Redox Control of Endothelial Function and Dysfunction: Molecular Mechanisms and Therapeutic Opportunities
Abstract
The endothelium is essential for the maintenance of vascular homeostasis. Central to this role is the production of endothelium-derived nitric oxide (EDNO), synthesized by the endothelial isoform of nitric oxide synthase (eNOS). Endothelial dysfunction, manifested as impaired EDNO bioactivity, is an important early event in the development of various vascular diseases, including hypertension, diabetes, and atherosclerosis. The degree of impairment of EDNO bioactivity is a determinant of future vascular complications. Accordingly, growing interest exists in defining the pathologic mechanisms involved. Considerable evidence supports a causal role for the enhanced production of reactive oxygen species (ROS) by vascular cells. ROS directly inactivate EDNO, act as cell-signaling molecules, and promote protein dysfunction, events that contribute to the initiation and progression of endothelial dysfunction. Increasing data indicate that strategies designed to limit vascular ROS production can restore endothelial function in humans with vascular complications. The purpose of this review is to outline the various ways in which ROS can influence endothelial function and dysfunction, describe the redox mechanisms involved, and discuss approaches for preventing endothelial dysfunction that may highlight future therapeutic opportunities in the treatment of cardiovascular disease.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
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?
Elevated reactive oxygen species lead to endothelial dysfunction, an early event in atherosclerosis pathogenesis that occurs mainly during atherosclerotic lesion formation.
“Indeed, elevated ROS levels lead to endothelial dysfunction171, an early event in atherosclerosis pathogenesis that occurs mainly in atherosclerotic lesion formation172,173.”
From Mitochondrial and metabolic dysfunction in ageing and age-related diseases (2022) · cites this paper as [171]
Cites
3 retracted
Ushio‐Fukai, M., Tang, Y., Fukai, T., Dikalov, S., Ma, Y., Fujimoto, M., Quinn, M. T., Pagano, P. J., Johnson, C., & Alexander, R. W. (2002) · Circulation Research · doi:10.1161/01.res.0000046227.65158.f8 · Cited by 463 · see citing works
RetractedAbid, M. R., Tsai, J. C., Spokes, K., Deshpande, S. S., Irani, K., & Aird, W. C. (2001) · The FASEB Journal · doi:10.1096/fj.01-0338fje · Cited by 157 · see citing works
RetractedUncoupling of Endothelial Nitric Oxidase Synthase by Hypochlorous Acid
Xu, J., Xie, Z., Reece, R., Pimental, D. R., & Zou, M. (2006) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000249394.94588.82 · Cited by 144 · see citing works
RetractedThe 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
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
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
Endothelial dysfunction in cardiovascular diseases: the role of oxidant stress
Cai, H., & Harrison, D. G. (2000) · Circulation Research · doi:10.1161/01.res.87.10.840 · Cited by 3,839 · see citing works
Circulating endothelial progenitor cells, vascular function, and cardiovascular risk
Hill, J. M., Zalos, G., Halcox, J. P. J., Schenke, W. H., Waclawiw, M. A., Quyyumi, A. A., & Finkel, T. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa022287 · Cited by 3,423 · see citing works
Angiotensin II stimulates NADH and NADPH oxidase activity in cultured vascular smooth muscle cells.
Griendling, K. K., Minieri, C. A., Ollerenshaw, J. D., & Alexander, R. W. (1994) · Circulation Research · doi:10.1161/01.res.74.6.1141 · Cited by 2,735 · 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
Schächinger, V., Britten, M. B., & Zeiher, A. M. (2000) · Circulation · doi:10.1161/01.cir.101.16.1899 · Cited by 2,584 · 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
Paradoxical Vasoconstriction Induced by Acetylcholine in Atherosclerotic Coronary Arteries
Ludmer, P. L., Selwyn, A. P., Shook, T., Wayne, R. R., Mudge, G. H., Alexander, R. W., & Ganz, P. (1986) · New England Journal of Medicine · doi:10.1056/nejm198610233151702 · Cited by 2,422 · see citing works
The Pecking Order of Free Radicals and Antioxidants: Lipid Peroxidation, α-Tocopherol, and Ascorbate
Buettner, G. R. (1993) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1993.1074 · Cited by 2,417 · cited 1× · see citing works
“Although capable of mediating oneelectron oxidation reactions, O2 represents a stronger reductant than oxidant (60).”
Superoxide anion is involved in the breakdown of endothelium-derived vascular relaxing factor
Gryglewski, R. J., Palmer, R. M. J., & Moncada, S. (1986) · Nature · doi:10.1038/320454a0 · Cited by 2,407 · 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
Urbich, C., & Dimmeler, S. (2004) · Circulation Research · doi:10.1161/01.res.0000137877.89448.78 · Cited by 2,364 · see citing works
Garg, U. C., & Hassid, A. (1989) · Journal of Clinical Investigation · doi:10.1172/jci114081 · Cited by 2,154 · 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
Book ReviewAmbulatory Pediatric Care
Steinberg, J. B. (1989) · New England Journal of Medicine · doi:10.1056/nejm198901053200122 · Cited by 2,121 · see citing works
Hypertension in mice lacking the gene for endothelial nitric oxide synthase
Huang, P. L., Huang, Z., Mashimo, H., Bloch, K. D., Moskowitz, M. A., Bevan, J. A., & Fishman, M. C. (1995) · Nature · doi:10.1038/377239a0 · Cited by 2,070 · see citing works
Circulating endothelial progenitor cells and cardiovascular outcomes
Werner, N., Kosiol, S., Schiegl, T., Ahlers, P., Walenta, K., Link, A., Böhm, M., & Nickenig, G. (2005) · New England Journal of Medicine · doi:10.1056/nejmoa043814 · Cited by 2,048 · see citing works
Long-Term Follow-Up of Patients With Mild Coronary Artery Disease and Endothelial Dysfunction
Suwaidi, J. M. S. A., Hamasaki, S., Higano, S. T., Nishimura, R. A., Holmes, D. R., & Lerman, A. (2000) · Circulation · doi:10.1161/01.cir.101.9.948 · Cited by 2,044 · see citing works
Heitzer, T., Schlinzig, T., Krohn, K., Meinertz, T., & Münzel, T. (2001) · Circulation · doi:10.1161/hc4601.099485 · Cited by 1,961 · see citing works
Mitochondrial reactive oxygen species trigger hypoxia-induced transcription
Chandel, N. S., Maltepe, E., Goldwasser, E., Mathieu, C. E., Simon, M. C., & Schumacker, P. T. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.20.11715 · Cited by 1,926 · see citing works
Upregulation of Endothelial Nitric Oxide Synthase by HMG CoA Reductase Inhibitors
Laufs, U., Fata, V. L., Plutzky, J., & Liao, J. K. (1998) · Circulation · doi:10.1161/01.cir.97.12.1129 · Cited by 1,837 · see citing works
Role of endothelium-derived nitric oxide in the regulation of blood pressure.
Rees, D. D., Palmer, R. M. J., & Moncada, S. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.9.3375 · Cited by 1,827 · see citing works
Kamata, H., Honda, S.-I., Maeda, S., Chang, L., Hirata, H., & Karin, M. (2005) · Cell · doi:10.1016/j.cell.2004.12.041 · Cited by 1,792 · see citing works
The p66shc adaptor protein controls oxidative stress response and life span in mammals
Migliaccio, E., Giorgio, M., Mele, S., Pelicci, G., Reboldi, P., Pandolfi, P. P., Lanfrancone, L., & Pelicci, P. G. (1999) · Nature · doi:10.1038/46311 · Cited by 1,712 · see citing works
Landmesser, U., Dikalov, S., Price, S. R., McCann, L., Fukai, T., Holland, S. M., Mitch, W. E., & Harrison, D. G. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200314172 · Cited by 1,660 · see citing works
Landmesser, U., Dikalov, S., Price, S. R., McCann, L. A., Fukai, T., Holland, S. M., Mitch, W. E., & Harrison, D. G. (2003) · Journal of Clinical Investigation · doi:10.1172/jci14172 · Cited by 1,652 · see citing works
Hydrogen peroxide sensing and signaling
Veal, E. A., Day, A. M., & Morgan, B. A. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.03.016 · Cited by 1,604 · see citing works
Mitochondrial complex III is required for hypoxia-induced ROS production and cellular oxygen sensing
Guzy, R. D., Hoyos, B., Robin, E., Chen, H., Liu, L., Mansfield, K. D., Simon, M. C., Hammerling, U., & Schumacker, P. T. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.05.001 · Cited by 1,545 · see citing works
Formation of nitric oxide-derived inflammatory oxidants by myeloperoxidase in neutrophils
Eiserich, J. P., Hristova, M., Cross, C. E., Jones, A. D., Freeman, B. A., Halliwell, B., & van der Vliet, A. (1998) · Nature · doi:10.1038/34923 · Cited by 1,496 · 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
Zhang, D. D., & Hannink, M. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.22.8137-8151.2003 · Cited by 1,480 · see citing works
Kureishi, Y., Luo, Z., Shiojima, I., Bialik, A., Fulton, D. J., Lefer, D. J., Sessa, W. C., & Walsh, K. (2000) · Nature Medicine · doi:10.1038/79510 · Cited by 1,437 · see citing works
Oxidant signals and oxidative stress
Finkel, T. (2003) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(03)00002-4 · Cited by 1,393 · see citing works
Treasure, C. B., Klein, J., Weintraub, W. S., Talley, J., Stillabower, M., Kosinski, A. S., Zhang, J., Boccuzzi, S., Cedarholm, J. C., & Alexander, R. (1995) · New England Journal of Medicine · doi:10.1056/nejm199502233320801 · Cited by 1,335 · see citing works
Essential role of endothelial nitric oxide synthase for mobilization of stem and progenitor cells
Aicher, A., Heeschen, C., Mildner-Rihm, C., Urbich, C., Ihling, C. H., Technau‐Ihling, K., Zeiher, A. M., & Dimmeler, S. (2003) · Nature Medicine · doi:10.1038/nm948 · Cited by 1,297 · see citing works
Role of oxidative stress in atherosclerosis
Harrison, D., Griendling, K. K., Landmesser, U., Hornig, B., & Drexler, H. (2003) · The American Journal of Cardiology · doi:10.1016/s0002-9149(02)03144-2 · Cited by 1,275 · see citing works
Pleiotropic Effects of 3-Hydroxy-3-Methylglutaryl Coenzyme A Reductase Inhibitors
Takemoto, M., & Liao, J. K. (2001) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/hq1101.098486 · Cited by 1,272 · see citing works
Daugherty, A., Dunn, J. L., Rateri, D. L., & Heinecke, J. W. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117342 · Cited by 1,269 · see citing works
Mitochondrial biogenesis in mammals: the role of endogenous nitric oxide
Nisoli, E., Clementi, E., Paolucci, C., Cozzi, V., Tonello, C., Sciorati, C., Bracale, R., Valerio, A., Francolini, M., Moncada, S., et al. (2003) · Science · doi:10.1126/science.1079368 · Cited by 1,243 · see citing works
Böger, R. H., Bode-Böger, S. M., Szuba, A., Tsao, P. S., Chan, J. R., Tangphao, O., Blaschke, T. F., & Cooke, J. P. (1998) · Circulation · doi:10.1161/01.cir.98.18.1842 · Cited by 1,181 · see citing works
Mechanisms Underlying Endothelial Dysfunction in Diabetes Mellitus
Hink, U., Li, H., Mollnau, H., Oelze, M., Matheis, E., Hartmann, M., Skatchkov, M. P., Thaiss, F., Stahl, R. A. K., Warnholtz, A., et al. (2001) · Circulation Research · doi:10.1161/01.res.88.2.e14 · Cited by 1,176 · see citing works
Giorgio, M., Migliaccio, E., Orsini, F., Paolucci, D., Moroni, M., Contursi, C., Pelliccia, G., Luzi, L., Minucci, S., Marcaccio, M., et al. (2005) · Cell · doi:10.1016/j.cell.2005.05.011 · Cited by 1,176 · see citing works
Targeting Antioxidants to Mitochondria by Conjugation to Lipophilic Cations
Murphy, M. P., & Smith, R. A. J. (2007) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.47.120505.105110 · Cited by 1,173 · see citing works
Coronary vasomotor response to acetylcholine relates to risk factors for coronary artery disease.
Vita, J. A., Treasure, C. B., Nabel, E. G., McLenachan, J. M., Fish, R. D., Yeung, A. C., Vekshtein, V. I., Selwyn, A. P., & Ganz, P. (1990) · Circulation · doi:10.1161/01.cir.81.2.491 · Cited by 1,172 · see citing works
Killing activity of neutrophils is mediated through activation of proteases by K+ flux
Reeves, E. P., Lu, H., Jacobs, H. L., Messina, C. G. M., Bolsover, S., Gabella, G., Potma, E. O., Warley, A., Roes, J., & Segal, A. W. (2002) · Nature · doi:10.1038/416291a · Cited by 1,153 · 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
Calorie restriction promotes mitochondrial biogenesis by inducing the expression of eNOS
Nisoli, E., Tonello, C., Cardile, A., Cozzi, V., Bracale, R., Tedesco, L., Falcone, S., Valerio, A., Cantoni, O., Clementi, E., et al. (2005) · Science · doi:10.1126/science.1117728 · Cited by 1,107 · see citing works
Membrane transport of hydrogen peroxide
Bienert, G. P., Schjoerring, J. K., & Jahn, T. P. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.02.015 · Cited by 1,079 · see citing works
Marui, N., Offermann, M. K., Swerlick, R., Kunsch, C., Rosen, C. A., Ahmad, M., Alexander, R. W., & Medford, R. M. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116778 · Cited by 1,072 · see citing works
Prognostic Value of Myeloperoxidase in Patients with Chest Pain
Brennan, M., Penn, M. S., Lente, F. V., Nambi, V., Shishehbor, M. H., Aviles, R. J., Goormastic, M., Pepoy, M. L., McErlean, E. S., Topol, E. J., et al. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa035003 · Cited by 1,071 · see citing works
&NA; (1996) · Journal of Occupational and Environmental Medicine · doi:10.1097/00043764-199605000-00005 · Cited by 1,070 · see citing works
Carew, T. E., Schwenke, D. C., & Steinberg, D. H. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.21.7725 · Cited by 1,040 · 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
Dynamic activation of endothelial nitric oxide synthase by Hsp90
García‐Cardeña, G., Fan, R., Shah, V. H., Sorrentino, R., Cirino, G., Papapetropoulos, A., & Sessa, W. C. (1998) · Nature · doi:10.1038/33934 · Cited by 1,029 · see citing works
Myeloperoxidase Serum Levels Predict Risk in Patients With Acute Coronary Syndromes
Baldus, S. E., Heeschen, C., Meinertz, T., Zeiher, A. M., Eiserich, J. P., Münzel, T. F., Simoons, M. L., & Hamm, C. W. (2003) · Circulation · doi:10.1161/01.cir.0000090690.67322.51 · Cited by 1,007 · see citing works
Vasa‐Nicotera, M., Fichtlscherer, S., Adler, K., Aicher, A., Martin, H., Zeiher, A. M., & Dimmeler, S. (2001) · Circulation · doi:10.1161/hc2401.092816 · Cited by 1,007 · see citing works
Wakabayashi, N., Dinkova-Kostova, A. T., Holtzclaw, W. D., Kang, M.-I., Kobayashi, A., Yamamoto, M., Kensler, T. W., & Talalay, P. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307301101 · Cited by 986 · see citing works
Mechanisms of Increased Vascular Superoxide Production in Human Diabetes Mellitus
Guzik, T. J., Mussa, S., Gastaldi, D., Sadowski, J., Ratnatunga, C., Pillai, R. G., & Channon, K. M. (2002) · Circulation · doi:10.1161/01.cir.0000012748.58444.08 · Cited by 979 · 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
Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
Salmeen, A., Andersen, J. N., Myers, M. P., Meng, T.-C., Hinks, J. A., Tonks, N. K., & Barford, D. (2003) · Nature · doi:10.1038/nature01680 · Cited by 951 · see citing works
Denu, J. M., & Tanner, K. G. (1998) · Biochemistry · doi:10.1021/bi973035t · Cited by 945 · see citing works
Association Between Myeloperoxidase Levels and Risk of Coronary Artery Disease
Zhang, R. (2001) · JAMA · doi:10.1001/jama.286.17.2136 · Cited by 919 · see citing works
Redox activation of Fos‐Jun DNA binding activity is mediated by a DNA repair enzyme.
Xanthoudakis, S., Miao, G. G., Wang, F., Pan, Y., & Curran, T. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05411.x · Cited by 913 · see citing works
Cytochrome P450 2C is an EDHF synthase in coronary arteries
Fißlthaler, B., Popp, R., Kiss, L., Potente, M., Harder, D. R., Fleming, I., & Busse, R. (1999) · Nature · doi:10.1038/46816 · Cited by 911 · see citing works
Du, X. L., Edelstein, D., Dimmeler, S., Ju, Q., Sui, C., & Brownlee, M. (2001) · Journal of Clinical Investigation · doi:10.1172/jci11235 · Cited by 907 · see citing works
Uncoupling: new approaches to an old problem of bioenergetics
Skulachev, V. P. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(97)00091-1 · Cited by 893 · see citing works
Mattagajasingh, I., Kim, C.-S., Naqvi, A., Yamamori, T., Hoffman, T. A., Jung, S.-B., DeRicco, J., Kasuno, K., & Irani, K. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0704329104 · Cited by 881 · see citing works
Kugiyama, K., Kerns, S. A., Morrisett, J. D., Roberts, R., & Henry, P. D. (1990) · Nature · doi:10.1038/344160a0 · Cited by 858 · see citing works
Superoxide Production and Expression of Nox Family Proteins in Human Atherosclerosis
Sorescu, D., Weiss, D., Lassègue, B., Clempus, R. E., Szöcs, K., Sorescu, G. P., Valppu, L., Quinn, M. T., Lambeth, J. D., Vega, J. D., et al. (2002) · Circulation · doi:10.1161/01.cir.0000012917.74432.66 · Cited by 847 · see citing works
Hazen, S. L., & Heinecke, J. W. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119379 · 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
Du, X., Matsumura, T., Edelstein, D., Rossetti, L., Zsengellér, Z. K., Szabó, C., & Brownlee, M. (2003) · Journal of Clinical Investigation · doi:10.1172/jci18127 · Cited by 832 · see citing works
Matthews, J. R., Wakasugi, N., Virelizier, J., Yodoi, J., & Hay, R. T. (1992) · Nucleic Acids Research · doi:10.1093/nar/20.15.3821 · Cited by 831 · see citing works
Direct evidence for the importance of endothelium-derived nitric oxide in vascular remodeling.
Rudic, R. D., Shesely, E. G., Maeda, N., Smithies, O., Segal, S. S., & Sessa, W. C. (1998) · Journal of Clinical Investigation · doi:10.1172/jci1699 · Cited by 821 · see citing works
Homologs of gp91 phox : cloning and tissue expression of Nox3, Nox4, and Nox5
Cheng, G., Cao, Z., Xu, X., Meir, E. G. V., & Lambeth, J. D. (2001) · Gene · doi:10.1016/s0378-1119(01)00449-8 · Cited by 820 · see citing works
L-arginine improves endothelium-dependent vasodilation in hypercholesterolemic humans.
Creager, M. A., Gallagher, S. J., Girerd, X. J., Coleman, S. M., Dzau, V. J., & Cooke, J. P. (1992) · Journal of Clinical Investigation · doi:10.1172/jci115987 · Cited by 813 · see citing works
Lander, H. M., Tauras, J. M., Ogiste, J. S., Hori, O., Moss, R. A., & Schmidt, A. M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.28.17810 · Cited by 813 · see citing works
Drexler, H., Zeiher, A. M., Meinzer, K., & Just, H. (1991) · The Lancet · doi:10.1016/0140-6736(91)92372-9 · Cited by 801 · see citing works
Stocker, R., Bowry, V. W., & Frei, B. B. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.5.1646 · Cited by 794 · see citing works
Is NF-kappaB the sensor of oxidative stress?
Li, N., & Karin, M. (1999) · PubMed · Cited by 786 · see citing works
Gokce, N., Keaney, J. F., Hunter, L. M., Watkins, M. T., Menzoı́an, J. O., & Vita, J. A. (2002) · Circulation · doi:10.1161/01.cir.0000012543.55874.47 · Cited by 782 · see citing works
Role of Dicer and Drosha for Endothelial MicroRNA Expression and Angiogenesis
Kuehbacher, A., Urbich, C., Zeiher, A. M., & Dimmeler, S. (2007) · Circulation Research · doi:10.1161/circresaha.107.153916 · Cited by 782 · see citing works
Fleming, I., Fisslthaler, B., Dimmeler, S., Kemp, B. E., & Busse, R. (2001) · Circulation Research · doi:10.1161/hh1101.092677 · Cited by 770 · see citing works
Watson, A. D., Leitinger, N., Navab, M., Faull, K. F., Hörkkö, S., Witztum, J. L., Palinski, W., Schwenke, D., Salomon, R. G., Sha, W., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.21.13597 · Cited by 753 · see citing works
Evgenov, O. V., Pacher, P., Schmidt, P. M., Haskó, G., Schmidt, H. H. H. W., & Stasch, J. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2038 · Cited by 750 · see citing works
Yuhanna, I. S., Zhu, Y., Cox, B. E., Hahner, L., Osborne-Lawrence, S. L., Lu, P., Marcel, Y. L., Anderson, R. G. W., Mendelsohn, M. E., Hobbs, H. H., et al. (2001) · Nature Medicine · doi:10.1038/89986 · Cited by 742 · see citing works
Apocynin Is Not an Inhibitor of Vascular NADPH Oxidases but an Antioxidant
Heumüller, S., Wind, S., Barbosa-Sicard, E., Schmidt, H. H. H. W., Busse, R., Schröder, K., & Brandes, R. P. (2008) · Hypertension · doi:10.1161/hypertensionaha.107.100214 · Cited by 735 · see citing works
Laursen, J. B., Somers, M., Kurz, S., McCann, L., Warnholtz, A., Freeman, B. A., Tarpey, M., Fukai, T., & Harrison, D. G. (2001) · Circulation · doi:10.1161/01.cir.103.9.1282 · Cited by 721 · see citing works
Hydrogen peroxide is an endothelium-derived hyperpolarizing factor in mice
Matoba, T., Shimokawa, H., Nakashima, M., Hirakawa, Y., Mukai, Y., Hirano, K., Kanaide, H., & Takeshita, A. (2000) · Journal of Clinical Investigation · doi:10.1172/jci10506 · Cited by 721 · 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
Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins
Rhee, S. G., Kang, S. W., Jeong, W., Chang, T.-S., Yang, K., & Woo, H. A. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.02.004 · Cited by 709 · see citing works
Protein carbamylation links inflammation, smoking, uremia and atherogenesis
Wang, Z., Nicholls, S. J., Rodríguez, E. R., Kummu, O., Hörkkö, S., Barnard, J., Reynolds, W. F., Topol, E. J., DiDonato, J. A., & Hazen, S. L. (2007) · Nature Medicine · doi:10.1038/nm1637 · Cited by 706 · see citing works
Redox Redux: Revisiting PTPs and the Control of Cell Signaling
Tonks, N. K. (2005) · Cell · doi:10.1016/j.cell.2005.05.016 · Cited by 702 · see citing works
Is NF‐κB the sensor of oxidative stress?
Li, N., & Karin, M. (1999) · The FASEB Journal · doi:10.1096/fasebj.13.10.1137 · Cited by 702 · see citing works
Protein kinase C signaling and oxidative stress
Gopalakrishna, R., & Jaken, S. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00221-5 · Cited by 701 · cited 2× · see citing works
“cysteines in the C-terminal catalytic domain can inhibit PKC activity (184).”
HMG-CoA reductase inhibitor mobilizes bone marrow–derived endothelial progenitor cells
Llevadot, J., Murasawa, S., Kureishi, Y., Uchida, S., Masuda, H., Kawamoto, A., Walsh, K., Isner, J. M., & Asahara, T. (2001) · Journal of Clinical Investigation · doi:10.1172/jci13131 · Cited by 701 · see citing works
Sugiyama, S., Okada, Y., Sukhova, G. K., Virmani, R., Heinecke, J. W., & Libby, P. (2001) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64036-9 · Cited by 699 · see citing works
HDL induces NO-dependent vasorelaxation via the lysophospholipid receptor S1P3
Nofer, J., van der Giet, M., Tölle, M., Wolinska, I., Lipinski, K. V. W., Baba, H. A., Tietge, U. J. F., Gödecke, A., Ishii, I., Kleuser, B., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci18004 · Cited by 694 · see citing works
Myeloperoxidase, a Leukocyte-Derived Vascular NO Oxidase
Eiserich, J. P., Baldus, S. E., Brennan, M., Ma, W., Zhang, C., Tousson, A., Castro, L., Lusis, A. J., Nauseef, W. M., White, C. R., et al. (2002) · Science · doi:10.1126/science.1106830 · Cited by 685 · see citing works
Mollnau, H., Wendt, M., Szöcs, K., Lassègue, B., Schulz, E., Oelze, M., Li, H., Bodenschatz, M., August, M., Kleschyov, A. L., et al. (2002) · Circulation Research · doi:10.1161/01.res.0000012569.55432.02 · Cited by 676 · see citing works
Increased NADH-Oxidase–Mediated Superoxide Production in the Early Stages of Atherosclerosis
Warnholtz, A., Nickenig, G., Schulz, E., Macharzina, R. R., Bräsen, J. H., Skatchkov, M. P., Heitzer, T. A., Stasch, J. P., Griendling, K. K., Harrison, D. G., et al. (1999) · Circulation · doi:10.1161/01.cir.99.15.2027 · Cited by 676 · 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
S-Glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide
Adachi, T. K., Weisbrod, R. M., Pimentel, D. R., Ying, J., Sharov, V. S., Schöneich, C., & Cohen, R. A. (2004) · Nature Medicine · doi:10.1038/nm1119 · Cited by 662 · see citing works
Stolk, J. N., Hiltermann, T. J. N., Dijkman, J. H., & Verhoeven, A. J. (1994) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.11.1.8018341 · Cited by 650 · see citing works
Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B
van Montfort, R. L. M., Congreve, M., Tisi, D., Carr, R. A. E., & Jhoti, H. (2003) · Nature · doi:10.1038/nature01681 · Cited by 642 · see citing works
Kwon, J., Lee, S.-R., Yang, K.-S., Ahn, Y., Kim, Y. J., Stadtman, E. R., & Rhee, S. G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407396101 · Cited by 631 · see citing works
Kuhlencordt, P. J., Gyurko, R., Han, F., Scherrer‐Crosbie, M., Aretz, T. H., Hajjar, R. J., Picard, M. H., & Huang, P. L. (2001) · Circulation · doi:10.1161/hc2901.091399 · Cited by 631 · see citing works
Kissner, R., Nauser, T., Bugnon, P., Lye, P. G., & Koppenol, W. H. (1997) · Chemical Research in Toxicology · doi:10.1021/tx970160x · Cited by 629 · see citing works
NOX4 activity is determined by mRNA levels and reveals a unique pattern of ROS generation
Serrander, L., Cartier, L., Bedard, K., Banfi, B., Lardy, B., Plastre, O., Sienkiewicz, A., Fórró, L., Schlegel, W., & Krause, K.-H. (2007) · Biochemical Journal · doi:10.1042/bj20061903 · Cited by 627 · see citing works
Crystal Structure of Constitutive Endothelial Nitric Oxide Synthase
Raman, C. S., Li, H., Pavel Martasek, E., Král, V., Masters, B. S. S., & Poulos, T. L. (1998) · Cell · doi:10.1016/s0092-8674(00)81718-3 · Cited by 621 · see citing works
Yamagishi, S., Edelstein, D., Du, X.-L., Kaneda, Y., Guzmán, M., & Brownlee, M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007383200 · Cited by 620 · see citing works
Heparan Sulfate Proteoglycan Is a Mechanosensor on Endothelial Cells
Florian, J. A., Kosky, J. R., Ainslie, K. M., Pang, Z., Dull, R. O., & Tarbell, J. M. (2003) · Circulation Research · doi:10.1161/01.res.0000101744.47866.d5 · Cited by 619 · see citing works
Reciprocal Regulation of Endothelial Nitric-oxide Synthase by Ca2+-Calmodulin and Caveolin
Michel, J. B., Féron, O., Sacks, D. B., & Michel, T. M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.25.15583 · Cited by 613 · see citing works
HMG-CoA reductase inhibitor mobilizes bone marrow–derived endothelial progenitor cells
Llevadot, J., Murasawa, S., Kureishi, Y., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci200113131 · Cited by 611 · see citing works
Distinct Roles of Thioredoxin in the Cytoplasm and in the Nucleus
Hirota, K., Murata, M., Sachi, Y., Nakamura, H., Takeuchi, J. S., Mori, K., & Yodoi, J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.39.27891 · Cited by 610 · see citing works
HDL induces NO-dependent vasorelaxation via the lysophospholipid receptor S1P3
Nofer, J., van der Giet, M., Tölle, M., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200418004 · Cited by 607 · see citing works
Zou, M., Shi, C., & Cohen, R. A. (2002) · Journal of Clinical Investigation · doi:10.1172/jci14442 · Cited by 603 · see citing works
Görlach, A., Brandes, R. P., Nguyen, K., Amidi, M., Dehghani, F., & Busse, R. (2000) · Circulation Research · doi:10.1161/01.res.87.1.26 · Cited by 598 · cited 1× · see citing works
“Hence, as reliable antibodies became available, protein expression of p22phox and Nox2 in endothelial cells, both in culture and in situ, was confirmed by numerous investigators (40, 41, 185, 311).”
Goossens, V., Grooten, J., Vos, K. J. D., & Fiers, W. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.18.8115 · Cited by 595 · see citing works
Presence of hypochlorite-modified proteins in human atherosclerotic lesions.
Hazell, L. J., Arnold, L., Flowers, D., Waeg, G., Malle, E., & Stocker, R. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118576 · Cited by 592 · see citing works
Cellular Antioxidant Effects of Atorvastatin In Vitro and In Vivo
Waßmann, S., Laufs, U., Müller, K., Konkol, C., Ahlbory, K., Bäumer, A. T., Linz, W., Böhm, M., & Nickenig, G. (2002) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/hq0202.104081 · Cited by 591 · see citing works
Tetrahydrobiopterin restores endothelial function in hypercholesterolemia.
Stroes, E. S. G., Kastelein, J. J. P., Cosentino, F., Erkelens, W. D., Wever, R. M. F., Koomans, H. A., Lüscher, T. F., & Rabelink, T. J. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119131 · Cited by 588 · see citing works
Ascorbic Acid Reverses Endothelial Vasomotor Dysfunction in Patients With Coronary Artery Disease
Levine, G. N., Frei, B., Koulouris, S. N., Gerhard, M. D., Keaney, J. F., & Vita, J. A. (1996) · Circulation · doi:10.1161/01.cir.93.6.1107 · Cited by 582 · see citing works
Dicer Is Required for Embryonic Angiogenesis during Mouse Development*
Yang, W., Yang, D. D., Na, S., Sandusky, G., Zhang, Q., & Zhao, G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413394200 · Cited by 582 · see citing works
Casella, G., Carr, E., Davies, J. I., Belch, J. J. F., & Struthers, A. D. (2006) · Circulation · doi:10.1161/circulationaha.106.651117 · Cited by 574 · see citing works
Role of p47 phox in Vascular Oxidative Stress and Hypertension Caused by Angiotensin II
Landmesser, U., Cai, H. “., Dikalov, S., McCann, L. A., Hwang, J., Jo, H., Holland, S. M., & Harrison, D. G. (2002) · Hypertension · doi:10.1161/01.hyp.0000032100.23772.98 · Cited by 572 · see citing works
Nitric oxide activates TRP channels by cysteine S-nitrosylation
Yoshida, T., Inoue, R., Morii, T., Takahashi, N., Yamamoto, S., Hara, Y., Tominaga, M., Shimizu, S., Sato, Y., & Mori, Y. (2006) · Nature Chemical Biology · doi:10.1038/nchembio821 · Cited by 566 · see citing works
Reversing the Inactivation of Peroxiredoxins Caused by Cysteine Sulfinic Acid Formation
Woo, H. A., Chae, H. Z., Hwang, S. C., Yang, K., Kang, S. W., Kim, K., & Rhee, S. G. (2003) · Science · doi:10.1126/science.1080273 · Cited by 558 · see citing works
Direct Evidence of Endothelial Oxidative Stress With Aging in Humans
Donato, A. J., Eskurza, I., Silver, A., Levy, A., Pierce, G. L., Gates, P. E., & Seals, D. R. (2007) · Circulation Research · doi:10.1161/01.res.0000269183.13937.e8 · Cited by 558 · see citing works
Antioxidant Vitamin C Improves Endothelial Dysfunction in Chronic Smokers
Heitzer, T., Just, H., & Mu¨nzel, T. (1996) · Circulation · doi:10.1161/01.cir.94.1.6 · Cited by 554 · see citing works
Duffy, S. J., Keaney, J. F., HOLBROOK, M. M., Gokce, N., Swerdloff, P. L., Frei, B. B., & Vita, J. A. (2001) · Circulation · doi:10.1161/01.cir.104.2.151 · Cited by 552 · see citing works
Essential Roles of S-Nitrosothiols in Vascular Homeostasis and Endotoxic Shock
Liu, L., Yan, Y., Zeng, M., Zhang, J., Hanes, M. A., Ahearn, G. S., McMahon, T., Dickfeld, T. L., Marshall, H. E., Que, L. G., et al. (2004) · Cell · doi:10.1016/s0092-8674(04)00131-x · Cited by 546 · see citing works
Oxidized Low-density Lipoprotein Decreases the Expression of Endothelial Nitric Oxide Synthase
Liao, J. K., Shin, W. S., Lee, W. Y., & Clark, S. L. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.1.319 · Cited by 541 · see citing works
Endothelium‐dependent inhibition of platelet aggregation
Azuma, H., Ishikawa, M., & Sekizaki, S. (1986) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.1986.tb10218.x · Cited by 532 · 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
Diet-induced atherosclerosis increases the release of nitrogen oxides from rabbit aorta.
Minor, R. L., Myers, P. R., Guerra, R., Bates, J. N., & Harrison, D. G. (1990) · Journal of Clinical Investigation · doi:10.1172/jci114949 · Cited by 517 · see citing works
Wagner, A. H., Köhler, T. C., Rueckschloss, U., Just, I., & Hecker, M. (2000) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.20.1.61 · Cited by 517 · see citing works
Pueyo, M. E., Gonzalez, W., Nicoletti, A., Savoie, F., Arnal, J., & Michel, J. (2000) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.20.3.645 · Cited by 516 · see citing works
Regulation of Nox and Duox enzymatic activity and expression.
Lambeth, J., Kawahara, T., & Diebold, B. (2007) · Free Radical Biology & Medicine · doi:10.1016/j.freeradbiomed.2007.03.028 · Cited by 509 · see citing works
Allopurinol Improves Endothelial Dysfunction in Chronic Heart Failure
Farquharson, C. A. J., Butler, R., Hill, A., Belch, J. J. F., & Struthers, A. D. (2002) · Circulation · doi:10.1161/01.cir.0000022140.61460.1d · Cited by 504 · see citing works
Regulation of endothelial and myocardial NO synthesis by multi-site eNOS phosphorylation
Mount, P. F., Kemp, B. E., & Power, D. A. (2007) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2006.05.023 · Cited by 498 · see citing works
The role of heparan sulphate in inflammation
Parish, C. R. (2006) · Nature reviews. Immunology · doi:10.1038/nri1918 · Cited by 498 · see citing works
Nox4 as the Major Catalytic Component of an Endothelial NAD(P)H Oxidase
Ago, T., Kitazono, T., Ooboshi, H., Iyama, T., Han, Y. H., Takada, J., Wakisaka, M., Ibayashi, S., Utsumi, H., & Iida, M. (2004) · Circulation · doi:10.1161/01.cir.0000105680.92873.70 · Cited by 497 · see citing works
Polyphenols and cardiovascular disease: effects on endothelial and platelet function
Vita, J. A. (2005) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/81.1.292s · Cited by 495 · see citing works
Pinton, P., Rimessi, A., Marchi, S., Orsini, F., Migliaccio, E., Giorgio, M., Contursi, C., Minucci, S., Mantovani, F., Wieckowski, M., et al. (2007) · Science · doi:10.1126/science.1135380 · Cited by 494 · see citing works
Two Novel Proteins Activate Superoxide Generation by the NADPH Oxidase NOX1
Bánfi, B., Clark, R. A., Steger, K., & Krause, K.-H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200613200 · Cited by 491 · see citing works
p47phox is required for atherosclerotic lesion progression in ApoE–/– mice
Barry-Lane, P. A., Patterson, C., van der Merwe, M., Hu, Z., Holland, S. M., Yeh, E. T. H., & Runge, M. S. (2001) · Journal of Clinical Investigation · doi:10.1172/jci200111927 · Cited by 489 · 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
A Molecular Redox Switch on p21
Lander, H. M., Hajjar, D. P., Hempstead, B. L., Mirza, U. A., Chait, B. T., Campbell, S. L., & Quilliam, L. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.7.4323 · Cited by 488 · see citing works
Brennan, M.-L., Wu, W., Fu, X., Shen, Z., Song, W., Frost, H., Vadseth, C., Narine, L., Lenkiewicz, E., Borchers, M. T., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112400200 · Cited by 486 · see citing works
Wang, L., Fuster, M. M., Sriramarao, P., & Esko, J. D. (2005) · Nature Immunology · doi:10.1038/ni1233 · Cited by 479 · see citing works
Mitochondrial Integrity and Function in Atherogenesis
Ballinger, S. W., Patterson, C., Knight-Lozano, C. A., Burow, D. L., Conklin, C. A., Hu, Z., Reuf, J., Horaist, C., Lebovitz, R. M., Hunter, G. C., et al. (2002) · Circulation · doi:10.1161/01.cir.0000023921.93743.89 · Cited by 478 · 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
Dermal Wound Healing Is Subject to Redox Control
Roy, S., Khanna, S., Nallu, K., Hunt, T. K., & Sen, C. K. (2006) · Molecular Therapy · doi:10.1016/j.ymthe.2005.07.684 · Cited by 472 · see citing works
Pritchard, K. A., Groszek, L., Smalley, D. M., Sessa, W. C., Wu, M., Villalon, P., Wolin, M. S., & Stemerman, M. B. (1995) · Circulation Research · doi:10.1161/01.res.77.3.510 · Cited by 471 · see citing works
Nox1 Is Involved in Angiotensin II–Mediated Hypertension: A Study in Nox1-Deficient Mice
Matsuno, K., Yamada, H., Iwata, K., Jin, D., Katsuyama, M., Matsuki, M., Takai, S., Yamanishi, K., Miyazaki, M., Matsubara, H., et al. (2005) · Circulation · doi:10.1161/circulationaha.105.573709 · Cited by 470 · see citing works
Thiol redox control via thioredoxin and glutaredoxin systems
Holmgren, A., Johansson, C., Berndt, C., Lönn, M. E., Hudemann, C., & Lillig, C. H. (2005) · Biochemical Society Transactions · doi:10.1042/bst20051375 · Cited by 463 · see citing works
Allopurinol Normalizes Endothelial Dysfunction in Type 2 Diabetics With Mild Hypertension
Butler, R., Morris, A. D., Belch, J. J. F., Hill, A., & Struthers, A. D. (2000) · Hypertension · doi:10.1161/01.hyp.35.3.746 · Cited by 463 · see citing works
McNally, J. S., Davis, M. E., Giddens, D. P., Saha, A., Hwang, J., Dikalov, S., Jo, H., & Harrison, D. G. (2003) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00515.2003 · Cited by 461 · see citing works
Cysteine Redox Sensor in PKGIa Enables Oxidant-Induced Activation
Burgoyne, J. R., Madhani, M., Cuello, F., Charles, R. L., Brennan, J. P., Schröder, E., Browning, D. D., & Eaton, P. (2007) · Science · doi:10.1126/science.1144318 · Cited by 457 · see citing works
Stasch, J., Schmidt, P. M., Nedvetsky, P. I., Nedvetskaya, T. Y., Kumar, A. H. S., Meurer, S., Deile, M., Taye, A., Knorr, A., Lapp, H., et al. (2006) · Journal of Clinical Investigation · doi:10.1172/jci28371 · Cited by 456 · see citing works
Giannoni, E., Buricchi, F., Raugei, G., Ramponi, G., & Chiarugi, P. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.15.6391-6403.2005 · Cited by 455 · see citing works
Role for Hydrogen Peroxide in Flow-Induced Dilation of Human Coronary Arterioles
Miura, H., Bosnjak, J. J., Ning, G., Saito, T., Miura, M., & Gutterman, D. D. (2003) · Circulation Research · doi:10.1161/01.res.0000054200.44505.ab · Cited by 454 · see citing works
Tetrahydrobiopterin Improves Endothelium-Dependent Vasodilation in Chronic Smokers
Heitzer, T. A., Brockhoff, C. J., Mayer, B., Warnholtz, A., Mollnau, H., Henne, S., Meinertz, T., & Münzel, T. F. (2000) · Circulation Research · doi:10.1161/01.res.86.2.e36 · Cited by 449 · see citing works
Ballinger, S. W., Patterson, C., Yan, C.-N., Doan, R., Burow, D. L., Young, C. G., Yakes, F. M., Houten, B. V., Ballinger, C. A., Freeman, B. Α., et al. (2000) · Circulation Research · doi:10.1161/01.res.86.9.960 · Cited by 442 · see citing works
Reynaert, N. L., van der Vliet, A., Guala, A. S., McGovern, T., Hristova, M., Pantano, C., Heintz, N. H., Heim, J., Ho, Y.-S., Matthews, D. E., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603290103 · Cited by 442 · see citing works
Dikalova, A., Clempus, R., Lassègue, B., Cheng, G., McCoy, J., Dikalov, S., Martin, A. S., Lyle, A., Weber, D. S., Weiss, D., et al. (2005) · Circulation · doi:10.1161/circulationaha.105.538934 · Cited by 438 · 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
Zhang, R., Brennan, M.-L., Shen, Z., MacPherson, J. C., Schmitt, D., Molenda, C. E., & Hazen, S. L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m209124200 · Cited by 432 · see citing works
Myeloperoxidase mediates neutrophil activation by association with CD11b/CD18 integrins
Lau, D., Mollnau, H., Eiserich, J. P., Freeman, B. Α., Daiber, A., Gehling, U. M., Brümmer, J., Rudolph, V., Münzel, T. F., Heitzer, T. A., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405193102 · Cited by 431 · see citing works
Drummond, G. R., Cai, H., Davis, M. E., Ramasamy, S., & Harrison, D. G. (2000) · Circulation Research · doi:10.1161/01.res.86.3.347 · Cited by 430 · see citing works
Self-citationMitochondrial nitric oxide synthase
Ghafourifar, P., & Cadenas, E. (2005) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2005.02.005 · Cited by 429 · see citing works
Nitrolinoleic acid. An endogenous peroxisome proliferator-activated receptor γ ligand
Schopfer, F. J., Lin, Y., Baker, P. R. S., Cui, T., Garcia-Barrio, M., Zhang, J., Chen, K., Chen, Y. E., & Freeman, B. A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408384102 · Cited by 428 · see citing works
Redox-Dependent Transcriptional Regulation
Liu, H., Colavitti, R., Rovira, I. I., & Finkel, T. (2005) · Circulation Research · doi:10.1161/01.res.0000188210.72062.10 · Cited by 427 · see citing works
Heitzer, T., Krohn, K., Albers, S., & Meinertz, T. (2000) · Diabetologia · doi:10.1007/s001250051551 · Cited by 427 · see citing works
Landmesser, U., Bahlmann, F. H., Mueller, M. F., Spiekermann, S., Kirchhoff, N., Schulz, S., Manes, C., Fischer, D., de Groot, K., Fliser, D., et al. (2005) · Circulation · doi:10.1161/01.cir.0000164260.82417.3f · Cited by 425 · see citing works
THE REGULATION AND PHARMACOLOGY OF ENDOTHELIAL NITRIC OXIDE SYNTHASE
Dudzinski, D. M., Igarashi, J., Greif, D. M., & Michel, T. M. (2005) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.44.101802.121844 · Cited by 425 · see citing works
Leikert, J. F., Räthel, T. R., Wohlfart, P., Cheynier, V., Vollmar, A. M., & Dirsch, V. M. (2002) · Circulation · doi:10.1161/01.cir.0000034445.31543.43 · Cited by 424 · see citing works
Landmesser, U., Engberding, N., Bahlmann, F. H., Schaefer, A., Wiencke, A., Heineke, A., Spiekermann, S., Hilfiker‐Kleiner, D., Templin, C., Kotlarz, D., et al. (2004) · Circulation · doi:10.1161/01.cir.0000143232.67642.7a · Cited by 423 · see citing works
Heller, R., Unbehaun, A., Schellenberg, B., Mayer, B., Werner‐Felmayer, G., & Werner, E. R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m004392200 · Cited by 421 · see citing works
Nitric Oxide and Cyclic GMP in Cell Signaling and Drug Development
Murad, F. (2006) · New England Journal of Medicine · doi:10.1056/nejmsa063904 · Cited by 420 · see citing works
Gardner, P. R., Nguyen, D., & White, C. W. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.25.12248 · Cited by 414 · see citing works
Féron, O., Dessy, C., Moniotte, S., Desager, J., & Balligand, J. (1999) · Journal of Clinical Investigation · doi:10.1172/jci4829 · Cited by 413 · see citing works
Thum, T., Fraccarollo, D., Schultheiß, M., Froese, S., Galuppo, P., Widder, J. D., Tsikas, D., Ertl, G., & Bauersachs, J. K. (2007) · Diabetes · doi:10.2337/db06-0699 · Cited by 411 · see citing works
Mitochondrial dysfunction in cardiovascular disease
Ballinger, S. W. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.02.014 · Cited by 405 · see citing works
Regulation of PDGF signalling and vascular remodelling by peroxiredoxin II
Choi, M. H., Lee, I. K., Kim, G. W., Kim, B. U., Han, Y.-H., Yu, D.-Y., Park, H. S., Kim, K. Y., Lee, J. S., Choi, C., et al. (2005) · Nature · doi:10.1038/nature03587 · Cited by 403 · see citing works
Regulatory functions of ubiquitination in the immune system
Ben‐Neriah, Y. (2002) · Nature Immunology · doi:10.1038/ni0102-20 · Cited by 403 · see citing works
Life history of eNOS: partners and pathways
DUDZINSKI, D., & MICHEL, T. (2007) · Cardiovascular Research · doi:10.1016/j.cardiores.2007.03.023 · Cited by 400 · see citing works
Jackson, T. S., Xu, A., Vita, J. A., & Keaney, J. F. (1998) · Circulation Research · doi:10.1161/01.res.83.9.916 · Cited by 400 · cited 2× · see citing works
“In support of this, ex vivo vessel studies determined that millimolar concentrations of ascorbate are required to prevent O2 -mediated impairment in EDNO bioactivity (245).”
Haendeler, J., Hoffmann, J., Tischler, V., Berk, B. C., Zeiher, A. M., & Dimmeler, S. (2002) · Nature Cell Biology · doi:10.1038/ncb851 · Cited by 399 · see citing works
Mügge, A., Elwell, J. H., Peterson, T. E., Hofmeyer, T. G., Heistad, D. D., & Harrison, D. G. (1991) · Circulation Research · doi:10.1161/01.res.69.5.1293 · Cited by 399 · see citing works
Nitric Oxide Is a Physiological Substrate for Mammalian Peroxidases
Abu‐Soud, H. M., & Hazen, S. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.48.37524 · Cited by 398 · see citing works
Li, J., & Shah, A. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110073200 · Cited by 395 · see citing works
Peskin, A. V., Low, F. M., Paton, L. N., Maghzal, G. J., Hampton, M. B., & Winterbourn, C. C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700339200 · Cited by 394 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Incalza, M. A., D’Oria, R., Natalicchio, A., Perrini, S., Laviola, L., & Giorgino, F. (2017) · Vascular Pharmacology · doi:10.1016/j.vph.2017.05.005 · Cited by 1,375 · see citing works
Coronary Microvascular Dysfunction
Crea, F., Lanza, G. A., & Camici, P. G. (2013) · Springer eBooks · doi:10.1007/978-88-470-5367-0 · Cited by 1,295 · see citing works
Mitochondrial and metabolic dysfunction in ageing and age-related diseases
Amorim, J. A., Coppotelli, G., Rolo, A. P., Palmeira, C. M., Ross, J. M., & Sinclair, D. A. (2022) · Nature Reviews Endocrinology · doi:10.1038/s41574-021-00626-7 · Cited by 990 · see citing works
Combating oxidative stress in vascular disease: NADPH oxidases as therapeutic targets
Drummond, G. R., Selemidis, S., Griendling, K. K., & Sobey, C. G. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3403 · Cited by 899 · see citing works
Self-citationReactive oxygen species, heat stress and oxidative-induced mitochondrial damage. A review
Slimen, I. B., Najar, T., Ghram, A., Debbabi, H., Mrad, M. B., & Abderrabba, M. (2014) · International Journal of Hyperthermia · doi:10.3109/02656736.2014.971446 · Cited by 880 · see citing works
Oxidant Mechanisms in Renal Injury and Disease
Ratliff, B. B., Abdulmahdi, W., Pawar, R. D., & Wolin, M. S. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6665 · Cited by 699 · see citing works
Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation
Tejero, J., Shiva, S., & Gladwin, M. T. (2019) · Physiological Reviews · doi:10.1152/physrev.00036.2017 · Cited by 541 · see citing works
Thioredoxins and Glutaredoxins: Unifying Elements in Redox Biology
Meyer, Y., Buchanan, B. B., Vignols, F., & Reichheld, J. (2009) · Annual Review of Genetics · doi:10.1146/annurev-genet-102108-134201 · Cited by 482 · see citing works
Tirichen, H., Yaigoub, H., Xu, W., Wu, C., Li, R., & Li, Y. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.627837 · Cited by 431 · see citing works
Oxidative Stress-Mediated Atherosclerosis: Mechanisms and Therapies
Yang, X., Li, Y., Li, Y., Ren, X., Zhang, X., Hu, D., Gao, Y., Xing, Y., & Shang, H. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.00600 · Cited by 410 · see citing works
Reactive oxygen species: Destroyers or messengers?
Bartosz, G. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2008.11.009 · Cited by 379 · see citing works
The Role of Oxidative Stress in Cardiac Disease: From Physiological Response to Injury Factor
D’Oria, R., Schipani, R., Leonardini, A., Natalicchio, A., Perrini, S., Cignarelli, A., Laviola, L., & Giorgino, F. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/5732956 · Cited by 387 · see citing works
Wang, Q., Zhang, M., Torres, G., Wu, S., Ouyang, C., Xie, Z., & Zou, M.-H. (2017) · Diabetes · doi:10.2337/db16-0915 · Cited by 370 · see citing works
Oxidative stress in early diabetic nephropathy: fueling the fire
Singh, D. K., Winocour, P. H., & Farrington, K. (2010) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2010.212 · Cited by 354 · see citing works
Daiber, A. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.01.032 · Cited by 347 · see citing works
Hsieh, H., Liu, C.-A., Huang, B., Tseng, A. H.-H., & Wang, D. L. (2014) · Journal of Biomedical Science · doi:10.1186/1423-0127-21-3 · Cited by 333 · see citing works
Vascular NAD(P)H oxidase activation in diabetes: a double-edged sword in redox signalling
Gao, L., & Mann, G. E. (2009) · Cardiovascular Research · doi:10.1093/cvr/cvp031 · Cited by 330 · see citing works
Endothelial NADPH oxidases: which NOX to target in vascular disease?
Drummond, G. R., & Sobey, C. G. (2014) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2014.06.012 · Cited by 315 · see citing works
Self-citationJudkins, C. P., Diep, H., Broughton, B. R. S., Mast, A. E., Hooker, E. U., Miller, A. A., Selemidis, S., Dusting, G. J., Sobey, C. G., & Drummond, G. R. (2010) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00799.2009 · Cited by 299 · see citing works
Self-citationMitochondria and Reactive Oxygen Species
Addabbo, F., Montagnani, M., & Goligorsky, M. S. (2009) · Hypertension · doi:10.1161/hypertensionaha.109.130054 · Cited by 294 · see citing works
Cellular signaling and NO production
Michel, T. M., & Vanhoutte, P. M. (2010) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-009-0765-9 · Cited by 287 · see citing works
Zinc and Regulation of Inflammatory Cytokines: Implications for Cardiometabolic Disease
Foster, M. J., & Samman, S. (2012) · Nutrients · doi:10.3390/nu4070676 · Cited by 281 · see citing works
Sadiq, I. Z. (2021) · Current Molecular Medicine · doi:10.2174/1566524022666211222161637 · Cited by 284 · see citing works
Role of indoleamine 2,3-dioxygenase in health and disease
Yeung, A. W. S., Terentis, A. C., King, N. J. C., & Thomas, S. R. (2015) · Clinical Science · doi:10.1042/cs20140392 · Cited by 235 · see citing works
Self-citationParhiz, H., Shuvaev, V. V., Pardi, N., Khoshnejad, M., Kiseleva, R. Y., Brenner, J. S., Uhler, T., Tuyishime, S., Mui, B. L., Tam, Y. K., et al. (2018) · Journal of Controlled Release · doi:10.1016/j.jconrel.2018.10.015 · Cited by 233 · see citing works
Redox signaling in cardiovascular health and disease
Madamanchi, N. R., & Runge, M. S. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.04.001 · Cited by 223 · see citing works
van Golen, R. F., van Gulik, T. M., & Heger, M. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.01.013 · Cited by 221 · see citing works
Regulation of the Cerebral Circulation by Arterial Carbon Dioxide
Hoiland, R. L., Fisher, J. A., & Ainslie, P. N. (2019) · Comprehensive physiology · doi:10.1002/cphy.c180021 · Cited by 260 · see citing works
Hydrogen peroxide signaling in vascular endothelial cells
Bretón-Romero, R., & Lamas, S. (2014) · Redox Biology · doi:10.1016/j.redox.2014.02.005 · Cited by 209 · see citing works
Regulation of Endothelial Function by Mitochondrial Reactive Oxygen Species
Widlansky, M. E., & Gutterman, D. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3642 · Cited by 211 · see citing works
Oxidative stress and endothelial dysfunction in cerebrovascular disease
Chrissobolis, S. (2010) · Frontiers in bioscience · doi:10.2741/3816 · Cited by 203 · see citing works
Regulation of VEGF-induced endothelial cell migration by mitochondrial reactive oxygen species
Wang, Y., Zang, Q. S., Liu, Z., Wu, Q., Maass, D. L., Dulan, G., Shaul, P. W., Melito, L. M., Frantz, D. E., Kilgore, J. A., et al. (2011) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00322.2010 · Cited by 199 · see citing works
Vascular Targeting of Nanocarriers: Perplexing Aspects of the Seemingly Straightforward Paradigm
Howard, M. D., Zern, B. J., Anselmo, A. C., Shuvaev, V. V., Mitragotri, S., & Muzykantov, V. R. (2014) · ACS Nano · doi:10.1021/nn500136z · Cited by 197 · see citing works
Role of Forkhead Transcription Factors in Diabetes-Induced Oxidative Stress
Ponugoti, B., Dong, G., & Graves, D. T. (2012) · Experimental Diabetes Research · doi:10.1155/2012/939751 · Cited by 193 · see citing works
Thioredoxin Interacting Protein: Redox Dependent and Independent Regulatory Mechanisms
Spindel, O. N., WORLD, C., & Berk, B. C. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4137 · Cited by 193 · see citing works
Oxidative Stress in Hypertension: Role of the Kidney
Araújo, M., & Wilcox, C. S. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5259 · Cited by 187 · see citing works
Cheng, X., Siow, R. C. M., & Mann, G. E. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3283 · Cited by 181 · see citing works
Oxidative Stress as Pathogenesis of Cardiovascular Risk Associated with Metabolic Syndrome
Otani, H. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3739 · Cited by 181 · see citing works
Mechanisms of Acupuncture in the Regulation of Oxidative Stress in Treating Ischemic Stroke
Su, X.-T., Wang, L., Ma, S., Cao, Y., Yang, N., Lin, L., Fisher, M., Yang, J., & Liu, C. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/7875396 · Cited by 174 · see citing works
Ultrasound and Microbubble-Induced Intra- and Intercellular Bioeffects in Primary Endothelial Cells
Juffermans, L. J. M., Dijk, A. V., Jongenelen, C. A. M., Drukarch, B., Reijerkerk, A., de Vries, H. E., Otto Kamp, B., & Musters, R. J. P. (2009) · Ultrasound in Medicine & Biology · doi:10.1016/j.ultrasmedbio.2009.06.1091 · Cited by 171 · see citing works
Modulation of endothelial nitric oxide by plant-derived products
Schmitt, C. A., & Dirsch, V. M. (2009) · Nitric Oxide · doi:10.1016/j.niox.2009.05.006 · Cited by 169 · 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
Update on Inflammatory Biomarkers and Treatments in Ischemic Stroke
Bonaventura, A., Liberale, L., Vecchié, A., Casula, M., Carbone, F., Dallegri, F., & Montecucco, F. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17121967 · Cited by 166 · see citing works
Endothelial Dysfunction and Its Clinical Implications
Poredoš, P., Visnovič-Poredoš, A., & Gregorič, I. D. (2021) · Angiology · doi:10.1177/0003319720987752 · Cited by 161 · see citing works
Zinc and Redox Signaling: Perturbations Associated with Cardiovascular Disease and Diabetes Mellitus
Foster, M. J., & Samman, S. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3111 · Cited by 149 · see citing works
Impacts of exercise interventions on different diseases and organ functions in mice
Guo, S., Huang, Y., Yan, Z., Huang, H., Hong, S., & Liu, T. (2019) · Journal of sport and health science/Journal of Sport and Health Science · doi:10.1016/j.jshs.2019.07.004 · Cited by 150 · see citing works
Yang, Z., von Ballmoos, M. C. W., Faessler, D., Völzmann, J., Ortmann, J., Diehm, N., Kalka-Moll, W. M., Baumgärtner, I., Santo, S. D., & Kalka, C. (2010) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2010.02.022 · Cited by 148 · see citing works
Loot, A. E., Schreiber, J. G., Fißlthaler, B., & Fleming, I. (2009) · The Journal of Experimental Medicine · doi:10.1084/jem.20090449 · Cited by 144 · see citing works
Ventilation, Oxidative Stress, and Nitric Oxide in Hypobaric versus Normobaric Hypoxia
Faiss, R., Pialoux, V., Sartori, C. S., Faës, C., Dériaz, O., & Millet, G. P. (2013) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e31826d5aa2 · Cited by 139 · see citing works
Renal Endothelial Dysfunction in Diabetic Nephropathy
Cheng, H., & Harris, R. C. (2014) · Cardiovascular & Haematological Disorders - Drug Targets · doi:10.2174/1871529x14666140401110841 · Cited by 138 · see citing works
Wang, J., Alexanian, A., Ying, R., Kizhakekuttu, T. J., Dharmashankar, K., Vasquez-Vivar, J., Gutterman, D. D., & Widlansky, M. E. (2011) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.111.227389 · Cited by 134 · see citing works
Endothelial Dysfunction: The Common Consequence in Diabetes and Hypertension
Wong, W. T., Wong, S. L., Tian, X. Y., & Huang, Y. (2010) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0b013e3181d7671c · Cited by 135 · see citing works
Oxidative stress is associated with impaired arterial elasticity
Patel, R. S., Mheid, I. A., Morris, A. A., Ahmed, Y. A., Kavtaradze, N., Ali, S., Dabhadkar, K. C., Brigham, K. L., Hooper, W. C., Alexander, R. W., et al. (2011) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2011.04.033 · Cited by 135 · see citing works
Li, S., Nagothu, K. K., Desai, V. G., Lee, T., Branham, W. S., Moland, C. L., Megyesi, J. K., Crew, M. D., & Portilla, D. (2009) · Kidney International · doi:10.1038/ki.2009.330 · Cited by 134 · see citing works
Traumatic Brain Injury and NADPH Oxidase: A Deep Relationship
Angeloni, C., Prata, C., Sega, F. V. D., Piperno, R., & Hrelia, S. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/370312 · Cited by 133 · see citing works
Zhou, H., & Toan, S. (2020) · Biomolecules · doi:10.3390/biom10010085 · Cited by 133 · see citing works
Epigenetic Regulation of Oxidative Stress in Ischemic Stroke
Zhao, H., Han, Z., Ji, X., & Luo, Y. (2016) · Aging and Disease · doi:10.14336/ad.2015.1009 · Cited by 131 · see citing works
Use of Dimedone-Based Chemical Probes for Sulfenic Acid Detection
Klomsiri, C., Nelson, K. J., Bechtold, E., Soito, L., Johnson, L. C., Lowther, W. T., Ryu, S. E., King, S. B., Furdui, C. M., & Poole, L. B. (2010) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(10)73003-2 · Cited by 131 · see citing works
Oxidative Stress in Cell Death and Cardiovascular Diseases
Xu, T., Ding, W., Ji, X., Ao, X., Liu, Y., Yu, W., & Wang, J. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/9030563 · Cited by 131 · see citing works
Cross-talk Between Nitrate-Nitrite-NO and NO Synthase Pathways in Control of Vascular NO Homeostasis
Carlström, M., Liu, M., Yang, T., Zollbrecht, C., Huang, L., Peleli, M., Borniquel, S., Kishikawa, H., Hezel, M., Persson, A. E. G., et al. (2015) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5481 · Cited by 130 · see citing works
Wu, B. J., Yan, L., Charlton, F., Witting, P. K., Barter, P. J., & Rye, K. (2010) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.109.201129 · Cited by 129 · see citing works
Self-citationUse of Dimedone-Based Chemical Probes for Sulfenic Acid Detection
Nelson, K. J., Klomsiri, C., Codreanu, S. G., Soito, L., Liebler, D. C., Rogers, L. C., Daniel, L. W., & Poole, L. B. (2010) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(10)73004-4 · Cited by 126 · see citing works
Lee, D.-Y., Wauquier, F., Eid, A. A., Roman, L. J., Ghosh-Choudhury, G., Khazim, K., Block, K. L., & Gorin, Y. C. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.470971 · Cited by 125 · see citing works
Tumor mechanics and metabolic dysfunction
Tung, J. C., Barnes, J. M., Desai, S. R., Sistrunk, C., Conklin, M. W., Schedin, P. S., Eliceiri, K. W., Keely, P. J., Seewaldt, V. L., & Weaver, V. M. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.11.020 · Cited by 124 · see citing works
Dietary flavonoid quercetin stimulates vasorelaxation in aortic vessels
Khoo, N. K. H., White, C. R., Pozzo‐Miller, L. D., Zhou, F., Constance, C., Inoue, T., Patel, R. P., & Parks, D. A. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.04.022 · Cited by 123 · see citing works
Shen, Y., Croft, K. D., Hodgson, J. M., Kyle, R. A., Lee, I.-L. E., Wang, Y., Stocker, R., & Ward, N. C. (2012) · Biochemical Pharmacology · doi:10.1016/j.bcp.2012.07.016 · Cited by 117 · see citing works
Endothelial Targeting of Antibody-Decorated Polymeric Filomicelles
Shuvaev, V. V., Ilies, M. A., Simone, E. A., Zaitsev, S. V., Kim, Y., Cai, S., Mahmud, A., Dziubla, T. D., Muro, S., Discher, D. E., et al. (2011) · ACS Nano · doi:10.1021/nn2015453 · Cited by 116 · see citing works
Protective Effects of Short-Chain Fatty Acids on Endothelial Dysfunction Induced by Angiotensin II
Robles‐Vera, I., Toral, M., de la Visitación, N., Aguilera-Sánchez, N., Redondo, J. M., & Duarte, J. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00277 · Cited by 118 · see citing works
Thomas, K., Zondler, L., Ludwig, N., Kardell, M., Lüneburg, C., Henke, K., Mersmann, S., Margraf, A., Spieker, T., Tekath, T., et al. (2022) · JCI Insight · doi:10.1172/jci.insight.163161 · Cited by 103 · see citing works
Delayed Graft Function in Kidney Transplant: Risk Factors, Consequences and Prevention Strategies
Ponticelli, C., Reggiani, F., & Moroni, G. L. (2022) · Journal of Personalized Medicine · doi:10.3390/jpm12101557 · Cited by 116 · see citing works
Nox isoforms in vascular pathophysiology: insights from transgenic and knockout mouse models
Rivera, J., Sobey, C. G., Walduck, A. K., & Drummond, G. R. (2010) · Redox Report · doi:10.1179/174329210x12650506623401 · Cited by 105 · see citing works
Self-citationJarajapu, Y. P. R., Bhatwadekar, A. D., Caballero, S., Hazra, S., Shenoy, V., Medina, R. J., Kent, D., Stitt, A. W., Thut, C. J., Finney, E. M., et al. (2012) · Diabetes · doi:10.2337/db12-0808 · Cited by 104 · see citing works
Palozza, P., Parrone, N., Simone, R. E., & Catalano, A. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.06.031 · Cited by 103 · see citing works
Howard, M. D., Greineder, C. F., Hood, E. D., & Muzykantov, V. R. (2014) · Journal of Controlled Release · doi:10.1016/j.jconrel.2013.12.035 · Cited by 100 · see citing works
The opposing roles of NO and oxidative stress in cardiovascular disease
Ritchie, R. H., Drummond, G. R., Sobey, C. G., Silva, T. M. D., & Kemp‐Harper, B. K. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.12.017 · Cited by 98 · see citing works
Self-citationThe Future Challenge of Reactive Oxygen Species (ROS) in Hypertension: From Bench to Bed Side
Togliatto, G., Lombardo, G., & Brizzi, M. F. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18091988 · Cited by 98 · see citing works
Oxidative Stress and Erectile Dysfunction: Pathophysiology, Impacts, and Potential Treatments
Kaltsas, A., Zikopoulos, A., Dimitriadis, F., Sheshi, D., Politis, M., Moustakli, E., Symeonidis, E. N., Chrisofos, M., Sofikitis, N., & Zachariou, A. (2024) · Current Issues in Molecular Biology · doi:10.3390/cimb46080521 · Cited by 95 · see citing works
Redox signaling, Nox5 and vascular remodeling in hypertension
Montezano, A. C., Tsiropoulou, S., Dulak-Lis, M., Harvey, A., Camargo, L. D. L., & Touyz, R. M. (2015) · Current Opinion in Nephrology and Hypertension · doi:10.1097/mnh.0000000000000153 · Cited by 93 · see citing works
Macrophages Offer A Paradigm Switch for CNS Delivery of Therapeutic Proteins
Klyachko, N. L., Haney, M. J., Zhao, Y., Manickam, D. S., Mahajan, V., Suresh, P., Hingtgen, S. D., Mosley, R. L., Gendelman, H. E., Kabanov, A. V., et al. (2014) · Nanomedicine · doi:10.2217/nnm.13.115 · Cited by 92 · see citing works
PECAM‐targeted delivery of SOD inhibits endothelial inflammatory response
Shuvaev, V. V., Han, J., Yu, K. R. T., Huang, S., Hawkins, B. J., Madesh, M., Nakada, M. T., & Muzykantov, V. R. (2010) · The FASEB Journal · doi:10.1096/fj.10-169789 · Cited by 90 · see citing works
Pialoux, V., Brown, A. D., Leigh, R., Friedenreich, C. M., & Poulin, M. J. (2009) · Hypertension · doi:10.1161/hypertensionaha.109.138917 · Cited by 90 · see citing works
Thiol Redox Transitions in Cell Signaling: a Lesson from N-Acetylcysteine
Parasassi, T., Brunelli, R., Costa, G., Spirito, M. D., Krasnowska, E. K., Lundeberg, T., Pittaluga, E., & Ursini, F. (2010) · The Scientific World JOURNAL · doi:10.1100/tsw.2010.104 · Cited by 90 · see citing works
Biological chemistry of superoxide radicals
Winterbourn, C. C. (2020) · ChemTexts · doi:10.1007/s40828-019-0101-8 · Cited by 89 · see citing works
Impacts of Heat Stress-Induced Oxidative Stress on the Milk Protein Biosynthesis of Dairy Cows
Guo, Z., Gao, S., Ouyang, J., Ma, L., & Bu, D. (2021) · Animals · doi:10.3390/ani11030726 · Cited by 89 · see citing works
Tian, X. Y., Wong, W. T., Leung, F. P., Zhang, Y., Wáng, Y. X. J., Lee, H. K., Ng, C., Chen, Z., Yao, X., Au, C. L., et al. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3874 · Cited by 86 · see citing works
Shear flow increases S-nitrosylation of proteins in endothelial cells
Huang, B., Chen, S. C., & Wang, D. L. (2009) · Cardiovascular Research · doi:10.1093/cvr/cvp154 · Cited by 85 · see citing works
The Mechanisms of Restenosis and Relevance to Next Generation Stent Design
Clare, J., Ganly, J., Bursill, C. A., Sümer, H., Kingshott, P., & de Haan, J. B. (2022) · Biomolecules · doi:10.3390/biom12030430 · Cited by 82 · see citing works
Hua, S., Song, C., Geczy, C. L., Freedman, B., & Witting, P. K. (2009) · Redox Report · doi:10.1179/135100009x12525712409490 · Cited by 82 · see citing works
Self-citationRowlands, D. J., Chapple, S. J., Siow, R. C. M., & Mann, G. E. (2011) · Hypertension · doi:10.1161/hypertensionaha.110.162198 · Cited by 82 · see citing works
Reactive Oxygen Species and Oxidative Stress in Vascular‐Related Diseases
Cheng, X., Hu, Y., Yang, T., Wu, N., & Wang, X.-N. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/7906091 · Cited by 81 · see citing works
Cellular bioenergetics is regulated by PARP1 under resting conditions and during oxidative stress
Módis, K., Gerő, D., Erdélyi, K., Szoleczky, P., DeWitt, D. S., & Szabó, C. (2011) · Biochemical Pharmacology · doi:10.1016/j.bcp.2011.12.014 · Cited by 81 · see citing works
Roy, B. (2025) · Medical Sciences · doi:10.3390/medsci13030087 · Cited by 89 · see citing works
Tang, Y., Jacobi, A., Vater, C., Zou, X., & Stiehler, M. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.04.008 · Cited by 80 · see citing works
Khoo, N. K. H., Rudolph, V., Cole, M. P., Golin-Bisello, F., Schopfer, F. J., Woodcock, S. R., Batthyany, C., & Freeman, B. A. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.10.046 · Cited by 79 · see citing works
Regulation of thrombosis and vascular function by protein methionine oxidation
Gu, S. X., Stevens, J. W., & Lentz, S. R. (2015) · Blood · doi:10.1182/blood-2015-01-544676 · Cited by 79 · see citing works
A Novel Strategy for Global Analysis of the Dynamic Thiol Redox Proteome
Martínez-Acedo, P., Núñez, E., Sánchez-Gómez, F. J., Moreno, M., Ramos, E. M., Izquierdo-Álvarez, A., Miró‐Casas, E., Mesa, R., Rodríguez, P., Martı́nez-Ruiz, A., et al. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.016469 · Cited by 77 · see citing works
Maiocchi, S. L., Ku, J., Thai, T., Chan, E., Rees, M. D., & Thomas, S. R. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107711 · Cited by 75 · see citing works
Self-citationHood, E. D., Greineder, C. F., Dodia, C., Han, J., Mesaros, C., Shuvaev, V. V., Blair, I. A., Fisher, A. B., & Muzykantov, V. R. (2012) · Journal of Controlled Release · doi:10.1016/j.jconrel.2012.08.031 · Cited by 76 · see citing works
Hemoglobin disorders and endothelial cell interactions
Conran, N., & Costa, F. F. (2009) · Clinical Biochemistry · doi:10.1016/j.clinbiochem.2009.06.024 · Cited by 75 · see citing works
Faria, A. M., Papadimitriou, A., Silva, K. C., de Faria, J. M. L., & de Faria, J. B. L. (2012) · Diabetes · doi:10.2337/db11-1241 · Cited by 76 · see citing works
- Authors
- Thomas, S. R., Witting, P. K., & Drummond, G. R.
- Affiliations
- UNSW Sydney (AU)
- Concord Repatriation General Hospital (AU)
- Monash University (AU)
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2008-10
- Volume
- 10
- Issue
- 10
- Pages
- 1713-1766
- ISSN
- 1523-0864 (ISSN-L)
- 1557-7716
- OpenAlex
- W2014374142
- Cited by
- 383
- References
- 577
- Citations by year
- 2026: 7 · 2025: 7 · 2024: 9 · 2023: 7 · 2022: 18 · 2021: 12 · 2020: 20 · 2019: 13 · 2018: 13 · 2017: 24 · 2016: 23 · 2015: 17 · 2014: 38 · 2013: 22 · 2012: 42
- FWCI
- 4.00
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Antioxidants and Redox Signaling (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiovascular Health and Disease Prevention
- Keywords
- endothelial dysfunction, endothelial function, reactive oxygen species, nitric oxide, endothelial nitric oxide synthase, redox signaling, vascular homeostasis, hypertension, diabetes mellitus, atherosclerosis, cardiovascular disease, antioxidant therapy
- MeSH terms
- Angiotensin-Converting Enzyme Inhibitors, Animals, Antioxidants, Endothelium, Vascular, Humans, Hydrogen Peroxide, Mitochondria, Nitric Oxide, Oxidation-Reduction, Oxidoreductases, Phosphoric Monoester Hydrolases, Protein Kinases, Superoxides, Thioredoxins, Transcription Factors, Vascular Diseases, Lipid Peroxidation, Oxidative Stress, Hydroxymethylglutaryl-CoA Reductase Inhibitors, Endothelial Cells, Nitric Oxide Synthase Type III
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