Positive and Negative Regulation of Insulin Signaling by Reactive Oxygen and Nitrogen Species
Abstract
Regulated production of reactive oxygen species (ROS)/reactive nitrogen species (RNS) adequately balanced by antioxidant systems is a prerequisite for the participation of these active substances in physiological processes, including insulin action. Yet, increasing evidence implicates ROS and RNS as negative regulators of insulin signaling, rendering them putative mediators in the development of insulin resistance, a common endocrine abnormality that accompanies obesity and is a risk factor of type 2 diabetes. This review deals with this dual, seemingly contradictory, function of ROS and RNS in regulating insulin action: the major processes for ROS and RNS generation and detoxification are presented, and a critical review of the evidence that they participate in the positive and negative regulation of insulin action is provided. The cellular and molecular mechanisms by which ROS and RNS are thought to participate in normal insulin action and in the induction of insulin resistance are then described. Finally, we explore the potential usefulness and the challenges in modulating the oxidant-antioxidant balance as a potentially promising, but currently disappointing, means of improving insulin action in insulin resistance-associated conditions, leading causes of human morbidity and mortality of our era.
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Increased ROS in adipocytes exposed to excess free fatty acids does not depend on enhanced mitochondrial flux, but on high levels of TNFα and ER stress as well as upregulation of NOX enzymes.
“Recently, it has been demonstrated that increased ROS in adipocytes exposed to an excess of FFAs does not depend on enhanced mitochondrial flux, but on high levels of TNFα and ER stress as well as the upregulation of aforementioned NOX enzymes ([8](#B8), [60](#B60)).”
From Mitochondrial fatty acid oxidation in obesity (2013) · cites this paper as [8]
ROS have the capacity to interfere with insulin signaling, since they activate several downstream pathways involving MAPK, JNK/IKKβ, and JAK/STAT, which are key contributors to the development of insulin resistance in obesity and type 2 diabetes.
“ROS have the capacity to interfere with insulin signaling, since they activate several downstream pathways involving MAPK, JNK/IKKβ, and JAK/STAT, which are key contributors to the development of insulin resistance in obesity and type 2 diabetes ([8](#B8), [75](#B75)).”
From Mitochondrial fatty acid oxidation in obesity (2013) · cites this paper as [8]
In obesity, excess free fatty acids increase NOX-mediated ROS generation.
“In obesity, the excess of FFAs increases NOX-mediated ROS generation.”
From Mitochondrial fatty acid oxidation in obesity (2013) · cites this paper as [8]
ROS are produced normally during mitochondrial respiration and are essential signal transducers that regulate several cell processes in skeletal muscle, including the insulin pathway.
“However, these molecules are produced normally during mitochondrial respiration and are essential signal transducers that regulate several cell processes in SkM ([8](#B8)), including the insulin pathway ([64](#B64), [65](#B65)).”
From Mitochondrial fatty acid oxidation in obesity (2013) · cites this paper as [8]
Cites
2 retracted
Insulin Stimulates PKCζ-mediated Phosphorylation of Insulin Receptor Substrate-1 (IRS-1)
Liu, Y., Paz, K., Herschkovitz, A., Alt, A., Tennenbaum, T., Sampson, S. R., Ohba, M., Kuroki, T., LeRoith, D., & Zick, Y. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007281200 · Cited by 158 · see citing works
RetractedEl‐Remessy, A. B., Bartoli, M., Platt, D. H., Fulton, D. J., & Caldwell, R. B. (2004) · Journal of Cell Science · doi:10.1242/jcs.01612 · Cited by 147 · see citing works
RetractedObesity is associated with macrophage accumulation in adipose tissue
Weisberg, S. P., McCann, D., Desai, M., Rosenbaum, M., Leibel, R. L., & Ferrante, A. W. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200319246 · Cited by 10,041 · see citing works
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
Biochemistry and molecular cell biology of diabetic complications
Brownlee, M. (2001) · Nature · doi:10.1038/414813a · Cited by 9,107 · see citing works
Stratton, I. M. (2000) · BMJ · doi:10.1136/bmj.321.7258.405 · Cited by 9,059 · see citing works
The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology
Bedard, K., & Krause, K.-H. (2007) · Physiological Reviews · doi:10.1152/physrev.00044.2005 · Cited by 6,989 · see citing works
Xu, H., Barnes, G. T., Yang, Q., Tan, G., Yang, D., Chou, C. J., Sole, J., Nichols, A., Ross, J. S., Tartaglia, L. A., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200319451 · Cited by 6,760 · see citing works
Nitric Oxide and Peroxynitrite in Health and Disease
Pacher, P., Beckman, J. S., & Liaudet, L. (2007) · Physiological Reviews · doi:10.1152/physrev.00029.2006 · Cited by 6,390 · see citing works
Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
Sarbassov, D. D., Guertin, D. A., Ali, S. M., & Sabatini, D. M. (2005) · Science · doi:10.1126/science.1106148 · Cited by 6,216 · see citing works
Hydroperoxide metabolism in mammalian organs.
Chance, B., Sies, H., & Boveris, A. (1979) · Physiological Reviews · doi:10.1152/physrev.1979.59.3.527 · Cited by 5,827 · 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
Mitochondrial formation of reactive oxygen species
Turrens, J. F. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.049478 · Cited by 5,084 · see citing works
Normalizing mitochondrial superoxide production blocks three pathways of hyperglycaemic damage
Nishikawa, T., Edelstein, D., Du, X. L., Yamagishi, S.-I., Matsumura, T., Kaneda, Y., Yorek, M. A., Beebe, D., Oates, P. J., Hammes, H.-P., et al. (2000) · Nature · doi:10.1038/35008121 · Cited by 4,277 · see citing works
Nitric oxide synthases: structure, function and inhibition
ALDERTON, W. K., COOPER, C. E., & KNOWLES, R. G. (2001) · Biochemical Journal · doi:10.1042/bj3570593 · Cited by 4,110 · see citing works
Nitric oxide synthases: structure, function and inhibition
ALDERTON, W. K., Cooper, C. E., & Knowles, R. G. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3570593 · Cited by 4,106 · 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
Role of Oxidative Stress in Development of Complications in Diabetes
Baynes, J. (1991) · Diabetes · doi:10.2337/diab.40.4.405 · Cited by 3,791 · see citing works
Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation
Dimmeler, S., Fleming, I., Fisslthaler, B., Hermann, C., Busse, R., & Zeiher, A. M. (1999) · Nature · doi:10.1038/21224 · Cited by 3,591 · see citing works
Nitric oxide synthases: Roles, tolls, and controls
Nathan, C., & Xie, Q. W. (1994) · Cell · doi:10.1016/0092-8674(94)90266-6 · Cited by 2,920 · see citing works
Role of Oxidative Modifications in Atherosclerosis
Stocker, R., & Keaney, J. F. (2004) · Physiological Reviews · doi:10.1152/physrev.00047.2003 · Cited by 2,611 · see citing works
Meta-Analysis: High-Dosage Vitamin E Supplementation May Increase All-Cause Mortality
Miller, E. R., Pastor-Barriuso, R., Dalal, D., Riemersma, R. A., Appel, L. J., & Guallar, E. (2005) · Annals of Internal Medicine · doi:10.7326/0003-4819-142-1-200501040-00110 · Cited by 2,577 · 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
Sundaresan, M., Yu, Z.-X., Ferrans, V. J., Irani, K., & Finkel, T. (1995) · Science · doi:10.1126/science.270.5234.296 · Cited by 2,520 · see citing works
Monnier, L., Mas, E., Ginet, C., Michel, F., Villon, L., Cristol, J.-P., & Colette, C. (2006) · JAMA · doi:10.1001/jama.295.14.1681 · Cited by 2,444 · see citing works
Nonalcoholic Fatty Liver Disease: From Steatosis to Cirrhosis
Farrell, G. C., & Larter, C. Z. (2006) · Hepatology · doi:10.1002/hep.20973 · Cited by 2,413 · see citing works
Özcan, U., Yilmaz, E., Özcan, L., Furuhashi, M., Vaillancourt, E., Smith, R. O., Görgün, C. Z., & Hotamisligil, G. S. (2006) · Science · doi:10.1126/science.1128294 · Cited by 2,413 · see citing works
Mammalian thioredoxin is a direct inhibitor of apoptosis signal‐regulating kinase (ASK) 1
Saitoh, M., Nishitoh, H., Fujii, M., Takeda, K., Tobiume, K., Sawada, Y., Kawabata, M., Miyazono, K., & Ichijo, H. (1998) · The EMBO Journal · doi:10.1093/emboj/17.9.2596 · Cited by 2,377 · see citing works
Bjelakovic, G., Nikolova, D., Gluud, L. L., Simonetti, R. G., & Gluud, C. (2007) · JAMA · doi:10.1001/jama.297.8.842 · Cited by 2,275 · see citing works
Oxidative Stress and Stress-Activated Signaling Pathways: A Unifying Hypothesis of Type 2 Diabetes
Evans, J. L., Goldfine, I. D., Maddux, B. A., & Grodsky, G. M. (2002) · Endocrine Reviews · doi:10.1210/er.2001-0039 · Cited by 2,232 · see citing works
Elchebly, M., Payette, P., Michaliszyn, E., Cromlish, W., Collins, S., Loy, A. L., Normandin, D., Cheng, A., Himms-Hagen, J., Chan, C.-C., et al. (1999) · Science · doi:10.1126/science.283.5407.1544 · Cited by 2,210 · see citing works
Impaired Mitochondrial Activity in the Insulin-Resistant Offspring of Patients with Type 2 Diabetes
Petersen, K. F., Dufour, S., Befroy, D., Garcia, R., & Shulman, G. I. (2004) · New England Journal of Medicine · doi:10.1056/nejmoa031314 · Cited by 2,193 · see citing works
Kohen, R., & Nyska, A. (2002) · Toxicologic Pathology · doi:10.1080/01926230290166724 · Cited by 2,178 · see citing works
Protein S-nitrosylation: Purview and parameters
Hess, D. T., Matsumoto, A., Kim, S.-O., Marshall, H. E., & Stamler, J. S. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1569 · Cited by 2,153 · see citing works
Serum retinol binding protein 4 contributes to insulin resistance in obesity and type 2 diabetes
Yang, Q., Graham, T. E., Mody, N., Preitner, F., Peroni, O. D., Zabolotny, J. M., Kotani, K., Quadro, L., & Kahn, B. B. (2005) · Nature · doi:10.1038/nature03711 · Cited by 2,086 · see citing works
Oxidative damage and mitochondrial decay in aging.
Shigenaga, M. K., Hagen, T. M., & Ames, B. N. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.23.10771 · Cited by 2,055 · see citing works
Antioxidant and redox regulation of gene transcription
Sen, C. K., & Packer, L. (1996) · The FASEB Journal · doi:10.1096/fasebj.10.7.8635688 · Cited by 1,996 · see citing works
Alpha-lipoic acid as a biological antioxidant
Packer, L., Witt, E. H., & Tritschler, H. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(95)00017-r · Cited by 1,995 · see citing works
Oxidative Stress and Diabetic Vascular Complications
Giugliano, D., Ceriello, A., & Paolisso, G. (1996) · Diabetes Care · doi:10.2337/diacare.19.3.257 · Cited by 1,938 · see citing works
Cloning and Characterization of Inducible Nitric Oxide Synthase from Mouse Macrophages
Xie, Q. W., Cho, H. J., Calaycay, J. R., Mumford, R. A., Swiderek, K. M., Lee, T. D., Ding, A. H., Troso, T., & Nathan, C. (1992) · Science · doi:10.1126/science.1373522 · Cited by 1,888 · see citing works
Thioredoxin and Glutaredoxin Systems
Holmgren, A. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)71625-6 · Cited by 1,804 · see citing works
Bantle (2008) · doi:10.2337/dc08-s061 · Cited by 1,795 · see citing works
Antioxidants in Human Health and Disease
Halliwell, B. B. (1996) · Annual Review of Nutrition · doi:10.1146/annurev.nu.16.070196.000341 · Cited by 1,707 · see citing works
Regulation of biosynthesis of nitric oxide.
Nathan, C., & Xie, Q. W. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36703-0 · Cited by 1,669 · see citing works
Kim, J.-A., Montagnani, M., Koh, K. K., & Quon, M. J. (2006) · Circulation · doi:10.1161/circulationaha.105.563213 · Cited by 1,652 · see citing works
Oxidative Stress and Vascular Disease
Madamanchi, N. R., Vendrov, A., & Runge, M. S. (2005) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/01.atv.0000150649.39934.13 · Cited by 1,618 · see citing works
Endoplasmic Reticulum Stress and Oxidative Stress: A Vicious Cycle or a Double-Edged Sword?
Malhotra, J. D., & Kaufman, R. J. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1782 · Cited by 1,555 · see citing works
Hayes, J. D., & McLellan, L. I. (1999) · Free Radical Research · doi:10.1080/10715769900300851 · Cited by 1,528 · see citing works
Aguirre, V., Uchida, T., Yenush, L., Davis, R., & White, M. F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.12.9047 · Cited by 1,487 · see citing works
Superoxide generation by endothelial nitric oxide synthase: The influence of cofactors
Vásquez-Vivar, J., Kalyanaraman, B., Martásek, P., Hogg, N., Masters, B. S. S., Karoui, H., Tordo, P., & Pritchard, K. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.16.9220 · Cited by 1,484 · see citing works
Evans, J. L., Goldfine, I. D., Maddux, B. A., & Grodsky, G. M. (2003) · Diabetes · doi:10.2337/diabetes.52.1.1 · Cited by 1,482 · see citing works
Rushmore, T. H., Morton, M. R., & Pickett, C. B. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99004-6 · Cited by 1,464 · see citing works
Nitric oxide, oxidants, and protein tyrosine nitration
Radí, R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307446101 · Cited by 1,456 · see citing works
Protein S-nitrosylation: a physiological signal for neuronal nitric oxide
Jaffrey, S. R., Erdjument‐Bromage, H., Ferris, C. D., Tempst, P., & Snyder, S. H. (2001) · Nature Cell Biology · doi:10.1038/35055104 · Cited by 1,402 · see citing works
Translational Control Is Required for the Unfolded Protein Response and In Vivo Glucose Homeostasis
Scheuner, D. L., Song, B., McEwen, E. L., Liu, C., Laybutt, D. R., Gillespie, P. J., Saunders, T. L., Bonner‐Weir, S., & Kaufman, R. J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00265-9 · Cited by 1,355 · see citing works
Retinol-Binding Protein 4 and Insulin Resistance in Lean, Obese, and Diabetic Subjects
Graham, T. E., Yang, Q., Blüher, M., Hammarstedt, A., Ciaraldi, T. P., Henry, R. R., Wason, C. J., Oberbach, A., Jansson, P.-A., Smith, U., et al. (2006) · New England Journal of Medicine · doi:10.1056/nejmoa054862 · Cited by 1,319 · see citing works
Yan, S. D., Schmidt, A. M., Anderson, G. M., Zhang, J., Brett, J., Zou, Y., Pinsky, D. J., & Stern, D. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36966-1 · Cited by 1,305 · see citing works
Keaney, J. F., Larson, M. G., Vasan, R. S., Wilson, P. W. F., Lipinska, I., Corey, D., Massaro, J. M., Sutherland, P., Vita, J. A., & Benjamin, E. J. (2003) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/01.atv.0000058402.34138.11 · Cited by 1,304 · see citing works
Lipotoxic heart disease in obese rats: Implications for human obesity
Zhou, Y.-T., Grayburn, P., Karim, A., Shimabukuro, M., Higa, M., Baetens, D., Orci, L., & Unger, R. H. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.4.1784 · Cited by 1,265 · see citing works
Adipose Tissue Hypoxia in Obesity and Its Impact on Adipocytokine Dysregulation
Hosogai, N., Fukuhara, A., Oshima, K., Miyata, Y., Tanaka, S., Segawa, K., Furukawa, S., Tochino, Y., Komuro, R., Matsuda, M., et al. (2007) · Diabetes · doi:10.2337/db06-0911 · Cited by 1,257 · cited 2× · see citing works
“All of these conditions or factors have been implicated as causative factors in insulin resistance of adipose tissue and/or muscle (143, 184, 185, 193).”
BackgroundAdipose-selective targeting of the GLUT4 gene impairs insulin action in muscle and liver
Abel, E. D., Peroni, O. D., Kim, J. K., Kim, Y., Boss, O., Hadro, E., Minnemann, T., Shulman, G. I., & Kahn, B. B. (2001) · Nature · doi:10.1038/35055575 · Cited by 1,253 · see citing works
Klaman, L. D., Boss, O., Peroni, O. D., Kim, J. K., Martino, J. L., Zabolotny, J. M., Moghal, N., Lubkin, M., Kim, Y.-B., Sharpe, A. H., et al. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.15.5479-5489.2000 · Cited by 1,235 · 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
Harding, H. P., Zeng, H., Zhang, Y., Jungries, R., Chung, P., Plesken, H., Sabatini, D. D., & Ron, D. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00264-7 · Cited by 1,217 · see citing works
Epidermal Growth Factor (EGF)-induced Generation of Hydrogen Peroxide
Bae, Y. S., Kang, S. W., Seo, M. S., Baines, I., Tekle, E., Chock, P. B., & Rhee, S. G. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.1.217 · Cited by 1,208 · see citing works
4-Hydroxy-2-nonenal: a product and mediator of oxidative stress
Uchida, K. (2003) · Progress in Lipid Research · doi:10.1016/s0163-7827(03)00014-6 · Cited by 1,164 · see citing works
Ron, D., & Habener, J. F. (1992) · Genes & Development · doi:10.1101/gad.6.3.439 · Cited by 1,156 · see citing works
Advances in Male Contraception
Page, S. T., Amory, J. K., & Bremner, W. J. (2008) · Endocrine Reviews · doi:10.1210/er.2007-0041 · Cited by 1,134 · see citing works
REGULATION OF GENE EXPRESSION BY REACTIVE OXYGEN
Dalton, T. P., Shertzer, H. G., & Puga, A. (1999) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.39.1.67 · Cited by 1,112 · see citing works
Activation of NADPH oxidase by AGE links oxidant stress to altered gene expression via RAGE
Wautier, M., Chappey, O., Corda, S., Stern, D. M., Schmidt, A. M., & Wautier, J. (2001) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2001.280.5.e685 · Cited by 1,076 · see citing works
S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding
Hara, M. R., Agrawal, N., Kim, S. F., Cascio, M. B., Fujimuro, M., Ozeki, Y., Takahashi, M., Cheah, J. H., Tankou, S. K., Hester, L. D., et al. (2005) · Nature Cell Biology · doi:10.1038/ncb1268 · Cited by 1,071 · see citing works
Reversible Inactivation of the Tumor Suppressor PTEN by H2O2
Lee, S.-R., Yang, K., Kwon, J., Lee, C., Jeong, W., & Rhee, S. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111899200 · Cited by 1,061 · 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
Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo
Meng, T.-C., Fukada, T., & Tonks, N. K. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00445-8 · Cited by 1,040 · see citing works
The Molecular Basis of Skeletal Muscle Atrophy
Jackman, R. W., & Kandarian, S. C. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00579.2003 · Cited by 1,008 · see citing works
Diabetes and mitochondrial function: Role of hyperglycemia and oxidative stress
Rolo, A. P., & Palmeira, C. M. (2006) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2006.01.003 · Cited by 1,007 · see citing works
The endoplasmic reticulum: a multifunctional signaling organelle
Berridge, M. J. (2002) · Cell Calcium · doi:10.1016/s0143416002001823 · Cited by 978 · see citing works
Lee, S.-R., Kwon, K.-S., Kim, S.-R., & Rhee, S. G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.25.15366 · Cited by 969 · see citing works
Protein carbonylation in human diseases
Dalle-Donne, I., Giustarini, D., Colombo, R., Rossi, R., & Milzani, A. (2003) · Trends in Molecular Medicine · doi:10.1016/s1471-4914(03)00031-5 · Cited by 961 · see citing works
Reactive oxygen species in tumor progression
Peter, S. F. (2005) · Frontiers in bioscience · doi:10.2741/1667 · Cited by 957 · see citing works
Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide.
Holmgren, A. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)83562-7 · Cited by 929 · see citing works
IRS proteins and the common path to diabetes
White, M. F. (2002) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00514.2001 · Cited by 925 · see citing works
Hotamışlıgil, G. S., Johnson, R. S., Distel, R. J., Ellis, R., Papaioannou, V. E., & Spiegelman, B. M. (1996) · Science · doi:10.1126/science.274.5291.1377 · Cited by 917 · see citing works
Protein glycation and oxidative stress in diabetes mellitus and ageing
Wolff, S. P., Jiang, Z. Y., & Hunt, J. V. (1991) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(91)90040-a · Cited by 886 · see citing works
Cardiovascular Actions of Insulin
Muniyappa, R., Montagnani, M., Koh, K. K., & Quon, M. J. (2007) · Endocrine Reviews · doi:10.1210/er.2007-0006 · Cited by 872 · see citing works
TRB3: A <i>tribbles</i> Homolog That Inhibits Akt/PKB Activation by Insulin in Liver
Du, K., Herzig, S., Kulkarni, R. N., & Montminy, M. (2003) · Science · doi:10.1126/science.1079817 · Cited by 842 · see citing works
Identification of Renox, an NAD(P)H oxidase in kidney
Geiszt, M., Kopp, J. B., Várnai, P., & Leto, T. L. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.130135897 · Cited by 840 · see citing works
Bonnard, C., Durand, A., Peyrol, S., Chanseaume, E., Chauvin, M.-A., Morio, B., Vidal, H., & Rieusset, J. (2008) · Journal of Clinical Investigation · doi:10.1172/jci32601 · Cited by 819 · see citing works
Delépine, M., Nicolino, M., Barrett, T., Golamaully, M., Mark Lathrop, G., & Julier, C. (2000) · Nature Genetics · doi:10.1038/78085 · Cited by 813 · see citing works
Mitochondrial Dysfunction in Atherosclerosis
Madamanchi, N. R., & Runge, M. S. (2007) · Circulation Research · doi:10.1161/01.res.0000258450.44413.96 · Cited by 794 · see citing works
Role of oxidative carbonylation in protein quality control and senescence
Nyström, T. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600599 · Cited by 791 · see citing works
Functional analysis of Nox4 reveals unique characteristics compared to other NADPH oxidases
Martyn, K. D., Frederick, L. M., von Loehneysen, K., Dinauer, M. C., & Knaus, U. G. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2005.03.023 · Cited by 783 · see citing works
The role of TNFα and TNF receptors in obesity and insulin resistance
Hotamisligil, G. S. (1999) · Journal of Internal Medicine · doi:10.1046/j.1365-2796.1999.00490.x · Cited by 780 · see citing works
Serine Phosphorylation of Insulin Receptor Substrate 1 by Inhibitor κB Kinase Complex
Gao, Z., Hwang, D. H., Bataille, F., Lefevre, M., York, D. A., Quon, M. J., & Ye, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m209459200 · Cited by 777 · see citing works
Hayashi, T., Hirshman, M. F., Kurth, E. J., Winder, W. W., & Goodyear, L. J. (1998) · Diabetes · doi:10.2337/diab.47.8.1369 · Cited by 774 · see citing works
Regulation of protein function by S‐glutathiolation in response to oxidative and nitrosative stress
Klatt, P., & Lamas, S. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01601.x · Cited by 751 · see citing works
Zeng, G., Nystrom, F. H., Ravichandran, L. V., Cong, L.-N., Kirby, M., Mostowski, H., & Quon, M. J. (2000) · Circulation · doi:10.1161/01.cir.101.13.1539 · Cited by 745 · see citing works
Davı̀, G., Ciabattoni, G., Consoli, A., Mezzetti, A., Falco, A., Santarone, S., Pennese, E., Vitacolonna, E., Bucciarelli, T., Costantini, F., et al. (1999) · Circulation · doi:10.1161/01.cir.99.2.224 · Cited by 742 · see citing works
Zeng, G., & Quon, M. J. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118871 · Cited by 726 · see citing works
Thioredoxin and Related Molecules–From Biology to Health and Disease
Lillig, C. H., & Holmgren, A. (2007) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.9.25 · Cited by 724 · see citing works
Effects of Long-Term Selenium Supplementation on the Incidence of Type 2 Diabetes
Stranges, S., Marshall, J. R., Natarajan, R., Donahue, R. P., Trevisan, M., Combs, G. F., Cappuccio, F. P., Ceriello, A., & Reid, M. E. (2007) · Annals of Internal Medicine · doi:10.7326/0003-4819-147-4-200708210-00175 · Cited by 715 · see citing works
5' AMP-activated protein kinase activation causes GLUT4 translocation in skeletal muscle.
Kurth-Kraczek, E. J., Hirshman, M. F., Goodyear, L. J., & Winder, W. W. (1999) · Diabetes · doi:10.2337/diabetes.48.8.1667 · Cited by 715 · see citing works
Kaneto, H., Kajimoto, Y., Miyagawa, J., Matsuoka, T., Fujitani, Y., Umayahara, Y., Hanafusa, T., Matsuzawa, Y., Yamasaki, Y., & Hori, M. (1999) · Diabetes · doi:10.2337/diabetes.48.12.2398 · Cited by 713 · see citing works
Han, D., Antunes, F., Canali, R., Rettori, D., & Cadenas, E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210269200 · Cited by 711 · see citing works
(S)NO Signals: Translocation, Regulation, and a Consensus Motif
Stamler, J. S., Toone, E. J., Lipton, S. A., & Sucher, N. J. (1997) · Neuron · doi:10.1016/s0896-6273(00)80310-4 · Cited by 674 · see citing works
Recent advances torwards understanding redox mechanisms in the activation of nuclear factor κb
Janssen-Heininger, Y. M. W., Poynter, M. E., & Baeuerle, P. A. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00218-5 · Cited by 666 · see citing works
Neuroprotection by the Metabolic Antioxidant α-Lipoic Acid
Packer, L., Tritschler, H. J., & Wessel, K. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00269-9 · Cited by 639 · see citing works
Kuboki, K., Jiang, Z. Y., Takahara, N., Ha, S. W., Igarashi, M., Yamauchi, T., Feener, E. P., Herbert, T. P., Rhodes, C. J., & King, G. L. (2000) · Circulation · doi:10.1161/01.cir.101.6.676 · Cited by 636 · see citing works
Degradation of Misfolded Proteins Prevents ER-Derived Oxidative Stress and Cell Death
Haynes, C. M., Titus, E. A., & Cooper, A. A. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.08.025 · Cited by 627 · see citing works
The Endoplasmic Reticulum: Folding, Calcium Homeostasis, Signaling, and Redox Control
Görlach, A., Klappa, P., & Kietzmann, T. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1391 · Cited by 616 · see citing works
Mitochondrial remodeling in adipose tissue associated with obesity and treatment with rosiglitazone.
Wilson-Fritch, L., Nicoloro, S., Chouinard, M., Lazar, M. A., Chui, P. C., Leszyk, J., Straubhaar, J., Czech, M. P., & Corvera, S. (2004) · Journal of Clinical Investigation · doi:10.1172/jci21752 · Cited by 616 · see citing works
Redox regulation of PI 3‐kinase signalling via inactivation of PTEN
Leslie, N. R., Bennett, D., Lindsay, Y. E., Stewart, H., Gray, A., & Downes, C. P. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg513 · Cited by 614 · see citing works
Mice overexpressing human uncoupling protein-3 in skeletal muscle are hyperphagic and lean
Clapham, J. C., Arch, J. R. S., Chapman, H., Haynes, A., Lister, C., Moore, G. B. T., Piercy, V., Carter, S. A., Lehner, I., Smith, S. A., et al. (2000) · Nature · doi:10.1038/35019082 · Cited by 604 · see citing works
Rui, L., Aguirre, V., Kim, J. K., Shulman, G. I., Lee, A., Corbould, A. M., Dunaif, A. E., & White, M. F. (2001) · Journal of Clinical Investigation · doi:10.1172/jci10934 · Cited by 600 · see citing works
Regulation of γ-Glutamylcysteine Synthetase Subunit Gene Expression by the Transcription Factor Nrf2
Wild, A. C., Moinova, H., & Mulcahy, R. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.47.33627 · Cited by 595 · see citing works
Schmitz-Peiffer, C., Craig, D. L., & Biden, T. J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.34.24202 · Cited by 592 · see citing works
The Molecular Basis for Oxidative Stress-Induced Insulin Resistance
Evans, J. L., Maddux, B. A., & Goldfine, I. D. (2005) · Antioxidants & Redox Signaling · doi:10.1089/ars.2005.7.1040 · Cited by 587 · see citing works
Gregor, M. F., & Hotamisligil, G. S. (2007) · Journal of Lipid Research · doi:10.1194/jlr.r700007-jlr200 · Cited by 586 · see citing works
Increased myocardial NADPH oxidase activity in human heart failure
Heymes, C., Bendall, J. K., Ratajczak, P., Cave, A. C., Samuel, J., Hasenfuss, G. P., & Shah, A. M. (2003) · Journal of the American College of Cardiology · doi:10.1016/s0735-1097(03)00471-6 · Cited by 582 · see citing works
Mitochondrial respiration is decreased in skeletal muscle of patients with type 2 diabetes
Mogensen, M., Sahlin, K., Fernström, M., Glintborg, D., Vind, B. F., Beck-Nielsen, H., & Højlund, K. (2007) · Diabetes · doi:10.2337/db06-0981 · Cited by 573 · see citing works
Mechanisms that regulate production of reactive oxygen species by cytochrome P450
Zangar, R. C. (2004) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2004.01.018 · Cited by 555 · see citing works
Coordination of ER and oxidative stress signaling: The PERK/Nrf2 signaling pathway
Cullinan, S. B., & Diehl, J. A. (2006) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.09.018 · Cited by 554 · see citing works
Kopecky, J., Clarke, G., Enerbäck, S., Spiegelman, B., & Kozak, L. P. (1995) · Journal of Clinical Investigation · doi:10.1172/jci118363 · Cited by 553 · see citing works
Hunt, J. V., Smith, C. C., & Wolff, S. P. (1990) · Diabetes · doi:10.2337/diab.39.11.1420 · Cited by 553 · see citing works
Cloned human brain nitric oxide synthase is highly expressed in skeletal muscle
Nakane, M., Schmidt, H. H. H. W., Pollock, J. S., Förstermann, U., & Murad, F. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)81210-q · Cited by 546 · see citing works
Montagnani, M., Chen, H., Barr, V. A., & Quon, M. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103702200 · Cited by 543 · see citing works
Platelet Activation in Obese Women
Davı̀, G., Guagnano, M. T., Ciabattoni, G., Basili, S., Falco, A., Marinopiccoli, M., Nutini, M., Sensi, S., & Patrono, C. (2002) · JAMA · doi:10.1001/jama.288.16.2008 · Cited by 542 · see citing works
Perreault, M., & Marette, A. (2001) · Nature Medicine · doi:10.1038/nm1001-1138 · Cited by 540 · see citing works
The Unfolded Protein Response: A Pathway That Links Insulin Demand with β-Cell Failure and Diabetes
Scheuner, D., & Kaufman, R. J. (2008) · Endocrine Reviews · doi:10.1210/er.2007-0039 · Cited by 525 · see citing works
AMPK: A Key Sensor of Fuel and Energy Status in Skeletal Muscle
Hardie, D. G., & Sakamoto, K. (2006) · Physiology · doi:10.1152/physiol.00044.2005 · Cited by 519 · see citing works
A Novel Superoxide-producing NAD(P)H Oxidase in Kidney
Shiose, A., Kuroda, J., Tsuruya, K., Hirai, M., Hirakata, H., Naito, S., Hattori, M., Sakaki, Y., & Sumimoto, H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007597200 · Cited by 517 · see citing works
Mahadev, K., Motoshima, H., Wu, X., Ruddy, J. M., Arnold, R. S., Cheng, G., Lambeth, J. D., & Goldstein, B. J. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.5.1844-1854.2004 · Cited by 513 · see citing works
Selenium and endocrine systems
Beckett, G. J., & Arthur, J. R. (2005) · Journal of Endocrinology · doi:10.1677/joe.1.05971 · Cited by 513 · see citing works
Mahadev, K., Zilbering, A., Zhu, L., & Goldstein, B. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100109200 · Cited by 509 · see citing works
Feskens, E. J. M., Virtanen, S. M., Räsänen, L., Tuomilehto, J. O., Stengård, J., Pekkanen, J., Nissinen, A. M., & Kromhout, D. (1995) · Diabetes Care · doi:10.2337/diacare.18.8.1104 · Cited by 504 · see citing works
Biological selectivity and functional aspects of protein tyrosine nitration
Ischiropoulos, H. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00814-3 · Cited by 500 · 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
Lund, S., Holman, G. D., Schmitz, O., & Pedersen, O. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.13.5817 · Cited by 492 · see citing works
Regulation of PTP1B via Glutathionylation of the Active Site Cysteine 215
Barrett, W. C., DeGnore, J. P., König, S., Fales, H. M., Keng, Y., Zhang, Z., Yim, M. B., & Chock, P. B. (1999) · Biochemistry · doi:10.1021/bi990240v · Cited by 488 · 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
Self-citationCotgreave, I. A., & Gerdes, R. G. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7812 · Cited by 481 · see citing works
Endoplasmic Reticulum Stress: Signaling the Unfolded Protein Response
Lai, E., Teodoro, T., & Volchuk, A. (2007) · Physiology · doi:10.1152/physiol.00050.2006 · Cited by 478 · see citing works
Factors Associated with Oxidative Stress in Human Populations
Block, G. (2002) · American Journal of Epidemiology · doi:10.1093/aje/kwf029 · Cited by 475 · see citing works
Cellular regulation of endothelial nitric oxide synthase
Govers, R., & Rabelink, T. J. (2001) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.2001.280.2.f193 · Cited by 474 · see citing works
Free radical biology and medicine: it's a gas, man!
Pryor, W. A., Houk, K. N., Foote, C. S., Fukuto, J. M., Ignarro, L. J., Squadrito, G. L., & Davies, K. J. A. (2006) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00614.2005 · Cited by 465 · see citing works
Involvement of Endoplasmic Reticulum Stress in Insulin Resistance and Diabetes
Nakatani, Y., Kaneto, H., Kawamori, D., Yoshiuchi, K., Hatazaki, M., Matsuoka, T., Ozawa, K., Ogawa, S., Hori, M., Yamasaki, Y., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m411860200 · Cited by 462 · see citing works
Prevention of glucose toxicity in HIT-T15 cells and Zucker diabetic fatty rats by antioxidants
Tanaka, Y., Gleason, C. E., Tran, P. O. T., Harmon, J. S., & Robertson, R. P. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.19.10857 · Cited by 460 · see citing works
Specificity of a third kind: reactive oxygen and nitrogen intermediates in cell signaling
Nathan, C. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200318174 · Cited by 455 · see citing works
Wells, W. W., Xu, D. P., Yang, Y., & Rocque, P. A. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55401-6 · Cited by 450 · see citing works
Akt1 regulates pathological angiogenesis, vascular maturation and permeability in vivo
Chen, J., Somanath, P. R., Razorenova, O. V., Chen, W. S., Hay, N., BORNSTEIN, P. K., & Byzova, T. V. (2005) · Nature Medicine · doi:10.1038/nm1307 · Cited by 450 · see citing works
Reactive oxygen species as essential mediators of cell adhesion
Chiarugi, P., Pani, G., Giannoni, E., Taddei, L., Colavitti, R., Raugei, G., Symons, M. C. R., Borrello, S., Galeotti, T., & Ramponi, G. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211118 · Cited by 444 · see citing works
Chemistry, physiology and pathology of free radicals
Bergendi, L., Beneš, L., Ďuračková, Z., & Ferencĭk, M. (1999) · Life Sciences · doi:10.1016/s0024-3205(99)00439-7 · Cited by 439 · see citing works
Inoguchi, T., Sonta, T., Tsubouchi, H., Etoh, T., Kakimoto, M., Sonoda, N., Sato, N., Sekiguchi, N., Kobayashi, K., Sumimoto, H., et al. (2003) · Journal of the American Society of Nephrology · doi:10.1097/01.asn.0000077407.90309.65 · Cited by 435 · see citing works
Pédruzzi, E., Guichard, C., Ollivier, V., Driss, F., Fay, M., Prunet, C., Marie, J., Pouzet, C., Samadi, M. H., Elbim, C., et al. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.24.10703-10717.2004 · Cited by 435 · see citing works
Oxidative stress and potential interventions to reduce oxidative stress in overweight and obesity
Vincent, H. K., Innes, K. E., & Vincent, K. R. (2007) · Diabetes Obesity and Metabolism · doi:10.1111/j.1463-1326.2007.00692.x · Cited by 432 · see citing works
Mitochondrial reactive oxygen species-mediated signaling in endothelial cells
Zhang, D. X., & Gutterman, D. D. (2007) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01283.2006 · Cited by 432 · see citing works
Heffetz, D., Bushkin, I., Dror, R., & Zick, Y. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39885-0 · Cited by 429 · see citing works
Dietary Antioxidant Intake and Risk of Type 2 Diabetes
Montonen, J., Knekt, P., Järvinen, R., & Reunanen, A. (2004) · Diabetes Care · doi:10.2337/diacare.27.2.362 · Cited by 423 · see citing works
Higashi, M., Shimokawa, H., Hattori, T., Hiroki, J., Mukai, Y., Morikawa, K., Ichiki, T., Takahashi, S., & Takeshita, A. (2003) · Circulation Research · doi:10.1161/01.res.0000096650.91688.28 · Cited by 420 · see citing works
Detection of nitrotyrosine in the diabetic plasma: evidence of oxidative stress
Mercuri, F., Tonutti, L., Taboga, C., Ceriello, A., Assaloni, R., Motz, E., & Quagliaro, L. (2001) · Diabetologia · doi:10.1007/s001250100529 · Cited by 418 · see citing works
Molecular Basis of Insulin-stimulated GLUT4 Vesicle Trafficking
Pessin, J. E., Thurmond, D. C., Elmendorf, J. S., Coker, K. J., & Okada, S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.5.2593 · Cited by 413 · see citing works
UV-induced reactive oxygen species in photocarcinogenesis and photoaging.
Scharffetter‐Kochanek, K., Wlaschek, M., Brenneisen, P., Schauen, M., Blaudschun, R., & Wenk, J. (1997) · PubMed · Cited by 406 · see citing works
Maddux, B. A., See, W., Lawrence, J. C., Goldfine, A. L., Goldfine, I. D., & Evans, J. L. (2001) · Diabetes · doi:10.2337/diabetes.50.2.404 · Cited by 405 · see citing works
Xue, X., Piao, J., Nakajima, A., Komazawa‐Sakon, S., Kojima, Y., Mori, K., Yagita∥, H., Okumura, K., Harding, H. P., & Nakano, H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505818200 · Cited by 400 · see citing works
Human studies related to protein oxidation: protein carbonyl content as a marker of damage.
Chevion, M., Berenshtein, E., & Stadtman, E. R. (2000) · PubMed · Cited by 400 · see citing works
Reactions of 4-hydroxynonenal with proteins and cellular targets
Petersen, D. R., & Doorn, J. A. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.06.012 · Cited by 393 · see citing works
Ames, B. N., Shigenaga, M. K., & Hagen, T. M. (1995) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/0925-4439(95)00024-x · Cited by 391 · see citing works
Gopaul, N. K., Änggård, E. E., Mallet, A. I., Betteridge, D. J., Wolff, S. P., & Nourooz-Zadeh, J. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00649-t · Cited by 390 · see citing works
Xanthine Oxidase Is Involved in Free Radical Production in Type 1 Diabetes
Desco, C., Asensi, M. A., Márquez, R., Martínez-Valls, J. F., Vento, M., Pallardó, F. V., Sastre, J., & Viña, J. (2002) · Diabetes · doi:10.2337/diabetes.51.4.1118 · Cited by 390 · see citing works
Proposed mechanisms for the induction of insulin resistance by oxidative stress
Bloch-Damti, A., & Bashan, N. (2005) · Antioxidants & Redox Signaling · doi:10.1089/ars.2005.7.1553 · Cited by 388 · see citing works
Self-citationBalligand, J., Kobzik, L., Han, X., Kaye, D. M., Belhassen, L., O’Hara, D. S., Kelly, R. A., Smith, T. W., & Michel, T. M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.24.14582 · Cited by 388 · see citing works
Serum Selenium and Diabetes in U.S. Adults
Bleys, J., Navas‐Acién, A., & Güallar, E. (2007) · Diabetes Care · doi:10.2337/dc06-1726 · Cited by 384 · see citing works
Protein Nitration in Cardiovascular Diseases
Turko, I. V., & Murad, F. (2002) · Pharmacological Reviews · doi:10.1124/pr.54.4.619 · Cited by 372 · see citing works
Powell, D. J., Hajduch, É., Kular, G. S., & Hundal, H. S. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.21.7794-7808.2003 · Cited by 371 · see citing works
Stephens, J. M., & Pekala, P. H. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54714-1 · Cited by 370 · see citing works
GLUT4 heterozygous knockout mice develop muscle insulin resistance and diabetes
Stenbit, A. E., Tsao, T., Li, J., Burcelin, R., Geenen, D. L., Factor, S. M., Houseknecht, K. L., Katz, E. B., & Charron, M. J. (1997) · Nature Medicine · doi:10.1038/nm1097-1096 · Cited by 367 · see citing works
Oxidative Stress and Programmed Cell Death in Diabetic Neuropathy
Vincent, A. M., Brownlee, M., & Russell, J. W. (2002) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2002.tb02108.x · Cited by 362 · see citing works
Corda, S., Laplace, C., Vicaut, É., & Duranteau, J. (2001) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.24.6.4228 · Cited by 352 · see citing works
Modulation of Oxidant and Antioxidant Enzyme Expression and Function in Vascular Cells
Waßmann, S., Wassmann, K., & Nickenig, G. (2004) · Hypertension · doi:10.1161/01.hyp.0000142232.29764.a7 · Cited by 352 · see citing works
Shah, V. H., Haddad, F., García‐Cardeña, G., Frangos, J. A., Mennone, A., Groszmann, R. J., & Sessa, W. C. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119842 · Cited by 349 · see citing works
Thallas‐Bonke, V., Thorpe, S. R., Coughlan, M. T., Fukami, K., Yap, F. Y. T., Sourris, K. C., Penfold, S. A., Bach, L. A., Cooper, M. E., & Forbes, J. M. (2007) · Diabetes · doi:10.2337/db07-1119 · Cited by 345 · see citing works
Kiritoshi, S., Nishikawa, T., Sonoda, K., Kukidome, D., Senokuchi, T., Matsuo, T., Matsumura, T., Tokunaga, H., Brownlee, M., & Araki, E. (2003) · Diabetes · doi:10.2337/diabetes.52.10.2570 · Cited by 345 · see citing works
Tumor Necrosis Factor-α Induces Endothelial Dysfunction in the Prediabetic Metabolic Syndrome
Picchi, A., Gao, X. J., Belmadani, S., Potter, B. J., Focardi, M., Chilian, W. M., & Zhang, C. (2006) · Circulation Research · doi:10.1161/01.res.0000229685.37402.80 · Cited by 343 · see citing works
Fruit and Vegetable Consumption and Diabetes Mellitus Incidence among U.S. Adults
Ford, E. S., & Mokdad, A. H. (2001) · Preventive Medicine · doi:10.1006/pmed.2000.0772 · Cited by 341 · see citing works
Reversible Glutathionylation Regulates Actin Polymerization in A431 Cells
Wang, J., Boja, E. S., Tan, W., Tekle, E., Fales, H. M., English, S., Mieyal, J. J., & Chock, P. B. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100415200 · Cited by 336 · see citing works
Protein oxidation in response to increased transcriptional or translational errors
Dukan, S., Farewell, A., Ballesteros, M., Taddéi, F., Radman, M., & Nyström, T. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.100422497 · Cited by 334 · see citing works
Shinozaki, K., Kashiwagi, A., Nishio, Y., Okamura, T., Yoshida, Y., Masada, M., Toda, N., & Kikkawa, R. (1999) · Diabetes · doi:10.2337/diabetes.48.12.2437 · Cited by 329 · see citing works
Expression and Localization of NOX2 and NOX4 in Primary Human Endothelial Cells
van Buul, J. D., Fernandez‐Borja, M., Anthony, E. C., & Hordijk, P. L. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.308 · Cited by 326 · see citing works
Mitochondrial reactive oxygen species reduce insulin secretion by pancreatic β-cells
Sakai, K., Matsumoto, K., Nishikawa, T., Suefuji, M., Nakamaru, K., Hirashima, Y., Kawashima, J., Shirotani, T., Ichinose, K., Brownlee, M., et al. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)02832-2 · Cited by 323 · see citing works
Ser/Thr Phosphorylation of IRS Proteins: A Molecular Basis for Insulin Resistance
Zick, Y. (2005) · Science s STKE · doi:10.1126/stke.2682005pe4 · Cited by 320 · see citing works
Paolisso, G., D'Amore, A., Giugliano, D., Ceriello, A., Varricchio, M., & D'Onofrio, F. (1993) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/57.5.650 · Cited by 316 · see citing works
Ridnour, L. A., Thomas, D. D., Mancardi, D., Espey, M. G., Miranda, K. M., Paolocci, N., Feelisch, M., Fukuto, J., & Wink, D. A. (2004) · Biological Chemistry · doi:10.1515/bc.2004.001 · Cited by 312 · see citing works
Diet-induced changes in uncoupling proteins in obesity-prone and obesity-resistant strains of mice
Surwit, R. S., Wang, S., Petro, A. E., Sanchı́s, D., Raimbault, S., Ricquier, D., & Collins, S. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.7.4061 · Cited by 311 · see citing works
Contraction signaling to glucose transport in skeletal muscle
Jessen, N., & Goodyear, L. J. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00175.2005 · Cited by 311 · cited 1× · see citing works
“AMPK is a central signaling kinase mediating increased glucose uptake in muscle under conditions of high AMP/ATP ratio, like hypoxia and muscle contraction, constituting a non-insulin-dependent pathway to increase muscle glucose utilization (119, 159, 162, 181, 213, 246).”
BackgroundMohr, S., Hallak, H., de Boitte, A., Lapetina, E. G., & Brüne, B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.14.9427 · Cited by 309 · see citing works
He, Y., & Häder, D. P. (2002) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/s1011-1344(02)00231-2 · Cited by 305 · see citing works
Tirosh, A., Potashnik, R., Bashan, N., & Rudich, A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.15.10595 · Cited by 301 · see citing works
Self-citationMahadev, K., Wu, X., Zilbering, A., Zhu, L., Lawrence, J. T. R., & Goldstein, B. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105061200 · Cited by 298 · see citing works
Shankar, R. R., Yu-ling, W., Shen, H.-Q., Zhu, J. S., & Baron, A. (2000) · Diabetes · doi:10.2337/diabetes.49.5.684 · Cited by 297 · see citing works
Angiotensin II-induced NADPH Oxidase Activation Impairs Insulin Signaling in Skeletal Muscle Cells
Wei, Y., Sowers, J. R., Nistala, R., Gong, H., Uptergrove, G. M., Clark, S. E., Morris, E. M., Szary, N. M., Manrique, C. M., & Stump, C. S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601320200 · Cited by 297 · see citing works
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1 of the 489 references couldn’t be matched to a known paper.
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Oxidative stress, aging, and diseases
Liguori, I., Russo, G., Curcio, F., Bulli, G., Aran, L., Della-Morte, D., Gargiulo, G., Testa, G., Cacciatore, F., Bonaduce, D., et al. (2018) · Clinical Interventions in Aging · doi:10.2147/cia.s158513 · Cited by 3,979 · see citing works
Mechanisms of Insulin Action and Insulin Resistance
Petersen, M. C., & Shulman, G. I. (2018) · Physiological Reviews · doi:10.1152/physrev.00063.2017 · Cited by 3,028 · see citing works
Free Radicals: Properties, Sources, Targets, and Their Implication in Various Diseases
Phaniendra, A., Jestadi, D. B., & Periyasamy, L. (2015) · Indian Journal of Clinical Biochemistry · doi:10.1007/s12291-014-0446-0 · Cited by 2,886 · see citing works
Brigelius-Flohé, R., & Maiorino, M. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.11.020 · Cited by 1,904 · see citing works
Design Strategies for Water-Soluble Small Molecular Chromogenic and Fluorogenic Probes
Li, X., Gao, X., Shi, W. S., & Ma, H. (2013) · Chemical Reviews · doi:10.1021/cr300508p · Cited by 1,734 · see citing works
Graves, D. B. (2012) · Journal of Physics D Applied Physics · doi:10.1088/0022-3727/45/26/263001 · Cited by 1,512 · see citing works
Mitochondrial ROS Signaling in Organismal Homeostasis
Shadel, G. S., & Horvath, T. L. (2015) · Cell · doi:10.1016/j.cell.2015.10.001 · Cited by 1,353 · see citing works
Mitochondria in oxidative stress, inflammation and aging: from mechanisms to therapeutic advances
Xu, X., Pang, Y., & Fan, X. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02253-4 · Cited by 939 · see citing works
Tebay, L. E., Robertson, H., Durant, S. T., Vitale, S. R., Penning, T. M., Dinkova-Kostova, A. T., & Hayes, J. D. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.021 · Cited by 837 · see citing works
Gambini, J., Inglés, M., González, G. O., López-Grueso, R., Bonet-Costa, V., Gimeno-Mallench, L., Mas‐Bargues, C., Abdelaziz, K. M., Gómez‐Cabrera, M. C., Viña, J., et al. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/837042 · Cited by 752 · see citing works
Free Radical Properties, Source and Targets, Antioxidant Consumption and Health
Martemucci, G., Costagliola, C., Mariano, M., D’Andrea, L., Napolitano, P., & D‘Alessandro, A. G. (2022) · Oxygen · doi:10.3390/oxygen2020006 · Cited by 781 · see citing works
Mechanisms of insulin resistance in obesity
Ye, J. (2013) · Frontiers of Medicine · doi:10.1007/s11684-013-0262-6 · Cited by 699 · see citing works
A Unique Approach to Development of Near-Infrared Fluorescent Sensors for in Vivo Imaging
Yuan, L., Lin, W., Zhao, S., Gao, W., Chen, B., He, L., & Zhu, S. (2012) · Journal of the American Chemical Society · doi:10.1021/ja305802v · Cited by 682 · see citing works
Weidinger, A., & Kozlov, A. V. (2015) · Biomolecules · doi:10.3390/biom5020472 · Cited by 648 · see citing works
The Essential Element Manganese, Oxidative Stress, and Metabolic Diseases: Links and Interactions
Li, L., & Yang, X. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/7580707 · Cited by 660 · see citing works
Insulin resistance is a cellular antioxidant defense mechanism
Hoehn, K. L., Salmon, A. B., Hohnen-Behrens, C., Turner, N., Hoy, A. J., Maghzal, G. J., Stocker, R., Van Remmen, H., Kraegen, E. W., Cooney, G. J., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0902380106 · Cited by 540 · see citing works
Potential health hazards of eating red meat
Wolk, A. (2016) · Journal of Internal Medicine · doi:10.1111/joim.12543 · Cited by 524 · see citing works
Ohta, S. (2014) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2014.04.006 · Cited by 526 · see citing works
Insulin Resistance, Obesity and Lipotoxicity
Yazıcı, D., & Sezer, H. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-48382-5_12 · Cited by 507 · see citing works
Reactive Oxygen Species in Skeletal Muscle Signaling
Barbieri, E., & Sestili, P. (2011) · Journal of Signal Transduction · doi:10.1155/2012/982794 · Cited by 414 · see citing works
Oxidative Stress in Diabetes: Implications for Vascular and Other Complications
Pitocco, D., Tesauro, M., Rizzi, A., Ghirlanda, G., & Cardillo, C. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms141121525 · Cited by 409 · see citing works
Role of mitochondrial reactive oxygen species in homeostasis regulation
Zhang, B., Pan, C., Feng, C., Yan, C., Yu, Y., Chen, Z., Guo, C., & Wang, X. (2022) · Redox Report · doi:10.1080/13510002.2022.2046423 · Cited by 397 · see citing works
Yuan, L., Lin, W., Xie, Y., Chen, B., & Zhu, S. (2011) · Journal of the American Chemical Society · doi:10.1021/ja2100577 · Cited by 387 · see citing works
Redox Control of the Cell Cycle in Health and Disease
Sarsour, E. H., Kumar, M. G., Chaudhuri, L., Kalen, A. L., & Goswami, P. C. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2513 · Cited by 379 · see citing works
Induction of Oxidative Stress in Kidney
Özbek, E. (2012) · International Journal of Nephrology · doi:10.1155/2012/465897 · Cited by 377 · see citing works
Redox Regulation by Keap1 and Nrf2 Controls Intestinal Stem Cell Proliferation in Drosophila
Hochmuth, C. E., Biteau, B., Bohmann, D., & Jasper, H. (2011) · Cell stem cell · doi:10.1016/j.stem.2010.12.006 · Cited by 364 · see citing works
Mas‐Bargues, C., Escrivá, C., Dromant, M., Borrás, C., & Viña, J. (2021) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2021.108941 · Cited by 347 · see citing works
Oxidative Stress, Nitric Oxide, and Diabetes
Pitocco, D., Zaccardi, F., Stasio, E. D., Romitelli, F., Santini, S. A., Zuppi, C., & Ghirlanda, G. (2010) · The Review of Diabetic Studies · doi:10.1900/rds.2010.7.15 · Cited by 335 · see citing works
Lee, H.-Y., Choi, C. S., Birkenfeld, A. L., Alves, T. C., Jornayvaz, F. R., Jurczak, M. J., Zhang, D., Woo, D. K., Shadel, G. S., Ladiges, W., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.11.004 · Cited by 319 · see citing works
Linking mitochondrial bioenergetics to insulin resistance via redox biology
Fisher-Wellman, K. H., & Neufer, P. D. (2012) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2011.12.008 · Cited by 316 · see citing works
Molecular Mechanisms behind Free Radical Scavengers Function against Oxidative Stress
Ahmadinejad, F., Møller, S. G., Chaleshtori, M. H., Bidkhori, G., & Jami, M. (2017) · Antioxidants · doi:10.3390/antiox6030051 · Cited by 299 · see citing works
Martins, A. R., Nachbar, R. T., Gorjão, R., Vinolo, M. A. R., Festuccia, W. T., Lambertucci, R. H., Cury‐Boaventura, M. F., Silveira, L. R., Curi, R., & Hirabara, S. M. (2012) · Lipids in Health and Disease · doi:10.1186/1476-511x-11-30 · Cited by 288 · see citing works
Bensellam, M., Laybutt, D., & Jonas, J. (2012) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2012.08.003 · Cited by 282 · see citing works
AGE restriction in diabetes mellitus: a paradigm shift
Vlassara, H., & Striker, G. E. (2011) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2011.74 · Cited by 277 · see citing works
Muscle Atrophy Induced by Mechanical Unloading: Mechanisms and Potential Countermeasures
Gao, Y., Arfat, Y., Wang, H., & Goswami, N. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00235 · Cited by 275 · see citing works
Diabetes and Alpha Lipoic Acid
Golbidi, S., Badran, M., & Laher, I. (2011) · Frontiers in Pharmacology · doi:10.3389/fphar.2011.00069 · Cited by 261 · see citing works
Sadiq, I. Z. (2021) · Current Molecular Medicine · doi:10.2174/1566524022666211222161637 · Cited by 284 · see citing works
Hormones and oxidative stress: an overview
Chainy, G., & Sahoo, D. K. (2019) · Free radical research · doi:10.1080/10715762.2019.1702656 · Cited by 235 · see citing works
Bajaj, S., & Khan, A. A. (2012) · Indian Journal of Endocrinology and Metabolism · doi:10.4103/2230-8210.104057 · Cited by 262 · see citing works
Mitochondrial fatty acid oxidation in obesity
Serra, D., Mera, P., Malandrino, M. I., Mir, J. F., & Herrero, L. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4875 · Cited by 246 · see citing works
White adipose tissue mitochondrial metabolism in health and in obesity
Heinonen, S., Jokinen, R., Rissanen, A., & Pietiläinen, K. H. (2019) · Obesity Reviews · doi:10.1111/obr.12958 · Cited by 243 · see citing works
Molecular Hydrogen as a Novel Antioxidant
Ohta, S. (2015) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2014.11.038 · Cited by 224 · see citing works
Role of Oxidative Stress as Key Regulator of Muscle Wasting during Cachexia
Ábrigo, J., Elorza, Á. A., Riedel, C. A., Vilos, C., Simón, F., Cabrera, D., Estrada, L. D., & Cabello‐Verrugio, C. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/2063179 · Cited by 221 · see citing works
Health Benefits of Fasting and Caloric Restriction
Golbidi, S., Daiber, A., Korać, B., Li, H., Essop, M. F., & Laher, I. (2017) · Current Diabetes Reports · doi:10.1007/s11892-017-0951-7 · Cited by 218 · see citing works
Dong, B., Song, X., Kong, X., Wang, C., Tang, Y., Liu, Y., & Lin, W. (2016) · Advanced Materials · doi:10.1002/adma.201602939 · Cited by 217 · see citing works
The dynamic plasticity of insulin production in β-cells
Boland, B. B., Rhodes, C. J., & Grimsby, J. S. (2017) · Molecular Metabolism · doi:10.1016/j.molmet.2017.04.010 · Cited by 194 · see citing works
Emerging Role of Nitric Oxide and Heat Shock Proteins in Insulin Resistance
Molina, M. N., Ferder, L., & Manucha, W. A. (2015) · Current Hypertension Reports · doi:10.1007/s11906-015-0615-4 · Cited by 199 · see citing works
Antioxidants in the Treatment of Diabetes
Golbidi, S., Ebadi, S. A., & Laher, I. (2011) · Current Diabetes Reviews · doi:10.2174/157339911794940729 · Cited by 197 · see citing works
Rudrappa, S. S., Wilkinson, D. J., Greenhaff, P. L., Smith, K., IDRIS, I. R., & Atherton, P. J. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2016.00361 · Cited by 194 · see citing works
Postprandial metabolic events and fruit-derived phenolics: a review of the science
Burton‐Freeman, B. M. (2010) · British Journal Of Nutrition · doi:10.1017/s0007114510003909 · Cited by 185 · see citing works
Kim, Y., Keogh, J., & Clifton, P. (2015) · Metabolism · doi:10.1016/j.metabol.2015.03.008 · Cited by 181 · see citing works
Molecular Targets Related to Inflammation and Insulin Resistance and Potential Interventions
Hirabara, S. M., Gorjão, R., Vinolo, M. A. R., Rodrigues, A. C., Nachbar, R. T., & Curi, R. (2012) · BioMed Research International · doi:10.1155/2012/379024 · Cited by 178 · see citing works
ROS signaling and redox biology in endothelial cells
Panieri, E., & Santoro, M. M. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1928-9 · Cited by 168 · see citing works
Yu, Z., Shao, W., Chiang, Y., Foltz, W. D., Zhang, Z., Ling, W., Fantus, I. G., & Jin, T. (2010) · Diabetologia · doi:10.1007/s00125-010-2001-8 · Cited by 173 · see citing works
Chiurchiù, V., & Maccarrone, M. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3547 · Cited by 171 · see citing works
Mita, Y., Nakayama, K., Inari, S., Nishito, Y., Yoshioka, Y., Sakai, N., Sotani, K., Nagamura, T., Kuzuhara, Y., Inagaki, K., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01863-z · Cited by 170 · see citing works
Methods for Assessing Mitochondrial Function in Diabetes
Perry, C. G. R., Kane, D. A., Lanza, I. R., & Neufer, P. D. (2013) · Diabetes · doi:10.2337/db12-1219 · Cited by 169 · see citing works
Corby‐Harris, V., Drexler, A., de Jong, L. W., Antonova, Y., Pakpour, N., Ziegler, R., Ramberg, F. B., Lewis, E. E., Brown, J. M., Luckhart, S., et al. (2010) · PLoS Pathogens · doi:10.1371/annotation/738ac91f-8c41-4bf5-9a39-bddf0b777a89 · Cited by 169 · see citing works
Pi, J., Bai, Y., Daniel, K. W., Liu, D., Lyght, O., Edelstein, D., Brownlee, M., Corkey, B. E., & Collins, S. (2009) · Endocrinology · doi:10.1210/en.2008-1642 · Cited by 163 · see citing works
Reactive species and diabetes: counteracting oxidative stress to improve health
Pérez‐Matute, P., Zulet, M. Á., & Martínez, J. A. (2009) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2009.08.005 · Cited by 160 · see citing works
Vascular actions of insulin with implications for endothelial dysfunction
Potenza, M. A., Addabbo, F., & Montagnani, M. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00297.2009 · Cited by 162 · see citing works
Agil, A., Reiter, R. J., Jiménez‐Aranda, A., Arias, R. I., Navarro‐Alarcón, M., Marchal, J. A., Adem, A., & Fernández‐Vázquez, G. (2012) · Journal of Pineal Research · doi:10.1111/jpi.12012 · Cited by 159 · see citing works
Imaging ROS signaling in cells and animals
Wang, X., Fang, H., Huang, Z., Shang, W. H., Hou, T., Cheng, A., & Cheng, H. (2013) · Journal of Molecular Medicine · doi:10.1007/s00109-013-1067-4 · Cited by 163 · see citing works
Pillon, N. J., Croze, M. L., Vella, R., Soulère, L., Lagarde, M., & Soulage, C. O. (2012) · Endocrinology · doi:10.1210/en.2011-1957 · Cited by 154 · see citing works
Redox Control of the Survival of Healthy and Diseased Cells
Zhang, Y., Du, Y., Le, W., Wang, K., Kieffer, N., & Zhang, J. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3685 · Cited by 156 · see citing works
Redox biology of exercise: an integrative and comparative consideration of some overlooked issues
Nikolaidis, M. G., Kyparos, A., Spanou, C., Paschalis, V., Theodorou, A. A., & Vrabas, I. S. (2012) · Journal of Experimental Biology · doi:10.1242/jeb.067470 · Cited by 152 · see citing works
Antioxidant and Anti-Inflammatory Effects of Exercise in Diabetic Patients
Golbidi, S., Badran, M., & Laher, I. (2011) · Experimental Diabetes Research · doi:10.1155/2012/941868 · Cited by 151 · see citing works
Regulation of Redox Signaling by Selenoproteins
Hawkes, W. C., & Alkan, Z. (2010) · Biological Trace Element Research · doi:10.1007/s12011-010-8656-7 · Cited by 151 · see citing works
Teodoro, J. S., Nunes, S., Rolo, A. P., Reis, F., & Palmeira, C. M. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2018.01857 · Cited by 149 · see citing works
Corby‐Harris, V., Drexler, A., de Jong, L. W., Antonova, Y., Pakpour, N., Ziegler, R., Ramberg, F. B., Lewis, E. E., Brown, J. M., Luckhart, S., et al. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1001003 · Cited by 148 · see citing works
Vlassara, H., Uribarri, J., Cai, W., Goodman, S., Pyzik, R., Post, J. B., Grosjean, F., Woodward, M., & Striker, G. E. (2012) · Clinical Journal of the American Society of Nephrology · doi:10.2215/cjn.12891211 · Cited by 143 · see citing works
Linking Alzheimer's disease to insulin resistance: the FoxO response to oxidative stress
Manolopoulos, K. N., Klotz, L.-O., Korsten, P., Bornstein, S. R., & Barthel, A. (2010) · Molecular Psychiatry · doi:10.1038/mp.2010.17 · Cited by 150 · see citing works
Chung, M. J., Cho, S., Bhuiyan, M. J. H., Kim, K. H., & Lee, S. (2010) · British Journal Of Nutrition · doi:10.1017/s0007114510001765 · Cited by 136 · see citing works
Metal-based anti-diabetic drugs: advances and challenges
Levina, A., & Lay, P. A. (2011) · Dalton Transactions · doi:10.1039/c1dt10380f · Cited by 135 · see citing works
Cinnamon effects on metabolic syndrome: a review based on its mechanisms.
Mollazadeh, H., & Hosseinzadeh, H. (2016) · Europe PMC (PubMed Central) · doi:10.22038/ijbms.2016.7906 · Cited by 145 · see citing works
Morgan, A. E., Mooney, K. M., Wilkinson, S. J., Pickles, N. A., & Auley, M. T. M. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.03.008 · Cited by 136 · see citing works
Forkhead Box O as a Sensor, Mediator, and Regulator of Redox Signaling
de Keizer, P. L. J., Burgering, B. M. T., & Dansen, T. B. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3403 · Cited by 131 · see citing works
Multi-mechanisms are involved in reactive oxygen species regulation of mTORC1 signaling
Li, M., Zhao, L., Liu, J., Liu, A., Jia, C., Ma, D., Jiang, Y., & Bai, X. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.05.015 · Cited by 129 · see citing works
D’Cruz, S. C., Jubendradass, R., Mannu, J., Rani, S. J. A., & Mathur, P. P. (2011) · Food and Chemical Toxicology · doi:10.1016/j.fct.2011.11.041 · Cited by 126 · see citing works
Monosodium glutamate-induced oxidative kidney damage and possible mechanisms: a mini-review
Sharma, A. (2015) · Journal of Biomedical Science · doi:10.1186/s12929-015-0192-5 · Cited by 123 · see citing works
Sim, C., & Denlinger, D. L. (2011) · Journal of Insect Physiology · doi:10.1016/j.jinsphys.2011.01.012 · Cited by 122 · see citing works
Murdolo, G., Piroddi, M., Luchetti, F., Tortoioli, C., Canonico, B., Zerbinati, C., Galli, F., & Iuliano, L. (2012) · Biochimie · doi:10.1016/j.biochi.2012.12.014 · Cited by 120 · see citing works
Sex Differences in Cancer Cachexia
Zhong, X.-L., & Zimmers, T. (2020) · Current Osteoporosis Reports · doi:10.1007/s11914-020-00628-w · Cited by 98 · see citing works
Vergoni, B., Cornejo, P.-J., Gilleron, J., Djedaini, M., Ceppo, F., Jacquel, A., Bouget, G., Ginet, C., Gonzalez, T., Maillet, J., et al. (2016) · Diabetes · doi:10.2337/db16-0014 · Cited by 119 · see citing works
Samjoo, I. A., Safdar, A., Hamadeh, M. J., Raha, S., & Tarnopolsky, M. A. (2013) · Nutrition and Diabetes · doi:10.1038/nutd.2013.30 · Cited by 118 · see citing works
Longato, L., Tong, M., Wands, J. R., & de la Monte, S. M. (2011) · Hepatology Research · doi:10.1111/j.1872-034x.2011.00934.x · Cited by 117 · see citing works
Oxidative Stress and Diabetic Kidney Disease
Stanton, R. C. (2011) · Current Diabetes Reports · doi:10.1007/s11892-011-0196-9 · Cited by 112 · see citing works
Hypomorphism in human NSMCE2 linked to primordial dwarfism and insulin resistance
Payne, F., Colnaghi, R., Rocha, N., Seth, A., Harris, J., Carpenter, G., Bottomley, W. E., Wheeler, E., Wong, S., Saudek, V., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci73264 · Cited by 112 · see citing works
Recent developments in manganese corrole chemistry
Liu, H., Mahmood, M. H., Qiu, S., & Chang, C. K. (2013) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.12.017 · Cited by 111 · see citing works
Redox regulation of the insulin signalling pathway
Lennicke, C., & Cochemé, H. M. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101964 · Cited by 111 · see citing works
Influence of exercise intensity on systemic oxidative stress and antioxidant capacity
Parker, L., McGuckin, T., & Leicht, A. S. (2013) · Clinical Physiology and Functional Imaging · doi:10.1111/cpf.12108 · Cited by 110 · see citing works
van Golen, R. F., Reiniers, M. J., Vrisekoop, N., Zuurbier, C. J., Olthof, P. B., van Rheenen, J., van Gulik, T. M., Parsons, B. J., & Heger, M. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5751 · Cited by 110 · see citing works
Essential actions of melatonin in protecting the ovary from oxidative damage
Cruz, M. H. C., Leal, C. L. V., da Cruz, J. F., Tan, D. X., & Reiter, R. J. (2014) · Theriogenology · doi:10.1016/j.theriogenology.2014.07.011 · Cited by 110 · see citing works
Kaur, U., Banerjee, P., Bir, A., Sinha, M. S., Biswas, A., & Chakrabarti, S. (2015) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026615666150114160543 · Cited by 107 · see citing works
Zhu, T., Ren, N., Liu, X., Dong, Y., Wang, R., Gao, J., Sun, J., Zhu, Y., Wang, L., Fan, C., et al. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202015650 · Cited by 106 · see citing works
Muscle insulin resistance: assault by lipids, cytokines and local macrophages
Kewalramani, G., Bilan, P. J., & Klip, A. (2010) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0b013e32833aabd9 · Cited by 106 · see citing works
Zhou, Y., Zhang, X., Yang, S., Li, Y., Qing, Z., Zheng, J., Li, J., & Yang, R. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.7b00073 · Cited by 102 · see citing works
Bansal, G., Singh, S., Monga, V., Veeraveedu, P. T., & Chawla, P. A. (2019) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2019.103271 · Cited by 101 · see citing works
Signaling of Reactive Oxygen and Nitrogen Species in Diabetes Mellitus
Afanasʹev, I. B. (2010) · Oxidative Medicine and Cellular Longevity · doi:10.4161/oxim.3.6.14415 · Cited by 100 · see citing works
A new model for mitochondrial membrane potential production and storage
Bagkos, G., Koufopoulos, K., & Piperi, C. (2014) · Medical Hypotheses · doi:10.1016/j.mehy.2014.05.001 · Cited by 98 · see citing works
- Authors
- Bashan, N., Kovsan, J., Kachko, I., Ovadia, H., & Rudich, A.
- Affiliations
- Ben-Gurion University of the Negev (IL)
- ORCID
- Rudich, Assaf
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2009-01
- Volume
- 89
- Issue
- 1
- Pages
- 27-71
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W2110657098
- Cited by
- 542
- References
- 489
- Citations by year
- 2026: 4 · 2025: 20 · 2024: 20 · 2023: 16 · 2022: 28 · 2021: 26 · 2020: 29 · 2019: 42 · 2018: 27 · 2017: 31 · 2016: 39 · 2015: 48 · 2014: 49 · 2013: 43 · 2012: 42
- FWCI
- 3.03
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Physiological Reviews (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Keywords
- insulin signaling, reactive oxygen species, reactive nitrogen species, insulin resistance, type 2 diabetes, obesity, antioxidant defense, prooxidant-antioxidant balance, insulin action, oxidative stress
- MeSH terms
- Animals, Antioxidants, Humans, Insulin, Insulin Resistance, Signal Transduction, Reactive Oxygen Species, Oxidative Stress, Reactive Nitrogen Species
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