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Selective Targeting of a Redox-active Ubiquinone to Mitochondria within Cells
Open accessAbstract
With the recognition of the central role of mitochondria in apoptosis, there is a need to develop specific tools to manipulate mitochondrial function within cells. Here we report on the development of a novel antioxidant that selectively blocks mitochondrial oxidative damage, enabling the roles of mitochondrial oxidative stress in different types of cell death to be inferred. This antioxidant, named mitoQ, is a ubiquinone derivative targeted to mitochondria by covalent attachment to a lipophilic triphenylphosphonium cation through an aliphatic carbon chain. Due to the large mitochondrial membrane potential, the cation was accumulated within mitochondria inside cells, where the ubiquinone moiety inserted into the lipid bilayer and was reduced by the respiratory chain. The ubiquinol derivative thus formed was an effective antioxidant that prevented lipid peroxidation and protected mitochondria from oxidative damage. After detoxifying a reactive oxygen species, the ubiquinol moiety was regenerated by the respiratory chain enabling its antioxidant activity to be recycled. In cell culture studies, the mitochondrially localized antioxidant protected mammalian cells from hydrogen peroxide-induced apoptosis but not from apoptosis induced by staurosporine or tumor necrosis factor-alpha. This was compared with untargeted ubiquinone analogs, which were ineffective in preventing apoptosis. These results suggest that mitochondrial oxidative stress may be a critical step in apoptosis induced by hydrogen peroxide but not for apoptosis induced by staurosporine or tumor necrosis factor-alpha. We have shown that selectively manipulating mitochondrial antioxidant status with targeted and recyclable antioxidants is a feasible approach to investigate the role of mitochondrial oxidative damage in apoptotic cell death. This approach will have further applications in investigating mitochondrial dysfunction in a range of experimental models.
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In the citing paper
“There is extensive in vitro evidence that the concentrations of MitoQ used here have no impact on mitochondrial functions, such as ATP production, membrane potential, or ROS production in cells or mitochondria, but do prevent mitochondrial oxidative damage under conditions that lead to oxidative stress (Kelso et al., 2001; Jauslin et al., 2003; Saretzki et al., 2003; Asin-Cayuelaa et al., 2004).”
From The mitochondria-targeted antioxidant MitoQ prevents loss of spatial memory retention and early neuropathology in a transgenic mouse model of Alzheimer’s disease (2011) · cites this paper as Kelso et al., 2001
In the citing paper
“This small molecule consists of the antioxidant ubiquinol linked to the lipophilic cation triphenylphosphonium (500).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [500]
In the citing paper
“Moreover, treatment with MitoQ, a substance known to scavenge matrix mtROS (see Section 6) [314,315], gave contrasting results: only IL-1β cleavage was reduced, whereas TNF and IL-10 levels remained unaltered.”
From Functions of ROS in Macrophages and Antimicrobial Immunity (2021) · cites this paper as [315]
In the citing paper
“whereas MitoQ is an analog of ubiquinone and prevents lipid peroxidation in mitochondrial membranes [314,315].”
From Functions of ROS in Macrophages and Antimicrobial Immunity (2021) · cites this paper as [315]
In the citing paper
“One approach to this involves the synthesis of compounds linking agents such as redox forms of quinone (ubiquinol and ubiquinone) or vitamin E to form alkylated triphenylphosphonium compounds. These are lipophilic cations avidly taken up into the relatively negative mitochondrial matrix (162).”
From Mitochondrial Dysfunction in Diabetes: From Molecular Mechanisms to Functional Significance and Therapeutic Opportunities (2010) · cites this paper as [162]
In the citing paper
“Two such compounds (alkyltriphenylphosphonium cations) incorporating ubiquinone or vitamin E, termed mitoQ and mitoVit E, respectively, have been synthesized (162).”
