The DOI matches its Crossref record; 94 of the 94 references it cites were found in a registry or an index.
NAD(P)H Oxidase: Role in Cardiovascular Biology and Disease
Abstract
Abstract —Reactive oxygen species have emerged as important molecules in cardiovascular function. Recent work has shown that NAD(P)H oxidases are major sources of superoxide in vascular cells and myocytes. The biochemical characterization, activation paradigms, structure, and function of this enzyme are now partly understood. Vascular NAD(P)H oxidases share some, but not all, characteristics of the neutrophil enzyme. In response to growth factors and cytokines, they produce superoxide, which is metabolized to hydrogen peroxide, and both of these reactive oxygen species serve as second messengers to activate multiple intracellular signaling pathways. The vascular NAD(P)H oxidases have been found to be essential in the physiological response of vascular cells, including growth, migration, and modification of the extracellular matrix. They have also been linked to hypertension and to pathological states associated with uncontrolled growth and inflammation, such as atherosclerosis.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“NOXs are multiprotein enzyme complexes that catalyze the electron transfer to molecular oxygen to form ROS, more commonly superoxide, but also hydrogen peroxide (79, 252, 383, 546, 912).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [383]
In the citing paper
“Endothelial cells are a natural source of NO•, and NO• may be generated in mitochondria (137, 139), and with O2•−, to produce ONOO− (and ONOOH), which can modulate cell function”
From Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function (2009) · cites this paper as [137]
In the citing paper
“Both enzymes have been implicated as important prooxidant enzymes contributing to hypertension [32,50,51].”
From Sodium nitrite downregulates vascular NADPH oxidase and exerts antihypertensive effects in hypertension (2011) · cites this paper as [51]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
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
Self-citationGalis, Z. S., Sukhova, G. K., Lark, M. W., & Libby, P. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117619 · Cited by 2,537
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
Rajagopalan, S., Kurz, S. D., Münzel, T. F., Tarpey, M. M., Freeman, B. Α., Griendling, K. K., & Harrison, D. G. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118623 · Cited by 2,466
Self-citationHypercholesterolemia increases endothelial superoxide anion production.
Ohara, Y., Peterson, T. E., & Harrison, D. G. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116491 · Cited by 1,765
Mitogenic Signaling Mediated by Oxidants in Ras-Transformed Fibroblasts
Irani, K., Xia, Y., Zweier, J. L., Sollott, S. J., Der, C. J., Fearon, E. R., Sundaresan, M., Finkel, T., & Goldschmidt-Clermont, P. J. (1997) · Science · doi:10.1126/science.275.5306.1649 · Cited by 1,588
Cell transformation by the superoxide-generating oxidase Mox1
Suh, Y.-A., Arnold, R. S., Lassegue, B., Shi, J., Xu, X., Sorescu, D., Chung, A. B., Griendling, K. K., & Lambeth, J. D. (1999) · Nature · doi:10.1038/43459 · Cited by 1,480
Self-citationRajagopalan, S., Meng, X. P., Ramasamy, S., Harrison, D. G., & Galis, Z. S. (1996) · Journal of Clinical Investigation · doi:10.1172/jci119076 · Cited by 1,137
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
Angiotensin II induces hypertrophy, not hyperplasia, of cultured rat aortic smooth muscle cells.
Geisterfer, A. A., Peach, M. J., & Owens, G. K. (1988) · Circulation Research · doi:10.1161/01.res.62.4.749 · Cited by 1,071
Protein kinase B (c-Akt): a multifunctional mediator of phosphatidylinositol 3-kinase activation
Coffer, P. J., Jin, J., & Woodgett, J. R. (1998) · Biochemical Journal · doi:10.1042/bj3350001 · Cited by 1,064
Lee, S.-R., Kwon, K.-S., Kim, S.-R., & Rhee, S. G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.25.15366 · Cited by 969
Role of Superoxide in Angiotensin II–Induced but Not Catecholamine-Induced Hypertension
Laursen, J. B., Rajagopalan, S., Galis, Z. S., Tarpey, M. M., Freeman, B. Α., & Harrison, D. G. (1997) · Circulation · doi:10.1161/01.cir.95.3.588 · 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
Ushio‐Fukai, M., Zafari, A. M., Fukui, T., Ishizaka, N., & Griendling, K. K. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.38.23317 · Cited by 766
Self-citationDoes superoxide underlie the pathogenesis of hypertension?
Nakazono, K., Watanabe, N., Matsuno, K., Sasaki, J., Sato, T., & Inoue, M. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.22.10045 · Cited by 746
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
Self-citationMeier, B., Radeke, H. H., Selle, S., Younes, M., Sies, H., Resch, K., & Habermehl, G. (1989) · Biochemical Journal · doi:10.1042/bj2630539 · Cited by 650
Ushio‐Fukai, M., Alexander, R. W., Akers, M., & Griendling, K. K. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.24.15022 · Cited by 648
Self-citationMiller, F. J., Gutterman, D. D., Rios, C., Heistad, D. D., & Davidson, B. L. (1998) · Circulation Research · doi:10.1161/01.res.82.12.1298 · Cited by 623
Role of NADH/NADPH Oxidase–Derived H 2 O 2 in Angiotensin II–Induced Vascular Hypertrophy
Zafari, A. M., Ushio‐Fukai, M., Akers, M., Yin, Q., Shah, A. A., Harrison, D. G., Taylor, W. R., & Griendling, K. K. (1998) · Hypertension · doi:10.1161/01.hyp.32.3.488 · Cited by 610
Self-citationOscillatory and Steady Laminar Shear Stress Differentially Affect Human Endothelial Redox State
Keulenaer, G. W. D., Chappell, D. C., Ishizaka, N., Nerem, R. M., Alexander, R. W., & Griendling, K. K. (1998) · Circulation Research · doi:10.1161/01.res.82.10.1094 · Cited by 605
Self-citationZweier, J. L., Kuppusamy, P., & Lutty, G. A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.11.4046 · Cited by 601
Ushio‐Fukai, M., Alexander, R. W., Akers, M., Yin, Q., Fujio, Y., Walsh, K., & Griendling, K. K. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.32.22699 · Cited by 558
Self-citationAngiotensin II-stimulated protein synthesis in cultured vascular smooth muscle cells.
Berk, B. C., Vekshtein, V. I., Gordon, H. M., & Tsuda, T. (1989) · Hypertension · doi:10.1161/01.hyp.13.4.305 · Cited by 555
p22phox mRNA Expression and NADPH Oxidase Activity Are Increased in Aortas From Hypertensive Rats
Fukui, T., Ishizaka, N., Rajagopalan, S., Laursen, J. B., Capers, Q., Taylor, W. R., Harrison, D. G., de Leon, H., Wilcox, J. N., & Griendling, K. K. (1997) · Circulation Research · doi:10.1161/01.res.80.1.45 · Cited by 553
Self-citationNADH oxidoreductase is a major source of superoxide anion in bovine coronary artery endothelium
Mohazzab, K. M., Kaminski, P. M., & Wolin, M. S. (1994) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1994.266.6.h2568 · Cited by 536
Li, Y., Zhu, H., Kuppusamy, P., Roubaud, V., Zweier, J. L., & Trush, M. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.4.2015 · Cited by 526
Nakamura, K., Fushimi, K., Kouchi, H., Mihara, K., Miyazaki, M., Ohe, T., & Namba, M. (1998) · Circulation · doi:10.1161/01.cir.98.8.794 · Cited by 510
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
Parkos, C. A., Allen, R. A., Cochrane, C. G., & Jesaitis, A. J. (1987) · Journal of Clinical Investigation · doi:10.1172/jci113128 · Cited by 455
Pagano, P. J., Clark, J. K., Cifuentes-Pagano, M. E., Clark, S. M., Callis, G. M., & Quinn, M. T. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.26.14483 · Cited by 455
Big Mitogen-activated Protein Kinase 1 (BMK1) Is a Redox-sensitive Kinase
Abe, J., Kusuhara, M., Ulevitch, R. J., Berk, B. C., & Lee, J.-D. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.28.16586 · Cited by 441
Expression of phagocyte NADPH oxidase components in human endothelial cells
Jones, S. A., O’Donnell, V. B., Wood, J. D., Broughton, J. P., Hughes, E. J., & Jones, O. T. (1996) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1996.271.4.h1626 · Cited by 427
Thannickal, V. J., & Fanburg, B. L. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.51.30334 · Cited by 424
Baas, A. S., & Berk, B. C. (1995) · Circulation Research · doi:10.1161/01.res.77.1.29 · Cited by 415
p21 as a Common Signaling Target of Reactive Free Radicals and Cellular Redox Stress
Lander, H. M., Ogiste, J. S., Teng, K. K., & Novogrodsky, A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.36.21195 · Cited by 405
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
Chen, X.-L., Tummala, P. E., Olbrych, M. T., Alexander, R. W., & Medford, R. M. (1998) · Circulation Research · doi:10.1161/01.res.83.9.952 · Cited by 384
Lucigenin chemiluminescence in the assessment of neutrophil superoxide production
Gyllenhammar, H. (1987) · Journal of Immunological Methods · doi:10.1016/0022-1759(87)90461-3 · Cited by 355
In Vivo Evidence for Microvascular Oxidative Stress in Spontaneously Hypertensive Rats
Suzuki, H., SWEI, A., Zweifach, B. W., & Schmid‐Schönbein, G. W. (1995) · Hypertension · doi:10.1161/01.hyp.25.5.1083 · Cited by 340
Stimulation of a Vascular Smooth Muscle Cell NAD(P)H Oxidase by Thrombin
Patterson, C., Ruef, J., Madamanchi, N. R., Barry-Lane, P., Hu, Z., Horaist, C., Ballinger, C. A., Brasier, A. R., Bode, C., & Runge, M. S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.28.19814 · Cited by 330
Clerk, A., Fuller, S. J., Michael, A., & Sugden, P. H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.13.7228 · Cited by 314
Tumour necrosis factor α activates a p22phox-based NADH oxidase in vascular smooth muscle
KEULENAER, W. G. D., Alexander, R. W., Ushio‐Fukai, M., Ishizaka, N., & Griendling, K. K. (1998) · Biochemical Journal · doi:10.1042/bj3290653 · Cited by 308
Self-citationAn NADPH oxidase superoxide-generating system in the rabbit aorta
Pagano, P. J., Ito, Y., Tornheim, K., Gallop, P. M., Tauber, A. I., & Cohen, R. A. (1995) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1995.268.6.h2274 · Cited by 302
Satriano, J. A., Shuldiner, M., Hora, K., Xing, Y., Shan, Z., & Schlöndorff, D. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116737 · Cited by 274
Angiotensin II induces superoxide anion production by mesangial cells
Jaimes, E. A., Galcerán, J., & Raij, L. R. (1998) · Kidney International · doi:10.1046/j.1523-1755.1998.00068.x · Cited by 271
O 2 sensing is preserved in mice lacking the gp91 phox subunit of NADPH oxidase
Archer, S. L., Reeve, H. L., Michelakis, E. D., Puttagunta, L., Waite, R. E., Nelson, D. P., Dinauer, M. C., & Weir, Ε. K. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.14.7944 · Cited by 260
Marumo, T., Schini‐Kerth, V. B., Fißlthaler, B., & Busse, R. (1997) · Circulation · doi:10.1161/01.cir.96.7.2361 · Cited by 252
Oxidative Stress in the Dahl Hypertensive Rat
SWEI, A., Lacy, F., DeLano, F. A., & Schmid‐Schönbein, G. W. (1997) · Hypertension · doi:10.1161/01.hyp.30.6.1628 · Cited by 236
Identification of a superoxide-generating NADPH oxidase system in human fibroblasts
Meier, B., Cross, A. R., Hancock, J. T., Kaup, F. ‐., & Jones, O. T. G. (1991) · Biochemical Journal · doi:10.1042/bj2750241 · Cited by 229
Pagano, P. J., Chanock, S. J., Siwik, D. A., Colucci, W. S., & Clark, J. K. (1998) · Hypertension · doi:10.1161/01.hyp.32.2.331 · Cited by 226
Bhunia, A. K., Han, H., Snowden, A., & Chatterjee, S. B. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.25.15642 · Cited by 200
Redox control of vascular smooth muscle proliferation
Griendling, K. K., & Ushio‐Fukai, M. (1998) · Journal of Laboratory and Clinical Medicine · doi:10.1016/s0022-2143(98)90019-1 · Cited by 199
Self-citationChiu, J., Wung, B., Shyy, J. Y. J., Hsieh, H. J., & Wang, D. L. (1997) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.17.12.3570 · Cited by 192
Subunit structure of the mammalian exocyst complex
Kee, Y., Yoo, J.-S., Hazuka, C. D., Peterson, K. E., Hsu, S.-C., & Scheller, R. H. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.26.14438 · Cited by 189
Bayraktutan, U. (1998) · Cardiovascular Research · doi:10.1016/s0008-6363(98)00003-0 · Cited by 186
Molecular adaptation of vascular endothelial cells to oxidative stress
Lü, D., Maulik, N., Moraru, I. I., Kreutzer, D. L., & DAS, D. K. (1993) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1993.264.3.c715 · Cited by 177
Cyclic strain induces an oxidative stress in endothelial cells
Howard, A. B., Alexander, R. W., Nerem, R. M., Griendling, K. K., & Taylor, W. R. (1997) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1997.272.2.c421 · Cited by 171
Self-citationRedox Regulation of Signal Transduction in Cardiac and Smooth Muscle
Suzuki, Y., & Ford, G. D. (1999) · Journal of Molecular and Cellular Cardiology · doi:10.1006/jmcc.1998.0872 · Cited by 170
The expression of NADPH oxidase components in human glomerular mesangial cells
Jones, S. A., Hancock, J. T., Jones, O. T., Neubauer, A., & Topley, N. (1995) · Journal of the American Society of Nephrology · doi:10.1681/asn.v571483 · Cited by 163
N -Acetyl-Cysteine Decreases the Matrix-Degrading Capacity of Macrophage-Derived Foam Cells
Galis, Z. S., Asanuma, K., Godin, D., & Meng, X. (1998) · Circulation · doi:10.1161/01.cir.97.24.2445 · Cited by 159
Sites of superoxide anion production detected by lucigenin in calf pulmonary artery smooth muscle
Mohazzab-H., K. M., & Wolin, M. S. (1994) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1994.267.6.l815 · Cited by 159
Zulueta, J. J., Yu, F. S., Hertig, I. A., Thannickal, V. J., & Hassoun, P. M. (1995) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.12.1.7529030 · Cited by 151
Yeh, L.-H., Park, Y. J., Hansalia, R. J., Ahmed, I. S., Deshpande, S. S., Goldschmidt‐Clermont, P. J., Irani, K., & Alevriadou, B. R. (1999) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1999.276.4.c838 · Cited by 149
Phan, S. H., Gannon, D. E., Varani, J., Ryan, U. S., & Ward, P. A. (1989) · PubMed Central · Cited by 147
Radeke, H. H., Cross, A. R., Hancock, J. T., Jones, O. T., Nakamura, M., Kaever, V., & Resch, K. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54815-8 · Cited by 144
Lactate and P o 2 Modulate Superoxide Anion Production in Bovine Cardiac Myocytes
Mohazzab-H., K. M., Kaminski, P. M., & Wolin, M. S. (1997) · Circulation · doi:10.1161/01.cir.96.2.614 · Cited by 140
Dusi, S., Bianca, V. D., Grzeskowiak, M., & Rossi, F. (1993) · Biochemical Journal · doi:10.1042/bj2900173 · Cited by 123
Mohazzab, K. M., & Wolin, M. S. (1994) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1994.267.6.l823 · Cited by 122
Meier, B., Jesaitis, A. J., Emmendörffer, A., Roesler, J., & Quinn, M. T. (1993) · Biochemical Journal · doi:10.1042/bj2890481 · Cited by 117
Taher, M. M., Garcia, J. G. N., & Natarajan, V. (1993) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1993.1281 · Cited by 109
Cytochrome b-558 α-subunit cloning and expression in rat aortic smooth muscle cells
Fukui, T., Lassegue, B. P., Kai, H., Alexander, R. W., & Griendling, K. K. (1995) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(95)00098-4 · Cited by 108
Self-citationBhunia, A. K., Arai, T., Bulkley, G. B., & Chatterjee, S. B. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.51.34349 · Cited by 107
Role of oxygen radicals generated by NADPH oxidase in apoptosis induced in human leukemia cells.
Hiraoka, W., Vazquez, N., Nieves‐Neira, W., et al. (1998) · Journal of Clinical Investigation · doi:10.1172/jci3437 · Cited by 106
Activation of NADPH oxidase is required for macrophage-mediated oxidation of low-density lipoprotein
Aviram, M., Rosenblat, M., Etzioni, A., & Lévy, R. (1996) · Metabolism · doi:10.1016/s0026-0495(96)90005-0 · Cited by 105
Nishio, E., & Watanabe, Y. (1997) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0701171 · Cited by 102
NADH/NADPH Oxidase and Vascular Function
Griendling, K. K., & Ushio‐Fukai, M. (1997) · Trends in Cardiovascular Medicine · doi:10.1016/s1050-1738(97)00088-1 · Cited by 99
Self-citationWu, Y., Kwon, K., & Rhee, S. G. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01415-x · Cited by 98
Marumo, T., Schini‐Kerth, V. B., Brandes, R. P., & Busse, R. (1998) · Hypertension · doi:10.1161/01.hyp.32.6.1083 · Cited by 89
Keulenaer, G. W. D., Ushio‐Fukai, M., Yin, Q., Chung, A. B., Lyons, P. R., Ishizaka, N., Kalpana, R., Taylor, W. R., Alexander, R. W., & Griendling, K. K. (2000) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.20.2.385 · Cited by 88
Self-citationZafari, A. M., Ushio‐Fukai, M., Minieri, C. A., et al. (1999) · Antioxidants and Redox Signaling · doi:10.1089/ars.1999.1.2-167 · Cited by 86
Self-citationMohazzab-H., K. M., Kaminski, P. M., Fayngersh, R. P., & Wolin, M. S. (1996) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1996.270.3.h1044 · Cited by 86
Roos, D. (1996) · Frontiers in bioscience · doi:10.2741/a117 · Cited by 76
Superoxide anion production by rabbit thoracic aorta: effect of endothelium-derived nitric oxide
Pagano, P. J., Tornheim, K., & Cohen, R. A. (1993) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1993.265.2.h707 · Cited by 76
O’Donnell, V. B., & Azzi, A. (1996) · Biochemical Journal · doi:10.1042/bj3180805 · Cited by 74
Jones, O. T. G. (1994) · BioEssays · doi:10.1002/bies.950161211 · Cited by 74
Yagisawa, M., Yuo, A., Yonemaru, M., Imajoh‐Ohmi, S., Kanegasaki, S., Yazaki, Y., & Takaku, F. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.1691 · Cited by 72
Targets of oxidative stress in cardiovascular system
Chakraborti, S., Chakraborti, T., Michael, J. R., Batabyal, S., & Ghosh, S. K. (1998) · Molecular and Cellular Biochemistry · doi:10.1023/a:1006802903504 · Cited by 70
Pu, M., Akhand, A. A., Kato, M., Hamaguchi, M., Koike, T., Iwata, H., Sabe, H., Suzuki, H., & Nakashima, I. (1996) · PubMed · Cited by 66
Toshiyuki, A. R. A. I., Kelly, S. A., Brengman, M. L., TAKANO, M., Smith, E. H., Goldschmidt‐Clermont, P. J., & Bulkley, G. B. (1998) · Biochemical Journal · doi:10.1042/bj3310853 · Cited by 51
Nemani, R. K., & Lee, E. Y. C. (1993) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1993.1004 · Cited by 43
Nitric oxide and reactive oxygen species in vascular injury
Rubbo, H., Tarpey, M. M., & Freeman, B. Α. (1995) · Biochemical Society Symposia · doi:10.1042/bss0610033 · Cited by 41
Regulation of the Superoxide Releasing System in Human Fibroblasts
Meier, B. (1996) · Advances in experimental medicine and biology · doi:10.1007/978-1-4757-9480-9_15 · Cited by 10
Research works printed but not linked: 20
- 10.1161/res.74.6.8187280 · DOI
- 10.1161/circ.96.2.614 · DOI
- 10.1161/hyp.32.3.488 · DOI
- 10.1161/hyp.32.2.331 · DOI
- 10.1161/circ.96.7.2361 · DOI
- 10.1161/res.82.10.1094 · DOI
- 10.1161/atvb.17.12.3570 · DOI
- 10.1161/res.80.1.45 · DOI
- 10.1161/hyp.32.6.1083 · DOI
- 10.1161/res.69.5.1934359 · DOI
- 10.1161/res.83.9.952 · DOI
- 10.1161/atvb.20.2.385 · DOI
- 10.1161/res.62.4.3280155 · DOI
- 10.1161/circ.98.8.794 · DOI
- 10.1161/circ.99.15.2027 · DOI
- 10.1161/res.82.12.1298 · DOI
- 10.1161/circ.97.24.2445 · DOI
- 10.1161/hyp.25.5.1083 · DOI
- 10.1161/circ.95.3.588 · DOI
- 10.1161/hyp.30.6.1628 · DOI
Cited by
Sorted by citations
Free Radicals in the Physiological Control of Cell Function
Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855
The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology
Bedard, K., & Krause, K.-H. (2007) · Physiological Reviews · doi:10.1152/physrev.00044.2005 · Cited by 6,989
Nitric Oxide and Peroxynitrite in Health and Disease
Pacher, P., Beckman, J. S., & Liaudet, L. (2007) · Physiological Reviews · doi:10.1152/physrev.00029.2006 · Cited by 6,390
Increased oxidative stress in obesity and its impact on metabolic syndrome
Furukawa, S., Fujita, T., Shimabukuro, M., Iwaki, M., Yamada, Y., Nakajima, Y., Nakayama, O., Makishima, M., Matsuda, M., & Shimomura, I. (2004) · Journal of Clinical Investigation · doi:10.1172/jci21625 · Cited by 5,508
Nitric oxide synthases: regulation and function
Forstermann, U., & Sessa, W. C. (2012) · European Heart Journal · doi:10.1093/eurheartj/ehr304 · Cited by 4,409
Metadata
- Authors
- Griendling, K. K., Sorescu, D., & Ushio-Fukai, M.
- Affiliations
- Emory University (US)
- From the Department of Medicine, Division of Cardiology, Emory University, Atlanta, Ga.
- ORCID
- Griendling, Kathy K.
- Venue
- Circulation Research
- Published
- 2000-03-17
- Volume
- 86
- Issue
- 5
- Pages
- 494-501
- ISSN
- 0009-7330 (ISSN-L)
- 1524-4571
- OpenAlex
- W2123799914
- Cited by
- 2,886
- References
- 94
- Citations by year
- 2026: 14 · 2025: 29 · 2024: 27 · 2023: 39 · 2022: 43 · 2021: 62 · 2020: 70 · 2019: 51 · 2018: 64 · 2017: 54 · 2016: 79 · 2015: 79 · 2014: 124 · 2013: 131 · 2012: 137
- FWCI
- 19.54
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Circulation Research (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Heart, Lung, and Blood Institute (HL 58000, HL38206, HL58863, P01HL058000, R01HL058863)
- Topics
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- NADPH oxidase, reactive oxygen species, superoxide, hydrogen peroxide, vascular cells, growth factor signaling, cytokine signaling, intracellular signaling, cell migration, extracellular matrix remodeling, hypertension, atherosclerosis, inflammation
- MeSH terms
- Arteries, Arteriosclerosis, Humans, Myocardium, Reactive Oxygen Species, NADPH Oxidases
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