Mitochondrial formation of reactive oxygen species
Open accessAbstract
The reduction of oxygen to water proceeds via one electron at a time. In the mitochondrial respiratory chain, Complex IV (cytochrome oxidase) retains all partially reduced intermediates until full reduction is achieved. Other redox centres in the electron transport chain, however, may leak electrons to oxygen, partially reducing this molecule to superoxide anion (O(2)(−)•). Even though O(2)(−)• is not a strong oxidant, it is a precursor of most other reactive oxygen species, and it also becomes involved in the propagation of oxidative chain reactions. Despite the presence of various antioxidant defences, the mitochondrion appears to be the main intracellular source of these oxidants. This review describes the main mitochondrial sources of reactive species and the antioxidant defences that evolved to prevent oxidative damage in all the mitochondrial compartments. We also discuss various physiological and pathological scenarios resulting from an increased steady state concentration of mitochondrial oxidants.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Superoxide anion •O2− is also produced in the mitochondrial matrix at complexes I to IV during the mitochondrial respiration process.
“Superoxide anion •O2− is also produced in the mitochondrial matrix at complexes I to IV during the mitochondrial respiration process [10].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [10]
Complexes I and II produce ROS only into the mitochondrial matrix.
“Although complexes I and II produce ROS only into the matrix”
From Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes (2010) · cites this paper as [1]
Complex III can produce ROS on both sides of the mitochondrial inner membrane.
“complex III can produce ROS on both sides of the mitochondrial inner membrane 1, 3”
From Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes (2010) · cites this paper as [1]
Complexes I, II, and III of the electron transport chain contain sites where electrons can prematurely reduce oxygen, resulting in superoxide formation.
“Complexes I, II, and III of the electron transport chain contain sites wherein electrons can prematurely reduce oxygen, resulting in the formation of superoxide 1, 2.”
From Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes (2010) · cites this paper as [1]
Cites
Free Radicals in the Physiological Control of Cell Function
Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855 · see citing works
Li, P., Nijhawan, D., Budihardjo, I., Srinivasula, S. M., Ahmad, M., Alnemri, E. S., & Wang, X. (1997) · Cell · doi:10.1016/s0092-8674(00)80434-1 · Cited by 7,289 · see citing works
Hydroperoxide metabolism in mammalian organs.
Chance, B., Sies, H., & Boveris, A. (1979) · Physiological Reviews · doi:10.1152/physrev.1979.59.3.527 · Cited by 5,827 · see citing works
Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly
Beckman, J. S., & Koppenol, W. H. (1996) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1996.271.5.c1424 · Cited by 5,513 · see citing works
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
Oxyl radicals, redox-sensitive signalling cascades and antioxidants
Genestra, M. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2007.04.009 · Cited by 4,930 · see citing works
Superoxide radical and superoxide dismutases
Fridovich, I. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.000525 · Cited by 3,455 · see citing works
Liu, R., Paxton, W. A., Choe, S., Ceradini, D., Martin, S. R., Horuk, R., MacDonald, M. E., Stuhlmann, H., Koup, R. A., & Landau, N. R. (1996) · Cell · doi:10.1016/s0092-8674(00)80110-5 · Cited by 3,074 · see citing works
Mitochondrial free radical generation, oxidative stress, and aging
Cadenas, E., & Davies, K. J. A. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00317-8 · Cited by 3,010 · see citing works
THE MITOCHONDRIAL DEATH/LIFE REGULATOR IN APOPTOSIS AND NECROSIS
Kroemer, G., Dallaporta, B., & Resche-Rigon, M. (1998) · Annual Review of Physiology · doi:10.1146/annurev.physiol.60.1.619 · Cited by 1,971 · see citing works
Mitochondrial reactive oxygen species trigger hypoxia-induced transcription
Chandel, N. S., Maltepe, E., Goldwasser, E., Mathieu, C. E., Simon, M. C., & Schumacker, P. T. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.20.11715 · Cited by 1,926 · see citing works
Normal oxidative damage to mitochondrial and nuclear DNA is extensive.
Richter, C., Park, J. W., & Ames, B. N. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.17.6465 · Cited by 1,730 · see citing works
Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
Turrens, J. F., & Boveris, A. (1980) · Biochemical Journal · doi:10.1042/bj1910421 · Cited by 1,601 · see citing works
Self-citationThe cellular production of hydrogen peroxide
Boveris, A., Oshino, N., & Chance, B. (1972) · Biochemical Journal · doi:10.1042/bj1280617 · Cited by 1,549 · see citing works
Orr, W. C., & Sohal, R. S. (1994) · Science · doi:10.1126/science.8108730 · Cited by 1,461 · see citing works
Rubbo, H., Radí, R., Trujillo, M., Telleri, R., Kalyanaraman, B., Barnes, S., KIRK, M. C., & Freeman, B. Α. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47160-8 · Cited by 1,350 · see citing works
Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria
Turrens, J. F., Alexandre, A., & Lehninger, A. L. (1985) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(85)90293-0 · Cited by 1,214 · see citing works
Self-citationStadtman, E. R., & Levine, R. L. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06187.x · Cited by 1,037 · see citing works
Subcellular Distribution of Superoxide Dismutases (SOD) in Rat Liver
Okado‐Matsumoto, A., & Fridovich, I. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105395200 · Cited by 1,013 · see citing works
Oxygen poisoning and x-irradiation: a mechanism in common
Gerschman, R., Gilbert, D. L., Nye, S. W., Dwyer, P., & Fenn, W. O. (1954) · Science · doi:10.1126/science.119.3097.623 · Cited by 961 · cited 2× · see citing works
“Interestingly, this phenomenon was proposed to be associated with oxygen free radicals 15 years before the discovery of O2 • as a normal intracellular metabolite (Gerschman et al. 1954).”
