Cited by 480Mitochondrial Function and PathologyRedox biology and oxidative stressNitric Oxide and Endothelin Effects

The DOI matches its Crossref record; 84 of the 84 references it cites were found in a registry or an index.

Tissue-, substrate-, and site-specific characteristics of mitochondrial reactive oxygen species generation

Open access

Tahara, Erich B., Navarete, Felipe D.T., Kowaltowski, Alicia J.·2009·Free Radical Biology and Medicine

DOI 10.1016/j.freeradbiomed.2009.02.008

Open this paper in CoChat — free account Open PDF

Abstract

Reactive oxygen species are a by-product of mitochondrial oxidative phosphorylation, derived from a small quantity of superoxide radicals generated during electron transport. We conducted a comprehensive and quantitative study of oxygen consumption, inner membrane potentials, and H(2)O(2) release in mitochondria isolated from rat brain, heart, kidney, liver, and skeletal muscle, using various respiratory substrates (alpha-ketoglutarate, glutamate, succinate, glycerol phosphate, and palmitoyl carnitine). The locations and properties of reactive oxygen species formation were determined using oxidative phosphorylation and the respiratory chain modulators oligomycin, rotenone, myxothiazol, and antimycin A and the uncoupler CCCP. We found that in mitochondria isolated from most tissues incubated under physiologically relevant conditions, reactive oxygen release accounts for 0.1-0.2% of O(2) consumed. Our findings support an important participation of flavoenzymes and complex III and a substantial role for reverse electron transport to complex I as reactive oxygen species sources. Our results also indicate that succinate is an important substrate for isolated mitochondrial reactive oxygen production in brain, heart, kidney, and skeletal muscle, whereas fatty acids generate significant quantities of oxidants in kidney and liver. Finally, we found that increasing respiratory rates is an effective way to prevent mitochondrial oxidant release under many, but not all, conditions. Altogether, our data uncover and quantify many tissue-, substrate-, and site-specific characteristics of mitochondrial ROS release.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1016/j.freeradbiomed.2009.02.008

Cites

84 of 84 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 316,394
Free radicals in biology and medicine
Gutteridge, J. M. C. (1991) · General Pharmacology The Vascular System · doi:10.1016/0306-3623(91)90478-o · Cited by 17,178
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 formation of reactive oxygen species
Turrens, J. F. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.049478 · Cited by 5,084
Mitochondria, Oxidants, and Aging
Balaban, R. S., Nemoto, S., & Finkel, T. (2005) · Cell · doi:10.1016/j.cell.2005.02.001 · Cited by 4,388
Oxidative Stress, Caloric Restriction, and Aging
Sohal, R. S., & Weindruch, R. H. (1996) · Science · doi:10.1126/science.273.5271.59 · Cited by 3,133
The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen
Boveris, A., & Chance, B. (1973) · Biochemical Journal · doi:10.1042/bj1340707 · Cited by 2,626
Calcium, ATP, and ROS: a mitochondrial love-hate triangle
Brookes, P. S., Yoon, Y., Robotham, J. L., Anders, M. W., & Sheu, S.-S. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00139.2004 · Cited by 2,575
Pathways of Oxidative Damage
Imlay, J. A. (2003) · Annual Review of Microbiology · doi:10.1146/annurev.micro.57.030502.090938 · Cited by 2,201
High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria
Korshunov, S. S., Skulachev, V. P., & Starkov, A. A. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01159-9 · Cited by 1,727

Show all 83 references

Sorted by citations

Items 101–200 of 480

Mild Mitochondrial Uncoupling and Calorie Restriction Increase Fasting eNOS, Akt and Mitochondrial Biogenesis
Cerqueira, F. M., Laurindo, F. R. M., & Kowaltowski, A. J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018433 · Cited by 89
Self-citation
Is “Preparation for Oxidative Stress” a Case of Physiological Conditioning Hormesis?
de Oliveira, M. F., Geihs, M. A., França, T. F. A., Moreira, D. C., & Hermes‐Lima, M. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00945 · Cited by 86
Mitochondrial compartmentalization of redox processes
Cardoso, A. R., Chausse, B., da Cunha, F. M., Luévano‐Martínez, L. A., Marazzi, T. B. M., Pessoa, P. S., Queliconi, B. B., & Kowaltowski, A. J. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.03.008 · Cited by 86
Self-citation
Intermittent Fasting Results in Tissue-Specific Changes in Bioenergetics and Redox State
Chausse, B., Vieira‐Lara, M. A., Sanchez, A. B., de Medeiros, M. H. G., & Kowaltowski, A. J. (2015) · PLoS ONE · doi:10.1371/journal.pone.0120413 · Cited by 84
Self-citation
The small GTPase Rac1 is a novel binding partner of Bcl-2 and stabilizes its antiapoptotic activity
Velaithan, R., Kang, J., Hirpara, J. L., Loh, T. K. S., Goh, B. C., Bras, M. L., Brenner, C., Clement, M., & Pervaiz, S. (2011) · Blood · doi:10.1182/blood-2010-08-301283 · Cited by 87
Diet-Sensitive Sources of Reactive Oxygen Species in Liver Mitochondria: Role of Very Long Chain Acyl-CoA Dehydrogenases
Cardoso, A. R., Kakimoto, P. A., & Kowaltowski, A. J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0077088 · Cited by 86
Self-citation
Mitochondrial accumulation of APP and Aβ: significance for Alzheimer disease pathogenesis
Pavlov, P. F., Petersen, C. H., Glaser, E. G., & Ankarcrona, M. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00892.x · Cited by 84
Invited review: Thermal effects on oxidative stress in vertebrate ectotherms
Ritchie, D., & Friesen, C. R. (2021) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/j.cbpa.2021.111082 · Cited by 84
Molecular and Supramolecular Structure of the Mitochondrial Oxidative Phosphorylation System: Implications for Pathology
Nesci, S., Trombetti, F., Pagliarani, A., Ventrella, V., Algieri, C., Tioli, G., & Lenaz, G. (2021) · Life · doi:10.3390/life11030242 · Cited by 84
An integrated overview on the regulation of sperm metabolism (glycolysis-Krebs cycle-oxidative phosphorylation)
Peña, F. J., Ortiz-Rodriguez, J. M., Gaitskell‐Phillips, G., Gil, M. C., Ortega‐Ferrusola, C., & Martín‐Cano, F. E. (2021) · Animal Reproduction Science · doi:10.1016/j.anireprosci.2021.106805 · Cited by 80
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
Detection of Hydrogen Peroxide with Fluorescent Dyes
Rezende, F., Brandes, R. P., & Schröder, K. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7401 · Cited by 81
Mitochondrial redox potential during contraction in single intact muscle fibers
Michaelson, L. P., Shi, G., Ward, C. W., & Rodney, G. G. (2010) · Muscle & Nerve · doi:10.1002/mus.21724 · Cited by 82
Physiological and pathophysiological role of reactive oxygen species and reactive nitrogen species in the kidney
Ishimoto, Y., Tanaka, T., Yoshida, Y., & Inagi, R. (2018) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/1440-1681.13018 · Cited by 78
Differential effects of short- and long-term high-fat diet feeding on hepatic fatty acid metabolism in rats
Čiapaitė, J., van den Broek, N. M. A., Brinke, H. T., Nicolay, K., Jeneson, J. A. L., Houten, S. M., & Prompers, J. J. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2011.05.005 · Cited by 79
Redox-Dependent Loss of Flavin by Mitochondrial Complex I in Brain Ischemia/Reperfusion Injury
Степанова, А., Sosunov, S. A., Niatsetskaya, Z. V., Konràd, C., Starkov, A. A., Manfredi, G., Wittig, I., Ten, V. S., & Galkin, A. S. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7693 · Cited by 77
Mitochondrial oxidative stress and dysfunction induced by isoniazid: study on isolated rat liver and brain mitochondria
Ahadpour, M., Eskandari, M. R., Mashayekhi, V., Tehrani, K. H. M. E., Jafarian, I., Naserzadeh, P., & Hosseini, M. (2015) · Drug and Chemical Toxicology · doi:10.3109/01480545.2015.1092039 · Cited by 76
BAM15 treats mouse sepsis and kidney injury, linking mortality, mitochondrial DNA, tubule damage, and neutrophils
Tsuji, T., Tsuji, T., Yamashita, T., Hayase, N., Hu, X., Yuen, P. S. T., & Star, R. A. (2023) · Journal of Clinical Investigation · doi:10.1172/jci152401 · Cited by 75
Increased mitochondrial substrate sensitivity in skeletal muscle of patients with type 2 diabetes.
Larsen, S., Stride, N., Hey-Mogensen, M., Hansen, C. N., Andersen, J. L., Madsbad, S., Worm, D., Helge, J. W., & Dela, F. (2011) · Diabetologia · doi:10.1007/s00125-011-2098-4 · Cited by 73
Retrodifferentiation of Human Tumor Hepatocytes to Stem Cells Leads to Metabolic Reprogramming and Chemoresistance
Fekir, K., Dubois‐Pot‐Schneider, H., Désert, R., Daniel, Y., Glaise, D., Rauch, C., Morel, F., Fromenty, B., Musso, O. C., Cabillic, F., et al. (2019) · Cancer Research · doi:10.1158/0008-5472.can-18-2110 · Cited by 73
The Long Life of Birds: The Rat-Pigeon Comparison Revisited
Montgomery, M. K., Hulbert, A. J., & Buttemer, W. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024138 · Cited by 77
Redox regulation in health and disease — Therapeutic potential of berberine
Siow, Y. L., Sarna, L. K., & Karmin, O. (2011) · Food Research International · doi:10.1016/j.foodres.2010.12.038 · Cited by 72
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
Attenuation of oxidative damage by targeting mitochondrial complex I in neonatal hypoxic-ischemic brain injury
Kim, M., Степанова, А., Niatsetskaya, Z. V., Sosunov, S. A., Arndt, S., Murphy, M. P., Galkin, A. S., & Ten, V. S. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.06.040 · Cited by 74
The Emerging Roles of Nicotinamide Adenine Dinucleotide Phosphate Oxidase 2 in Skeletal Muscle Redox Signaling and Metabolism
Henríquez‐Olguín, C., Boronat, S., Cabello‐Verrugio, C., Jaimovich, E., Hidalgo, E., & Jensen, T. E. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7678 · Cited by 71
Ferroptosis: A Potential Therapeutic Target in Acute Kidney Injury
Hosohata, K., Harnsirikarn, T., & Chokesuwattanaskul, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23126583 · Cited by 73
Oxidative Stress in the Healthy and Wounded Hepatocyte: A Cellular Organelles Perspective
Mello, T., Zanieri, F., Ceni, E., & Galli, A. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/8327410 · Cited by 72
Hepatitis C Virus-Induced Mitochondrial Dysfunctions
Brault, C., Levy, P. L., & Bartosch, B. (2013) · Viruses · doi:10.3390/v5030954 · Cited by 70
Metabolic Regulation of Hematopoietic Stem Cells
Morganti, C., Cabezas‐Wallscheid, N., & Ito, K. (2022) · HemaSphere · doi:10.1097/hs9.0000000000000740 · Cited by 82
Aldehydic load and aldehyde dehydrogenase 2 profile during the progression of post-myocardial infarction cardiomyopathy: Benefits of Alda-1
Gomes, M. K., Bechara, L. R. G., Lima, V. M., Ribeiro, M. A. C., Campos, J. C., Dourado, P. M. M., Kowaltowski, A. J., Mochly‐Rosen, D., & Ferreira, J. C. B. (2014) · International Journal of Cardiology · doi:10.1016/j.ijcard.2014.10.140 · Cited by 69
Self-citation
The fatty acid oxidation enzyme long-chain acyl-CoA dehydrogenase can be a source of mitochondrial hydrogen peroxide
Zhang, Y., Bharathi, S. S., Beck, M. E., & Goetzman, E. S. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101253 · Cited by 68
H2O2 release from the very long chain acyl-CoA dehydrogenase
Kakimoto, P. A., Tamaki, F. K., Cardoso, A. R., Marana, S. R., & Kowaltowski, A. J. (2015) · Redox Biology · doi:10.1016/j.redox.2015.02.003 · Cited by 67
Self-citation
From Past to Present: The Link Between Reactive Oxygen Species in Sperm and Male Infertility
Villaverde, A. I. S. B., Netherton, J. K., & Baker, M. A. (2019) · Antioxidants · doi:10.3390/antiox8120616 · Cited by 69
Induction of mitochondrial permeability transition (MPT) pore opening and ROS formation as a mechanism for methamphetamine-induced mitochondrial toxicity
Mashayekhi, V., Eskandari, M. R., Kobarfard, F., Khajeamiri, A. R., & Hosseini, M. (2013) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-013-0919-3 · Cited by 64
Partitioning of superoxide and hydrogen peroxide production by mitochondrial respiratory complex I
Grivennikova, V. G., & Vinogradov, A. D. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.01.002 · Cited by 64
Mitochondria and Cardiac Hypertrophy.
Facundo, H. D. T. F., Brainard, R. E., Caldas, F. R. D. L., & Lucas, A. M. B. (2017) · Advances in Experimental Medicine and Biology · doi:10.1007/978-3-319-55330-6_11 · Cited by 70
The Hsp60 folding machinery is crucial for manganese superoxide dismutase folding and function
Magnoni, R., Palmfeldt, J., Hansen, J., Christensen, J., Corydon, T. J., & Bross, P. (2013) · Free Radical Research · doi:10.3109/10715762.2013.858147 · Cited by 63
Mitochondrial Mechanisms of Apoptosis and Necroptosis in Liver Diseases
Chu, Q., Gu, X., Zheng, Q., Wang, J., & Zhu, H. (2021) · Analytical Cellular Pathology · doi:10.1155/2021/8900122 · Cited by 62
Regulation of Stem Cell Fate by ROS-mediated Alteration of Metabolism
Ryu, J. M., Lee, H. J., Jung, Y. H., Lee, K. H., Kim, D. I., Kim, J. Y., Ko, S. H., Choi, G. E., Chai, I. I., Song, E. J., et al. (2015) · International Journal of Stem Cells · doi:10.15283/ijsc.2015.8.1.24 · Cited by 62
Depleted uranium induces disruption of energy homeostasis and oxidative stress in isolated rat brain mitochondria
Shaki, F., Hosseini, M., Ghazi‐Khansari, M., & Pourahmad, J. (2013) · Metallomics · doi:10.1039/c3mt00019b · Cited by 61
A Case for Microtubule Vulnerability in Amyotrophic Lateral Sclerosis: Altered Dynamics During Disease
Clark, J. A., Yeaman, E. J., Blizzard, C. A., Chuckowree, J. A., & Dickson, T. C. (2016) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2016.00204 · Cited by 66
Prevention of Postoperative Atrial Fibrillation: Novel and Safe Strategy Based on the Modulation of the Antioxidant System
Rodrigo, R. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00093 · Cited by 59
Heart‐Specific Knockout of the Mitochondrial Thioredoxin Reductase ( Txnrd2 ) Induces Metabolic and Contractile Dysfunction in the Aging Myocardium
Kiermayer, C., Northrup, E., Schrewe, A., Walch, A. K., de Angelis, M. H., Schoensiegel, F., Zischka, H., Prehn, C. P., Adamski, J., Bekeredjian, R., et al. (2015) · Journal of the American Heart Association · doi:10.1161/jaha.115.002153 · Cited by 60
The Role of Reactive Oxygen Species in Adipogenic Differentiation
de Villiers, D., Potgieter, M., Ambele, M. A., Adam, L. T., Durandt, C., & Pepper, M. S. (2017) · Advances in experimental medicine and biology · doi:10.1007/5584_2017_119 · Cited by 62
Intermittent Fasting Induces Hypothalamic Modifications Resulting in Low Feeding Efficiency, Low Body Mass and Overeating
Chausse, B., Solon, C., da Silva, C. C. C., dos Reis, I. G. M., Manchado-Gobatto, F. D. B., Gobatto, C. A., Velloso, L. A., & Kowaltowski, A. J. (2014) · Endocrinology · doi:10.1210/en.2013-2057 · Cited by 59
Self-citation
Mitochondrial stress: Balancing friend and foe
Runkel, E. D., Baumeister, R., & Schulze, E. (2014) · Experimental Gerontology · doi:10.1016/j.exger.2014.02.013 · Cited by 59
Reactive oxygen species in cancer: Mechanistic insights and therapeutic innovations
Ma, N., Wang, Y., Li, X., Xu, M., & Tan, D. (2025) · Cell Stress and Chaperones · doi:10.1016/j.cstres.2025.100108 · Cited by 60
Mitochondrial Physiology in the Major Arbovirus Vector Aedes aegypti: Substrate Preferences and Sexual Differences Define Respiratory Capacity and Superoxide Production
Soares, J. B. R. C., Gaviraghi, A., & de Oliveira, M. F. (2015) · PLoS ONE · doi:10.1371/journal.pone.0120600 · Cited by 63
Metabolism Regulation and Redox State: Insight into the Role of Superoxide Dismutase 1
Damiano, S., Sozio, C., Rosa, G. L., Guida, B., Faraonio, R., Santillo, M., & Mondola, P. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186606 · Cited by 59
Engineering protein A affinity chromatography.
Jungbauer, A., & Hahn, R. (2004) · PubMed · Cited by 56
Persistently Altered Brain Mitochondrial Bioenergetics After Apparently Successful Resuscitation From Cardiac Arrest
Kilbaugh, T. J., Sutton, R. M., Karlsson, M., Hansson, M. J., Naim, M. Y., Morgan, R. W., Bratinov, G. D., Lampe, J. W., Nadkarni, V., Becker, L. B., et al. (2015) · Journal of the American Heart Association · doi:10.1161/jaha.115.002232 · Cited by 55
Strategies to detect mitochondrial oxidants
Kowaltowski, A. J. (2018) · Redox Biology · doi:10.1016/j.redox.2018.101065 · Cited by 55
Self-citation
Thiamine Triphosphate Synthesis in Rat Brain Occurs in Mitochondria and Is Coupled to the Respiratory Chain
Gangolf, M., Wins, P., Thiry, M., Moualij, B. E., & Bettendorff, L. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.054379 · Cited by 54
Mitochondrial ion transport pathways: Role in metabolic diseases
Cardoso, A. R., Queliconi, B. B., & Kowaltowski, A. J. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.12.017 · Cited by 54
Self-citation
Respiratory complex II: ROS production and the kinetics of ubiquinone reduction
Grivennikova, V. G., Kozlovsky, V. S., & Vinogradov, A. D. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.10.008 · Cited by 54
Mitochondrial and Reactive Oxygen Species Signaling Coordinate Stem Cell Fate Decisions and Life Long Maintenance
Khacho, M., & Slack, R. S. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7228 · Cited by 54
Insight into the effect of biomaterials on osteogenic differentiation of mesenchymal stem cells: A review from a mitochondrial perspective
Feng, Z., Jin, M., Liang, J., Kang, J., Yang, H., Guo, S., & Sun, X. (2023) · Acta Biomaterialia · doi:10.1016/j.actbio.2023.03.032 · Cited by 52
Comparative Studies of Oxidative Stress and Mitochondrial Function in Aging
Shi, Y., Buffenstein, R., Pulliam, D. A., & Remmen, H. V. (2010) · Integrative and Comparative Biology · doi:10.1093/icb/icq079 · Cited by 52
Analyses of the three 1-Cys Peroxiredoxins from Aspergillus fumigatus reveal that cytosolic Prx1 is central to H2O2 metabolism and virulence
Rocha, M. C., de Godoy, K. F., Bannitz-Fernandes, R., Fabri, J. H. T. M., Barbosa, M. M. F., de Castro, P. A., Almeida, F. B. D. R., Goldman, G. H., da Cunha, A. F., Netto, L. E. S., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-30108-2 · Cited by 53
Emerging roles of β-cell mitochondria in type-2-diabetes
Las, G., Oliveira, M. F., & Shirihai, O. S. (2020) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2019.100843 · Cited by 51
The entangled ER-mitochondrial axis as a potential therapeutic strategy in neurodegeneration: A tangled duo unchained
Joshi, A. U., Kornfeld, O. S., & Mochly‐Rosen, D. (2016) · Cell Calcium · doi:10.1016/j.ceca.2016.04.010 · Cited by 55
Glycosylation as new pharmacological strategies for diseases associated with excessive angiogenesis
Bousseau, S., Vergori, L., Soleti, R., Lenaers, G., Martínez, M. C., & Andriantsitohaina, R. (2018) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2018.06.003 · Cited by 51
Production of extracellular superoxide radical in microorganisms and its environmental implications: A review
He, Z., Li, Q., Yao, X., Zhang, D., & Pan, X. (2023) · Environmental Pollution · doi:10.1016/j.envpol.2023.122563 · Cited by 50
Plasma and salivary total antioxidant capacity in healthy controls compared with aggressive and chronic periodontitis patients
Başer, Ü., Işık, H. G., Çifçibaşı, E., Ademoğlu, E., & Yalçın, F. (2015) · Saudi Medical Journal · doi:10.15537/smj.2015.7.11954 · Cited by 50
Carbonic anhydrase III regulates peroxisome proliferator-activated receptor-γ2
Mitterberger, M. C., Kim, G., Rostek, U., Levine, R. L., & Zwerschke, W. (2012) · Experimental Cell Research · doi:10.1016/j.yexcr.2012.02.011 · Cited by 49
An investigation of the occurrence and properties of the mitochondrial intermediate-conductance Ca2+-activated K+ channel mtKCa3.1
Nicola Sassi, A., Marchi, U. D., Fioretti, B., Biasutto, L., Gulbins, E., Franciolini, F., Szabó, I., & Zoratti, M. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.12.015 · Cited by 49
A silybin-phospholipids complex counteracts rat fatty liver degeneration and mitochondrial oxidative changes
Grattagliano, I. (2013) · World Journal of Gastroenterology · doi:10.3748/wjg.v19.i20.3007 · Cited by 48
Mitochondria in Early Forebrain Development: From Neurulation to Mid-Corticogenesis
Fame, R. M., & Lehtinen, M. K. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.780207 · Cited by 47
Inhaled Methane Limits the Mitochondrial Electron Transport Chain Dysfunction during Experimental Liver Ischemia-Reperfusion Injury
Strifler, G., Tuboly, E., Szél, E., Kaszonyi, E., Cao, C., Kaszaki, J., Mészáros, A., Boros, M., & Hartmann, P. (2016) · PLoS ONE · doi:10.1371/journal.pone.0146363 · Cited by 46
Tissue and sex specificities in Ca2+ handling by isolated mitochondria in conditions avoiding the permeability transition
Chweih, H., Castilho, R. F., & Figueira, T. R. (2015) · Experimental Physiology · doi:10.1113/ep085248 · Cited by 45
Targeting of mitochondrial reactive oxygen species production does not avert lipid-induced insulin resistance in muscle tissue from mice
Paglialunga, S., van Bree, B., Bosma, M., Valdecantos, M. P., Amengual-Cladera, E., Jörgensen, J. A., van Beurden, D., den Hartog, G. J. M., Ouwens, D. M., Briedé, J. J., et al. (2012) · Diabetologia · doi:10.1007/s00125-012-2626-x · Cited by 48
Mitochondrial hydrogen peroxide production as determined by the pyridine nucleotide pool and its redox state
Kareyeva, A. V., Grivennikova, V. G., & Vinogradov, A. D. (2012) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.03.033 · Cited by 45
Caloric restriction protects livers from ischemia/reperfusion damage by preventing Ca2+-induced mitochondrial permeability transition
Menezes‐Filho, S. L., Amigo, I., Prado, F. M., Cayuela, N. C., Koike, M. K., Pinto, I. F. D., Miyamoto, S., Montero, E. F. D. S., de Medeiros, M. H. G., & Kowaltowski, A. J. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.06.013 · Cited by 45
Self-citation
The mechanism of protective effect of crocin against liver mitochondrial toxicity caused by arsenic III
Yousefsani, B. S., Pourahmad, J., & Hosseinzadeh, H. (2017) · Toxicology Mechanisms and Methods · doi:10.1080/15376516.2017.1368054 · Cited by 45
Beneficial effects of white wine polyphenols-enriched diet on Alzheimer’s disease-like pathology
Mendes, D., Oliveira, M. M., Moreira, P. I., Coutinho, J., Nunes, F. M., Pereira, D. M., Valentão, P., Andrade, P. B., & Videira, R. A. (2018) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2018.02.001 · Cited by 48
The cardioprotective effects of icariin on the isoprenaline-induced takotsubo-like rat model: Involvement of reactive oxygen species and the TLR4/NF-κB signaling pathway
Qi, C., Shao, Y., Liu, X., Wang, D., & Li, X. (2019) · International Immunopharmacology · doi:10.1016/j.intimp.2019.105733 · Cited by 45
Mechanistic Approaches of Internalization, Subcellular Trafficking, and Cytotoxicity of Nanoparticles for Targeting the Small Intestine
Madni, A., Rehman, S., Sultan, H., Khan, M. M., Ahmad, F., Raza, M. R., Rai, N., & Parveen, F. (2020) · AAPS PharmSciTech · doi:10.1208/s12249-020-01873-z · Cited by 47
Metabolic control analysis of mitochondrial aconitase: influence over respiration and mitochondrial superoxide and hydrogen peroxide production
Scandroglio, F., Tórtora, V., Radí, R., & Castro, L. (2014) · Free Radical Research · doi:10.3109/10715762.2014.900175 · Cited by 42
Rheological Abnormalities in Human Erythrocytes Subjected to Oxidative Inflammation
Maruyama, T., Hieda, M., Mawatari, S., & Fujino, T. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.837926 · Cited by 44
Stem Cell and Oxidative Stress-Inflammation Cycle
Buzoğlu, H. D., Buruş, A., Bayazıt, Y., & Goldberg, M. (2022) · Current Stem Cell Research & Therapy · doi:10.2174/1574888x17666221012151425 · Cited by 41
Being right on Q: shaping eukaryotic evolution
Speijer, D. (2016) · Biochemical Journal · doi:10.1042/bcj20160647 · Cited by 41
Mitochondrial NADH redox potential impacts the reactive oxygen species production of reverse Electron transfer through complex I
Dubouchaud, H., Walter, L., Rigoulet, M., & Batandier, C. (2018) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-018-9767-7 · Cited by 41
Dysfunctional stem and progenitor cells impair fracture healing with age
Wagner, D. R., Karnik, S. J., Gunderson, Z. J., Nielsen, J. J., Fennimore, A., Promer, H., Lowery, J. W., Loghmani, M. T., Low, P. S., McKinley, T. O., et al. (2019) · World Journal of Stem Cells · doi:10.4252/wjsc.v11.i6.281 · Cited by 41
Metabolite Profiles Reveal Energy Failure and Impaired Beta-Oxidation in Liver of Mice with Complex III Deficiency Due to a BCS1L Mutation
Kotarsky, H., Keller, M., Davoudi, M., Levéen, P., Karikoski, R., Enot, D. P., & Fellman, V. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041156 · Cited by 42
Effect of aging on formation of reactive oxygen species by mitochondria of rat heart
Kuka, S., Tatarková, Z., Račay, P., Lehotský, J., Dobrota, D., & Kaplán, P. (2014) · General Physiology and Biophysics · doi:10.4149/gpb_2013049 · Cited by 40
Effects of bioenergetics, temperature and cadmium on liver mitochondria reactive oxygen species production and consumption
Okoye, C. N., MacDonald-Jay, N., & Kamunde, C. (2019) · Aquatic Toxicology · doi:10.1016/j.aquatox.2019.105264 · Cited by 40
Oxidative Inactivation of Liver Mitochondria in High Fructose Diet-Induced Metabolic Syndrome in Rats: Effect of Glycyrrhizin Treatment
Sil, R., & Chakraborti, A. S. (2016) · Phytotherapy Research · doi:10.1002/ptr.5654 · Cited by 40
Systems biology of antioxidants
Andriantsitohaina, R., Duluc, L., Rodríguez, J., del Valle, L. G., Guevara-García, M., Simard, G., Soleti, R., Su, D., Velázquez‐Pérez, L., Wilson, J. X., et al. (2012) · Clinical Science · doi:10.1042/cs20110643 · Cited by 42
Mitochondrial Function in Human Neuroblastoma Cells Is Up-Regulated and Protected by NQO1, a Plasma Membrane Redox Enzyme
Kim, J., Kim, S.-K., Kim, H. K., Mattson, M. P., & Hyun, D. H. (2013) · PLoS ONE · doi:10.1371/journal.pone.0069030 · Cited by 39
Mitochondrial flash as a novel biomarker of mitochondrial respiration in the heart
Gong, G., Liu, X., Zhang, H., Sheu, S., & Wang, W. (2015) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00462.2015 · Cited by 38
Cellular crosstalk in cardioprotection: Where and when do reactive oxygen species play a role?
Martins‐Marques, T., Rodríguez‐Sinovas, A., & Girão, H. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.03.044 · Cited by 38
RTG1- and RTG2-dependent retrograde signaling controls mitochondrial activity and stress resistance in Saccharomyces cerevisiae
Torelli, N. Q., Ferreira-Júnior, J. R., Kowaltowski, A. J., & da Cunha, F. M. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.12.025 · Cited by 37
Self-citation
Penehyclidine hydrochloride preconditioning provides cardiac protection in a rat model of myocardial ischemia/reperfusion injury via the mechanism of mitochondrial dynamics mechanism
Yang, Y., Zhao, L., & Ma, J. (2017) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2017.07.031 · Cited by 37
Flux through mitochondrial redox circuits linked to nicotinamide nucleotide transhydrogenase generates counterbalance changes in energy expenditure
Smith, C. D., Schmidt, C. A., Lin, C., Fisher‐Wellman, K. H., & Neufer, P. D. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013899 · Cited by 37
On the Redox Control of B Lymphocyte Differentiation and Function
Bertolotti, M., Sitia, R., & Rubartelli, A. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4252 · Cited by 37
Mitochondrial complex I inhibition triggers NAD+-independent glucose oxidation via successive NADPH formation, “futile” fatty acid cycling, and FADH2 oxidation
Abrosimov, R., Baeken, M. W., Hauf, S., Wittig, I., Hajieva, P., Perrone, C. E., & Moosmann, B. (2024) · GeroScience · doi:10.1007/s11357-023-01059-y · Cited by 37
Reactive Oxygen Species (ROS) in Metabolic Disease—Don’t Shoot the Metabolic Messenger
Lindsay, R. T., & Rhodes, C. J. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26062622 · Cited by 37
Brown adipose tissue mitochondria oxidizing fatty acids generate high levels of reactive oxygen species irrespective of the uncoupling protein-1 activity state
Schönfeld, P., & Wojtczak, L. (2011) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2011.12.009 · Cited by 36
Small Maf functions in the maintenance of germline stem cells in the Drosophila testis
Tan, S. W. S., Yip, G. W. C., Suda, T., & Baeg, G. H. (2017) · Redox Biology · doi:10.1016/j.redox.2017.12.002 · Cited by 35
Investigation of lipidomic perturbations in oxidatively stressed subcellular organelles and exosomes by asymmetrical flow field–flow fractionation and nanoflow ultrahigh performance liquid chromatography–tandem mass spectrometry
Yang, J. S., Kim, J. Y., Lee, J. C., & Moon, M. H. (2019) · Analytica Chimica Acta · doi:10.1016/j.aca.2019.04.069 · Cited by 36

Authors: Tahara, E. B., Navarete, F. D. T., & Kowaltowski, A. J.
Affiliations: Universidade de São Paulo (BR)
Corresponding author: Kowaltowski, Alicia J.
ORCID: Tahara, Erich B.
Navarete, Felipe D.T.
Kowaltowski, Alicia J.
Venue: Free Radical Biology and Medicine
Publisher: Elsevier BV
Published: 2009-05
Volume: 46
Issue: 9
Pages: 1283-1297
ISSN: 0891-5849 (ISSN-L)
DOI: 10.1016/j.freeradbiomed.2009.02.008
OpenAlex: W2079100436
Cited by: 479
References: 83
Citations by year: 2026: 15 · 2025: 18 · 2024: 34 · 2023: 19 · 2022: 28 · 2021: 33 · 2020: 27 · 2019: 23 · 2018: 27 · 2017: 28 · 2016: 31 · 2015: 45 · 2014: 25 · 2013: 28 · 2012: 34
FWCI: 12.96
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 298 d)
Locations: Free Radical Biology and Medicine (publishedVersion)
PubMed (publishedVersion)
Scientific Electronic Library Online (São Paulo Research Foundation, Latin American and Caribbean Center on Health Sciences Information, Conselho Nacional de Desenvolvimento Científico e Tecnológico) (publishedVersion)
Funders: Fundação de Amparo à Pesquisa do Estado de São Paulo
Conselho Nacional de Desenvolvimento Científico e Tecnológico
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
Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
Keywords: mitochondrial reactive oxygen species, superoxide, oxidative phosphorylation, respiratory substrates, succinic acid, fatty acids, palmitoylcarnitine, flavoenzyme, cytochrome bc1 complex, reverse electron transfer, complex I, mitochondrial membrane potential, hydrogen peroxide release, oxygen consumption, tissue-specific differences, brain, heart, kidney, liver, skeletal muscle
MeSH terms: Animals, Brain, Kidney, Liver, Male, Mitochondria, Myocardium, Organ Specificity, Oxidative Phosphorylation, Oxygen Consumption, Substrate Specificity, Rats, Sprague-Dawley, Reactive Oxygen Species, Oxidative Stress, Muscle, Skeletal, Electron Transport Chain Complex Proteins, Membrane Transport Modulators, Rats, Membrane Potential, Mitochondrial

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Tissue-, substrate-, and site-specific characteristics of mitochondrial reactive oxygen species generation

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks