ10 Deficiency","volume":"96","author":"Haack","year":"2015","journal-title":"Am. J. Hum. Genet."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1038\/s41525-019-0091-x","article-title":"Primary coenzyme Q10 deficiency-7: Expanded phenotypic spectrum and a founder mutation in southern Chinese","volume":"4","author":"Yu","year":"2019","journal-title":"npj Genom. Med."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"592","DOI":"10.1016\/j.kint.2022.02.040","article-title":"Variation of the clinical spectrum and genotype-phenotype associations in Coenzyme Q10 deficiency associated glomerulopathy","volume":"102","author":"Drovandi","year":"2022","journal-title":"Kidney Int."},{"key":"ref_86","first-page":"23","article-title":"A fatal case of COQ7-associated primary coenzyme Q10 deficiency","volume":"47","author":"Kwong","year":"2019","journal-title":"JIMD Rep."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"558","DOI":"10.1016\/j.ajhg.2009.03.018","article-title":"A Nonsense Mutation in COQ9 Causes Autosomal-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_88","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1038\/ejhg.2015.133","article-title":"Fatal neonatal encephalopathy and lactic acidosis caused by a homozygous loss-of-function variant in COQ9","volume":"24","author":"Danhauser","year":"2016","journal-title":"Eur. J. Hum. Genet."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"1422","DOI":"10.1093\/brain\/awab041","article-title":"Biallelic variants in HPDL cause pure and complicated hereditary spastic paraplegia","volume":"144","author":"Wiessner","year":"2021","journal-title":"Brain J. Neurol."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1016\/j.jgg.2021.01.009","article-title":"HPDL deficiency causes a neuromuscular disease by impairing the mitochondrial respiration","volume":"48","author":"Sun","year":"2021","journal-title":"J. Genet. Genomics"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"524","DOI":"10.1038\/s41436-020-01010-y","article-title":"Biallelic variants in HPDL, encoding 4-hydroxyphenylpyruvate dioxygenase-like protein, lead to an infantile neurodegenerative condition","volume":"23","author":"Ghosh","year":"2021","journal-title":"Genet. Med."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"364","DOI":"10.1016\/j.ajhg.2020.06.015","article-title":"Bi-allelic HPDL Variants Cause a Neurodegenerative Disease Ranging from Neonatal Encephalopathy to Adolescent-Onset Spastic Paraplegia","volume":"107","author":"Husain","year":"2020","journal-title":"Am. J. Hum. Genet."},{"key":"ref_93","doi-asserted-by":"crossref","unstructured":"Baggiani, M., Damiani, D., Privitera, F., Della Vecchia, S., Tessa, A., and Santorelli, F.M. (2024). Generation and Characterization of hiPS Lines from Three Patients Affected by Different Forms of HPDL-Related Neurological Disorders. Int. J. Mol. Sci., 25.","DOI":"10.3390\/ijms251910614"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1086\/500092","article-title":"A Mutation in Para-Hydroxybenzoate-Polyprenyl Transferase (COQ2) Causes Primary Coenzyme Q10 Deficiency","volume":"78","author":"Quinzii","year":"2006","journal-title":"Am. J. Hum. Genet."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"440","DOI":"10.1002\/ajmg.a.61983","article-title":"Clinical spectrum in multiple families with primary COQ10 deficiency","volume":"185","author":"Hashemi","year":"2021","journal-title":"Am. J. Med. Genet. Part A."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1007\/s12311-019-01011-x","article-title":"COQ4 Mutation Leads to Childhood-Onset Ataxia Improved by CoQ10 Administration","volume":"18","author":"Caglayan","year":"2019","journal-title":"Cerebellum"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1002\/ana.25751","article-title":"Clinico-Genetic, Imaging and Molecular Delineation of COQ8A-Ataxia: A Multicenter Study of 59 Patients","volume":"88","author":"Schirinzi","year":"2020","journal-title":"Ann. Neurol."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/j.ejpn.2011.07.016","article-title":"The use of muscle biopsy in the diagnosis of undefined ataxia with cerebellar atrophy in children","volume":"16","author":"Terracciano","year":"2012","journal-title":"Eur. J. Paediatr. Neurol."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1515\/jpem-2019-0245","article-title":"A rare case of primary coenzyme Q10 deficiency due to COQ9 mutation","volume":"33","author":"Olgac","year":"2020","journal-title":"J. Pediatr. Endocrinol. Metab. JPEM"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"959","DOI":"10.1111\/jdi.70022","article-title":"Two cases of neonatal hyperglycemia caused by a homozygous COQ9 stop-gain variant","volume":"16","author":"Donis","year":"2025","journal-title":"J. Diabetes Investig."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1002\/humu.23345","article-title":"A novel inborn error of the coenzyme Q10 biosynthesis pathway: Cerebellar ataxia and static encephalomyopathy due to COQ5 C-methyltransferase deficiency","volume":"39","author":"Malicdan","year":"2018","journal-title":"Hum. Mutat."},{"key":"ref_102","doi-asserted-by":"crossref","unstructured":"Wang, N., Zheng, Y., Zhang, L., Tian, X., Fang, Y., Qi, M., Du, J., Chen, S., Chen, S., and Li, J. (2021). A Family Segregating Lethal Primary Coenzyme Q10 Deficiency Due to Two Novel COQ6 Variants. Front. Genet., 12.","DOI":"10.3389\/fgene.2021.811833"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1007\/s12041-024-01477-7","article-title":"COQ7 splice site variant causing a spastic paraparesis phenotype in siblings","volume":"103","author":"Sait","year":"2024","journal-title":"J. Genet."