Cited by 5,084Mitochondrial Function and PathologyRedox biology and oxidative stressAntioxidant Activity and Oxidative Stress

The DOI matches its Crossref record; 111 of the 112 references it cites were found in a registry or an index.

Mitochondrial formation of reactive oxygen species

Open access

Turrens, J. F.·2003·The Journal of Physiology

DOI 10.1113/jphysiol.2003.049478PMC PMC2343396

Open this paper in CoChat — free account

Abstract

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

Crossref · 10.1113/jphysiol.2003.049478

Cites

111 of 111 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Free Radicals in the Physiological Control of Cell Function
Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855
Cytochrome c and dATP-Dependent Formation of Apaf-1/Caspase-9 Complex Initiates an Apoptotic Protease Cascade
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
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
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
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
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
Superoxide radical and superoxide dismutases
Fridovich, I. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.000525 · Cited by 3,455
Homozygous Defect in HIV-1 Coreceptor Accounts for Resistance of Some Multiply-Exposed Individuals to HIV-1 Infection
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
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
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 1,975

Flagged first, then by citations

Show all 112 references

1 of the 112 references couldn’t be matched to a known paper.

Sorted by citations

Items 501–600 of 1,035

Mitochondrial Sirtuins and Their Relationships with Metabolic Disease and Cancer
Kumar, S., & Lombard, D. B. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6213 · Cited by 160
Redox Signaling in Plant Heat Stress Response
Fortunato, S., Lasorella, C., Dipierro, N., Vita, F., & de Pinto, M. C. (2023) · Antioxidants · doi:10.3390/antiox12030605 · Cited by 167
Hydrogen sulfide and the liver
Mani, S., Cao, W., Wu, L., & Wang, R. (2014) · Nitric Oxide · doi:10.1016/j.niox.2014.02.006 · Cited by 157
The sterile immune response during hepatic ischemia/reperfusion
van Golen, R. F., van Gulik, T. M., & Heger, M. (2012) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2012.04.006 · Cited by 163
A mitochondria-localized two-photon fluorescent probe for ratiometric imaging of hydrogen peroxide in live tissue
Masanta, G., Heo, C. H., Lim, C. S., Bae, S. K., Cho, B. R., & Kim, H. M. (2012) · Chemical Communications · doi:10.1039/c2cc00034b · Cited by 158
A Role for Mitochondrial Dysfunction in Perpetuating Radiation-Induced Genomic Instability
Kim, G. J., Fiskum, G. M., & Morgan, W. F. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-3036 · Cited by 158
Effects of ocean acidification on immune responses of the Pacific oyster Crassostrea gigas
Wang, Q., Cao, R., Ning, X., You, L., Mu, C., Wang, C., Lei, W., Cong, M., Wu, H., & Zhao, J. (2015) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2015.12.025 · Cited by 162
[Ca2+] Signaling between Mitochondria and Endoplasmic Reticulum in Neurons Is Regulated by Microtubules
Mironov, S. L., Ivannikov, M. V., & Johansson, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409819200 · Cited by 164
Mitochondrial permeability transition pore: Sensitivity to opening and mechanistic dependence on substrate availability
Briston, T., Roberts, M., Lewis, S., Powney, B., M. Staddon, J., Szabadkai, G., & Duchen, M. R. (2017) · Scientific Reports · doi:10.1038/s41598-017-10673-8 · Cited by 152
Marine invertebrate mitochondria and oxidative stress
Abele, D. (2006) · Frontiers in bioscience · doi:10.2741/2115 · Cited by 162
Brain mitochondrial dysfunction in aging, neurodegeneration and Parkinson's disease
Navarro, A. (2010) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2010.00034 · Cited by 162
Oxidative stress, cellular senescence and ageing
Pole, A., Dimri, M., & Dimri, G. P. (2016) · AIMS molecular science · doi:10.3934/molsci.2016.3.300 · Cited by 168
B vitamins attenuate the epigenetic effects of ambient fine particles in a pilot human intervention trial
Zhong, J., Karlsson, O., Wang, G., Li, J., Guo, Y., Lin, X., Zemplenyi, M., Sánchez-Guerra, M., Trevisi, L., Urch, B., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1618545114 · Cited by 159
The excessive use of antioxidant therapy: a possible cause of male infertility?
Henkel, R., Sandhu, I. S., & Agarwal, A. (2019) · Andrologia · doi:10.1111/and.13162 · Cited by 169
Role of proline and pyrroline-5-carboxylate metabolism in plant defense against invading pathogens
Qamar, A. (2015) · Frontiers in Plant Science · doi:10.3389/fpls.2015.00503 · Cited by 155
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
Methanobactin and the Link between Copper and Bacterial Methane Oxidation
DiSpirito, A. A., Semrau, J. D., Murrell, J. C., Gallagher, W. H., Dennison, C., & Vuilleumier, S. (2016) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00058-15 · Cited by 155
Astrocyte alterations in neurodegenerative pathologies and their modeling in human induced pluripotent stem cell platforms
Oksanen, M., Lehtonen, Š., Jaronen, M., Goldsteins, G., Hämäläinen, R. H., & Koıstınaho, J. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03111-7 · Cited by 166
Apoptosis effector mechanisms: A requiem performed in different keys
Hail, N., Carter, B. Z., Konopleva, M. Y., & Andreeff, M. (2006) · APOPTOSIS · doi:10.1007/s10495-006-6712-8 · Cited by 159
Sex-specific differences in mitochondria biogenesis, morphology, respiratory function, and ros homeostasis in young mouse heart and brain
Khalifa, A. R. M., Abdel‐Rahman, E. A., Mahmoud, A. M., Ali, M. H., Noureldin, M., Saber, S. H., Mohsen, M., & Ali, S. S. (2017) · Physiological Reports · doi:10.14814/phy2.13125 · Cited by 154
Hypoxia and Metabolic Properties of Hematopoietic Stem Cells
Zhang, C. C., & Sadek, H. A. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.5019 · Cited by 160
Arctigenin, a dietary phytoestrogen, induces apoptosis of estrogen receptor-negative breast cancer cells through the ROS/p38 MAPK pathway and epigenetic regulation
Hsieh, C.-J., Kuo, P., Hsu, Y.-C., Huang, Y., Tsai, E., & Hsu, Y. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.10.004 · Cited by 154
Oxygen Distribution in the Rabbit Eye and Oxygen Consumption by the Lens
Shui, Y., Fu, J.-J., Garcia, C. M., Dattilo, L. K., Rajagopal, R., McMillan, S., Mak, G., Holekamp, N. M., Lewis, A., & Beebe, D. C. (2006) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.05-1475 · Cited by 154
Opposing Effects of Glutathione Depletion and Follicle-Stimulating Hormone on Reactive Oxygen Species and Apoptosis in Cultured Preovulatory Rat Follicles
Tsai-Turton, M., & Luderer, U. (2005) · Endocrinology · doi:10.1210/en.2005-1281 · Cited by 154
Mitochondrial Oxidative Damage in Aging and Alzheimer′s Disease: Implications for Mitochondrially Targeted Antioxidant Therapeutics
Reddy, P. H. (2006) · BioMed Research International · doi:10.1155/jbb/2006/31372 · Cited by 154
