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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
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Items 501–600 of 847
Zhang, D., Yan, H., Hu, J., Zhang, J.-P., Teng, M., Tong, D., Fei, X., Zhang, Q., Fang, Y.-D., Liang, G., et al. (2012) · Journal of Proteomics · doi:10.1016/j.jprot.2012.09.024 · Cited by 16
Kadota, Y., Suzuki, S., Ideta, S., Fukinbara, Y., Kawakami, T., Imai, H., Nakagawa, Y., & Sato, M. (2009) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2009.09.060 · Cited by 16
Salles, G. N., Pereira, F. A. D. S., Soares, C. P., Marciano, F. R., Hölscher, C., Webster, T. J., & Lobo, A. O. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-0200-0 · Cited by 17
Pick, E. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101765 · Cited by 17
Ushakiran, P., Haria, J., Rani, R., & Singh, S. K. (2025) · Tissue Barriers · doi:10.1080/21688370.2025.2537991 · Cited by 15
Dithianon exposure induces dopaminergic neurotoxicity in Caenorhabditis elegans
Lee, Y., Choi, S., & Kim, K. W. (2023) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2023.114752 · Cited by 15
Impact of mitochondrial lipid alterations on liver disease mechanisms and progression
Fàbrega, L., Fernández-Checa, J. C., de la Rosa, L. C., & García‐Ruiz, C. (2024) · Exploration of Digestive Diseases · doi:10.37349/edd.2024.00057 · Cited by 16
Zolotukhin, P. V., Kozlova, Y., Dovzhik, A. D., Коваленко, К. А., Kutsyn, K., Александрова, А. А., & Shkurat, T. P. (2013) · Molecular BioSystems · doi:10.1039/c3mb70096h · Cited by 15
Transcriptome analysis in mitochondrial disorders
Elstner, M., & Turnbull, D. M. (2011) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2011.07.018 · Cited by 15
Piecuch, A., Brzozowa-Zasada, M., Dziewit, B., Segiet, O. A., Kurek, J., Kowalczyk-Ziomek, G. I., Wojnicz, R., & Helewski, K. J. (2016) · Gastroenterology Review · doi:10.5114/pg.2016.57943 · Cited by 15
Reactive Oxygen Species, Cellular Redox Homeostasis and Cancer
Mydin, R. B. S. M. N., & Okekpa, S. I. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.76096 · Cited by 17
Cioffi, F., Senese, R., Petito, G., Lasala, P., de Lange, P., Silvestri, E., Lombardi, A., Moreno, M., Goglia, F., & Lanni, A. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00216 · Cited by 15
An In Vitro Study on Mitochondrial Compensatory Response Induced by Gliadin Peptides in Caco-2 Cells
Orlando, A., Chimienti, G., Pesce, V., Fracasso, F., Lezza, A. M. S., & Russo, F. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20081862 · Cited by 15
Physiological Functions of Mitochondrial Reactive Oxygen Species
Choi, T. G., & Kim, S. S. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.88386 · Cited by 22
Wang, C., Hu, J., Chen, Z., Wang, Y., Lu, S., Zhang, Y., Li, Y., Xiang, Y., Ji, Y., Zeng, C. C., et al. (2020) · Stem Cell Research & Therapy · doi:10.1186/s13287-020-02010-0 · Cited by 15
Selivanov, V. A., Zagubnaya, O. A., Nartsissov, Y. R., & Cascante, M. (2021) · PLoS ONE · doi:10.1371/journal.pone.0255164 · Cited by 15
Molecular interaction of HIC, an agonist of P2Y1 receptor, and its role in prostate cancer apoptosis
Le, H. T. T., Murugesan, A., Ramesh, T., Yli-Harja, O. P., Saravanan, K. M., & Kandhavelu, M. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.08.103 · Cited by 15
Reactive Oxygen Species: Friends and Foes of Signal Transduction
Retta, S. F., Chiarugi, P., Trabalzini, L., Pinton, P., & Belkin, A. M. (2012) · Journal of Signal Transduction · doi:10.1155/2012/534029 · Cited by 16
Wang, R., Zheng, X., Zhang, L., Zhou, B., Hu, H., Li, Z., Zhang, L., Lin, Y., & Wang, X. (2017) · Scientific Reports · doi:10.1038/srep41715 · Cited by 15
Kurtar, S. N. K., Gönül, İ., & Köse, M. (2017) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2017.09.067 · Cited by 15
Effect of Pulsed Therapeutic Ultrasound and Diosmin on Skeletal Muscle Oxidative Parameters
Filho, L. F. S., Menezes, P. D. P., Santana, D. V. S., Lima, B. S., Saravanan, S., de Almeida, G. K. M., Filho, J. E. R. M., Santos, M. M. B., Araújo, A. A. D. S., & de Oliveira, E. D. (2017) · Ultrasound in Medicine & Biology · doi:10.1016/j.ultrasmedbio.2017.09.009 · Cited by 15
A potential role for astaxanthin in the treatment of bone diseases (Review)
Valenti, M. T., Perduca, M., Romanelli, M. G., Mottes, M., & Carbonare, L. D. (2020) · Molecular Medicine Reports · doi:10.3892/mmr.2020.11284 · Cited by 16
Mechanisms and therapeutic perspectives of mitochondrial dysfunction of macrophages in periodontitis
Jia, Y., Li, Z., Huang, P., Wang, Y., & Yang, B. (2025) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2025.1634909 · Cited by 17
Jin, J., Chang, S., Xu, S., Xia, G., Wong, J. M. J., Fang, Y., Jia, P., & Ding, X. (2023) · Journal of Immunology Research · doi:10.1155/2023/5513507 · Cited by 14
Balcázar, N., Betancur, L. I., Muñoz, D. L., Cabrera, F. J., Castaño, A., Echeverri, F., & Acı́n, S. (2021) · Molecules · doi:10.3390/molecules26082282 · Cited by 14
Home Sweet Home: Plasmodium vivax-Infected Reticulocytes—The Younger the Better?
Thomson-Luque, R., & Bautista, J. M. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.675156 · Cited by 14
Antioxidant response to severe hypoxia in Brandt's vole Lasiopodomys brandtii
Shi, L., Chen, B., Wang, X., Huang, M., Congcong, Q. I. A. O., Wang, J., & Wang, Z. (2021) · Integrative Zoology · doi:10.1111/1749-4877.12602 · Cited by 14
Helal, M. H. S., Das, U., Bandy, B., Islam, A., Nazarali, A. J., & Dimmock, J. R. (2012) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2012.12.016 · Cited by 14
Boronate-Based Fluorescent Probes as a Prominent Tool for H2O2 Sensing and Recognition
Wang, L., Hou, X., Fang, H., & Yang, X. (2021) · Current Medicinal Chemistry · doi:10.2174/0929867328666210902101642 · Cited by 13
Biological autoluminescence as a perturbance-free method for monitoring oxidation in biosystems
Vahalová, P., & Cifra, M. (2022) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2022.10.009 · Cited by 14
Gauthier, A. G., Lin, M., Zefi, S., Kulkarni, A., Thakur, G. A., Ashby, C. R., & Mantell, L. L. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102614 · Cited by 13
Kubat, G. B., Ülger, Ö., Atalay, Ö., Fatsa, T., Türkel, İ., Özerkliğ, B., Çelik, E., Ozenc, E., Şımşek, G., & Tuncer, M. (2024) · Journal of Muscle Research and Cell Motility · doi:10.1007/s10974-024-09676-6 · Cited by 13
Bergandi, L., Palladino, G., Meduri, A., Luca, L. D., & Silvagno, F. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25126404 · Cited by 16
Lin, B., Chen, Z., Xu, Y. F., Zhang, H., Liu, J., & Qian, X. H. (2011) · Leukemia Research · doi:10.1016/j.leukres.2011.01.029 · Cited by 13
Zonisamide Administration Improves Fatty Acid β-Oxidation in Parkinson’s Disease
Ueno, S., Saiki, S., Fujimaki, M., Takeshige‐Amano, H., Hatano, T., Oyama, G., Ishikawa, K., Yamaguchi, A., Nojiri, S., Akamatsu, W., et al. (2018) · Cells · doi:10.3390/cells8010014 · Cited by 14
Trzeciak, E. R., Zimmer, N., Gehringer, I., Stein, L., Graefen, B., Schupp, J., Stephan, A., Rietz, S., Prantner, M., & Tuettenberg, A. (2022) · Cells · doi:10.3390/cells11060930 · Cited by 13
Owens, C. E., Daniels, K. M., Ealy, A. D., Knowlton, K. F., & Cockrum, R. (2020) · Journal of Dairy Science · doi:10.3168/jds.2019-18050 · Cited by 14
Xiong, G., Zhang, B., Song, B., Luo, H., Zhao, L., Wang, Z., Zhou, Z., & Chang, X. (2021) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2021.147386 · Cited by 13