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"1583","DOI":"10.1007\/s00467-024-06596-y","article-title":"PDSS1 mutations-associated steroid-resistant nephrotic syndrome: Case report and review of literature","volume":"40","author":"Habib","year":"2025","journal-title":"Pediatr. Nephrol."},{"key":"ref_105","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_106","doi-asserted-by":"crossref","first-page":"664","DOI":"10.1007\/s12311-017-0846-9","article-title":"Three-Year Follow-Up of High-Dose Ubiquinol Supplementation in a Case of Familial Multiple System Atrophy with Compound Heterozygous COQ2 Mutations","volume":"16","author":"Mitsui","year":"2017","journal-title":"Cerebellum"},{"key":"ref_107","first-page":"100877","article-title":"A novel COQ7 mutation causing primarily neuromuscular pathology and its treatment options","volume":"31","author":"Wang","year":"2022","journal-title":"Mol. Genet. Metab. Rep."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"e14529","DOI":"10.1111\/cns.14529","article-title":"Biallelic variants in the COQ4 gene caused hereditary spastic paraplegia predominant phenotype","volume":"30","author":"Wei","year":"2024","journal-title":"CNS Neurosci. Ther."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"1067","DOI":"10.1002\/acn3.52037","article-title":"Homozygous variant in COQ7 causes autosomal recessive hereditary spastic paraplegia","volume":"11","author":"Qiu","year":"2024","journal-title":"Ann. Clin. Transl. Neurol."},{"key":"ref_110","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_111","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1002\/acn3.51232","article-title":"Missense PDSS1 mutations in CoenzymeQ10 synthesis cause optic atrophy and sensorineural deafness","volume":"8","author":"Nardecchia","year":"2021","journal-title":"Ann. Clin. Transl. Neurol."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1007\/s00467-017-3814-1","article-title":"Diffuse mesangial sclerosis in a PDSS2 mutation-induced coenzyme Q10 deficiency","volume":"33","author":"Brinyiczki","year":"2018","journal-title":"Pediatr. Nephrol."},{"key":"ref_113","first-page":"3","article-title":"Distal phalangeal erythema in an infant with biallelic PDSS1 mutations: Expanding the phenotype of primary Coenzyme Q10 deficiency","volume":"62","author":"Bellusci","year":"2021","journal-title":"JIMD Rep."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1111\/j.1442-200X.2012.03644.x","article-title":"Next-generation sequencing for mitochondrial diseases: A wide diagnostic spectrum","volume":"54","author":"Vasta","year":"2012","journal-title":"Pediatr. Int."},{"key":"ref_115","first-page":"100800","article-title":"Leigh syndrome-like MRI changes in a patient with biallelic HPDL variants treated with ketogenic diet","volume":"29","author":"Uematsu","year":"2021","journal-title":"Mol. Genet. Metab. Rep."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"4191","DOI":"10.1093\/brain\/awad158","article-title":"Biallelic variants in COQ7 cause distal hereditary motor neuropathy with upper motor neuron signs","volume":"146","author":"Rebelo","year":"2023","journal-title":"Brain"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"e27","DOI":"10.1093\/brain\/awad040","article-title":"Biallelic variants in the COQ7 gene cause distal hereditary motor neuropathy in two Chinese families","volume":"146","author":"Liu","year":"2023","journal-title":"Brain"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"e117","DOI":"10.1093\/brain\/awad212","article-title":"Axonal Charcot-Marie-Tooth disease due to COQ7 mutation: Expanding the genetic and clinical spectrum","volume":"146","author":"Zhang","year":"2023","journal-title":"Brain"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1038\/s41525-022-00330-z","article-title":"Biallelic variants in coenzyme Q10 biosynthesis pathway genes cause a retinitis pigmentosa phenotype","volume":"7","author":"Jurkute","year":"2022","journal-title":"npj Genom. Med."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1136\/jnnp-2011-301258","article-title":"Adult-onset cerebellar ataxia due to mutations in CABC1\/ADCK3","volume":"83","author":"Horvath","year":"2012","journal-title":"J. Neurol. Neurosurg. Psychiatry"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1111\/cge.12742","article-title":"Cerebellar ataxia and severe muscle CoQ10 deficiency in a patient with a novel mutation in ADCK3","volume":"90","author":"Barca","year":"2016","journal-title":"Clin. Genet."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"5179","DOI":"10.1172\/JCI69000","article-title":"ADCK4 mutations promote steroid-resistant nephrotic syndrome through CoQ10 biosynthesis disruption","volume":"123","author":"Ashraf","year":"2013","journal-title":"J. Clin. Investig."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"e8880","DOI":"10.1097\/MD.0000000000008880","article-title":"Coenzyme Q10 supplementation therapy for 2 children with proteinuria renal disease and ADCK4 mutation: Case reports and literature review","volume":"96","author":"Feng","year":"2017","journal-title":"Medicine"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"1181","DOI":"10.1007\/s00467-017-3590-y","article-title":"Spectrum of mutations in Chinese children with steroid-resistant nephrotic syndrome","volume":"32","author":"Wang","year":"2017","journal-title":"Pediatr. Nephrol."