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Metabolism and function of coenzyme Q
Open accessAbstract
Coenzyme Q (CoQ) is present in all cells and membranes and in addition to be a member of the mitochondrial respiratory chain it has also several other functions of great importance for the cellular metabolism. This review summarizes the findings available to day concerning CoQ distribution, biosynthesis, regulatory modifications and its participation in cellular metabolism. There are a number of indications that this lipid is not always functioning by its direct presence at the site of action but also using e.g. receptor expression modifications, signal transduction mechanisms and action through its metabolites. The biosynthesis of CoQ is studied in great detail in bacteria and yeast but only to a limited extent in animal tissues and therefore the informations available is restricted. However, it is known that the CoQ is compartmentalized in the cell with multiple sites of biosynthesis, breakdown and regulation which is the basis of functional specialization. Some regulatory mechanisms concerning amount and biosynthesis are established and nuclear transcription factors are partly identified in this process. Using appropriate ligands of nuclear receptors the biosynthetic rate can be increased in experimental system which raises the possibility of drug-induced upregulation of the lipid in deficiency. During aging and pathophysiological conditions the tissue concentration of CoQ is modified which influences cellular functions. In this case the extent of disturbances is dependent on the localization and the modified distribution of the lipid at cellular and membrane levels.
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“HMG-CoA blockade is more potent at inhibiting cholesterol biosynthesis than CoQ biosynthesis because of differing Km values for trans-prenyltransferase (leads to CoQ) and squalene synthetase (leads to cholesterol) at the farnesyl-PP branch point (315).”
From Mitochondrial Dysfunction in Diabetes: From Molecular Mechanisms to Functional Significance and Therapeutic Opportunities (2010) · cites this paper as [315]
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Cites
Free Radicals in the Physiological Control of Cell Function
Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855
Green, D. R., & Reed, J. C. (1998) · Science · doi:10.1126/science.281.5381.1309 · Cited by 9,051
Hydroperoxide metabolism in mammalian organs.
Chance, B., Sies, H., & Boveris, A. (1979) · Physiological Reviews · doi:10.1152/physrev.1979.59.3.527 · Cited by 5,827
A Receptor-Mediated Pathway for Cholesterol Homeostasis
Brown, M. S., & Goldstein, J. L. (1986) · Science · doi:10.1126/science.3513311 · Cited by 5,703
Regulation of the mevalonate pathway
Goldstein, J. L., & Brown, M. S. (1990) · Nature · doi:10.1038/343425a0 · Cited by 5,394
Prusiner, S. B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13363 · Cited by 5,373
Oxygen toxicity, oxygen radicals, transition metals and disease
Halliwell, B., & Gutteridge, J. M. C. (1984) · Biochemical Journal · doi:10.1042/bj2190001 · Cited by 5,330
Activation of a member of the steroid hormone receptor superfamily by peroxisome proliferators
Issemann, I., & Green, S. (1990) · Nature · doi:10.1038/347645a0 · Cited by 3,519
Mitochondrial free radical generation, oxidative stress, and aging
Cadenas, E., & Davies, K. J. A. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00317-8 · Cited by 3,010
Hörlein, A., Näär, A. M., Heinzel, T., Torchia, J., Gloss, B. R., Kurokawa, R., Ryan, A. K., Kamei, Y., Söderström, M., Glass, C. K., et al. (1995) · Nature · doi:10.1038/377397a0 · Cited by 2,072
Flagged first, then by citations
2 of the 323 references couldn’t be matched to a known paper.
Research works printed but not linked: 4
- van Duijn, 1987, Influence of dolichols on lipid polymorphism in model membranes and the consequences for phospholipid flip-flop and vesicle fusion, Chem. Scr., 27, 95
- Nobuyoshi, 1984, Levels of coenzyme Q10 in biopsies of left ventricular muscle and influence of administration of coenzyme Q10, vol. 4, 221
- Kitamura, 1984, Myocardial tissue level of coenzyme Q10 in patients with cardiac failure, vol. 4, 243
- J. Grünler, Compartmentalization of lipid metabolism in rat liver, PhD thesis. Stockholm University, 2000.