From Mitochondrial Dysfunction in Diabetes: From Molecular Mechanisms to Functional Significance and Therapeutic Opportunities (2010) · cites this paper as [162]
Citations
Cites
DETERMINATION OF SERUM PROTEINS BY MEANS OF THE BIURET REACTION
Gornall, A. G., Bardawill, C. J., & David, M. M. (1949) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)57021-6 · Cited by 16,164
Beckman, J. S., Beckman, T. W., Chen, J., Marshall, P. A., & Freeman, B. A. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.4.1620 · Cited by 7,029
Oxidants, antioxidants, and the degenerative diseases of aging.
Ames, B. N., Shigenaga, M. K., & Hagen, T. M. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.17.7915 · Cited by 5,958
The Free Radical Theory of Aging Matures
BECKMAN, K. B., & AMES, B. N. (1998) · Physiological Reviews · doi:10.1152/physrev.1998.78.2.547 · Cited by 3,879
Luo, X., Budihardjo, I., Zou, H., Slaughter, C., & Wang, X. (1998) · Cell · doi:10.1016/s0092-8674(00)81589-5 · Cited by 3,626
Mitochondrial diseases in man and mouse
Wallace, D. C. (1999) · Science · doi:10.1126/science.283.5407.1482 · Cited by 3,060
A model for p53-induced apoptosis
Polyak, K., Xia, Y., Zweier, J. L., Kinzler, K. W., & Vogelstein, B. (1997) · Nature · doi:10.1038/38525 · Cited by 2,500
THE MITOCHONDRIAL DEATH/LIFE REGULATOR IN APOPTOSIS AND NECROSIS
Kroemer, G., Dallaporta, B., & Resche-Rigon, M. (1998) · Annual Review of Physiology · doi:10.1146/annurev.physiol.60.1.619 · Cited by 1,975
Michikawa, Y., Mazzucchelli, F., Bresolin, N., Scarlato, G., & Attardi, G. M. (1999) · Science · doi:10.1126/science.286.5440.774 · Cited by 724
Dual regulation of caspase activity by hydrogen peroxide: implications for apoptosis
Hampton, M. B., & Orrenius, S. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01068-5 · Cited by 663
Flagged first, then by citations
Research works printed but not linked: 2
- Ernster, 1992, Biofactors, 3, 241
- Schopfer, 2000, Biochem. J., 349, 35, 10.1042/bj3490035 · DOI
Cited by
Sorted by citations
Items 501–600 of 1,000
Nochi, Z., Olsen, R. K. J., & Gregersen, N. (2017) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-017-0047-1 · Cited by 49
Reactive Species in Huntington Disease: Are They Really the Radicals You Want to Catch?
Bono-Yagüe, J., Gómez-Escribano, A. P., Millán, J. M., & Vázquez‐Manrique, R. P. (2020) · Antioxidants · doi:10.3390/antiox9070577 · Cited by 52
NKX3.1 Localization to Mitochondria Suppresses Prostate Cancer Initiation
Papachristodoulou, A., Rodríguez-Calero, A., Panja, S., Margolskee, E. M., Virk, R. K., Milner, T. A., Martina, L. P., Kim, J. Y., Bernardo, M. D., Williams, A. B., et al. (2021) · Cancer Discovery · doi:10.1158/2159-8290.cd-20-1765 · Cited by 51
Mao, G., Kraus, G. A., Kim, I., Spurlock, M. E., Bailey, T. B., Zhang, Q., & Beitz, D. C. (2010) · The Journal of Nutrition · doi:10.3945/jn.110.121715 · Cited by 48
Shyam, R., Ogando, D. G., Choi, M., Liton, P. B., & Bonanno, J. A. (2021) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.62.12.15 · Cited by 48
Mechanisms of Mitochondrial Malfunction in Alzheimer’s Disease: New Therapeutic Hope
Nabi, S. U., Khan, A., Siddiqui, E. M., Rehman, M. U., Alshahrani, S., Arafah, A. M., Mehan, S., Alsaffar, R. M., Alexiou, A. T., & Shen, B. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/4759963 · Cited by 51
Zhao, L., Ling, L., Lu, J., Jiang, F., Sun, J., Zhang, Z., Huang, Y., Liu, X., Zhu, Y., Fu, X., et al. (2022) · Bioengineering & Translational Medicine · doi:10.1002/btm2.10460 · Cited by 48
Plecitá‐Hlavatá, L., Ježek, J., & Ježek, P. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.02.015 · Cited by 49
Ripcke, J., Zarse, K., Ristow, M., & Birringer, M. (2009) · ChemBioChem · doi:10.1002/cbic.200900159 · Cited by 48
Antioxidants successfully reduce ROS production in propionic acidemia fibroblasts
Gallego‐Villar, L., Pérez, B., Ugarte, M., Desviat, L. R., & Richard, E. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.08.091 · Cited by 48
Mitochondria dysfunction: A novel therapeutic target in pathological lung remodeling or bystander?
Rowlands, D. J. (2016) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2016.06.019 · Cited by 48
Responsive hetero-organelle partition conferred fluorogenic sensing of mitochondrial depolarization
Xue, Z., Zhao, H., Liu, J., Han, J., & Han, S. (2016) · Chemical Science · doi:10.1039/c6sc04158b · Cited by 48
New opportunities for targeting redox dysregulation in cardiovascular disease
Bubb, K. J., Drummond, G. R., & Figtree, G. A. (2019) · Cardiovascular Research · doi:10.1093/cvr/cvz183 · Cited by 50
Arauna, D., Furrianca, M. C., Espinosa‐Parrilla, Y., Eduardo Fuentes, Q., Alarcón, M. A., & Palomo, I. F. (2019) · Molecules · doi:10.3390/molecules24234259 · Cited by 50
Broome, S. C., Pham, T., Braakhuis, A. J., Narang, R. K., Wang, H. W., Hickey, A. J., Mitchell, C. J., & Merry, T. L. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102341 · Cited by 48
The role of mitochondrial reactive oxygen species in insulin resistance
Ayer, A., Fazakerley, D. J., James, D. E., & Stocker, R. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.11.007 · Cited by 50
Leo, S., Szabadkai, G., & Rizzuto, R. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1427.019 · Cited by 48
Fearon, I. M. (2006) · Cardiovascular Research · doi:10.1016/j.cardiores.2005.11.019 · Cited by 47
Protective effect of tubuloside B on TNFalpha-induced apoptosis in neuronal cells.
MinDENG, Jin-yuanZHAO, Xiao-dongJU, Peng-feiTU, Yong-jiang, & Zheng-binLI (2004) · PubMed · Cited by 46
Synthesis of triphenylphosphonium vitamin E derivatives as mitochondria-targeted antioxidants
Jameson, V. J. A., Cochemé, H. M., Logan, A., Hanton, L. R., Smith, R. A. J., & Murphy, M. P. (2015) · Tetrahedron · doi:10.1016/j.tet.2015.09.014 · Cited by 47
Self-citationSilachev, D. N., Исаев, Н. К., Pevzner, I. B., Zorova, L. D., Stelmashook, E. V., Novikova, S. V., Plotnikov, E. Y., Skulachev, V. P., & Zorov, D. B. (2012) · PLoS ONE · doi:10.1371/journal.pone.0051553 · Cited by 46
Pandareesh, M. D., Shrivash, M. K., Kumar, H. N. N., Misra, K., & Bharath, M. M. S. (2016) · Neurochemical Research · doi:10.1007/s11064-016-2034-6 · Cited by 46
Zhang, S., Li, J., Hu, S., Wu, F., & Zhang, X. (2018) · International Journal of Nanomedicine · doi:10.2147/ijn.s165590 · Cited by 46
Loss of Mitochondrial Control Impacts Renal Health
Srivastava, S. P., Kanasaki, K., & Goodwin, J. E. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.543973 · Cited by 48
Shang, Y., Xue, W., Kong, J., Chen, Y., Qiu, X., An, X., Li, Y., Wang, H., & An, J. (2021) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2021.151899 · Cited by 45
Martel, C., Huynh, L. H., Garnier, A., Ventura‐Clapier, R., & Brenner, C. (2012) · Biochemistry Research International · doi:10.1155/2012/213403 · Cited by 47
Long-Circulating Amphiphilic Doxorubicin for Tumor Mitochondria-Specific Targeting
Xi, J., Li, M. C., Jing, B., An, M., Yu, C., Pinnock, C. B., Zhu, Y., Lam, M. T., & Liu, H. (2018) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.8b17399 · Cited by 45
Lin, P., & Duann, P. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.01050 · Cited by 45