Miyamoto, T., Kitamura, N., Ono, M., Nakamura, Y., Yoshida, M., Kamino, H., Murai, R., Yamada, T., & Arakawa, H. (2012) · Scientific Reports · doi:10.1038/srep00379 · Cited by 13
Niveta, J. P. S., John, C. M., & Arockiasamy, S. (2023) · Molecular Biology Reports · doi:10.1007/s11033-023-08938-9 · Cited by 12
Secondary follicles enable efficient germline mtDNA base editing at hard-to-edit site
Xie, Q., Wu, H., Long, H., Xiao, C., Qiu, J., Yu, W., Jiang, X., Liu, J., Zhang, S., Lyu, Q., et al. (2024) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2024.102170 · Cited by 12
Oxidative Stress in the Pathogenesis of Neurodegenerative Diseases
Jurcău, M. C., Jurcău, A., & Diaconu, R.-G. (2024) · Stresses · doi:10.3390/stresses4040055 · Cited by 19
Plate-Based Measurement of Superoxide and Hydrogen Peroxide Production by Isolated Mitochondria
Wong, H. S., Monternier, P., Orr, A. L., & Brand, M. D. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-7831-1_16 · Cited by 12
Skeletal muscle mitoflashes, pH, and the role of uncoupling protein-3
McBride, S., Wei‐LaPierre, L., McMurray, F., Macfarlane, M., Qiu, X., Patten, D. A., Dirksen, R. T., & Harper, M. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.01.018 · Cited by 12
Sun, L., Zhou, F., Shao, Y., Lv, Z., & Li, C. (2020) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2020.04.060 · Cited by 12
Potential Roles of mtDNA Mutations in PCOS-IR: A Review
Dong, X., Liu, C., Zhuo, G., & Ding, Y. (2023) · Diabetes Metabolic Syndrome and Obesity · doi:10.2147/dmso.s393960 · Cited by 12
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Kitagaki, H. (2009) · Biotechnology and Applied Biochemistry · doi:10.1042/ba20090032 · Cited by 12
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Wang, Y., Wang, Y., Marcus, S., & Busenlehner, L. S. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.06.017 · Cited by 12
Zou, T., Yu, B., Yu, J., Mao, X., Zheng, P., He, J., Huang, Z., He, D., & Chen, D. (2016) · animal · doi:10.1017/s1751731116001269 · Cited by 12
Respirometric reserve capacity of cumulus cell mitochondria correlates with oocyte maturity
Anderson, S. H., Glassner, M. J., Melnikov, A., Friedman, G., & Orynbayeva, Z. (2018) · Journal of Assisted Reproduction and Genetics · doi:10.1007/s10815-018-1271-9 · Cited by 12
Lee, K. H., Kim, U. J., Cha, M., & Lee, B. H. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22041608 · Cited by 12
Li, X., Li, M., Huang, M., Li, J., Huang, S., Wang, B., Gao, Y. Z., Wang, Z., & Shi, L. (2023) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2023.164537 · Cited by 11
Kumar, R., Chhikara, B. S., Zeybekler, S. E., Gupta, D., Kaur, G., Chhillar, M., Aggarwal, A. K., & Rahdar, A. (2023) · Toxicology Research · doi:10.1093/toxres/tfad086 · Cited by 11
Xu, T., Chu, C., Xue, S., Jiang, T., Wang, Y., Xia, W., & Lin, H. (2025) · Journal of Translational Medicine · doi:10.1186/s12967-025-06080-7 · Cited by 14
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Lambiri, D. W., & Levin, L. A. (2022) · Biomolecules · doi:10.3390/biom12101411 · Cited by 11
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Wang, X., Li, L., & Meng, X. (2024) · Antioxidants · doi:10.3390/antiox13101156 · Cited by 14
Jung, Y. Y., Ha, I. J., Lee, M., & Ahn, K. S. (2022) · Antioxidants · doi:10.3390/antiox12010051 · Cited by 10
Guo, Y., Lu, N., He, Q., Wang, B., Cao, S., & Wang, Y. (2023) · Aquatic Toxicology · doi:10.1016/j.aquatox.2023.106536 · Cited by 10
Adamczyk, B., Niedziela, N., & Adamczyk-Sowa, M. H. (2017) · Codon Publications eBooks · doi:10.15586/codon.multiplesclerosis.2017.ch10 · Cited by 10
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Scheckhuber, C. Q., Hamann, A., Brust, D., & Osiewacz, H. D. (2011) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-007-2561-4_11 · Cited by 10
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Macasoi, I. G., Mioc, A., Mioc, M., Racoviceanu, R., Şoica, I., Chevereșan, A., Dehelean, C. A., & Dumitraşcu, V. (2019) · Current Medicinal Chemistry · doi:10.2174/0929867326666190712150638 · Cited by 10
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Dadson, P., Honka, M., Suomi, T., Haridas, P. A. N., Rokka, A., Palani, S., Goltseva, E., Wang, N., Roivainen, A., Salminen, P. T. P., et al. (2025) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00220.2024 · Cited by 10
Wang, H., Zhao, T., Wang, X., Wang, D., & Zhang, Y. T. (2022) · Plasma Processes and Polymers · doi:10.1002/ppap.202200083 · Cited by 9
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Li, C., Zhang, Y., Liu, R., & Mai, Y. (2021) · Bioengineered · doi:10.1080/21655979.2021.1960767 · Cited by 9
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do Nascimento, N. C., dos Santos, A. P., Mohallem, R., Aryal, U. K., Xie, J. H., Cox, A. D., & Sivasankar, M. P. (2021) · Journal of Proteomics · doi:10.1016/j.jprot.2021.104431 · Cited by 9
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Zoccarato, F., Miotto, C., Cavallini, L., & Alexandre, A. (2011) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-011-9363-6 · Cited by 8
Su, Y., Sun, C., Sun, X., Wu, R., Zhang, X., & Tu, Y. (2020) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-020-03279-w · Cited by 8
Li, B., An, D., & Zhu, S. (2022) · Cytotechnology · doi:10.1007/s10616-021-00518-8 · Cited by 8
Wu, L., Liu, X., Wu, S., Wang, F., Lu, M., Wang, F., & Hu, R. (2023) · Journal of Food Measurement & Characterization · doi:10.1007/s11694-023-02163-5 · Cited by 8
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Chiu, W. K., Towheed, A., & Palladino, M. J. (2014) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-416618-9.00014-5 · Cited by 8
Zhu, L., Lu, Y., Zhang, J., & Hu, Q. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-63245-2_25 · Cited by 9
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Pereira, H. A. B. S., Araújo, T. T., Dionizio, A. S., Trevizol, J. S., Pereira, F. S., Iano, F. G., Ximenes, V. F., & Buzalaf, M. A. R. (2021) · Heliyon · doi:10.1016/j.heliyon.2021.e06028 · Cited by 8
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Song, M., Zhang, J., Huo, S., Zhang, X., Cui, Y., & Li, Y. (2023) · Food and Chemical Toxicology · doi:10.1016/j.fct.2023.113762 · Cited by 9
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Cheng, W., Larson, J. M., & Samet, J. M. (2013) · Methods · doi:10.1016/j.ymeth.2013.06.008 · Cited by 8
Ansari, M., & Kurian, G. A. (2017) · Asian Pacific Journal of Tropical Biomedicine · doi:10.1016/j.apjtb.2017.09.020 · Cited by 8
Boussada, M., Dias, T. R., Crisóstomo, L., Akacha, A. B., Ali, R. B., May, M. V. E., Alves, M. G., & Oliveira, P. F. (2019) · Theriogenology · doi:10.1016/j.theriogenology.2019.08.030 · Cited by 8
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Sood, P. K., Verma, S., Nahar, U., & Nehru, B. (2015) · Neurochemical Research · doi:10.1007/s11064-015-1653-7 · Cited by 8
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Rahman, A. U., & Panichayupakaranant, P. (2024) · Antioxidants · doi:10.1002/9781394270576.ch2 · Cited by 8
Birrell, J. H., Verberk, W. C. E. P., & Woods, H. A. (2024) · Current Research in Insect Science · doi:10.1016/j.cris.2024.100095 · Cited by 8
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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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