Cited by
Sorted by citations
Items 401–500 of 999
Rauchová, H., Drahota, Z., Bergamini, C., Fato, R., & Lenaz, G. (2008) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-008-9134-1 · Cited by 27
Is there a place for coenzyme Q in the management of metabolic disorders associated with obesity?
Sohet, F. M., & Delzenne, N. M. (2012) · Nutrition Reviews · doi:10.1111/j.1753-4887.2012.00526.x · Cited by 27
Liaubet, L., Lobjois, V., Faraut, T., Tircazes, A., Benne, F., Iannuccelli, N., Pires, J., Glénisson, J., Robic, A., Roy, P. L., et al. (2011) · BMC Genomics · doi:10.1186/1471-2164-12-548 · Cited by 31
Guescini, M., Tiano, L., Genova, M. L., Polidori, E., Silvestri, S., Orlando, P., Fimognari, C., Calcabrini, C., Stocchi, V., & Sestili, P. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/7083049 · Cited by 32
Intracellular cholesterol accumulation and coenzyme Q10 deficiency in Familial Hypercholesterolemia
Suarez-Rivero, J. M., de la Mata, M., Pavón, A. D., Paz, M. V., Povea-Cabello, S., Cotán, D., Álvarez-Córdoba, M., Villalón-García, I., Ybot‐González, P., Salas, J. J., et al. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.10.009 · Cited by 27
Lu, M., Zhou, Y., Wang, Z., Xia, Z., Ren, J., & Guo, Q. (2019) · Journal of Human Genetics · doi:10.1038/s10038-019-0563-y · Cited by 27
Effect of coenzyme Q10 supplementation on diabetes induced memory deficits in rats
Omidi, G., Karimi, S. A., Rezvani-Kamran, A., Monsef, A., Shahidi, ., & Komaki, A. (2019) · Metabolic Brain Disease · doi:10.1007/s11011-019-00402-7 · Cited by 27
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Kagan, V. E., Straub, A. C., Tyurina, Y. Y., Kapralov, A. A., Hall, R., Wenzel, S. E., Mallampalli, R. K., & Bayır, H. (2023) · Antioxidants and Redox Signaling · doi:10.1089/ars.2022.0154 · Cited by 30
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Ushikoshi‐Nakayama, R., Ryo, K., Yamazaki, T., Kaneko, M., Sugano, T., Ito, Y., Matsumoto, N., & Saito, I. (2019) · PLoS ONE · doi:10.1371/journal.pone.0214495 · Cited by 26
Jin, J., Zhang, S., Wu, B., Chen, Z., Zhang, G., & Tratnyek, P. G. (2019) · Environmental Science & Technology · doi:10.1021/acs.est.9b02751 · Cited by 26
Yang, H., Tsai, C.-H., Shrestha, S., Lee, C.-C., Liao, J., & Hseu, Y. (2021) · Food and Chemical Toxicology · doi:10.1016/j.fct.2021.112384 · Cited by 27
Ashraf, K., Tajeri, S., Arnold, C.-S., Amanzougaghene, N., Franetich, J., Vantaux, A., Soulard, V., Bordessoulles, M., Cazals, G., Bousema, T., et al. (2021) · Life Science Alliance · doi:10.26508/lsa.202101237 · Cited by 26
Combined Supplementation of Coenzyme Q10 and Other Nutrients in Specific Medical Conditions
Tippairote, T., Bjørklund, G., Gasmi, A., Semenova, Y. M., Peana, M., Chirumbolo, S., & Hangan, T. (2022) · Nutrients · doi:10.3390/nu14204383 · Cited by 28
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Jarmuszkiewicz, W., Dominiak, K., Budzinska, A., Wojcicki, K., & Gałgański, Ł. (2023) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2803061 · Cited by 27
Biani, F. F. D., & Zanello, P. (2016) · Inorganica Chimica Acta · doi:10.1016/j.ica.2016.09.028 · Cited by 27
Gómez, F., Saiki, R., Chin, R., Srinivasan, C., & Clarke, C. F. (2012) · Gene · doi:10.1016/j.gene.2012.06.023 · Cited by 26
