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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
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Zorov, D. B., Juhaszova, M., & Sollott, S. J. (2014) · Physiological Reviews · doi:10.1152/physrev.00026.2013 · Cited by 5,383
Calcium, ATP, and ROS: a mitochondrial love-hate triangle
Brookes, P. S., Yoon, Y., Robotham, J. L., Anders, M. W., & Sheu, S.-S. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00139.2004 · Cited by 2,575
The role of iron and reactive oxygen species in cell death
Dixon, S. J., & Stockwell, B. R. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1416 · Cited by 2,381
Mills, E. L., Kelly, B., Logan, A., Costa, A. S. H., Varma, M., Bryant, C. E., Tourlomousis, P., Däbritz, J. H. M., Gottlieb, E., Latorre, I., et al. (2016) · Cell · doi:10.1016/j.cell.2016.08.064 · Cited by 2,291
Self-citationMelatonin as an antioxidant: under promises but over delivers
Reiter, R. J., Mayo, J. C., Tan, D. X., Sainz, R. M., Alatorre-Jiménez, M. A., & Qin, L. (2016) · Journal of Pineal Research · doi:10.1111/jpi.12360 · Cited by 1,777
Zielonka, J., Joseph, J., Sikora, A., Hardy, M., Ouari, O., Vasquez-Vivar, J., Cheng, G., Lopez, M., & Kalyanaraman, B. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00042 · Cited by 1,683
Bhatti, J. S., Bhatti, G. K., & Reddy, P. H. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.11.010 · Cited by 1,655
Targeting mitochondria for cancer therapy
Fulda, S., Galluzzi, L., & Kroemer, G. (2010) · Nature Reviews Drug Discovery · doi:10.1038/nrd3137 · Cited by 1,678
Li, N., Ragheb, K., Lawler, G., Sturgis, J., Rajwa, B. P., Melendez, J. A., & Robinson, J. P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210432200 · Cited by 1,465
Targeting Antioxidants to Mitochondria by Conjugation to Lipophilic Cations
Murphy, M. P., & Smith, R. A. J. (2007) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.47.120505.105110 · Cited by 1,173
Self-citationMitochondrial dysfunction and oxidative stress in heart disease
Peoples, J. N., Saraf, A., Ghazal, N., Pham, T. T., & Kwong, J. Q. (2019) · Experimental & Molecular Medicine · doi:10.1038/s12276-019-0355-7 · Cited by 950
Polyphenols and Human Health: Prevention of Disease and Mechanisms of Action
Vauzour, D., Rodriguez‐Mateos, A., Corona, G., Oruña-Concha, M. J., & Spencer, J. P. E. (2010) · Nutrients · doi:10.3390/nu2111106 · Cited by 885
Mitochondria as a therapeutic target for common pathologies
Murphy, M. P., & Hartley, R. C. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2018.174 · Cited by 846
Self-citationDistinct fission signatures predict mitochondrial degradation or biogenesis.
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Li, X., Fang, P., Mai, J., Choi, E. T., Wang, H., & Yang, X. (2013) · Journal of Hematology & Oncology · doi:10.1186/1756-8722-6-19 · Cited by 860
Zhao, K., Zhao, G.-M., Wu, D., Soong, Y., Birk, A. V., Schiller, P. W., & Szeto, H. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402999200 · Cited by 782
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Sivitz, W. I., & Yorek, M. A. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2531 · Cited by 742
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Dubois‐Deruy, E., Peugnet, V., Turkieh, A., & Pinet, F. (2020) · Antioxidants · doi:10.3390/antiox9090864 · Cited by 694
Mitochondrial dysfunction in diabetic kidney disease
Forbes, J. M., & Thorburn, D. R. (2018) · Nature Reviews Nephrology · doi:10.1038/nrneph.2018.9 · Cited by 650
Functions of ROS in Macrophages and Antimicrobial Immunity
Herb, M., & Schramm, M. (2021) · Antioxidants · doi:10.3390/antiox10020313 · Cited by 633
Targeting an antioxidant to mitochondria decreases cardiac ischemia-reperfusion injury
Adlam, V. J., Harrison, J. C., Porteous, C. M., James, A. M., Smith, R. A. J., Murphy, M. P., & Sammut, I. A. (2005) · The FASEB Journal · doi:10.1096/fj.05-3718com · Cited by 618
Self-citationOxidative stress and mitochondrial dysfunction in sepsis
Galley, H. F. (2011) · British Journal of Anaesthesia · doi:10.1093/bja/aer093 · Cited by 627
Josefsen, L. B., & Boyle, R. W. (2012) · Theranostics · doi:10.7150/thno.4571 · Cited by 589
A Mitochondrial Switch Promotes Tumor Metastasis
Porporato, P. E., Payen, V. L., Pérez‐Escuredo, J., Saedeleer, C. J. D., Danhier, P., Copetti, T., Dhup, S., Tardy, M., Vazeille, T., Bouzin, C., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.06.043 · Cited by 571
Targeting lipophilic cations to mitochondria
Murphy, M. P. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.03.029 · Cited by 598
Self-citationMelatonin as a mitochondria-targeted antioxidant: one of evolution's best ideas
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Animal and human studies with the mitochondria‐targeted antioxidant MitoQ
Smith, R. A. J., & Murphy, M. P. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05627.x · Cited by 560
Self-citationSources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation
Tejero, J., Shiva, S., & Gladwin, M. T. (2019) · Physiological Reviews · doi:10.1152/physrev.00036.2017 · Cited by 541
Snow, B. J., Rolfe, F. L., Lockhart, M. M., Frampton, C. M., O'Sullivan, J. D., Fung, V., Smith, R. A. J., Murphy, M. P., Taylor, K. M., & On behalf of the Protect Study Group (2010) · Movement Disorders · doi:10.1002/mds.23148 · Cited by 606
Self-citationColell, A., Ricci, J.-E., Tait, S., Milasta, S., Maurer, U., Bouchier-Hayes, L., Fitzgerald, P., Guio-Carrion, A., Waterhouse, N. J., Li, C. W., et al. (2007) · Cell · doi:10.1016/j.cell.2007.03.045 · Cited by 516
Ross, M. F., Kelso, G. F., Blaikie, F. H., James, A. M., Cochemé, H. M., Filipovska, A., Ros, T. D., Hurd, T. R., Smith, R. A. J., & Murphy, M. P. (2005) · Biochemistry (Moscow) · doi:10.1007/s10541-005-0104-5 · Cited by 504
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Zhang, W., Hu, X., Shen, Q., & Xing, D. (2019) · Nature Communications · doi:10.1038/s41467-019-09566-3 · Cited by 446
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Liu, S., Liu, J., Wang, Y., Deng, F., & Deng, Z. (2025) · MedComm · doi:10.1002/mco2.70268 · Cited by 485
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Hwang, P. M., Bunz, F., Yu, J., Rago, C., Chan, T. A.-T., Murphy, M. P., Kelso, G. F., Smith, R. A. J., Kinzler, K. W., & Vogelstein, B. (2001) · Nature Medicine · doi:10.1038/nm1001-1111 · Cited by 430
Self-citationTargeting antioxidants to mitochondria: A new therapeutic direction
Sheu, S., Nauduri, D., & Anders, M. W. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2005.10.007 · Cited by 417
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Miriyala, S., Spasojević, I., Tovmasyan, A. G., Salvemini, D., Vujašković, Ž., Clair, D. K. S., & Batinic̈‐Haberle, I. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.12.002 · Cited by 413
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Self-citationBioenergetic aspects of apoptosis, necrosis and mitoptosis
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Gane, E. J., Weilert, F., Orr, D. W., Keogh, G. F., Gibson, M., Lockhart, M. M., Frampton, C. M., Taylor, K. M., Smith, R. A. J., & Murphy, M. P. (2010) · Liver International · doi:10.1111/j.1478-3231.2010.02250.x · Cited by 379
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Fisicaro, P., Barili, V., Montanini, B., Acerbi, G., Ferracin, M., Guerrieri, F., Salerno, D., Boni, C., Massari, M., Cavallo, M. C., et al. (2017) · Nature Medicine · doi:10.1038/nm.4275 · Cited by 356
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Graham, D., Huynh, N. N., Hamilton, C. A., Beattie, E., Smith, R. A. J., Cochemé, H. M., Murphy, M. P., & Dominiczak, A. F. (2009) · Hypertension · doi:10.1161/hypertensionaha.109.130351 · Cited by 367
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James, A. M., Cochemé, H. M., Smith, R. A. J., & Murphy, M. P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501527200 · Cited by 353
Self-citationOsellame, L. D., Rahim, A. A., Hargreaves, I. P., Gegg, M. E., Richard-Loendt, A., Brandner, S., Waddington, S. N., Schapira, A. H. V., & Duchen, M. R. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.04.014 · Cited by 338
Antonenko, Y. N., Avetisyan, A. V., Bakeeva, L. E., Chernyak, B. V., Chertkov, V. A., Domnina, L. V., Ivanova, O. Y., Izyumov, D. S., Khailova, L. S., Klishin, S. S., et al. (2008) · Biochemistry (Moscow) · doi:10.1134/s0006297908120018 · Cited by 328
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Battogtokh, G., Choi, Y. S., Kang, D. S., Park, S. J., Shim, M. S., Huh, K. M., Cho, Y., Lee, J. Y., Lee, H. S., & Kang, H. C. (2018) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2018.05.006 · Cited by 318
Cassina, P., Cassina, A., Pehar, M., Castellanos, R., Gandelman, M., de León, A., Robinson, K. M., Mason, R. P., Beckman, J. S., Barbeito, L., et al. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.5308-07.2008 · Cited by 324
Murphy, M. P., Echtay, K. S., Blaikie, F. H., Asin-Cayuela, J., Cochemé, H. M., Green, K., Buckingham, J. A., Taylor, E. R., Hurrell, F., Hughes, G., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308529200 · Cited by 313
Self-citationMolecular Strategies for Targeting Antioxidants to Mitochondria: Therapeutic Implications
Apostolova, N., & Víctor, V. M. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.5952 · Cited by 311
Papucci, L., Schiavone, N., Witort, E. J., Donnini, M., Lapucci, A., Tempestini, A., Formigli, L., Zecchi‐Orlandini, S., Orlandini, G., Carella, G., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302297200 · Cited by 308
High anxiety trait: A vulnerable phenotype for stress-induced depression
Weger, M., & Sandi, C. (2018) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2018.01.012 · Cited by 289
Targeting mitochondria for cardiovascular disorders: therapeutic potential and obstacles
Bonora, M., Wieckowski, M. R., Sinclair, D. A., Kroemer, G., Pinton, P., & Galluzzi, L. (2018) · Nature Reviews Cardiology · doi:10.1038/s41569-018-0074-0 · Cited by 308
Mitochondria: regulators of signal transduction by reactive oxygen and nitrogen species
Brookes, P. S., Levonen, A.-L., Shiva, S., Sarti, P., & Darley-Usmar, V. M. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00901-2 · Cited by 298
Dong, L.-F., Low, P., Dyason, J. C., Wang, X.-F., Procházka, L., Witting, P. K., Freeman, R., Swettenham, E., Vališ, K., Liu, J., et al. (2008) · Oncogene · doi:10.1038/onc.2008.69 · Cited by 297
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Biswas, S., & Torchilin, V. P. (2013) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2013.11.004 · Cited by 298
Ilekis, J. V., Tsilou, E. T., Fisher, S. J., Abrahams, V. M., Soares, M. J., Cross, J. C., Zamudio, S., Illsley, N. P., Myatt, L., Colvis, C. M., et al. (2016) · American Journal of Obstetrics and Gynecology · doi:10.1016/j.ajog.2016.03.001 · Cited by 298
Koopman, W. J. H., Verkaart, S., Visch, H.-J., van der Westhuizen, F. H., Murphy, M. P., van den Heuvel, L. P., Smeitink, J. A. M., & Willems, P. H. G. M. (2005) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00607.2004 · Cited by 296
Self-citationMitochondria: A therapeutic target in neurodegeneration
Moreira, P. I., Zhu, X., Wang, X., Lee, H., Nunomura, A., Petersen, R. B., Perry, G. L., & Smith, M. A. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.10.007 · Cited by 292
Sandoval-Acuña, C., Ferreira, J., & Speisky, H. (2014) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2014.05.017 · Cited by 288
Biswas, S., Dodwadkar, N. S., Deshpande, P. P., & Torchilin, V. P. (2012) · Journal of Controlled Release · doi:10.1016/j.jconrel.2012.01.009 · Cited by 281
Functional Estrogen Receptors in the Mitochondria of Breast Cancer Cells
Pedram, A., Razandi, M., Wallace, D. C., & Levin, E. R. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-11-1013 · Cited by 282
Gallium and its competing roles with iron in biological systems
Chitambar, C. R. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.04.027 · Cited by 287
Charlton, N. C., Mastyugin, M., Török, B., & Török, M. (2023) · Molecules · doi:10.3390/molecules28031057 · Cited by 292
Vawter, M. (2002) · Schizophrenia Research · doi:10.1016/s0920-9964(01)00377-2 · Cited by 275
Functional role of mitochondrial reactive oxygen species in physiology
Angelova, P. R., & Abramov, A. Y. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.06.005 · Cited by 275
Lee, J. H., Park, A., Oh, K., Lee, S. C., Kim, W. K., & Bae, K. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20194924 · Cited by 280
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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