BackgroundBABIOR, B. M., Lambeth, J. D., & Nauseef, W. M. (2002) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2642 · Cited by 911 · see citing works
Dual Function of the Selenoprotein PHGPx During Sperm Maturation
Ursini, F., Heim, S., Kieß, M., Maiorino, M., Roveri, A., Wissing, J. B., & Flohé, L. (1999) · Science · doi:10.1126/science.285.5432.1393 · Cited by 902 · see citing works
Signal transduction to hypoxia-inducible factor 1
Semenza, G. L. (2002) · Biochemical Pharmacology · doi:10.1016/s0006-2952(02)01168-1 · Cited by 860 · see citing works
Cadenas, E., Boveris, A., Ragan, C. I., & Stoppani, A. O. M. (1977) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(77)90035-2 · Cited by 855 · see citing works
The superoxide-generating NADPH oxidase: structural aspects and activation mechanism
Vignais, P. V. (2002) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-002-8520-9 · Cited by 773 · see citing works
Cai, J., & Jones, D. P. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.19.11401 · Cited by 765 · see citing works
Poderoso, J. J., Carreras, M. C., Lisdero, C., Riobó, N., Schöpfer, F., & Boveris, A. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0146 · Cited by 726 · see citing works
Differential Inhibitory Action of Nitric Oxide and Peroxynitrite on Mitochondrial Electron Transport
Cassina, A., & Radí, R. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0178 · Cited by 725 · see citing works
Finucane, D., Bossy‐Wetzel, E., Waterhouse, N. J., Cotter, T. G., & Green, D. R. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.4.2225 · Cited by 714 · see citing works
Han, D., Antunes, F., Canali, R., Rettori, D., & Cadenas, E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210269200 · Cited by 711 · see citing works
Sherer, T., Kim, J.-H., Betarbet, R. S., & Greenamyre, J. T. (2002) · Experimental Neurology · doi:10.1006/exnr.2002.8072 · Cited by 707 · see citing works
Kaur, H., & Halliwell, B. B. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00722-5 · Cited by 706 · see citing works
Kushnareva, Y., Murphy, A. N., & Andreyev, A. Y. (2002) · Biochemical Journal · doi:10.1042/bj20021121 · Cited by 677 · see citing works
Role of ubiquinone in the mitochondrial generation of hydrogen peroxide
Boveris, A., Cadenas, E., & Stoppani, A. O. M. (1976) · Biochemical Journal · doi:10.1042/bj1560435 · Cited by 655 · see citing works
Borrás, C., Sastre, J., García-Sala, D., Lloret, A., Pallardó, F. V., & Viña, J. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01356-4 · Cited by 654 · see citing works
Peroxynitrite reactions and formation in mitochondria
Radí, R., Cassina, A., Hodara, R., Quijano, C., & Castro, L. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01111-5 · Cited by 635 · see citing works
Animal models of Parkinson's disease
Betarbet, R. S., Sherer, T., & Greenamyre, J. T. (2002) · BioEssays · doi:10.1002/bies.10067 · Cited by 600 · see citing works
Trumpower, B. L. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38410-8 · Cited by 596 · see citing works
Lenaz, G. (2001) · IUBMB Life · doi:10.1080/15216540152845957 · Cited by 585 · see citing works
Detection of catalase in rat heart mitochondria.
Radi, R., Turrens, J. F., Chang, L. Y., Bush, K. M., Crapo, J. D., & Freeman, B. A. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54740-2 · Cited by 573 · see citing works
Self-citationProduction 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
Methods of Detection of Vascular Reactive Species
Tarpey, M. M., & Fridovich, I. (2001) · Circulation Research · doi:10.1161/hh1501.094365 · Cited by 552 · see citing works
Misfolded CuZnSOD and amyotrophic lateral sclerosis
Valentine, J. S., & Hart, P. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0730423100 · Cited by 546 · see citing works
Han, D., WILLIAMS, E., & Cadenas, E. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3530411 · Cited by 516 · see citing works
Shimoda‐Matsubayashi, S., Matsumine, H., Kobayashi, T., Nakagawa-Hattori, Y., Shimizu, Y., & Mizuno, Y. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.1394 · Cited by 498 · see citing works
Barja, G. (1999) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1005427919188 · Cited by 494 · see citing works
Ku, H., Brunk, U. T., & Sohal, R. S. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90165-q · Cited by 488 · see citing works
Wittenberg, B. A., & Wittenberg, J. B. (1989) · Annual Review of Physiology · doi:10.1146/annurev.ph.51.030189.004233 · Cited by 468 · see citing works
The effect of hyperoxia on superoxide production by lung submitochondrial particles
Turrens, J. F., Freeman, B. Α., Levitt, J. G., & Crapo, J. D. (1982) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(82)90518-5 · Cited by 448 · see citing works
Self-citationAmes, B. N., Shigenaga, M. K., & Hagen, T. M. (1995) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/0925-4439(95)00024-x · Cited by 391 · see citing works
Sutton, A., Khoury, H., Prip‐Buus, C., Cepanec, C., Pessayre, D., & Degoul, F. (2003) · PubMed · doi:10.1097/01.fpc.0000054067.64000.8f · Cited by 389 · see citing works
Superoxide dismutase: The first twenty years (1968–1988)
McCord, J. M., & Fridovich, I. (1988) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(88)90109-8 · Cited by 381 · see citing works
Nomura, K., Imai, H., Koumura, T., Kobayashi, T., & Nakagawa, Y. (2000) · Biochemical Journal · doi:10.1042/0264-6021:3510183 · Cited by 373 · see citing works
Protein oxidative damage is associated with life expectancy of houseflies.
Sohal, R. S., Agarwal, S., Dubey, A., & Orr, W. C. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.15.7255 · Cited by 354 · see citing works
Luminol and lucigenin as detectors for O2ṡ−
Faulkner, K. M., & Fridovich, I. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90044-u · Cited by 342 · see citing works
Selective microglial activation in the rat rotenone model of Parkinson's disease
Sherer, T., Betarbet, R. S., Kim, J.-H., & Greenamyre, J. T. (2003) · Neuroscience Letters · doi:10.1016/s0304-3940(03)00172-1 · Cited by 317 · see citing works
Genova, M. L., Ventura, B., Giuliano, G., Bovina, C., Formiggini, G., Castelli, G. P., & Lenaz, G. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02850-2 · Cited by 297 · see citing works
Nitric Oxide and Peroxynitrite Interactions with Mitochondria
Radí, R., Cassina, A., & Hodara, R. (2002) · Biological Chemistry · doi:10.1515/bc.2002.044 · Cited by 293 · see citing works
Hypoxic but not anoxic stabilization of HIF-1α requires mitochondrial reactive oxygen species
Schroedl, C., McClintock, D. S., Budinger, G. R. S., & Chandel, N. S. (2002) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00014.2002 · Cited by 266 · see citing works
Hoeberichts, F. A., & Woltering, E. J. (2002) · BioEssays · doi:10.1002/bies.10175 · Cited by 257 · see citing works
Generation of Superoxide Anion by Succinate-Cytochromec Reductase from Bovine Heart Mitochondria
Zhang, L., Yu, L. P. C., & Yu, C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.51.33972 · Cited by 253 · see citing works
Superoxide Radical and Superoxide Dismutases
Fridovich, I. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.64.1.97 · Cited by 248 · see citing works
Amyotrophic lateral sclerosis: A proposed mechanism
Okado‐Matsumoto, A., & Fridovich, I. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.132260399 · Cited by 247 · see citing works
Mitochondrial function and dysfunction in the cell: its relevance to aging and aging-related disease
Nicholls, D. G. (2002) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(02)00077-8 · Cited by 246 · see citing works
The Metabolism of Tyramine by Monoamine Oxidase A/B Causes Oxidative Damage to Mitochondrial DNA
Hauptmann, N., Grimsby, J. S., Shih, J. C., & Cadenas, E. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0510 · Cited by 221 · see citing works
Superoxide and iron: Partners in crime
Liochev, S. I., & Fridovich, I. (1999) · International Union of Biochemistry and Molecular Biology: Life · doi:10.1080/152165499307161 · Cited by 219 · see citing works
Cytochrome P450: progress and predictions
Coon, M. J., Ding, X., Pernecky, S. J., & Vaz, A. D. N. (1992) · The FASEB Journal · doi:10.1096/fasebj.6.2.1537454 · Cited by 209 · see citing works
The participation of coenzyme Q in free radical production and antioxidation
Beyer, R. E. (1990) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(90)90154-b · Cited by 209 · see citing works
Vectorial Chemiosmotic Processes
Mitchell, P. D. (1977) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.46.070177.005024 · Cited by 204 · see citing works
Barja, G., & Herrero, A. (1998) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1020592719405 · Cited by 203 · see citing works
The NADPH Oxidase of Endothelial Cells
BABIOR, B. M. (2000) · IUBMB Life · doi:10.1080/713803730 · Cited by 196 · see citing works
Circulating xanthine oxidase: potential mediator of ischemic injury
Yokoyama, Y., Beckman, J. S., Beckman, T. K., Wheat, J. K., Cash, T., Freeman, B. Α., & Parks, D. A. (1990) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.1990.258.4.g564 · Cited by 188 · see citing works
Redox regulation of manganese superoxide dismutase
Warner, B. B., Stuart, L., Gebb, S. A., & Wispé, J. R. (1996) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1996.271.1.l150 · Cited by 178 · see citing works
The Rotary Machine in the Cell, ATP Synthase
Noji, H., & Yoshida, M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.r000021200 · Cited by 175 · see citing works
Increase in manganese superoxide dismutase activity in the mouse heart after X-irradiation
Oberley, L. W., Clair, D. K. S., Autor, A. P., & Oberley, T. D. (1987) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(87)90082-8 · Cited by 168 · see citing works
Mitochondria as subcellular targets for clinically useful anthracyclines
Jung, K., & Reszka, R. C. (2001) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(01)00128-4 · Cited by 156 · see citing works
The reaction between the superoxide anion radical and cytochrome c
Butler, J., Jayson, G. G., & Swallow, A. J. (1975) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(75)90124-3 · Cited by 149 · see citing works
Problems associated with spin trapping oxygen-centered free radicals in biological systems
Pou, S., Hassett, D. J., Britigan, B. E., Cohen, M. S., & Rosen, G. M. (1989) · Analytical Biochemistry · doi:10.1016/0003-2697(89)90002-x · Cited by 148 · see citing works
Myxothiazol Induces H2O2 Production from Mitochondrial Respiratory Chain
Starkov, A. A., & Fiskum, G. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.4409 · Cited by 133 · see citing works
Thiol modulation of TNF? and IL-1 induced MnSOD gene expression and activation of NF-?B
Das, K. C., Lewis-Molock, Y., & White, C. W. (1995) · Molecular and Cellular Biochemistry · doi:10.1007/bf00929502 · Cited by 129 · see citing works
