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The Role of Mitochondria in Reactive Oxygen Species Metabolism and Signaling
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Oxidative stress is considered a major contributor to the etiology of both “normal” senescence and severe pathologies with serious public health implications. Several cellular sources, including mitochondria, are known to produce significant amounts of reactive oxygen species (ROS) that may contribute to intracellular oxidative stress. Mitochondria possess at least 10 known sites that are capable of generating ROS, but they also feature a sophisticated multilayered ROS defense system that is much less studied. This review summarizes the current knowledge about major components involved in mitochondrial ROS metabolism and factors that regulate ROS generation and removal at the level of mitochondria. An integrative systemic approach is applied to analysis of mitochondrial ROS metabolism, which is “dissected” into ROS generation, ROS emission, and ROS scavenging. The in vitro ROS‐producing capacity of several mitochondrial sites is compared in the metabolic context and the role of mitochondria in ROS‐dependent intracellular signaling is discussed.
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“The succinate concentration in different tissues and mitochondria is in the submillimolar range under aerobic conditions [22,72,73], indicating that complex II is not working at maximal velocity under 'standard conditions'.”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [22]
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“The highly effective mitochondrial antioxidative defense system encompasses the thioredoxin/peroxiredoxin system as well as the glutathione/glutathione peroxidase system (overview in [22,117]).”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [22]
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Cites
Free radicals and antioxidants in normal physiological functions and human disease
Valko, M., Leibfritz, D., Moncol, J., Cronin, M. T. D., Mazur, M., & Telser, J. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2006.07.001 · Cited by 14,269
McCord, J. M., & Fridovich, I. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63504-5 · Cited by 12,952
Free Radicals in the Physiological Control of Cell Function
Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855
Mitochondrial Dysfunction and Oxidative Stress in Neurodegenerative Diseases
Lin, M. T., & Beal, M. F. (2006) · Nature · doi:10.1038/nature05292 · Cited by 6,455
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
Mitochondrial formation of reactive oxygen species
Turrens, J. F. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.049478 · Cited by 5,084
Boveris, A., & Chance, B. (1973) · Biochemical Journal · doi:10.1042/bj1340707 · Cited by 2,626
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
Role of reactive oxygen species in the pathophysiology of human reproduction.
Agarwal, A., Saleh, R., & Bedaiwy, M. (2003) · Fertility and Sterility · doi:10.1016/s0015-0282(02)04948-8 · Cited by 1,578
Oxygen, oxidative stress, hypoxia, and heart failure
Giordano, F. J. (2005) · Journal of Clinical Investigation · doi:10.1172/jci24408 · Cited by 1,515
Research works printed but not linked: 2
- 10.1172/JCI200524408 · DOI
- 10.1111/j.1469-7793.2003.00335.x · DOI · Paper page
Cited by
Sorted by citations
Items 201–300 of 847
Paoli, A., & Cerullo, G. (2023) · Antioxidants · doi:10.3390/antiox12051065 · Cited by 79