The cardioprotective effects elicited by p66Shc ablation demonstrate the crucial role of mitochondrial ROS formation in ischemia/reperfusion injury
Carpi, A., Menabò, R., Kaludercic, N., Pelicci, P. G., Lisa, F. D., & Giorgio, M. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.04.001 · Cited by 152
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
Interplay Between Mitochondrial Peroxiredoxins and ROS in Cancer Development and Progression
Ismail, T., Kim, Y., Lee, H., Lee, D., & Lee, H. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20184407 · Cited by 154
Oxidative Stress, Mitochondrial Dysfunction, and Neuroprotection of Polyphenols with Respect to Resveratrol in Parkinson’s Disease
Kung, H., Lin, K.-J., Kung, C., & Lin, T. (2021) · Biomedicines · doi:10.3390/biomedicines9080918 · Cited by 165
Redox Regulation in Cancer Stem Cells
Ding, S., Li, C., Cheng, N., Cui, X., Xu, X., & Zhou, G. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/750798 · Cited by 159
Redox biology of exercise: an integrative and comparative consideration of some overlooked issues
Nikolaidis, M. G., Kyparos, A., Spanou, C., Paschalis, V., Theodorou, A. A., & Vrabas, I. S. (2012) · Journal of Experimental Biology · doi:10.1242/jeb.067470 · Cited by 152
Mitochondria: An Organelle of Bacterial Origin Controlling Inflammation
Meyer, A., LAVERNY, G., Bernardi, L., Charles, A. L., Alsaleh, G., Pottecher, J., Sibilia, J., & Gény, B. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00536 · Cited by 153
Peroxidase Activity of Human Hemoproteins: Keeping the Fire under Control
Vlasova, I. I. (2018) · Molecules · doi:10.3390/molecules23102561 · Cited by 150
Brahmi (Bacopa monnieri): An ayurvedic herb against the Alzheimer's disease
Dubey, T., & Chinnathambi, S. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.108153 · Cited by 151
Apoptosis Induced by Persistent Single-strand Breaks in Mitochondrial Genome
Tann, A. W., Boldogh, I. R., Meiß, G., Qian, W., Houten, B. V., MITRA, S. P., & Szczęsny, B. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.215715 · Cited by 155
Ionizing radiation biomarkers in epidemiological studies – An update
Hall, J. A., Jeggo, P. A., West, C., Gomolka, M., Quintens, R., Badie, C., Laurent, O., Aerts, A., Anastasov, N., Azimzadeh, O., et al. (2017) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2017.01.001 · Cited by 155
Twenty years of the ‘Preparation for Oxidative Stress’ (POS) theory: Ecophysiological advantages and molecular strategies
Giraud‐Billoud, M., Rivera‐Ingraham, G. A., Moreira, D. C., Burmester, T., Castro‐Vazquez, A., Carvajalino-Fernández, J. M., Dafré, A. L., Niu, C., Tremblay, N., Paital, B., et al. (2019) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/j.cbpa.2019.04.004 · Cited by 151
Neurobiological effects of gallic acid: current perspectives
Bhuia, M. S., Rahaman, M. M., Islam, T., Bappi, M. H., Sikder, M. I., Hossain, K. N., Akter, F., Prottay, A. A. S., Rokonuzzman, M., Gürer, E. S., et al. (2023) · Chinese Medicine · doi:10.1186/s13020-023-00735-7 · Cited by 163
Visible light driven photodynamic anticancer activity of graphene oxide/TiO2 hybrid
Hu, Z., Huang, Y., Sun, S., Guan, W., Yao, Y., Tang, P., & Li, C. (2011) · Carbon · doi:10.1016/j.carbon.2011.10.002 · Cited by 150
Detection Technologies for Reactive Oxygen Species: Fluorescence and Electrochemical Methods and Their Applications
Duanghathaipornsuk, S., Farrell, E. J., Alba‐Rubio, A. C., Zelenay, P., & Kim, D. (2021) · Biosensors · doi:10.3390/bios11020030 · Cited by 149
Epigallocatechin Gallate Is the Most Effective Catechin Against Antioxidant Stress via Hydrogen Peroxide and Radical Scavenging Activity
