The DOI matches its Crossref record; 130 of the 130 references it cites were found in a registry or an index.
Targeting Antioxidants to Mitochondria by Conjugation to Lipophilic Cations
Abstract
Mitochondrial oxidative damage contributes to a range of degenerative diseases. Consequently, the selective inhibition of mitochondrial oxidative damage is a promising therapeutic strategy. One way to do this is to invent antioxidants that are selectively accumulated into mitochondria within patients. Such mitochondria-targeted antioxidants have been developed by conjugating the lipophilic triphenylphosphonium cation to an antioxidant moiety, such as ubiquinol or α-tocopherol. These compounds pass easily through all biological membranes, including the blood-brain barrier, and into muscle cells and thus reach those tissues most affected by mitochondrial oxidative damage. Furthermore, because of their positive charge they are accumulated several-hundredfold within mitochondria driven by the membrane potential, enhancing the protection of mitochondria from oxidative damage. These compounds protect mitochondria from damage following oral delivery and may therefore form the basis for mitochondria-protective therapies. Here we review the background and work to date on this class of mitochondria-targeted antioxidants.
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In the citing paper
“MitoQ rapidly crosses the blood– brain barrier and neuronal membranes and concentrates several hundred-fold in mitochondria driven by the high membrane potential across the inner mitochondrial membrane (IMM; Murphy and Smith, 2007).”
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 Murphy and Smith, 2007
In the citing paper
“The recently developed, mitochondria-targeted antioxidant MitoQ (mitoquinone mesylate: [10-(4,5-dimethoxy-2-methyl-3,6-dioxo-1,4-cycloheexadienlyl) decyl triphenylphosphonium methanesulfonate]) possesses these qualities (James et al., 2005, 2007; Murphy and Smith, 2007).”
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 Murphy and Smith, 2007
In the citing paper
“Although in most cases this semiquinone is rapidly oxidized, its reaction with oxygen leads to superoxide production at this site (567, 678).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [678]
In the citing paper
“Although the majority of electrons entering the ETC ultimately reduce oxygen to water at complex IV, a small proportion (~2–11%) of electrons escape from the chain at complex I or III to generate superoxide (34, 115, 678).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [678]
In the citing paper
“Importantly, specific complex III inhibitors, such as Antimycin A, can stabilize this semiquinone radical, significantly enhancing superoxide production by complex III (678).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [678]
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 [314]
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 [314]
In the citing paper
“MitoTEMPO is a combination of the antioxidant TEMPO attached to the TPP group and hence dismutates O2●− to H2O2 in the mitochondrial matrix [314,391]”
From Functions of ROS in Macrophages and Antimicrobial Immunity (2021) · cites this paper as [314]
In the citing paper
“MitoTEMPO and MitoQ both are targeted to and accumulated in mitochondria due to their TPP group.”
From Functions of ROS in Macrophages and Antimicrobial Immunity (2021) · cites this paper as [314]
Citations
Cites
Lipinski, C. A., Lombardo, F., Dominy, B. W., & Feeney, P. J. (2001) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(00)00129-0 · Cited by 18,139
Lipinski, C. A., Lombardo, F., Dominy, B. W., & Feeney, P. J. (1997) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(96)00423-1 · Cited by 11,484
Biochemistry and molecular cell biology of diabetic complications
Brownlee, M. (2001) · Nature · doi:10.1038/414813a · Cited by 9,107
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
Mitochondria, Oxidants, and Aging
Balaban, R. S., Nemoto, S., & Finkel, T. (2005) · Cell · doi:10.1016/j.cell.2005.02.001 · Cited by 4,388
BIOCHEMISTRY OF MULTIDRUG RESISTANCE MEDIATED BY THE MULTIDRUG TRANSPORTER
Gottesman, M. M., & PASTAN, I. (1993) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.62.070193.002125 · Cited by 3,569
The Pathophysiology of Mitochondrial Cell Death
Green, D. R., & Kroemer, G. (2004) · Science · doi:10.1126/science.1099320 · Cited by 3,487
Mitochondrial diseases in man and mouse
Wallace, D. C. (1999) · Science · doi:10.1126/science.283.5407.1482 · Cited by 3,060
Strategies of antioxidant defense
SIES, H. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb18025.x · Cited by 1,976
Research works printed but not linked: 4
- Nicholls DG, 2002, Bioenergetics 3
- Ross MF, 2005, Biochemistry, 70, 222
- Pletjushkina OY, 2006, Biochemistry, 71, 60
- Calabrese EJ, 2006, Curr. Opin. Drug Discov. Dev, 9, 117
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Mróz, P., Pawlak, A. M., Satti, M., Lee, H., Wharton, T., Gali, H., Sarna, T., & Hamblin, M. R. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.05.005 · Cited by 260
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Neužil, J., Dong, L., Rohlena, J., Truksa, J., & Ralph, S. J. (2012) · Mitochondrion · doi:10.1016/j.mito.2012.07.112 · Cited by 255
Umehara, T., Winstanley, Y. E., Andreas, E., Morimoto, A., Williams, E. J., Smith, K. M., Carroll, J., Febbraio, M. A., Shimada, M., Russell, D. L., et al. (2022) · Science Advances · doi:10.1126/sciadv.abn4564 · Cited by 250
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Xu, J., Chi, F., Guo, T., Punj, V., Lee, W. N. P., French, S. W., & Tsukamoto, H. (2015) · Journal of Clinical Investigation · doi:10.1172/jci76468 · Cited by 241
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James, A. M., Sharpley, M. S., Manas, A.-R. B., Frerman, F. E., Hirst, J., Smith, R. A. J., & Murphy, M. P. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611463200 · Cited by 262
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Zhang, Y., Khalique, A., Du, X., Gao, Z., Wu, J., Zhang, X., Zhang, R., Sun, Z., Liu, Q., Xu, Z., et al. (2021) · Advanced Materials · doi:10.1002/adma.202006570 · Cited by 233
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Cao, H., Cheng, Y., Gao, H., Zhuang, J., Zhang, W., Bian, Q., Wang, F., Du, Y., Li, Z., Kong, D., et al. (2020) · ACS Nano · doi:10.1021/acsnano.9b08207 · Cited by 220
Cunha‐Oliveira, T., Montezinho, L., Mendes, C., Firuzi, O., Saso, L., Oliveira, P. J., & Silva, F. S. G. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/5021694 · Cited by 220
Maharjan, S., Oku, M., Tsuda, M., Hoseki, J., & Sakai, Y. (2014) · Scientific Reports · doi:10.1038/srep05896 · Cited by 212
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Self-citationBayır, H., & Kagan, V. E. (2008) · Critical Care · doi:10.1186/cc6779 · Cited by 202
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Skulachev, V. P. (2007) · Biochemistry (Moscow) · doi:10.1134/s0006297907120139 · Cited by 190
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Reddy, P. H. (2009) · CNS Spectrums · doi:10.1017/s1092852900024901 · Cited by 192
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Zhang, L., Wang, D., Yang, K., Sheng, D., Tan, B., Wang, Z., Ran, H., Yi, H., Zhong, Y., Lin, H., et al. (2018) · Advanced Science · doi:10.1002/advs.201800049 · Cited by 186
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Wiens, K. E., & Ernst, J. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005809 · Cited by 176
Pang, B., Dong, G., Pang, T., Sun, X., Liu, X., Nie, Y., & Chang, X. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1422686 · Cited by 175
Wang, K., Zhu, C., He, Y., Zhang, Z., Zhou, W., Nafees, M., Guo, Y., Wang, X., & Guo, Z. (2019) · Angewandte Chemie International Edition · doi:10.1002/anie.201900387 · Cited by 173
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Morton, H., Kshirsagar, S., Orlov, E., Bunquin, L. E., Sawant, N. A., Boleng, L., George, M., Basu, T., Ramasubramanian, B., Pradeepkiran, J. A., et al. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.07.013 · Cited by 172
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Szeto, H. H., & Schiller, P. W. (2011) · Pharmaceutical Research · doi:10.1007/s11095-011-0476-8 · Cited by 175
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Gruber, J. (2008) · Frontiers in bioscience · doi:10.2741/3174 · Cited by 171
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Vanova, K. H., Kraus, M., Neužil, J., & Rohlena, J. (2020) · Redox Report · doi:10.1080/13510002.2020.1752002 · Cited by 166
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Du, F., Min, Y., Zeng, F., Yu, C., & Wu, S. (2013) · Small · doi:10.1002/smll.201302036 · Cited by 162
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Self-citationNanoparticle formulations in the diagnosis and therapy of Alzheimer's disease
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Gal, K. L., Schmidt, E. E., & Sayin, V. I. (2021) · Antioxidants · doi:10.3390/antiox10091377 · Cited by 169
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Masanta, G., Heo, C. H., Lim, C. S., Bae, S. K., Cho, B. R., & Kim, H. M. (2012) · Chemical Communications · doi:10.1039/c2cc00034b · Cited by 158
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Higgins, G. C., Beart, P. M., Shin, Y. S., Chen, M. J., Cheung, N. S., & Nagley, P. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100321 · Cited by 160
Liu, J., Jin, C., Yuan, B., Liu, X., Chen, Y., Ji, L., & Chao, H. (2017) · Chemical Communications · doi:10.1039/c6cc10015e · Cited by 158
Sandoval-Acuña, C., Torrealba, N., Tomková, V., Jadhav, S. B., Blažková, K., Merta, L., Lettlová, S., Adamcova, M. K., Rösel, D., Brábek, J., et al. (2021) · Cancer Research · doi:10.1158/0008-5472.can-20-1628 · Cited by 158
V. Skulachev, M., N. Antonenko, Y., N. Anisimov, V., V. Chernyak, B., A. Cherepanov, D., A. Chistyakov, V., V. Egorov, M., G. Kolosova, N., A. Korshunova, G., G. Lyamzaev, K., et al. (2011) · Current Drug Targets · doi:10.2174/138945011795528859 · Cited by 156
Swarnakar, N. K., Jain, A., Singh, R. P., Godugu, C., Das, M., & Jain, S. (2011) · Biomaterials · doi:10.1016/j.biomaterials.2011.05.079 · Cited by 155
Kumar, A., & Singh, A. (2015) · Frontiers in Pharmacology · doi:10.3389/fphar.2015.00206 · Cited by 157
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Cha, M.-Y., Kim, D. K., & Mook‐Jung, I. (2015) · Experimental & Molecular Medicine · doi:10.1038/emm.2014.122 · Cited by 157
Detection and manipulation of mitochondrial reactive oxygen species in mammalian cells
Forkink, M., Smeitink, J. A. M., Brock, R. E., Willems, P. H. G. M., & Koopman, W. J. H. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.01.022 · Cited by 154
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Metadata
- Authors
- Murphy, M. P., & Smith, R. A. J.
- Affiliations
- MRC Mitochondrial Biology Unit (GB)
- University of Otago (NZ)
- ORCID
- Murphy, Michael P.
- Venue
- Annual Review of Pharmacology and Toxicology
- Publisher
- Annual Reviews
- Published
- 2007-02-01
- Volume
- 47
- Issue
- 1
- Pages
- 629-656
- ISSN
- 0362-1642 (ISSN-L)
- 1545-4304
- OpenAlex
- W2140014506
- Cited by
- 1,173
- References
- 130
- Citations by year
- 2026: 64 · 2025: 62 · 2024: 72 · 2023: 42 · 2022: 65 · 2021: 67 · 2020: 61 · 2019: 57 · 2018: 61 · 2017: 62 · 2016: 67 · 2015: 67 · 2014: 62 · 2013: 59 · 2012: 68
- FWCI
- 2.97
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The Annual Review of Pharmacology and Toxicology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Coenzyme Q10 studies and effects
- Life Sciences › Neuroscience › Neurology › Neuroprotection in Cerebral Ischemia
- Keywords
- mitochondria-targeted antioxidants, triphenylphosphonium cation, lipophilic cations, mitochondrial oxidative damage, ubiquinol, alpha-tocopherol, mitochondrial membrane potential, blood-brain barrier, oral drug delivery, degenerative diseases, mitochondrial protection
- MeSH terms
- Antioxidants, Cations, Drug Carriers, Humans, Membrane Potentials, Mitochondria, Tissue Distribution, Drug Delivery Systems, Reactive Oxygen Species, Mitochondrial Diseases
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