Mitochondria: regulators of signal transduction by reactive oxygen and nitrogen species
Abstract
The functional role of mitochondria in cell physiology has previously centered around metabolism, with oxidative phosphorylation playing a pivotal role. Recently, however, this perspective has changed significantly with the realization that mitochondria are active participants in signal transduction pathways, not simply the passive recipients of injunctions from the rest of the cell. In this review the emerging role of the mitochondrion in cell signaling is discussed in the context of cytochrome c release, hydrogen peroxide formation from the respiratory chain, and the nitric oxide-cytochrome c oxidase signaling pathway.
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The high affinity and rapid binding of NO to ferrous heme are important biologically for regulation of mitochondrial respiration at CcOx.
“The high affinity and rapid binding to ferrous heme are important biologically for the activation of sGC to generate the second messenger cGMP and the regulation of mitochondrial respiration at CcOx (9–16).”
From What Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology (2010) · cites this paper as [9]
The high affinity and rapid binding of NO to ferrous heme are important biologically for activation of sGC to generate cGMP.
“The high affinity and rapid binding to ferrous heme are important biologically for the activation of sGC to generate the second messenger cGMP and the regulation of mitochondrial respiration at CcOx (9–16).”
From What Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology (2010) · cites this paper as [9]
Cites
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 · see citing works
Normalizing mitochondrial superoxide production blocks three pathways of hyperglycaemic damage
Nishikawa, T., Edelstein, D., Du, X. L., Yamagishi, S.-I., Matsumura, T., Kaneda, Y., Yorek, M. A., Beebe, D., Oates, P. J., Hammes, H.-P., et al. (2000) · Nature · doi:10.1038/35008121 · Cited by 4,277 · see citing works
Boveris, A., & Chance, B. (1973) · Biochemical Journal · doi:10.1042/bj1340707 · Cited by 2,626 · see citing works
Cleeter, M. W. J., Cooper, J. M., Darley-Usmar, V. M., Moncada, S., & Schapira, A. H. V. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00424-2 · Cited by 1,241 · see citing works
Self-citationRedox Regulation of Cellular Signalling
Kamata, H., & Hirata, H. (1999) · Cellular Signalling · doi:10.1016/s0898-6568(98)00037-0 · Cited by 1,150 · see citing works
Selective Targeting of a Redox-active Ubiquinone to Mitochondria within Cells
Kelso, G. F., Porteous, C. M., Coulter, C. V., Hughes, G., Porteous, W. K., Ledgerwood, E. C., Smith, R. A. J., & Murphy, M. P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009093200 · Cited by 1,091 · see citing works
Brown, G. C., & Cooper, C. E. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)01290-3 · Cited by 1,055 · see citing works
Schulze‐Osthoff, K., Bakker, A. C., Vanhaesebroeck, B., Beyaert, R., Jacob, W. A., & Fiers, W. C. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42768-8 · Cited by 935 · see citing works
Superoxide production by the mitochondrial respiratory chain
Turrens, J. F. (1997) · Bioscience Reports · doi:10.1023/a:1027374931887 · Cited by 903 · see citing works
Kim, Y.-M., Talanian, R. V., & Billiar, T. R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.49.31138 · Cited by 887 · see citing works
Clementi, E., Brown, G. C., Feelisch, M., & Moncada, S. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.13.7631 · Cited by 863 · see citing works
Thomas, D. D., Liu, X., Kantrow, S. P., & Lancaster, J. R. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.1.355 · Cited by 760 · see citing works
García‐Cardeña, G., Oh, P., Liu, J., Schnitzer, J. E., & Sessa, W. C. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.13.6448 · Cited by 679 · see citing works
Bcl‐2 family: Life‐or‐death switch
Tsujimoto, Y., & Shimizu, S. (2000) · FEBS Letters · doi:10.1016/s0014-5793(99)01761-5 · Cited by 671 · see citing works
Quantification of the contribution of various steps to the control of mitochondrial respiration.
Groen, A. K., Wanders, R. J. A., Westerhoff, H. V., van der Meer, R., & Tager, J. M. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)81026-8 · Cited by 629 · see citing works
Liu, X., Miller, M. J. S., Joshi, M. S., Thomas, D. D., & Lancaster, J. R. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.5.2175 · Cited by 602 · see citing works
Goossens, V., Grooten, J., Vos, K. J. D., & Fiers, W. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.18.8115 · Cited by 595 · see citing works
Production of Nitric Oxide by Mitochondria
Giulivi, C., Poderoso, J. J., & Boveris, A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.18.11038 · Cited by 572 · see citing works
Nitric oxide synthase activity in mitochondria
Ghafourifar, P., & Richter, C. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01397-5 · Cited by 567 · see citing works
Pueyo, M. E., Gonzalez, W., Nicoletti, A., Savoie, F., Arnal, J., & Michel, J. (2000) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.20.3.645 · Cited by 516 · see citing works
Biological aspects of reactive nitrogen species
Patel, R. P., McAndrew, J., Sellak, H., White, C. R., Jo, H., Freeman, B. A., & Darley-Usmar, V. M. (1999) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(99)00028-6 · Cited by 498 · see citing works
Self-citationNitric Oxide as a Bifunctional Regulator of Apoptosis
Kim, Y., Bombeck, C. A., & Billiar, T. R. (1999) · Circulation Research · doi:10.1161/01.res.84.3.253 · Cited by 463 · see citing works
Ballinger, S. W., Patterson, C., Yan, C.-N., Doan, R., Burow, D. L., Young, C. G., Yakes, F. M., Houten, B. V., Ballinger, C. A., Freeman, B. Α., et al. (2000) · Circulation Research · doi:10.1161/01.res.86.9.960 · Cited by 442 · see citing works
Diffusion of Nitric Oxide in the Aorta Wall Monitored in Situ by Porphyrinic Microsensors
Malinski, T., Taha, Z., Grunfeld, S., Patton, S. R., Kapturczak, M., & Tomboulian, P. (1993) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1993.1735 · Cited by 417 · see citing works
Nitric Oxide‐Mediated Inhibition of the Mitochondrial Respiratory Chain in Cultured Astrocytes
Bolaños, J. P., Peuchen, S., Heales, S., Land, J. M., & Clark, J. B. (1994) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1994.63030910.x · Cited by 413 · see citing works
Role for mitochondrial oxidants as regulators of cellular metabolism
Nemoto, S., Takeda, K., Yu, Z.-X., Ferrans, V. J., & Finkel, T. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.19.7311-7318.2000 · Cited by 393 · see citing works
Brookes, P. S., Salinas, E. P., Darley-Usmar, K., Eiserich, J. P., Freeman, B. A., Darley-Usmar, V. M., & Anderson, P. G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001077200 · Cited by 321 · see citing works
Self-citationSchaper, J., Meiser, E., & Stämmler, G. (1985) · Circulation Research · doi:10.1161/01.res.56.3.377 · Cited by 296 · see citing works
Galdo, N. A. R., Clementi, E., Melani, M., Boveris, A., Cadenas, E., Moncada, S., & Poderoso, J. J. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3590139 · Cited by 278 · see citing works
RIOBÓ, N. A., CLEMENTI, E., MELANI, M., BOVERIS, A., CADENAS, E., MONCADA, S., & PODEROSO, J. J. (2001) · Biochemical Journal · doi:10.1042/bj3590139 · Cited by 278 · see citing works
Inhibition of Mitochondrial ATP Generation by Nitric Oxide Switches Apoptosis to Necrosis
Leist, M., Single, B., Naumann, H., Fava, E., Simon, B., Kühnle, S., & Nicotera, P. (1999) · Experimental Cell Research · doi:10.1006/excr.1999.4514 · Cited by 275 · see citing works
Rubbo, H., Parthasarathy, S., Barnes, S., KIRK, M. C., Kalyanaraman, B., & Freeman, B. Α. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.9935 · Cited by 263 · see citing works
Ceramide Interaction with the Respiratory Chain of Heart Mitochondria
Di Paola, M., Cocco, T., & Lorusso, M. (2000) · Biochemistry · doi:10.1021/bi9924415 · Cited by 262 · see citing works
Mitochondrial Nitric Oxide Synthase: A Ubiquitous Regulator of Oxidative Phosphorylation?
Bates, T. E., Loesch, A., Burnstock, G., & Clark, J. B. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.0008 · Cited by 245 · see citing works
Xie, Y.-W., Shen, W., Zhao, G., Xu, X., Wolin, M. S., & Hintze, T. H. (1996) · Circulation Research · doi:10.1161/01.res.79.3.381 · Cited by 229 · see citing works
Nitric oxide stimulates glucose transport and metabolism in rat skeletal muscle in vitro
Young, M. E., Radda, G. K., & Leighton, B. (1997) · Biochemical Journal · doi:10.1042/bj3220223 · Cited by 214 · see citing works
Shiva, S., Brookes, P. S., Patel, R. P., Anderson, P. G., & Darley-Usmar, V. M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.131128898 · Cited by 212 · see citing works
Self-citationPorter, R. K., Hulbert, A. J., & Brand, M. D. (1996) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.1996.271.6.r1550 · Cited by 208 · see citing works
Torres, J., Darley-Usmar, V. M., & Wilson, M. T. (1995) · Biochemical Journal · doi:10.1042/bj3120169 · Cited by 206 · see citing works
Self-citationImmunocytochemical Evidence for a Mitochondrially Located Nitric Oxide Synthase in Brain and Liver
Bates, T. E., Loesch, A., Burnstock, G., & Clark, J. B. (1995) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1995.2213 · Cited by 204 · see citing works
Borutaitė, V., Jekabsone, A., & Brown, G. C. (2000) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(00)00178-x · Cited by 197 · see citing works
NO: an inhibitor of cell death
Liu, L., & Stamler, J. S. (1999) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400578 · Cited by 190 · see citing works
Poderoso, J. J., Lisdero, C. L., Schopfer, F. J., Galdo, N. A. R., Carreras, M. C., Cadenas, E., & Boveris, A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.53.37709 · Cited by 183 · see citing works
Nitric Oxide and Cytochrome c Oxidase: Mechanisms of Inhibition and NO Degradation
Sarti, P., Giuffrè, A., Forte, E., Mastronicola, D., Barone, M. C., & Brunori, M. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3117 · Cited by 168 · see citing works
Self-citationPeroxynitrite causes calcium efflux from mitochondria which is prevented by Cyclosporin A
Packer, M. A., & Murphy, M. P. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00461-7 · Cited by 143 · see citing works
Brookes, P., & Darley-Usmar, V. M. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00805-x · Cited by 137 · see citing works
Self-citationStudies of the primary oxygen intermediate in the reaction of fully reduced cytochrome oxidase.
