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Mitochondrial pharmacology
Open accessAbstract
Mitochondria are being recognized as key factors in many unexpected areas of biomedical science. In addition to their well-known roles in oxidative phosphorylation and metabolism, it is now clear that mitochondria are also central to cell death, neoplasia, cell differentiation, the innate immune system, oxygen and hypoxia sensing, and calcium metabolism. Disruption to these processes contributes to a range of human pathologies, making mitochondria a potentially important, but currently seemingly neglected, therapeutic target. Mitochondrial dysfunction is often associated with oxidative damage, calcium dyshomeostasis, defective ATP synthesis, or induction of the permeability transition pore. Consequently, therapies designed to prevent these types of damage are beneficial and can be used to treat many diverse and apparently unrelated indications. Here we outline the biological properties that make mitochondria important determinants of health and disease, and describe the pharmacological strategies being developed to address mitochondrial dysfunction.
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1 retracted
Wenz, T., Diaz, F., Spiegelman, B. M., & Moraes, C. T. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.07.006 · Cited by 297
RetractedHow mitochondria produce reactive oxygen species
Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207
Self-citationThe Whole Structure of the 13-Subunit Oxidized Cytochrome c Oxidase at 2.8 Å
Tsukihara, T., Aoyama, H., Yamashita, E., Tomizaki, T., Yamaguchi, H., Shinzawa-Itoh, K., Nakashima, R., Yaono, R., & Yoshikawa, S. (1996) · Science · doi:10.1126/science.272.5265.1136 · Cited by 2,100
Goto, Y.-I., Nonaka, I., & Horai, S. (1990) · Nature · doi:10.1038/348651a0 · Cited by 2,070
Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes
Milne, J. C., Lambert, P. D., Schenk, S., Carney, D. P., Smith, J. J., Gagne, D. J., Jin, L., Boss, O., Perni, R. B., Vu, C. B., et al. (2007) · Nature · doi:10.1038/nature06261 · Cited by 1,707
Targeting mitochondria for cancer therapy
Fulda, S., Galluzzi, L., & Kroemer, G. (2010) · Nature Reviews Drug Discovery · doi:10.1038/nrd3137 · Cited by 1,629
Selective degradation of mitochondria by mitophagy
Kim, I., Rodriguez-Enriquez, S., & Lemasters, J. J. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.03.034 · Cited by 1,558
Resveratrol Ameliorates Aging-Related Metabolic Phenotypes by Inhibiting cAMP Phosphodiesterases
Park, S.-J., Ahmad, F., Philp, A., Baar, K., Williams, T., Luo, H., Ke, H., Rehmann, H., Taussig, R., Brown, A. L., et al. (2012) · Cell · doi:10.1016/j.cell.2012.01.017 · Cited by 1,349
Effect of Cyclosporine on Reperfusion Injury in Acute Myocardial Infarction
Piot, C., Croisille, P., Staat, P., Thibault, H., Rioufol, G., Mewton, N., Elbelghiti, R., Cung, T. T., Bonnefoy, E., Angoulvant, D., et al. (2008) · New England Journal of Medicine · doi:10.1056/nejmoa071142 · Cited by 1,339
Complete Structure of the 11-Subunit Bovine Mitochondrial Cytochrome bc 1 Complex
Iwata, S., Lee, J. W., Okada, K., Lee, J. K., Iwata, M., Rasmussen, B., Link, T. A., Ramaswamy, S., & Jap, B. K. (1998) · Science · doi:10.1126/science.281.5373.64 · Cited by 1,253
Mitochondria and the Autophagy–Inflammation–Cell Death Axis in Organismal Aging
Green, D. R., Galluzzi, L., & Kroemer, G. (2011) · Science · doi:10.1126/science.1201940 · Cited by 1,245
Regulation of pgc-1α, a nodal regulator of mitochondrial biogenesis
Fernandez-Marcos, P. J., & Auwerx, J. (2011) · The American Journal of Clinical Nutrition · doi:10.3945/ajcn.110.001917 · Cited by 1,237
Cassidy-Stone, A., Chipuk, J. E., Ingerman, E., Song, C., Yoo, C., Kuwana, T., Kurth, M. J., Shaw, J. T., Hinshaw, J. E., Green, D. R., et al. (2008) · Developmental Cell · doi:10.1016/j.devcel.2007.11.019 · Cited by 1,200
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-citationStructure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside
Pebay-Peyroula, E., Dahout-Gonzalez, C., Kahn, R., Trézéguet, V., Lauquin, G. J.-M., & Brandolin, G. (2003) · Nature · doi:10.1038/nature02056 · Cited by 998
Sundaresan, N. R., Gupta, M., Kim, G., Rajamohan, S. B., Isbatan, A., & Gupta, M. P. (2009) · Journal of Clinical Investigation · doi:10.1172/jci39162 · Cited by 995
Inhibiting Mitochondrial Fission Protects the Heart Against Ischemia/Reperfusion Injury
Ong, S.-B., Subrayan, S., Lim, S. Y., Yellon, D. M., Davidson, S. M., & Hausenloy, D. J. (2010) · Circulation · doi:10.1161/circulationaha.109.906610 · Cited by 986
Transcriptional control of mitochondrial biogenesis: the central role of PGC-1
Ventura-Clapier, R., Garnier, A., & Veksler, V. (2008) · Cardiovascular Research · doi:10.1093/cvr/cvn098 · Cited by 932
Crystal Structure of Mitochondrial Respiratory Membrane Protein Complex II
Sun, F., Huo, X., Zhai, Y., Wang, A., Xu, J., Su, D., Bartlam, M., & Rao, Z. (2005) · Cell · doi:10.1016/j.cell.2005.05.025 · Cited by 881
Unraveling the biological roles of reactive oxygen species
Murphy, M. P., Holmgren, A., Larsson, N.-G., Halliwell, B., Chang, C. J., Kalyanaraman, B., Rhee, S. G., Thornalley, P. J., Partridge, L., Gems, D., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.03.010 · Cited by 836
Self-citationTherapeutic Targeting of Mitochondrial Superoxide in Hypertension
Dikalova, A. E., Bikineyeva, A. T., Budzyn, K., Nazarewicz, R. R., McCann, L., Lewis, W., Harrison, D. G., & Dikalov, S. I. (2010) · Circulation Research · doi:10.1161/circresaha.109.214601 · Cited by 737
Mitochondrial Energetics and Therapeutics
Wallace, D. C., Fan, W., & Procaccio, V. (2010) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev.pathol.4.110807.092314 · Cited by 730
The genetics and pathology of oxidative phosphorylation
Smeitink, J., van den Heuvel, L., & DiMauro, S. (2001) · Nature Reviews Genetics · doi:10.1038/35072063 · Cited by 724
Mitochondrial Complex III ROS Regulate Adipocyte Differentiation
Tormos, K. V., Anso, E., Hamanaka, R. B., Eisenbart, J., Joseph, J., Kalyanaraman, B., & Chandel, N. S. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.08.007 · Cited by 663
The architecture of respiratory complex I
Efremov, R. G., Baradaran, R., & Sazanov, L. A. (2010) · Nature · doi:10.1038/nature09066 · Cited by 617
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-citationThe Mitochondrial Proteome and Human Disease
Calvo, S. E., & Mootha, V. K. (2010) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev-genom-082509-141720 · Cited by 590
Mitochondrial permeability transition in Ca2+-dependent apoptosis and necrosis
Rasola, A., & Bernardi, P. (2011) · Cell Calcium · doi:10.1016/j.ceca.2011.04.007 · Cited by 563
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 547
Self-citationMitochondria—A Nexus for Aging, Calorie Restriction, and Sirtuins?
Guarente, L. (2008) · Cell · doi:10.1016/j.cell.2008.01.007 · Cited by 513
Mitochondrial dysfunction and apoptosis in myopathic mice with collagen VI deficiency
Irwin, W. A., Bergamin, N., Sabatelli, P., Reggiani, C., Megighian, A., Merlini, L., Braghetta, P., Columbaro, M., Volpin, D., Bressan, G. M., et al. (2003) · Nature Genetics · doi:10.1038/ng1270 · Cited by 509
McManus, M. J., Murphy, M. P., & Franklin, J. L. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.0552-11.2011 · Cited by 432
Self-citationAn Attempt to Prevent Senescence: A Mitochondrial Approach
Skulachev, V. P., Anisimov, V. N., Antonenko, Y. N., Bakeeva, L. E., Chernyak, B. V., Erichev, V. P., Filenko, O. F., Kalinina, N. I., Kapelko, V. I., Kolosova, N. G., et al. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.12.008 · Cited by 430
Mitochondria-Targeted Small Molecule Therapeutics and Probes
Smith, R. A. J., Hartley, R. C., & Murphy, M. P. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.3969 · Cited by 399
Self-citationGane, 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
Self-citationTargeting Mitochondrial Dysfunction: Role for PINK1 and Parkin in Mitochondrial Quality Control
Narendra, D. P., & Youle, R. J. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3799 · Cited by 367
Effect of idebenone on cardiomyopathy in Friedreich's ataxia: a preliminary study
Rustin, P., von Kleist-Retzow, J.-C., Chantrel-Groussard, K., Sidi, D., Munnich, A., & Rötig, A. (1999) · The Lancet · doi:10.1016/s0140-6736(99)01341-0 · Cited by 349
Targeting Mitochondria with Organelle‐Specific Compounds: Strategies and Applications
Yousif, L. F., Stewart, K. M., & Kelley, S. O. (2009) · ChemBioChem · doi:10.1002/cbic.200900185 · Cited by 330
Cochemé, H. M., Quin, C., McQuaker, S. J., Cabreiro, F., Logan, A., Prime, T. A., Abakumova, I., Patel, J. V., Fearnley, I. M., James, A. M., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.02.003 · Cited by 313
Self-citationBjelakovic, G., Nikolova, D., Gluud, L. L., Simonetti, R. G., & Gluud, C. (2008) · Cochrane Database of Systematic Reviews · doi:10.1002/14651858.cd007176 · Cited by 302
In Vivo Correction of COX Deficiency by Activation of the AMPK/PGC-1α Axis
Viscomi, C., Bottani, E., Civiletto, G., Cerutti, R., Moggio, M., Fagiolari, G., Schon, E. A., Lamperti, C., & Zeviani, M. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.04.011 · Cited by 292
Eleff, S., Kennaway, N. G., Buist, N. R., Darley-Usmar, V. M., Capaldi, R. A., Bank, W. J., & Chance, B. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.11.3529 · Cited by 273
Mitochondrial uncoupling as a target for drug development for the treatment of obesity.
Harper, J. A., Dickinson, K., & Brand, M. D. (2001) · Obesity Reviews · doi:10.1046/j.1467-789x.2001.00043.x · Cited by 250
Mitochondria in innate immunity
Arnoult, D., Soares, F., Tattoli, I., & Girardin, S. E. (2011) · EMBO reports · doi:10.1038/embor.2011.157 · Cited by 249
Halestrap, A. (2005) · Nature · doi:10.1038/434578a · Cited by 239
CONTROL OF ELECTRON FLUX THROUGH THE RESPIRATORY CHAIN IN MITOCHONDRIA AND CELLS
BRAND, M. D., & MURPHY, M. P. (1987) · Biological Reviews · doi:10.1111/j.1469-185x.1987.tb01265.x · Cited by 239
Self-citationPrime, T. A., Blaikie, F. H., Evans, C., Nadtochiy, S. M., James, A. M., Dahm, C. C., Vitturi, D. A., Patel, R. P., Hiley, C. R., Abakumova, I., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903250106 · Cited by 222
Self-citationRodriguez-Cuenca, S., Cochemé, H. M., Logan, A., Abakumova, I., Prime, T. A., Rose, C., Vidal-Puig, A., Smith, A. C., Rubinsztein, D. C., Fearnley, I. M., et al. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.10.039 · Cited by 218
Self-citationMerlini, L., Angelin, A., Tiepolo, T., Braghetta, P., Sabatelli, P., Zamparelli, A., Ferlini, A., Maraldi, N. M., Bonaldo, P., & Bernardi, P. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800962105 · Cited by 208
Dong, L.-F., Jameson, V. J. A., Tilly, D., Cerny, J., Mahdavian, E., Marín-Hernández, A., Hernández-Esquivel, L., Rodríguez-Enríquez, S., Stursa, J., Witting, P. K., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.186643 · Cited by 200
Self-citationMitochondrial respiratory chain disorders II: neurodegenerative disorders and nuclear gene defects
Leonard, J., & Schapira, A. (2000) · The Lancet · doi:10.1016/s0140-6736(99)05226-5 · Cited by 198
Penetrating cation/fatty acid anion pair as a mitochondria-targeted protonophore
Severin, F. F., Severina, I. I., Antonenko, Y. N., Rokitskaya, T. I., Cherepanov, D. A., Mokhova, E. N., Vyssokikh, M. Y., Pustovidko, A. V., Markova, O. V., Yaguzhinsky, L. S., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910216107 · Cited by 196
Neuroprotection by a mitochondria-targeted drug in a Parkinson's disease model
Ghosh, A., Chandran, K., Kalivendi, S. V., Joseph, J., Antholine, W. E., Hillard, C. J., Kanthasamy, A., Kanthasamy, A., & Kalyanaraman, B. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.08.028 · Cited by 190
Dhanasekaran, A., Kotamraju, S., Karunakaran, C., Kalivendi, S. V., Thomas, S., Joseph, J., & Kalyanaraman, B. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.04.016 · Cited by 190
Mercer, J. R., Yu, E., Figg, N., Cheng, K.-K., Prime, T. A., Griffin, J. L., Masoodi, M., Vidal-Puig, A., Murphy, M. P., & Bennett, M. R. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.11.026 · Cited by 188
Self-citationOn the structure of the stator of the mitochondrial ATP synthase
Dickson, V. K., Silvester, J. A., Fearnley, I. M., Leslie, A. G. W., & Walker, J. E. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601177 · Cited by 187
NQO1-Dependent Redox Cycling of Idebenone: Effects on Cellular Redox Potential and Energy Levels
Haefeli, R. H., Erb, M., Gemperli, A. C., Robay, D., Courdier Fruh, I., Anklin, C., Dallmann, R., & Gueven, N. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017963 · Cited by 187
Fernandez-Ayala, D. J. M., Sanz, A., Vartiainen, S., Kemppainen, K. K., Babusiak, M., Mustalahti, E., Costa, R., Tuomela, T., Zeviani, M., Chung, J., et al. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.03.004 · Cited by 181
Novel Therapies Targeting Inner Mitochondrial Membrane—From Discovery to Clinical Development
Szeto, H. H., & Schiller, P. W. (2011) · Pharmaceutical Research · doi:10.1007/s11095-011-0476-8 · Cited by 170
Roles of mitochondria in human disease
Duchen, M. R., & Szabadkai, G. (2010) · Essays in Biochemistry · doi:10.1042/bse0470115 · Cited by 168
Saada, A., Vogel, R. O., Hoefs, S. J., van den Brand, M. A., Wessels, H. J., Willems, P. H., Venselaar, H., Shaag, A., Barghuti, F., Reish, O., et al. (2009) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2009.04.020 · Cited by 168
A therapeutic role for sirtuins in diseases of aging?
WESTPHAL, C., DIPP, M., & GUARENTE, L. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.09.008 · Cited by 168
Mitochondria‐Penetrating Peptides: Sequence Effects and Model Cargo Transport
Yousif, L. F., Stewart, K. M., Horton, K. L., & Kelley, S. O. (2009) · ChemBioChem · doi:10.1002/cbic.200900017 · Cited by 167
Sanz, A., Soikkeli, M., Portero‐Otín, M., Wilson, A. M., Kemppainen, E., Mcilroy, G. D., Ellilä, S., Kemppainen, K. K., Tuomela, T., Lakanmaa, M., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911539107 · Cited by 149
Protective Role of Methylene Blue in Alzheimer's Disease via Mitochondria and Cytochrome c Oxidase
Atamna, H., & Kumar, R. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100414 · Cited by 142
Hansson, M. J., Mattiasson, G., Månsson, R., Karlsson, J., Keep, M. F., Waldmeier, P. C., Rüegg, U. T., Dumont, J., Besseghir, K., & Elmér, E. (2004) · Journal of Bioenergetics and Biomembranes · doi:10.1023/b:jobb.0000041776.31885.45 · Cited by 142
Mitochondrial uncouplers with an extraordinary dynamic range
Lou, P.-H., Hansen, B. S., Olsen, P. H., Tullin, S., Murphy, M. P., & Brand, M. D. (2007) · Biochemical Journal · doi:10.1042/bj20070606 · Cited by 141
Self-citationAssembly factors of human mitochondrial complex I and their defects in disease
McKenzie, M., & Ryan, M. T. (2010) · IUBMB Life · doi:10.1002/iub.335 · Cited by 139
Dichloroacetate as metabolic therapy for myocardial ischemia and failure
Bersin, R. M., & Stacpoole, P. W. (1997) · American Heart Journal · doi:10.1016/s0002-8703(97)80007-5 · Cited by 138
Chouchani, E. T., Hurd, T. R., Nadtochiy, S. M., Brookes, P. S., Fearnley, I. M., Lilley, K. S., Smith, R. A. J., & Murphy, M. P. (2010) · Biochemical Journal · doi:10.1042/bj20100633 · Cited by 137
Self-citationSynthesis and Characterization of a Triphenylphosphonium-conjugated Peroxidase Mimetic
Filipovska, A., Kelso, G. F., Brown, S. E., Beer, S. M., Smith, R. A. J., & Murphy, M. P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501148200 · Cited by 130
Self-citationPreclinical evaluation of novel triphenylphosphonium salts with broad-spectrum activity
Millard, M., Pathania, D., Shabaik, Y., Taheri, L., Deng, J., & Neamati, N. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013131 · Cited by 129
Autosomal recessive myosclerosis myopathy is a collagen VI disorder
Merlini, L., Martoni, E., Grumati, P., Sabatelli, P., Squarzoni, S., Urciuolo, A., Ferlini, A., Gualandi, F., & Bonaldo, P. (2008) · Neurology · doi:10.1212/01.wnl.0000327611.01687.5e · Cited by 125
Mitochondria-targeted ubiquinone (MitoQ) decreases ethanol-dependent micro and macro hepatosteatosis
Chacko, B. K., Srivastava, A., Johnson, M. S., Benavides, G. A., Chang, M. J., Ye, Y., Jhala, N., Murphy, M. P., Kalyanaraman, B., & Darley-Usmar, V. M. (2011) · Hepatology · doi:10.1002/hep.24377 · Cited by 122
Self-citationPorteous, C. M., Logan, A., Evans, C., Ledgerwood, E. C., Menon, D. K., Aigbirhio, F., Smith, R. A. J., & Murphy, M. P. (2010) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2010.06.001 · Cited by 121
Self-citationChalmers, S., Caldwell, S. T., Quin, C., Prime, T. A., James, A. M., Cairns, A. G., Murphy, M. P., McCarron, J. G., & Hartley, R. C. (2011) · Journal of the American Chemical Society · doi:10.1021/ja2077922 · Cited by 118
Self-citationThe inheritance of pathogenic mitochondrial DNA mutations
Cree, L. M., Samuels, D. C., & Chinnery, P. F. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.03.002 · Cited by 96
Mitchell, T., Rotaru, D., Saba, H., Smith, R. A. J., Murphy, M. P., & MacMillan-Crow, L. A. (2011) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.110.176743 · Cited by 84
Self-citationProgress and prospects: gene therapy for mitochondrial DNA disease
Kyriakouli, D. S., Boesch, P., Taylor, R. W., & Lightowlers, R. N. (2008) · Gene Therapy · doi:10.1038/gt.2008.91 · Cited by 76
Malouitre, S. D. M., Dube, H., Selwood, D. L., & Crompton, M. (2009) · Biochemical Journal · doi:10.1042/bj20090332 · Cited by 73
Lei, W., Xie, J., Hou, Y., Jiang, G., Zhang, H., Wang, P., Wang, X., & Zhang, B. (2009) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/j.jphotobiol.2009.12.003 · Cited by 70
What makes the mitochondria a killer? Can we condition them to be less destructive?
Murphy, E., & Steenbergen, C. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.09.003 · Cited by 67
Pereira, M. P., & Kelley, S. O. (2011) · Journal of the American Chemical Society · doi:10.1021/ja110246u · Cited by 63
Therapy of Collagen VI-Related Myopathies (Bethlem and Ullrich)
Merlini, L., & Bernardi, P. (2008) · Neurotherapeutics · doi:10.1016/j.nurt.2008.08.004 · Cited by 58
64Cu-Labeled Phosphonium Cations as PET Radiotracers for Tumor Imaging
Zhou, Y., & Liu, S. (2011) · Bioconjugate Chemistry · doi:10.1021/bc200106p · Cited by 56
Ripcke, J., Zarse, K., Ristow, M., & Birringer, M. (2009) · ChemBioChem · doi:10.1002/cbic.200900159 · Cited by 48
31P-MRS of skeletal muscle is not a sensitive diagnostic test for mitochondrial myopathy
Jeppesen, T. D., Quistorff, B., Wibrand, F., & Vissing, J. (2007) · Journal of Neurology · doi:10.1007/s00415-006-0229-5 · Cited by 44
Mitochondrial myopathies: developments in treatment
Hassani, A., Horváth, R., & Chinnery, P. F. (2010) · Current Opinion in Neurology · doi:10.1097/wco.0b013e32833d1096 · Cited by 44
Lee, H.-Y., Kaneki, M., Andreas, J., Tompkins, R. G., & Martyn, J. A. J. (2011) · Shock · doi:10.1097/shk.0b013e3182366872 · Cited by 41
Molecules and roles of mitochondrial calcium signaling
Mammucari, C., Patrón, M., Granatiero, V., & Rizzuto, R. (2011) · BioFactors · doi:10.1002/biof.160 · Cited by 38
Nicolau, S. M., de Diego, A. M. G., Cortés, L., Egea, J., Gonzalez, J., Mosquera, M., López, M. G., Hernández-Guijo, J. M., & de Diego, A. M. G. (2009) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.109.154765 · Cited by 35
Mitochondrial disorders of the nuclear genome.
Angelini, C. I., Bello, L., Spinazzi, M., & Ferrati, C. (2009) · PubMed · Cited by 34
Efficacy of Pt(Rh-123)2 as a radiosensitizer with fractionated x rays
Teicher, B. A., Holden, S. A., & Cathcart, K. N. S. (1987) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/0360-3016(87)90197-0 · Cited by 22
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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
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Kluge, M. A., Fetterman, J. L., & Vita, J. A. (2013) · Circulation Research · doi:10.1161/circresaha.111.300233 · Cited by 508
Birk, A. V., Liu, S., Soong, Y., Mills, W., Singh, P., Warren, J. D., Seshan, S. V., Pardee, J. D., & Szeto, H. H. (2013) · Journal of the American Society of Nephrology · doi:10.1681/asn.2012121216 · Cited by 479
Coupling Krebs cycle metabolites to signalling in immunity and cancer
Ryan, D. G., Murphy, M. P., Frezza, C., Prag, H. A., Chouchani, E. T., O’Neill, L. A., & Mills, E. L. (2018) · Nature Metabolism · doi:10.1038/s42255-018-0014-7 · Cited by 398
Self-citationMünzel, T., Gori, T., Keaney, J. F., Maack, C., & Daiber, A. (2015) · European Heart Journal · doi:10.1093/eurheartj/ehv305 · Cited by 394
Metadata
- Authors
- Smith, R. A. J., Hartley, R. C., Cochemé, H. M., & Murphy, M. P.
- Venue
- Trends in Pharmacological Sciences
- Publisher
- Elsevier BV
- Published
- 2012-06
- Volume
- 33
- Issue
- 6
- Pages
- 341-352
- ISSN
- 0165-6147 (ISSN-L)
- OpenAlex
- W4210273716
- Cited by
- 499
- References
- 93
- FWCI
- 2.29
- Type
- journal article
- Language
- en
- Open access
- hybrid
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