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Yang, Y.-Y., Vasta, V., Hahn, S., Gangoiti, J. A., Opheim, E., Sedensky, M. M., & Morgan, P. G. (2011) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2011.06.009 · Cited by 26
Horecký, J., Gvozdjáková, A., Kucharská, J., Obrenovich, M. E., Palacios, H. H., Li, Y., Vančová, O., & Aliev, G. M. (2011) · Current Alzheimer Research · doi:10.2174/156720511798192727 · Cited by 26
Mohammadi‐Bardbori, A., Najibi, A., Amirzadegan, N., Gharibi, R., Dashti, A., Omidi, M., Saeedi, A., Ghaffarian‐Bahraman, A., & Niknahad, H. (2015) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2015.05.041 · Cited by 26
Treatment of steroid-resistant nephrotic syndrome in the genomic era
Bensimhon, A. R., Williams, A. E., & Gbadegesin, R. (2018) · Pediatric Nephrology · doi:10.1007/s00467-018-4093-1 · Cited by 26
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Villalba, J. M., & Navas, P. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.01.055 · Cited by 26
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Ratnam, D. V., Bhardwaj, V., & Kumar, M. N. V. R. (2006) · Talanta · doi:10.1016/j.talanta.2006.02.057 · Cited by 26
Anion resonances and above-threshold dynamics of coenzyme Q 0
Bull, J. N., West, C. W., & Verlet, J. R. R. (2015) · Physical Chemistry Chemical Physics · doi:10.1039/c5cp02145f · Cited by 25
p-Benzoquinone as a Privileged Scaffold of Pharmacological Significance: A Review
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Yi, Y. Y., Shin, H. J., Choi, S. G., Kang, J. W., Song, H., Kim, S. K., & Kim, D. W. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21103703 · Cited by 26
Schwank-Xu, C., Forsberg, E., Bentinger, M., Zhao, A., Ansurudeen, I., Dallner, G., Catrina, S., Brismar, K., & Tekle, M. (2021) · Antioxidants · doi:10.3390/antiox10050793 · Cited by 25
Self-citationDuong, Q. V., Levitsky, Y., Dessinger, M. J., Strubbe, J. O., & Bazil, J. N. (2021) · Function · doi:10.1093/function/zqab050 · Cited by 26
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Artuch, R., Salviati, L., Jackson, S., Hirano, M., & Navas, P. (2009) · Advances in experimental medicine and biology · doi:10.1007/978-90-481-2813-6_8 · Cited by 25
Fato, R., Bergamini, C., Leoni, S., Pinna, A., Carta, F., Cardascia, N., Ferrari, T. M., Sborgia, C., & Lenaz, G. (2009) · Acta Ophthalmologica · doi:10.1111/j.1755-3768.2009.01632.x · Cited by 25
Niklowitz, P., Döring, F., Paulussen, M., & Menke, T. (2013) · Analytical Biochemistry · doi:10.1016/j.ab.2013.02.015 · Cited by 25
Nukui, K., Yamagishi, T., Miyawaki, H., Kettawan, A., Okamoto, T., & Sato, K. (2007) · Journal of Nutritional Science and Vitaminology · doi:10.3177/jnsv.53.187 · Cited by 25
Quirk, A., Lardner, M. J., Tun, Z., & Burgess, I. J. (2016) · Langmuir · doi:10.1021/acs.langmuir.5b04263 · Cited by 25
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Masoudi, R., Sharafi, M., & Pourazadi, L. (2019) · Cryobiology · doi:10.1016/j.cryobiol.2019.03.003 · Cited by 25
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Asencio, C., Navas, P., Cabello, J., Schnabel, R., Cypser, J. R., Johnson, T. E., & Rodríguez‐Aguilera, J. C. (2008) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2008.10.004 · Cited by 25
Stacpoole, P. W., deGrauw, T. J., Feigenbaum, A. S. J., Hoppel, C. L., Kerr, D. S., McCandless, S. E., Miles, M. V., Robinson, B. H., & Tang, P. (2012) · Mitochondrion · doi:10.1016/j.mito.2012.09.005 · Cited by 25