Zaza, G., Granata, S., Masola, V., Rugiu, C., Fantin, F., Gesualdo, L., Schena, F. P., & Lupo, A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0077847 · Cited by 75
Klinger, H., Rinnerthaler, M., Lam, Y. T., Laun, P., Heeren, G., Klocker, A., Simon‐Nobbe, B., Dickinson, J. R., Dawes, I. W., & Breitenbach, M. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.03.016 · Cited by 75
Mitochondrial Defects Confer Tolerance against Cellulose Deficiency
Hu, Z., Vanderhaeghen, R., Cools, T., Wang, Y., Clercq, I. D., Leroux, O., Nguyen, L., Belt, K., Millar, A. H., Audenaert, D., et al. (2016) · The Plant Cell · doi:10.1105/tpc.16.00540 · Cited by 74
Impairment of mitochondrial function by particulate matter: Implications for the brain
Chew, S., Kołosowska, N., Saveleva, L., Malm, T., & Kanninen, K. M. (2020) · Neurochemistry International · doi:10.1016/j.neuint.2020.104694 · Cited by 77
The Metabolic Syndrome, a Human Disease
Alemany, M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25042251 · Cited by 86
Ergothioneine and its prospects as an anti-ageing compound
Apparoo, Y., Phan, C., Kuppusamy, U. R., & Sabaratnam, V. (2022) · Experimental Gerontology · doi:10.1016/j.exger.2022.111982 · Cited by 73
von Stockum, S., Giorgio, V., Trevisan, E., Lippe, G., Glick, G. D., Forte, M. A., Da‐Ré, C., Checchetto, V., Mazzotta, G. M., Costa, R., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.c114.629766 · Cited by 75
Understanding Long COVID; Mitochondrial Health and Adaptation—Old Pathways, New Problems
Nunn, A. V. W., Guy, G. W., Brysch, W., & Bell, J. D. (2022) · Biomedicines · doi:10.3390/biomedicines10123113 · Cited by 74
Sendtner, N., Seitz, R., Brandl, N., Müller, M., & Gülow, K. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262010240 · Cited by 81
Hroudová, J., Singh, N., Fišar, Z., & Ghosh, K. K. (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.03.084 · Cited by 71
Rahman, M. A., Rahman, M. H., Biswas, P., Hossain, M. S., Islam, R., Hannan, M. A., Uddin, M. J., & Rhim, H. (2020) · Antioxidants · doi:10.3390/antiox10010023 · Cited by 71
Neri, M., Riezzo, I., Pomara, C., Schiavone, S., & Turillazzi, E. (2016) · Mediators of Inflammation · doi:10.1155/2016/3423450 · Cited by 71
Ma, X., Luo, Q., Zhu, H., Liu, X., Dong, Z., Zhang, K., Zou, Y., Wu, J., Ge, J., & Sun, A. (2018) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.13677 · Cited by 69
Recent advances in the pathogenesis of microvascular complications in diabetes
Park, S., Kang, H., Jeon, J., Kim, M., & Lee, I. (2019) · Archives of Pharmacal Research · doi:10.1007/s12272-019-01130-3 · Cited by 69
Novel Therapeutic Strategies for Traumatic Brain Injury: Acute Antioxidant Reinforcement
Fernández-Gajardo, R., Matamala, J. M., Carrasco, R. A., Gutiérrez, R., Melo, R., & Rodrigo, R. (2014) · CNS Drugs · doi:10.1007/s40263-013-0138-y · Cited by 69
Mitochondrial flashes: new insights into mitochondrial ROS signalling and beyond
Hou, T., Wang, X., Ma, Q., & Cheng, H. (2014) · The Journal of Physiology · doi:10.1113/jphysiol.2014.275735 · Cited by 70
Houghton, M. J., Kerimi, A., Tumova, S., Boyle, J. P., & Williamson, G. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.09.037 · Cited by 68
Pathak, T., Guéguinou, M., Walter, V., Delierneux, C., Johnson, M. T., Zhang, X., Xin, P., Yoast, R. E., Emrich, S. M., Yochum, G. S., et al. (2020) · eLife · doi:10.7554/elife.59686 · Cited by 72
Uusitalo, L. M., & Hempel, N. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms130910660 · Cited by 68
Muller, B., Lewis, N., Adeniyi, T., Leese, H. J., Brison, D. R., & Sturmey, R. G. (2019) · Scientific Reports · doi:10.1038/s41598-019-53066-9 · Cited by 67
Mitochondrially-targeted treatment strategies
Bozi, L. H. M., Campos, J. C., Zambelli, V. O., Ferreira, N. D., & Ferreira, J. C. B. (2019) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2019.100836 · Cited by 67
Slepchenko, K. G., Lu, Q., & Li, Y. V. (2017) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00048.2017 · Cited by 66
Hypoxic pulmonary vasoconstriction: mechanisms of oxygen-sensing
Evans, A. M., Hardie, D. G., Peers, C., & Mahmoud, A. D. (2010) · Current Opinion in Anaesthesiology · doi:10.1097/aco.0b013e3283421201 · Cited by 65
Dröse, S., Bleier, L., & Brandt, U. (2011) · Molecular Pharmacology · doi:10.1124/mol.110.070342 · Cited by 64
Darwesh, A. M., Bassiouni, W., Sosnowski, D. K., & Seubert, J. M. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107703 · Cited by 66
The Biphasic Effect of Flavonoids on Oxidative Stress and Cell Proliferation in Breast Cancer Cells
Xi, X., Wang, J., Qin, Y., You, Y., Huang, W., & Zhan, J. (2022) · Antioxidants · doi:10.3390/antiox11040622 · Cited by 64
Ambrus, A., Nemeria, N. S., Törőcsik, B., Tretter, L., Nilsson, M., Jordan, F., & Ádám‐Vizi, V. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.10.001 · Cited by 64
Partitioning of superoxide and hydrogen peroxide production by mitochondrial respiratory complex I
Grivennikova, V. G., & Vinogradov, A. D. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.01.002 · Cited by 64
Unraveling the neurotoxicity of titanium dioxide nanoparticles: focusing on molecular mechanisms
Song, B., Zhang, Y., Liu, J., Feng, X., Zhou, T., & Shao, L. (2016) · Beilstein Journal of Nanotechnology · doi:10.3762/bjnano.7.57 · Cited by 67
Mitochondrial Metabolism in Major Neurological Diseases
Zhou, Z., Austin, G. L., Young, L. E. A., Johnson, L. A., & Sun, R. C. (2018) · Cells · doi:10.3390/cells7120229 · Cited by 67
Mitochondrial-Targeted Catalase
Dai, D., Chiao, Y. A., Martin, G. M., Marcinek, D. J., Basisty, N., Quarles, E. K., & Rabinovitch, P. S. (2017) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2016.12.015 · Cited by 65
Kôrge, P., John, S., Calmettes, G., & Weiss, J. N. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.768325 · Cited by 63
Ma, J.-M., Yin, G., Lu, Z., Xie, P., Zhou, H., Liu, J., & Yu, L. (2018) · Phytotherapy Research · doi:10.1002/ptr.6108 · Cited by 63
Chen, Y., Gu, Y., Zhao, H., & Zhou, Y. (2020) · Poultry Science · doi:10.1016/j.psj.2020.12.017 · Cited by 62
A paradoxical role of reactive oxygen species in cancer signaling pathway: Physiology and pathology
Ramalingam, V., & Rajaram, R. (2020) · Process Biochemistry · doi:10.1016/j.procbio.2020.09.032 · Cited by 61
Kurth, D. G., Belfiore, C., Gorriti, M. F., Cortez, N., Farı́as, M. E., & Albarracín, V. H. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00328 · Cited by 58
Wang, Y., Yu, H., Pu, X., & Du, G. (2013) · Molecules · doi:10.3390/molecules181214726 · Cited by 61
The hypoxia-tolerant vertebrate brain: Arresting synaptic activity
Buck, L. T., & Pamenter, M. E. (2017) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2017.11.015 · Cited by 64
Chang, A. L., & Doering, T. L. (2018) · mBio · doi:10.1128/mbio.01375-18 · Cited by 58
Targeting a mitochondrial potassium channel to fight cancer
Leanza, L., Venturini, E., Kadow, S., Carpinteiro, A., Gulbins, E., & Becker, K. A. (2014) · Cell Calcium · doi:10.1016/j.ceca.2014.09.006 · Cited by 60
Slade, L., Chalker, J., Kuksal, N., Young, A., Gardiner, D., & Mailloux, R. J. (2017) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2017.05.010 · Cited by 60
