The 2-Oxoacid Dehydrogenase Complexes in Mitochondria Can Produce Superoxide/Hydrogen Peroxide at Much Higher Rates Than Complex I

How mitochondria produce reactive oxygen species

Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207

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

Mitochondrial metabolism of reactive oxygen species

Andreyev, A. Y., Kushnareva, Y. E., & Starkov, A. A. (2005) · Biochemistry (Moscow) · doi:10.1007/s10541-005-0102-7 · Cited by 1,336

The sites and topology of mitochondrial superoxide production

Brand, M. D. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.01.003 · Cited by 1,217

Activation of molecular oxygen by flavins and flavoproteins.

Massey, V. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31664-2 · Cited by 823

The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria

Kußmaul, L., & Hirst, J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510977103 · Cited by 745

Mitochondrial α-Ketoglutarate Dehydrogenase Complex Generates Reactive Oxygen Species

Starkov, A. A., Fiskum, G. M., Chinopoulos, C., Lorenzo, B. J., Browne, S. E., Patel, M. S., & Beal, M. F. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.1899-04.2004 · Cited by 711

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

α-KETO ACID DEHYDROGENASE COMPLEXES, X. REGULATION OF THE ACTIVITY OF THE PYRUVATE DEHYDROGENASE COMPLEX FROM BEEF KIDNEY MITOCHONDRIA BY PHOSPHORYLATION AND DEPHOSPHORYLATION

Linn, T. C., Pettit, F. H., & Reed, L. J. (1969) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.62.1.234 · Cited by 671

Mitochondrial Complex II Can Generate Reactive Oxygen Species at High Rates in Both the Forward and Reverse Reactions

Quinlan, C. L., Orr, A. L., Perevoshchikova, I. V., Treberg, J. R., Ackrell, B. A., & Brand, M. D. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.374629 · Cited by 670

Reactive Oxygen Species in Metabolic and Inflammatory Signaling

Forrester, S. J., Kikuchi, D. S., Hernandes, M. S., Xu, Q., & Griendling, K. K. (2018) · Circulation Research · doi:10.1161/circresaha.117.311401 · Cited by 2,081

Lipid peroxidation and ferroptosis: The role of GSH and GPx4

Ursini, F., & Maiorino, M. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.02.027 · Cited by 1,954

Mitochondrial ROS in cancer: initiators, amplifiers or an Achilles' heel?

Sabharwal, S. S., & Schumacker, P. T. (2014) · Nature reviews. Cancer · doi:10.1038/nrc3803 · Cited by 1,681

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

The Role of the Reactive Oxygen Species and Oxidative Stress in the Pathomechanism of the Age‐Related Ocular Diseases and Other Pathologies of the Anterior and Posterior Eye Segments in Adults

Nita, M., & Grzybowski, A. E. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/3164734 · Cited by 1,510

Reactive oxygen species and mitochondria: A nexus of cellular homeostasis

Dunn, J. D., Álvarez, L., Zhang, X., & Soldati, T. (2015) · Redox Biology · doi:10.1016/j.redox.2015.09.005 · Cited by 1,233

Mitochondrial generation of superoxide and hydrogen peroxide as the source of mitochondrial redox signaling

Brand, M. D. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.001 · Cited by 1,063

The Redox Code

Jones, D. P., & Sies, H. (2015) · Antioxidants & Redox Signaling · doi:10.1089/ars.2015.6247 · Cited by 647

Glutathione and mitochondria

Ribas, V., García‐Ruiz, C., & Fernández-Checa, J. C. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00151 · Cited by 585

Lipoic acid metabolism and mitochondrial redox regulation

Solmonson, A., & DeBerardinis, R. J. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.tm117.000259 · Cited by 505

Production of superoxide and hydrogen peroxide from specific mitochondrial sites under different bioenergetic conditions

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

Generation of Reactive Oxygen Species by Mitochondria

Hernansanz‐Agustín, P., & Enrı́quez, J. A. (2021) · Antioxidants · doi:10.3390/antiox10030415 · Cited by 424

Mitochondrial metabolism mediates oxidative stress and inflammation in fatty liver

Satapati, S., Kucejová, B., Duarte, J. A. G., Fletcher, J. A., Reynolds, L., Sunny, N. E., He, T., Nair, L. A., Livingston, K. A., Fu, X., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci82204 · Cited by 403

Pathogenesis of Chronic Hyperglycemia: From Reductive Stress to Oxidative Stress

Yan, L. (2014) · Journal of Diabetes Research · doi:10.1155/2014/137919 · Cited by 425

Interactions between mitochondrial reactive oxygen species and cellular glucose metabolism

Liemburg-Apers, D. C., Willems, P. H. G. M., Koopman, W. J. H., & Grefte, S. (2015) · Archives of Toxicology · doi:10.1007/s00204-015-1520-y · Cited by 412

Reactive oxygen species, nutrition, hypoxia and diseases: Problems solved?

Görlach, A., Dimova, E. Y., Petry, A., Martínez-Ruiz, A., Hernansanz‐Agustín, P., Rolo, A. P., Palmeira, C. M., & Kietzmann, T. (2015) · Redox Biology · doi:10.1016/j.redox.2015.08.016 · Cited by 364

The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications

Carrico, C., Meyer, J. G., He, W., Gibson, B. W., & Verdin, E. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.01.016 · Cited by 331

Sites of superoxide and hydrogen peroxide production by muscle mitochondria assessed ex vivo under conditions mimicking rest and exercise

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

Superoxide Radicals in the Execution of Cell Death

Fujii, J., Homma, T., & Osaki, T. (2022) · Antioxidants · doi:10.3390/antiox11030501 · Cited by 337

Mitochondrial Management of Reactive Oxygen Species

Napolitano, G., Fasciolo, G., & Venditti, P. (2021) · Antioxidants · doi:10.3390/antiox10111824 · Cited by 305

Teaching the fundamentals of electron transfer reactions in mitochondria and the production and detection of reactive oxygen species

Mailloux, R. J. (2015) · Redox Biology · doi:10.1016/j.redox.2015.02.001 · Cited by 292

An Update on Mitochondrial Reactive Oxygen Species Production

Mailloux, R. J. (2020) · Antioxidants · doi:10.3390/antiox9060472 · Cited by 286

Sulforaphane reactivates cellular antioxidant defense by inducing Nrf2/ARE/Prdx6 activity during aging and oxidative stress

Kubo, E., Chhunchha, B., Singh, P., Sasaki, H., & Singh, D. P. (2017) · Scientific Reports · doi:10.1038/s41598-017-14520-8 · Cited by 239

Suppressors of Superoxide-H 2 O 2 Production at Site I Q of Mitochondrial Complex I Protect against Stem Cell Hyperplasia and Ischemia-Reperfusion Injury

Brand, M. D., Goncalves, R. L. S., Orr, A. L., Vargas, L., Gerencser, A. A., Borch Jensen, M., Wang, Y. T., Melov, S., Turk, C. N., Matzen, J. T., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.08.012 · Cited by 228

Antioxidant supplements and endurance exercise: Current evidence and mechanistic insights

Mason, S. A., Trewin, A. J., Parker, L., & Wadley, G. D. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101471 · Cited by 236

Exploring the molecular interface between hypoxia-inducible factor signalling and mitochondria

Thomas, L. W., & Ashcroft, M. A. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03039-y · Cited by 219

Dichloroacetate and cancer: New home for an orphan drug?

Kankotia, S., & Stacpoole, P. W. (2014) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2014.08.005 · Cited by 226

Cross-Talk between Oxidative Stress and Inflammation in Preeclampsia

Tenório, M. B., Ferreira, R. C., Moura, F. A., Bueno, N. B., de Oliveira, A. C. M., & Goulart, M. O. F. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/8238727 · Cited by 213

Elucidating the contribution of mitochondrial glutathione to ferroptosis in cardiomyocytes

Jang, S., Chapa‐Dubocq, X. R., Tyurina, Y. Y., Croix, C. M. S., Kapralov, A. A., Tyurin, V. A., Bayır, H., Kagan, V. E., & Javadov, S. A. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102021 · Cited by 210

Increased reactive oxygen species production during reductive stress: The roles of mitochondrial glutathione and thioredoxin reductases

Kôrge, P., Calmettes, G., & Weiss, J. N. (2015) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2015.02.012 · Cited by 199

Sources and implications of NADH/NAD+ redox imbalance in diabetes and its complications

Yan, L.-J., Wu, J., Jin, Z., & Zheng, H. (2016) · Diabetes, Metabolic Syndrome and Obesity: Targets and Therapy · doi:10.2147/dmso.s106087 · Cited by 198

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

Flavonoids and type 2 diabetes: Evidence of efficacy in clinical and animal studies and delivery strategies to enhance their therapeutic efficacy

Hussain, T., Tan, B., Murtaza, G., Liu, G., Rahu, N., Kalhoro, M. S., Kalhoro, D. H., Adebowale, T. O., Mazhar, M. U., Rehman, Z. U., et al. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.104629 · Cited by 208

Amino acid catabolism in Alzheimer’s disease brain: Friend or foe?

Griffin, J. W. D., & Bradshaw, P. C. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/5472792 · Cited by 185

Insights into the respiratory chain and oxidative stress

Larosa, V., & Remacle, C. (2018) · Bioscience Reports · doi:10.1042/bsr20171492 · Cited by 192

Mitochondrial protein interaction landscape of SS-31

Chavez, J. D., Tang, X., Campbell, M. D., Reyes, G., Kramer, P. A., Stuppard, R., Keller, A., Zhang, H., Rabinovitch, P. S., Marcinek, D. J., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2002250117 · Cited by 182

Modelling mitochondrial ROS production by the respiratory chain

Mazat, J., Devin, A., & Ransac, S. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03381-1 · Cited by 194

Dihydrolipoamide dehydrogenase regulates cystine deprivation-induced ferroptosis in head and neck cancer

Shin, D., Lee, J., You, J. H., Kim, D., & Roh, J. (2020) · Redox Biology · doi:10.1016/j.redox.2019.101418 · Cited by 179

Use the Protonmotive Force: Mitochondrial Uncoupling and Reactive Oxygen Species

Berry, B. J., Trewin, A. J., Amitrano, A. M., Kim, M., & Wojtovich, A. P. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.03.025 · Cited by 180

Heat exposure induces oxidative stress and DNA damage in the male germ line†

Houston, B. J., Nixon, B., Martin, J. H., Iuliis, G. N. D., Trigg, N. A., Bromfield, E. G., McEwan, K. E., & Aitken, R. J. (2018) · Biology of Reproduction · doi:10.1093/biolre/ioy009 · Cited by 162

Targeting Ferroptosis against Ischemia/Reperfusion Cardiac Injury

Lillo‐Moya, J., Rojas-Solé, C., Muñoz-Salamanca, D., Panieri, E., Saso, L., & Rodrigo, R. (2021) · Antioxidants · doi:10.3390/antiox10050667 · Cited by 166

The RNA-binding protein HuR is essential for the B cell antibody response

Díaz‐Muñoz, M. D., Bell, S. E., Fairfax, K. A., Monzón‐Casanova, E., Cunningham, A. F., Gonzàlez-Porta, M., Andrews, S., Bunik, V. I., Zarnack, K., Curk, T., et al. (2015) · Nature Immunology · doi:10.1038/ni.3115 · Cited by 159

The mitochondrial unfolded protein response (UPRmt): shielding against toxicity to mitochondria in cancer

Inigo, J. R., & Chandra, D. (2022) · Journal of Hematology & Oncology · doi:10.1186/s13045-022-01317-0 · Cited by 160

Metabolic Flexibility in Cancer: Targeting the Pyruvate Dehydrogenase Kinase:Pyruvate Dehydrogenase Axis

Woolbright, B. L., Rajendran, G., Harris, R. A., & Taylor, J. A. (2019) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-19-0079 · Cited by 157

The redox language in neurodegenerative diseases: oxidative post-translational modifications by hydrogen peroxide

Lee, Y. M., He, W., & Liou, Y. (2021) · Cell Death and Disease · doi:10.1038/s41419-020-03355-3 · Cited by 157

Cellular and mitochondrial mechanisms of atrial fibrillation

Mason, F. E., Pronto, J. R. D., Alhussini, K., Maack, C., & Voigt, N. (2020) · Basic Research in Cardiology · doi:10.1007/s00395-020-00827-7 · Cited by 147

Polyol pathway and redox balance in diabetes

Garg, S. S., & Gupta, J. (2022) · Pharmacological Research · doi:10.1016/j.phrs.2022.106326 · Cited by 158

Mitochondrial Dysfunction in the Aging Retina

Eells, J. T. (2019) · Biology · doi:10.3390/biology8020031 · Cited by 144

Ischemic A/D transition of mitochondrial complex I and its role in ROS generation

Dröse, S., Степанова, А., & Galkin, A. S. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2015.12.013 · Cited by 140

Intracellular Sources of ROS/H2O2 in Health and Neurodegeneration: Spotlight on Endoplasmic Reticulum

Konno, T., Melo, E. P., Chambers, J. E., & Avezov, E. (2021) · Cells · doi:10.3390/cells10020233 · Cited by 143

Linking Oxidative Stress and Proteinopathy in Alzheimer’s Disease

Sharma, C., & Kim, S. R. (2021) · Antioxidants · doi:10.3390/antiox10081231 · Cited by 145

Hypoxia Dictates Metabolic Rewiring of Tumors: Implications for Chemoresistance

Belisario, D. C., Kopecka, J., Pasino, M., Akman, M., De Smaele, E., Donadelli, M., & Riganti, C. (2020) · Cells · doi:10.3390/cells9122598 · Cited by 133

Hyperglycemic Stress and Carbon Stress in Diabetic Glucotoxicity

Luo, X., Wu, J., Jing, S., & Yan, L. (2016) · Aging and Disease · doi:10.14336/ad.2015.0702 · Cited by 145

Protein S-glutathionlyation links energy metabolism to redox signaling in mitochondria

Mailloux, R. J., & Treberg, J. R. (2015) · Redox Biology · doi:10.1016/j.redox.2015.12.010 · Cited by 137

The α-ketoglutarate dehydrogenase complex in cancer metabolic plasticity

Vatrinet, R., Leone, G., Luise, M. D., Girolimetti, G., Vidone, M., Gasparre, G., & Porcelli, A. M. (2017) · Cancer & Metabolism · doi:10.1186/s40170-017-0165-0 · Cited by 133

S-glutathionylation reactions in mitochondrial function and disease

Mailloux, R. J., & Willmore, W. G. (2014) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2014.00068 · Cited by 130

Molecular mechanisms of the non-coenzyme action of thiamin in brain: biochemical, structural and pathway analysis

Mkrtchyan, G. V., Aleshin, V. A., IuM, P., Kaehne, T., di Salvo, M. L., Parroni, A., Contestabile, R., Vovk, A. I., Bettendorff, L., & Bunik, V. I. (2015) · Scientific Reports · doi:10.1038/srep12583 · Cited by 128

Riding the tiger – physiological and pathological effects of superoxide and hydrogen peroxide generated in the mitochondrial matrix

Brand, M. D. (2020) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2020.1828258 · Cited by 123

Protein-mediated assembly of succinate dehydrogenase and its cofactors

Vranken, J. G. V., Na, U., Winge, D. R., & Rutter, J. P. (2014) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2014.990556 · Cited by 122

Pyruvate dehydrogenase complex and nicotinamide nucleotide transhydrogenase constitute an energy-consuming redox circuit

Fisher‐Wellman, K. H., Lin, C., RYAN, T. E., Reese, L., Gilliam, L. A. A., Cathey, B. L., Lark, D. S., Smith, C. D., Muoio, D. M., & Neufer, P. D. (2015) · Biochemical Journal · doi:10.1042/bj20141447 · Cited by 121

Mitochondrial reactive oxygen species production by fish muscle mitochondria: Potential role in acute heat-induced oxidative stress

Banh, S., Wiens, L. M., Sotiri, E., & Treberg, J. R. (2015) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2015.10.001 · Cited by 119

The Contribution of Nicotinamide Nucleotide Transhydrogenase to Peroxide Detoxification Is Dependent on the Respiratory State and Counterbalanced by Other Sources of NADPH in Liver Mitochondria

Ronchi, J. A., Francisco, A., Passos, L. A., Figueira, T. R., & Castilho, R. F. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.730473 · Cited by 119

Mitochondria in Diabetic Kidney Disease

Ahmad, A. A., Draves, S. O., & Rosca, M. G. (2021) · Cells · doi:10.3390/cells10112945 · Cited by 118

Known unknowns of cardiolipin signaling: The best is yet to come

Maguire, J. J., Tyurina, Y. Y., Mohammadyani, D., Kapralov, A. A., Anthonymuthu, T. S., Qu, F., Amoscato, A. A., Sparvero, L. J., Tyurin, V. A., Planas-Iglesias, J., et al. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.08.001 · Cited by 120

Oxidative stress mediates ethanol-induced skeletal muscle mitochondrial dysfunction and dysregulated protein synthesis and autophagy

Kumar, A., Davuluri, G., Welch, N., Kim, A., Gangadhariah, M. H., Allawy, A., Priyadarshini, A., McMullen, M. R., Sandlers, Y. I., Willard, B. B., et al. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.09.031 · Cited by 112

Silence superoxide dismutase 1 (SOD1): a promising therapeutic target for amyotrophic lateral sclerosis (ALS)

Abati, E., Bresolin, N., Comi, G. P., & Corti, S. P. (2020) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2020.1738390 · Cited by 107

Mitochondrial Cristae Morphology Reflecting Metabolism, Superoxide Formation, Redox Homeostasis, and Pathology

Ježek, P., Jabůrek, M., Holendová, B., Engstová, H., & Dlasková, A. (2023) · Antioxidants and Redox Signaling · doi:10.1089/ars.2022.0173 · Cited by 117

Mitochondrial Oxidative Stress in the Retinal Pigment Epithelium Leads to Localized Retinal Degeneration

Mao, H., Seo, S. J., Biswal, M. R., Li, H., Conners, M., Nandyala, A. S., Jones, K., Le, Y.-Z., & Lewin, A. S. (2014) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.14-14633 · Cited by 110

The role of mitochondrial ROS in antibacterial immunity

Pinegin, B. V., Vorobjeva, N. V., Pashenkov, M. V., & Chernyak, B. V. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.26117 · Cited by 108

How Do ROS Induce NETosis? Oxidative DNA Damage, DNA Repair, and Chromatin Decondensation

Azzouz, D., & Palaniyar, N. (2024) · Biomolecules · doi:10.3390/biom14101307 · Cited by 120

Mitochondrial reactive oxygen species: Do they extend or shorten animal lifespan?

Sanz, A. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.03.018 · Cited by 111

Melatonin alleviates heat stress-induced oxidative stress and apoptosis in human spermatozoa

Zhao, F., Whiting, S., Lambourne, S. R., Aitken, R. J., & Sun, Y. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.01.014 · Cited by 102

Escaping Death: Mitochondrial Redox Homeostasis in Cancer Cells

Ciccarese, F., & Ciminale, V. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00117 · Cited by 104

Cysteine-mediated redox signalling in the mitochondria

Bak, D. W., & Weerapana, E. (2014) · Molecular BioSystems · doi:10.1039/c4mb00571f · Cited by 102

Induction of mitochondrial reactive oxygen species production by GSH mediated S-glutathionylation of 2-oxoglutarate dehydrogenase

Mailloux, R. J., Ayre, D. C., & Christian, S. L. (2016) · Redox Biology · doi:10.1016/j.redox.2016.02.002 · Cited by 99

Interplay Between Reactive Oxygen/Reactive Nitrogen Species and Metabolism in Vascular Biology and Disease

Ushio‐Fukai, M., Ash, D., Nagarkoti, S., de Chantemèle, E. J. B., Fulton, D. J., & Fukai, T. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8161 · Cited by 99

Relationship between Oxidative Stress, Circadian Rhythms, and AMD

Fanjul‐Moles, M. L., & López-Riquelme, G. O. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/7420637 · Cited by 97

Aging: A mitochondrial DNA perspective, critical analysis and an update

Shokolenko, I. N. (2014) · World Journal of Experimental Medicine · doi:10.5493/wjem.v4.i4.46 · Cited by 101

Oxidative Stress and Mitochondrial Dysfunction Associated with Peripheral Neuropathy in Type 1 Diabetes

Eftekharpour, E., & Fernyhough, P. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2021.0152 · Cited by 97

Production of superoxide/H2O2 by dihydroorotate dehydrogenase in rat skeletal muscle mitochondria

Hey‐Mogensen, M., Goncalves, R. L. S., Orr, A. L., & Brand, M. D. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.04.007 · Cited by 84

The thioredoxin and glutathione-dependent H2O2 consumption pathways in muscle mitochondria: Involvement in H2O2 metabolism and consequence to H2O2 efflux assays

Munro, D., Banh, S., Sotiri, E., Tamanna, N., & Treberg, J. R. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.014 · Cited by 82

Catalytic Coupling of Oxidative Phosphorylation, ATP Demand, and Reactive Oxygen Species Generation

Bazil, J. N., Beard, D. A., & Vinnakota, K. C. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2015.09.036 · Cited by 81

Proteomics characterization of mitochondrial‐derived vesicles under oxidative stress

Vasam, G., Nadeau, R., Cadete, V. J. J., Lavallée‐Adam, M., Menzies, K. J., & Burelle, Y. (2021) · The FASEB Journal · doi:10.1096/fj.202002151r · Cited by 87

Complex I and complex III inhibition specifically increase cytosolic hydrogen peroxide levels without inducing oxidative stress in HEK293 cells

Forkink, M., Basit, F., Teixeira, J., Swarts, H. G. P., Koopman, W. J. H., & Willems, P. H. G. M. (2015) · Redox Biology · doi:10.1016/j.redox.2015.09.003 · Cited by 81

Sources of superoxide/H2O2 during mitochondrial proline oxidation

Goncalves, R. L. S., Rothschild, D. E., Quinlan, C. L., Scott, G. K., Benz, C. C., & Brand, M. D. (2014) · Redox Biology · doi:10.1016/j.redox.2014.07.003 · Cited by 79

Protein S-glutathionylation alters superoxide/hydrogen peroxide emission from pyruvate dehydrogenase complex

O’Brien, M., Chalker, J., Slade, L., Gardiner, D., & Mailloux, R. J. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.02.046 · Cited by 82

2-Oxoglutarate dehydrogenase is a more significant source of O2·−/H2O2 than pyruvate dehydrogenase in cardiac and liver tissue

Mailloux, R. J., Gardiner, D., & O’Brien, M. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.06.014 · Cited by 79

What sustains the multidrug resistance phenotype beyond ABC efflux transporters? Looking beyond the tip of the iceberg

Alexa‐Stratulat, T., Pešić, M., Gašparović, A. Č., Trougakos, I. P., & Riganti, C. (2019) · Drug Resistance Updates · doi:10.1016/j.drup.2019.100643 · Cited by 77

Progress in understanding the molecular oxygen paradox – function of mitochondrial reactive oxygen species in cell signaling

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