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"444","DOI":"10.1016\/j.bbrc.2018.10.102","article-title":"A novel ADCK4 mutation in a Chinese family with ADCK4-Associated glomerulopathy","volume":"506","author":"Yang","year":"2018","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_126","doi-asserted-by":"crossref","unstructured":"Zhai, S., Zhang, L., Sun, B., Zhang, Y., and Ma, Q. (2020). Early-onset COQ8B (ADCK4) glomerulopathy in a child with isolated proteinuria: A case report and literature review. BMC Nephrol., 21.","DOI":"10.1186\/s12882-020-02038-7"},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1186\/s13023-020-01600-8","article-title":"Compound heterozygous inheritance of two novel COQ2 variants results in familial coenzyme Q deficiency","volume":"15","author":"Abdelhakim","year":"2020","journal-title":"Orphanet J. Rare Dis."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1111\/cge.12960","article-title":"Further phenotypic heterogeneity of CoQ10 deficiency associated with steroid resistant nephrotic syndrome and novel COQ2 and COQ6 variants","volume":"92","author":"Gigante","year":"2017","journal-title":"Clin. Genet."},{"key":"ref_129","first-page":"37","article-title":"COQ6 mutation in patients with nephrotic syndrome, sensorineural deafness, and optic atrophy","volume":"54","author":"Garaix","year":"2020","journal-title":"JIMD Rep."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"103621","DOI":"10.1016\/j.ejmg.2019.01.011","article-title":"Primary coenzyme Q10 Deficiency-6 (COQ10D6): Two siblings with variable expressivity of the renal phenotype","volume":"63","author":"Toksoy","year":"2020","journal-title":"Eur. J. Med. Genet."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1080\/0886022X.2020.1864402","article-title":"COQ2 mutation associated isolated nephropathy in two siblings from a Chinese pedigree","volume":"43","author":"Li","year":"2021","journal-title":"Ren. Fail."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"101298","DOI":"10.1016\/j.ajoc.2022.101298","article-title":"Retinitis pigmentosa with optic neuropathy and COQ2 mutations: A case report","volume":"25","author":"Kurata","year":"2022","journal-title":"Am. J. Ophthalmol. Case Rep."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"106822","DOI":"10.1016\/j.nbd.2025.106822","article-title":"iPSC models of mitochondrial diseases","volume":"207","author":"Heiduschka","year":"2025","journal-title":"Neurobiol. Dis."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1016\/j.scr.2016.09.007","article-title":"Generation, genome edition and characterization of iPSC lines from a patient with coenzyme Q 10 deficiency harboring a heterozygous mutation in COQ4 gene","volume":"24","author":"Navas","year":"2017","journal-title":"Stem Cell Res."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"14215","DOI":"10.1038\/s41598-018-32573-1","article-title":"The pathogenesis linked to coenzyme Q10 insufficiency in iPSC-derived neurons from patients with multiple-system atrophy","volume":"8","author":"Nakamoto","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"1073","DOI":"10.1016\/j.bbabio.2016.03.010","article-title":"Coenzyme Q biosynthesis and its role in the respiratory chain structure","volume":"1857","author":"Navas","year":"2016","journal-title":"Biochim. Biophys. Acta (BBA)-Bioenerg."},{"key":"ref_137","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_138","doi-asserted-by":"crossref","first-page":"902","DOI":"10.1016\/j.bbabio.2016.02.013","article-title":"Structure and function of mitochondrial complex I","volume":"1857","author":"Wirth","year":"2016","journal-title":"Biochim. Biophys. Acta (BBA)-Bioenerg."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/j.ymgme.2020.09.009","article-title":"The genetic basis of isolated mitochondrial complex II deficiency","volume":"131","author":"Fullerton","year":"2020","journal-title":"Mol. Genet. Metab."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"788","DOI":"10.1016\/j.bbabio.2011.02.006","article-title":"The Q cycle of cytochrome bc complexes: A structure perspective","volume":"1807","author":"Cramer","year":"2011","journal-title":"Biochim. Biophys. Acta (BBA)-Bioenerg."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"296","DOI":"10.1016\/j.mito.2020.10.004","article-title":"Complex IV\u2014The regulatory center of mitochondrial oxidative phosphorylation","volume":"58","author":"Kadenbach","year":"2021","journal-title":"Mitochondrion"},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1515\/bmc-2019-0001","article-title":"ATP Synthase: Structure, Function and Inhibition","volume":"10","author":"Neupane","year":"2019","journal-title":"Biomol. Concepts"},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1159\/000363364","article-title":"Coenzyme Q and the Respiratory Chain: Coenzyme Q Pool and Mitochondrial Supercomplexes","volume":"5","author":"Enriquez","year":"2014","journal-title":"Mol. Syndromol."},{"key":"ref_144","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_145","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1042\/BST20190930","article-title":"The road to the structure of the mitochondrial respiratory chain supercomplex","volume":"48","author":"Caruana","year":"2020","journal-title":"Biochem. Soc. Trans."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1016\/j.bbabio.2013.11.002","article-title":"Functional role of mitochondrial respiratory supercomplexes","volume":"1837","author":"Genova","year":"2014","journal-title":"Biochim. Biophys. Acta (BBA)-Bioenerg."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"444","DOI":"10.1016\/j.bbabio.2013.12.009","article-title":"The function of the respiratory supercomplexes: The plasticity model","volume":"1837","author":"Enriquez","year":"2014","journal-title":"Biochim. Biophys. Acta (BBA)-Bioenerg."