Diomede, F., Marconi, G. D., Guarnieri, S., D’Attilio, M., Cavalcanti, M. F. X. B., Mariggiò, M. A., Pizzicannella, J., & Trubiani, O. (2019) · Materials · doi:10.3390/ma13010130 · Cited by 60
Amyotrophic lateral sclerosis pathogenesis: a journey through the secretory pathway
Nassif, M., Matus, S., Castillo, K., & Hetz, C. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2991 · Cited by 60
Fakhri, S., Gravandi, M. M., Abdian, S., Akkol, E. K., Farzaei, M. H., & Sobarzo‐Sánchez, E. (2021) · Molecules · doi:10.3390/molecules26195985 · Cited by 60
Sampath, H., Batra, A. K., Vartanian, V. L., Carmical, J. R., Prusak, D. J., King, I. B., Lowell, B., Earley, L. F., Wood, T. G., Marks, D. L., et al. (2011) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00387.2010 · Cited by 59
Ferroptosis in cancer: revealing the multifaceted functions of mitochondria
Ding, X., Cui, L., Mi, Y., Hu, J., Cai, Z., Tang, Q., Yang, L., Yang, Z., Wang, Q., Li, H., et al. (2025) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-025-05812-8 · Cited by 64
Wang, Q., Chen, W., Bai, L., Chen, W., Padilla, M. T., Lin, A. S., Shi, S., Wang, X., & Lin, Y. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.526152 · Cited by 57
Gómez‐Serrano, M., Camafeita, E., López, J. A., Rubio, M. Á., Lesmes, I. B., García‐Consuegra, I., García‐Santos, E., Lago, J., Sánchez-Pernaute, A., Torres, A., et al. (2016) · Redox Biology · doi:10.1016/j.redox.2016.12.013 · Cited by 60
Mitochondrial dynamics and neuronal fate in Parkinson's disease
Santos, D., & Cardoso, S. M. (2012) · Mitochondrion · doi:10.1016/j.mito.2012.05.002 · Cited by 60
Fusarium mycotoxins: The major food contaminants
Qu, Z., Ren, X., Du, Z., Hou, J., Li, Y., Yao, Y., & An, Y. (2024) · mLife · doi:10.1002/mlf2.12112 · Cited by 56
Romero-Morales, A. I., Robertson, G. L., Rastogi, A., Rasmussen, M. L., Temuri, H., McElroy, G. S., Chakrabarty, R. P., Hsu, L., Almonacid, P. M., Millis, B. A., et al. (2022) · Development · doi:10.1242/dev.199914 · Cited by 58
Molecular Mechanisms of Retinal Pigment Epithelium Dysfunction in Age-Related Macular Degeneration
Kim, J., Lee, Y. J., & Won, J. Y. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222212298 · Cited by 61
Kilbaugh, T. J., Sutton, R. M., Karlsson, M., Hansson, M. J., Naim, M. Y., Morgan, R. W., Bratinov, G. D., Lampe, J. W., Nadkarni, V., Becker, L. B., et al. (2015) · Journal of the American Heart Association · doi:10.1161/jaha.115.002232 · Cited by 55
Zhou, J., Zhang, Y., Li, S., Zhou, Q., Lu, Y., Shi, J., Liu, J., Wu, Q., & Zhou, S. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110351 · Cited by 55
Nakamura, S., Tanaka, J., Imada, T., Shimoda, H., & Tsubota, K. (2014) · Journal of Functional Foods · doi:10.1016/j.jff.2014.06.027 · Cited by 54
Ambrus, A., & Ádám‐Vizi, V. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.05.018 · Cited by 54
Wang, T., Huang, X., Jiang, X., Hu, M., Huang, W., & Wang, Y. (2019) · Aquatic Toxicology · doi:10.1016/j.aquatox.2019.04.012 · Cited by 54
Mitochondria as intracellular signalling organelles. An update
Popov, L. (2023) · Cellular Signalling · doi:10.1016/j.cellsig.2023.110794 · Cited by 57
Kaur, A., Brigden, K. W. L., Cashman, T. F., Fraser, S. T., & New, E. J. (2015) · Organic & Biomolecular Chemistry · doi:10.1039/c5ob00928f · Cited by 52
Rajak, P., Dutta, M., Khatun, S., Mandi, M., & Roy, S. (2016) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2016.09.067 · Cited by 52
Ye, Z., Zhang, H., Kong, F., Lan, J., Yi, S., Jia, W., Zheng, S. S., Guo, Y., & Zhan, X. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/9259297 · Cited by 52