Blackmore, R. S., Greenwood, C., & Gibson, Q. H. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54989-9 · Cited by 125 · see citing works
Peroxynitrite and Brain Mitochondria: Evidence for Increased Proton Leak
Brookes, P. S., Land, J. M., Clark, J. B., & Heales, S. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.70052195.x · Cited by 125 · see citing works
Self-citationBeauvais, F., Michel, L., & Dubertret, L. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00188-f · Cited by 124 · see citing works
Gadelha, F. R., Thomson, L., Fagian, M. M., Costa, A. D. T., Radí, R., & Vercesi, A. E. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0259 · Cited by 122 · see citing works
Cassarino, D. S., Halvorsen, E. M., Swerdlow, R. H., Abramova, N. N., Parker, W. D., Sturgill, T. W., & Bennett, J. P. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0741384.x · Cited by 121 · see citing works
Superoxide production by mitochondria in the presence of nitric oxide forms peroxynitrite
Packer, M. A., Porteous, C. M., & Murphy, M. P. (1996) · IUBMB Life · doi:10.1080/15216549600201103 · Cited by 118 · see citing works
Cytochrome c oxidase rapidly metabolises nitric oxide to nitrite
Torres, J., Sharpe, M. A., Rosquist, A., Cooper, C. E., & Wilson, M. T. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01682-3 · Cited by 109 · see citing works
Nitric oxide as a competitive inhibitor of oxygen consumption in the mitochondrial respiratory chain
Brown, G. C. (2000) · Acta Physiologica Scandinavica · doi:10.1046/j.1365-201x.2000.00718.x · Cited by 108 · see citing works
Liu, T., Stern, A., Roberts, L. J., & Morrow, J. D. (1999) · Journal of Biomedical Science · doi:10.1007/bf02253564 · Cited by 107 · see citing works
Formation of nanomolar concentrations of S-nitroso-albumin in human plasma by nitric oxide
Marley, R., Patel, R. P., Orie, N. N., CEASER, E. K., Darley-Usmar, V. M., & Moore, K. P. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00627-x · Cited by 104 · see citing works
Self-citationMitochondrial Genetic Control of Assembly and Function of Complex I in Mammalian Cells
Chomyn, A. (2001) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1010791204961 · Cited by 90 · see citing works
[Redox regulation of cellular signaling].
Suzuki, Y. (1997) · PubMed · Cited by 90 · see citing works
Yu, X. X., Barger, J. L., Boyer, B. B., Brand, M. D., Pan, G., & Adams, S. H. (2000) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2000.279.2.e433 · Cited by 81 · see citing works
Paxinou, E., Weisse, M., Chen, Q., Souza, J. M., Hertkorn, C., Selak, M. A., Daikhin, E., Yudkoff, M., Sowa, G., Sessa, W. C., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.201293198 · Cited by 77 · see citing works
Papadopoulou, L. C., Theophilidis, G., Thomopoulos, G. N., & Tsiftsoglou, A. S. (1999) · Biochemical Pharmacology · doi:10.1016/s0006-2952(98)00305-0 · Cited by 75 · see citing works
Giuffrè, A., Barone, M. C., Mastronicola, D., D’Itri, E., Sarti, P., & Brunori, M. (2000) · Biochemistry · doi:10.1021/bi000447k · Cited by 75 · see citing works
Self-citationRedox Regulation of GA-binding Protein-α DNA Binding Activity
Martin, M. E., Chinenov, Y. V., Yu, M., Schmidt, T., & Yang, X.-Y. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.41.25617 · Cited by 65 · see citing works
Leist, M., Single, B., Naumann, H., Fava, E., Simon, B., Kühnle, S., & Nicotera, P. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0491 · Cited by 64 · see citing works
Bogoyevitch, M. A., Ng, D. C. H., Court, N. W., Draper, K. A., Dhillon, A. S., & Abas, L. (2000) · Journal of Molecular and Cellular Cardiology · doi:10.1006/jmcc.2000.1187 · Cited by 62 · see citing works
Brookes, P. S., Zhang, J., Dai, L., Zhou, F., Parks, D. A., Darley-Usmar, V. M., & Anderson, P. G. (2001) · Journal of Molecular and Cellular Cardiology · doi:10.1006/jmcc.2000.1276 · Cited by 61 · see citing works
Self-citationCytochrome c Oxidase Subunit III
You, K.-R., Wen, J., Lee, S.-T., & Kim, D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109284200 · Cited by 56 · see citing works
Endogenous nitric oxide in the control of skeletal muscle oxygen extraction during exercise
Shen, W., Xu, X., Ochoa, M., Zhao, G., Bernstein, R. D., Forfia, P. R., & Hintze, T. H. (2000) · Acta Physiologica Scandinavica · doi:10.1046/j.1365-201x.2000.00719.x · Cited by 53 · see citing works
Expression of bovine and mouse endothelial cell antioxidant enzymes following TNF-α exposure
Shaffer, J. B., Treanor, C. P., & Vecchio, P. J. D. (1990) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(90)90064-p · Cited by 52 · see citing works