Young, T. A., Cunningham, C. C., & Bailey, S. M. (2002) · Archives of Biochemistry and Biophysics · doi:10.1016/s0003-9861(02)00338-7 · Cited by 128 · see citing works
Repair of alkylation and oxidative damage in mitochondrial DNA
LeDoux, S. P., Driggers, W. J., Hollensworth, B. S., & Wilson, G. L. (1999) · Mutation Research/DNA Repair · doi:10.1016/s0921-8777(99)00026-9 · Cited by 110 · see citing works
Lopez‐Torres, M., Pérez‐Campo, R., Rojas, C., Cadenas, S., & Barja, G. (1993) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(93)90047-u · Cited by 107 · see citing works
Drahota, Z., Chowdhury, S. R., Floryk, D., Mráček, T., Wilhelm, J., Rauchová, H., Lenaz, G., & Houštěk, J. (2002) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1015123908918 · Cited by 106 · see citing works
Lucigenin as mediator of superoxide production: revisited
Liochev, S. I., & Fridovich, I. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00121-x · Cited by 101 · see citing works
Optic Neuropathy Induced by Reductions in Mitochondrial Superoxide Dismutase
Qi, X., Lewin, A. S., Hauswirth, W. W., & Guy, J. R. (2003) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.02-0864 · Cited by 98 · see citing works
Dihydroorotate-dependent superoxide producton in rat brain and liver
Forman, H. J., & Kennedy, J. (1976) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(76)90252-6 · Cited by 95 · see citing works
Fang, J. S., & Beattie, D. S. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01328-x · Cited by 94 · see citing works
Oxygen dependence of mitochondrial nitric oxide synthase activity
Álvarez, S., Valdez, L. B., Zaobornyj, T., & Boveris, A. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00818-0 · Cited by 94 · see citing works
Hydrogen-Peroxide Metabolism in Skeletal-Muscle Mitochondria
Phung, C.-T., Ezieme, J. A., & Turrens, J. F. (1994) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1994.1528 · Cited by 89 · see citing works
Self-citationMurley, J. S., Kataoka, Y., Hallahan, D. E., Roberts, J. C., & Grdina, D. J. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00554-8 · Cited by 86 · see citing works
The two redox potentials for oxygen reduction to superoxide
Wood, P. M. (1987) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(87)90123-x · Cited by 86 · see citing works
Guidot, D. M., Repine, J. E., Kitlowski, A. D., Flores, S. C., Nelson, S. K., Wright, R. M., & McCord, J. M. (1995) · Journal of Clinical Investigation · doi:10.1172/jci118100 · Cited by 81 · see citing works
Grasbon-Frodl, E. M., Kösel, S., Rieß, O., Müller, U., Mehraein, P., & Graeber, M. B. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9998 · Cited by 79 · see citing works
Oxidative DNA damage processing and changes with aging
Bohr, V. A., Anson, R. M., Mazur, S. J., & Dianov, G. L. (1998) · Toxicology Letters · doi:10.1016/s0378-4274(98)00280-x · Cited by 72 · see citing works
Redox Regulation of the Mitochondrial Permeability Transition Pore
Chernyak, B. V. (1997) · Bioscience Reports · doi:10.1023/a:1027384628678 · Cited by 69 · see citing works
O2 sensing in hypoxic pulmonary vasoconstriction: the mitochondrial door re-opens
Waypa, G. B., & Schumacker, P. T. (2002) · Respiratory Physiology & Neurobiology · doi:10.1016/s1569-9048(02)00051-4 · Cited by 69 · see citing works
Vitamin E Oxidation in Rat Liver Mitochondria
Ham, A. L., & Liebler, D. C. (1995) · Biochemistry · doi:10.1021/bi00017a007 · Cited by 68 · see citing works
Picker, S. D., & Fridovich, I. (1984) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(84)90056-0 · Cited by 64 · see citing works
Mitochondrial lipid peroxidation by cumene hydroperoxide and its prevention by succinate
Bindoli, A., Cavallini, L., & Jocelyn, P. C. (1982) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(82)90192-x · Cited by 63 · see citing works
Superoxide from Glucose Oxidase or from Nitroblue Tetrazolium?
Liochev, S. I., & Fridovich, I. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.1247 · Cited by 62 · see citing works
Induction of TNF-α and MnSOD by endotoxin: role of membrane CD14 and Toll-like receptor-4
Tsan, M., Clark, R. N., Goyert, S. M., & White, J. E. (2001) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.2001.280.6.c1422 · Cited by 58 · see citing works
Mechanisms of hyperoxic injury to the pulmonary microcirculation.
Jd, C., Freeman, B. A., Barry, B. E., Turrens, J. F., & Young, S. (1983) · PubMed · Cited by 56 · see citing works
Self-citationHypoxia, anoxia, and O2 sensing: the search continues
Schumacker, P. T. (2002) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00205.2002 · Cited by 53 · see citing works
The cytochrome c peroxidase activity of cytochrome oxidase.
Orii, Y. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34056-0 · Cited by 51 · see citing works
Cooper, C. E., & Davies, N. A. (2000) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(00)00176-6 · Cited by 48 · see citing works
THE EFFECTS OF SEX STEROID HORMONES UPON LONGEVITY IN RATS
Asdell, S. A., Doornenbal, H., JOSHI, S. R., & Sperling, G. A. (1967) · Reproduction · doi:10.1530/jrf.0.0140113 · Cited by 48 · see citing works
Eto, Y., Kang, D., Hasegawa, E., Takeshige, K., & Minakami, S. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90493-g · Cited by 34 · see citing works
Trojanowski, J. Q. (2002) · Experimental Neurology · doi:10.1006/exnr.2002.8082 · Cited by 34 · see citing works
Evidence for superoxide radical production by a simple flavoprotein: glucose oxidase.