Mitochondrial activity in gametes and transmission of viable mtDNA
Milani, L., & Ghiselli, F. (2015) · Biology Direct · doi:10.1186/s13062-015-0057-6 · Cited by 53
Yan, W., Kang, Y., Ji, X., Li, S., Li, Y., Zhang, G., Cui, H., & Shi, G. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/1202459 · Cited by 50
Redox control of non-shivering thermogenesis
Lettieri‐Barbato, D. (2019) · Molecular Metabolism · doi:10.1016/j.molmet.2019.04.002 · Cited by 52
The effect of heat stress on hematological parameters and oxidative stress among bakery workers
Gharibi, V., Khanjani, N., Heidari, H., Ebrahimi, M. H., & Hosseinabadi, M. B. (2020) · Toxicology and Industrial Health · doi:10.1177/0748233719899824 · Cited by 50
Sahni, P. V., Zhang, J., Sosunov, S. A., Galkin, A. S., Niatsetskaya, Z. V., Starkov, A. A., Brookes, P. S., & Ten, V. S. (2017) · Pediatric Research · doi:10.1038/pr.2017.277 · Cited by 50
Self-citationModica-Napolitano, J. S., Bharath, L. P., Hanlon, A. J., & Hurley, L. D. (2019) · Biomolecules · doi:10.3390/biom9080298 · Cited by 52
Wu, F., Wang, J., Wang, Y., Kwok, T.-T., Kong, S., & Wong, C. (2009) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2009.05.008 · Cited by 50
Heat stress causes dysfunctional autophagy in oxidative skeletal muscle
Brownstein, A. J., Ganesan, S., Summers, C. M., Pearce, S., Hale, B. J., Ross, J. W., Gabler, N. K., Seibert, J. T., Rhoads, R. P., Baumgard, L. H., et al. (2017) · Physiological Reports · doi:10.14814/phy2.13317 · Cited by 48
Is there a room for GABA in ROS and RNS signalling?
Bor, M., & Türkan, İ. (2019) · Environmental and Experimental Botany · doi:10.1016/j.envexpbot.2019.02.015 · Cited by 48
SIRT3 gene expression: A link between inherited mitochondrial DNA variants and oxidative stress
D’Aquila, P., Rose, G., Panno, M. L., Passarino, G., & Bellizzi, D. (2012) · Gene · doi:10.1016/j.gene.2012.01.042 · Cited by 47
Panov, A. V., Kubalik, N., Zinchenko, N., Ridings, D. M., Radoff, D. A., Hemendinger, R. A., Brooks, B. R., & Bonkovsky, H. L. (2011) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00528.2010 · Cited by 47
Oxygen-dependence of mitochondrial ROS production as detected by Amplex Red assay
Grivennikova, V. G., Kareyeva, A. V., & Vinogradov, A. D. (2018) · Redox Biology · doi:10.1016/j.redox.2018.04.014 · Cited by 47
Dings, M. P. G., van der Zalm, A. P., Bootsma, S., van Maanen, T., Waasdorp, C., van den Ende, T., Liu, D., Bailey, P. J., Köster, J., Zwijnenburg, D. A., et al. (2022) · Cell Reports Medicine · doi:10.1016/j.xcrm.2022.100802 · Cited by 47
Kareyeva, A. V., Grivennikova, V. G., & Vinogradov, A. D. (2012) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.03.033 · Cited by 45
Mazumder, S., De, R., Sarkar, S., Siddiqui, A. A., Saha, S. J., Banerjee, C., Iqbal, M. S., Nag, S., Debsharma, S., & Bandyopadhyay, U. (2016) · Biochemical Pharmacology · doi:10.1016/j.bcp.2016.09.027 · Cited by 47
Free radicals: what they are and what they do
Tvrdá, E., & Benko, F. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-815972-9.00001-9 · Cited by 46
Hussain, Z., Thu, H. E., Elsayed, I., Abourehab, M. A. S., Khan, S., Sohail, M. F., Sarfraz, R. M., & Farooq, M. A. (2020) · Journal of Controlled Release · doi:10.1016/j.jconrel.2020.10.053 · Cited by 45
Rifampicin and Parkinson’s disease
Bi, W., Zhu, L., Jing, X., Liang, Y., & Tao, E. (2012) · Neurological Sciences · doi:10.1007/s10072-012-1156-0 · Cited by 46
Novel Therapeutic Approaches to Liver Fibrosis Based on Targeting Oxidative Stress
Blas‐García, A., & Apostolova, N. (2023) · Antioxidants · doi:10.3390/antiox12081567 · Cited by 51
Lu, J. G., Qian, H.-Y., Liu, L., Zhou, B., Xiao, Y., Mao, J., An, G., Rui, M., Wang, T., & Zhu, C. (2014) · Neurological Sciences · doi:10.1007/s10072-014-1813-6 · Cited by 45
Wu, L., Guo, X., Hartson, S. D., Davis, M. A., He, H., Medeiros, D. M., Wang, W., Clarke, S. L., Lucas, E. A., Smith, B. J., et al. (2016) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201600576 · Cited by 45
Long‐Term Alteration of Reactive Oxygen Species Led to Multidrug Resistance in MCF‐7 Cells
Cen, J., Zhang, L., Liu, F., Zhang, F., & Ji, B. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/7053451 · Cited by 45
Rajapakse, D., Curtis, T. M., Chen, M., & Xu, H. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/6926485 · Cited by 45
Peris, D., Arias, A., Orlić, S., Belloch, C., Pérez‐Través, L., Querol, A., & Barrio, E. (2017) · Molecular Phylogenetics and Evolution · doi:10.1016/j.ympev.2017.02.008 · Cited by 45
Phytosterols: Targeting Neuroinflammation in Neurodegeneration
Dash, R., Mitra, S., Ali, M. C., Oktaviani, D. F., Hannan, M. A., Choi, S. M., & Moon, I. S. (2020) · Current Pharmaceutical Design · doi:10.2174/1381612826666200628022812 · Cited by 47
Banstola, A., Poudel, K., Pathak, S., Shrestha, P. S., Kim, J. O., Jeong, J., & Yook, S. (2021) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.1c03594 · Cited by 46
Wang, Y., Jinjun, Z., Yang, W. P., Bi, Y., Chi, J., Tian, J., & Li, W. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.12.012 · Cited by 44
Fetisova, E. K., Avetisyan, A. V., Izyumov, D. S., Korotetskaya, M. V., Chernyak, B. V., & Skulachev, V. P. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.12.002 · Cited by 45
Glutathione System and Oxidative Stress in Health and Disease
Bagatini, M. D. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.82965 · Cited by 48
Enzyme Therapeutic for Ischemia and Reperfusion Injury in Organ Transplantation
Yan, R., Ren, J., Wen, J., Cao, Z., Wu, D., Qin, M., Xu, D., Castillo, R., Li, F., Wang, F., et al. (2021) · Advanced Materials · doi:10.1002/adma.202105670 · Cited by 44
Tzankova, V. I., Gorinova, C., Kondeva-Burdina, M., Simeonova, R., Philipov, S., Konstantinov, S., Petrov, P. D., Galabov, D., & Yoncheva, K. (2016) · Food and Chemical Toxicology · doi:10.1016/j.fct.2016.08.026 · Cited by 42
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Metadata
- Authors
- Starkov, A. A.
- Affiliations
- Cornell University (US)
- Corresponding author
- Starkov, Anatoly A.
- ORCID
- Starkov, Anatoly A.
- Venue
- Annals of the New York Academy of Sciences
- Publisher
- Wiley
- Published
- 2008-12
- Volume
- 1147
- Issue
- 1
- Pages
- 37-52
- ISSN
- 0077-8923 (ISSN-L)
- 1749-6632
- PMC
- PMC2869479
- OpenAlex
- W2053022803
- Cited by
- 846
- References
- 86
- Citations by year
- 2026: 39 · 2025: 39 · 2024: 42 · 2023: 66 · 2022: 67 · 2021: 78 · 2020: 74 · 2019: 55 · 2018: 42 · 2017: 46 · 2016: 50 · 2015: 39 · 2014: 38 · 2013: 41 · 2012: 39
- FWCI
- 2.32
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Annals of the New York Academy of Sciences (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute on Aging (AG014930, P01AG014930)
- 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 › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- mitochondria, reactive oxygen species, oxidative stress, ROS signaling, reactive oxygen species scavenging, aging, cellular senescence
- MeSH terms
- Humans, Mitochondria, Signal Transduction, Reactive Oxygen Species, Oxidative Stress
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