Reactive oxygen species in health and disease
Open accessAbstract
During the past decades, it became obvious that reactive oxygen species (ROS) exert a multitude of biological effects covering a wide spectrum that ranges from physiological regulatory functions to damaging alterations participating in the pathogenesis of increasing number of diseases. This review summarizes the key roles played by the ROS in both health and disease. ROS are metabolic products arising from various cells; two cellular organelles are intimately involved in their production and metabolism, namely, the endoplasmic reticulum and the mitochondria. Updates on research that tremendously aided in confirming the fundamental roles of both organelles in redox regulation will be discussed as well. Although not comprehensive, this review will provide brief perspective on some of the current research conducted in this area for better understanding of the ROS actions in various conditions of health and disease.
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
Cites
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?
Chronic oxidative stress and resultant oxidative damage have been implicated in many human diseases including cardiovascular disease, neurodegenerative diseases, diabetes, cancer, and aging.
“Chronic oxidative stress and the resultant oxidative damage have been implicated in many human diseases including cardiovascular disease, neurodegenerative diseases, diabetes, cancer, and the aging process [18,19,20,21,22].”
From Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease (2022) · cites this paper as [19]
ROS are free radicals and chemically reactive molecules derived from oxygen.
“ROS are plenty of free radicals and chemically reactive molecules derived from oxygen molecule [41].”
From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [41]
Excessive production of ROS, usually termed oxidative stress, is caused by increased production and/or insufficient presence of endogenous antioxidants.
“Excessive production of ROS, usually termed oxidative stress, are caused by increased production and/or insufficient presence of endogenous antioxidants [41].”
From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [41]
Most ROS are generated as byproducts of mitochondrial electron transportation from the reduction of molecular oxygen to produce superoxide.
“Most ROS are generated as byproducts of mitochondrial electron transportation from the reduction of molecular oxygen to produce superoxide [41].”
From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [41]
Oxidative stress damages fats, DNA, and proteins in a cell, which can lead to diseases such as diabetes, cancer, neurodegenerative disease, and cardiovascular disease.
“Oxidative stress is considered detrimental because of its damage to fats, deoxyribonucleic acid, and proteins in a cell, which can lead to numerous diseases such as diabetes, cancer, neurodegenerative disease, and cardiovascular disease (CVD) [41].”
From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [41]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Free Radicals in the Physiological Control of Cell Function
Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855 · see citing works
Inflammation and metabolic disorders
Hotamisligil, G. S. (2006) · Nature · doi:10.1038/nature05485 · Cited by 9,199 · see citing works
Signal integration in the endoplasmic reticulum unfolded protein response
Ron, D., & Walter, P. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2199 · Cited by 6,308 · see citing works
A role for mitochondria in nlrp3 inflammasome activation
Zhou, R., Yazdi, A. S., Menu, P., & Tschopp, J. (2011) · Nature · doi:10.1038/nature09663 · Cited by 5,602 · see citing works
Increased oxidative stress in obesity and its impact on metabolic syndrome
Furukawa, S., Fujita, T., Shimabukuro, M., Iwaki, M., Yamada, Y., Nakajima, Y., Nakayama, O., Makishima, M., Matsuda, M., & Shimomura, I. (2004) · Journal of Clinical Investigation · doi:10.1172/jci21625 · Cited by 5,508 · see citing works
Inflammation, stress, and diabetes
Wellen, K. E., & Hotamisligil, G. S. (2005) · Journal of Clinical Investigation · doi:10.1172/jci25102 · Cited by 4,143 · see citing works
Endoplasmic Reticulum Stress Links Obesity, Insulin Action, and Type 2 Diabetes
Özcan, U., Cao, Q., Yilmaz, E., Lee, A.-H., Iwakoshi, N. N., Özdelen, E., Tuncman, G., Görgün, C., Glimcher, L. H., & Hotamisligil, G. S. (2004) · Science · doi:10.1126/science.1103160 · Cited by 3,844 · see citing works
TLR4 links innate immunity and fatty acid-induced insulin resistance
Shi, H., Kokoeva, M. V., Inouye, K., Tzameli, I., Yin, H., & Flier, J. S. (2006) · Journal of Clinical Investigation · doi:10.1172/jci28898 · Cited by 3,690 · see citing works
Hotamisligil, G. S., Arner, P., Caro, J. F., Atkinson, R. L., & Spiegelman, B. M. (1995) · Journal of Clinical Investigation · doi:10.1172/jci117936 · Cited by 3,543 · see citing works
An Integrated Stress Response Regulates Amino Acid Metabolism and Resistance to Oxidative Stress
Harding, H. P., Zhang, Y., Zeng, H., Novoa, I., Lu, P. D., Calfon, M. A., Sadri, N., Yun, C., Popko, B., Paules, R. S., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00105-9 · Cited by 3,336 · see citing works
Mitochondrial diseases in man and mouse
Wallace, D. C. (1999) · Science · doi:10.1126/science.283.5407.1482 · Cited by 3,060 · see citing works
THE MAMMALIAN UNFOLDED PROTEIN RESPONSE
Schröder, M., & Kaufman, R. J. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.074134 · Cited by 3,035 · see citing works
Urano, F., Wang, X.-Z., Bertolotti, A., Zhang, Y., Chung, P., Harding, H. P., & Ron, D. (2000) · Science · doi:10.1126/science.287.5453.664 · Cited by 2,997 · see citing works
Innate Immune Activation Through Nalp3 Inflammasome Sensing of Asbestos and Silica
Dostert, C., Pétrilli, V., Van Bruggen, R., Steele, C., Mossman, B. T., & Tschopp, J. (2008) · Science · doi:10.1126/science.1156995 · Cited by 2,658 · see citing works
Reactive oxygen species have a causal role in multiple forms of insulin resistance
Houstis, N., Rosen, E. D., & Lander, E. S. (2006) · Nature · doi:10.1038/nature04634 · Cited by 2,525 · see citing works
Oncogene-induced Nrf2 transcription promotes ROS detoxification and tumorigenesis
DeNicola, G. M., Karreth, F. A., Humpton, T. J., Gopinathan, A., Wei, C., Frese, K., Mangal, D., Yu, K. H., Yeo, C. J., Calhoun, E. S., et al. (2011) · Nature · doi:10.1038/nature10189 · Cited by 2,277 · see citing works
Local and systemic insulin resistance resulting from hepatic activation of IKK-β and NF-κB
Cai, D., Yuan, M., Frantz, D. F., Melendez, P. A., Hansen, L., Lee, J., & Shoelson, S. E. (2005) · Nature Medicine · doi:10.1038/nm1166 · Cited by 2,245 · see citing works
The immune response in atherosclerosis: a double-edged sword
Hansson, G. K., & Libby, P. (2006) · Nature reviews. Immunology · doi:10.1038/nri1882 · Cited by 2,176 · see citing works
Yuan, M., Konstantopoulos, N., Lee, J., Hansen, L., Li, Z.-W., Karin, M., & Shoelson, S. E. (2001) · Science · doi:10.1126/science.1061620 · Cited by 1,884 · see citing works
IKK-β links inflammation to obesity-induced insulin resistance
Arkan, M. C., Hevener, A. L., Greten, F. R., Maeda, S., Li, Z.-W., Long, J. M., Wynshaw-Boris, A., Poli, G., Olefsky, J., & Karin, M. (2005) · Nature Medicine · doi:10.1038/nm1185 · Cited by 1,773 · see citing works
Superoxide activates mitochondrial uncoupling proteins
Echtay, K. S., Roussel, D., St-Pierre, J., Jekabsons, M. B., Cadenas, S., Stuart, J. A., Harper, J. A., Roebuck, S. J., Morrison, A., Pickering, S., et al. (2002) · Nature · doi:10.1038/415096a · Cited by 1,382 · see citing works
Nrf2 Is a Direct PERK Substrate and Effector of PERK-Dependent Cell Survival
Cullinan, S. B., Zhang, D. D., Hannink, M., Arvisais, E. W., Kaufman, R. J., & Diehl, J. A. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.20.7198-7209.2003 · Cited by 1,233 · see citing works
Tiedge, M., Lortz, S., Drinkgern, J., & Lenzen, S. (1997) · Diabetes · doi:10.2337/diab.46.11.1733 · Cited by 1,211 · see citing works
The antioxidant function of the p53 tumor suppressor
Sablina, A. A., Budanov, A. V., Ilyinskaya, G. V., Agapova, L. S., Kravchenko, J. E., & Chumakov, P. M. (2005) · Nature Medicine · doi:10.1038/nm1320 · Cited by 1,110 · see citing works
Mechanistic Studies of the Nrf2-Keap1 Signaling Pathway
Zhang, D. D. (2006) · Drug Metabolism Reviews · doi:10.1080/03602530600971974 · Cited by 1,091 · see citing works
Robertson, R. P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.r400019200 · Cited by 1,078 · see citing works
Oxidative protein folding in eukaryotes
Tu, B. P., & Weissman, J. S. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200311055 · Cited by 1,041 · see citing works
ATP-dependent reduction of cysteine–sulphinic acid by S. cerevisiae sulphiredoxin
Biteau, B., Labarre, J., & Tolédano, M. B. (2003) · Nature · doi:10.1038/nature02075 · Cited by 970 · see citing works
Zhang, C.-Y., Baffy, G., Perret, P., Krauss, S., Peroni, O., Grujic, D., Hagen, T., Vidal-Puig, A. J., Boss, O., Kim, Y.-B., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00378-6 · Cited by 917 · see citing works
Guzy, R. D., & Schumacker, P. T. (2006) · Experimental Physiology · doi:10.1113/expphysiol.2006.033506 · Cited by 881 · see citing works
NRF2 and KEAP1 mutations: permanent activation of an adaptive response in cancer
Hayes, J. D., & McMahon, M. J. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2008.12.008 · Cited by 870 · see citing works
Mitofusin-2 Determines Mitochondrial Network Architecture and Mitochondrial Metabolism
Bach, D., Pich, S., Soriano, F. X., Vega, N., Baumgartner, B., Oriola, J., Daugaard, J. R., Lloberas, J., Camps, M., Zierath, J. R., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212754200 · Cited by 832 · cited 1× · see citing works
“As an example, reduced expression of mitofusin 2 (Mfn2), one of the mitochondrial proteins responsible for its dynamic morphology, was demonstrated to be partly responsible for decreased glucose oxidation and cell respiration in obesity [49].”
BackgroundMitochondrial proton and electron leaks
Jastroch, M., Divakaruni, A. S., Mookerjee, S., Treberg, J. R., & Brand, M. D. (2010) · Essays in Biochemistry · doi:10.1042/bse0470053 · Cited by 829 · see citing works
Virbasius, J. V., & Scarpulla, R. C. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.4.1309 · Cited by 819 · see citing works
Cullinan, S. B., & Diehl, J. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m314219200 · Cited by 739 · see citing works
TNF-α Is a Predictor of Insulin Resistance in Human Pregnancy
Kirwan, J. P., Hauguel-De Mouzon, S., Lepercq, J., Challier, J.-C., Huston-Presley, L., Friedman, J. E., Kalhan, S. C., & Catalano, P. M. (2002) · Diabetes · doi:10.2337/diabetes.51.7.2207 · Cited by 738 · see citing works
UCP2 mediates ghrelin’s action on NPY/AgRP neurons by lowering free radicals
Andrews, Z. B., Liu, Z.-W., Walllingford, N., Erion, D. M., Borok, E., Friedman, J. M., Tschöp, M. H., Shanabrough, M., Cline, G., Shulman, G. I., et al. (2008) · Nature · doi:10.1038/nature07181 · Cited by 710 · see citing works
Doughan, A. K., Harrison, D. G., & Dikalov, S. I. (2008) · Circulation Research · doi:10.1161/circresaha.107.162800 · Cited by 710 · see citing works
Oxidative stress during viral infection: A review
Schwarz, K. B. (1996) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(96)00131-1 · Cited by 652 · see citing works
Role of Reactive Oxygen Species in the Progression of Type 2 Diabetes and Atherosclerosis
Kaneto, H., Katakami, N., Matsuhisa, M., & Matsuoka, T. (2010) · Mediators of Inflammation · doi:10.1155/2010/453892 · Cited by 577 · see citing works
The role of mitochondria in the pathogenesis of type 2 diabetes
Patti, M.-E., & Corvera, S. (2010) · Endocrine Reviews · doi:10.1210/er.2009-0027 · Cited by 551 · see citing works
Dai, D.-F., Johnson, S. C., Villarin, J. J., Chin, M. T., Nieves-Cintrón, M., Chen, T., Marcinek, D. J., Dorn, G. W., Kang, Y. J., Prolla, T. A., et al. (2011) · Circulation Research · doi:10.1161/circresaha.110.232306 · Cited by 527 · see citing works
Mitochondrial function in normal and diabetic β-cells
Maechler, P., & Wollheim, C. B. (2001) · Nature · doi:10.1038/414807a · Cited by 519 · see citing works
Inflammaging: disturbed interplay between autophagy and inflammasomes
Salminen, A., Kaarniranta, K., & Kauppinen, A. (2012) · Aging · doi:10.18632/aging.100444 · Cited by 511 · see citing works
The Hyperglycemia-induced Inflammatory Response in Adipocytes
Lin, Y., Berg, A. H., Iyengar, P., Lam, T. K. T., Giacca, A., Combs, T. P., Rajala, M. W., Du, X., Rollman, B., Li, W., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m411863200 · Cited by 497 · see citing works
The mitochondrial UPR – protecting organelle protein homeostasis
Haynes, C. M., & Ron, D. (2010) · Journal of Cell Science · doi:10.1242/jcs.075119 · Cited by 490 · see citing works
Prolonged oxidative stress impairs insulin-induced GLUT4 translocation in 3T3-L1 adipocytes.
Rudich, A., Tirosh, A., Potashnik, R., Hemi, R., Kanety, H., & Bashan, N. (1998) · Diabetes · doi:10.2337/diabetes.47.10.1562 · Cited by 483 · see citing works
Summers, S. A., Garza, L. A., Zhou, H., & Birnbaum, M. J. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.9.5457 · Cited by 475 · see citing works
Silva, J. P., Köhler, M., Graff, C., Oldfors, A., Magnuson, M. A., Berggren, P.-O., & Larsson, N.-G. (2000) · Nature Genetics · doi:10.1038/81649 · Cited by 433 · see citing works
The stimulus-secretion coupling of glucose-induced insulin release
Malaisse, W. J., Hutton, J. C., Kawazu, S., Herchuelz, A., Valverde, I., & Sener, A. (1979) · Diabetologia · doi:10.1007/bf01223623 · Cited by 426 · see citing works
Oxidative Stress Is Associated with Adiposity and Insulin Resistance in Men
Urakawa, H., Katsuki, A., Sumida, Y., Gabazza, E. C., Murashima, S., Morioka, K., Maruyama, N., Kitagawa, N., Tanaka, T., Hori, Y., et al. (2003) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2003-030202 · Cited by 416 · see citing works
Mitochondrial dynamics and division in budding yeast
Shaw, J. M., & Nunnari, J. (2002) · Trends in Cell Biology · doi:10.1016/s0962-8924(01)02246-2 · Cited by 375 · see citing works
Hydrogen Peroxide Alters Mitochondrial Activation and Insulin Secretion in Pancreatic Beta Cells
Maechler, P., Jornot, L., & Wollheim, C. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.39.27905 · Cited by 359 · see citing works
Chan, C. B., De Leo, D., Joseph, J. W., McQuaid, T. S., Ha, X. F., Xu, F., Tsushima, R. G., Pennefather, P. S., Salapatek, A. M. F., & Wheeler, M. B. (2001) · Diabetes · doi:10.2337/diabetes.50.6.1302 · Cited by 341 · see citing works
Liu, Y., Zhao, H., Li, H., Kalyanaraman, B., Nicolosi, A. C., & Gutterman, D. D. (2003) · Circulation Research · doi:10.1161/01.res.0000091261.19387.ae · Cited by 323 · see citing works
Salminen, A., Ojala, J. O., Kaarniranta, K., & Kauppinen, A. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-0962-0 · Cited by 304 · see citing works
Mitochondria: Sovereign of inflammation?
Tschopp, J. (2011) · European Journal of Immunology · doi:10.1002/eji.201141436 · Cited by 292 · see citing works
The pancreatic beta-cell as a fuel sensor: an electrophysiologist's viewpoint
Rorsman, P. (1997) · Diabetologia · doi:10.1007/s001250050706 · Cited by 278 · see citing works
The role of glucocorticoid action in the pathophysiology of the Metabolic Syndrome
Wang, M. (2005) · Nutrition & Metabolism · doi:10.1186/1743-7075-2-3 · Cited by 276 · see citing works
Mitochondrial ROS fuel the inflammasome
Sorbara, M. T., & Girardin, S. E. (2011) · Cell Research · doi:10.1038/cr.2011.20 · Cited by 274 · see citing works
Ceramide Interaction with the Respiratory Chain of Heart Mitochondria
Di Paola, M., Cocco, T., & Lorusso, M. (2000) · Biochemistry · doi:10.1021/bi9924415 · Cited by 262 · see citing works
Han, C. Y., Kargi, A. Y., Omer, M., Chan, C. K., Wabitsch, M., O’Brien, K. D., Wight, T. N., & Chait, A. (2009) · Diabetes · doi:10.2337/db09-0925 · Cited by 248 · see citing works
Familial amyotrophic lateral sclerosis
Hand, C. K., & Rouleau, G. A. (2002) · Muscle & Nerve · doi:10.1002/mus.10001 · Cited by 235 · see citing works
Role of reactive oxygen species in contraction‐mediated glucose transport in mouse skeletal muscle
Sandström, M., Zhang, S., Bruton, J. D., Silva, J., Reid, M. B., Westerblad, H., & Katz, A. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.110601 · Cited by 210 · see citing works
Lee, H. K., Song, J., Shin, C. S., Park, D. J., Park, K. S., Lee, K. U., & Koh, C.-S. (1998) · Diabetes Research and Clinical Practice · doi:10.1016/s0168-8227(98)00110-7 · Cited by 208 · see citing works
Wenzel, P., Schuhmacher, S., Kienhöfer, J., Müller, J., Hortmann, M., Oelze, M., Schulz, E., Treiber, N., Kawamoto, T., Scharffetter-Kochanek, K., et al. (2008) · Cardiovascular Research · doi:10.1093/cvr/cvn182 · Cited by 207 · see citing works
Summers, S. A., & Nelson, D. H. (2005) · Diabetes · doi:10.2337/diabetes.54.3.591 · Cited by 185 · see citing works
Subramanian, S., Han, C. Y., Chiba, T., McMillen, T. S., Wang, S. A., Haw, A., Kirk, E. A., O’Brien, K. D., & Chait, A. (2008) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.107.157685 · Cited by 182 · see citing works
Rajendran, R., Garva, R., Krstic–Demonacos, M., & Demonacos, C. (2011) · BioMed Research International · doi:10.1155/2011/368276 · Cited by 173 · see citing works
Chen, Y., Cai, J.-Y., Murphy, T., & Jones, D. P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202026200 · Cited by 166 · see citing works
Fuel utilization by hypothalamic neurons: roles for ROS.
Horvath, T., Andrews, Z., & Diano, S. (2009) · Trends in endocrinology and metabolism · doi:10.1016/j.tem.2008.10.003 · Cited by 159 · see citing works
Endonuclease G is a novel determinant of cardiac hypertrophy and mitochondrial function
McDermott‐Roe, C., Ye, J., Ahmed, R., Sun, X.-M., Serafin, A. M., Ware, J. S., Bottolo, L., Muckett, P. J., Cañas, X., Zhang, J., et al. (2011) · Nature · doi:10.1038/nature10490 · Cited by 157 · see citing works
Berzosa, C., Cebrián, I., Fuentes‐Broto, L., Gómez-Trullén, E. M., Piedrafita, E., Martínez‐Ballarín, E., López‐Pingarrón, L., Reiter, R. J., & García, J. J. (2011) · BioMed Research International · doi:10.1155/2011/540458 · Cited by 153 · see citing works
Effects of depletion of mitochondrial DNA in metabolism secretion coupling in INS-1 cells.
Kennedy, E. D., Maechler, P., & Wollheim, C. B. (1998) · Diabetes · doi:10.2337/diabetes.47.3.374 · Cited by 151 · see citing works
Soejima, A., Inoue, K., Takai, D., Kaneko, M., Ishihara, H., Oka, Y., & Hayashi, J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.42.26194 · Cited by 149 · see citing works
The effect of sepsis on the oxidation of carbohydrate and fat
Stoner, H. B., Little, R., Frayn, K. N., Elebute, A. E., Tresadern, J. C., & Gross, E. (1983) · British journal of surgery · doi:10.1002/bjs.1800700113 · Cited by 147 · see citing works
Hypoxia‐inducible factor 1 and cancer pathogenesis
Semenza, G. L. (2008) · IUBMB Life · doi:10.1002/iub.93 · Cited by 145 · see citing works
Zhang, H., Luo, Y., Zhang, W., He, Y., Dai, S., Zhang, R., Huang, Y., Bernatchez, P., Giordano, F. J., Shadel, G., et al. (2007) · American Journal of Pathology · doi:10.2353/ajpath.2007.060960 · Cited by 145 · see citing works
Antioxidant and cytoprotective responses to redox stress
Mathers, J. E., Fraser, J. A., McMahon, M. J., Saunders, R. D. C., Hayes, J. D., & McLellan, L. I. (2004) · Biochemical Society Symposia · doi:10.1042/bss0710157 · Cited by 134 · see citing works
Reliene, R., Fischer, E., & Schiestl, R. H. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-0442 · Cited by 128 · see citing works
N‐acetylcysteine – passe‐partout or much ado about nothing?
Aitio, M. (2005) · British Journal of Clinical Pharmacology · doi:10.1111/j.1365-2125.2005.02523.x · Cited by 125 · see citing works
Antonetti, D. A., Reynet, C., & Kahn, C. R. (1995) · Journal of Clinical Investigation · doi:10.1172/jci117790 · Cited by 120 · see citing works
Oxidative Imbalance in HIV‐1 Infected Patients Treated with Antiretroviral Therapy
Mandas, A., Iorio, E. L., Congiu, M. G., et al. (2009) · BioMed Research International · doi:10.1155/2009/749575 · Cited by 109 · see citing works
Islets and their antioxidant defense
Acharya, J. D., & Ghaskadbi, S. (2010) · Islets · doi:10.4161/isl.2.4.12219 · Cited by 108 · see citing works
Saraswathi, V., Gao, L., Morrow, J. D., Chait, A., Niswender, K. D., & Hasty, A. H. (2007) · Journal of Nutrition · doi:10.1093/jn/137.7.1776 · Cited by 103 · see citing works
A key role for mitochondria in endothelial signaling by plasma cysteine/cystine redox potential
Go, Y.-M., Park, H., Koval, M., Orr, M., Reed, M., Liang, Y., Smith, D., Pohl, J., & Jones, D. P. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.10.050 · Cited by 103 · see citing works
Samuhasaneeto, S., Thong‐Ngam, D., Kulaputana, O., Suyasunanont, D., & Klaikeaw, N. (2009) · BioMed Research International · doi:10.1155/2009/981963 · Cited by 101 · see citing works
Shan, Q., Lu, J. L., Zheng, Y., Li, J., Zhou, Z., Hu, B., Zhang, Z.-F., Fan, S., Mao, Z., Wang, Y., et al. (2009) · BioMed Research International · doi:10.1155/2009/564737 · Cited by 101 · see citing works
Antioxidant N-acetyl cysteine reduces incidence and multiplicity of lymphoma in Atm deficient mice
Reliene, R., & Schiestl, R. H. (2006) · DNA repair · doi:10.1016/j.dnarep.2006.05.003 · Cited by 97 · see citing works
Mitochondrial DNA and inflammatory diseases
Escames, G., López, L. C., García, J. A., García‐Corzo, L., Ortiz, F., & Acuña-Castroviejo, D. (2011) · Human Genetics · doi:10.1007/s00439-011-1057-y · Cited by 96 · see citing works
Mitochondrial thioredoxin in regulation of oxidant‐induced cell death
Chen, Y., Cai, J., & Jones, D. P. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.11.007 · Cited by 92 · see citing works
Mitochondrial Dysfunction as an Initiating Event in Atherogenesis: A Plausible Hypothesis
Puddu, P., Puddu, G. M., Galletti, L., Cravero, E., & Muscari, A. (2005) · Cardiology · doi:10.1159/000083440 · Cited by 87 · see citing works
The Non-coding RNA gadd7 Is a Regulator of Lipid-induced Oxidative and Endoplasmic Reticulum Stress
Brookheart, R. T., Michel, C. I., Listenberger, L. L., Ory, D. S., & Schaffer, J. E. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m806209200 · Cited by 83 · see citing works
Tsuruzoe, K., Araki, E., Furukawa, N., Shirotani, T., Matsumoto, K., Kaneko, K. B., Motoshima, H., Yoshizato, K., Shirakami, A., Kishikawa, H., et al. (1998) · Diabetes · doi:10.2337/diabetes.47.4.621 · Cited by 82 · see citing works
Xia, R., Zhao, B., Wu, Y., Hou, J., Zhang, L., Xu, J., & Xia, Z. (2011) · BioMed Research International · doi:10.1155/2011/767930 · Cited by 74 · see citing works
Perera, R. M., & Bardeesy, N. M. (2011) · Nature · doi:10.1038/475043a · Cited by 71 · see citing works
RegB/RegA, A Global Redox-Responding Two-Component System
Wu, J., & Bauer, C. E. (2008) · Advances in experimental medicine and biology · doi:10.1007/978-0-387-78885-2_9 · Cited by 64 · see citing works
Rottlerin Inhibits ROS Formation and Prevents NFκB Activation in MCF‐7 and HT‐29 Cells
Maioli, E., Greci, L., Souček, K., et al. (2009) · BioMed Research International · doi:10.1155/2009/742936 · Cited by 59 · see citing works
Chen, J., & Stinnett, A. (2008) · Laboratory Investigation · doi:10.1038/labinvest.2008.92 · Cited by 57 · see citing works
Chapman, I. M. (2008) · KARGER eBooks · doi:10.1159/000115358 · Cited by 48 · see citing works
Effects of acute exercise on lung antioxidant enzymes in young and old rats
Hatao, H., Oh‐ishi, S., Itoh, M., Leeuwenburgh, C., Ohno, H., Ookawara, T., Kishi, K., Yagyu, H., Nakamura, H., & Matsuoka, T. (2006) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2005.12.008 · Cited by 47 · see citing works
Merry, T. L., Wadley, G. D., Stathis, C. G., GARNHAM, A. P., Rattigan, S., Hargreaves, M., & McConell, G. K. (2010) · The Journal of Physiology · doi:10.1113/jphysiol.2009.184333 · Cited by 43 · see citing works
Meijer, C. A., Haen, P. A. A. L., van Dijk, R. A., Hira, M., Hamming, J. F., van Bockel, J. H., & Lindeman, J. H. N. (2011) · Clinical Science · doi:10.1042/cs20110234 · Cited by 42 · see citing works
Cecere, F., Iuliano, A., Albano, F., Zappelli, C., Castellano, I., Grimaldi, P., Masullo, M., Vendittis, E. D., & Ruocco, M. R. (2010) · BioMed Research International · doi:10.1155/2010/801726 · Cited by 42 · see citing works
Redox regulation in anabolic and catabolic processes
Dröge, W. (2006) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/01.mco.0000222098.98514.40 · Cited by 40 · see citing works
Genome‐Wide Transcriptional Profiling of the Response of Staphylococcus aureus to Cryptotanshinone
Feng, H., Xiang, H., Zhang, J., Liu, G., Guo, N., Wang, X., Wu, X., Deng, X., & Yu, L. (2009) · BioMed Research International · doi:10.1155/2009/617509 · Cited by 33 · see citing works
PEDF in Diabetic Retinopathy: A Protective Effect of Oxidative Stress
Zhu, X., & Zou, H. (2012) · BioMed Research International · doi:10.1155/2012/580687 · Cited by 33 · see citing works
Do Reactive Oxygen Species Regulate Skeletal Muscle Glucose Uptake During Contraction?
Merry, T. L., & McConell, G. K. (2011) · Exercise and Sport Sciences Reviews · doi:10.1097/jes.0b013e318245837b · Cited by 30 · see citing works
Shin, D., Martínez, S. S., Parsons, M., Jayaweera, D. T., Campa, A. L., & Baum, M. K. (2012) · International Journal of Bioscience Biochemistry and Bioinformatics · doi:10.7763/ijbbb.2012.v2.104 · Cited by 30 · see citing works
Epoetin Delta Reduces Oxidative Stress in Primary Human Renal Tubular Cells
Beuf, A. D., Hou, X., D’Haese, P. C., et al. (2010) · BioMed Research International · doi:10.1155/2010/395785 · Cited by 20 · see citing works
Tsai, J.-H., Chen, H.-W., Chen, Y.-W., et al. (2010) · BioMed Research International · doi:10.1155/2010/486267 · Cited by 11 · see citing works
[Bactericidal action of hydrogen peroxide, peroxides, and oxidizing compounds].
Lw, H. (1950) · PubMed · Cited by 3 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Ros and ros-mediated cellular signaling
Zhang, J., Wang, X., Vikash, V., Ye, Q., Wu, D., Liu, Y., & Dong, W. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/4350965 · Cited by 1,980 · see citing works
Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease
Ngo, V., & Duennwald, M. L. (2022) · Antioxidants · doi:10.3390/antiox11122345 · Cited by 1,130 · see citing works
ROS Generation and Antioxidant Defense Systems in Normal and Malignant Cells
Snezhkina, A. V., Kudryavtseva, A. V., Kardymon, O. L., Savvateeva, M. V., Melnikova, N. V., Krasnov, G. S., & Dmitriev, A. A. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/6175804 · Cited by 934 · see citing works
Oxidative Stress in Human Pathology and Aging: Molecular Mechanisms and Perspectives
Hajam, Y. A., Rani, R., Ganie, S. Y., Sheikh, T. A., Javaid, D., Qadri, S. S., Pramodh, S., Alsulimani, A., Alkhanani, M. F., Harakeh, S., et al. (2022) · Cells · doi:10.3390/cells11030552 · Cited by 915 · see citing works
Mitochondrial dysfunction in obesity
de Mello, A. H., Costa, A. B., Engel, J. D. G., & Rezin, G. T. (2018) · Life Sciences · doi:10.1016/j.lfs.2017.11.019 · Cited by 508 · see citing works
Redox Mechanism of Reactive Oxygen Species in Exercise
He, F., Li, J., Liu, Z., Chuang, C.-C., Yang, W., & Zuo, L. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2016.00486 · Cited by 385 · see citing works
AMPK, Mitochondrial Function, and Cardiovascular Disease
Wu, S., & Zou, M.-H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21144987 · Cited by 286 · see citing works
Barrea, L., Marzullo, P., Muscogiuri, G., Di Somma, C., Scacchi, M., Orio, F., Aimaretti, G., Colao, A., & Savastano, S. (2018) · Nutrition Research Reviews · doi:10.1017/s0954422418000136 · Cited by 171 · see citing works
Hou, J., Zheng, D., Fung, G., Deng, H., Chen, L., Liang, J., Jiang, Y., & Hu, Y. (2016) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/cjpp-2015-0073 · Cited by 89 · see citing works
Lee, H.-T., Wu, T.-H., Lin, C.-S., Lee, C.-S., Wei, Y.-H., Tsai, C.-Y., & Chang, D.-M. (2016) · Mitochondrion · doi:10.1016/j.mito.2016.05.007 · Cited by 69 · see citing works
Antioxidant intervention attenuates oxidative stress in children and teenagers with Down syndrome
Parisotto, E. B., Garlet, T. R., Cavalli, V. L. D. L. O., Zamoner, A., da Rosa, J. S., Bastos, J., Micke, G. A., Fröde, T. S., Pedrosa, R. C., & Wilhelm Filho, D. (2014) · Research in Developmental Disabilities · doi:10.1016/j.ridd.2014.03.013 · Cited by 34 · see citing works
Sarfraz, M., Khan, A., Batiha, G. E.-S., Akhtar, M. F., Saleem, A., Ajiboye, B. O., Kamal, M., Ali, A., Alotaibi, N. M., Aaghaz, S., et al. (2023) · Cancers · doi:10.3390/cancers15164194 · Cited by 20 · see citing works
Effects of a 12-week aerobic exercise on markers of hypertension in men
Baghaiee, B., Karimi, P., Ebrahimi, K., Dabagh Nikoo kheslat, S., Sadeghi Zali, M. H., Daneshian Moghaddam, A. M., & Sadaghian, M. (2018) · Journal of Cardiovascular and Thoracic Research · doi:10.15171/jcvtr.2018.26 · Cited by 14 · see citing works
- Authors
- Alfadda, A. A., & Sallam, R. M.
- Affiliations
- King Saud University (SA)
- Corresponding author
- Alfadda, Assim A.
- Venue
- Journal of Biomedicine and Biotechnology
- Publisher
- Wiley
- Published
- 2012
- Volume
- 2012
- Pages
- 1-14
- ISSN
- 1110-7243 (ISSN-L)
- 1110-7251
- PMC
- PMC3424049
- OpenAlex
- W2108409617
- Cited by
- 824
- References
- 112
- Citations by year
- 2026: 19 · 2025: 55 · 2024: 60 · 2023: 71 · 2022: 74 · 2021: 72 · 2020: 81 · 2019: 62 · 2018: 65 · 2017: 65 · 2016: 48 · 2015: 58 · 2014: 56 · 2013: 33 · 2012: 2
- FWCI
- 4.35
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- BioMed Research International (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- National Plan for Sciences and Technology and Innovation, KSA (08-MED513-02)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Keywords
- reactive oxygen species, redox regulation, endoplasmic reticulum, mitochondria, oxidative stress, pathogenesis, physiological regulation
- MeSH terms
- Animals, Antioxidants, Disease, Health, Humans, Oxidation-Reduction, Reactive Oxygen Species, Oxidative Stress
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