Al‐Bekairi, A. M., Nagi, M. N., Shoeb, H. A., & Al‐Sawaf, H. A. (1994) · PubMed · Cited by 4 · see citing works
Flagged first, then by citations
1 of the 112 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
How mitochondria produce reactive oxygen species
Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207 · see citing works
Sharma, P., Jha, A. B., Dubey, R. S., & Pessarakli, M. (2012) · Journal of Botany · doi:10.1155/2012/217037 · Cited by 5,492 · see citing works
Mitochondrial Reactive Oxygen Species (ROS) and ROS-Induced ROS Release
Zorov, D. B., Juhaszova, M., & Sollott, S. J. (2014) · Physiological Reviews · doi:10.1152/physrev.00026.2013 · Cited by 5,383 · see citing works
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 · see citing works
Ighodaro, O. M., & Akinloye, O. A. (2017) · Alexandria Journal of Medicine · doi:10.1016/j.ajme.2017.09.001 · Cited by 3,970 · see citing works
Glutathione Metabolism and Its Implications for Health
Wu, G., Lupton, J. R., Turner, N. D., Fang, Y.-Z., & Yang, S. (2004) · The Journal of Nutrition · doi:10.1093/jn/134.3.489 · Cited by 3,842 · see citing works
Cytotoxicity and Genotoxicity of Silver Nanoparticles in Human Cells
Asharani, P. V., Low, G. K. M., Hande, M. P., & Valiyaveettil, S. (2008) · ACS Nano · doi:10.1021/nn800596w · Cited by 3,714 · see citing works
Reactive oxygen species, cellular redox systems, and apoptosis
Circu, M. L., & Aw, T. Y. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.12.022 · Cited by 3,340 · see citing works
Das, K., & Roychoudhury, A. (2014) · Frontiers in Environmental Science · doi:10.3389/fenvs.2014.00053 · Cited by 3,141 · see citing works
Oxidative stress and neurodegeneration: where are we now?
Halliwell, B. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03907.x · Cited by 2,614 · see citing works
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
Hydrogen acts as a therapeutic antioxidant by selectively reducing cytotoxic oxygen radicals
Ohsawa, I., Ishikawa, M., Takahashi, K., Watanabe, M., Nishimaki, K., Yamagata, K., Katsura, K., Katayama, Y., Asoh, S., & Ohta, S. (2007) · Nature Medicine · doi:10.1038/nm1577 · Cited by 2,572 · see citing works
Skeletal muscle fatigue: cellular mechanisms
Allen, D. G., Lamb, G. D., & Westerblad, H. (2008) · Physiological Reviews · doi:10.1152/physrev.00015.2007 · Cited by 2,495 · see citing works
Reactive Species and Antioxidants. Redox Biology Is a Fundamental Theme of Aerobic Life
Halliwell, B. B. (2006) · PLANT PHYSIOLOGY · doi:10.1104/pp.106.077073 · Cited by 2,402 · see citing works
Reactive oxygen species generating systems meeting challenges of photodynamic cancer therapy
Zhou, Z., Song, J., Nie, L., & Chen, X. S. (2016) · Chemical Society Reviews · doi:10.1039/c6cs00271d · Cited by 2,104 · see citing works
Ros and ros-mediated cellular signaling
Zhang, J., Wang, X., Vikash, V., Ye, Q., Wu, D., Liu, Y., & Dong, W. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/4350965 · Cited by 1,980 · see citing works
The Role of Oxidative Stress in Parkinson's Disease
Dias, V., Junn, E., & Mouradian, M. M. (2013) · Journal of Parkinson’s Disease · doi:10.3233/jpd-130230 · Cited by 1,845 · see citing works
Mechanisms of Nanoparticle-Induced Oxidative Stress and Toxicity
Manke, A., Wang, L., & Rojanasakul, Y. (2013) · BioMed Research International · doi:10.1155/2013/942916 · Cited by 1,736 · see citing works
Melatonin as an antioxidant: under promises but over delivers
Reiter, R. J., Mayo, J. C., Tan, D. X., Sainz, R. M., Alatorre-Jiménez, M. A., & Qin, L. (2016) · Journal of Pineal Research · doi:10.1111/jpi.12360 · Cited by 1,741 · see citing works
Bhatti, J. S., Bhatti, G. K., & Reddy, P. H. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.11.010 · Cited by 1,655 · see citing works
Abiotic Stress and Reactive Oxygen Species: Generation, Signaling, and Defense Mechanisms
Sachdev, S., Ansari, S. A., Ansari, M. I., Fujita, M., & Hasanuzzaman, M. (2021) · Antioxidants · doi:10.3390/antiox10020277 · Cited by 1,590 · see citing works
Calcium and ROS: A mutual interplay
Görlach, A., Bertram, K., Hudecova, S., & Krizanova, O. (2015) · Redox Biology · doi:10.1016/j.redox.2015.08.010 · Cited by 1,546 · see citing works
Reperfusion injury and reactive oxygen species: The evolution of a concept
Granger, D. N., & Kvietys, P. R. (2015) · Redox Biology · doi:10.1016/j.redox.2015.08.020 · Cited by 1,510 · see citing works
Potential Role of Carotenoids as Antioxidants in Human Health and Disease
Fiedor, J., & Burda, K. (2014) · Nutrients · doi:10.3390/nu6020466 · Cited by 1,420 · see citing works
Mitochondrial electron transport chain, ROS generation and uncoupling (Review)
Zhao, R., Jiang, S., Zhang, L., & Yu, Z. (2019) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2019.4188 · Cited by 1,415 · see citing works
The role of oxidative stress in neurodegenerative diseases
Kim, G. H., Kim, J. E., Rhie, S. J., & Yoon, S. (2015) · Experimental Neurobiology · doi:10.5607/en.2015.24.4.325 · Cited by 1,355 · see citing works
Sena, L. A., Li, S., Jairaman, A., Prakriya, M., Ezponda, T., Hildeman, D. A., Wang, C.-R., Schumacker, P. T., Licht, J. D., Perlman, H., et al. (2013) · Immunity · doi:10.1016/j.immuni.2012.10.020 · Cited by 1,338 · see citing works