Bioenergetics in cardiac hypertrophy: mitochondrial respiration as a pathological target of NO·
Dai, L., Brookes, P. S., Darley-Usmar, V. M., & Anderson, P. G. (2001) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.2001.281.6.h2261 · Cited by 44 · see citing works
Self-citationAbas, L., Bogoyevitch, M. A., & Guppy, M. (2000) · Biochemical Journal · doi:10.1042/0264-6021:3490119 · Cited by 43 · see citing works
Determination of the structures of respiratory enzyme complexes from mammalian mitochondria
Walker, J. E. (1995) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/0925-4439(95)00031-x · Cited by 42 · see citing works
Nitric oxide-dependent downregulation of adipocyte UCP-2 expression by tumor necrosis factor-α
Merial, C., Bouloumié, A., Trocheris, V., Lafontan, M., & Galitzky, J. (2000) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.2000.279.4.c1100 · Cited by 35 · see citing works
Abas, L., Bogoyevitch, M. A., & Guppy, M. (2000) · Biochemical Journal · doi:10.1042/bj3490119 · Cited by 30 · see citing works
Flagged first, then by citations
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Sorted by citations
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 · see citing works
Self-citationSuperoxide Dismutases: Role in Redox Signaling, Vascular Function, and Diseases
Fukai, T., & Ushio‐Fukai, M. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.3999 · Cited by 2,009 · see citing works
Role of oxygen radicals in DNA damage and cancer incidence
Valko, M., Izakovic, M., Mazur, M., Rhodes, C. J., & Telser, J. (2004) · Molecular and Cellular Biochemistry · doi:10.1023/b:mcbi.0000049134.69131.89 · Cited by 1,820 · see citing works
Antioxidant responses and cellular adjustments to oxidative stress
Espinosa-Diez, C., Miguel, V., Mennerich, D., Kietzmann, T., Sánchez-Pérez, P., Cadenas, S., & Lamas, S. (2015) · Redox Biology · doi:10.1016/j.redox.2015.07.008 · Cited by 1,046 · see citing works
Valavanidis, A., Vlachogianni, T., Fiotakis, K., & Loridas, S. (2013) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph10093886 · Cited by 910 · see citing works
Butow, R. A., & Avadhani, N. G. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00179-0 · Cited by 882 · see citing works
Mitochondrial Dysfunction in Atherosclerosis
Madamanchi, N. R., & Runge, M. S. (2007) · Circulation Research · doi:10.1161/01.res.0000258450.44413.96 · Cited by 794 · see citing works
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Dikalov, S. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.06.033 · Cited by 783 · see citing works
Thioredoxin reductase: A target for gold compounds acting as potential anticancer drugs
Bindoli, A., Rigobello, M. P., Scutari, G., Gabbiani, C., Casini, A., & Luigi Messori, A. (2009) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2009.02.026 · Cited by 594 · see citing works
Mikkelsen, R. B., & Wardman, P. (2003) · Oncogene · doi:10.1038/sj.onc.1206663 · Cited by 591 · see citing works
Mitochondrial Signaling in Mammalian Cells Activated by Red and Near‐IR Radiation
Karu, T. I. (2008) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.2008.00394.x · Cited by 575 · see citing works
Mitochondrial localization of estrogen receptor β
Yang, S.-H., Liu, R., Perez, E., Wen, Y., Stevens, S. M., Valencia, T. G., Brun‐Zinkernagel, A., Prókai, L., Will, Y., Dykens, J. A., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0306948101 · Cited by 501 · see citing works
Stowe, D. F., & Camara, A. K. S. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2331 · Cited by 471 · see citing works
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Robert, F. F. (2009) · Frontiers in bioscience · doi:10.2741/3303 · Cited by 439 · see citing works
Redox regulation of glial inflammatory response to lipopolysaccharide and interferonγ
Pawate, S., Shen, Q., Fan, F., & Bhat, N. R. (2004) · Journal of Neuroscience Research · doi:10.1002/jnr.20180 · Cited by 428 · see citing works
Nitric oxide and cell viability in inflammatory cells: a role for NO in macrophage function and fate
Boscá, L., Zeini, M., Través, P. G., & Hortelano, S. (2005) · Toxicology · doi:10.1016/j.tox.2004.11.035 · Cited by 356 · see citing works
Nitric oxide signaling: Classical, less classical, and nonclassical mechanisms
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Free Radicals, Mitochondria, and Oxidized Lipids
Gutiérrez, J., Ballinger, S. W., Darley-Usmar, V. M., & Landar, A. L. (2006) · Circulation Research · doi:10.1161/01.res.0000248212.86638.e9 · Cited by 319 · see citing works
Self-citationFree radicals, mitochondria, and hypoxia–ischemia in the developing brain
Blomgren, K., & Hagberg, H. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.08.040 · Cited by 310 · see citing works
What Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology
Hill, B. G., Dranka, B. P., Bailey, S. M., Lancaster, J. R., & Darley-Usmar, V. M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r110.101618 · Cited by 310 · see citing works
Self-citationRegulation of sperm function by reactive oxygen species
Ford, W. C. L. (2004) · Human Reproduction Update · doi:10.1093/humupd/dmh034 · Cited by 305 · see citing works
Molecular 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 303 · see citing works
Nitric oxide and mitochondrial biogenesis
Nisoli, E., & Carruba, M. O. (2006) · Journal of Cell Science · doi:10.1242/jcs.03062 · Cited by 278 · see citing works
Ghouleh, I. A., Khoo, N. K. H., Knaus, U. G., Griendling, K. K., Touyz, R. M., Thannickal, V. J., Barchowsky, A., Nauseef, W. M., Kelley, E. E., Bauer, P. M., et al. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.06.011 · Cited by 249 · see citing works
Self-citationThiol Chemistry in Peroxidase Catalysis and Redox Signaling
Bindoli, A., Fukuto, J. M., & Forman, H. J. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2063 · Cited by 242 · see citing works
Sabri, A., Hughie, H. H., & Lucchesi, P. A. (2003) · Antioxidants and Redox Signaling · doi:10.1089/152308603770380034 · Cited by 236 · see citing works
Kim, J., Xu, M., Xo, R., Mates, A., Wilson, G. L., Pearsall, A. W., & Grishko, V. I. (2009) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2009.09.008 · Cited by 235 · see citing works
Nox enzymes as novel targets for drug development
Lambeth, J. D., Krause, K.-H., & Clark, R. A. (2008) · Seminars in Immunopathology · doi:10.1007/s00281-008-0123-6 · Cited by 212 · see citing works
The coordination of nuclear and mitochondrial communication during aging and calorie restriction
Finley, L. W. S., & Haigis, M. C. (2009) · Ageing Research Reviews · doi:10.1016/j.arr.2009.03.003 · Cited by 207 · see citing works
Oxidative stress and apoptosis: a new treatment paradigm in cancer
Ryan, H. E. (2006) · Frontiers in bioscience · doi:10.2741/1798 · Cited by 202 · see citing works
The effects of superoxide dismutase on H2O2 formation
Liochev, S. I., & Fridovich, I. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.02.015 · Cited by 202 · see citing works
Enalapril and losartan attenuate mitochondrial dysfunction in aged rats
de Cavanagh, E. M. V., Piotrkowski, B., Basso, N., Stella, I., Inserra, F., Ferder, L., & Fraga, C. G. (2003) · The FASEB Journal · doi:10.1096/fj.02-0063fje · Cited by 185 · see citing works
Pathological apoptosis in the developing brain
Blomgren, K., Leist, M., & Groc, L. (2007) · APOPTOSIS · doi:10.1007/s10495-007-0754-4 · Cited by 181 · see citing works
Cooper, C. E., & Giulivi, C. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00310.2006 · Cited by 176 · see citing works
Boll, M.-C., Alcaraz-Zubeldia, M., Montes, S., & Rios, C. (2008) · Neurochemical Research · doi:10.1007/s11064-008-9610-3 · Cited by 173 · see citing works
Burwell, L. S., & Brookes, P. S. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1845 · Cited by 172 · see citing works
Self-citationThe Complex Interplay between Mitochondria, ROS and Entire Cellular Metabolism
Kuznetsov, A. V., Margreiter, R., Ausserlechner, M. J., & Hagenbuchner, J. (2022) · Antioxidants · doi:10.3390/antiox11101995 · Cited by 168 · see citing works
Hoffman, D. L., Salter, J. D., & Brookes, P. S. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00699.2006 · Cited by 167 · see citing works
Self-citationHan, D., Canali, R., Garcia, J., Aguilera, R., Gallaher, T. K., & Cadenas, E. (2005) · Biochemistry · doi:10.1021/bi0509393 · Cited by 161 · see citing works
Keller, A., Mohamed, A., Dröse, S., Brandt, U., Fleming, I., & Brandes, R. P. (2004) · Free Radical Research · doi:10.1080/10715760400022145 · Cited by 157 · see citing works
Mitochondrial dysfunction, oxidative stress, and major depressive disorder
Tobe, E. (2013) · Neuropsychiatric Disease and Treatment · doi:10.2147/ndt.s44282 · Cited by 156 · see citing works
Mitochondrial nitric oxide synthase
Brookes, P. S. (2003) · Mitochondrion · doi:10.1016/j.mito.2003.10.001 · Cited by 154 · see citing works
Self-citationPast decade study of snake venom l-amino acid oxidase
Guo, C., Liu, S., Yao, Y., Zhang, Q., & Sun, M. (2012) · Toxicon · doi:10.1016/j.toxicon.2012.05.001 · Cited by 153 · see citing works
Hughes, G., Murphy, M. P., & Ledgerwood, E. C. (2005) · Biochemical Journal · doi:10.1042/bj20050078 · Cited by 151 · see citing works
Żmijewski, J. W., Moellering, D. R., Goffe, C. L., Landar, A. L., Ramachandran, A., & Darley-Usmar, V. M. (2005) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00015.2005 · Cited by 148 · see citing works
Self-citationLiu, F., Patterson, T. A., Sadovova, N., Zhang, X., Liu, S., Zou, X., Hanig, J. P., Paule, M. G., Slikker, W., & Wang, C. (2012) · Toxicological Sciences · doi:10.1093/toxsci/kfs296 · Cited by 147 · see citing works
Landar, A. L., Żmijewski, J. W., Dickinson, D. A., Goffe, C. L., Johnson, M. S., Milne, G. L., Zanoni, G., Vidari, G., Morrow, J. D., & Darley-Usmar, V. M. (2005) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01087.2005 · Cited by 139 · see citing works
Self-citationOxidative Modification of Proteins: An Emerging Mechanism of Cell Signaling
Wall, S. B., Oh, J., Diers, A. R., & Landar, A. L. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00369 · Cited by 136 · see citing works
Passamonti, M., & Ghiselli, F. (2009) · DNA and Cell Biology · doi:10.1089/dna.2008.0807 · Cited by 136 · see citing works
Nuclear-Mitochondrial Interactions
Walker, B. R., & Moraes, C. T. (2022) · Biomolecules · doi:10.3390/biom12030427 · Cited by 136 · see citing works
Tsatmali, M., Walcott, E. C., & Crossin, K. L. (2005) · Brain Research · doi:10.1016/j.brainres.2005.01.087 · Cited by 133 · see citing works
Isolation of a new l-amino acid oxidase from Crotalus durissus cascavella venom
Toyama, M. H., Toyama, D. D. O., Passero, L. F. D., Laurenti, M. D., Corbett, C. E. P., Tomokane, T. Y., Fonseca, F. V., Antunes, E., Joazeiro, P. P., Beriam, L. O. S., et al. (2005) · Toxicon · doi:10.1016/j.toxicon.2005.09.008 · Cited by 130 · see citing works
Chowdhury, A. R., Zielonka, J., Kalyanaraman, B., Hartley, R. C., Murphy, M. P., & Avadhani, N. G. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101606 · Cited by 128 · see citing works
Menna‐Barreto, R. F. S., & de Castro, S. L. (2014) · BioMed Research International · doi:10.1155/2014/614014 · Cited by 126 · see citing works
Dikalov, S., Polienko, Y. F., & Kirilyuk, I. A. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7396 · Cited by 122 · see citing works
Celastrol ameliorates liver metabolic damage caused by a high-fat diet through Sirt1
Zhang, Y., Geng, C., Liu, X., Li, M., Gao, M., Liu, X., Fang, F., & Chang, Y. (2016) · Molecular Metabolism · doi:10.1016/j.molmet.2016.11.002 · Cited by 120 · see citing works
Redox Control, Redox Signaling, and Redox Homeostasis in Plant Cells
Dietz, K. (2003) · International review of cytology · doi:10.1016/s0074-7696(03)28004-9 · Cited by 121 · see citing works
de Cavanagh, E. M. V., Toblli, J. E., Ferder, L., Piotrkowski, B., Stella, I., & Inserra, F. (2006) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00615.2005 · Cited by 120 · see citing works
de Cavanagh, E. M. V., Ferder, M., Inserra, F., & Ferder, L. (2009) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01176.2008 · Cited by 116 · see citing works
Control of Mitochondrial Respiration by NO., Effects of Low Oxygen and Respiratory State
Brookes, P. S., Kraus, D. W., Shiva, S., Doeller, J. E., Barone, M.-C., Patel, R. P., Lancaster, J. R., & Darley-Usmar, V. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211784200 · Cited by 118 · see citing works
Self-citationValenzuela, R., Costa-Besada, M. A., Iglesias‐González, J., Pérez‐Costas, E., Villar‐Cheda, B., Garrido‐Gil, P., Meléndez‐Ferro, M., Soto‐Otero, R., Lanciego, J. L., Henrion, D., et al. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.327 · Cited by 114 · see citing works
Shiva, S., Oh, J.-Y., Landar, A. L., Ulasova, E., Venkatraman, A., Bailey, S. M., & Darley-Usmar, V. M. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.10.037 · Cited by 112 · see citing works
Self-citationCell signalling by oxidized lipids and the role of reactive oxygen species in the endothelium
Zmijewski, J. W., Landar, A., Watanabe, N., Dickinson, D. A., Noguchi, N., & Darley-Usmar, V. M. (2005) · Biochemical Society Transactions · doi:10.1042/bst20051385 · Cited by 112 · see citing works
Self-citationNitration of the mitochondrial complex I subunit NDUFB8 elicits RIP1- and RIP3-mediated necrosis
Davis, C. W., Hawkins, B. J., Ramasamy, S., Irrinki, K. M., Cameron, B. A., Islam, K., Daswani, V. P., Doonan, P. J., Manevich, Y., & Madesh, M. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.11.001 · Cited by 111 · see citing works
Persistent mitochondrial damage by nitric oxide and its derivatives: neuropathological implications
Bolaños, J. P. (2010) · Frontiers in Neuroenergetics · doi:10.3389/neuro.14.001.2010 · Cited by 110 · see citing works
