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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
Flagged first, then by citations
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Items 101–200 of 847
The Dual Role of Myeloperoxidase in Immune Response
Arnhold, J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218057 · Cited by 172
Gualtieri, R., Kalthur, G., Barbato, V., Longobardi, S., Rella, F. D., Adiga, S. K., & Talevi, R. (2021) · Antioxidants · doi:10.3390/antiox10071025 · Cited by 173
Leuner, K., Müller, W. E., & Reichert, A. S. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8307-4 · Cited by 160
Protein Misfolding and Cellular Stress: An Overview
Gregersen, N., & Bross, P. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-756-3_1 · Cited by 163
Insulin Resistance and Mitochondrial Dysfunction
González-Franquesa, A., & Patti, M. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-55330-6_25 · Cited by 160
Mitochondrial respiratory chain complexes as sources and targets of thiol-based redox-regulation
Dröse, S., Brandt, U., & Wittig, I. (2014) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2014.02.006 · Cited by 155
Adamczyk, B., & Adamczyk-Sowa, M. H. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/1973834 · Cited by 155
Detection and manipulation of mitochondrial reactive oxygen species in mammalian cells
Forkink, M., Smeitink, J. A. M., Brock, R. E., Willems, P. H. G. M., & Koopman, W. J. H. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.01.022 · Cited by 154
Jiang, Z., Hu, Z., Zeng, L., Lu, W., Zhang, H., Li, T., & Xiao, H. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.01.011 · Cited by 149
Cen, M., Ouyang, W., Zhang, W., Yang, L., Lin, X., Dai, M., Hu, H., Tang, H., Liu, H., Xia, J., et al. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101936 · Cited by 149
Reactive Oxygen Species: Beyond Their Reactive Behavior
Tauffenberger, A., & Magistretti, P. J. (2021) · Neurochemical Research · doi:10.1007/s11064-020-03208-7 · Cited by 157
Oxidative Stress, Antioxidants and Hypertension
Amponsah-Offeh, M., Diaba‐Nuhoho, P., Speier, S., & Morawietz, H. (2023) · Antioxidants · doi:10.3390/antiox12020281 · Cited by 169
The Role of Hydrogen Peroxide in Environmental Adaptation of Oral Microbial Communities
Zhu, L. D., & Kreth, J. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/717843 · Cited by 151
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
Mitochondrial function/dysfunction in white adipose tissue
Boudina, S., & Graham, T. E. (2014) · Experimental Physiology · doi:10.1113/expphysiol.2014.081414 · Cited by 151
Jurcău, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111847 · Cited by 152
Chinopoulos, C. (2013) · Journal of Neuroscience Research · doi:10.1002/jnr.23196 · Cited by 148
Ganguly, U., Kaur, U., Chakrabarti, S. S., Sharma, P., Agrawal, B. K., Saso, L., & Chakrabarti, S. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/7086512 · Cited by 157
Upregulated autophagy protects cardiomyocytes from oxidative stress-induced toxicity
Dutta, D., Xu, J., Js, K., Dunn, W. A., & Leeuwenburgh, C. (2013) · Autophagy · doi:10.4161/auto.22971 · Cited by 143
Zhu, Z., Kawai, T., Umehara, T., Hoque, S. A. M., Zeng, W., & Shimada, M. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.06.018 · Cited by 144
Robey, R. B., Weisz, J., Kuemmerle, N. B., Salzberg, A. C., Berg, A. S., Brown, D. G., Maurer, L. L., Palorini, R., Al‐Mulla, F., Al-Temaimi, R. A., et al. (2015) · Carcinogenesis · doi:10.1093/carcin/bgv037 · Cited by 143
Dumont, M., Stack, C., Elipenahli, C., Jainuddin, S., Gerges, M., Starkova, N. N., Yang, L., Starkov, A. A., & Beal, F. M. (2011) · The FASEB Journal · doi:10.1096/fj.11-186650 · Cited by 139
Self-citationRalph, S. J., Moreno-Sánchez, R., Neuzil, J., & Rodríguez-Enríquez, S. (2011) · Pharmaceutical Research · doi:10.1007/s11095-011-0566-7 · Cited by 126
Mitochondria as a centrally positioned hub in the innate immune response
Sandhir, R., Halder, A., & Sunkaria, A. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.10.020 · Cited by 135
Oxidative stress in the haematopoietic niche regulates the cellular immune response in Drosophila
Sinenko, S. A., Shim, J., & Banerjee, U. K. (2011) · EMBO Reports · doi:10.1038/embor.2011.223 · Cited by 142
Catechin induced longevity in C. elegans: From key regulator genes to disposable soma
Saul, N., Pietsch, K., Menzel, R., Stürzenbaum, S. R., & Steinberg, C. E. W. (2009) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2009.05.005 · Cited by 133
Hyperglycemic Stress and Carbon Stress in Diabetic Glucotoxicity
Luo, X., Wu, J., Jing, S., & Yan, L. (2016) · Aging and Disease · doi:10.14336/ad.2015.0702 · Cited by 145
Siebels, I., & Dröse, S. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.06.005 · Cited by 130
Zhou, B.-H., Zhao, J., Liu, J., Zhang, J., Li, J., & Wang, H.-W. (2015) · Chemosphere · doi:10.1016/j.chemosphere.2015.08.030 · Cited by 129
Multi-mechanisms are involved in reactive oxygen species regulation of mTORC1 signaling
Li, M., Zhao, L., Liu, J., Liu, A., Jia, C., Ma, D., Jiang, Y., & Bai, X. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.05.015 · Cited by 132
Wood, E., Hall, K., & Tate, W. P. (2020) · Chronic Diseases and Translational Medicine · doi:10.1016/j.cdtm.2020.11.002 · Cited by 132
Pasdois, P., Parker, J. E., Griffiths, E. J., & Halestrap, A. P. (2011) · Biochemical Journal · doi:10.1042/bj20101957 · Cited by 127
Biochemistry of Reactive Oxygen and Nitrogen Species
Özcan, A., & ÖĞÜN, M. (2015) · InTech eBooks · doi:10.5772/61193 · Cited by 140
Mitochondria and the thermal limits of ectotherms
Chung, D. J., & Schulte, P. M. (2020) · Journal of Experimental Biology · doi:10.1242/jeb.227801 · Cited by 132
Pathophysiological importance of aggregated damaged proteins
Höhn, A., Jung, T., & Grune, T. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.02.028 · Cited by 130
Brand, M. D. (2020) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2020.1828258 · Cited by 123
Mitochondria-controlled signaling mechanisms of brain protection in hypoxia
Lukyanova, L. D., & Kirova, Y. I. (2015) · Frontiers in Neuroscience · doi:10.3389/fnins.2015.00320 · Cited by 126
Perevoshchikova, I. V., Quinlan, C. L., Orr, A. L., Gerencser, A. A., & Brand, M. D. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.04.006 · Cited by 121
Are mitochondria the main contributor of reactive oxygen species in cells?
Zhang, Y., & Wong, H. S. (2021) · Journal of Experimental Biology · doi:10.1242/jeb.221606 · Cited by 128
García‐Ruiz, C., Baulies, A., Marí, M., García-Rovés, P. M., & Fernández-Checa, J. C. (2013) · Free Radical Research · doi:10.3109/10715762.2013.830717 · Cited by 119
Speijer, D. (2010) · BioEssays · doi:10.1002/bies.201000097 · Cited by 117
Measurement of Mitochondrial ROS Production
Starkov, A. A. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-756-3_16 · Cited by 122
Self-citationMcGregor, G. H., Campbell, A. D., Fey, S. K., Tumanov, S., Sumpton, D. P., Blanco, G. R., Mackay, G., Nixon, C., Vázquez, A., Sansom, O. J., et al. (2019) · Cancer Research · doi:10.1158/0008-5472.can-19-0644 · Cited by 116
Hatle, K. M., Gummadidala, P. M., Navasa, N., Bernardo, E., Dodge, J. T., Silverstrim, B., Fortner, K. A., Burg, E., Suratt, B. T., Hammer, J., et al. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00189-13 · Cited by 117
del Valle, M. L., Dworshak, J., Sharma, A. K., Ibrahim, A. S., Al‐Shabrawey, M., & Sharma, S. (2018) · Experimental Eye Research · doi:10.1016/j.exer.2018.09.009 · Cited by 113
Neuropathic Pain: the Dysfunction of Drp1, Mitochondria, and ROS Homeostasis
Dai, C., Guo, Y., & Chu, X.-Y. (2020) · Neurotoxicity Research · doi:10.1007/s12640-020-00257-2 · Cited by 111
Madkour, M. I., El-Serafi, A. T., Jahrami, H., Sherif, N. M., Hassan, R. E., Awadallah, S. M., & Faris, M. E. (2019) · Diabetes Research and Clinical Practice · doi:10.1016/j.diabres.2019.107801 · Cited by 112
Mitochondrial respiration in blood platelets of depressive patients
Hroudová, J., Fišar, Z., Kitzlerová, E., Zvěřová, M., & Raboch, J. (2013) · Mitochondrion · doi:10.1016/j.mito.2013.05.005 · Cited by 108
Human placental metabolic adaptation to chronic hypoxia, high altitude: hypoxic preconditioning
Tissot van Patot, M. C., Murray, A. J., Beckey, V., Cindrova-Davies, T., Johns, J., Zwerdlinger, L., Jauniaux, E., Burton, G. J., & Serkova, N. J. (2010) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00383.2009 · Cited by 107
Role of Oxidative Stress in Liver Disorders
Conde de la Rosa, L., Goicoechea, L., Torres, S., Garcia-Ruiz, C., & Fernandez-Checa, J. C. (2022) · Livers · doi:10.3390/livers2040023 · Cited by 107
Ji, W., Wei, S., Hao, P., Xing, J., Yuan, Q., Wang, J., Xu, F., & Chen, Y. (2016) · Frontiers in Pharmacology · doi:10.3389/fphar.2016.00101 · Cited by 106
Cahill‐Smith, S., & Li, J. (2014) · British Journal of Clinical Pharmacology · doi:10.1111/bcp.12357 · Cited by 109
Ten, V. S., & Starkov, A. A. (2012) · Neurology Research International · doi:10.1155/2012/542976 · Cited by 104
Self-citationEffects of Tea Catechins on Alzheimer’s Disease: Recent Updates and Perspectives
Ide, K., Matsuoka, N., Yamada, H., Furushima, D., & Kawakami, K. (2018) · Molecules · doi:10.3390/molecules23092357 · Cited by 103
Hakiminia, B., Alikiaii, B., Khorvash, F., & Mousavi, S. (2022) · Fundamental and Clinical Pharmacology · doi:10.1111/fcp.12767 · Cited by 106
Moreno‐Sánchez, R., Hernández‐Esquivel, L., Rivero‐Segura, N. A., Marín‐Hernández, A., Neuzil, J., Ralph, S. J., & Rodríguez‐Enríquez, S. (2013) · The FEBS Journal · doi:10.1111/febs.12086 · Cited by 100
Choi, E., Nguyen, T.-T., Gupta, N., Iwase, S., & Seo, Y. A. (2018) · Scientific Reports · doi:10.1038/s41598-018-21464-0 · Cited by 98
Oxidative stress and use of antioxidants in fish semen cryopreservation
Sandoval‐Vargas, L., Jiménez, M. S., Risopatrón, J., Figueroa, E., Cabrita, E., & Isler, I. V. (2020) · Reviews in Aquaculture · doi:10.1111/raq.12479 · Cited by 99
Degenerative diseases, oxidative stress and cytochrome c oxidase function
Kadenbach, B., Ramzan, R., & Vogt, S. K. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2009.02.004 · Cited by 97
Pasdois, P., Parker, J. E., & Halestrap, A. P. (2013) · Journal of the American Heart Association · doi:10.1161/jaha.112.005645 · Cited by 98
Aguilar, E., de Mas, I. M., Zodda, E., Marín, S., Morrish, F. M., Selivanov, V. A., Meca‐Cortés, Ó., Delowar, H., Pons, M., Izquierdo, I., et al. (2016) · Stem Cells · doi:10.1002/stem.2286 · Cited by 97
An estimate of extracellular vesicle secretion rates of human blood cells
Auber, M., & Svenningsen, P. (2022) · Journal of Extracellular Biology · doi:10.1002/jex2.46 · Cited by 102
Living on the Edge: ROS Homeostasis in Cancer Cells and Its Potential as a Therapeutic Target
Brandl, N., Seitz, R., Sendtner, N., Müller, M., & Gülow, K. (2025) · Antioxidants · doi:10.3390/antiox14081002 · Cited by 113
Glutamate and Mitochondria: Two Prominent Players in the Oxidative Stress-Induced Neurodegeneration
Cassano, T., Pace, L., Bedse, G., Lavecchia, A. M., Marco, F. D., Gaetani, S., & Serviddio, G. (2015) · Current Alzheimer Research · doi:10.2174/1567205013666151218132725 · Cited by 96
Ten, V. S., Yao, J., Ratner, V. I., Sosunov, S. A., Fraser, D. A., Botto, M., Sivasankar, B., Morgan, B. P., Silverstein, S. C., Stark, R. I., et al. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.5249-09.2010 · Cited by 95
Self-citationZhang, J., Wu, D., Vikash, V., Song, J. T., Wang, J., Yi, J., & Dong, W. (2015) · Digestive Diseases and Sciences · doi:10.1007/s10620-015-3696-7 · Cited by 95
Oxidative Stress and Marine Carotenoids: Application by Using Nanoformulations
Genç, Y., Bardakçı, H., Yücel, Ç., Karatoprak, G. Ş., Akkol, E. K., Barak, T. H., & Sobarzo‐Sánchez, E. (2020) · Marine Drugs · doi:10.3390/md18080423 · Cited by 99
Oxyresveratrol abrogates oxidative stress by activating ERK–Nrf2 pathway in the liver
Choi, H. Y., Lee, J., Jegal, K. H., Cho, I. J., Kim, Y. W., & Kim, S. C. (2015) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2015.06.024 · Cited by 94
Permeability Effects on the Efficiency of Antioxidant Nanoreactors
Louzao, I., & van Hest, J. C. M. (2013) · Biomacromolecules · doi:10.1021/bm400493b · Cited by 93
Mitochondrial genome evolution in yeasts: an all-encompassing view
Freel, K. C., Friedrich, A., & Schacherer, J. (2015) · FEMS Yeast Research · doi:10.1093/femsyr/fov023 · Cited by 92
Inhibitory Effect of Lycopene on Amyloid-β-Induced Apoptosis in Neuronal Cells
Hwang, S., Lim, J. W., & Kim, H. (2017) · Nutrients · doi:10.3390/nu9080883 · Cited by 92
Sharma, V., & Mehdi, M. M. (2023) · Neurochemistry International · doi:10.1016/j.neuint.2023.105490 · Cited by 100
Metabolic defects provide a spark for the epigenetic switch in cancer
Hitchler, M. J., & Domann, F. E. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.04.010 · Cited by 91
Sabarwal, A., Agarwal, R., & Singh, R. P. (2016) · Molecular Carcinogenesis · doi:10.1002/mc.22512 · Cited by 93
Mitochondrial ion channels as oncological targets
Leanza, L., Zoratti, M., Gulbins, E., & Szabó, I. (2014) · Oncogene · doi:10.1038/onc.2013.578 · Cited by 93
Molecular mechanisms of oxidative stress in stroke and cancer
Chavda, V. K., Chaurasia, B. K., Garg, K., Deora, H., Umana, G. E., Palmisciano, P., Scalia, G., & Lu, B. (2021) · Brain Disorders · doi:10.1016/j.dscb.2021.100029 · Cited by 98
Mitochondria-mediated Ferroptosis in Diseases Therapy: From Molecular Mechanisms to Implications
Feng, F., He, S., Li, X., He, J., & Luo, L. (2023) · Aging and Disease · doi:10.14336/ad.2023.0717 · Cited by 92
Hauser, D. N., Dukes, A. A., Mortimer, A. D., & Hastings, T. G. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.06.030 · Cited by 87
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Ding, Z., Liu, S., Wang, X., Mathur, P., Dai, Y., Theus, S. A., Deng, X., Fan, Y., & Mehta, J. L. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6631 · Cited by 92
Sepsis‐Induced Cardiomyopathy: Oxidative Implications in the Initiation and Resolution of the Damage
Tsolaki, V., Makris, D. A., Mantzarlis, K. D., & Zakynthinos, E. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/7393525 · Cited by 85
Rehfeldt, S. C. H., Laufer, S., & Goettert, M. I. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22073701 · Cited by 86
Pérez‐Matute, P., Pérez‐Martínez, L., Blanco, J. R., & Oteo, J. A. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/493413 · Cited by 84
Peris, D., Pérez‐Torrado, R., Hittinger, C. T., Barrio, E., & Querol, A. (2017) · Yeast · doi:10.1002/yea.3283 · Cited by 84
Pascual‐Ahuir, A., Manzanares‐Estreder, S., & Proft, M. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/9860841 · Cited by 87
The Impact of Estradiol on Neurogenesis and Cognitive Functions in Alzheimer’s Disease
Negah, S. S., Hajali, V., Moradi, H. R., & Gorji, A. (2019) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-019-00733-0 · Cited by 83
Munro, D., Banh, S., Sotiri, E., Tamanna, N., & Treberg, J. R. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.014 · Cited by 82
Montalvo, R. N., Doerr, V., Min, K., Szeto, H. H., & Smuder, A. J. (2019) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00299.2019 · Cited by 83
Hepatic miR-144 Drives Fumarase Activity Preventing NRF2 Activation During Obesity
Azzimato, V., Chen, P., Barreby, E., Morgantini, C., Levi, L., Vankova, A., Jager, J., Sulen, A., Diotallevi, M., Shen, J. X., et al. (2021) · Gastroenterology · doi:10.1053/j.gastro.2021.08.030 · Cited by 81
The role of oxidative stress in patients with recurrent pregnancy loss: a review
Zejnullahu, V. A., Zejnullahu, V. A., & Kosumi, E. (2021) · Reproductive Health · doi:10.1186/s12978-021-01257-x · Cited by 88
Bhattacharjee, N., & Borah, A. (2016) · Neurochemistry International · doi:10.1016/j.neuint.2016.10.001 · Cited by 82
Wang, Y., Lilienfeldt, N., & Hekimi, S. (2024) · Physiological Reviews · doi:10.1152/physrev.00040.2023 · Cited by 88
Forkink, M., Basit, F., Teixeira, J., Swarts, H. G. P., Koopman, W. J. H., & Willems, P. H. G. M. (2015) · Redox Biology · doi:10.1016/j.redox.2015.09.003 · Cited by 81
Scavenging of H2O2 by mouse brain mitochondria
Starkov, A. A., Andreyev, A. Y., Zhang, S. F., Starkova, N. N., Korneeva, M., Syromyatnikov, M., & Popov, V. N. (2014) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-014-9581-9 · Cited by 80
Self-citationGuix, F. X., Wahle, T., Vennekens, K. M., Snellinx, A., Chávez‐Gutiérrez, L., ILL‐Raga, G., Ramos‐Fernández, E., Guardia‐Laguarta, C., Lleó, A., Arimon, M., et al. (2012) · EMBO Molecular Medicine · doi:10.1002/emmm.201200243 · Cited by 82
DdCBE mediates efficient and inheritable modifications in mouse mitochondrial genome
Guo, J., Chen, X., Liu, Z., Sun, H., Zhou, Y., Dai, Y., Ma, Y., He, L., Qian, X., Wang, J., et al. (2021) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2021.11.016 · Cited by 77
Yu, L., Wang, W., Pang, W., Xiao, Z.-H., Jiang, Y., & Hong, Y. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-161216 · Cited by 77
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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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