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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
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
Free Radicals: Properties, Sources, Targets, and Their Implication in Various Diseases
Phaniendra, A., Jestadi, D. B., & Periyasamy, L. (2015) · Indian Journal of Clinical Biochemistry · doi:10.1007/s12291-014-0446-0 · Cited by 2,886
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
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 1,550
Brand, M. D. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.001 · Cited by 1,063
Reactive Oxygen Species in Cancer: Current Findings and Future Directions
Nakamura, H., & Takada, K. (2021) · Cancer Science · doi:10.1111/cas.15068 · Cited by 1,027
Mitochondrial dysfunction and oxidative stress in Parkinson's disease
Subramaniam, S., & Chesselet, M. (2013) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2013.04.004 · Cited by 953
Pisoschi, A. M., Pop, A., Iordache, F., Stanca, L., Predoi, G., & Șerban, A. I. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112891 · Cited by 883
Mitochondrial dysfunction in Parkinson's disease
Winklhofer, K. F., & Haass, C. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.08.013 · Cited by 688
Oxidative Stress in Cancer Cell Metabolism
Arfin, S., Jha, N. K., Jha, S. K., Kesari, K. K., Ruokolainen, J., Roychoudhury, S., Rathi, B., & Kumar, D. (2021) · Antioxidants · doi:10.3390/antiox10050642 · Cited by 721
Mitochondrial DNA mutations and human disease
Tuppen, H. A. L., Blakely, E. L., Turnbull, D. M., & Taylor, R. W. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.09.005 · Cited by 676
“They are the major source of endogenous reactive oxygen species (ROS) [4] and they host other important biochemical pathways, including the tricarboxylic acid (TCA) cycle and parts of the urea cycle [5].”
BackgroundThe NLRP3 inflammasome in acute myocardial infarction
Toldo, S. A., & Abbate, A. (2017) · Nature Reviews Cardiology · doi:10.1038/nrcardio.2017.161 · Cited by 694
Adaptive response to oxidative stress: Bacteria, fungi, plants and animals
Lushchak, V. I. (2010) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2010.10.004 · Cited by 670
Atashi, F., Modarressi, A., & Pepper, M. S. (2015) · Stem Cells and Development · doi:10.1089/scd.2014.0484 · Cited by 660
Role of peroxisomes in ros/rns-metabolism: Implications for human disease
Fransen, M., Nordgren, M., Wang, B., & Apanasets, O. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.12.001 · Cited by 644
Exner, N., Lutz, A. K., Haass, C., & Winklhofer, K. F. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.170 · Cited by 677
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 658
Oxidative stress in ALS: Key role in motor neuron injury and therapeutic target
Barber, S. C., & Shaw, P. J. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.11.018 · Cited by 647
Parkinson's disease: Mechanisms, translational models and management strategies
Raza, C., Anjum, R., & Shakeel, N. U. A. (2019) · Life Sciences · doi:10.1016/j.lfs.2019.03.057 · Cited by 628
Bernardi, P., Rasola, A., Forte, M. A., & Lippe, G. (2015) · Physiological Reviews · doi:10.1152/physrev.00001.2015 · Cited by 598
Ferroptosis and Cancer: Mitochondria Meet the “Iron Maiden” Cell Death
Battaglia, A. M., Chirillo, R., Aversa, I., Sacco, A., Costanzo, F. S., & Biamonte, F. (2020) · Cells · doi:10.3390/cells9061505 · Cited by 593
The role of mitochondria in the pathogenesis of type 2 diabetes
Patti, M.-E., & Corvera, S. (2010) · Endocrine Reviews · doi:10.1210/er.2009-0027 · Cited by 551
Molecular Mechanisms of Superoxide Production by the Mitochondrial Respiratory Chain
Dröse, S., & Brandt, U. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-3573-0_6 · Cited by 537
Wong, H. S., Dighe, P. A., Mezera, V., Monternier, P., & Brand, M. D. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r117.789271 · Cited by 493
Reducing oxidative/nitrosative stress: a newly-discovered genre for melatonin
Reiter, R. J., Paredes, S. D., Manchester, L. C., & Tan, D.-X. (2009) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230903044914 · Cited by 483
Leyane, T. S., Jere, S. W., & Houreld, N. N. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23137273 · Cited by 536
Signaling pathways in Parkinson’s disease: molecular mechanisms and therapeutic interventions
Xu, D.-C., Yong, C., Xu, Y., Chen-Yu, S., & Peng, L. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01353-3 · Cited by 528
Autophagy Protects the Proximal Tubule from Degeneration and Acute Ischemic Injury
Kimura, T., Takabatake, Y., Takahashi, A., Kaimori, J.-Y., Matsui, I., Namba, T., Kitamura, H., Niimura, F., Matsusaka, T., Soga, T., et al. (2011) · Journal of the American Society of Nephrology · doi:10.1681/asn.2010070705 · Cited by 461
Yu, W., Dittenhafer‐Reed, K. E., & Denu, J. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.355206 · Cited by 452
Bell, E. L., Emerling, B. M., Ricoult, S. J. H., & Guarente, L. (2011) · Oncogene · doi:10.1038/onc.2011.37 · Cited by 440
Mammalian Mitochondrial Complex I: Biogenesis, Regulation, and Reactive Oxygen Species Generation
Koopman, W. J. H., Nijtmans, L. G. J., Dieteren, C. E. J., Roestenberg, P., Valsecchi, F., Smeitink, J. A. M., & Willems, P. H. G. M. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2743 · Cited by 411
Roles of Autophagy in Oxidative Stress
Yun, H. R., Jo, Y. H., Kim, J., Shin, Y., Kim, S. S., & Choi, T. G. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21093289 · Cited by 413
Wright, C., Milne, S., & Leeson, H. (2014) · Reproductive Biomedicine Online · doi:10.1016/j.rbmo.2014.02.004 · Cited by 389
Neri, M., Riezzo, I., Pascale, N., Pomara, C., & Turillazzi, E. (2017) · Mediators of Inflammation · doi:10.1155/2017/7018393 · Cited by 379
Superoxide generation by complex III: From mechanistic rationales to functional consequences
Bleier, L., & Dröse, S. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.12.002 · Cited by 369
Cheng, G., Kong, R., Zhang, L., & Zhang, J. (2012) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2012.02025.x · Cited by 359
Damage to dopaminergic neurons by oxidative stress in Parkinson's disease (Review)
Guo, J., Zhao, X., Li, Y., Li, G., & Liu, X. (2018) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2018.3406 · Cited by 353
Goncalves, R. L. S., Quinlan, C. L., Perevoshchikova, I. V., Hey-Mogensen, M., & Brand, M. D. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.619072 · Cited by 329
Mitochondrial Dysfunctions in Neurodegenerative Diseases: Relevance to Alzheimer’s Disease
Hroudová, J., Singh, N., & Fišar, Z. (2014) · BioMed Research International · doi:10.1155/2014/175062 · Cited by 319
Regulation of Yeast Chronological Life Span by TORC1 via Adaptive Mitochondrial ROS Signaling
Pan, Y., Schroeder, E. A., Ocampo, A., Barrientos, A., & Shadel, G. S. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.03.018 · Cited by 324
Mitochondria and microbiota dysfunction in COVID-19 pathogenesis
Saleh, J., Peyssonnaux, C., Singh, K. K., & Edeas, M. A. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.06.008 · Cited by 307
Mitochondrial oxidative stress promotes atrial fibrillation
Xie, W., Santulli, G., Reiken, S. R., Yuan, Q., Osborne, B. W., Chen, B.-X., & Marks, A. R. (2015) · Scientific Reports · doi:10.1038/srep11427 · Cited by 303
Chen, X., Li, X., Zhang, W., He, J., Xu, B., Lei, B., Wang, Z., Cates, C. A., Rousselle, T. V., & Li, J. (2018) · Metabolism · doi:10.1016/j.metabol.2018.03.004 · Cited by 298
Inhibitory Effect of Astaxanthin on Oxidative Stress-Induced Mitochondrial Dysfunction-A Mini-Review
Kim, S. H., & Kim, H. (2018) · Nutrients · doi:10.3390/nu10091137 · Cited by 291
Brown, G. C., & Borutaitė, V. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.02.001 · Cited by 295
NADPH oxidases in cardiovascular disease
Brandes, R. P., Weißmann, N., & Schröder, K. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.04.030 · Cited by 273
Red fluorescent genetically encoded indicator for intracellular hydrogen peroxide
Ermakova, Y. G., Bilan, D. S., Matlashov, M. E., Mishina, N. M., Markvicheva, K. N., Subach, O. M., Subach, F. V., Bogeski, I., Hoth, M., Enikolopov, G., et al. (2014) · Nature Communications · doi:10.1038/ncomms6222 · Cited by 270
Overview of the Mechanisms of Oxidative Stress: Impact in Inflammation of the Airway Diseases
Albano, G. D., Gagliardo, R. P., Montalbano, A. M., & Profita, M. (2022) · Antioxidants · doi:10.3390/antiox11112237 · Cited by 284
Gibson, G. E., Starkov, A. A., Blass, J. P., Ratan, R. R., & Beal, M. F. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.08.010 · Cited by 258
Self-citationRole of DJ-1 in the mechanism of pathogenesis of Parkinson's disease
Dolgacheva, L. P., Berezhnov, A. V., Fedotova, E. I., Zinchenko, V. P., & Abramov, A. Y. (2019) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-019-09798-4 · Cited by 254
Mitophagy in Cancer: A Tale of Adaptation
Vara‐Pérez, M., Felipe‐Abrio, B., & Agostinis, P. (2019) · Cells · doi:10.3390/cells8050493 · Cited by 264
OXPHOS mutations and neurodegeneration
Koopman, W. J. H., Distelmaier, F., Smeitink, J. A. M., & Willems, P. H. G. M. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.300 · Cited by 270
Mitochondrial Dysfunction and Oxidative Stress Caused by Cryopreservation in Reproductive Cells
Gualtieri, R., Kalthur, G., Barbato, V., Nardo, M. D., Adiga, S. K., & Talevi, R. (2021) · Antioxidants · doi:10.3390/antiox10030337 · Cited by 255
Xanthophyll cycle – a mechanism protecting plants against oxidative stress
Latowski, D., Kuczyńska, P., & Strzałka, K. (2011) · Redox Report · doi:10.1179/174329211x13020951739938 · Cited by 259
Differential Redox Regulation of ORAI Ion Channels: A Mechanism to Tune Cellular Calcium Signaling
Bogeski, I., Kummerow, C., Alansary, D., Schwarz, E. C., Koehler, R., Kozai, D., Takahashi, N., Peinelt, C., Griesemer, D., Bozem, M., et al. (2010) · Science Signaling · doi:10.1126/scisignal.2000672 · Cited by 254
Calcium and Mitochondrial Reactive Oxygen Species Generation: How to Read the Facts
Ádám‐Vizi, V., & Starkov, A. A. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100465 · Cited by 253
Self-citationMitochondrial function in immune cells in health and disease
Faas, M. M., & de Vos, P. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.165845 · Cited by 252
Diaz, B., Shani, G., Pass, I., Anderson, D., Quintavalle, M., & Courtneidge, S. A. (2009) · Science Signaling · doi:10.1126/scisignal.2000368 · Cited by 242
Redox activation of Nrf2 & NF-κB: A double end sword?
Buelna-Chontal, M., & Zazueta, C. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.08.007 · Cited by 239
The roles of reactive oxygen species and antioxidants in cryopreservation
Len, J. S., Koh, W. S. D., & Tan, S. (2019) · Bioscience Reports · doi:10.1042/bsr20191601 · Cited by 257
Oxidative Stress and Huntington’s Disease: The Good, the Bad, and the Ugly
Kumar, A., & Ratan, R. R. (2016) · Journal of Huntington s Disease · doi:10.3233/jhd-160205 · Cited by 236
Jurcău, M. C., Andronie-Cioara, F. L., Jurcău, A., Marcu, F., Ţiț, D. M., Pașcalău, N., & Nistor-Cseppentö, D. C. (2022) · Antioxidants · doi:10.3390/antiox11112167 · Cited by 226
Protein Oxidative Modifications: Beneficial Roles in Disease and Health.
Cai, Z., & Yan, L. (2013) · PubMed · Cited by 227
Cardamonin inhibits breast cancer growth by repressing HIF-1α-dependent metabolic reprogramming
Jin, J., Qiu, S., Wang, P., Liang, X., Huang, F., Wu, H., Zhang, B., Zhang, W., Tian, X.-H., Xu, R., et al. (2019) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-019-1351-4 · Cited by 226
Mitochondrial Functionality in Male Fertility: From Spermatogenesis to Fertilization
Park, Y.-J., & Pang, M. (2021) · Antioxidants · doi:10.3390/antiox10010098 · Cited by 225
Role of redox metabolism for adaptation of aquatic animals to drastic changes in oxygen availability
Welker, A. F., Moreira, D. C., Campos, E. G., & Hermes‐Lima, M. (2013) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/j.cbpa.2013.04.003 · Cited by 217
Martínez, A., Portero‐Otín, M., Pamplona, R., & Ferrer, I. (2009) · Brain Pathology · doi:10.1111/j.1750-3639.2009.00326.x · Cited by 217
A radical shift in perspective: mitochondria as regulators of reactive oxygen species
Munro, D., & Treberg, J. R. (2017) · Journal of Experimental Biology · doi:10.1242/jeb.132142 · Cited by 220
Shi, K., Gao, Z., Shi, T., Song, P., Ren, L., Huang, H., & Ji, X. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.00793 · Cited by 211
Dröse, S. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.01.004 · Cited by 201
The Impact of Oxidative Stress on Adipose Tissue Energy Balance
Masschelin, P. M., Cox, A. R., Chernis, N., & Hartig, S. M. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2019.01638 · Cited by 207
Genetically encoded fluorescent redox sensors
Lukyanov, K. A., & Belousov, V. V. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.05.030 · Cited by 206
Autophagy: Regulation and role in disease
Meijer, A. J., & Codogno, P. (2009) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408360903044068 · Cited by 215
Is there more to aging than mitochondrial DNA and reactive oxygen species?
ALEXEYEV, M. F. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07269.x · Cited by 196
Kaarniranta, K., Pawłowska, E., Szczepańska, J., Jabłkowska, A., & Błasiak, J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20102374 · Cited by 193
Mitochondrial ROS metabolism: 10 Years later
Andreyev, A. Y., Kushnareva, Y. E., Murphy, A. N., & Starkov, A. A. (2015) · Biochemistry (Moscow) · doi:10.1134/s0006297915050028 · Cited by 196
Self-citationSomasundaran, S., Constable, I. J., Mellough, C., & Carvalho, L. S. (2020) · Clinical and Experimental Ophthalmology · doi:10.1111/ceo.13834 · Cited by 206
Diverting Glycolysis to Combat Oxidative Stress
Mullarky, E., & Cantley, L. C. (2015) · Springer eBooks · doi:10.1007/978-4-431-55651-0_1 · Cited by 197
Toward a unifying hypothesis of metabolic syndrome
Bremer, A. A., Mietus-Snyder, M., & Lustig, R. H. (2012) · PEDIATRICS · doi:10.1542/peds.2011-2912 · Cited by 186
Insights into the respiratory chain and oxidative stress
Larosa, V., & Remacle, C. (2018) · Bioscience Reports · doi:10.1042/bsr20171492 · Cited by 192
Mitochondrial cholesterol: Metabolism and impact on redox biology and disease
Goicoechea, L., de la Rosa, L. C., Torres, S., García‐Ruiz, C., & Fernández-Checa, J. C. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102643 · Cited by 196
Neurodegeneration as a consequence of failed mitochondrial maintenance
Karbowski, M., & Neutzner, A. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0921-0 · Cited by 187
The emerging potential of cold atmospheric plasma in skin biology
Busco, G., Robert, É., Hammas, N., Pouvesle, J., & Grillon, C. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.10.004 · Cited by 191
Deconvoluting the role of reactive oxygen species and autophagy in human diseases
Wen, X., Wu, J., Wang, F., Liu, B., Huang, C., & Wei, Y. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.07.013 · Cited by 181
Functions and evolution of selenoprotein methionine sulfoxide reductases
Lee, B. C., Dikiy, A., Kim, H.-Y., & Gladyshev, V. N. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.04.014 · Cited by 178
Mitochondria as a target in treatment
Frantz, M., & Wipf, P. (2010) · Environmental and Molecular Mutagenesis · doi:10.1002/em.20554 · Cited by 183
Chronic stress as a risk factor for Alzheimer’s disease
Machado, A., Herrera, A. J., de Pablos, R. M., Espinosa‐Oliva, A. M., Soto, M. S., Ayala, A., Venero, J. L., Santiago, M., Villarán, R. F., Delgado‐Cortés, M. J., et al. (2014) · Reviews in the Neurosciences · doi:10.1515/revneuro-2014-0035 · Cited by 187
Han, B., Jiang, W., Liu, H., Wang, J., Zheng, K., Cui, P., Feng, Y., Dang, C., Bu, Y., Wang, Q. M., et al. (2020) · Theranostics · doi:10.7150/thno.37119 · Cited by 179
Ferrer, I. (2012) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2012.03.005 · Cited by 174
Kawamata, H., & Manfredi, G. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3212 · Cited by 171
Ferrer, I. (2009) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-009-9243-5 · Cited by 172
Sarewicz, M., & Osyczka, A. (2014) · Physiological Reviews · doi:10.1152/physrev.00006.2014 · Cited by 178
The Signaling Pathways Involved in Chondrocyte Differentiation and Hypertrophic Differentiation
Li, J., & Dong, S. (2016) · Stem Cells International · doi:10.1155/2016/2470351 · Cited by 170
Dambrova, M., Zuurbier, C. J., Borutaitė, V., Liepinsh, E., & Makrecka‐Kuka, M. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.01.036 · Cited by 169
Roles of reactive oxygen species in inflammation and cancer
Yu, Y., Liu, S., Yang, L., Song, P., Liu, Z., Liu, X., Yan, X., & Dong, Q. (2024) · MedComm · doi:10.1002/mco2.519 · Cited by 180
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Pérez‐Matute, P., Zulet, M. Á., & Martínez, J. A. (2009) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2009.08.005 · Cited by 162
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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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