Mitochondrial Dysfunction and Kidney Stone Disease
Chaiyarit, S., & Thongboonkerd, V. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.566506 · Cited by 109 · see citing works
Tyrosine phosphorylation in mitochondria: A new frontier in mitochondrial signaling
Salvi, M., Brunati, A. M., & Toninello, A. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.02.006 · Cited by 107 · see citing works
Identification of an inducible nitric oxide synthase in diaphragm mitochondria from septic mice
López, L. C., Escames, G., Tapias, V., Utrilla, P., León, J., & Acuña-Castroviejo, D. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.09.008 · Cited by 107 · see citing works
Possible Mechanisms of Neurodegeneration in Schizophrenia
Pérez‐Neri, I., Ramírez‐Bermúdez, J., Montes, S., & Rı́os, C. (2006) · Neurochemical Research · doi:10.1007/s11064-006-9162-3 · Cited by 100 · see citing works
Nitric oxide and cytochrome oxidase: reaction mechanisms from the enzyme to the cell
Sarti, P., Giuffrè, A., Barone, M. C., Forte, E., Mastronicola, D., & Brunori, M. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01326-6 · Cited by 100 · see citing works
Self-citationYin, L., Kosugi, M., & Kufe, D. W. (2011) · Blood · doi:10.1182/blood-2011-07-369686 · Cited by 97 · see citing works
Watanabe, N., Zmijewski, J. W., Takabe, W., Umezu‐Goto, M., Goffe, C. L., Sekine, A., Landar, A. L., Watanabe, A., Aoki, J., Arai, H., et al. (2006) · American Journal Of Pathology · doi:10.2353/ajpath.2006.050648 · Cited by 96 · see citing works
Self-citationMitochondrial Uncoupling Proteins in the Central Nervous System
Kim‐Han, J. S., & Dugan, L. L. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.1173 · Cited by 95 · see citing works
Sudawan, B., Chang, C.-S., Chao, H.-F., Ku, M. S. B., & Yen, Y.-F. (2016) · BMC Plant Biology · doi:10.1186/s12870-016-0889-y · Cited by 93 · see citing works
Vanin, A. F., Svistunenko, D. A., Mikoyan, V. D., Сереженков, В. А., Fryer, M. J., Baker, N. R., & Cooper, C. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312601200 · Cited by 93 · see citing works
Suliman, H. B., Welty‐Wolf, K. E., Carraway, M. S., Schwartz, D. A., Hollingsworth, J. W., & Piantadosi, C. A. (2005) · The FASEB Journal · doi:10.1096/fj.04-3500fje · Cited by 92 · see citing works
Walford, G. A., Moussignac, R., Scribner, A. W., Loscalzo, J., & Leopold, J. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310582200 · Cited by 89 · see citing works
Martinc, B., Grabnar, I., & Vovk, T. (2012) · Current Neuropharmacology · doi:10.2174/157015912804143504 · Cited by 88 · see citing works
Myoglobin and mitochondria: A relationship bound by oxygen and nitric oxide
Kamga, C., Krishnamurthy, S., & Shiva, S. (2012) · Nitric Oxide · doi:10.1016/j.niox.2012.03.005 · Cited by 86 · see citing works
Self-citationEvens, A. M., Lecane, P. S., Magda, D. J., Prachand, S., Singhal, S., Nelson, J. S., Miller, R. A., Gartenhaus, R. B., & Gordon, L. I. (2004) · Blood · doi:10.1182/blood-2004-03-0964 · Cited by 85 · see citing works
Lee, J. Y., Jung, G., Heo, H. J., Yun, M. R., Park, J. Y., Bae, S. S., Hong, K. W., Lee, W. S., & Kim, C. D. (2006) · Toxicology Letters · doi:10.1016/j.toxlet.2006.07.305 · Cited by 85 · see citing works
Laser therapy: A review of its mechanism of action and potential medical applications
Tata, D. B., & Waynant, R. W. (2010) · Laser & Photonics Review · doi:10.1002/lpor.200900032 · Cited by 85 · see citing works
Inhibition of mitochondrial function induces an integrated stress response in oligodendroglia
Silva, J. M., Wong, A., Carelli, V., & Cortopassi, G. A. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.02.005 · Cited by 84 · see citing works
Lisdat, F., Dronov, R., Möhwald, H., Scheller, F. W., & Kurth, D. G. (2008) · Chemical Communications · doi:10.1039/b813559b · Cited by 82 · see citing works
Buerk, D. G., Lamkin-Kennard, K. A., & Jaron, D. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00178-3 · Cited by 80 · see citing works
Ortiz, F., García, J. A. G., Acuña-Castroviejo, D., Doerrier, C., López, A., Venegas, C., Volt, H., Luna‐Sánchez, M., López, L. C., & Escames, G. (2013) · Journal of Pineal Research · doi:10.1111/jpi.12099 · Cited by 79 · see citing works
Feifel, S. C., Stieger, K. R., Lokstein, H., Lux, H., & Lisdat, F. (2015) · Journal of Materials Chemistry A · doi:10.1039/c5ta00656b · Cited by 77 · see citing works
Cappellari, G. G., Zanetti, M., Semolic, A., Vinci, P., Ruozi, G., Falcione, A., Filigheddu, N., Guarnieri, G., Graziani, A., Giacca, M., et al. (2016) · Diabetes · doi:10.2337/db15-1019 · Cited by 77 · see citing works
Mitochondrial Ca2+ Homeostasis: Emerging Roles and Clinical Significance in Cardiac Remodeling
Zhang, D., Wang, F., Li, P., & Gao, Y. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23063025 · Cited by 75 · see citing works
Modulation of GSH levels in ABCC1 expressing tumor cells triggers apoptosis through oxidative stress
Laberge, R.-M., Karwatsky, J., Lincoln, M. C., Leimanis, M. L., & Georges, E. (2007) · Biochemical Pharmacology · doi:10.1016/j.bcp.2007.02.005 · Cited by 75 · see citing works
Nitric oxide and the respiratory enzyme
Brunori, M., Forte, E., Arese, M., Mastronicola, D., Giuffrè, A., & Sarti, P. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.05.011 · Cited by 74 · see citing works
Self-citationNew insights into male (in)fertility: the importance of NO
Buzadžić, B., Vučetić, M., Janković, A., Stančić, A., Korać, A., Korać, B., & Otašević, V. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12675 · Cited by 71 · see citing works
Mattsson, M., & Simkó, M. (2014) · Frontiers in Public Health · doi:10.3389/fpubh.2014.00132 · Cited by 71 · see citing works
Dronov, R., Kurth, D. G., Möhwald, H., Scheller, F. W., & Lisdat, F. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200704049 · Cited by 71 · see citing works
Ingram, T. E., Fraser, A. G., Bleasdale, R. A., Ellins, E. A., Margulescu, A. D., Halcox, J. P., & James, P. E. (2013) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2013.03.050 · Cited by 69 · see citing works
Biochemical Basis for Functional Ingredient Design from Fruits
Jacob, J. K., Tiwari, K., Correa-Betanzo, J., Misran, A. B., Chandrasekaran, R., & Paliyath, G. (2012) · Annual Review of Food Science and Technology · doi:10.1146/annurev-food-022811-101127 · Cited by 69 · see citing works
Application of nanotechnology to herbal antioxidants as improved phytomedicine: An expanding horizon
Mishra, Y., Amin, H. I. M., Mishra, V., Vyas, M., Prabhakar, P. K., Gupta, M., Kanday, R., Sudhakar, K., Saini, S., Hromić‐Jahjefendić, A., et al. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113413 · Cited by 69 · see citing works
Mitochondria-targeted heme oxygenase-1 decreases oxidative stress in renal epithelial cells
Bolisetty, S., Traylor, A., Zarjou, A., Johnson, M. S., Benavides, G. A., Ricart, K. C., Boddu, R., Moore, R. D., Landar, A. L., Barnes, S., et al. (2013) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00160.2013 · Cited by 68 · see citing works
Self-citationProteomic analysis of mitochondria from Caenorhabditis elegans
Li, J., Cai, T., Wu, P., Cui, Z., Chen, X., Hou, J., Xie, Z., Xue, P., Shi, L., Liu, P., et al. (2009) · PROTEOMICS · doi:10.1002/pmic.200900101 · Cited by 67 · see citing works
Redox biology and the interface between bioenergetics, autophagy and circadian control of metabolism
Wende, A. R., Young, M. E., Chatham, J. C., Zhang, J., Rajasekaran, N. S., & Darley-Usmar, V. M. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.05.022 · Cited by 65 · see citing works
Self-citation
- Authors
- Brookes, P. S., Levonen, A.-L., Shiva, S., Sarti, P., & Darley-Usmar, V. M.
- Affiliations
- University of Alabama at Birmingham (US)
- Sapienza University of Rome (IT)
- Corresponding author
- Darley-Usmar, Victor M.
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2002-09
- Volume
- 33
- Issue
- 6
- Pages
- 755-764
- ISSN
- 0891-5849 (ISSN-L)
- OpenAlex
- W1748754899
- Cited by
- 298
- References
- 72
- Citations by year
- 2025: 2 · 2024: 5 · 2023: 1 · 2022: 6 · 2021: 1 · 2020: 3 · 2019: 9 · 2018: 9 · 2017: 10 · 2016: 12 · 2015: 14 · 2014: 13 · 2013: 13 · 2012: 21
- FWCI
- 7.09
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- IRIS Research product catalog (Sapienza University of Rome) (submittedVersion)
- Funders
- American Heart Association
- National Institutes of Health (1r03aa012613-01)
- National Institute on Alcohol Abuse and Alcoholism (AA 12613)
- National Heart, Lung, and Blood Institute (R01HL058031, HL-58031)
- National Institute of Environmental Health Sciences (R01ES010167, ES-10167)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- mitochondria, signal transduction, reactive oxygen species, reactive nitrogen species, cytochrome c release, hydrogen peroxide, electron transport chain, nitric oxide, cytochrome c oxidase, mitochondrial signaling
- MeSH terms
- Adenosine Triphosphate, Animals, Cytochrome c Group, Electron Transport Complex IV, Free Radicals, Humans, Hydrogen Peroxide, Mitochondria, Models, Biological, Models, Chemical, Nitric Oxide, Oxidation-Reduction, Time Factors, Signal Transduction, Apoptosis, Reactive Oxygen Species, Reactive Nitrogen Species
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