Serviddio, G., Romano, A. D., Cassano, T., Bellanti, F., Altomare, E., & Vendemiale, G. (2011) · Current Pharmaceutical Design · doi:10.2174/138161211796904740 · Cited by 45
Truksa, J., Dong, L., Rohlena, J., Štursa, J., Vondrusová, M., Goodwin, J., Nguyen, M. N., Kľučková, K., Rychtarčíková, Z., Lettlová, S., et al. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5594 · Cited by 44
Pátková, J., Anděl, M., & Trnka, J. (2014) · Cellular Physiology and Biochemistry · doi:10.1159/000358709 · Cited by 46
Whiteman, M., Spencer, J. P. E., Szeto, H. H., & Armstrong, J. S. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1879 · Cited by 44
Misfolding of short-chain acyl-CoA dehydrogenase leads to mitochondrial fission and oxidative stress
Schmidt, S. P., Corydon, T. J., Pedersen, C. B., Bross, P., & Gregersen, N. V. (2010) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2010.03.009 · Cited by 45
Roles of reactive oxygen species and selected antioxidants in regulation of cellular metabolism.
Stańczyk, M. B., Gromadzińska, J., & Wąsowicz, W. (2005) · PubMed · Cited by 44
Mitochondrial medicine and the neurodegenerative mitochondriopathies
Swerdlow, R. H. (2009) · Pharmaceuticals · doi:10.3390/ph2030150 · Cited by 43
Cunniff, B., Benson, K., Stumpff, J. K., Newick, K., Held, P., Taatjes, D. J., Joseph, J., Kalyanaraman, B., & Heintz, N. H. (2012) · Journal of Cellular Physiology · doi:10.1002/jcp.24232 · Cited by 43
MitoQ Blunts Mitochondrial and Renal Damage during Cold Preservation of Porcine Kidneys
Parajuli, N., Campbell, L. H., Marine, A., Brockbank, K. G. M., & MacMillan-Crow, L. A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0048590 · Cited by 43
Alkhaldi, A. A. M., Martínek, J., Panicucci, B., Dardonville, C. Y., Zı́ková, A., & de Koning, H. P. (2015) · International Journal for Parasitology Drugs and Drug Resistance · doi:10.1016/j.ijpddr.2015.12.002 · Cited by 43
Mitochondrial dysfunction activates lysosomal-dependent mitophagy selectively in cancer cells
Biel, T. G., & Rao, V. A. (2017) · Oncotarget · doi:10.18632/oncotarget.23171 · Cited by 44
Erlich, J. R., To, E. E., Liong, S., Brooks, R. D., Vlahos, R., O’Leary, J. J., Brooks, D. A., & Selemidis, S. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8028 · Cited by 45
Xu, K., Chen, J., Kong, X., Mu, F., Lu, T., & Lu, Y. (2020) · Medical Gas Research · doi:10.4103/2045-9912.285560 · Cited by 43
NAD Depletion Mediates Cytotoxicity in Human Neurons With Autophagy Deficiency
Sun, C., Seranova, E., Cohen, M. A., Chipara, M., Roberts, J., Astuti, D., Palhegyi, A. M., Acharjee, A., Sedlackova, L., Kataura, T., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2023.112372 · Cited by 43
Self-citationXu, Y., & Kalyanaraman, B. (2006) · Free Radical Research · doi:10.1080/10715760600911147 · Cited by 43
Ferroptosis contributes to catecholamine-induced cardiotoxicity and pathological remodeling
Chen, Y., Guo, X., Zeng, Y., Mo, X., Hong, S., He, H., Li, J., Steinmetz, R. N., & Liu, Q. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.07.025 · Cited by 42
Mitochondria-targeted penetrating cations as carriers of hydrophobic anions through lipid membranes
Rokitskaya, T. I., Sumbatyan, N. V., Tashlitsky, V. N., Korshunova, G. A., Antonenko, Y. N., & Skulachev, V. P. (2010) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2010.05.018 · Cited by 42
Effect of long-term maternal smoking on the offspring’s lung health
Sukjamnong, S., Chan, Y. L., Zakarya, R., Saad, S., Sharma, P. K., Santiyanont, R., Chen, H., & Oliver, B. G. G. (2017) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00134.2017 · Cited by 42
Targeted Antioxidants in Exercise-Induced Mitochondrial Oxidative Stress: Emphasis on DNA Damage
Williamson, J., & Davison, G. W. (2020) · Antioxidants · doi:10.3390/antiox9111142 · Cited by 43
Scott, H., Phillips, T. J., Sze, Y., Alfieri, A., Rogers, M. F., Volpato, V., Case, C. P., & Brunton, P. J. (2020) · Neurobiology of Stress · doi:10.1016/j.ynstr.2020.100281 · Cited by 43
Kim, A., Murphy, M., & Oberley, T. (2005) · Free Radical Biology & Medicine · doi:10.1016/j.freeradbiomed.2004.10.030 · Cited by 46
Self-citationPalao‐Suay, R., Aguilar, M. R., Parra-Ruiz, F. J., Fernández‐Gutiérrez, M., Parra, J., Sánchez‐Rodríguez, C., Fernández, R. S., Rodrigáñez, L., & Román, J. S. (2015) · Biomacromolecules · doi:10.1021/acs.biomac.5b00130 · Cited by 41
Loss of Mcl-1 Protein and Inhibition of Electron Transport Chain Together Induce Anoxic Cell Death
Brunelle, J. K., Shroff, E. H., Perlman, H., Strasser, A., Moraes, C. T., Flavell, R. A., Danial, N. N., Keith, B., Thompson, C. B., & Chandel, N. S. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01535-06 · Cited by 41
Targeting mitochondrial function to treat optic neuropathy
Gueven, N., Nadikudi, M., Daniel, A., & Chhetri, J. (2016) · Mitochondrion · doi:10.1016/j.mito.2016.07.013 · Cited by 40
Aiming for the target: Mitochondrial drug delivery in traumatic brain injury
Lamade, A. M., Kenny, E., Anthonymuthu, T. S., Soysal, E., Clark, R. S. B., Kagan, V. E., & Bayır, H. (2018) · Neuropharmacology · doi:10.1016/j.neuropharm.2018.07.014 · Cited by 41
Xu, K., Chen, J., Kong, X., Qian, W., Mu, F., Lu, T., & Lu, Y. (2020) · Medical Gas Research · doi:10.4103/2045-9912.304221 · Cited by 41
Kumar, P., Wang, M., Isachenko, E., Rahimi, G., Mallmann, P. K., Wang, W., von Brandenstein, M., & Isachenko, V. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.672862 · Cited by 41
Duveau, D. Y., Arce, P. M., Schoenfeld, R. A., Raghav, N., Cortopassi, G. A., & Hecht, S. M. (2010) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2010.06.104 · Cited by 40
Fluorescence microscopy imaging of mitochondrial metabolism in cancer cells
Gooz, M. B., & Maldonado, E. N. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1152553 · Cited by 44
Fluorogenic Ubiquinone Analogue for Monitoring Chemical and Biological Redox Processes
Greene, L. E., Godin, R., & Cosa, G. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b06899 · Cited by 39
Mitochondria and Nucleus Dual Delivery System To Overcome DOX Resistance
Cui, H., Huan, M., Ye, W., Liu, D., Teng, Z., Mei, Q., & Zhou, S. (2017) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.6b01016 · Cited by 39
Mitochondria-Targeted Compounds to Assess and Improve Human Sperm Function
Escada‐Rebelo, S., Cristo, M. I., Ramalho‐Santos, J., & Amaral, S. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2021.0238 · Cited by 40
Han, L., Xie, L., Li, L.-H., Zhang, X., Zhang, R., & Wang, H. (2009) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2009.03.005 · Cited by 39
Death-associated Protein Kinase as a Sensor of Mitochondrial Membrane Potential
Shang, T., Joseph, J., Hillard, C. J., & Kalyanaraman, B. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506466200 · Cited by 39
Mitochondrial Targeted Antioxidant in Cerebral Ischemia
Ahmed, E., Donovan, T., Yujiao, L., & Zhang, Q. (2015) · Journal of Neurology and Neuroscience · doi:10.21767/2171-6625.100017 · Cited by 38
Bandaru, L. J. M., Ayyalasomayajula, N., Murumulla, L., & Challa, S. (2022) · BioMetals · doi:10.1007/s10534-021-00360-7 · Cited by 39
Yang, H., Korivi, M., Lin, M., Chen, S., Chou, C., & Hseu, Y. (2015) · Biochemical Pharmacology · doi:10.1016/j.bcp.2015.09.003 · Cited by 38
Targeting Mitochondria as Therapeutic Strategy for Metabolic Disorders
Sorriento, D., Pascale, A. V., Finelli, R., Carillo, A. L., Annunziata, R., Trimarco, B., & Iaccarino, G. (2014) · The Scientific World JOURNAL · doi:10.1155/2014/604685 · Cited by 39
RetractedMultiple Triphenylphosphonium Cations Shuttle a Hydrophilic Peptide into Mitochondria
Abu-Gosh, S. E., Kolvazon, N., Tirosh, B., Ringel, I., & Yavin, E. (2009) · Molecular Pharmaceutics · doi:10.1021/mp900032r · Cited by 38
Effects of the Mitochondria‐Targeted Antioxidant Mitoquinone in Murine Acute Pancreatitis
Huang, W., Cash, N. J., Li, W., Szatmary, P., Mukherjee, R., Armstrong, J. A., Chvanov, M., Tepikin, A. V., Murphy, M. P., Sutton, R., et al. (2015) · Mediators of Inflammation · doi:10.1155/2015/901780 · Cited by 38
Self-citationTeixeira, J., Soares, P., Benfeito, S., Gaspar, A., Garrido, J. M. P. J., Murphy, M. P., & Borges, F. (2012) · Free Radical Research · doi:10.3109/10715762.2012.662593 · Cited by 40
Self-citationBond, S. T., Kim, J., Calkin, A. C., & Drew, B. G. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00543 · Cited by 38
Kim, Y., Kumar, A., Chang, C., & Pyaram, K. (2017) · The Journal of Immunology · doi:10.4049/jimmunol.1700567 · Cited by 39
Coenzyme Q Functionalized CdTe/ZnS Quantum Dots for Reactive Oxygen Species (ROS) Imaging
Qin, L., Ma, W., Li, D., Li, Y., Chen, X. S., Kraatz, H., James, T. D., & Long, Y. (2011) · Chemistry - A European Journal · doi:10.1002/chem.201003749 · Cited by 38
Gan, L., Wang, Z., Si, J., Zhou, R., Sun, C., Liu, Y., Ye, Y., Zhang, Y., Liu, Z., & Zhang, H. (2018) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2018.01.003 · Cited by 37
The role of mitochondria in metabolic disease: a special emphasis on heart dysfunction
Federico, M., de la Fuente, S., Palomeque, J., & Sheu, S. (2021) · The Journal of Physiology · doi:10.1113/jp279376 · Cited by 37
Hamed, M. O., Logan, A., Gruszczyk, A. V., Beach, T. E., James, A. M., Dare, A. J., Barlow, A. D., Martin, J. L., Georgakopoulos, N., Gane, A., et al. (2021) · British journal of surgery · doi:10.1093/bjs/znab108 · Cited by 37
Self-citationMetabolic manipulators: a well founded strategy to combat mitochondrial dysfunction
Koene, S., & Smeitink, J. A. M. (2010) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-010-9162-y · Cited by 38
Schauen, M., Spitkovsky, D., Schubert, J., Fischer, J. H., Hayashi, J., & Wiesner, R. J. (2006) · Journal of Cellular Physiology · doi:10.1002/jcp.20711 · Cited by 37
Liu, Y., Liu, Y., Shi, P., Hu, X., Fan, X., Wu, Y., Pan, J., Bai, Q., & Li, Q. (2024) · Journal of Nanobiotechnology · doi:10.1186/s12951-024-02924-4 · Cited by 36
Young, K. A., Hosseini, M., Mistry, J. J., Morganti, C., Mills, T., Cai, X., James, B., Nye, G. J., Fournier, N. R., Voisin, V., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-57238-2 · Cited by 36
Aurousseau, B., Gruffat, D., & Durand, D. (2006) · annales de biologie animale biochimie biophysique · doi:10.1051/rnd:2006045 · Cited by 39
H. Swerdlow, R. (2011) · Current Pharmaceutical Design · doi:10.2174/138161211798072535 · Cited by 35
Yo, K., Yu, Y., Zhao, G., Bonab, A. A., Aikawa, N., Tompkins, R. G., & Fischman, A. J. (2012) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00098.2012 · Cited by 35
Treatment with antioxidants ameliorates oxidative damage in a mouse model of propionic acidemia
Rivera‐Barahona, A., Alonso-Barroso, E., Pérez, B., Murphy, M. P., Richard, E., & Desviat, L. R. (2017) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2017.07.009 · Cited by 37
Self-citationSingh‐Mallah, G., Nair, S., Sandberg, M., Mallard, C. E., & Hagberg, H. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7779 · Cited by 35
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Metadata
- Authors
- Kelso, G. F., Porteous, C. M., Coulter, C. V., Hughes, G., Porteous, W. K., Ledgerwood, E. C., Smith, R. A. J., & Murphy, M. P.
- Affiliations
- University of Otago (NZ)
- Corresponding author
- Murphy, Michael P.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2001-02
- Volume
- 276
- Issue
- 7
- Pages
- 4588-4596
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2017692041
- Cited by
- 1,091
- References
- 51
- Citations by year
- 2026: 33 · 2025: 33 · 2024: 53 · 2023: 52 · 2022: 57 · 2021: 65 · 2020: 60 · 2019: 43 · 2018: 57 · 2017: 50 · 2016: 52 · 2015: 51 · 2014: 43 · 2013: 37 · 2012: 47
- FWCI
- 7.80
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- 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 › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- MitoQ, mitochondrial targeting, triphenylphosphonium cation, mitochondrial membrane potential, mitochondrial oxidative stress, hydrogen peroxide-induced apoptosis, staurosporine-induced apoptosis, lipid peroxidation, electron transport chain, mitochondrial dysfunction
- MeSH terms
- Animals, Antioxidants, Biological Transport, Active, Cattle, Cell Survival, Electron Transport, Humans, Hydrogen Peroxide, Mitochondria, Multienzyme Complexes, Organophosphorus Compounds, Oxidation-Reduction, Tumor Cells, Cultured, Ubiquinone, Apoptosis, Oxidative Stress, Jurkat Cells, Rats
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