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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
Research works printed but not linked: 2
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- 10.1111/j.1469-7793.2003.00335.x · DOI · Paper page
Cited by
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Items 301–400 of 847
Methods to evaluate the toxicity of engineered nanomaterials for biomedical applications: a review
Patel, G., Patra, C., Srinivas, S. P., Kumawat, M., Navya, P. N., & Daima, H. K. (2021) · Environmental Chemistry Letters · doi:10.1007/s10311-021-01280-1 · Cited by 42
Mitochondria and Cellular Redox State on the Route from Ageing to Alzheimer's Disease
Abate, G., Vezzoli, M., Sandri, M., Rungratanawanich, W., Memo, M., & Uberti, D. (2020) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2020.111385 · Cited by 41
Alda-1, an activator of ALDH2, ameliorates Achilles tendinopathy in cellular and mouse models
Liu, Y.-C., Wang, H., Huang, Y., Weng, Y.-H., Chen, R., Tsai, W., Yeh, T., Lu, C.-S., Chen, Y., Lin, Y.-W., et al. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.113919 · Cited by 41
Management of ROS and Regulatory Cell Death in Myocardial Ischemia–Reperfusion Injury
Gong, G., Wan, W., Zhang, X., Chen, X., & Yin, J. P. (2024) · Molecular Biotechnology · doi:10.1007/s12033-024-01173-y · Cited by 46
Cortical spreading depression in traumatic brain injuries: Is there a role for astrocytes?
Torrente, D., Cabezas, R., Ávila-Rodriguez, M., García‐Segura, L. M., Barreto, G. E., & Guedes, R. C. A. (2014) · Neuroscience Letters · doi:10.1016/j.neulet.2013.12.058 · Cited by 43
Molecular base of biochemical complex I deficiency
Hoefs, S. J. G., Rodenburg, R. J., Smeitink, J. A. M., & van den Heuvel, L. P. (2012) · Mitochondrion · doi:10.1016/j.mito.2012.07.106 · Cited by 41
Basisty, N., Dai, D., Gagnidze, A., Gitari, L., Fredrickson, J., Maina, Y., Beyer, R. P., Emond, M. J., Hsieh, E. J., MacCoss, M. J., et al. (2016) · Aging Cell · doi:10.1111/acel.12472 · Cited by 41
Dubouchaud, H., Walter, L., Rigoulet, M., & Batandier, C. (2018) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-018-9767-7 · Cited by 41
Lipid oxidation dysregulation: an emerging player in the pathophysiology of sepsis
Muniz‐Santos, R., Costa, G. L. A., de Almeida, M. A. P., Moraes-de-Souza, I., Brito, M. A. D. S. M., Silva, A. R., & Gonçalves-de-Albuquerque, C. F. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1224335 · Cited by 43
Ömür, A. D., & Çoyan, K. (2016) · Veterinární Medicína · doi:10.17221/8677-vetmed · Cited by 40
How do yeast sense mitochondrial dysfunction?
Кнорре, Д. А., Соколов, С. С., Zyrina, A. N., & Severin, F. F. (2016) · Microbial Cell · doi:10.15698/mic2016.11.537 · Cited by 39
Do antibiotics cause mitochondrial and immune cell dysfunction? A literature review
Khpal, M., & Singer, M. (2022) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkac025 · Cited by 38
Redox signaling and reactive oxygen species in hypoxic pulmonary vasoconstriction
Fuchs, B., Sommer, N., Dietrich, A., SCHERMULY, R. T., Ghofrani, H. A., Grimminger, F., Seeger, W., Gudermann, T. W., & Weißmann, N. (2010) · Respiratory Physiology & Neurobiology · doi:10.1016/j.resp.2010.08.013 · Cited by 39
RETRACTED ARTICLE: DDB2, an Essential Mediator of Premature Senescence
Roy, N., Stoyanova, T. I., Dominguez‐Brauer, C., Park, H. J., Bagchi, S., & Raychaudhuri, P. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01480-09 · Cited by 39
RetractedForty years later: Mitochondria as therapeutic targets in muscle diseases
Zulian, A., Schiavone, M., Giorgio, V., & Bernardi, P. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.09.043 · Cited by 40
Krupenko, N. I., Sharma, J., Pediaditakis, P., Helke, K. L., Hall, M. S., Du, X., Sumner, S., & Krupenko, S. A. (2020) · Human Genomics · doi:10.1186/s40246-020-00291-3 · Cited by 39
Forghani, P., Rashid, A., Sun, F., Liu, R., Li, D., Lee, M. R., Hwang, H., Maxwell, J. T., Mandawat, A., Wu, R., et al. (2021) · Journal of the American Heart Association · doi:10.1161/jaha.121.022247 · Cited by 40
Selected Functions and Disorders of Mitochondrial Metabolism under Lead Exposure
Chlubek, M., & Baranowska‐Bosiacka, I. (2024) · Cells · doi:10.3390/cells13141182 · Cited by 43
Wang, S., Zhang, F., Zhao, G., Cheng, Y., Wu, T., Wu, B., & Zhang, Y. (2017) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.13121 · Cited by 38
Handlogten, M. W., Zhu, M., & Ahuja, S. (2018) · Biochemical Engineering Journal · doi:10.1016/j.bej.2018.01.031 · Cited by 38
α-Synuclein aggregation and transmission in Parkinson’s disease: a link to mitochondria and lysosome
Wang, R., Sun, H., Ren, H., & Wang, G. (2020) · Science China Life Sciences · doi:10.1007/s11427-020-1756-9 · Cited by 38
Khan, M. S., Nasiripour, S., & Bopassa, J. C. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26136416 · Cited by 48
Ferroptosis in Cancer and Inflammatory Diseases: Mechanisms and Therapeutic Implications
Shen, G., Liu, J., Wang, Y., Deng, Z., & Deng, F. (2025) · MedComm · doi:10.1002/mco2.70349 · Cited by 47
Structure, Regulation and Biophysics of ICRAC, STIM/Orai1
Derler, I., Madl, J., Schütz, G. J., & Romanin, C. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-2888-2_16 · Cited by 40
Cerium Oxide Nanoparticles for the Treatment of Neurological Oxidative Stress Diseases
Estevez, A. Y., & Erlichman, J. S. (2011) · ACS symposium series · doi:10.1021/bk-2011-1083.ch009 · Cited by 37
Cui, Y., Liu, K. W. K., Liang, Y., Ip, M., & Mak, J. (2017) · Toxicology Letters · doi:10.1016/j.toxlet.2017.01.005 · Cited by 37
Mitochondrial imaging in live or fixed tissues using a luminescent iridium complex
Sorvina, A., Bader, C. A., Darby, J. R. T., Lock, M. C., Soo, J. Y., Johnson, I. R. D., Caporale, C., Voelcker, N. H., Stagni, S., Massi, M., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-24672-w · Cited by 37
Li, S.-M. H., Liu, S., Chang, Y., Ho, C., & Huang, S. (2018) · Journal of Biomedical Science · doi:10.1186/s12929-018-0478-5 · Cited by 40
Banba, A., Tsuji, A., Kimura, H., Murai, M., & Miyoshi, H. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.007687 · Cited by 40
Younas, Z., Mashwani, Z., Ahmad, I., Khan, M., Zaman, S., Sawati, L., & Sohail, S. (2023) · Molecules · doi:10.3390/molecules28031064 · Cited by 37
Dietary Strategies for Relieving Stress in Pet Dogs and Cats
Fan, Z., Bian, Z., Huang, H., Liu, T., Ren, R., Chen, X., Zhang, X., Wang, Y., Deng, B., & Zhang, L. (2023) · Antioxidants · doi:10.3390/antiox12030545 · Cited by 39
The activities of MYC, MNT and the MAX-interactome in lymphocyte proliferation and oncogenesis
Link, J. M., & Hurlin, P. J. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.04.004 · Cited by 36
Wang, H., Zhao, W., Liu, J., Tan, P., Tian, W., & Zhou, B.-H. (2017) · Biological Trace Element Research · doi:10.1007/s12011-017-0983-5 · Cited by 36
Yu, K., Wang, T., Li, Y., Wang, C., Wang, X., Zhang, M., Xie, Y., Li, S., An, Z., & Ye, T. (2017) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2017.05.097 · Cited by 35
Mitoproteomics: Tackling Mitochondrial Dysfunction in Human Disease
Gómez‐Serrano, M., Camafeita, E., Loureiro, M., & Peral, B. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/1435934 · Cited by 38
Reactive oxygen species triggers unconventional secretion of antioxidants and Acb1
Cruz-García, D., Brouwers, N., Malhotra, V., & Curwin, A. J. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.201905028 · Cited by 36
The Role of Melatonin to Ameliorate Oxidative Stress in Sperm Cells
Makris, A., Alevra, A. I., Exadactylos, A., & Papadopoulos, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242015056 · Cited by 39
Synergistic effects of carotenoids: Therapeutic benefits on human health
Islam, F., Khan, J., Zehravi, M., Das, R. C., Haque, M. A., Banu, A., Parwaiz, S., Nainu, F., Nafady, M. H., Shahriar, S. M. S., et al. (2023) · Process Biochemistry · doi:10.1016/j.procbio.2023.11.033 · Cited by 35
Ceruloplasmin Protects Against Rotenone-Induced Oxidative Stress and Neurotoxicity
Hineno, A., Kaneko, K., Yoshida, K., & Ikeda, S. (2011) · Neurochemical Research · doi:10.1007/s11064-011-0537-8 · Cited by 35
da Silva, L. C. N., Alves, N. M. P., de Castro, M. C. A. B., Pereira, V. R. A., Varejão, N., Coelho, L. C. B. B., de Figueiredo, R. C. B. Q., & Correia, M. T. D. S. (2014) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2014.09.045 · Cited by 35
The mitochondrial PKCδ/retinol signal complex exerts real-time control on energy homeostasis
Kim, Y., & Hämmerling, U. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2020.158614 · Cited by 36
Cellular and Functional Physiopathology of Bull Sperm With Altered Sperm Freezability
Hitit, M., Uğur, M. R., Dinh, T. T., Sajeev, D., Kaya, A., Topper, E., Tan, W. F., & Memili, E. (2020) · Frontiers in Veterinary Science · doi:10.3389/fvets.2020.581137 · Cited by 35
Zhu, X., Zhang, Y., Wang, Y., Zhang, H., Wang, X., Tang, H., Huang, H., Zhou, Z., Chen, B., & Sun, L. (2021) · Phytomedicine · doi:10.1016/j.phymed.2021.153807 · Cited by 35
Tomar, N., Zhang, X., Kandel, S. M., Sadri, S., Yang, C., Liang, M., Audi, S. H., Cowley, A. W., & Dash, R. K. (2021) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2021.148518 · Cited by 34
Surin, A. M., Khiroug, S. S., Gorbacheva, L. R., Khodorov, B. I., Pinelis, V. G., & Khiroug, L. (2013) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2012.00102 · Cited by 36
[Mitochondrial reactive oxygen species].
Nishikawa, T., Kukidome, D., & Araki, E. (2016) · PubMed · Cited by 38
Neuroprotection through Stimulation of Mitochondrial Antioxidant Protein Expression
Greco, T., & Fiskum, G. M. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100519 · Cited by 34
Replicative aging as a source of cell heterogeneity in budding yeast
Кнорре, Д. А., Azbarova, A. V., Galkina, K. V., Feniouk, B. A., & Severin, F. F. (2018) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2018.09.001 · Cited by 33
Effects of copper and temperature on heart mitochondrial hydrogen peroxide production
Isei, M. O., & Kamunde, C. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.12.006 · Cited by 35
Glomerular endothelial derived vesicles mediate podocyte dysfunction: A potential role for miRNA
Hill, N. R., Michell, D. L., Ramirez-Solano, M. A., Sheng, Q., Pusey, C. D., Vickers, K. C., & Woollard, K. J. (2020) · PLoS ONE · doi:10.1371/journal.pone.0224852 · Cited by 34
Ashhar, M. U., Vyas, P., Vohora, D., Sahoo, P. K., Nigam, K., Dang, S., Ali, J., & Baboota, S. (2022) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2022.121683 · Cited by 36
Endogenous cross-talk of fungal metabolites
Sheridan, K. J., Dolan, S. K., & Doyle, S. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00732 · Cited by 37
The evolution of individuality revisited
Radzvilavicius, A. L., & Blackstone, N. W. (2018) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12412 · Cited by 38
Sharma, H., Sharma, N., & An, S. S. A. (2023) · Antioxidants · doi:10.3390/antiox12051089 · Cited by 33
NOX-induced oxidative stress is a primary trigger of major neurodegenerative disorders
Zilberter, Y., Tabuena, D. R., & Zilberter, M. Y. (2023) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2023.102539 · Cited by 35
Kamunde, C., Sharaf, M. S., & MacDonald, N. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.05.064 · Cited by 35
Nagy, B., Polak, M., Ozohanics, O., Zámbó, Z., Szabó, E., Hubert, Á., Jordan, F., Nováček, J., Ádám‐Vizi, V., & Ambrus, A. (2021) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2021.129889 · Cited by 33
Atlante, A., & Valenti, D. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242115951 · Cited by 33
Mitochondria: A Promising Convergent Target for the Treatment of Amyotrophic Lateral Sclerosis
Cunha‐Oliveira, T., Montezinho, L., Simões, R. F., de Carvalho, M., Ferreiro, E. B., & Silva, F. S. G. (2024) · Cells · doi:10.3390/cells13030248 · Cited by 34
Dukoff, D. J., Hogg, D. W., Hawrsyh, P. J., & Buck, L. T. (2014) · Journal of Experimental Biology · doi:10.1242/jeb.105825 · Cited by 31
Brito, M. M., Lúcio, C. F., Angrimani, D. D. S. R., Losano, J. D. D. A., Dalmazzo, A., Nichi, M., & Vannucchi, C. I. (2016) · Animal Biotechnology · doi:10.1080/10495398.2016.1203797 · Cited by 32
Sun, D., Gong, L., Xie, J., Gu, X., Li, Y., Cao, Q., Li, Q., Luodan, A., Gu, Z., & Xu, H. (2018) · 中国科学通报:英文版 · doi:10.1016/j.scib.2018.05.037 · Cited by 32
Early life tobacco exposure and children’s telomere length: The HELIX project
Osorio-Yáñez, C., Clemente, D. B. P., Maître, L., Vives-Usano, M., Bustamante, M., Martinez, D. R., Casas, M., Alexander, J., Thomsen, C., Chatzi, L., et al. (2019) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2019.135028 · Cited by 32
Manoeuvrability and biocompatibility of endodontic tricalcium silicate-based putties
Sun, Q., Meng, M., Steed, J. N., Sidow, S. J., Bergeron, B. E., Niu, L., Ma, J.-Z., & Tay, F. R. (2020) · Journal of Dentistry · doi:10.1016/j.jdent.2020.103530 · Cited by 35
The FOXO signaling axis displays conjoined functions in redox homeostasis and stemness
Soh, R., Hardy, A., & Nieden, N. I. Z. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.04.022 · Cited by 33
Nakao, K., Minato, N., & Üemoto, S. (2015) · Springer eBooks · doi:10.1007/978-4-431-55651-0 · Cited by 34
Bidooki, S. H., Alejo, T., Sánchez-Marco, J., Martínez‐Beamonte, R., Abuobeid, R., Burillo, J. C., Lasheras, R., Sebastián, V., Rodriguez‐Yoldi, M. J., Arruebo, M., et al. (2022) · Antioxidants · doi:10.3390/antiox11030581 · Cited by 32
Santos, F. M., Mesquita, J., Sousa, J. P. C., Ciordia, S., Paradela, A., & Tomaz, C. T. (2022) · Antioxidants · doi:10.3390/antiox11030505 · Cited by 32
Kôrge, P., Calmettes, G., John, S., & Weiss, J. N. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.768317 · Cited by 32
Dai, X., Sun, F., Deng, K., Lin, G., Yin, W., Chen, H., Yang, D., Liu, K., Zhang, Y., & Huang, L. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232214217 · Cited by 32
Mechanism of chronic dietary iron overload-induced liver damage in mice
Liu, D., He, H., Yin, D., Que, A.-L., Tang, L., Liao, Z., Huang, Q., & He, M. L. (2013) · Molecular Medicine Reports · doi:10.3892/mmr.2013.1316 · Cited by 32
Zoccarato, F., Cavallini, L., & Alexandre, A. (2009) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-009-9238-2 · Cited by 31
Preserving organelle vitality: peroxisomal quality control mechanisms in yeast
Aksam, E. B., de Vries, B., van der Klei, I. J., & Kiel, J. A. K. W. (2009) · FEMS Yeast Research · doi:10.1111/j.1567-1364.2009.00534.x · Cited by 32
Sil, S., Ghosh, T., Ghosh, R., & Gupta, P. (2016) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2016.12.007 · Cited by 31
He, B., Wang, X., Zhu, J., Kong, B., Wei, L. J., Jin, Y., & Fu, Z. (2019) · Environmental Pollution · doi:10.1016/j.envpol.2019.04.044 · Cited by 31
Li, G., Liao, Y., Hu, J., Lu, L., Zhang, Y., Li, B., & An, T. (2019) · Environmental Pollution · doi:10.1016/j.envpol.2019.06.059 · Cited by 31
Woźniak, E., Broncel, M., Bukowska, B., & Gorzelak‐Pabiś, P. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21061953 · Cited by 31
Free Radical Medicine and Biology
Das, K. K., Das, S. N., Biradar, M. S., Bobbarala, V., & Tata, S. S. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.77829 · Cited by 32
COL8A2 Regulates the Fate of Corneal Endothelial Cells
Hwang, J. S., Ma, D. J., Choi, J., & Shin, Y. J. (2020) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.61.11.26 · Cited by 32
Photobiomodulation of mineralisation in mesenchymal stem cells
Mohamad, S. A., Milward, M. R., Hadis, M. A., Kuehne, S. A., & Cooper, P. R. (2021) · Photochemical & Photobiological Sciences · doi:10.1007/s43630-021-00047-5 · Cited by 33
Roles of Phase Separation for Cellular Redox Maintenance
Saito, Y., & Kimura, W. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.691946 · Cited by 30
Skulachev, V. P., Vyssokikh, M. Y., Chernyak, B. V., Mulkidjanian, A. Y., Skulachev, M. V., Shilovsky, G. A., Lyamzaev, K. G., Borisov, V. B., Severin, F. F., & Садовничий, В. А. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241612540 · Cited by 35
Unifying mechanism behind the onset of acquired epilepsy
Zilberter, Y., Popova, I. Y., & Zilberter, M. Y. (2021) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2021.11.009 · Cited by 32
Sun, Y., Kinsela, A. S., & Waite, T. D. (2022) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2022.153727 · Cited by 30
Bai, L., Xu, X., Wang, Q., Xu, S., Ju, W., Wang, X., Chen, W., He, W., Tang, H., & Lin, Y. (2012) · Molecular Pharmacology · doi:10.1124/mol.111.076653 · Cited by 30
Mitochondria-Mediated Anticancer Effects of Non-Thermal Atmospheric Plasma
Zhunussova, A., Vitol, E. A., Polyak, B., Tuleukhanov, S. T., Brooks, A. D., Sensenig, R., Friedman, G., & Orynbayeva, Z. (2016) · PLoS ONE · doi:10.1371/journal.pone.0156818 · Cited by 32
Gureev, A. P., Syromyatnikov, M., Gorbacheva, T., Starkov, A. A., & Popov, V. N. (2016) · Neuroscience Research · doi:10.1016/j.neures.2016.07.006 · Cited by 30
Self-citationZyrina, A. N., Smirnova, E. A., Маркова, О. В., Severin, F. F., & Кнорре, Д. А. (2016) · Applied and Environmental Microbiology · doi:10.1128/aem.02759-16 · Cited by 31
Hedges, C. P., Wilkinson, R. T., Devaux, J. B. L., & Hickey, A. J. (2019) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/j.cbpa.2019.01.002 · Cited by 29
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Lee, H., Gu, M. J., Lee, J., Lee, S., Kim, Y., & Ha, S. K. (2021) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.202000799 · Cited by 29
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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