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Al-Ghamdi, M., Al-Ayadhi, L., & El-Ansary, A. (2014) · BMC Neuroscience · doi:10.1186/1471-2202-15-34 · Cited by 25
Gray, J. P., Karandrea, S., Burgos, D. Z., Jaiswal, A. A., & Heart, E. A. (2016) · Toxicology Letters · doi:10.1016/j.toxlet.2016.08.021 · Cited by 24
Lee, J.-S., Warkad, S. D., Shinde, P. B., Kuwar, A., & Nimse, S. B. (2020) · Arabian Journal of Chemistry · doi:10.1016/j.arabjc.2020.09.061 · Cited by 24
Feng, M., Swevers, L., & Sun, J. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.852702 · Cited by 24
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Stacpoole, P. W. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.05.002 · Cited by 24
Gharib, A., Paulis, D. D., Li, B., Augeul, L., Couture-Lepetit, E., Gomez, L., Angoulvant, D., & Ovize, M. (2012) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2012.02.005 · Cited by 26
Yen, H., Li, S.-H., Majima, H. J., Huang, Y.-H., Chen, C.-P., Liu, C., Tu, Y., & Chen, C. (2011) · Free Radical Research · doi:10.3109/10715762.2011.572969 · Cited by 24
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Saneto, R. P. (2017) · Advances in genetics · doi:10.1016/bs.adgen.2017.06.002 · Cited by 23
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Băran, I., Ionescu, D. N., Privitera, S., Scordino, A., Mocanu, M., Musumeci, F., Grasso, R., Gulino, M., Iftime, A., Tofolean, I. T., et al. (2013) · Journal of Biomedical Optics · doi:10.1117/1.jbo.18.12.127006 · Cited by 24
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Zhou, X., Yuan, Y., Yang, Y., Rutzke, M. A., Thannhauser, T. W., Kochian, L. V., & Li, L. (2009) · PLANT PHYSIOLOGY · doi:10.1104/pp.109.142521 · Cited by 24
Masotta, N. E., Höcht, C., Contin, M. D., Lucangioli, S. E., Rojas, A. M., & Tripodi, V. P. (2020) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2020.119315 · Cited by 23
Zhang, Y., Gao, S., Zhang, P., Sun, H., Lu, R., Yu, R., Li, Y., Zhang, K., & Li, B. (2022) · Molecular Genetics and Genomics · doi:10.1007/s00438-022-01890-6 · Cited by 22
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López, L. C., Luna‐Sánchez, M., García‐Corzo, L., Quinzii, C. M., & Hirano, M. (2014) · Molecular Syndromology · doi:10.1159/000360494 · Cited by 23
Xu, C., Bentinger, M., Savu, O., Moshfegh, A., Sunkari, V. G., Dallner, G., Świeżewska, E., Catrina, S., Brismar, K., & Tekle, M. (2016) · Journal of Diabetes and its Complications · doi:10.1016/j.jdiacomp.2016.10.010 · Cited by 24
Self-citationPala, R., Beyaz, F., Tuzcu, M., Er, B., Şahin, N., Çınar, V., & Şahin, K. (2018) · Physical Activity and Nutrition · doi:10.20463/jenb.2018.0019 · Cited by 24
Farries, G., Bryan, K. R., McGivney, C. L., McGettigan, P., Gough, K. F., Browne, J. A., MacHugh, D. E., Katz, L. M., & Hill, E. W. (2019) · Frontiers in Genetics · doi:10.3389/fgene.2019.01215 · Cited by 23
Wang, Y., & Hekimi, S. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101680 · Cited by 23
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Cordero, M. D., de Miguel, M., & Moreno‐Fernández, A. M. (2010) · Medicina Clínica · doi:10.1016/j.medcli.2010.01.030 · Cited by 23
Xiu, J., Nordberg, A. K., Shan, K.-R., Yu, W., Olsson, J. M., Nordman, T., Mousavi, M. T., & Guan, Z. (2005) · Journal of Neuroscience Research · doi:10.1002/jnr.20658 · Cited by 24
Self-citationThe role of ubiquinone in Caenorhabditis elegans longevity
Rodríguez‐Aguilera, J. C., Gavilán, Á., Asencio, C., & Navas, P. (2004) · Ageing Research Reviews · doi:10.1016/j.arr.2004.09.001 · Cited by 23
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Bautista-Ferrufino, M. R., Cordero, M. D., Sánchez-Alcázar, J. A., Illanes, M., Fernández-Rodríguez, A., Navas, P., & de Miguel, M. (2011) · Toxicology Letters · doi:10.1016/j.toxlet.2011.03.033 · Cited by 22
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Rebelo, A. P., Tomaselli, P. J., Medina, J., Wang, Y., Dohrn, M. F., Nývltová, E., Danzi, M. C., Garrett, M., Smith, S. E., Pestronk, A., et al. (2023) · Brain · doi:10.1093/brain/awad158 · Cited by 22
Eleiwa, N. Z. H., Elsayed, A., Said, E. N., Metwally, M. M. M., & Abd‐Elhakim, Y. M. (2023) · Food and Chemical Toxicology · doi:10.1016/j.fct.2023.114372 · Cited by 23
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Wang, H., Liu, Y., Che, S., Li, X., Tang, D., Lv, S., & Hai, Z. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1346585 · Cited by 24
Effect of water-soluble coenzyme Q10 on noise-induced hearing loss in guinea pigs
Hirose, Y., Sugahara, K., Mikuriya, T., Hashimoto, M., Shimogori, H., & Yamashita, H. (2008) · Acta Oto-Laryngologica · doi:10.1080/00016480801891694 · Cited by 22
Cascella, V., Giordano, P., Stavros Hatzopoulos, A., Petruccelli, J. D., Prosser, S., Simoni, E., Astolfi, L., Fetoni, A. R., Skarżyńśki, H., & Martini, A. (2012) · Medical Science Monitor · doi:10.12659/msm.882180 · Cited by 22
A rare case of primary coenzyme Q10 deficiency due to COQ9 mutation
Olgaç, A., Öztoprak, Ü., Kasapkara, Ç. S., Kılıç, M., Yüksel, D., Derinkuyu, B. E., Yıldız, Y. T., Ceylaner, S., & Ezgü, F. S. (2019) · Journal of Pediatric Endocrinology and Metabolism · doi:10.1515/jpem-2019-0245 · Cited by 22
Immunotherapy in antiphospholipid syndrome
López-Pedrera, C., Aguirre, M. A., Ruiz‐Limón, P., Pérez‐Sánchez, C., Jiménez, Y., Barbarroja, N., & Cuadrado, M. J. (2015) · International Immunopharmacology · doi:10.1016/j.intimp.2015.06.006 · Cited by 23
Adaptations to oxidative stress induced by vitamin E deficiency in rat liver
de Cabo, R., Burgess, J. R., & Navas, P. (2006) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-006-9050-1 · Cited by 22
Fragaki, K., Chaussenot, A., Benoist, J., Ait-El-Mkadem, S., Bannwarth, S., Rouzier, C., Cochaud, C., & Paquis‐Flucklinger, V. (2016) · Biological Research · doi:10.1186/s40659-015-0065-0 · Cited by 22
Kanda, M., Sugimoto, H., Nomoto, S., Oya, H., Shimizu, D., Takami, H., Hashimoto, R., Sonohara, F., Okamura, Y., Yamada, S., et al. (2014) · International Journal of Oncology · doi:10.3892/ijo.2014.2637 · Cited by 21
A comparative study into alterations of coenzyme Q redox status in ageing pigs, mice, and worms
Onur, S., Niklowitz, P., Fischer, A., Metges, C. C., Grune, T., Menke, T., Rimbach, G. H., & Döring, F. (2014) · BioFactors · doi:10.1002/biof.1160 · Cited by 21
Poulsen, V. K., Domenech, C. E., & Cerdá‐Olmedo, E. (2006) · Archives of Microbiology · doi:10.1007/s00203-006-0166-9 · Cited by 21
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González‐Aragón, D., Burón, M. I., López‐Lluch, G., Herman, M. D., Gómez-Dı́az, C., Navas, P., & Villalba, J. M. (2005) · BioFactors · doi:10.1002/biof.5520250105 · Cited by 21
Martino, G., Mugnai, C., Compagnone, D., Grotta, L., Carlo, M. D., & Sarti, F. M. (2014) · Animals · doi:10.3390/ani4020348 · Cited by 21
Yen, H., Liu, Y.-C., Kan, C.-C., Wei, H.-J., Lee, S., Wei, Y., Feng, Y.-H., Chen, C., & Huang, C. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.05.005 · Cited by 21
Baky, N. A. A., El-Orabi, N. F., Fadda, L. M., Abd-Elkader, O. H., & Ali, H. M. (2018) · Dose-Response · doi:10.1177/1559325818790158 · Cited by 23
Prosaposin regulates coenzyme Q10 levels in HepG2 cells, especially those in mitochondria
Kashiba, M., Oizumi, M., Suzuki, M., Sawamura, Y., Nagashima, K., Yoshimura, S., & Yamamoto, Y. (2014) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.13-106 · Cited by 22
Hermans, N., Cos, P., Meyer, G. R. Y. D., Maes, L. J. R. M., Pieters, L. A. C., Berghe, D. V., Vlietinck, A. J., & Bruyne, T. D. (2007) · Journal of Pharmacy and Pharmacology · doi:10.1211/jpp.59.1.0017 · Cited by 21
Fung, J. M.-W., Smith, R., Brown, M. A., Lau, S. H., Xie, D., Lau, G. K. K., & Guan, X. (2009) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-1472 · Cited by 21
Gutierrez-Mariscal, F. M., Yubero‐Serrano, E. M., Rangel-Zúñiga, O. A., Marı́n, C., García‐Ríos, A., Pérez‐Martínez, P., Delgado‐Lista, J., Malagón, M. M., Tinahones, F. J., Pérez‐Jiménez, F., et al. (2013) · The Journals of Gerontology Series A · doi:10.1093/gerona/glt174 · Cited by 21
Duberley, K. E. C., Hargreaves, I. P., Chaiwatanasirikul, K., Heales, S., Land, J. M., Rahman, S., Mills, K. A., & Eaton, S. D. (2013) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.6529 · Cited by 21
Awad, A. M., Venkataramanan, S., Nag, A., Galivanche, A. R., Bradley, M. C., Neves, L. T., Douglass, S., Clarke, C. F., & Johnson, T. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.798397 · Cited by 20
Soubeyrand, E., Kelly, M. E., Keene, S. A., Bernert, A. C., Latimer, S., Johnson, T. S., Elowsky, C. G., Colquhoun, T. A., Block, A. K., & Basset, G. J. C. (2019) · Biochemical Journal · doi:10.1042/bcj20190688 · Cited by 20
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Guile, M. D., Jain, A., Anderson, K. A., & Clarke, C. F. (2023) · Antioxidants · doi:10.3390/antiox12071391 · Cited by 22
Corral-Sarasa, J., Galvez, J. M. M., González‐García, P., Wendling, O., Jiménez-Sánchez, L., López-Herrador, S., Quinzii, C. M., Díaz-Casado, M. E., & López, L. C. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114148 · Cited by 20
Tang, M., Sperling, L. J., Berthold, D. A., Nesbitt, A. E., Gennis, R. B., & Rienstra, C. M. (2011) · Journal of the American Chemical Society · doi:10.1021/ja107775w · Cited by 20
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Khalili, M., & Ebrahimzadeh, M. A. (2015) · Majallah-i dānishgāh-i ̒ulūm-i pizishkī-i Māzandarān/Journal of Mazandaran University of Medical Sciences · Cited by 20
Coenzyme Q10 Intake From Food and Semen Parameters in a Subfertile Population
Tiseo, B. C., Gaskins, A. J., Hauser, R. B., Chavarro, J. E., & Tanrikut, C. (2016) · Urology · doi:10.1016/j.urology.2016.11.022 · Cited by 20
Yamada, Y., Burger, L., Kawamura, E., & Harashima, H. (2017) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b17-00609 · Cited by 20
HIF1a Inhibitor Rescues Acute-on-Chronic Liver Failure
Xie, F., Dong, J., Zhu, Y., Kefei, W., Liu, X., Chen, D., & Meng, Q. (2019) · Annals of Hepatology · doi:10.1016/j.aohep.2019.03.007 · Cited by 20
The activity of the DNA repair enzyme hOGG1 can be directly modulated by ubiquinol
Schniertshauer, D., Gebhard, D., van Beek, H., Nöth, V., Schon, J., & Bergemann, J. (2020) · DNA repair · doi:10.1016/j.dnarep.2019.102784 · Cited by 20
Mitochondrial diseases: expanding the diagnosis in the era of genetic testing
Saneto, R. P. (2020) · Journal of Translational Genetics and Genomics · doi:10.20517/jtgg.2020.40 · Cited by 21
Defining intermediates and redundancies in coenzyme Q precursor biosynthesis
Robinson, K. P., Jochem, A., Johnson, S. E., Reddy, T. R., Russell, J. D., Coon, J. J., & Pagliarini, D. J. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100643 · Cited by 19
Rao, R. N., Talluri, M. V. N. K., & Shinde, D. D. (2007) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2007.12.034 · Cited by 20
The Role of Direct and Indirect Polyphenolic Antioxidants in Protection Against Oxidative Stress
Christensen, L. P., & Christensen, K. B. (2013) · Polyphenols in Human Health and Disease · doi:10.1016/b978-0-12-398456-2.00023-2 · Cited by 20
Coenzyme Q is irreplaceable by demethoxy‐coenzyme Q in plasma membrane ofCaenorhabditis elegans
Arroyo, A., Santos‐Ocaña, C., Ruiz‐Ferrer, M., Padilla, S., Gavilán, Á., Rodríguez‐Aguilera, J. C., & Navas, P. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.02.025 · Cited by 20
Ca2+ increases the specific coenzyme Q10 content in Agrobacterium tumefaciens
Ha, S., Kim, S.-Y., Seo, J., Jeya, M., Zhang, Y., Ramu, T., Kim, I., & Lee, J.-K. (2009) · Bioprocess and Biosystems Engineering · doi:10.1007/s00449-009-0318-9 · Cited by 20
Lee, C.-F., LIU, C., CHEN, S., Sikorska, M., LIN, C., Chen, T., & Wei, Y. (2005) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1338.036 · Cited by 20
Metadata
- Authors
- Turunen, M., Olsson, J., & Dallner, G.
- Affiliations
- Karolinska University Hospital (SE)
- Karolinska Institutet (SE)
- Stockholm University (SE)
- Corresponding author
- Dallner, Gustav
- Venue
- Biochimica et Biophysica Acta (BBA) - Biomembranes
- Publisher
- Elsevier BV
- Published
- 2004-01
- Volume
- 1660
- Issue
- 1-2
- Pages
- 171-199
- ISSN
- 0005-2736 (ISSN-L)
- OpenAlex
- W1971714188
- Cited by
- 1,026
- References
- 323
- Citations by year
- 2026: 20 · 2025: 36 · 2024: 34 · 2023: 47 · 2022: 63 · 2021: 61 · 2020: 71 · 2019: 49 · 2018: 46 · 2017: 47 · 2016: 49 · 2015: 72 · 2014: 55 · 2013: 44 · 2012: 43
- FWCI
- 8.73
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Biomembranes (publishedVersion)
- PubMed (publishedVersion)
- 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
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Toxicology › Bioactive Compounds and Antitumor Agents
- Keywords
- coenzyme Q10, mitochondrial respiratory chain, coenzyme Q biosynthesis, cellular metabolism, nuclear transcription factors, nuclear receptors, signal transduction, aging, membrane localization
- MeSH terms
- Aging, Animals, Biological Transport, Diet, Escherichia coli, Half-Life, Humans, Mevalonic Acid, Oxidation-Reduction, Terpenes, Tissue Distribution, Ubiquinone, Models, Animal
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