Mitochondrial metabolism of reactive oxygen species
Andreyev, A. Y., Kushnareva, Y. E., & Starkov, A. A. (2005) · Biochemistry (Moscow) · doi:10.1007/s10541-005-0102-7 · Cited by 1,336 · see citing works
Mitochondrial Oxidative Stress: Implications for Cell Death
Orrenius, S., Gogvadze, V. G., & Zhivotovsky, B. (2006) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.47.120505.105122 · Cited by 1,266 · see citing works
The sites and topology of mitochondrial superoxide production
Brand, M. D. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.01.003 · Cited by 1,217 · see citing works
T cell metabolism drives immunity
Buck, M. D., O’Sullivan, D., & Pearce, E. L. (2015) · The Journal of Experimental Medicine · doi:10.1084/jem.20151159 · Cited by 1,190 · see citing works
Calcium and apoptosis: ER-mitochondria Ca2+ transfer in the control of apoptosis
Pinton, P., Giorgi, C., Siviero, R., Zecchini, E., & Rizzuto, R. (2008) · Oncogene · doi:10.1038/onc.2008.308 · Cited by 1,145 · see citing works
Mitochondria and reactive oxygen species
Kowaltowski, A. J., de Souza-Pinto, N. C., Castilho, R. F., & Vercesi, A. E. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.05.004 · Cited by 1,162 · see citing works
Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease
Ngo, V., & Duennwald, M. L. (2022) · Antioxidants · doi:10.3390/antiox11122345 · Cited by 1,130 · see citing works
Maltais, F., Decramer, M., Casaburi, R. H., Barreiro, E., Burelle, Y., Debigaré, R., Dekhuijzen, P. N. R., Franssen, F. M. E., Gayan‐Ramirez, G., Gea, J., et al. (2014) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201402-0373st · Cited by 1,113 · see citing works
Oxidative Stress in Aging Human Skin
Rinnerthaler, M., Bischof, J., Streubel, M., Trost, A., & Richter, K. (2015) · Biomolecules · doi:10.3390/biom5020545 · Cited by 1,053 · see citing works
Brand, M. D. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.001 · Cited by 1,063 · see citing works
Small-Molecule Two-Photon Probes for Bioimaging Applications
Kim, H. M., & Cho, B. R. (2015) · Chemical Reviews · doi:10.1021/cr5004425 · Cited by 1,047 · see citing works
Oxidative Stress, Mitochondrial Dysfunction, and Aging
Cui, H., Kong, Y., & Zhang, H. (2011) · Journal of Signal Transduction · doi:10.1155/2012/646354 · Cited by 1,036 · see citing works
Role of oxidative stress in Alzheimer’s disease
HUANG, W.-J., ZHANG, X., & CHEN, W.-W. (2016) · Biomedical Reports · doi:10.3892/br.2016.630 · Cited by 1,023 · see citing works
Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes
Hamanaka, R. B., & Chandel, N. S. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.04.002 · Cited by 1,011 · see citing works
Role of oxidative stress in the pathogenesis of nonalcoholic steatohepatitis
Rolo, A. P., Teodoro, J. S., & Palmeira, C. M. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.10.003 · Cited by 955 · see citing works
Long-Lived Emissive Probes for Time-Resolved Photoluminescence Bioimaging and Biosensing
Zhang, K. Y., Yu, Q., Wei, H., Liu, S., Zhao, Q., & Huang, W. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00425 · Cited by 922 · see citing works
Puente, B. N., Kimura, W., Muralidhar, S. A., Moon, J., Amatruda, J. F., Phelps, K. L., Grinsfelder, D. B., Rothermel, B. A., Chen, R., Garcia, J. A., et al. (2014) · Cell · doi:10.1016/j.cell.2014.03.032 · Cited by 905 · see citing works
Guzy, R. D., & Schumacker, P. T. (2006) · Experimental Physiology · doi:10.1113/expphysiol.2006.033506 · Cited by 881 · see citing works
Reactive oxygen species, heat stress and oxidative-induced mitochondrial damage. A review
Slimen, I. B., Najar, T., Ghram, A., Debbabi, H., Mrad, M. B., & Abderrabba, M. (2014) · International Journal of Hyperthermia · doi:10.3109/02656736.2014.971446 · Cited by 880 · see citing works
The role of mitochondria in reactive oxygen species metabolism and signaling
Starkov, A. A. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1427.015 · Cited by 846 · see citing works
Chemical Basis of Reactive Oxygen Species Reactivity and Involvement in Neurodegenerative Diseases
Collin, F. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20102407 · Cited by 822 · see citing works
Glutathione Is a Key Player in Metal-Induced Oxidative Stress Defenses
Jozefczak, M., Remans, T., Vangronsveld, J., & Cuypers, A. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms13033145 · Cited by 820 · see citing works
ROS/oxidative stress signaling in osteoarthritis.
Lepetsos, P., & Papavassiliou, A. (2016) · Biochimica et Biophysica Acta · doi:10.1016/j.bbadis.2016.01.003 · Cited by 776 · see citing works
Endothelial dysfunction — A major mediator of diabetic vascular disease
Sena, C. M., Pereira, A. M., & Seiça, R. M. F. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.08.006 · Cited by 796 · see citing works
Kubli, D. A., & Gustafsson, Å. B. (2012) · Circulation Research · doi:10.1161/circresaha.112.265819 · Cited by 792 · 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
Mitochondria in homeostasis of reactive oxygen species in cell, tissues, and organism.
Ježek, P., & Hlavatá, L. (2005) · International Journal of Biochemistry and Cell Biology · doi:10.1016/j.biocel.2005.05.013 · Cited by 771 · see citing works
Arnold, R. S., Sun, Q., Sun, C. Q., Richards, J. C., O’Hearn, S. F., Osunkoya, A. O., Wallace, D. C., & Petros, J. A. (2012) · BioMed Research International · doi:10.1155/2013/239257 · Cited by 737 · see citing works
Hypoxic Pulmonary Vasoconstriction
Sylvester, J. T., Shimoda, L. A., Aaronson, P. I., & Ward, J. P. T. (2012) · Physiological Reviews · doi:10.1152/physrev.00041.2010 · Cited by 727 · see citing works
Extending life span by increasing oxidative stress
Ristow, M., & Schmeisser, S. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.05.010 · Cited by 718 · see citing works
Kußmaul, L., & Hirst, J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510977103 · Cited by 720 · see citing works
Free Radical Properties, Source and Targets, Antioxidant Consumption and Health
Martemucci, G., Costagliola, C., Mariano, M., D’Andrea, L., Napolitano, P., & D‘Alessandro, A. G. (2022) · Oxygen · doi:10.3390/oxygen2020006 · Cited by 781 · see citing works
Oxidative stress in angiogenesis and vascular disease
Kim, Y.-W., & Byzova, T. V. (2013) · Blood · doi:10.1182/blood-2013-09-512749 · Cited by 709 · see citing works
Relationships among smoking, oxidative stress, inflammation, macromolecular damage, and cancer
Caliri, A. W., Tommasi, S., & Nia, A. B. (2021) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2021.108365 · Cited by 689 · see citing works
Molecular Mechanisms Linking Oxidative Stress and Diabetes Mellitus
Yaribeygi, H., Sathyapalan, T., Atkin, S. L., & Sahebkar, A. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/8609213 · Cited by 689 · see citing works
Abramov, A. Y., Scorziello, A., & Duchen, M. R. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.4468-06.2007 · Cited by 686 · see citing works
Free radicals and their impact on health and antioxidant defenses: a review
Chandimali, N., Bak, S. G., Park, E. H., Lim, H. J., Won, Y., Kim, E., Park, S., & Lee, S. (2025) · Cell Death Discovery · doi:10.1038/s41420-024-02278-8 · Cited by 689 · see citing works
Newsholme, P., Haber, E. P., Hirabara, S. M., Rebelato, E. L. O., Procopio, J., Morgan, D., Oliveira‐Emilio, H. C., Carpinelli, A. R., & Curi, R. (2007) · The Journal of Physiology · doi:10.1113/jphysiol.2007.135871 · Cited by 684 · see citing works
Base excision repair of oxidative DNA damage and association with cancer and aging
Maynard, S., Schurman, S. H., Harboe, C., de Souza-Pinto, N. C., & Bohr, V. A. (2008) · Carcinogenesis · doi:10.1093/carcin/bgn250 · Cited by 685 · see citing works
Pöschl, U., & Shiraiwa, M. (2015) · Chemical Reviews · doi:10.1021/cr500487s · Cited by 674 · see citing works
Reactive oxygen species, aging and articular cartilage homeostasis
Bolduc, J. A., Collins, J. A., & Loeser, R. F. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.08.038 · Cited by 659 · see citing works
Murri, M., Luque‐Ramírez, M., Insenser, M. R., Ojeda, M. O., & Escobar-Morreale, H. F. (2013) · Human Reproduction Update · doi:10.1093/humupd/dms059 · Cited by 657 · see citing works
The Role of Oxidative Stress and Hypoxia in Pancreatic Beta-Cell Dysfunction in Diabetes Mellitus
Gerber, P. A., & Rutter, G. A. (2017) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6755 · Cited by 654 · see citing works
Mitochondria-Ros Crosstalk in the Control of Cell Death and Aging
Marchi, S., Giorgi, C., Suski, J. M., Agnoletto, C., Bononi, A., Bonora, M., Marchi, E. D., Missiroli, S., Patergnani, S., Poletti, F., et al. (2011) · Journal of Signal Transduction · doi:10.1155/2012/329635 · Cited by 639 · see citing works
Oxidative stress and mitochondrial dysfunction in sepsis
Galley, H. F. (2011) · British Journal of Anaesthesia · doi:10.1093/bja/aer093 · Cited by 609 · see citing works
Bioenergetics and the formation of mitochondrial reactive oxygen species
Ádám‐Vizi, V., & Chinopoulos, C. (2006) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2006.10.005 · Cited by 613 · see citing works
A Molecular Web: Endoplasmic Reticulum Stress, Inflammation, and Oxidative Stress
Chaudhari, N., Talwar, P., Parimisetty, A., Lefebvre d’Hellencourt, C., & Ravanan, P. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00213 · Cited by 600 · see citing works
The inflammation highway: metabolism accelerates inflammatory traffic in obesity
Johnson, A. R., Justin Milner, J., & Makowski, L. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01151.x · Cited by 603 · see citing works
Taking a good look at free radicals in the aging process
Hekimi, S., Lapointe, J., & Wen, Y. (2011) · Trends in Cell Biology · doi:10.1016/j.tcb.2011.06.008 · Cited by 606 · see citing works
Savelieff, M. G., Nam, G., Kang, J., Lee, H. J., Lee, M., & Lim, M. H. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00138 · Cited by 603 · see citing works
Hasanuzzaman, M., Bhuyan, M. H. M. B., Parvin, K., Bhuiyan, T. F., Anee, T. I., Nahar, K., Hossen, M. S., Zulfiqar, F., Alam, M. M., & Fujita, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228695 · Cited by 603 · see citing works
Acetogenins from Annonaceae: recent progress in isolation, synthesis and mechanisms of action
Bermejo, A., Figadère, B., Zafra-Polo, M. C., Barrachina, I., Estornell, E., & Cortés, D. (2005) · Natural Product Reports · doi:10.1039/b500186m · Cited by 584 · see citing works
Redox regulation of the immune response
Morris, G., Gevezova, M., Sarafian, V. S., & Maes, M. H. J. (2022) · Cellular and Molecular Immunology · doi:10.1038/s41423-022-00902-0 · Cited by 600 · see citing works
Ageing, age-related diseases and oxidative stress: What to do next?
Luo, J., Mills, K., le Cessie, S., Noordam, R., & van Heemst, D. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2019.100982 · Cited by 581 · see citing works
Bell, E. L., Klimova, T. A., Eisenbart, J., Moraes, C. T., Murphy, M. P., Budinger, G. R. S., & Chandel, N. S. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200609074 · Cited by 568 · see citing works
The neuroprotective properties of calorie restriction, the ketogenic diet, and ketone bodies
Maalouf, M., Rho, J. M., & Mattson, M. P. (2008) · Brain Research Reviews · doi:10.1016/j.brainresrev.2008.09.002 · Cited by 575 · see citing works
Wang, P., Liu, W., Han, C., Wang, S., Bai, M., & Song, C. (2023) · Journal of Integrative Plant Biology · doi:10.1111/jipb.13601 · Cited by 571 · see citing works
Kell, D. B. (2009) · BMC Medical Genomics · doi:10.1186/1755-8794-2-2 · Cited by 554 · see citing works
Bactericidal Antibiotics Induce Mitochondrial Dysfunction and Oxidative Damage in Mammalian Cells
Kalghatgi, S., Spina, C. S., Costello, J. C., Liesa, M., Morones‐Ramírez, J. R., Slomovic, S., Molina, A. J. A., Shirihai, O. S., & Collins, J. J. (2013) · Science Translational Medicine · doi:10.1126/scitranslmed.3006055 · Cited by 565 · see citing works
Marković, Z. M., Harhaji-Trajkovic, L. M., Marković, B. M. T., Kepić, D., Arsikin, K. M., Jovanović, S., Pantovic, A., Dramićanin, M. D., & Trajković, V. (2010) · Biomaterials · doi:10.1016/j.biomaterials.2010.10.030 · Cited by 560 · see citing works
The role of mitochondria in amyotrophic lateral sclerosis
Smith, E. F., Shaw, P. J., & Vos, K. J. D. (2017) · Neuroscience Letters · doi:10.1016/j.neulet.2017.06.052 · Cited by 556 · see citing works
Chen, X., Zhong, Z., Xu, Z., Chen, L., & Wang, Y. (2010) · Free Radical Research · doi:10.3109/10715761003709802 · Cited by 548 · see citing works
Metals, oxidative stress and neurodegeneration: A focus on iron, manganese and mercury
Farina, M., Ávila, D. S., da Rocha, J. B. T., & Aschner, M. (2012) · Neurochemistry International · doi:10.1016/j.neuint.2012.12.006 · Cited by 558 · see citing works
The Ins and Outs of Cathepsins: Physiological Function and Role in Disease Management
Yadati, T., Houben, T., Bitorina, A., & Shiri-Sverdlov, R. (2020) · Cells · doi:10.3390/cells9071679 · Cited by 466 · see citing works
The role of mitochondria in osteoarthritis
Blanco, F. J., Rego‐Pérez, I., & Ruíz‐Romero, C. (2011) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2010.213 · Cited by 549 · see citing works
Positive and Negative Regulation of Insulin Signaling by Reactive Oxygen and Nitrogen Species
Bashan, N., Kovsan, J., Kachko, I., Ovadia, H., & Rudich, A. (2009) · Physiological Reviews · doi:10.1152/physrev.00014.2008 · Cited by 542 · see citing works
Energy metabolism and inflammation in brain aging and Alzheimer’s disease
Yin, F., Sancheti, H., Patil, I., & Cadenas, E. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.200 · Cited by 538 · see citing works
Uncoupling proteins and the control of mitochondrial reactive oxygen species production
Mailloux, R. J., & Harper, M. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.06.022 · Cited by 534 · see citing works
Oxidative stress: the vulnerable β-cell
Lenzen, S. (2008) · Biochemical Society Transactions · doi:10.1042/bst0360343 · Cited by 535 · see citing works
Relation between mitochondrial membrane potential and ROS formation.
Suski, J., Lebiedzińska, M., Bonora, M., Pinton, P., Duszyński, J., & Wieckowski, M. (2012) · Methods in molecular biology · doi:10.1007/978-1-61779-382-0_12 · Cited by 468 · see citing works
Peripheral Chemoreceptors: Function and Plasticity of the Carotid Body
Kumar, P., & Prabhakar, N. R. (2012) · Comprehensive physiology · doi:10.1002/cphy.c100069 · Cited by 532 · see citing works
The Role of Mitochondrial Function in the Oocyte and Embryo
Dumollard, R., Duchen, M. R., & Carroll, J. (2007) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/s0070-2153(06)77002-8 · Cited by 531 · see citing works
Mitochondrial generation of free radicals and hypoxic signaling
Poyton, R. Ο., Ball, K. A., & Castello, P. R. (2009) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2009.04.001 · Cited by 525 · see citing works
- Authors
- Turrens, J. F.
- Affiliations
- University of South Alabama (US)
- Corresponding author
- Turrens, J. F.
- Venue
- The Journal of Physiology
- Publisher
- Wiley
- Published
- 2003-10-15
- Volume
- 552
- Issue
- 2
- Pages
- 335-344
- ISSN
- 0022-3751 (ISSN-L)
- PMC
- PMC2343396
- OpenAlex
- W4247088117
- Cited by
- 5,084
- References
- 112
- Citations by year
- 2026: 134 · 2025: 218 · 2024: 213 · 2023: 277 · 2022: 301 · 2021: 324 · 2020: 324 · 2019: 283 · 2018: 279 · 2017: 302 · 2016: 253 · 2015: 277 · 2014: 289 · 2013: 290 · 2012: 258
- FWCI
- 25.45
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- The Journal of Physiology (publishedVersion)
- PubMed Central (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 › Redox biology and oxidative stress
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Keywords
- reactive oxygen species, mitochondrial respiration, electron transport chain, superoxide, cytochrome c oxidase, electron leakage, antioxidant defense, oxidative damage
- MeSH terms
- Aging, Animals, Antioxidants, Humans, Mitochondria, Nitric Oxide, Oxygen, Superoxides, Xenobiotics, Apoptosis, Reactive Oxygen Species, Oxidative Stress
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
