NAD(P)H Oxidase: Role in Cardiovascular Biology and Disease

Griendling, Kathy K.; Sorescu, Dan; Ushio-Fukai, Masuko

doi:10.1161/01.res.86.5.494

Cited by 2,886Nitric Oxide and Endothelin EffectsNeutrophil, Myeloperoxidase and Oxidative MechanismsRedox biology and oxidative stress

NAD(P)H Oxidase: Role in Cardiovascular Biology and Disease

Griendling, Kathy K., Sorescu, Dan, Ushio-Fukai, Masuko·2000·Circulation Research

DOI 10.1161/01.res.86.5.494

Open this paper in CoChat — free account

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.

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

Crossref · 10.1161/01.res.86.5.494

Cites

94 of 94 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

NOXs are multiprotein enzyme complexes that catalyze the electron transfer to molecular oxygen to form ROS, more commonly superoxide, but also hydrogen peroxide.
“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]
Endothelial cells are a natural source of NO•, and NO• may be generated in mitochondria, and with O2•−, produce ONOO−.
“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]
Both xanthine oxidase and NADPH oxidase have been implicated as important prooxidant enzymes contributing to hypertension.
“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.

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
Self-citation
Increased expression of matrix metalloproteinases and matrix degrading activity in vulnerable regions of human atherosclerotic plaques.
Galis, Z. S., Sukhova, G. K., Lark, M. W., & Libby, P. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117619 · Cited by 2,537 · see citing works
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 · see citing works
Angiotensin II-mediated hypertension in the rat increases vascular superoxide production via membrane NADH/NADPH oxidase activation. Contribution to alterations of vasomotor tone.
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 2,441 · see citing works
Self-citation
Hypercholesterolemia 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 · see citing works
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 · see citing works
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 · see citing works
Self-citation
Reactive oxygen species produced by macrophage-derived foam cells regulate the activity of vascular matrix metalloproteinases in vitro. Implications for atherosclerotic plaque stability.
Rajagopalan, 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 · see citing works
Vascular cell adhesion molecule-1 (VCAM-1) gene transcription and expression are regulated through an antioxidant-sensitive mechanism in human vascular endothelial cells
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
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 · see citing works
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 1,067 · see citing works
Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor
Lee, S.-R., Kwon, K.-S., Kim, S.-R., & Rhee, S. G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.25.15366 · Cited by 969 · see citing works
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 · see citing works
Activation of the Receptor for Advanced Glycation End Products Triggers a p21 -dependent Mitogen-activated Protein Kinase Pathway Regulated by Oxidant Stress
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
p22 Is a Critical Component of the Superoxide-generating NADH/NADPH Oxidase System and Regulates Angiotensin IIinduced Hypertrophy in Vascular Smooth Muscle Cells
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 · see citing works
Self-citation
Does 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 · 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
Self-citation
Human fibroblasts release reactive oxygen species in response to interleukin-1 or tumour necrosis factor-α
Meier, B., Radeke, H. H., Selle, S., Younes, M., Sies, H., Resch, K., & Habermehl, G. (1989) · Biochemical Journal · doi:10.1042/bj2630539 · Cited by 650 · see citing works
p38 Mitogen-activated Protein Kinase Is a Critical Component of the Redox-sensitive Signaling Pathways Activated by Angiotensin II
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 650 · see citing works
Self-citation
Superoxide Production in Vascular Smooth Muscle Contributes to Oxidative Stress and Impaired Relaxation in Atherosclerosis
Miller, 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 · see citing works
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 · see citing works
Self-citation
Oscillatory 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 · see citing works
Self-citation
Measurement of endothelial cell free radical generation: evidence for a central mechanism of free radical injury in postischemic tissues.
Zweier, 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 · see citing works
Reactive Oxygen Species Mediate the Activation of Akt/Protein Kinase B by Angiotensin II in Vascular Smooth Muscle Cells
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 · see citing works
Self-citation
Angiotensin 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 · see citing works
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 · see citing works
Self-citation
NADH 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 · see citing works
Validation of Lucigenin (Bis-N-methylacridinium) as a Chemilumigenic Probe for Detecting Superoxide Anion Radical Production by Enzymatic and Cellular Systems
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 · see citing works
Inhibitory Effects of Antioxidants on Neonatal Rat Cardiac Myocyte Hypertrophy Induced by Tumor Necrosis Factor-α and Angiotensin II
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 · 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
Purified cytochrome b from human granulocyte plasma membrane is comprised of two polypeptides with relative molecular weights of 91,000 and 22,000
Parkos, C. A., Allen, R. A., Cochrane, C. G., & Jesaitis, A. J. (1987) · Journal of Clinical Investigation · doi:10.1172/jci113128 · Cited by 455 · see citing works
Localization of a constitutively active, phagocyte-like NADPH oxidase in rabbit aortic adventitia: Enhancement by angiotensin II
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 · see citing works
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 · see citing works
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 · see citing works
Activation of an H2O2-generating NADH Oxidase in Human Lung Fibroblasts by Transforming Growth Factor β1
Thannickal, V. J., & Fanburg, B. L. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.51.30334 · Cited by 424 · see citing works
Differential Activation of Mitogen-Activated Protein Kinases by H 2 O 2 and O 2 − in Vascular Smooth Muscle Cells
Baas, A. S., & Berk, B. C. (1995) · Circulation Research · doi:10.1161/01.res.77.1.29 · Cited by 416 · see citing works
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 · see citing works
Chronic treatment with polyethylene-glycolated superoxide dismutase partially restores endothelium-dependent vascular relaxations in cholesterol-fed rabbits.
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
Angiotensin II Induces Monocyte Chemoattractant Protein-1 Gene Expression in Rat Vascular Smooth Muscle Cells
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 · see citing works
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 358 · see citing works
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 · see citing works
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 · see citing works
Stimulation of “Stress-regulated” Mitogen-activated Protein Kinases (Stress-activated Protein Kinases/c-Jun N-terminal Kinases and p38-Mitogen-activated Protein Kinases) in Perfused Rat Hearts by Oxidative and Other Stresses
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 · see citing works
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 · see citing works
Self-citation
An 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 · see citing works
Oxygen radicals as second messengers for expression of the monocyte chemoattractant protein, JE/MCP-1, and the monocyte colony-stimulating factor, CSF-1, in response to tumor necrosis factor-alpha and immunoglobulin G. Evidence for involvement of reduced nicotinamide adenine dinucleotide phosphate (NADPH)-dependent oxidase.
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 · see citing works
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 · see citing works
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 263 · see citing works
Platelet-Derived Growth Factor–Stimulated Superoxide Anion Production Modulates Activation of Transcription Factor NF-κB and Expression of Monocyte Chemoattractant Protein 1 in Human Aortic Smooth Muscle Cells
Marumo, T., Schini‐Kerth, V. B., Fißlthaler, B., & Busse, R. (1997) · Circulation · doi:10.1161/01.cir.96.7.2361 · Cited by 252 · see citing works
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 · see citing works
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 232 · see citing works
Angiotensin II Induces p67 phox mRNA Expression and NADPH Oxidase Superoxide Generation in Rabbit Aortic Adventitial Fibroblasts
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 · see citing works
Redox-regulated Signaling by Lactosylceramide in the Proliferation of Human Aortic Smooth Muscle Cells
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 · see citing works
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 · see citing works
Self-citation
Reactive Oxygen Species Are Involved in Shear Stress-Induced Intercellular Adhesion Molecule-1 Expression in Endothelial Cells
Chiu, 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 · see citing works
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 · see citing works
Expression of a functional neutrophil-type NADPH oxidase in cultured rat coronary microvascular endothelial cells
Bayraktutan, U. (1998) · Cardiovascular Research · doi:10.1016/s0008-6363(98)00003-0 · Cited by 186 · see citing works
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 · see citing works
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 · see citing works
Self-citation
Redox 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 · see citing works
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 · see citing works
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 160 · see citing works
Sites of superoxide anion production detected by lucigenin in calf pulmonary artery smooth muscle
Mohazzab, 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 · see citing works
Release of Hydrogen Peroxide in Response to Hypoxia-Reoxygenation: Role of an NAD(P)H Oxidase-Like Enzyme in Endothelial Cell Plasma Membrane
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 · see citing works
Shear-induced tyrosine phosphorylation in endothelial cells requires Rac1-dependent production of ROS
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 · see citing works
Xanthine oxidase activity in rat pulmonary artery endothelial cells and its alteration by activated neutrophils.
Phan, S. H., Gannon, D. E., Varani, J., Ryan, U. S., & Ward, P. A. (1989) · PubMed Central · Cited by 147 · see citing works
Functional expression of NADPH oxidase components (alpha- and beta-subunits of cytochrome b558 and 45-kDa flavoprotein) by intrinsic human glomerular mesangial cells.
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 · see citing works
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 · see citing works
Relationship between phosphorylation and translocation to the plasma membrane of p47phox and p67phox and activation of the NADPH oxidase in normal and Ca2+-depleted human neutrophils
Dusi, S., Bianca, V. D., Grzeskowiak, M., & Rossi, F. (1993) · Biochemical Journal · doi:10.1042/bj2900173 · Cited by 123 · see citing works
Properties of a superoxide anion-generating microsomal NADH oxidoreductase, a potential pulmonary artery PO2 sensor
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 · see citing works
The cytochrome b-558 molecules involved in the fibroblast and polymorphonuclear leucocyte superoxide-generating NADPH oxidase systems are structurally and genetically distinct
Meier, B., Jesaitis, A. J., Emmendörffer, A., Roesler, J., & Quinn, M. T. (1993) · Biochemical Journal · doi:10.1042/bj2890481 · Cited by 118 · see citing works
Hydroperoxide-Induced Diacylglycerol Formation and Protein Kinase C Activation in Vascular Endothelial Cells
Taher, M. M., Garcia, J. G. N., & Natarajan, V. (1993) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1993.1281 · Cited by 109 · see citing works
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 · see citing works
Self-citation
Lactosylceramide Mediates Tumor Necrosis Factor-α-induced Intercellular Adhesion Molecule-1 (ICAM-1) Expression and the Adhesion of Neutrophil in Human Umbilical Vein Endothelial Cells
Bhunia, 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 · see citing works
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 · see citing works
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 · see citing works
The involvement of reactive oxygen species and arachidonic acid in α1‐adrenoceptor‐induced smooth muscle cell proliferation and migration
Nishio, E., & Watanabe, Y. (1997) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0701171 · Cited by 102 · see citing works
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 · see citing works
Self-citation
Probing cellular protein targets of H2O2 with fluorescein‐conjugated iodoacetamide and antibodies to fluorescein
Wu, Y., Kwon, K., & Rhee, S. G. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01415-x · Cited by 98 · see citing works
Glucocorticoids Inhibit Superoxide Anion Production and p22 Phox mRNA Expression in Human Aortic Smooth Muscle Cells
Marumo, T., Schini‐Kerth, V. B., Brandes, R. P., & Busse, R. (1998) · Hypertension · doi:10.1161/01.hyp.32.6.1083 · Cited by 89 · see citing works
Convergence of Redox-Sensitive and Mitogen-Activated Protein Kinase Signaling Pathways in Tumor Necrosis Factor-α–Mediated Monocyte Chemoattractant Protein-1 Induction in Vascular Smooth Muscle Cells
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 · see citing works
Self-citation
Arachidonic Acid Metabolites Mediate Angiotensin II-Induced NADH/NADPH Oxidase Activity and Hypertrophy in Vascular Smooth Muscle Cells
Zafari, 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 · see citing works
Self-citation
Oxygen-elicited responses in calf coronary arteries: role of H2O2 production via NADH-derived superoxide
Mohazzab-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 · see citing works
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 · see citing works
Interactions between the components of the human NADPH oxidase A review about the intrigues in the phox family
Roos, D. (1996) · Frontiers in bioscience · doi:10.2741/a117 · Cited by 75 · see citing works
High rates of extracellular superoxide generation by cultured human fibroblasts: involvement of a lipid-metabolizing enzyme
O’Donnell, V. B., & Azzi, A. (1996) · Biochemical Journal · doi:10.1042/bj3180805 · Cited by 74 · see citing works
The regulation of superoxide production by the NADPH oxidase of neutrophils and other mammalian cells
Jones, O. T. G. (1994) · BioEssays · doi:10.1002/bies.950161211 · Cited by 74 · see citing works
Superoxide Release and NADPH Oxidase Components in Mature Human Phagocytes: Correlation between Functional Capacity and Amount of Functional Proteins
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 · see citing works
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 · see citing works
Evidence of a novel redox-linked activation mechanism for the Src kinase which is independent of tyrosine 527-mediated regulation.
Pu, M., Akhand, A. A., Kato, M., Hamaguchi, M., Koike, T., Iwata, H., Sabe, H., Suzuki, H., & Nakashima, I. (1996) · PubMed · Cited by 66 · see citing works
Ambient but not incremental oxidant generation effects intercellular adhesion molecule 1 induction by tumour necrosis factor α in endothelium
Toshiyuki, A. R. A. I., Kelly, S. A., Brengman, M. L., et al. (1998) · Biochemical Journal · doi:10.1042/bj3310853 · Cited by 52 · see citing works
Reactivity of Sulfhydryl Groups of the Catalytic Subunits of Rabbit Skeletal Muscle Protein Phosphatases 1 and 2A
Nemani, R. K., & Lee, E. Y. C. (1993) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1993.1004 · Cited by 43 · see citing works
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 · see citing works
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 · see citing works

Flagged first, then by citations

Research works printed but not linked: 6

[11]11. Mohazzab-H KM, Kaminski PM, Wolin MS. Lactate and PO2 modulate superoxide anion production in bovine cardiac myocytes: potential role of NADH oxidase. Circulation . 1997;96:614-620.
[12]12. Mohazzab-H KM, Wolin MS. Properties of a superoxide aniongenerating microsomal NADH oxidoreductase, a potential pulmonary artery PO 2 sensor. Am J Physiol . 1994;267:L823-L831.
[21]21. Zafari AM, Ushio-Fukai M, Akers M, Yin Q, Shah A, Harrison DG, Taylor WR, Griendling KK. Novel role of NADH/NADPH oxidasederived hydrogen peroxide in angiotensin II-induced hypertrophy of rat vascular smooth muscle cells. Hypertension . 1998;32:488-495.
[36]36. Suh Y, Arnold RS, Lasse `gue B, Shi J, Xu X, Sorescu D, Chung AB, Griendling KK, Lambeth JD. Cell transformation by the superoxidegenerating oxidase mox1. Nature . 1999;401:79-82.
[56]56. Rajagopalan S, Meng XP, Ramasamy S, Harrison DG, Galis ZS. Reactive oxygen species produced by macrophage-derived foam cells regulate the activity of vascular matrix metalloproteinases in vitro. J Clin Invest . 1996;98:2572-2579.
[77]77. De Keulenaer GW, Ushio-Fukai M, Yin Q, Chung AB, Lyons PR, Ishizaka N, Rengarajan K, Taylor WR, Alexander RW, Griendling KK. Convergence of redox-sensitive and mitogen activated protein kinase signaling pathways in TNFa -mediated MCP-1 induction in vascular smooth muscle cells. Arterioscler Thromb Vasc Biol . 2000;20:385-391.

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 · see citing works
The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology
Bedard, K., & Krause, K.-H. (2007) · Physiological Reviews · doi:10.1152/physrev.00044.2005 · Cited by 6,989 · see citing works
Nitric Oxide and Peroxynitrite in Health and Disease
Pacher, P., Beckman, J. S., & Liaudet, L. (2007) · Physiological Reviews · doi:10.1152/physrev.00029.2006 · Cited by 6,390 · see citing works
Increased oxidative stress in obesity and its impact on metabolic syndrome
Furukawa, S., Fujita, T., Shimabukuro, M., Iwaki, M., Yamada, Y., Nakajima, Y., Nakayama, O., Makishima, M., Matsuda, M., & Shimomura, I. (2004) · Journal of Clinical Investigation · doi:10.1172/jci21625 · Cited by 5,508 · see citing works
Nitric oxide synthases: regulation and function
Forstermann, U., & Sessa, W. C. (2012) · European Heart Journal · doi:10.1093/eurheartj/ehr304 · Cited by 4,409 · 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
A Novel Paradigm for Heart Failure With Preserved Ejection Fraction
Paulus, W. J., & Tschöpe, C. (2013) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2013.02.092 · Cited by 3,564 · see citing works
Endothelial Function and Dysfunction: Testing and Clinical Relevance
Deanfield, J. E., Halcox, J. P., & Rabelink, T. J. (2007) · Circulation · doi:10.1161/circulationaha.106.652859 · Cited by 2,710 · see citing works
Myeloperoxidase: friend and foe
Klebanoff, S. J. (2005) · Journal of Leukocyte Biology · doi:10.1189/jlb.1204697 · Cited by 2,282 · see citing works
Endothelial Nitric Oxide Synthase in Vascular Disease: From Marvel to Menace
Förstermann, U., & Münzel, T. (2006) · Circulation · doi:10.1161/circulationaha.105.602532 · Cited by 1,957 · see citing works
Angiotensin II cell signaling: physiological and pathological effects in the cardiovascular system
Mehta, P. K., & Griendling, K. K. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00287.2006 · Cited by 1,924 · see citing works
Self-citation
Oxidative Stress and Vascular Disease
Madamanchi, N. R., Vendrov, A., & Runge, M. S. (2005) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/01.atv.0000150649.39934.13 · Cited by 1,618 · see citing works
Oxidation of tetrahydrobiopterin leads to uncoupling of endothelial cell nitric oxide synthase in hypertension
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
Obesity and Systemic Oxidative Stress: Clinical Correlates of Oxidative Stress in The Framingham Study
Keaney, J. F., Larson, M. G., Vasan, R. S., Wilson, P. W. F., Lipinska, I., Corey, D., Massaro, J. M., Sutherland, P., Vita, J. A., & Benjamin, E. J. (2003) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/01.atv.0000058402.34138.11 · Cited by 1,304 · see citing works
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
Self-citation
Obstructive sleep apnoea syndrome – an oxidative stress disorder
Lavie, L. (2003) · Sleep Medicine Reviews · doi:10.1053/smrv.2002.0261 · Cited by 993 · see citing works
Reactive oxygen species and cell signaling: Respiratory burst in macrophage signaling
Forman, H. J., & Torres, M. (2002) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.2206007 · Cited by 891 · 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
Self-citation
Endothelial Function: A Critical Determinant in Atherosclerosis?
Landmesser, U., Hornig, B., & Drexler, H. (2004) · Circulation · doi:10.1161/01.cir.0000129501.88485.1f · Cited by 851 · see citing works
Novel gp91 phox Homologues in Vascular Smooth Muscle Cells: nox1 Mediates Angiotensin II–Induced Superoxide Formation and Redox-Sensitive Signaling Pathways
Lassègue, B., Sorescu, D., Szöcs, K., Yin, Q., Akers, M., Zhang, Y., Grant, S. L., Lambeth, J. D., & Griendling, K. K. (2001) · Circulation Research · doi:10.1161/hh0901.090299 · Cited by 839 · see citing works
Self-citation
Cross talk between mitochondria and NADPH oxidases
Dikalov, S. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.06.033 · Cited by 783 · see citing works
NAD(P)H Oxidase 4 Mediates Transforming Growth Factor-β1–Induced Differentiation of Cardiac Fibroblasts Into Myofibroblasts
Cucoranu, I., Clempus, R., Dikalova, A., Phelan, P. J., Ariyan, S., Dikalov, S., & Sorescu, D. (2005) · Circulation Research · doi:10.1161/01.res.0000187457.24338.3d · Cited by 786 · see citing works
Self-citation
Endothelial cell superoxide generation: regulation and relevance for cardiovascular pathophysiology
Li, J.-M., & Shah, A. M. (2004) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00124.2004 · Cited by 773 · see citing works
NADPH Oxidases (NOX): An Overview from Discovery, Molecular Mechanisms to Physiology and Pathology
Vermot, A., Petit-Härtlein, I., Smith, S. M. E., & Fieschi, F. (2021) · Antioxidants · doi:10.3390/antiox10060890 · Cited by 766 · see citing works
The vascular NAD(P)H oxidases as therapeutic targets in cardiovascular diseases
Cai, H., Griendling, K. K., & Harrison, D. G. (2003) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(03)00233-5 · Cited by 687 · see citing works
Self-citation
Placental oxidative stress: from miscarriage to preeclampsia
Burton, G. J., & Jauniaux, E. (2004) · Journal of the Society for Gynecologic Investigation · doi:10.1016/j.jsgi.2004.03.003 · Cited by 673 · see citing works
The Redox Code
Jones, D. P., & Sies, H. (2015) · Antioxidants & Redox Signaling · doi:10.1089/ars.2015.6247 · Cited by 647 · see citing works
Expression of a Functionally Active gp91phox-Containing Neutrophil-Type NAD(P)H Oxidase in Smooth Muscle Cells From Human Resistance Arteries: Regulation by Angiotensin II
Touyz, R. M., Chen, X., Tabet, F., Yao, G., He, G., Quinn, M. T., Pagano, P. J., & Schiffrin, E. L. (2002) · Circulation Research · doi:10.1161/01.res.0000020404.01971.2f · Cited by 590 · see citing works
Vascular inflammation and the renin-angiotensin system
Brasier, A. R., Recinos, A., & Eledrisi, M. S. (2002) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/01.atv.0000021412.56621.a2 · Cited by 586 · see citing works
Distinct Subcellular Localizations of Nox1 and Nox4 in Vascular Smooth Muscle Cells
Hilenski, L. L., Clempus, R. E., Quinn, M. T., Lambeth, J. D., & Griendling, K. K. (2004) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/01.atv.0000112024.13727.2c · Cited by 573 · see citing works
Self-citation
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
Cellular and molecular biology of aging endothelial cells
Donato, A. J., Morgan, R. G., Walker, A. E., & Lesniewski, L. A. (2015) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2015.01.021 · Cited by 538 · see citing works
New developments and novel therapeutic perspectives for vitamin C
Li, Y., & Schellhorn, H. E. (2007) · The Journal of Nutrition · doi:10.1093/jn/137.10.2171 · Cited by 508 · 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
The NADPH oxidase of professional phagocytes—prototype of the NOX electron transport chain systems
Cross, A. R., & Segal, A. W. (2004) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2004.03.008 · Cited by 489 · see citing works
Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function
Stowe, D. F., & Camara, A. K. S. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2331 · 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
T cells express a phagocyte-type NADPH oxidase that is activated after T cell receptor stimulation
Jackson, S. H., Devadas, S., Kwon, J., Pinto, L. A., & Williams, M. S. (2004) · Nature Immunology · doi:10.1038/ni1096 · Cited by 457 · see citing works
Discrete Generation of Superoxide and Hydrogen Peroxide by T Cell Receptor Stimulation
Devadas, S., Zaritskaya, L., Rhee, S. G., Oberley, L., & Williams, M. S. (2002) · The Journal of Experimental Medicine · doi:10.1084/jem.20010659 · Cited by 458 · see citing works
Mechanisms of Disease: oxidative stress and inflammation in the pathogenesis of hypertension
Vaziri, N. D., & Rodríguez-Iturbe, B. (2006) · Nature Clinical Practice Nephrology · doi:10.1038/ncpneph0283 · Cited by 442 · see citing works
Nox1 Overexpression Potentiates Angiotensin II-Induced Hypertension and Vascular Smooth Muscle Hypertrophy in Transgenic Mice
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
Self-citation
Nitric oxide, tetrahydrobiopterin, oxidative stress, and endothelial dysfunction in hypertension
Schulz, E., Jansen, T., Wenzel, P., Daiber, A., & Münzel, T. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1989 · Cited by 430 · see citing works
Pathophysiological role of oxidative stress in systolic and diastolic heart failure and its therapeutic implications
Münzel, T., Gori, T., Keaney, J. F., Maack, C., & Daiber, A. (2015) · European Heart Journal · doi:10.1093/eurheartj/ehv305 · Cited by 394 · see citing works
Hydrogen Peroxide Activates Endothelial Nitric-oxide Synthase through Coordinated Phosphorylation and Dephosphorylation via a Phosphoinositide 3-Kinase-dependent Signaling Pathway
Thomas, S. R., Chen, K., & Keaney, J. F. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109107200 · Cited by 381 · see citing works
Simultaneous detection of apoptosis and mitochondrial superoxide production in live cells by flow cytometry and confocal microscopy
Mukhopadhyay, P., Rajesh, M., Haskó, G., Hawkins, B. J., Madesh, M., & Pacher, P. (2007) · Nature Protocols · doi:10.1038/nprot.2007.327 · Cited by 373 · see citing works
Angiotensin II-Induced Production of Mitochondrial Reactive Oxygen Species: Potential Mechanisms and Relevance for Cardiovascular Disease
Dikalov, S. I., & Nazarewicz, R. R. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4604 · Cited by 356 · see citing works
Alcohol-induced hypertension: Mechanism and prevention
Husain, K., Ansari, R. A., & Ferder, L. (2014) · World Journal of Cardiology · doi:10.4330/wjc.v6.i5.245 · Cited by 345 · see citing works
Oxidative stress and dysregulation of NAD(P)H oxidase and antioxidant enzymes in diet-induced metabolic syndrome
Roberts, C. K., Barnard, R. J., Sindhu, R. K., Jurczak, M., Ehdaie, A., & Vaziri, N. D. (2006) · Metabolism · doi:10.1016/j.metabol.2006.02.022 · Cited by 322 · see citing works
Renin-angiotensin-aldosterone system and oxidative stress in cardiovascular insulin resistance
Cooper, S. A., Whaley-Connell, A., Habibi, J., Wei, Y., Lastra, G., Manrique, C., Stas, S., & Sowers, J. R. (2007) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00522.2007 · Cited by 317 · see citing works
Neuronal expression of the NADPH oxidase NOX4, and its regulation in mouse experimental brain ischemia
Vallet, P., Charnay, Y., Steger, K., Ogier-Denis, E., Kovari, E., Herrmann, F., Michel, J.-P., & Szanto, I. (2005) · Neuroscience · doi:10.1016/j.neuroscience.2004.12.038 · Cited by 291 · see citing works
Potential Role of Endotoxin as a Proinflammatory Mediator of Atherosclerosis
Stoll, L. L., Denning, G. M., & Weintraub, N. L. (2004) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/01.atv.0000147534.69062.dc · Cited by 288 · see citing works
Gut flora-dependent metabolite Trimethylamine-N-oxide accelerates endothelial cell senescence and vascular aging through oxidative stress
Ke, Y., Li, D., Zhao, M., Liu, C., Liu, J., Zeng, A., Shi, X., Cheng, S., Pan, B., Zheng, L., et al. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.01.007 · Cited by 285 · see citing works
Redox signaling across cell membranes
Fisher, A. B. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2378 · Cited by 269 · see citing works
Role of NAD(P)H Oxidase- and Mitochondria-Derived Reactive Oxygen Species in Cardioprotection of Ischemic Reperfusion Injury by Angiotensin II
Kimura, S., Zhang, G.-X., Nishiyama, A., Shokoji, T., Yao, L., Fan, Y.-Y., Rahman, M., Suzuki, T., Maeta, H., & Abe, Y. (2005) · Hypertension · doi:10.1161/01.hyp.0000163462.98381.7f · Cited by 264 · see citing works
Nox4 NADPH oxidase mediates oxidative stress and apoptosis caused by TNF-α in cerebral vascular endothelial cells
Basuroy, S., Bhattacharya, S., Leffler, C. W., & Parfenova, H. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00381.2008 · Cited by 254 · see citing works
Comparative pharmacology of chemically distinct nadph oxidase inhibitors
Wind, S., Beuerlein, K., Eucker, T., Müller, H., Scheurer, P., Armitage, M., Ho, H., Schmidt, H., & Wingler, K. (2010) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2010.00920.x · Cited by 241 · see citing works
Extracellular Superoxide Dismutase Is a Major Determinant of Nitric Oxide Bioavailability: In Vivo and Ex Vivo Evidence From ecSOD-Deficient Mice
Jung, O., Marklund, S. L., Geiger, H., Pedrazzini, T., Busse, R., & Brandes, R. P. (2003) · Circulation Research · doi:10.1161/01.res.0000092140.81594.a8 · Cited by 223 · see citing works
Endocannabinoids and cannabinoid receptors in ischaemia-reperfusion injury and preconditioning.
Pacher, P., & Haskó, G. (2008) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0707582 · Cited by 217 · see citing works
Oxidative Stress in Hypertension
de Champlain, J., Wu, R., Girouard, H., Karas, M., EL Midaoui, A., Laplante, M., & Wu, L. (2004) · Clinical and Experimental Hypertension · doi:10.1081/ceh-200031904 · Cited by 208 · see citing works
Critical Role of the NAD(P)H Oxidase Subunit p47 phox for Left Ventricular Remodeling/Dysfunction and Survival After Myocardial Infarction
Doerries, C., Grote, K., Hilfiker-Kleiner, D., Luchtefeld, M., Schaefer, A., Holland, S. M., Sorrentino, S., Manes, C., Schieffer, B., Drexler, H., et al. (2007) · Circulation Research · doi:10.1161/01.res.0000261657.76299.ff · Cited by 206 · see citing works
Antioxidative enzymes and increased oxidative stress in depressive women
Kodydková, J., Vávrová, L., Zeman, M., Jirák, R., Macášek, J., Staňková, B., Tvrzická, E., & Žák, A. (2009) · Clinical Biochemistry · doi:10.1016/j.clinbiochem.2009.06.006 · Cited by 197 · see citing works
New insights on oxidative stress in the artery wall
STOCKER, R., & KEANEY, J. F. (2005) · Journal of Thrombosis and Haemostasis · doi:10.1111/j.1538-7836.2005.01370.x · Cited by 188 · see citing works
Redefining the major contributors to superoxide production in contracting skeletal muscle. The role of NAD(P)H oxidases
Sakellariou, G. K., Jackson, M. J., & Vasilaki, A. (2014) · Free Radical Research · doi:10.3109/10715762.2013.830718 · Cited by 184 · see citing works
Oxidative Stress and Endothelial Dysfunction in Aortas of Aged Spontaneously Hypertensive Rats by NOX1/2 Is Reversed by NADPH Oxidase Inhibition
Wind, S., Beuerlein, K., Armitage, M. E., Taye, A., Kumar, A. H. S., Janowitz, D., Neff, C., Shah, A. M., Wingler, K., & Schmidt, H. H. H. W. (2010) · Hypertension · doi:10.1161/hypertensionaha.109.149187 · Cited by 181 · see citing works
Hypoxia-inducible Factor-1 Activation in Nonhypoxic Conditions: The Essential Role of Mitochondrial-derived Reactive Oxygen Species
Patten, D. A., Lafleur, V. N., Robitaille, G. A., Chan, D. A., Giaccia, A. J., & Richard, D. E. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-01-0025 · Cited by 171 · see citing works
Effects of HMG-CoA Reductase Inhibitors on Endothelial Function: Role of Microdomains and Oxidative Stress
Mason, R. P., Walter, M. F., & Jacob, R. F. (2004) · Circulation · doi:10.1161/01.cir.0000129503.62747.03 · Cited by 175 · see citing works
Dermal wound healing properties of redox-active grape seed proanthocyanidins
Khanna, S., Venojarvi, M., Roy, S., Sharma, N., Trikha, P., Bagchi, D., Bagchi, M., & Sen, C. K. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00999-1 · Cited by 173 · see citing works
Atherosclerosis Is Attenuated by Limiting Superoxide Generation in Both Macrophages and Vessel Wall Cells
Vendrov, A. E., Hakim, Z. S., Madamanchi, N. R., Rojas, M., Madamanchi, C., & Runge, M. S. (2007) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/atvbaha.107.152629 · Cited by 173 · see citing works
The Signaling Pathways Involved in Chondrocyte Differentiation and Hypertrophic Differentiation
Li, J., & Dong, S. (2016) · Stem Cells International · doi:10.1155/2016/2470351 · Cited by 170 · see citing works
Receptor Activation of NADPH Oxidases
Petry, A., Weitnauer, M., & Görlach, A. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.3026 · Cited by 162 · see citing works
Endothelial Nox2 Overexpression Potentiates Vascular Oxidative Stress and Hemodynamic Response to Angiotensin II: Studies in Endothelial-Targeted Nox2 Transgenic Mice
Bendall, J. K., Rinze, R., Adlam, D., Tatham, A. L., de Bono, J., & Channon, K. M. (2007) · Circulation Research · doi:10.1161/01.res.0000263381.83835.7b · Cited by 157 · see citing works
Increased NADPH-Oxidase Activity and Nox4 Expression During Chronic Hypertension Is Associated With Enhanced Cerebral Vasodilatation to NADPH In Vivo
Paravicini, T. M., Chrissobolis, S., Drummond, G. R., & Sobey, C. G. (2004) · Stroke · doi:10.1161/01.str.0000112974.37028.58 · Cited by 156 · see citing works
Hemorrhagic Shock Activation of NLRP3 Inflammasome in Lung Endothelial Cells
Xiang, M., Shi, X., Li, Y., Xu, J., Yin, L., Xiao, G., Scott, M. J., Billiar, T. R., Wilson, M. A., & Fan, J. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1102093 · Cited by 155 · see citing works
Sodium nitrite downregulates vascular NADPH oxidase and exerts antihypertensive effects in hypertension
Montenegro, M. F., Amaral, J. H., Pinheiro, L. C., Sakamoto, E. K., Ferreira, G. C., Reis, R. I., Marçal, D. M. O., Pereira, R. P., & Tanus-Santos, J. E. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.04.005 · Cited by 152 · see citing works
Small Concentrations of oxLDL Induce Capillary Tube Formation From Endothelial Cells via LOX-1–Dependent Redox-Sensitive Pathway
Dandapat, A., Hu, C., Sun, L., & Mehta, J. L. (2007) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/atvbaha.107.152272 · Cited by 148 · see citing works
NADPH Oxidases and Mitochondria in Vascular Senescence
Salazar, G. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19051327 · Cited by 133 · see citing works
Kaempferol Modulates Pro-Inflammatory NF-ΚB Activation by Suppressing Advanced Glycation Endproducts-Induced NADPH Oxidase
Kim, J. M., Lee, E. K., Kim, D. H., Yu, B. P., & Chung, H. Y. (2010) · AGE · doi:10.1007/s11357-009-9124-1 · Cited by 133 · see citing works
Hypoxia and Reoxygenation Induce Endothelial Nitric Oxide Synthase Uncoupling in Endothelial Cells through Tetrahydrobiopterin Depletion and S-Glutathionylation
De Pascali, F., Hemann, C., Samons, K., Chen, C.-A., & Zweier, J. L. (2014) · Biochemistry · doi:10.1021/bi500076r · Cited by 131 · see citing works
Aryl Hydrocarbon Receptor in Oxidative Stress as a Double Agent and Its Biological and Therapeutic Significance
Grishanova, A. Y., & Perepechaeva, M. L. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23126719 · Cited by 130 · see citing works
Phagocytic NADPH Oxidase Overactivity Underlies Oxidative Stress in Metabolic Syndrome
Fortuño, A., San José, G., Moreno, M. U., Beloqui, O., Díez, J., & Zalba, G. (2006) · Diabetes · doi:10.2337/diabetes.55.01.06.db05-0751 · Cited by 128 · see citing works
Mechanisms of Sudden Cardiac Death: Oxidants and Metabolism
Yang, K.-C., Kyle, J. W., Makielski, J. C., & Dudley, S. C. (2015) · Circulation Research · doi:10.1161/circresaha.116.304691 · Cited by 127 · see citing works
Differential effects of diabetes on the expression of the gp91phox homologues nox1 and nox4
Wendt, M. C., Daiber, A., Kleschyov, A. L., Mülsch, A., Sydow, K., Schulz, E., Chen, K., Keaney, J. F., Lassègue, B., Walter, U., et al. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.03.020 · Cited by 122 · see citing works
Self-citation
Mechanisms of Lipoapoptosis
Listenberger, L. L., & Schaffer, J. E. (2002) · Trends in Cardiovascular Medicine · doi:10.1016/s1050-1738(02)00152-4 · Cited by 123 · see citing works
Attenuation of brain damage and cognitive impairment by direct renin inhibition in mice with chronic cerebral hypoperfusion
Dong, Y.-F., Kataoka, K., Toyama, K., Sueta, D., Koibuchi, N., Yamamoto, E., Yata, K., Tomimoto, H., Ogawa, H., & Kim-Mitsuyama, S. (2011) · Hypertension · doi:10.1161/hypertensionaha.111.173534 · Cited by 109 · see citing works
Aging of the Nitric Oxide System: Are We as Old as Our NO?
Sverdlov, A. L., Ngo, D. T. M., Chan, W. P. A., Chirkov, Y. Y., & Horowitz, J. D. (2014) · Journal of the American Heart Association · doi:10.1161/jaha.114.000973 · Cited by 97 · see citing works
Endothelial Dysfunction in the Microcirculation of Patients with Obstructive Sleep Apnea
Patt, B. T., Jarjoura, D., Haddad, D. N., Sen, C. K., Roy, S., Flavahan, N. A., & Khayat, R. N. (2010) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201002-0162oc · Cited by 101 · see citing works
NADPH Oxidase Is Involved in Prostaglandin F2α-induced Hypertrophy of Vascular Smooth Muscle Cells
Katsuyama, M., Fan, C., & Yabe-Nishimura, C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111634200 · Cited by 95 · see citing works
Redox implications in adipose tissue (dys)function-A new look at old acquaintances
Jankovic, A., Korac, A., Buzadzic, B., Otasevic, V., Stancic, A., Daiber, A., & Korac, B. (2015) · Redox Biology · doi:10.1016/j.redox.2015.06.018 · Cited by 91 · see citing works
Role of reactive oxygen species in IL-1β-stimulated sustained ERK activation and MMP-9 induction
Gurjar, M. V., Deleon, J., Sharma, R. V., & Bhalla, R. C. (2001) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.2001.281.6.h2568 · Cited by 90 · see citing works
Increased levels of oxidative stress, subclinical inflammation, and myocardial fibrosis markers in primary aldosteronism patients
Stehr, C. B., Mellado, R., Ocaranza, M. P., Carvajal, C. A., Mosso, L., Becerra, E., Solis, M., García, L., Lavandero, S., Jalil, J., et al. (2010) · Journal of Hypertension · doi:10.1097/hjh.0b013e32833d0177 · Cited by 88 · see citing works
Novel Role of Protein Disulfide Isomerase in the Regulation of NADPH Oxidase Activity: Pathophysiological Implications in Vascular Diseases
Laurindo, F. R. M., Fernandes, D. C., Amanso, A. M., Lopes, L. R., & Santos, C. X. C. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.2011 · Cited by 87 · see citing works
Oxidative Stress and Obesity: The Chicken or the Egg?
Aroor, A. R., & DeMarco, V. G. (2014) · Diabetes · doi:10.2337/db14-0424 · Cited by 85 · see citing works
Inhibition of central angiotensin II enhances memory function and reduces oxidative stress status in rat hippocampus
Bild, W., Hritcu, L., Stefanescu, C., & Ciobica, A. (2013) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2012.12.009 · Cited by 83 · see citing works
Calcium, mitochondria and oxygen sensing in the pulmonary circulation
Ward, J. P. T., Snetkov, V. A., & Aaronson, P. I. (2004) · Cell Calcium · doi:10.1016/j.ceca.2004.02.017 · Cited by 45 · see citing works
Autocrine/paracrine pattern of superoxide production through NAD(P)H oxidase in coronary arterial myocytes
Zhang, G., Zhang, F., Muh, R., Yi, F., Chalupsky, K., Cai, H., & Li, P.-L. (2007) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00632.2006 · Cited by 42 · see citing works
Hydrogen peroxide restrains endothelium-derived nitric oxide bioactivity—Role for iron-dependent oxidative stress
Thomas, S. R., Schulz, E., & Keaney, J. F. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.05.012 · Cited by 37 · see citing works
Upregulation of Intermediate-Conductance Ca2+-Activated K+ Channels (KCNN4) in Porcine Coronary Smooth Muscle Requires NADPH Oxidase 5 (NOX5)
Gole, H. K. A., Tharp, D. L., & Bowles, D. K. (2014) · PLoS ONE · doi:10.1371/journal.pone.0105337 · Cited by 36 · see citing works
Targeting NADPH-oxidase by reactive oxygen species reveals an initial sensitive step in the assembly process
Ostuni, M. A., Gelinotte, M., Bizouarn, T., Baciou, L., & Houée-Levin, C. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.06.021 · Cited by 32 · see citing works
Resveratrol recruits rat muscle microvasculature via a nitric oxide-dependent mechanism that is blocked by TNFα
Wang, N., Ko, S.-H., Chai, W., Li, G., Barrett, E. J., Tao, L., Cao, W., & Liu, Z. (2011) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00414.2010 · Cited by 28 · see citing works
Hsp22 Overexpression Induces Myocardial Hypertrophy, Senescence and Reduced Life Span through Enhanced Oxidative Stress
Morin, D., Long, R., Panel, M., Laure, L., Taranu, A., Gueguen, C., Pons, S., Leoni, V., Caccia, C., Vatner, S. F., et al. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.04.035 · Cited by 24 · see citing works

Regulation of Superoxide Anion Production by NADPH Oxidase in Monocytes/Macrophages
Cathcart, M. K. (2003) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000097769.47306.12 · Cited by 365 · see citing works
Hv1 proton channels are required for high-level NADPH oxidase-dependent superoxide production during the phagocyte respiratory burst
Ramsey, I. S., Ruchti, E., Kaczmarek, J. S., & Clapham, D. E. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0902761106 · Cited by 255 · see citing works
Homocysteine stimulates NADPH oxidase-mediated superoxide production leading to endothelial dysfunction in rats
Edirimanne, V. E. R., Woo, C. W., Siow, Y. L., Pierce, G. N., Xie, J., & Karmin, O. (2007) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y07-112 · Cited by 82 · see citing works
NADPH-Induced Contractions of Mouse Aorta Do Not Involve NADPH Oxidase: A Role for P2X Receptors
Judkins, C. P., Sobey, C. G., Dang, T. T., Miller, A. A., Dusting, G. J., & Drummond, G. R. (2006) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.105.096610 · Cited by 24 · see citing works
Homocysteine stimulates phosphorylation of NADPH oxidase p47phoxand p67phoxsubunits in monocytes via protein kinase Cβ activation
Siow, Y. L., Au-Yeung, K. K. W., Woo, C. W., & Karmin, O. (2006) · Biochemical Journal · doi:10.1042/bj20051810 · Cited by 95 · see citing works

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
Publisher: Ovid Technologies (Wolters Kluwer Health)
Published: 2000-03-17
Volume: 86
Issue: 5
Pages: 494-501
ISSN: 0009-7330 (ISSN-L)
1524-4571
DOI: 10.1161/01.res.86.5.494
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 › 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

NAD(P)H Oxidase: Role in Cardiovascular Biology and Disease

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks