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Calcium, ATP, and ROS: a mitochondrial love-hate triangle
Abstract
The mitochondrion is at the core of cellular energy metabolism, being the site of most ATP generation. Calcium is a key regulator of mitochondrial function and acts at several levels within the organelle to stimulate ATP synthesis. However, the dysregulation of mitochondrial Ca(2+) homeostasis is now recognized to play a key role in several pathologies. For example, mitochondrial matrix Ca(2+) overload can lead to enhanced generation of reactive oxygen species, triggering of the permeability transition pore, and cytochrome c release, leading to apoptosis. Despite progress regarding the independent roles of both Ca(2+) and mitochondrial dysfunction in disease, the molecular mechanisms by which Ca(2+) can elicit mitochondrial dysfunction remain elusive. This review highlights the delicate balance between the positive and negative effects of Ca(2+) and the signaling events that perturb this balance. Overall, a "two-hit" hypothesis is developed, in which Ca(2+) plus another pathological stimulus can bring about mitochondrial dysfunction.
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“Peroxides produced by mitochondria can create nonenzymatic shunts in the TCA cycle (56, 121).”
From Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function (2009) · cites this paper as [56]
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“In turn, an increased Ca 2ϩ load in the mitochondrial matrix has been linked to increased ROS production and increased permeability transition pore opening, leading to apoptosis (40,45).”
From Simvastatin Effects on Skeletal Muscle (2013) · cites this paper as [45]
Citations
Cites
Free radicals in biology and medicine
Gutteridge, J. M. C. (1991) · General Pharmacology The Vascular System · doi:10.1016/0306-3623(91)90478-o · Cited by 17,178
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
Induction of Apoptotic Program in Cell-Free Extracts: Requirement for dATP and Cytochrome c
Liu, X., Kim, C. N., Yang, J., Jemmerson, R., & Wang, X. (1996) · Cell · doi:10.1016/s0092-8674(00)80085-9 · Cited by 5,167
Mitochondrial formation of reactive oxygen species
Turrens, J. F. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.049478 · Cited by 5,084
Nitric oxide synthases: structure, function and inhibition
ALDERTON, W. K., COOPER, C. E., & KNOWLES, R. G. (2001) · Biochemical Journal · doi:10.1042/bj3570593 · Cited by 4,110
Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., & Chan, D. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211046 · Cited by 2,601
The mitochondrial permeability transition pore and its role in cell death
CROMPTON, M. (1999) · Biochemical Journal · doi:10.1042/bj3410233 · Cited by 2,432
Shimizu, S., Narita, M., Tsujimoto, Y., & Tsujimoto, Y. (1999) · Nature · doi:10.1038/20959 · Cited by 2,178
Nitric oxide mediates glutamate neurotoxicity in primary cortical cultures.
Dawson, V. L., Dawson, T. M., London, E. D., Bredt, D. S., & Snyder, S. H. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.14.6368 · Cited by 2,174
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A model of the mitochondrial basis of bipolar disorder
Morris, G., Walder, K., McGee, S. L., Dean, O. M., Tye, S. J., Maes, M., & Berk, M. (2017) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2017.01.014 · Cited by 162
Mechanisms of modafinil: A review of current research
Gerrard, P., & Malcolm, R. (2007) · Neuropsychiatric Disease and Treatment · doi:10.2147/ndt.a911 · Cited by 160
Egnatchik, R. A., Leamy, A. K., Jacobson, D. A., Shiota, M., & Young, J. D. (2014) · Molecular Metabolism · doi:10.1016/j.molmet.2014.05.004 · Cited by 161
Uğuz, A. C., Nazıroğlu, M., Espino, J., Bejarano, I., González, D., Rodríguez, A. B., & Pariente, J. A. (2009) · The Journal of Membrane Biology · doi:10.1007/s00232-009-9212-2 · Cited by 161
Medication‐induced mitochondrial damage and disease
Neustadt, J. O., & Pieczenik, S. R. (2008) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200700075 · Cited by 158
Mitophagy in Cerebral Ischemia and Ischemia/Reperfusion Injury
Shen, L., Gan, Q., Yang, Y., Reis, C., Zhang, Z., Xu, S., Zhang, T., & Sun, C. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.687246 · Cited by 162
Human-Specific ARHGAP11B Acts in Mitochondria to Expand Neocortical Progenitors by Glutaminolysis
Namba, T., Dóczi, J., Pinson, A., Xing, L., Kalebic, N., Wilsch‐Bräuninger, M., Long, K. R., Vaid, S., Lauer, J. L., Bogdanova, A. I., et al. (2019) · Neuron · doi:10.1016/j.neuron.2019.11.027 · Cited by 161
Žaja, I., Bai, X., Liu, Y., Kikuchi, C., Došenović, S., Yan, Y., Canfield, S. G., & Bosnjak, Z. J. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.09.144 · Cited by 163
Redox Control of Calcium Channels: From Mechanisms to Therapeutic Opportunities
Hool, L. C., & Corry, B. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.1446 · Cited by 156
Sodium dichloroacetate selectively targets cells with defects in the mitochondrial ETC
Stockwin, L. H., Yu, S. X., Borgel, S. D., Hancock, C. N., Wolfe, T. L., Phillips, L. R., Hollingshead, M. G., & Newton, D. L. (2010) · International Journal of Cancer · doi:10.1002/ijc.25499 · Cited by 160
Oxygen sensing and signal transduction in hypoxic pulmonary vasoconstriction
Sommer, N., Strielkov, I. V., Pak, O., & Weißmann, N. (2015) · European Respiratory Journal · doi:10.1183/13993003.00945-2015 · Cited by 157
Xiong, S., George, S., Yu, H., Damoiseaux, R. D., France, B., Ng, K. W., & Loo, S. C. J. (2012) · Archives of Toxicology · doi:10.1007/s00204-012-0938-8 · Cited by 153
CaMKII oxidative activation and the pathogenesis of cardiac disease
Luczak, E. D., & Anderson, M. E. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.02.004 · Cited by 157
Mitochondria in vascular disease
Yu, E., Mercer, J. R., & Bennett, M. R. (2012) · Cardiovascular Research · doi:10.1093/cvr/cvs111 · Cited by 153
Bioenergetics, mitochondria, and cardiac myocyte differentiation
Porter, G. A., Hom, J. R., Hoffman, D. L., Quintanilla, R. A., Bentley, K. L. D. M., & Sheu, S.-S. (2011) · Progress in Pediatric Cardiology · doi:10.1016/j.ppedcard.2011.02.002 · Cited by 154
Self-citationLederer, C. W., Torrisi, A. A. M., Pantelidou, M., Santama, N., & Cavallaro, S. (2007) · BMC Genomics · doi:10.1186/1471-2164-8-26 · Cited by 152
Mitochondria as ATP consumers in cellular pathology
Chinopoulos, C., & Ádám‐Vizi, V. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.08.008 · Cited by 147
Dagvadorj, J., Shimada, K., Chen, S., Jones, H. D., Tumurkhuu, G., Zhang, W., Wawrowsky, K., Crother, T. R., & Arditi, M. (2015) · Immunity · doi:10.1016/j.immuni.2015.03.007 · Cited by 146
Mitochondrial Approaches to Protect Against Cardiac Ischemia and Reperfusion Injury
Camara, A. K. S., Bienengraeber, M., & Stowe, D. F. (2011) · Frontiers in Physiology · doi:10.3389/fphys.2011.00013 · Cited by 155
Jiang, Z., Hu, Z., Zeng, L., Lu, W., Zhang, H., Li, T., & Xiao, H. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.01.011 · Cited by 149
Mitochondria Regulate Neutrophil Activation by Generating ATP for Autocrine Purinergic Signaling
Bao, Y., Ledderose, C., Seier, T., Graf, A. F., Brix, B., Chong, E., & JUNGER, W. G. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.572495 · Cited by 147
Huntington’s Disease and Mitochondria
Farshbaf, M. J., & Ghaedi, K. (2017) · Neurotoxicity Research · doi:10.1007/s12640-017-9766-1 · Cited by 153
Duan, Y., Gross, R. A., & Sheu, S. (2007) · The Journal of Physiology · doi:10.1113/jphysiol.2007.145409 · Cited by 148
Self-citationMitochondrial Dysfunction Contributes to the Pathogenesis of Alzheimer’s Disease
Cabezas-Opazo, F., Vergara-Pulgar, K., Maria Jose Perez, J., Jara, C., Osorio‐Fuentealba, C., & Quintanilla, R. A. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/509654 · Cited by 155
Redox signaling in acute pancreatitis
Pérez, S., Pereda, J., Sabater-Orti, L., & Sastre, J. (2015) · Redox Biology · doi:10.1016/j.redox.2015.01.014 · Cited by 150
Mitochondrial criticality: A new concept at the turning point of life or death
Aon, M. A., Cortassa, S. C., Akar, F. G., & O'Rourke, B. P. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2005.06.008 · Cited by 146
Rotenone exerts developmental neurotoxicity in a human brain spheroid model
Pamies, D., Block, K., Lau, P., Gribaldo, L., Pardo, C. A., Barreras, P., Smirnova, L., Wiersma, D., Zhao, L., Harris, G., et al. (2018) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2018.02.003 · Cited by 155
Cardioprotection by metabolic shut-down and gradual wake-up
Burwell, L. S., Nadtochiy, S. M., & Brookes, P. S. (2009) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2009.02.026 · Cited by 146
Self-citationMohanta, T. K., Bashir, T., Hashem, A., Allah, E. F. A., Khan, A. L., & Al-Harrasi, A. S. (2018) · Journal of Plant Growth Regulation · doi:10.1007/s00344-018-9833-8 · Cited by 149
Regulation of aged skeletal muscle regeneration by circulating extracellular vesicles
Sahu, A., Clemens, Z. J., Shinde, S. N., Sivakumar, S., Pius, A., Bhatia, A., Picciolini, S., Carlomagno, C., Gualerzi, A., Bedoni, M., et al. (2021) · Nature Aging · doi:10.1038/s43587-021-00143-2 · Cited by 145
Bánsághi, S., Golenár, T., Madesh, M., Csordás, G., RamachandraRao, S., Sharma, K., Yule, D. I., Joseph, S. K., & Hajnóczky, G. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.504159 · Cited by 149
Adhesion-mediated mechanosignaling forces mitohormesis
Tharp, K. M., Higuchi‐Sanabria, R., Timblin, G. A., Ford, B., Garzón-Coral, C., Schneider, C. P., Muncie, J. M., Stashko, C., Daniele, J. R., Moore, A. S., et al. (2021) · Cell Metabolism · doi:10.1016/j.cmet.2021.04.017 · Cited by 147
Myocardial energetics in heart failure
Nickel, A. G., Löffler, J., & Maack, C. (2013) · Basic Research in Cardiology · doi:10.1007/s00395-013-0358-9 · Cited by 148
Nadtochiy, S. M., Burwell, L. S., & Brookes, P. S. (2007) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2007.01.010 · Cited by 142
Self-citationRybalka, E., Timpani, C. A., Cooke, M. B., Williams, A. D., & Hayes, A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0115763 · Cited by 143
Kirkman, D. L., Robinson, A. T., Rossman, M. J., Seals, D. R., & Edwards, D. G. (2021) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00917.2020 · Cited by 150
Jung, C., Martins, A. S., Ernst Niggli, A., & Shirokova, N. (2007) · Cardiovascular Research · doi:10.1093/cvr/cvm089 · Cited by 143
Garcı́a-Pérez, C., Hajnóczky, G., & Csordás, G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803385200 · Cited by 142
Hom, J., Gewandter, J. S., Michael, L., Sheu, S., & Yoon, Y. (2007) · Journal of Cellular Physiology · doi:10.1002/jcp.21051 · Cited by 142
Self-citationNew insights into the role of mitochondrial calcium homeostasis in cell migration
Paupe, V., & Prudent, J. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.05.039 · Cited by 146
Mitochondria as a target for neuroprotection: role of methylene blue and photobiomodulation
Yang, L., Youngblood, H. A., Wu, C., & Zhang, Q. (2020) · Translational Neurodegeneration · doi:10.1186/s40035-020-00197-z · Cited by 147
Sesquiterpene lactones: Adverse health effects and toxicity mechanisms
Amorim, M. H. R., da Costa, R. M. G., Lopes, C., & Bastos, M. M. S. M. (2013) · Critical Reviews in Toxicology · doi:10.3109/10408444.2013.813905 · Cited by 146
Piacenza, L., Irigoı́n, F., Álvarez, M. N., Peluffo, G., Taylor, M. C., Kelly, J. M., Wilkinson, S. R., & Radí, R. (2007) · Biochemical Journal · doi:10.1042/bj20061281 · Cited by 141
mTOR and differential activation of mitochondria orchestrate neutrophil chemotaxis
Bao, Y., Ledderose, C., Graf, A. F., Brix, B., Birsak, T., Lee, A., Zhang, J., & JUNGER, W. G. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201503066 · Cited by 141
Mitochondrial redox signaling enables repair of injured skeletal muscle cells
Horn, A. J., der Meulen, J. H. V., Defour, A., Hogarth, M. W., Sreetama, S. C., Reed, A., Scheffer, L., Chandel, N. S., & Jaiswal, J. K. (2017) · Science Signaling · doi:10.1126/scisignal.aaj1978 · Cited by 141
Zhao, S., Chen, F., Yin, Q., Wang, D., Han, W., & Zhang, Y. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.571810 · Cited by 145
Lin, K.-J., Lin, K.-L., Chen, S., Liou, C., Chuang, Y., Lin, H., & Lin, T. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20215312 · Cited by 141
Mutant Huntingtin Expression Induces Mitochondrial Calcium Handling Defects in Clonal Striatal Cells
Milakovic, T., Quintanilla, R. A., & Johnson, G. V. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603845200 · Cited by 142
DILISA, F., & BERNARDI, P. (2005) · Cardiovascular Research · doi:10.1016/j.cardiores.2005.02.009 · Cited by 139
Mitochondrial stress and the pathogenesis of diabetic neuropathy
Fernyhough, P., Chowdhury, S. R., & Schmidt, R. E. (2010) · Expert Review of Endocrinology & Metabolism · doi:10.1586/eem.09.55 · Cited by 142
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Viaud, M., Ivanov, S., Vujić, N., Duta-Mare, M., Aira, L. E., Barouillet, T., Garcia, E., Orange, F., Dugail, I., Hainault, I., et al. (2018) · Circulation Research · doi:10.1161/circresaha.117.312333 · Cited by 148
Li, Y., & Yao, H. (2016) · British Journal of Pharmacology · doi:10.1111/bph.13518 · Cited by 141
Bradykinin B1 and B2 receptors both have protective roles in renal ischemia/reperfusion injury
Kakoki, M., McGarrah, R. W., Kim, H.-S., & Smithies, O. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701617104 · Cited by 137
Petrosillo, G., Casanova, G., Matera, M., Ruggiero, F. M., & Paradies, G. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.10.036 · Cited by 137
Piccoli, C., Scrima, R., Quarato, G., D’Aprile, A., Ripoli, M. C., Lecce, L., Boffoli, D., Moradpour, D., & Capitanio, N. (2007) · Hepatology · doi:10.1002/hep.21679 · Cited by 134
A CaPful of mechanisms regulating the mitochondrial permeability transition
Lisa, F. D., & Bernardi, P. (2009) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2009.03.006 · Cited by 143
Health Effects of Trace Metals in Electronic Cigarette Aerosols—a Systematic Review
Gaur, S., & Agnihotri, R. (2018) · Biological Trace Element Research · doi:10.1007/s12011-018-1423-x · Cited by 150
Park, H., Yoon, N. G., Lee, J., Hu, S., Yoon, S., Kim, S. Y., Hong, J.-H., Nam, D., Chae, Y. C., Park, J. B., et al. (2020) · Experimental & Molecular Medicine · doi:10.1038/s12276-019-0360-x · Cited by 139
Gu, Z., Li, L., Wu, F., Zhao, P. Y., Yang, H. S., Liu, Y. S., Geng, Y., Zhao, M., & Su, L. (2015) · Scientific Reports · doi:10.1038/srep11497 · Cited by 136
Mitochondrial morphology regulates organellar Ca 2+ uptake and changes cellular Ca 2+ homeostasis
Kowaltowski, A. J., Menezes‐Filho, S. L., Assali, E. A., Gonçalves, I. G., Cabral‐Costa, J. V., Abreu, P., Miller, N., Nolasco, P., Laurindo, F. R. M., Bruni‐Cardoso, A., et al. (2019) · The FASEB Journal · doi:10.1096/fj.201901136r · Cited by 137
Anilkumar, U., Khacho, M., Cuillerier, A., Harris, R. A., Patten, D. A., Bilen, M., Iqbal, M. A., Guo, D. Y., Trudeau, L., Park, D. S., et al. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-2498-9 · Cited by 135
Mitochondrial dysfunction, oxidative stress, and major depressive disorder
Tobe, E. (2013) · Neuropsychiatric Disease and Treatment · doi:10.2147/ndt.s44282 · Cited by 156
Abnormal calcium homeostasis in peripheral neuropathies
Fernyhough, P., & Calcutt, N. A. (2009) · Cell Calcium · doi:10.1016/j.ceca.2009.11.008 · Cited by 134
A Large, Voltage-Dependent Channel, Isolated from Mitochondria by Water-Free Chloroform Extraction
Pavlov, E. V., Zakharian, E., Bladen, C., Diao, C. T. M., Grimbly, C., Reusch, R. N., & French, R. J. (2005) · Biophysical Journal · doi:10.1529/biophysj.104.057281 · Cited by 135
Cheng, A. J., Place, N., & Westerblad, H. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a029710 · Cited by 149
Kim, S., Joe, Y., Jeong, S. O., Zheng, M., Back, S. H., Park, S. W., Ryter, S. W., & Chung, H. (2013) · Innate Immunity · doi:10.1177/1753425913508593 · Cited by 132
Control of mitochondrial physiology and cell death by the Bcl-2 family proteins Bax and Bok
D’Orsi, B., Mateyka, J., & Prehn, J. H. M. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.03.010 · Cited by 134
Lu, X., Ginsburg, K. S., Kettlewell, S., Bossuyt, J., Smith, G. L., & Bers, D. M. (2012) · Circulation Research · doi:10.1161/circresaha.111.300501 · Cited by 131
Xia, T. (2006) · Frontiers in bioscience · doi:10.2741/2142 · Cited by 130
Muoio, D. M., & Koves, T. R. (2007) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/h07-083 · Cited by 129
Paschos, A., Pandya, R., Duivenvoorden, W., & Pinthus, J. H. (2013) · Prostate Cancer and Prostatic Diseases · doi:10.1038/pcan.2013.13 · Cited by 130
Ryanodine Receptor 1-Related Myopathies: Diagnostic and Therapeutic Approaches
Lawal, T. A., Todd, J. J., & Meilleur, K. G. (2018) · Neurotherapeutics · doi:10.1007/s13311-018-00677-1 · Cited by 131
Reiniers, M. J., van Golen, R. F., van Gulik, T. M., & Heger, M. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5486 · Cited by 134
Regulation of mitochondrial fission by intracellular Ca2+ in rat ventricular myocytes
Hom, J., Yu, T., Yoon, Y., Porter, G. A., & Sheu, S. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.03.018 · Cited by 130
Self-citationDai, S., Chen, T., Wang, Y., Zhu, J., Luo, P., Rao, W., Yang, Y., Fei, Z., & Jiang, X. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms150814591 · Cited by 127
The mitochondrial ATP synthase is a shared drug target for aging and dementia
Goldberg, J., Currais, A. J. M., Prior, M., Fischer, W. H., Chiruta, C., Ratliff, E. P., Daugherty, D., Dargusch, R., Finley, K. D., Esparza‐Moltó, P. B., et al. (2018) · Aging Cell · doi:10.1111/acel.12715 · Cited by 131
Amaroli, A., Ravera, S., Baldini, F., Benedicenti, S., Panfoli, I., & Vergani, L. (2018) · Lasers in Medical Science · doi:10.1007/s10103-018-2623-5 · Cited by 127
Oxidative stress serves as a key checkpoint for IL‐33 release by airway epithelium
Uchida, M., Anderson, E. L., Squillace, D. L., Patil, N. P., Maniak, P. J., Iijima, K., Kita, H., & O’Grady, S. M. (2017) · Allergy · doi:10.1111/all.13158 · Cited by 128
Heidari, R., Niknahad, H., Sadeghi, A., Mohammadi, H., Ghanbarinejad, V., Ommati, M. M., Hosseini, A. Z., Azarpira, N., Khodaei, F., Farshad, O., et al. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.04.010 · Cited by 126
Fridlyand, L. E., & Philipson, L. H. (2006) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1363.019 · Cited by 122
Smirlis, D., Duszenko, M., Jiménez-Ruı́z, A., Scoulica, E. V., Bastien, P., Fasel, N. J., & Soteriadou, K. (2010) · Parasites & Vectors · doi:10.1186/1756-3305-3-107 · Cited by 124
Yan, W., Chen, W., & Huang, L. (2008) · Journal of Controlled Release · doi:10.1016/j.jconrel.2008.05.005 · Cited by 125
Reactive oxygen species-mediated cardiac-reperfusion injury: Mechanisms and therapies
Bagheri, F., Khori, V., Alizadeh, A. M., Khalighfard, S., Khodayari, S., & Khodayari, H. (2016) · Life Sciences · doi:10.1016/j.lfs.2016.09.013 · Cited by 132
Aparicio‐Trejo, O. E., Reyes-Fermín, L. M., Briones‐Herrera, A., Tapia, E., León‐Contreras, J. C., Hernández‐Pando, R., Sánchez‐Lozada, L. G., & Pedraza‐Chaverrí, J. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.11.005 · Cited by 125
SGLT2 Inhibitors Play a Salutary Role in Heart Failure via Modulation of the Mitochondrial Function
Maejima, Y. (2020) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2019.00186 · Cited by 133
Brand, M. D. (2020) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2020.1828258 · Cited by 123
Mitochondria-Associated Endoplasmic Reticulum Membranes in Cardiovascular Diseases
Gao, P., Yan, Z., & Zhu, Z. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.604240 · Cited by 136
Li, R., Sun, Z., Zhao, Y., Li, L., Yang, X., Cen, J., Chen, S., Li, C., & Wang, Y. (2021) · Food Chemistry · doi:10.1016/j.foodchem.2021.129737 · Cited by 124
Madireddy, S., & Madireddy, S. (2023) · Brain Sciences · doi:10.3390/brainsci13050784 · Cited by 124
The Ca2+ leak paradox and “rogue ryanodine receptors”: SR Ca2+ efflux theory and practice
Sobie, E. A., Guatimosim, S., Gómez-Víquez, L., Song, L., Hartmann, H. A., SALEETJAFRI, M., & Lederer, W. J. (2005) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2005.06.010 · Cited by 124
Haynes, R. K., Chan, W. C., Lung, C., Uhlemann, A., Eckstein, U., Taramelli, D., Parapini, S., Monti, D., & Krishna, S. (2007) · ChemMedChem · doi:10.1002/cmdc.200700108 · Cited by 123
Toxicity of vanadium on isolated rat liver mitochondria: a new mechanistic approach
Hosseini, M., Shaki, F., Ghazi‐Khansari, M., & Pourahmad, J. (2012) · Metallomics · doi:10.1039/c2mt20198d · Cited by 122
Nadtochiy, S. M., Tompkins, A. J., & Brookes, P. S. (2006) · Biochemical Journal · doi:10.1042/bj20051927 · Cited by 127
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Metadata
- Authors
- Brookes, P. S., Yoon, Y., Robotham, J. L., Anders, M. W., & Sheu, S.-S.
- Affiliations
- University of Rochester Medicine (US)
- Venue
- American Journal of Physiology-Cell Physiology
- Publisher
- American Physiological Society
- Published
- 2004-10
- Volume
- 287
- Issue
- 4
- Pages
- C817-C833
- ISSN
- 0363-6143 (ISSN-L)
- 1522-1563
- OpenAlex
- W2068048197
- Cited by
- 2,575
- References
- 227
- Citations by year
- 2026: 72 · 2025: 112 · 2024: 126 · 2023: 138 · 2022: 144 · 2021: 177 · 2020: 162 · 2019: 134 · 2018: 125 · 2017: 125 · 2016: 122 · 2015: 125 · 2014: 124 · 2013: 129 · 2012: 124
- FWCI
- 5.61
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- American Journal of Physiology-Cell Physiology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Medical Center, University of Rochester
- National Heart, Lung, and Blood Institute (HL 33333, R01HL033333, HL-71158-01, R01HL071158)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK-061991, R01DK061991)
- National Institute of Neurological Disorders and Stroke (NS-37710, R01NS037710)
- Topics
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- mitochondrial calcium homeostasis, ATP production, reactive oxygen species, mitochondrial dysfunction, mitochondrial permeability transition pore, cytochrome c release, apoptosis, two-hit hypothesis, mitochondrial bioenergetics, calcium signaling
- MeSH terms
- Adenosine Triphosphate, Calcium, Energy Metabolism, Ion Channels, Mitochondria, Signal Transduction, Reactive Oxygen Species
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