},{"key":"ref_148","doi-asserted-by":"crossref","unstructured":"Bravo-Alonso, I., Navarrete, R., Vega, A.I., Ru\u00edz-Sala, P., Garc\u00eda Silva, M.T., Mart\u00edn-Hern\u00e1ndez, E., Quijada-Fraile, P., Belanger-Quintana, A., Stanescu, S., and Bueno, M. (2019). Genes and Variants Underlying Human Congenital Lactic Acidosis\u2014From Genetics to Personalized Treatment. J. Clin. Med., 8.","DOI":"10.3390\/jcm8111811"},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"3733","DOI":"10.1096\/fj.09-152728","article-title":"Reactive oxygen species, oxidative stress, and cell death correlate with level of CoQ10 deficiency","volume":"24","author":"Quinzii","year":"2010","journal-title":"FASEB J."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"145407","DOI":"10.1016\/j.gene.2021.145407","article-title":"Electron transfer flavoprotein and its role in mitochondrial energy metabolism in health and disease","volume":"776","author":"Henriques","year":"2021","journal-title":"Gene"},{"key":"ref_151","first-page":"e70035","article-title":"Late-Onset Multiple Acyl-CoA Dehydrogenase Deficiency (MADD): A Case Report with a Complex Biochemical Profile","volume":"66","author":"Penicaud","year":"2025","journal-title":"JIMD Rep."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"2037","DOI":"10.1093\/brain\/awm054","article-title":"The myopathic form of coenzyme Q10 deficiency is caused by mutations in the electron-transferring-flavoprotein dehydrogenase (ETFDH) gene","volume":"130","author":"Gempel","year":"2007","journal-title":"Brain J. Neurol."},{"key":"ref_153","doi-asserted-by":"crossref","unstructured":"Turton, N., Cufflin, N., Dewsbury, M., Fitzpatrick, O., Islam, R., Watler, L.L., McPartland, C., Whitelaw, S., Connor, C., and Morris, C. (2022). The Biochemical Assessment of Mitochondrial Respiratory Chain Disorders. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23137487"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"1254","DOI":"10.1038\/ejhg.2014.277","article-title":"Primary coenzyme Q10 deficiency presenting as fatal neonatal multiorgan failure","volume":"23","author":"Desbats","year":"2015","journal-title":"Eur. J. Hum. Genet. EJHG"},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1097\/WCO.0b013e32834ab528","article-title":"Coenzyme Q deficiency in muscle","volume":"24","author":"Trevisson","year":"2011","journal-title":"Curr. Opin. Neurol."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"2402","DOI":"10.1002\/jcsm.13574","article-title":"Prenatal and progressive coenzyme Q10 administration to mitigate muscle dysfunction in mitochondrial disease","volume":"15","author":"Zammit","year":"2024","journal-title":"J. Cachexia Sarcopenia Muscle"},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"96","DOI":"10.15252\/emmm.201606356","article-title":"Coenzyme Q deficiency causes impairment of the sulfide oxidation pathway","volume":"9","author":"Ziosi","year":"2017","journal-title":"EMBO Mol. Med."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1016\/j.bbabio.2012.11.014","article-title":"The function and the role of the mitochondrial glycerol-3-phosphate dehydrogenase in mammalian tissues","volume":"1827","author":"Drahota","year":"2013","journal-title":"Biochim. Biophys. Acta (BBA)-Bioenerg."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1016\/j.freeradbiomed.2025.01.009","article-title":"Coenzyme Q10 deficiency disrupts lipid metabolism by altering cholesterol homeostasis in neurons","volume":"229","author":"Pesini","year":"2025","journal-title":"Free Radic. Biol. Med."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1023\/A:1006859115450","article-title":"Dihydroorotat-ubiquinone oxidoreductase links mitochondria in the biosynthesis of pyrimidine nucleotides","volume":"174","author":"Schuster","year":"1997","journal-title":"Mol. Cell. Biochem."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"165759","DOI":"10.1016\/j.bbadis.2020.165759","article-title":"Dihydroorotate dehydrogenase in oxidative phosphorylation and cancer","volume":"1866","author":"Boukalova","year":"2020","journal-title":"Biochim. Biophys. Acta (BBA)-Mol. Basis Dis."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"500","DOI":"10.1126\/science.2814477","article-title":"Human cells lacking mtDNA: Repopulation with exogenous mitochondria by complementation","volume":"246","author":"King","year":"1989","journal-title":"Science"},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"1091","DOI":"10.1093\/hmg\/ddm058","article-title":"Missense mutation of the COQ2 gene causes defects of bioenergetics and de novo pyrimidine synthesis","volume":"16","author":"Salviati","year":"2007","journal-title":"Hum. Mol. Genet."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"742","DOI":"10.1016\/j.clinbiochem.2008.10.027","article-title":"Coenzyme Q10 deficiency associated with a mitochondrial DNA depletion syndrome: A case report","volume":"42","author":"Montero","year":"2009","journal-title":"Clin. Biochem."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1038\/s41420-021-00591-0","article-title":"Minimal mitochondrial respiration is required to prevent cell death by inhibition of mTOR signaling in CoQ-deficient cells","volume":"7","author":"Wang","year":"2021","journal-title":"Cell Death Discov."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"e1243","DOI":"10.1097\/SCS.0000000000011501","article-title":"Unveiling the Phenotypic Spectrum of Miller Syndrome: A Systematic Review","volume":"36","author":"Ombashi","year":"2025","journal-title":"J. Craniofac. Surg."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"607","DOI":"10.2741\/3947","article-title":"Proline dehydrogenase: A key enzyme in controlling cellular homeostasis","volume":"17","author":"Servet","year":"2012","journal-title":"Front. Biosci."},{"key":"ref_168","doi-asserted-by":"crossref","unstructured":"Pallag, G., Nazarian, S., Ravasz, D., Bui, D., Koml\u00f3di, T., Doerrier, C., Gnaiger, E., Seyfried, T.N., and Chinopoulos, C. (2022). Proline Oxidation Supports Mitochondrial ATP Production When Complex I Is Inhibited. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23095111"},{"key":"ref_169","doi-asserted-by":"crossref","unstructured":"Phang, J.M. (2022). The regulatory mechanisms of proline and hydroxyproline metabolism: Recent advances in perspective. Front. Oncol., 12.","DOI":"10.3389\/fonc.2022.1118675"},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1016\/j.freeradbiomed.2021.02.039","article-title":"The multiple roles of coenzyme Q in cellular homeostasis and their relevance for the pathogenesis of coenzyme Q deficiency","volume":"166","author":"Baschiera","year":"2021","journal-title":"Free Radic. Biol. Med."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1016\/j.abb.2013.07.018","article-title":"Human choline dehydrogenase: Medical promises and biochemical challenges","volume":"537","author":"Salvi","year":"2013","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_172","doi-asserted-by":"crossref","unstructured":"Steane, S.E., Kumar, V., Cuffe, J.S.M., Moritz, K.M., and Akison, L.K. (2022). Prenatal Choline Supplementation Alters One Carbon Metabolites in a Rat Model of Periconceptional Alcohol Exposure. Nutrients, 14.","DOI":"10.3390\/nu14091874"},{"key":"ref_173","doi-asserted-by":"crossref","unstructured":"Li, Y., Shen, X., Yang, X., Lian, F., Li, Y., Li, J., Huang, Y., Shen, W., and Liu, H. (2023). CHDH, a key mitochondrial enzyme, plays a diagnostic role in metabolic disorders diseases and tumor progression. Front. Genet., 14.","DOI":"10.3389\/fgene.2023.1240650"},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"1906","DOI":"10.4161\/auto.32177","article-title":"Choline dehydrogenase interacts with SQSTM1\/p62 to recruit LC3 and stimulate mitophagy","volume":"10","author":"Park","year":"2014","journal-title":"Autophagy"},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"30901","DOI":"10.1074\/jbc.M114.602664","article-title":"Organization of the human mitochondrial hydrogen sulfide oxidation pathway","volume":"289","author":"Libiad","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"6804","DOI":"10.1021\/bi300778t","article-title":"Human sulfide:quinone oxidoreductase catalyzes the first step in hydrogen sulfide metabolism and produces a sulfane sulfur metabolite","volume":"51","author":"Jackson","year":"2012","journal-title":"Biochemistry"},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"3352","DOI":"10.1111\/j.1742-4658.2008.06482.x","article-title":"Three enzymatic activities catalyze the oxidation of sulfide to thiosulfate in mammalian and invertebrate mitochondria","volume":"275","author":"Hildebrandt","year":"2008","journal-title":"FEBS J."},{"key":"ref_178","doi-asserted-by":"crossref","unstructured":"Quinzii, C.M., Luna-Sanchez, M., Ziosi, M., Hidalgo-Gutierrez, A., Kleiner, G., and Lopez, L.C. (2017). The Role of Sulfide Oxidation Impairment in the Pathogenesis of Primary CoQ Deficiency. Front. Physiol., 8.","DOI":"10.3389\/fphys.2017.00525"},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"78","DOI":"10.15252\/emmm.201606345","article-title":"CoQ deficiency causes disruption of mitochondrial sulfide oxidation, a new pathomechanism associated with this syndrome","volume":"9","author":"Hildebrandt","year":"2017","journal-title":"EMBO Mol. Med."},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"101772","DOI":"10.1016\/j.redox.2020.101772","article-title":"Effects of hydrogen sulfide on mitochondrial function and cellular bioenergetics","volume":"38","author":"Paul","year":"2021","journal-title":"Redox Biol."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/j.jare.2020.04.002","article-title":"Abnormalities of hydrogen sulfide and glutathione pathways in mitochondrial dysfunction","volume":"27","author":"Quinzii","year":"2021","journal-title":"J. Adv. Res."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1038\/cdd.2014.150","article-title":"Oxidative stress and autophagy: The clash between damage and metabolic needs","volume":"22","author":"Filomeni","year":"2015","journal-title":"Cell Death Differ."},{"key":"ref_183","doi-asserted-by":"crossref","unstructured":"Mailloux, R.J. (2020). An Update on Mitochondrial Reactive Oxygen Species Production. Antioxidants, 9.","DOI":"10.3390\/antiox9060472"},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1016\/j.imbio.2018.11.010","article-title":"Reactive oxygen species (ROS) in macrophage activation and function in diabetes","volume":"224","author":"Rendra","year":"2019","journal-title":"Immunobiology"},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"1302","DOI":"10.1126\/science.3287616","article-title":"DNA damage and oxygen radical toxicity","volume":"240","author":"Imlay","year":"1988","journal-title":"Science"},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/0309-1651(78)90032-2","article-title":"Biochemical mechanisms accounting for the toxic action of oxygen on living organisms: The key role of superoxide dismutase","volume":"2","author":"Halliwell","year":"1978","journal-title":"Cell Biol. Int. Rep."},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"9914","DOI":"10.1016\/S0021-9258(18)48021-0","article-title":"Protein damage and degradation by oxygen radicals. IV. Degradation of denatured protein","volume":"262","author":"Davies","year":"1987","journal-title":"J. Biol. Chem."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1016\/j.bbrc.2016.10.086","article-title":"Lipid peroxidation in cell death","volume":"482","author":"Gaschler","year":"2017","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1016\/j.freeradbiomed.2010.10.709","article-title":"Formation of 4-hydroxynonenal from cardiolipin oxidation: Intramolecular peroxyl radical addition and decomposition","volume":"50","author":"Liu","year":"2011","journal-title":"Free Radic. Biol. Med."},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"14205","DOI":"10.3748\/wjg.v20.i39.14205","article-title":"Oxidative stress, cardiolipin and mitochondrial dysfunction in nonalcoholic fatty liver disease","volume":"20","author":"Paradies","year":"2014","journal-title":"World J. Gastroenterol."},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"791","DOI":"10.1002\/iub.2018","article-title":"Mitochondrial dysfunctions in barth syndrome","volume":"71","author":"Ghosh","year":"2019","journal-title":"IUBMB Life"},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"1060","DOI":"10.1016\/j.cell.2012.03.042","article-title":"Ferroptosis: An iron-dependent form of nonapoptotic cell death","volume":"149","author":"Dixon","year":"2012","journal-title":"Cell"},{"key":"ref_193","doi-asserted-by":"crossref","unstructured":"Lyamzaev, K.G., Panteleeva, A.A., Simonyan, R.A., Avetisyan, A.V., and Chernyak, B.V. (2023). Mitochondrial Lipid Peroxidation Is Responsible for Ferroptosis. Cells, 12.","DOI":"10.3390\/cells12040611"},{"key":"ref_194","doi-asserted-by":"crossref","unstructured":"Garcia-Llorens, G., El Ouardi, M., and Valls-Belles, V. (2025). Oxidative Stress Fundamentals: Unraveling the Pathophysiological Role of Redox Imbalance in Non-Communicable Diseases. Appl. Sci., 15.","DOI":"10.3390\/app151810191"},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"32967","DOI":"10.1074\/jbc.M112.400663","article-title":"Protein carbonylation and adipocyte mitochondrial function","volume":"287","author":"Curtis","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_196","doi-asserted-by":"crossref","unstructured":"Reddy, V.P. (2023). Oxidative Stress in Health and Disease. Biomedicines, 11.","DOI":"10.3390\/biomedicines11112925"},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"825065","DOI":"10.1155\/2013\/825065","article-title":"Oxidative stress induces mitochondrial DNA damage and cytotoxicity through independent mechanisms in human cancer cells","volume":"2013","author":"Han","year":"2013","journal-title":"BioMed Res. Int."},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1042\/BCJ20220611","article-title":"Site IQ in mitochondrial complex I generates S1QEL-sensitive superoxide\/hydrogen peroxide in both the reverse and forward reactions","volume":"480","author":"Gibbs","year":"2023","journal-title":"Biochem. J."},{"key":"ref_199","first-page":"3","article-title":"Mitochondrial electron transport chain, ROS generation and uncoupling (Review)","volume":"44","author":"Zhao","year":"2019","journal-title":"Int. J. Mol. Med."},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/j.celrep.2016.03.009","article-title":"The CoQH2\/CoQ Ratio Serves as a Sensor of Respiratory Chain Efficiency","volume":"15","author":"Calvo","year":"2016","journal-title":"Cell Rep."},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"909","DOI":"10.1152\/physrev.00026.2013","article-title":"Mitochondrial reactive oxygen species (ROS) and ROS-induced ROS release","volume":"94","author":"Zorov","year":"2014","journal-title":"Physiol. Rev."},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1097\/WOX.0b013e3182439613","article-title":"Oxidative Stress and Antioxidant Defense","volume":"5","author":"Birben","year":"2012","journal-title":"World Allergy Organ. J."},{"key":"ref_203","doi-asserted-by":"crossref","unstructured":"Pei, J., Pan, X., Wei, G., and Hua, Y. (2023). Research progress of glutathione peroxidase family (GPX) in redoxidation. Front. Pharmacol., 14.","DOI":"10.3389\/fphar.2023.1147414"},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"3289","DOI":"10.1016\/j.bbagen.2012.11.020","article-title":"Glutathione peroxidases","volume":"1830","author":"Maiorino","year":"2013","journal-title":"Biochim. Biophys. Acta (BBA)-Gen. Subj."},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"2621","DOI":"10.1080\/15548627.2023.2218764","article-title":"GPX4 in cell death, autophagy, and disease","volume":"19","author":"Xie","year":"2023","journal-title":"Autophagy"},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1042\/BJ20121713","article-title":"Mammalian Trit1 is a tRNA([Ser]Sec)-isopentenyl transferase required for full selenoprotein expression","volume":"450","author":"Fradejas","year":"2013","journal-title":"Biochem. J."},{"key":"ref_207","doi-asserted-by":"crossref","unstructured":"Va\u0161kov\u00e1, J., Ko\u010dan, L., Va\u0161ko, L., and Perj\u00e9si, P. (2023). Glutathione-Related Enzymes and Proteins: A Review. Molecules, 28.","DOI":"10.3390\/molecules28031447"},{"key":"ref_208","first-page":"3","article-title":"Transplasma membrane electron transport: Enzymes involved and biological function","volume":"8","author":"Ly","year":"2003","journal-title":"Redox Rep. Commun. Free Radic. Res."},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"2289","DOI":"10.1089\/ars.2010.3247","article-title":"Trans-plasma membrane electron transport in mammals: Functional significance in health and disease","volume":"14","author":"Avigliano","year":"2011","journal-title":"Antioxid. Redox Signal."},{"key":"ref_210","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_211","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/j.cmet.2019.12.007","article-title":"The Antioxidant Role of Non-mitochondrial CoQ10: Mystery Solved!","volume":"31","author":"Santoro","year":"2020","journal-title":"Cell Metab."},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"L36","DOI":"10.1152\/ajplung.00283.2001","article-title":"Intracellular redox status affects transplasma membrane electron transport in pulmonary arterial endothelial cells","volume":"282","author":"Merker","year":"2002","journal-title":"Am. J. Physiol. Lung Cell. Mol. Physiol."},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/j.arr.2006.03.005","article-title":"The plasma membrane redox system in aging","volume":"5","author":"Hyun","year":"2006","journal-title":"Ageing Res. Rev."},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"103788","DOI":"10.1016\/j.redox.2025.103788","article-title":"DHODH-mediated mitochondrial redox homeostasis: A novel ferroptosis regulator and promising therapeutic target","volume":"85","author":"Cao","year":"2025","journal-title":"Redox Biol."},{"key":"ref_215","doi-asserted-by":"crossref","unstructured":"Lee, J., and Roh, J.-L. (2025). Dihydroorotate Dehydrogenase in Mitochondrial Ferroptosis and Cancer Therapy. Cells, 14.","DOI":"10.3390\/cells14231889"},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"586","DOI":"10.1038\/s41586-021-03539-7","article-title":"DHODH-mediated ferroptosis defence is a targetable vulnerability in cancer","volume":"593","author":"Mao","year":"2021","journal-title":"Nature"},{"key":"ref_217","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1016\/j.tcb.2023.06.002","article-title":"Ferroptosis in mitochondrial cardiomyopathy","volume":"34","author":"Ahola","year":"2024","journal-title":"Trends Cell Biol."},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1159\/000360494","article-title":"Pathomechanisms in Coenzyme Q10-Deficient Human Fibroblasts","volume":"5","author":"Quinzii","year":"2014","journal-title":"Mol. Syndromol."},{"key":"ref_219","doi-asserted-by":"crossref","first-page":"1874","DOI":"10.1096\/fj.07-100149","article-title":"Respiratory chain dysfunction and oxidative stress correlate with severity of primary CoQ10 deficiency","volume":"22","author":"Quinzii","year":"2008","journal-title":"FASEB J."},{"key":"ref_220","doi-asserted-by":"crossref","unstructured":"Quinzii, C.M., Tadesse, S., Naini, A., and Hirano, M. (2012). Effects of inhibiting CoQ10 biosynthesis with 4-nitrobenzoate in human fibroblasts. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0030606"},{"key":"ref_221","doi-asserted-by":"crossref","first-page":"612","DOI":"10.1096\/fj.12-209361","article-title":"Tissue-specific oxidative stress and loss of mitochondria in CoQ-deficient Pdss2 mutant mice","volume":"27","author":"Quinzii","year":"2013","journal-title":"FASEB J."},{"key":"ref_222","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.ymgme.2020.10.002","article-title":"Clinical trials in mitochondrial disorders, an update","volume":"131","author":"Almannai","year":"2020","journal-title":"Mol. Genet. Metab."},{"key":"ref_223","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1515\/hsz-2012-0119","article-title":"Mitophagy: Mechanisms, pathophysiological roles, and analysis","volume":"393","author":"Ding","year":"2012","journal-title":"Biol. Chem."},{"key":"ref_224","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/j.tibs.2020.11.007","article-title":"Mitochondrial Dysfunction and Mitophagy in Parkinson\u2019s Disease: From Mechanism to Therapy","volume":"46","author":"Malpartida","year":"2021","journal-title":"Trends Biochem. Sci."},{"key":"ref_225","doi-asserted-by":"crossref","first-page":"1812","DOI":"10.1161\/CIRCRESAHA.117.311082","article-title":"Autophagy and Mitophagy in Cardiovascular Disease","volume":"120","author":"Kroemer","year":"2017","journal-title":"Circ. Res."},{"key":"ref_226","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1016\/j.redox.2018.03.002","article-title":"Diverse roles of mitochondria in ischemic stroke","volume":"16","author":"Yang","year":"2018","journal-title":"Redox Biol."},{"key":"ref_227","doi-asserted-by":"crossref","first-page":"1396","DOI":"10.1080\/15548627.2022.2139080","article-title":"PINK1-PRKN mediated mitophagy: Differences between in vitro and in vivo models","volume":"19","author":"Han","year":"2023","journal-title":"Autophagy"},{"key":"ref_228","doi-asserted-by":"crossref","first-page":"114891","DOI":"10.1016\/j.bcp.2021.114891","article-title":"The role of FUNDC1 in mitophagy, mitochondrial dynamics and human diseases","volume":"197","author":"Liu","year":"2022","journal-title":"Biochem. Pharmacol."},{"key":"ref_229","doi-asserted-by":"crossref","first-page":"19","DOI":"10.4161\/auto.5.1.7174","article-title":"Coenzyme Q deficiency triggers mitochondria degradation by mitophagy","volume":"5","author":"Cordero","year":"2009","journal-title":"Autophagy"},{"key":"ref_230","doi-asserted-by":"crossref","first-page":"111124","DOI":"10.1016\/j.celrep.2022.111124","article-title":"Pathological mitophagy disrupts mitochondrial homeostasis in Leber\u2019s hereditary optic neuropathy","volume":"40","author":"Danese","year":"2022","journal-title":"Cell Rep."},{"key":"ref_231","doi-asserted-by":"crossref","unstructured":"Grazioli, S., and Pugin, J. (2018). Mitochondrial Damage-Associated Molecular Patterns: From Inflammatory Signaling to Human Diseases. Front. Immunol., 9.","DOI":"10.3389\/fimmu.2018.00832"},{"key":"ref_232","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/j.molmed.2014.11.008","article-title":"Mitochondria: Diversity in the regulation of the NLRP3 inflammasome","volume":"21","author":"Gurung","year":"2015","journal-title":"Trends Mol. Med."},{"key":"ref_233","doi-asserted-by":"crossref","first-page":"1403","DOI":"10.1038\/s41423-023-01086-x","article-title":"Mitochondrial DNA-triggered innate immune response: Mechanisms and diseases","volume":"20","author":"Hu","year":"2023","journal-title":"Cell. Mol. Immunol."},{"key":"ref_234","doi-asserted-by":"crossref","first-page":"1169","DOI":"10.1089\/ars.2013.5198","article-title":"NLRP3 Inflammasome Is Activated in Fibromyalgia: The Effect of Coenzyme Q10","volume":"20","author":"Cordero","year":"2014","journal-title":"Antioxid. Redox Signal."},{"key":"ref_235","doi-asserted-by":"crossref","first-page":"4266214","DOI":"10.1155\/2022\/4266214","article-title":"Coenzyme Q0 Inhibits NLRP3 Inflammasome Activation through Mitophagy Induction in LPS\/ATP-Stimulated Macrophages","volume":"2022","author":"Hseu","year":"2022","journal-title":"Oxidative Med. Cell. Longev."},{"key":"ref_236","doi-asserted-by":"crossref","unstructured":"Liang, Y., Han, Y., Xiao, L., Su, Y., Bao, T., Ji, X., Jia, L., and Zhang, J. (2025). Coenzyme Q10 modulates the immunity by enhancing mononuclear macrophage, NK cell activity, and regulating gut microbiota. Front. Nutr., 12.","DOI":"10.3389\/fnut.2025.1504831"},{"key":"ref_237","doi-asserted-by":"crossref","first-page":"877","DOI":"10.1161\/CIRCRESAHA.117.311401","article-title":"Reactive Oxygen Species in Metabolic and Inflammatory Signaling","volume":"122","author":"Forrester","year":"2018","journal-title":"Circ. Res."},{"key":"ref_238","doi-asserted-by":"crossref","first-page":"13944","DOI":"10.1038\/ncomms13944","article-title":"The mito-DAMP cardiolipin blocks IL-10 production causing persistent inflammation during bacterial pneumonia","volume":"8","author":"Chakraborty","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_239","doi-asserted-by":"crossref","first-page":"1368","DOI":"10.1089\/ars.2020.8211","article-title":"Hydrogen Sulfide in Inflammation: A Novel Mediator and Therapeutic Target","volume":"34","author":"Bhatia","year":"2021","journal-title":"Antioxid. Redox Signal."},{"key":"ref_240","doi-asserted-by":"crossref","first-page":"670","DOI":"10.15252\/emmm.201404632","article-title":"The clinical heterogeneity of coenzyme Q10 deficiency results from genotypic differences in the Coq9 gene","volume":"7","author":"Barca","year":"2015","journal-title":"EMBO Mol. Med."},{"key":"ref_241","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1016\/S0891-5849(02)00905-X","article-title":"Superoxide dismutase multigene family: A comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression","volume":"33","author":"Zelko","year":"2002","journal-title":"Free Radic. Biol. Med."},{"key":"ref_242","doi-asserted-by":"crossref","first-page":"490","DOI":"10.1016\/j.redox.2018.01.008","article-title":"13 reasons why the brain is susceptible to oxidative stress","volume":"15","author":"Cobley","year":"2018","journal-title":"Redox Biol."},{"key":"ref_243","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1186\/1550-2783-5-8","article-title":"Effects of acute and 14-day coenzyme Q10 supplementation on exercise performance in both trained and untrained individuals","volume":"5","author":"Cooke","year":"2008","journal-title":"J. Int. Soc. Sports Nutr."},{"key":"ref_244","doi-asserted-by":"crossref","first-page":"e200209","DOI":"10.1212\/NXG.0000000000200209","article-title":"Clinical Features, Biochemistry, Imaging, and Treatment Response in a Single-Center Cohort with Coenzyme Q10 Biosynthesis Disorders","volume":"10","author":"Wahedi","year":"2024","journal-title":"Neurol. Genet."},{"key":"ref_245","doi-asserted-by":"crossref","unstructured":"Guile, M.D., Jain, A., Anderson, K.A., and Clarke, C.F. (2023). New Insights on the Uptake and Trafficking of Coenzyme Q. Antioxidants, 12.","DOI":"10.3390\/antiox12071391"},{"key":"ref_246","doi-asserted-by":"crossref","first-page":"F1535","DOI":"10.1152\/ajprenal.90445.2008","article-title":"Coenzyme Q10 supplementation rescues renal disease in Pdss2kd\/kd mice with mutations in prenyl diphosphate synthase subunit 2","volume":"295","author":"Saiki","year":"2008","journal-title":"Am. J. Physiol.-Ren. Physiol."},{"key":"ref_247","doi-asserted-by":"crossref","first-page":"4635","DOI":"10.1111\/jcmm.17488","article-title":"The efficacy of coenzyme Q10 treatment in alleviating the symptoms of primary coenzyme Q10 deficiency: A systematic review","volume":"26","author":"Wang","year":"2022","journal-title":"J. Cell. Mol. Med."},{"key":"ref_248","doi-asserted-by":"crossref","unstructured":"Mantle, D., Millichap, L., Castro-Marrero, J., and Hargreaves, I.P. (2023). Primary Coenzyme Q10 Deficiency: An Update. Antioxidants, 12.","DOI":"10.3390\/antiox12081652"},{"key":"ref_249","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1016\/j.biocel.2014.02.003","article-title":"Effect of Coenzyme Q10 supplementation on mitochondrial electron transport chain activity and mitochondrial oxidative stress in Coenzyme Q10 deficient human neuronal cells","volume":"50","author":"Duberley","year":"2014","journal-title":"Int. J. Biochem. Cell Biol."}],"container-title":["Biomolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2218-273X\/16\/2\/302\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,2,26]],"date-time":"2026-02-26T05:14:20Z","timestamp":1772082860000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2218-273X\/16\/2\/302"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,2,14]]},"references-count":249,"journal-issue":{"issue":"2","published-online":{"date-parts":[[2026,2]]}},"alternative-id":["biom16020302"],"URL":"https:\/\/doi.org\/10.3390\/biom16020302","relation":{},"ISSN":["2218-273X"],"issn-type":[{"value":"2218-273X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,2,14]]}}}