He, J., Xu, L., Yang, L. J., & Wang, X. (2018) · Medical Science Monitor · doi:10.12659/msm.911175 · Cited by 148
Defenses against Oxidative Stress in Neisseria gonorrhoeae : a System Tailored for a Challenging Environment
Seib, K. L., Wu, H., Kidd, S. P., Apicella, M. A., Jennings, M. P., & McEwan, A. G. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00044-05 · Cited by 143
Oxidative Stress in Chagas Disease
Gupta, S., Wen, J.-J., & Garg, N. J. (2009) · Interdisciplinary Perspectives on Infectious Diseases · doi:10.1155/2009/190354 · Cited by 148
Small Molecule Mitochondrial Uncouplers and Their Therapeutic Potential
Childress, E. S., Alexopoulos, S. J., Hoehn, K. L., & Santos, W. L. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01182 · Cited by 148
Does the Glucose-Dependent Insulin Secretion Mechanism Itself Cause Oxidative Stress in Pancreatic β-Cells?
Fridlyand, L. E., & Philipson, L. H. (2004) · Diabetes · doi:10.2337/diabetes.53.8.1942 · Cited by 147
Mitochondria as a source and target of lipid peroxidation products in healthy and diseased heart
Anderson, E. J., Katunga, L. A., & Willis, M. S. (2011) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/j.1440-1681.2011.05641.x · Cited by 146
An Overview of Seasonal Changes in Oxidative Stress and Antioxidant Defence Parameters in Some Invertebrate and Vertebrate Species
Chainy, G. B. N., Paital, B., & Dandapat, J. (2016) · Scientifica · doi:10.1155/2016/6126570 · Cited by 146
Nanopreparations for mitochondria targeting drug delivery system: Current strategies and future prospective
Wang, Z., Guo, W., Kuang, X., Hou, S., & Liu, H. (2017) · Asian Journal of Pharmaceutical Sciences · doi:10.1016/j.ajps.2017.05.006 · Cited by 150
Early Events in Plant Abiotic Stress Signaling: Interplay Between Calcium, Reactive Oxygen Species and Phytohormones
Mohanta, 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
Redox-dependent gating of VDAC by mitoNEET
Lipper, C. H., Stofleth, J. T., Bai, F., Sohn, Y., Roy, S., Mittler, R., Nechushtai, R., Onuchic, J. N., & Jennings, P. A. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1908271116 · Cited by 147
Adaptive Responses to Hypoxia and/or Hyperoxia in Humans
Burtscher, J., Mallet, R. T., Pialoux, V., Millet, G. P., & Burtscher, M. (2022) · Antioxidants and Redox Signaling · doi:10.1089/ars.2021.0280 · Cited by 182
Polyol pathway and redox balance in diabetes
Garg, S. S., & Gupta, J. (2022) · Pharmacological Research · doi:10.1016/j.phrs.2022.106326 · Cited by 158
Regulation of free radical outflow from an isolated muscle bed in exercising humans
Bailey, D. M., Young, I. S., McEneny, J., Lawrenson, L., Kim, J., Barden, J., & Richardson, R. S. (2004) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00148.2004 · Cited by 146
Glutathione Redox State Regulates Mitochondrial Reactive OxygenProduction
Shen, D., Dalton, T. P., Nebert, D. W., & Shertzer, H. G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500095200 · Cited by 147
Bench-to-bedside review: Targeting antioxidants to mitochondria in sepsis
Galley, H. F. (2010) · Critical Care · doi:10.1186/cc9098 · Cited by 148
Controlling Redox Status for Stem Cell Survival, Expansion, and Differentiation
Sart, S., Song, L., & Li, Y. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/105135 · Cited by 143
Mitochondrial ROS and involvement of Bcl-2 as a mitochondrial ROS regulator
Chong, S. J. F., Low, I. C. C., & Pervaiz, S. (2014) · Mitochondrion · doi:10.1016/j.mito.2014.06.002 · Cited by 142
Alzheimer's disease: Effects of β-amyloid on mitochondria
Tillement, L., Lecanu, L., & Papadopoulos, V. (2010) · Mitochondrion · doi:10.1016/j.mito.2010.08.009 · Cited by 148
Mitochondrial contributions to vascular endothelial dysfunction, arterial stiffness, and cardiovascular diseases
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
Oxidative genome damage and its repair: implications in aging and neurodegenerative diseases
Hegde, M. L., Mantha, A. K., Hazra, T. K., Bhakat, K. K., Mitra, S., & Szczesny, B. (2012) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2012.01.005 · Cited by 141
Species- and tissue-specific relationships between mitochondrial permeability transition and generation of ROS in brain and liver mitochondria of rats and mice
Panov, A., Dikalov, S., Shalbuyeva, N., Hemendinger, R., Greenamyre, J. T., & Rosenfeld, J. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00202.2006 · Cited by 141
The Role of Reactive Species on Innate Immunity
Andrés, C., Pérez de la Lastra, J., Juan, C., Plou, F., & Pérez-Lebeña, E. (2022) · Vaccines · doi:10.3390/vaccines10101735 · Cited by 142
Atherogenic dyslipidemia and oxidative stress: a new look
Rizzo, M., Kotur‐Stevuljević, J., Berneis, K. K., Spinas, G. A., Rini, G. B., Jelić‐Ivanović, Z., Spasojević‐Kalimanovska, V., & Vekić, J. (2009) · Translational research · doi:10.1016/j.trsl.2009.01.008 · Cited by 143
Mitochondrial function and myocardial aging. A critical analysis of the role of permeability transition
DILISA, F., & BERNARDI, P. (2005) · Cardiovascular Research · doi:10.1016/j.cardiores.2005.02.009 · Cited by 139
Molecular Hydrogen: New Antioxidant and Anti-inflammatory Therapy for Rheumatoid Arthritis and Related Diseases
Ishibashi, T. (2013) · Current Pharmaceutical Design · doi:10.2174/13816128113199990507 · Cited by 141
Calcium signals and mitochondria at fertilisation
Dumollard, R., Duchen, M. R., & Sardet, C. (2006) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2006.02.009 · Cited by 141
Glucose Withdrawal Induces Oxidative Stress followed by Apoptosis in Glioblastoma Cells but not in Normal Human Astrocytes
Jelluma, N., Yang, X., Stokoe, D., Evan, G. I., Dansen, T. B., & Haas-Kogan, D. A. (2006) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-05-0061 · Cited by 144
Mitochondrial complex I deactivation is related to superoxide production in acute hypoxia
Hernansanz‐Agustín, P., Ramos, E. M., Navarro, E., Parada, E., Sánchez-López, N., Peláez-Aguado, L., Cabrera-García, J. D., Tello, D., Buendía, I., Marina, A., et al. (2017) · Redox Biology · doi:10.1016/j.redox.2017.04.025 · Cited by 141
Reactive Oxygen Species Interact With NLRP3 Inflammasomes and Are Involved in the Inflammation of Sepsis: From Mechanism to Treatment of Progression
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
Heat stress upregulates chaperone heat shock protein 70 and antioxidant manganese superoxide dismutase through reactive oxygen species (ROS), p38MAPK, and Akt
Mustafi, S. B., Chakraborty, P. K., Sharma, R. D., & Raha, S. (2009) · Cell Stress and Chaperones · doi:10.1007/s12192-009-0109-x · Cited by 140
Water-soluble fullerenes for medical applications
Rašović, I. (2016) · Materials Science and Technology · doi:10.1080/02670836.2016.1198114 · Cited by 140
Mitochondrial calcium transport and the redox nature of the calcium-induced membrane permeability transition
Vercesi, A. E., Castilho, R. F., Kowaltowski, A. J., Oliveira, H. C. F., de Souza-Pinto, N. C., Figueira, T. R., & Busanello, E. N. B. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.08.034 · Cited by 146
Dancing with reactive oxygen species generation and elimination in nanotheranostics for disease treatment
Zhou, Z., Ni, K., Deng, H., & Chen, X. S. (2020) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2020.06.006 · Cited by 139
Mitochondrial dynamics in Parkinson's disease
Laar, V. S. V., & Berman, S. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.03.019 · Cited by 141
Blockade of Electron Transport before Cardiac Ischemia with the Reversible Inhibitor Amobarbital Protects Rat Heart Mitochondria
Chen, Q., Hoppel, C. L., & Lesnefsky, E. J. (2005) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.105.091702 · Cited by 140
Mitochondria and arrhythmias
Yang, K., Bonini, M. G., & Dudley, S. C. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.03.033 · Cited by 139
Effect of elevated oxygen concentration on bacteria, yeasts, and cells propagated for production of biological compounds
Baez, A., & Shiloach, J. (2014) · Microbial Cell Factories · doi:10.1186/s12934-014-0181-5 · Cited by 139
Rapid dissolution of ZnO nanocrystals in acidic cancer microenvironment leading to preferential apoptosis
Sasidharan, A., Chandran, P., Menon, D., Raman, S., Nair, S. V., & Koyakutty, M. (2011) · Nanoscale · doi:10.1039/c1nr10272a · Cited by 140
Inhibition of Mitochondrial Complex I Leads to Decreased Motility and Membrane Integrity Related to Increased Hydrogen Peroxide and Reduced ATP Production, while the Inhibition of Glycolysis Has Less Impact on Sperm Motility
Plaza‐Dávila, M., Muñoz, P. M., Tapia, J. A., Ortega‐Ferrusola, C., da Silva, C. B., & Peña, F. J. (2015) · PLoS ONE · doi:10.1371/journal.pone.0138777 · Cited by 139
Mitochondria, Estrogen and Female Brain Aging
Lejri, I., Grimm, A., & Eckert, A. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00124 · Cited by 144
The Role of Reactive Oxygen Species in Acute Myeloid Leukaemia
Sillar, J. R., Germon, Z. P., Iuliis, G. N. D., & Dun, M. D. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20236003 · Cited by 139
Reactive oxygen species, antioxidants and fish mitochondria
Filho, D. W. (2006) · Frontiers in bioscience · doi:10.2741/2141 · Cited by 141
Decreased complex II respiration and HNE-modified SDH subunit in diabetic heart
Lashin, O., Szweda, P. A., Szweda, L. I., & Romani, A. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.10.040 · Cited by 139
Neuroprotective effects of gallic acid against hypoxia/reoxygenation-induced mitochondrial dysfunctions in vitro and cerebral ischemia/reperfusion injury in vivo
Sun, J., Li, Y., Ding, Y., Wang, J., Geng, J., Yang, H., Ren, J., Tang, J., & Gao, J. (2014) · Brain Research · doi:10.1016/j.brainres.2014.09.039 · Cited by 138
The Effect oftert-Butyl Hydroperoxide-Induced Oxidative Stress on Lean and Steatotic Rat HepatocytesIn Vitro
Kučera, O., Endlicher, R., Roušar, T., Lotková, H., Garnol, T., Drahota, Z., & Červinková, Z. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/752506 · Cited by 145
An update on oxidative stress-mediated organ pathophysiology
Rashid, K., Sinha, K., & Sil, P. C. (2013) · Food and Chemical Toxicology · doi:10.1016/j.fct.2013.09.026 · Cited by 142
The Behavioral Sequelae of Social Defeat Require Microglia and Are Driven by Oxidative Stress in Mice
Lehmann, M. L., Weigel, T. K., Poffenberger, C. N., & Herkenham, M. (2019) · The Journal of Neuroscience · doi:10.1523/jneurosci.0184-19.2019 · Cited by 138
Acute hypoxia produces a superoxide burst in cells
Hernansanz‐Agustín, P., Izquierdo-Álvarez, A., Sánchez-Gómez, F. J., Ramos, E. M., Villa-Piña, T., Lamas, S., Bogdanova, A. Y., & Martı́nez-Ruiz, A. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.03.011 · Cited by 137
Redox Control of Leukemia: From Molecular Mechanisms to Therapeutic Opportunities
Irwin, M. E., Valle, N. R.-D., & Chandra, J. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4258 · Cited by 146
Effect of physical training on mitochondrial respiration and reactive oxygen species release in skeletal muscle in patients with obesity and type 2 diabetes
Hey‐Mogensen, M., Højlund, K., Vind, B. F., Wang, L., Dela, F., Beck‐Nielsen, H., Fernström, M., & Sahlin, K. (2010) · Diabetologia · doi:10.1007/s00125-010-1813-x · Cited by 138
NADPH oxidase plays a central role in cone cell death in retinitis pigmentosa
Usui, S., Oveson, B. C., Lee, S. Y., Jo, Y., Yoshida, T., Miki, A., Miki, K., Iwase, T., Lu, L., & Campochiaro, P. A. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06195.x · Cited by 138
Mitochondrial ATP is required for the maintenance of membrane integrity in stallion spermatozoa, whereas motility requires both glycolysis and oxidative phosphorylation
Davila, M. P., Muñoz, P. M., Bolaños, J. M. G., Stout, T. A. E., Gadella, B. M., Tapia, J. A., da Silva, C. B., Ortega‐Ferrusola, C., & Peña, F. J. (2016) · Reproduction · doi:10.1530/rep-16-0409 · Cited by 137
Oxidative stress and altered mitochondrial protein expression in the absence of amyloid-β and tau pathology in iPSC-derived neurons from sporadic Alzheimer's disease patients
Birnbaum, J. H., Wanner, D., Gietl, A. F., Saake, A., Kündig, T. M., Hock, C., Nitsch, R. M., & Tackenberg, C. (2018) · Stem Cell Research · doi:10.1016/j.scr.2018.01.019 · Cited by 135
N-Acetylcysteine improves mitochondrial function and ameliorates behavioral deficits in the R6/1 mouse model of Huntington's disease
Wright, D. J., Renoir, T., Smith, Z. M., Frazier, A. E., Francis, P. S., Thorburn, D. R., McGee, S. L., Hannan, A. J., & Gray, L. J. (2015) · Translational Psychiatry · doi:10.1038/tp.2014.131 · Cited by 137
Cell Biology of Coral Bleaching
Oakley, C. A., & Davy, S. K. (2018) · Ecological studies · doi:10.1007/978-3-319-75393-5_8 · Cited by 136
The versatility of mitochondrial calcium signals: From stimulation of cell metabolism to induction of cell death
Rimessi, A., Giorgi, C., Pinton, P., & Rizzuto, R. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.05.449 · Cited by 140
Reactive Metabolites and AGE/RAGE-Mediated Cellular Dysfunction Affect the Aging Process – A Mini-Review
Fleming, T. H., Humpert, P. M., Nawroth, P. P., & Bierhaus, A. (2010) · Gerontology · doi:10.1159/000322087 · Cited by 139
Chemical diversity of biologically active metabolites in the sclerotia of Inonotus obliquus and submerged culture strategies for up-regulating their production
Zheng, W., Miao, K., Liu, Y., Zhao, Y., Zhang, M., Pan, S., & Dai, Y. (2010) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-010-2682-4 · Cited by 136
A systematic review of air pollution as a risk factor for cardiovascular disease in South Asia: Limited evidence from India and Pakistan
Yamamoto, S. S., Phalkey, R. K., & Malik, A. A. (2013) · International Journal of Hygiene and Environmental Health · doi:10.1016/j.ijheh.2013.08.003 · Cited by 138

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)
DOI: 10.1113/jphysiol.2003.049478
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
Licence: doi.wiley.com/10.1002/tdm_license_1 (tdm, 4339 d)
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 (medical) › 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

Mitochondrial formation of reactive oxygen species

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks