Production of Reactive Oxygen Species by Mitochondria

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

Topology of superoxide production from different sites in the mitochondrial electron transport chain

St-Pierre, J., Buckingham, J. A., Roebuck, S. J., & Brand, M. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207217200 · Cited by 1,545

Complete Structure of the 11-Subunit Bovine Mitochondrial Cytochrome bc 1 Complex

Iwata, S., Lee, J. W., Okada, K., Lee, J. K., Iwata, M., Rasmussen, B., Link, T. A., Ramaswamy, S., & Jap, B. K. (1998) · Science · doi:10.1126/science.281.5373.64 · Cited by 1,253

Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria

Turrens, J. F., Alexandre, A., & Lehninger, A. L. (1985) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(85)90293-0 · Cited by 1,214

Oxygen activation and the conservation of energy in cell respiration

Babcock, Ǵ., & Wikström, M. K. F. (1992) · Nature · doi:10.1038/356301a0 · Cited by 1,126

Biochemical properties of subsarcolemmal and interfibrillar mitochondria isolated from rat cardiac muscle

Palmer, J. W., Tandler, B., & Hoppel, C. L. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)75283-1 · Cited by 830

Mitochondrial Dysfunction in Cardiac Disease: Ischemia–Reperfusion, Aging, and Heart Failure

Lesnefsky, E. J., Moghaddas, S., Tandler, B., Kerner, J., & Hoppel, C. L. (2001) · Journal of Molecular and Cellular Cardiology · doi:10.1006/jmcc.2001.1378 · Cited by 719

Voltage-dependent anion channels control the release of the superoxide anion from mitochondria to cytosol

Han, D., Antunes, F., Canali, R., Rettori, D., & Cadenas, E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210269200 · Cited by 711

The protonmotive Q cycle. Energy transduction by coupling of proton translocation to electron transfer by the cytochrome bc1 complex.

Trumpower, B. L. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38410-8 · Cited by 598

Detection of catalase in rat heart mitochondria.

Radi, R., Turrens, J. F., Chang, L. Y., Bush, K. M., Crapo, J. D., & Freeman, B. A. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54740-2 · Cited by 573

Reversible Blockade of Complex I or Inhibition of PKCβ Reduces Activation and Mitochondria Translocation of p66Shc to Preserve Cardiac Function after Ischemia

Yang, M., Stowe, D. F., Udoh, K. B., Heisner, J. S., & Camara, A. K. S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0113534 · Cited by 29

Cross‐talk between L‐type Ca2+ channels and mitochondria

Viola, H. M., & Hool, L. C. (2009) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/j.1440-1681.2009.05277.x · Cited by 29

Effects of a high fat diet on liver mitochondria: increased ATP-sensitive K+ channel activity and reactive oxygen species generation

Cardoso, A. R., Cabral‐Costa, J. V., & Kowaltowski, A. J. (2010) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-010-9284-9 · Cited by 31

Mitochondria and NADPH oxidases are the major sources of TNF-α/cycloheximide-induced oxidative stress in murine intestinal epithelial MODE-K cells

Babu, D., Leclercq, G., Goossens, V., Berghe, T. V., Hamme, E. V., Vandenabeele, P., & Lefebvre, R. A. (2015) · Cellular Signalling · doi:10.1016/j.cellsig.2015.02.019 · Cited by 29

Controlled curcumin release via conjugation into PBAE nanogels enhances mitochondrial protection against oxidative stress

Gupta, P., Jordan, C. T., Mitov, M. I., Butterfield, D. A., Hilt, J. Z., & Dziubla, T. D. (2016) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2016.07.071 · Cited by 29

Mitochondrial Changes in Cancer

Rao, S. G. (2016) · Handbook of experimental pharmacology · doi:10.1007/164_2016_40 · Cited by 30

Effects of obesity and weight loss on mitochondrial structure and function and implications for colorectal cancer risk

Breininger, S. P., Malcomson, F. C., Afshar, S., Turnbull, D. M., Greaves, L. C., & Mathers, J. C. (2019) · Proceedings of The Nutrition Society · doi:10.1017/s0029665119000533 · Cited by 30

Fighting Cancer with Photodynamic Therapy and Nanotechnologies: Current Challenges and Future Directions

Ailioaie, L. M., Ailioaie, C., & Litscher, G. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26072969 · Cited by 34

Selenofuranoside Ameliorates Memory Loss in Alzheimer-Like Sporadic Dementia: AChE Activity, Oxidative Stress, and Inflammation Involvement

Spiazzi, C. C., Soares, M. B., Izaguirry, A. P., Vargas, L., Zanchi, M. M., Pavin, N. F., Affeldt, R. F., Lüdtke, D. S., Prigol, M., & Cibin, F. W. S. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/976908 · Cited by 28

BDE-154 Induces Mitochondrial Permeability Transition and Impairs Mitochondrial Bioenergetics

Pereira, L. C., Miranda, L. F. C., de Souza, A. O., & Dorta, D. J. (2014) · Journal of Toxicology and Environmental Health · doi:10.1080/15287394.2014.861337 · Cited by 28

Sepsis-induced Cardiac Mitochondrial Damage and Potential Therapeutic Interventions in the Elderly

Zang, Q. S. (2014) · Aging and Disease · doi:10.14336/ad.2014.0500137 · Cited by 28

Influence of a Hyperglycemic Microenvironment on a Diabetic Versus Healthy Rat Vascular Endothelium Reveals Distinguishable Mechanistic and Phenotypic Responses

Haspula, D., Vallejos, A. K., Moore, T. M., Tomar, N., Dash, R. K., & Hoffmann, B. R. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00558 · Cited by 28

Complex I and ATP synthase mediate membrane depolarization and matrix acidification by isoflurane in mitochondria

Pravdić, D., Hirata, N., Barber, L., Sedlić, F., Bosnjak, Z. J., & Bienengraeber, M. (2012) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2012.07.003 · Cited by 28

Cytochrome c signalosome in mitochondria

Díaz‐Moreno, I., García-Heredia, J. M., Dı́az-Quintana, A., & la Rosa, M. Á. D. (2011) · European Biophysics Journal · doi:10.1007/s00249-011-0774-4 · Cited by 29

Selectivity in ROS-Induced Peptide Backbone Bond Cleavage

Stringfellow, H. M., Jones, M. R., Green, M. C., Wilson, A. K., & Francisco, J. S. (2014) · The Journal of Physical Chemistry A · doi:10.1021/jp508877m · Cited by 28

Mitochondrion-associated protein peroxiredoxin 3 promotes benign prostatic hyperplasia through autophagy suppression and pyroptosis activation

Jiang, M., Han, Z., Li, W., Yue, F., Ye, J., Li, B., Cai, Z., Lü, J., Dong, W., Jiang, X., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.17927 · Cited by 28

Protective effect ofMomordica charantiawater extract against liver injury in restraint-stressed mice and the underlying mechanism

Deng, Y., Tang, Q., Zhang, Y., Zhang, R., Wei, Z., Tang, X., & Zhang, M. (2017) · Food & Nutrition Research · doi:10.1080/16546628.2017.1348864 · Cited by 28

Inhibition of Qi site of mitochondrial complex III with antimycin A decreases persistent and transient sodium currents via reactive oxygen species and protein kinase C in rat hippocampal CA1 cells

Lai, B., Zhang, L., Dong, L.-Y., Zhu, Y., Sun, F., & Zheng, P. (2005) · Experimental Neurology · doi:10.1016/j.expneurol.2005.03.005 · Cited by 28

Mitochondrial electron transport is inhibited by disappearance of metallothionein in human bronchial epithelial cells following exposure to silver nitrate

Miyayama, T., Arai, Y., Suzuki, N., & Hirano, S. (2013) · Toxicology · doi:10.1016/j.tox.2013.01.004 · Cited by 27

Exposure to lethal levels of benzo[ a ]pyrene or cadmium trigger distinct protein expression patterns in earthworms ( Eisenia fetida )

Zhang, L., Duan, X., He, N., Chen, X., Shi, J., Li, W., Xu, L., & Li, H. (2017) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2017.04.003 · Cited by 27

Cocoa flavanols, Nrf2 activation, and oxidative stress in peripheral artery disease: mechanistic findings in muscle based on outcomes from a randomized trial

Ismaeel, A., McDermott, M. M., Joshi, J. K., Sturgis, J. C., Zhang, D., Ho, K. J., Sufit, R. L., Ferrucci, L., Peterson, C. A., & Kosmac, K. (2024) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00573.2023 · Cited by 29

Cardiac proteomic responses to ischemia–reperfusion injury and ischemic preconditioning

Kim, H. K., Thu, V. T., Heo, H.-J., Kim, N., & Han, J. (2011) · Expert Review of Proteomics · doi:10.1586/epr.11.8 · Cited by 27

B7-H4 downregulation induces mitochondrial dysfunction and enhances doxorubicin sensitivity via the cAMP/CREB/PGC1-α signaling pathway in HeLa cells

Kim, H. K., Song, I.-S., Lee, S. Y., Jeong, S. H., Lee, S. R., Heo, H. J., Thu, V. T., Kim, N., Ko, K. S., Rhee, B. D., et al. (2014) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-014-1493-3 · Cited by 27

A traditional Chinese medicine JiuHuangLian (Rhizoma coptidis steamed with rice wine) reduces oxidative stress injury in type 2 diabetic rats

Li, J., Shen, X., & Meng, X. (2013) · Food and Chemical Toxicology · doi:10.1016/j.fct.2013.06.005 · Cited by 27

Molecular Cytotoxicity Mechanisms of Allyl Alcohol (Acrolein) in Budding Yeast

Golla, U., Bandi, G., & Tomar, R. S. (2015) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.5b00071 · Cited by 27

Oxidative lung injury correlates with one-lung ventilation time during pulmonary lobectomy: a study of exhaled breath condensate and blood

García‐de‐la‐Asunción, J., del Olmo, E. G., Perez-Griera, J., Martí, F., Galán, G., Aixelá, A. M., Wins, R., Guijarro, R., Arnau, A., Sarriá, B., et al. (2015) · European Journal of Cardio-Thoracic Surgery · doi:10.1093/ejcts/ezv207 · Cited by 30

Air pollution particles and iron homeostasis

Ghio, A. J., Soukup, J. M., & Dailey, L. A. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.05.026 · Cited by 27

Mcl-1 regulates reactive oxygen species via NOX4 during chemotherapy-induced senescence

Demelash, A., Pfannenstiel, L. W., Liu, L., & Gastman, B. (2017) · Oncotarget · doi:10.18632/oncotarget.15962 · Cited by 27

Pleiotropic Effects of Biguanides on Mitochondrial Reactive Oxygen Species Production

Pecinová, A., Drahota, Z., Kovalcikova, J., Kovářová, N., Pecina, P., Alán, L., Zima, M., Houštěk, J., & Mráček, T. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/7038603 · Cited by 27

Cross Talk Between Mitochondrial Reactive Oxygen Species and Sarcoplasmic Reticulum Calcium in Pulmonary Arterial Smooth Muscle Cells

Song, T., Zheng, Y., & Wang, Y.-X. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-63245-2_17 · Cited by 27

Department of Veterans Affairs Geriatric Research, Education and Clinical Centers: Translating Aging Research into Clinical Geriatrics

Supiano, M. A., Alessi, C., Chernoff, R., Goldberg, A., Morley, J. E., Schmader, K. E., & Shay, K. (2012) · Journal of the American Geriatrics Society · doi:10.1111/j.1532-5415.2012.04004.x · Cited by 27

Mitochondrial metabolism regulation and epigenetics in hypoxia

Laird, M., Ku, J. C., Raiten, J., Sriram, S., Moore, M., & Li, Y. (2024) · Frontiers in Physiology · doi:10.3389/fphys.2024.1393232 · Cited by 26

Lipid oxidation in minced beef meat with added Krebs cycle substrates to stabilise colour

Yi, G., Grabež, V., Bjelanović, M., Slinde, E., Olsen, K., Langsrud, Ø., Phung, V. T., Haug, A., Oostindjer, M., & Egelandsdal, B. (2015) · Food Chemistry · doi:10.1016/j.foodchem.2015.04.002 · Cited by 26

Hypothesis for the Mechanism of Ascorbic Acid Activity in Living Cells Related to Its Electron-Accepting Properties

Pshenichnyuk, S. A., Modelli, A., Lazneva, E. F., & Komolov, А. S. (2016) · The Journal of Physical Chemistry A · doi:10.1021/acs.jpca.6b02272 · Cited by 26

Optimization of a diagnostic platform for oxidation–reduction potential (ORP) measurement in human plasma

Polson, D. A., Villalba, N., & Freeman, K. (2018) · Redox Report · doi:10.1080/13510002.2018.1456000 · Cited by 26

(–)-Epicatechin Modulates Mitochondrial Redox in Vascular Cell Models of Oxidative Stress

Keller, A. C., Hull, S., Elajaili, H. B., Johnston, A., Knaub, L. A., Chun, J. H., Walker, L. A., Nozik‐Grayck, E., & Reusch, J. E. B. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/6392629 · Cited by 26

EFHD1 ablation inhibits cardiac mitoflash activation and protects cardiomyocytes from ischemia

Eberhardt, D., Lee, S. H., Yin, X., Balynas, A. M., Rekate, E. C., Kraiss, J. N., Lang, M. J., Walsh, M., Streiff, M. E., Corbin, A. C., et al. (2022) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2022.03.002 · Cited by 26

Mitochondrial ROS signalling requires uninterrupted electron flow and is lost during ageing in flies

Graham, C., Stefanatos, R. K. A., Yek, A. E. H., Spriggs, R. V., Loh, S. H. Y., Uribe, A. H., Zhang, T., Martins, L. M., Maddocks, O. D. K., Scialò, F., et al. (2022) · GeroScience · doi:10.1007/s11357-022-00555-x · Cited by 28

Sirtuins and redox signaling interplay in neurogenesis, neurodegenerative diseases, and neural cell reprogramming

Mormone, E., Iorio, E. L., Abate, L., & Rodolfo, C. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1073689 · Cited by 31

The Role of P53 in Myocardial Ischemia-Reperfusion Injury

Zhu, X.-Z., Qiu, Z., Lei, S., Leng, Y., Li, W., & Xia, Z. (2023) · Cardiovascular Drugs and Therapy · doi:10.1007/s10557-023-07480-x · Cited by 26

Inhibition of the mitochondrial respiratory chain function abrogates quartz induced DNA damage in lung epithelial cells

Li, H., Haberzettl, P., Albrecht, C., Höhr, D., Knaapen, A. M., Borm, P. J. A., & Schins, R. P. F. (2006) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2006.12.001 · Cited by 26

Superoxide dismutase deficiency enhances superoxide levels in brain tissues during oxygenation and hypoxia‐reoxygenation

Sasaki, T., Shimizu, T., Koyama, T., Sakai, M., Uchiyama, S., Kawakami, S., Noda, Y., Shirasawa, T., & Kojima, S. (2011) · Journal of Neuroscience Research · doi:10.1002/jnr.22581 · Cited by 26

Lidocaine depolarizes the mitochondrial membrane potential by intracellular alkalization in rat dorsal root ganglion neurons

Onizuka, S., Yonaha, T., Tamura, R., Kashiwada, M., Shirasaka, T., & Tsuneyoshi, I. (2011) · Journal of Anesthesia · doi:10.1007/s00540-010-1079-y · Cited by 26

Metabolic profile of the brown macroalga Sargassum cymosum (Phaeophyceae, Fucales) under laboratory UV radiation and salinity conditions

Polo, L. K., Felix, M. R. D. L., Kreusch, M., Pereira, D. T., Costa, G. B., Simioni, C., Martins, R. D. P., Latini, A., Floh, E. I. S., Chow, F., et al. (2014) · Journal of Applied Phycology · doi:10.1007/s10811-014-0381-8 · Cited by 27

Phyllanthus urinaria induces mitochondrial dysfunction in human osteosarcoma 143B cells associated with modulation of mitochondrial fission/fusion proteins

Huang, S., Bi, K.-W., Kuo, H., Lin, T., Liao, P.-L., Wang, P., Chuang, J., & Liou, C. (2014) · Mitochondrion · doi:10.1016/j.mito.2014.05.002 · Cited by 26

Usurping the mitochondrial supremacy: Extramitochondrial sources of reactive oxygen intermediates and their role in beta cell metabolism and insulin secretion

Gray, J. P., & Heart, E. A. (2010) · Toxicology Mechanisms and Methods · doi:10.3109/15376511003695181 · Cited by 27

Mitochondria-dependent regulation of Kv currents in rat pulmonary artery smooth muscle cells

Firth, A. L., Yuill, K. H., & Sv, S. (2008) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.90243.2008 · Cited by 26

Effect of oxidative phosphorylation signaling pathway on silkworm midgut following exposure to phoxim

Li, F., Xu, K., Ni, M., Wang, B., Gu, Z., Shen, W., & Li, B. (2015) · Environmental Toxicology · doi:10.1002/tox.22222 · Cited by 27

The antioxidant effect of mulberry and jamun fruit wines by ameliorating oxidative stress in streptozotocin-induced diabetic Wistar rats

Srikanta, A. H., Kumar, A., Sukhdeo, S. V., Peddha, M. S., & Govindaswamy, V. (2016) · Food & Function · doi:10.1039/c6fo00372a · Cited by 26

Role of transition metals present in air particulate matter on lung oxygen metabolism

Magnani, N., Marchini, T., Garcés, M., Mebert, A. M., Cáceres, L., Díaz, L. E., Desimone, M. F., & Evelson, P. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.10.009 · Cited by 26

Distinct radiation responses after in vitro mtDNA depletion are potentially related to oxidative stress

van Gisbergen, M. W., Voets, A. M., Biemans, R., Hoffmann, R. F., Drittij-Reijnders, M.-J., Haenen, G. R. M. M., Heijink, I. H., Rouschop, K. M. A., Dubois, L. J., & Lambin, P. (2017) · PLoS ONE · doi:10.1371/journal.pone.0182508 · Cited by 28

Oxidative stress, metabolic and mitochondrial abnormalities associated with autism spectrum disorder

Thorsen, M. (2020) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2020.04.018 · Cited by 26

VCP relocalization limits mitochondrial activity, GSH depletion and ferroptosis during starvation in PC3 prostate cancer cells

Ogor, P., Yoshida, T., Koike, M., & Kakizuka, A. (2021) · Genes to Cells · doi:10.1111/gtc.12872 · Cited by 26

Estrogen-related receptor alpha (ERRα) is a key regulator of intestinal homeostasis and protects against colitis

Tran, A., Scholtes, C., Songane, M., Champagne, C., Galarneau, L., Levasseur, M.-P., Fodil, N., Dufour, C. R., Giguère, V., & Saleh, M. (2021) · Scientific Reports · doi:10.1038/s41598-021-94499-5 · Cited by 27

Anti-apoptotic activity of the glutathione peroxidase homologue encoded by HIV-1

COHEN, I. R., Boya, P., Zhao, L., Métivier, D., Andréau, K., Perfettini, J., Weaver, J., Badley, A. D., Taylor, E. W., & Kroemer, G. (2004) · APOPTOSIS · doi:10.1023/b:appt.0000018800.87358.ba · Cited by 26

Mitochondrial Metabolic Suppression in Fasting and Daily Torpor: Consequences for Reactive Oxygen Species Production

Brown, J. C. L., & Staples, J. F. (2011) · Physiological and Biochemical Zoology · doi:10.1086/661639 · Cited by 28

UQCRH downregulation promotes Warburg effect in renal cell carcinoma cells

Luo, Y., Bengtsson, L. M., Wang, X., Huang, T., Liu, G., Murphy, S. P., Wang, C., Koren, J., Schafer, Z. T., & Lü, X. (2020) · Scientific Reports · doi:10.1038/s41598-020-72107-2 · Cited by 27

The role of mitochondrial oxidative stress and the tumor microenvironment in radiation-related cancer

Shimura, T. (2020) · Journal of Radiation Research · doi:10.1093/jrr/rraa090 · Cited by 26

Chlorogenic Acid Ameliorates Damage Induced by Fluorene-9-Bisphenol in Porcine Sertoli Cells

Zhang, S., Sun, B., Wang, D., Liu, Y., Li, J., Qi, J., Zhang, Y., Bai, C., & Liang, S. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.678772 · Cited by 25

Mitochondrial oxygen sensing of acute hypoxia in specialized cells - Is there a unifying mechanism?

Pak, O., Nolte, A., Knoepp, F., Giordano, L., Pecina, P., Hüttemann, M., Grossman, L. I., Weißmann, N., & Sommer, N. (2022) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2022.148911 · Cited by 25

Mitochondrial adaptations to calorie restriction and bariatric surgery in human skeletal muscle: a systematic review with meta-analysis

Pérez-Rodríguez, M., Huertas, J. R., Villalba, J. M., & Casuso, R. A. (2022) · Metabolism · doi:10.1016/j.metabol.2022.155336 · Cited by 26

An ursolic acid-enriched extract of Cynomorium songaricum protects against carbon tetrachloride hepatotoxicity and gentamicin nephrotoxicity in rats possibly through a mitochondrial pathway: A comparison with ursolic acid

Chen, J., Wong, H. S., Leung, H. Y., Leong, P. K., Chan, W. M., Chen, N., & Ko, K. M. (2014) · Journal of Functional Foods · doi:10.1016/j.jff.2014.01.027 · Cited by 25

Cardioprotection by modulation of mitochondrial respiration during ischemia–reperfusion: Role of apoptosis-inducing factor

Xu, A., Szczepanek, K., Hu, Y., Lesnefsky, E. J., & Chen, Q. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.05.033 · Cited by 25

Ca2+–CaM regulating viability of Candida guilliermondii under oxidative stress by acting on detergent resistant membrane proteins

An, B., Chen, Y., Li, B., Qin, G., & Tian, S. (2014) · Journal of Proteomics · doi:10.1016/j.jprot.2014.06.022 · Cited by 25

Ischemic preconditioning preserves mitochondrial membrane potential and limits reactive oxygen species production

Quarrie, R., Lee, D. S., Steinbaugh, G. E., Cramer, B., Erdahl, W. L., Pfeiffer, D. R., Zweier, J. L., & Crestanello, J. A. (2012) · Journal of Surgical Research · doi:10.1016/j.jss.2012.05.090 · Cited by 25

Dephosphorylation of the Rieske iron–sulfur protein after induction of the mitochondrial permeability transition

He, L., & Lemasters, J. J. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.06.170 · Cited by 26

Importance of Toll-like Receptor 2 in Mitochondrial Dysfunction during Polymicrobial Sepsis

Gong, Y., Zou, L., Feng, Y., Li, D., Cai, J., Chen, D., & Chao, W. (2014) · Anesthesiology · doi:10.1097/aln.0000000000000470 · Cited by 26

Age-related deficiencies in complex I endogenous substrate availability and reserve capacity of complex IV in cortical neuron electron transport

Jones, T. T., & Brewer, G. J. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.09.009 · Cited by 25

ROS-Inducing Agents for Cancer Chemotherapy

Kasiappan, R., & Safe, S. H. (2016) · Reactive Oxygen Species · doi:10.20455/ros.2016.805 · Cited by 27

ATP5B regulates mitochondrial fission and fusion in mammalian cells

Seo, H., Lee, I., Chung, H. S., Bae, G., Chang, M., Song, E., & Kim, J. M. (2016) · Animal Cells and Systems · doi:10.1080/19768354.2016.1188855 · Cited by 25

Thymoquinone, a biologically active component of Nigella sativa, induces mitochondrial production of reactive oxygen species and programmed death of tumor cells

Мартинович, Г. Г., Martinovich, I. V., Вчерашняя, А. В., Шадыро, О. И., & Cherenkevich, S. N. (2016) · BIOPHYSICS · doi:10.1134/s0006350916060154 · Cited by 25

Pandora's Box: mitochondrial defects in ischaemic heart disease and stroke

Andalib, S., Divani, A. A., Michel, T. M., Høilund‐Carlsen, P. F., Vafaee, M. S., & GJEDDE, A. H. (2017) · Expert Reviews in Molecular Medicine · doi:10.1017/erm.2017.5 · Cited by 25

ROS-induced near-homozygous genomes in thyroid cancer

Corver, W. E., Demmers, J. J. P. G., Oosting, J., Sahraeian, S., Boot, A., Ruano, D., van Wezel, T., & Morreau, H. M. (2017) · Endocrine Related Cancer · doi:10.1530/erc-17-0288 · Cited by 25

Characterization of the Mitochondrial Aerobic Metabolism in the Pre- and Perisynaptic Districts of the SOD1G93A Mouse Model of Amyotrophic Lateral Sclerosis

Ravera, S., Bonifacino, T., Bartolucci, M., Milanese, M., Gallia, E., Provenzano, F., Cortese, K., Panfoli, I., & Bonanno, G. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1059-z · Cited by 25

Detection of hydrogen peroxide production in the isolated rat lung using Amplex red

Audi, S. H., Friedly, N., Dash, R. K., Beyer, A., Clough, A. V., & Jacobs, E. R. (2018) · Free Radical Research · doi:10.1080/10715762.2018.1511051 · Cited by 25

Calcium overload decreases net free radical emission in cardiac mitochondria

Duong, Q. V., Hoffman, A., Zhong, K., Dessinger, M. J., Zhang, Y., & Bazil, J. N. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.01.005 · Cited by 25

CUT Domain Proteins in DNA Repair and Cancer

Ramdzan, Z. M., Vickridge, E., Faraco, C. C. F., & Nepveu, A. (2021) · Cancers · doi:10.3390/cancers13122953 · Cited by 26

Relevance of mitochondrial oxidative stress to arrhythmias: Innovative concepts to target treatments

Liu, C., Ma, N., Guo, Z., Zhang, Y., Zhang, J., Yang, F., Su, X., Zhang, G., Xiong, X., & Xing, Y. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.106027 · Cited by 25

Antioxidant activity in Spalax ehrenbergi: a possible adaptation to underground stress

Caballero, B., Tomás‐Zapico, C., Vega‐Naredo, I., Sierra, V., Tolivia, D., Hardeland, R., Rodríguez‐Colunga, M. J., Joel, A., Nevo, E., Avivi, A., et al. (2006) · Journal of Comparative Physiology A · doi:10.1007/s00359-006-0111-z · Cited by 25

Role of Endothelial Mitochondria in Oxidant Production and Modulation of Neutrophil Adherence

Ichikawa, H., Kokura, S., & Aw, T. Y. (2004) · Journal of Vascular Research · doi:10.1159/000081466 · Cited by 25

Ammonium‐dependent hydrogen peroxide production by mitochondria

Grivennikova, V. G., Cecchini, G., & Vinogradov, A. D. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.06.054 · Cited by 25

MITOCHONDRIAL COMPLEX III IS INVOLVED IN PROAPOPTOTIC BAK-INDUCED MICROVASCULAR ENDOTHELIAL CELL HYPERPERMEABILITY

Childs, E. W., Tharakan, B., Hunter, F. A., Isong, M., & Liggins, N. D. (2008) · Shock · doi:10.1097/shk.0b013e318157f524 · Cited by 25

Synthesis, crystal structure and antiradical effect of copper(ii) Schiff base complexes containing five-, six- and unusual seven-membered rings

Tokárová, Z., Valentová, J., Bojkova, Z., Kožı́šek, J., & Devı́nsky, F. (2011) · Dalton Transactions · doi:10.1039/c0dt00901f · Cited by 25

Immunolocalization of leptin and its receptor in the sheep ovary and in vitro effect of leptin on follicular development and oocyte maturation

Macedo, T. J. S., Santos, J. M. S., Bezerra, M. É. S., Menezes, V. G., Gouveia, B. B., Barbosa, L. M. R., Lins, T. L. B. G., do Monte, A. P. O., Barberino, R. S., Batista, A. M., et al. (2019) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2019.110506 · Cited by 24

Differential regulation of mitochondrial complex I and oxidative stress based on metastatic potential of colorectal cancer cells

Rai, N. K., Mathur, S., Singh, S. K., Tiwari, M., Singh, V. K., Haque, R., Tiwari, S., & Sharma, L. K. (2020) · Oncology Letters · doi:10.3892/ol.2020.12176 · Cited by 24

Targeting Mitophagy in Alzheimer’s Disease

Jayatunga, D. P. W., Hone, E., Bharadwaj, P., Garg, M. L., Verdile, G., Guillemin, G. J., & Martins, R. N. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-191258 · Cited by 25

Calpain-mediated protein targets in cardiac mitochondria following ischemia–reperfusion

Li, L., Thompson, J., Hu, Y., Lesnefsky, E. J., Willard, B. B., & Chen, Q. (2022) · Scientific Reports · doi:10.1038/s41598-021-03947-9 · Cited by 24

Palladium α-lipoic acid complex formulation enhances activities of Krebs cycle dehydrogenases and respiratory complexes I–IV in the heart of aged rats

Sudheesh, N. P., Ajith, T. A., Janardhanan, K. K., & Krishnan, C. V. (2009) · Food and Chemical Toxicology · doi:10.1016/j.fct.2009.05.032 · Cited by 24

Reactive oxygen species-independent rapid initiation of mitochondrial apoptotic pathway by chelerythrine

Funakoshi, T., Aki, T., Nakayama, H., Watanuki, Y., Imori, S., & Uemura, K. (2011) · Toxicology in Vitro · doi:10.1016/j.tiv.2011.05.028 · Cited by 24

Qo site of mitochondrial complex III is the source of increased superoxide after transient exposure to hydrogen peroxide

Viola, H. M., & Hool, L. C. (2010) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2010.07.015 · Cited by 24

Increased myocardial vulnerability to ischemia–reperfusion injury in the presence of left ventricular hypertrophy

Mølgaard, S., Faricelli, B., Salomonsson, M., Engstrøm, T., & Treiman, M. (2016) · Journal of Hypertension · doi:10.1097/hjh.0000000000000826 · Cited by 24

Glutathionylated and Fe–S cluster containing hMIA40 (CHCHD4) regulates ROS and mitochondrial complex III and IV activities of the electron transport chain

Thiriveedi, V., Mattam, U., Pattabhi, P., Bisoyi, V., Talari, N. K., Krishnamoorthy, T., & Sepuri, N. B. V. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101725 · Cited by 24

Identification of a Redox-Modulatory Interaction Between Uncoupling Protein 3 and Thioredoxin 2 in the Mitochondrial Intermembrane Space

Hirasaka, K., Lago, C. U., Kenaston, M. A., Fathe, K., Nowinski, S. M., Nikawa, T., & Mills, E. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.3888 · Cited by 24

Editor’s Highlight: Therapeutic Concentrations of Antidepressants Inhibit Pancreatic Beta-Cell Function via Mitochondrial Complex Inhibition

Elmorsy, E. M., Al-Ghafari, A. B., Helaly, A. M., Hisab, A. S., Oehrle, B., & Smith, P. A. (2017) · Toxicological Sciences · doi:10.1093/toxsci/kfx090 · Cited by 24

PPARγ-Independent Side Effects of Thiazolidinediones on Mitochondrial Redox State in Rat Isolated Hearts

Riess, M. L., Elorbany, R., Weihrauch, D., Stowe, D. F., & Camara, A. K. S. (2020) · Cells · doi:10.3390/cells9010252 · Cited by 23

Sestrins: Darkhorse in the regulation of mitochondrial health and metabolism

Kumar, A. A., Dhiman, D., & Shaha, C. (2020) · Molecular Biology Reports · doi:10.1007/s11033-020-05769-w · Cited by 23

Antimycin A-induced mitochondrial dysfunction regulates inflammasome signaling in human retinal pigment epithelial cells

Korhonen, E., Hytti, M., Piippo, N., Kaarniranta, K., & Kauppinen, A. (2021) · Experimental Eye Research · doi:10.1016/j.exer.2021.108687 · Cited by 23

Emerging antioxidant therapies in Friedreich’s ataxia

Edzeamey, F. J., Ramchunder, Z., Pourzand, C., & Virmouni, S. A. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1359618 · Cited by 23

Balanced Duality: H2O2-Based Therapy in Cancer and Its Protective Effects on Non-Malignant Tissues

Zaher, A., Petronek, M. S., Allen, B. G., & Mapuskar, K. A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25168885 · Cited by 23

Low-energy electron interaction with retusin extracted from Maackia amurensis: towards a molecular mechanism of the biological activity of flavonoids

Pshenichnyuk, S. A., Elkin, Y. N., Kulesh, N. I., Lazneva, E. F., & Komolov, А. S. (2015) · Physical Chemistry Chemical Physics · doi:10.1039/c5cp02890f · Cited by 23

Opposite Production of Reactive Oxygen Species by Complexes I and III during Heart Ischemia/Reperfusion

Bopassa, J. C., Zilberstein, N., Toro, L., & Stefani, E. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2009.12.3941

Critical role of mitochondrial ROS is dependent on their site of production on the electron transport chain in ischemic heart.

Madungwe, N. B., Zilberstein, N., Feng, Y., & Bopassa, J. C. (2016) · PubMed Central · Cited by 71

The Deleterious or Protective Action of ROS in the Heart Depends on their Production Site in the Mitochondrial Electron Transfer Chain

Bopassa, J. C., Zilberstein, N., Toro, L., & Stefani, E. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2011.11.779

Complex I-mediated reactive oxygen species generation: modulation by cytochrome c and NAD(P)+ oxidation–reduction state

Kushnareva, Y., Murphy, A. N., & Andreyev, A. Y. (2002) · Biochemical Journal · doi:10.1042/bj20021121 · Cited by 696

Reactive oxygen species are generated by the respiratory complex II – evidence for lack of contribution of the reverse electron flow in complex I

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