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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.
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“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]
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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 466
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
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 146
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
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
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
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
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
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
Role of Oxidative Modifications in Atherosclerosis
Stocker, R., & Keaney, J. F. (2004) · Physiological Reviews · doi:10.1152/physrev.00047.2003 · Cited by 2,651
Schächinger, V., Britten, M. B., & Zeiher, A. M. (2000) · Circulation · doi:10.1161/01.cir.101.16.1899 · Cited by 2,589
Requirement for Generation of H 2 O 2 for Platelet-Derived Growth Factor Signal Transduction
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
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
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×
“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 2,400
Urbich, C., & Dimmeler, S. (2004) · Circulation Research · doi:10.1161/01.res.0000137877.89448.78 · Cited by 2,388
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
Garg, U. C., & Hassid, A. (1989) · Journal of Clinical Investigation · doi:10.1172/jci114081 · Cited by 2,154
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
Book ReviewAmbulatory Pediatric Care
Steinberg, J. B. (1989) · New England Journal of Medicine · doi:10.1056/nejm198901053200122 · Cited by 2,105
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
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
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
Heitzer, T., Schlinzig, T., Krohn, K., Meinertz, T., & Münzel, T. (2001) · Circulation · doi:10.1161/hc4601.099485 · Cited by 1,961
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
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
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
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
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
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
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
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
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
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
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
Zhang, D. D., & Hannink, M. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.22.8137-8151.2003 · Cited by 1,480
Kureishi, Y., Luo, Z., Shiojima, I., Bialik, A., Fulton, D. J., Lefer, D. J., Sessa, W. C., & Walsh, K. X. (2000) · Nature Medicine · doi:10.1038/79510 · Cited by 1,438
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
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
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 1,311
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
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 1,274
Daugherty, A., Dunn, J. L., Rateri, D. L., & Heinecke, J. W. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117342 · Cited by 1,269
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
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 1,191
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
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
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
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
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
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 1,137
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 · cited 1×
“For example, eNOS-derived NO signals for mitochondrial biogenesis in response to calorie restriction, which may be important for extension of the mammalian life span (373, 374).”
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
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
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
&NA; (1996) · Journal of Occupational and Environmental Medicine · doi:10.1097/00043764-199605000-00005 · Cited by 1,071
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
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 1,036
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
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 1,010
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
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
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
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
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
Denu, J. M., & Tanner, K. G. (1998) · Biochemistry · doi:10.1021/bi973035t · Cited by 945
Association Between Myeloperoxidase Levels and Risk of Coronary Artery Disease
Zhang, R. (2001) · JAMA · doi:10.1001/jama.286.17.2136 · Cited by 919
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 912
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
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
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
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
Kugiyama, K., Kerns, S. A., Morrisett, J. D., Roberts, R., & Henry, P. D. (1990) · Nature · doi:10.1038/344160a0 · Cited by 858
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
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 843
Hazen, S. L., & Heinecke, J. W. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119379 · Cited by 842
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
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 836
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
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
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
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 809
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 797
Drexler, H., Zeiher, A. M., Meinzer, K., & Just, H. (1991) · The Lancet · doi:10.1016/0140-6736(91)92372-9 · Cited by 794
Is NF-kappaB the sensor of oxidative stress?
Li, N., & Karin, M. (1999) · PubMed · Cited by 786
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
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
Fleming, I., Fisslthaler, B., Dimmeler, S., Kemp, B. E., & Busse, R. (2001) · Circulation Research · doi:10.1161/hh1101.092677 · Cited by 770
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 758
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 753
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
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
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 722
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
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 718
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 714
Doughan, A. K., Harrison, D. G., & Dikalov, S. I. (2008) · Circulation Research · doi:10.1161/circresaha.107.162800 · Cited by 710
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 705
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
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
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×
“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
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
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
(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 679
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
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
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
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
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 646
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
Kissner, R., Nauser, T., Bugnon, P., Lye, P. G., & Koppenol, W. H. (1997) · Chemical Research in Toxicology · doi:10.1021/tx970160x · Cited by 629
Kuhlencordt, P., 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 628
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
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 626
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 622
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
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 615
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
Zou, M., Shi, C., & Cohen, R. A. (2002) · Journal of Clinical Investigation · doi:10.1172/jci14442 · Cited by 613
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
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
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×
“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
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
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 590
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
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
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 578
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 574
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
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 566
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
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 556
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
Dicer Is Required for Embryonic Angiogenesis during Mouse Development
Yang, W. J., Yang, D. D., Na, S., Sandusky, G. E., Zhang, Q. H., & Zhao, G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m413394200 · Cited by 547
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
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 543
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
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 523
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
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
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
The role of heparan sulphate in inflammation
Parish, C. R. (2006) · Nature reviews. Immunology · doi:10.1038/nri1918 · Cited by 513
Regulation of Nox and Duox enzymatic activity and expression
Lambeth, J. D., Kawahara, T., & Diebold, B. A. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.03.028 · Cited by 510
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
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 503
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
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
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
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
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
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
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
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 476
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 476
Pinton, P., Rimessi, A., Marchi, S., Orsini, F., Migliaccio, E., Giorgio, M., Contursi, C., Minucci, S., Mantovani, F., Wieckowski, M. R., et al. (2007) · Science · doi:10.1126/science.1135380 · Cited by 474
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
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 470
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 470
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
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 464
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
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 462
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 461
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
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 451
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
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 447
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
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 439
Mitochondrial nitric oxide synthase
Ghafourifar, P., & Cadenas, E. (2005) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2005.02.005 · Cited by 438
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
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
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
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
Self-citationRedox-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 429
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
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 427
Heitzer, T., Krohn, K., Albers, S., & Meinertz, T. (2000) · Diabetologia · doi:10.1007/s001250051551 · Cited by 427
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
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
Landmesser, U., Bahlmann, F. H., Mueller, M., 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 423
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
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
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 416
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
Wang, L., Fuster, M., Sriramarao, P., & Esko, J. D. (2005) · Nature Immunology · doi:10.1038/ni1233 · Cited by 413
Féron, O., Dessy, C., Moniotte, S., Desager, J., & Balligand, J. (1999) · Journal of Clinical Investigation · doi:10.1172/jci4829 · Cited by 413
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
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
Regulatory functions of ubiquitination in the immune system
Ben‐Neriah, Y. (2002) · Nature Immunology · doi:10.1038/ni0102-20 · Cited by 403
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
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×
“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).”
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 399
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
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
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 393
Role for mitochondrial oxidants as regulators of cellular metabolism
Nemoto, S., Takeda, K., Yu, Z.-X., Ferrans, V. J., & Finkel, T. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.19.7311-7318.2000 · Cited by 393
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Crea, F., Lanza, G. A., & Camici, P. G. (2013) · Springer eBooks · doi:10.1007/978-88-470-5367-0 · Cited by 1,295
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Drummond, G. R., Selemidis, S., Griendling, K. K., & Sobey, C. G. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3403 · Cited by 899
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 905
Metadata
- 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 (medical) › 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
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