NOX signaling in molecular cardiovascular mechanisms involved in the blood pressure homeostasis

Copper-Zinc Superoxide Dismutase (SOD1) Is Released by Microglial Cells and Confers Neuroprotection against 6-OHDA Neurotoxicity

Polazzi, E., Mengoni, I., Caprini, M., Peña‐Altamira, E., Kurtys, E., & Monti, B. (2012) · Neurosignals · doi:10.1159/000337115 · Cited by 9,023 · see citing works

Apparent hydroxyl radical production by peroxynitrite: Implications for endothelial injury from nitric oxide and superoxide

Beckman, J. S., Beckman, T. W., Chen, J., Marshall, P. A., & Freeman, B. A. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.4.1620 · Cited by 7,029 · 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

ROS function in redox signaling and oxidative stress

Schieber, M., & Chandel, N. S. (2014) · Current Biology · doi:10.1016/j.cub.2014.03.034 · Cited by 6,931 · see citing works

Journal of Biological Chemistry

Kurkinensp, M., CondongT, M. R., Blumberg, B., Barlow, D. P., Quiñones, S., Sausg, J., & Pihlajaniemisyy, T. (2021) · Journal of Biological Chemistry · doi:10.1074/jbc · Cited by 3,409 · see citing works

NOX enzymes and the biology of reactive oxygen

Lambeth, J. D. (2004) · Nature Reviews Immunology · doi:10.1038/nri1312 · Cited by 3,125 · 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

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

Oxidation of tetrahydrobiopterin leads to uncoupling of endothelial cell nitric oxide synthase in hypertension

Landmesser, U., Dikalov, S., Price, S. R., McCann, L. A., Fukai, T., Holland, S. M., Mitch, W. E., & Harrison, D. G. (2003) · Journal of Clinical Investigation · doi:10.1172/jci14172 · Cited by 1,652 · see citing works

Autocrine release of angiotensin II mediates stretch-induced hypertrophy of cardiac myocytes in vitro

Sadoshima, J.-I., Xu, Y., Slayter, H. S., & Izumo, S. (1993) · Cell · doi:10.1016/0092-8674(93)90541-w · Cited by 1,348 · see citing works

Oxidative stress: From basic research to clinical application

Sies, H. (1991) · The American Journal of Medicine · doi:10.1016/0002-9343(91)90281-2 · Cited by 1,332 · see citing works

Vascular NAD(P)H oxidases: specific features, expression, and regulation

Lassegue, B. P., & Clempus, R. E. (2003) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00758.2002 · Cited by 1,016 · see citing works

Signal Transduction Mechanisms Mediating the Physiological and Pathophysiological Actions of Angiotensin II in Vascular Smooth Muscle Cells

Touyz, R. M., & Schiffrin, E. L. (2000) · Pharmacological Reviews · doi:10.1016/s0031-6997(24)01471-6 · Cited by 933 · see citing works

The Neutrophil NADPH Oxidase

BABIOR, B. M., Lambeth, J. D., & Nauseef, W. M. (2002) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2642 · Cited by 911 · 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

Nox proteins in signal transduction

Brown, D. I., & Griendling, K. (2009) · Free Radical Biology & Medicine · doi:10.1016/j.freeradbiomed.2009.07.023 · Cited by 841 · see citing works

Functional analysis of Nox4 reveals unique characteristics compared to other NADPH oxidases

Martyn, K. D., Frederick, L. M., von Loehneysen, K., Dinauer, M. C., & Knaus, U. G. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2005.03.023 · Cited by 783 · see citing works

Biochemistry, Physiology, and Pathophysiology of NADPH Oxidases in the Cardiovascular System

Lassegue, B. P., Martín, A. S., & Griendling, K. K. (2012) · Circulation Research · doi:10.1161/circresaha.111.243972 · Cited by 768 · 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

Regulation of Phagocyte Oxygen Radical Production by the GTP-Binding Protein Rac 2

Knaus, U. G., Heyworth, P. G., Evans, T., Curnutte, J. T., & Bokoch, G. (1991) · Science · doi:10.1126/science.1660188 · Cited by 673 · see citing works

Cloning of Two Human Thyroid cDNAs Encoding New Members of the NADPH Oxidase Family

Deken, X. D., Wang, D., Many, M., Costagliola, S., Libert, F., Vassart, G., Dumont, J. E., & Miot, F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000916200 · Cited by 639 · see citing works

Nox4 Is a Protective Reactive Oxygen Species Generating Vascular NADPH Oxidase

Schröder, K., Zhang, M., Benkhoff, S., Mieth, A., Pliquett, R., Kosowski, J., Kruse, C., Luedike, P., Michaelis, U. R., Weissmann, N., et al. (2012) · Circulation Research · doi:10.1161/circresaha.112.267054 · Cited by 622 · see citing works

A gp91phox Containing NADPH Oxidase Selectively Expressed in Endothelial Cells Is a Major Source of Oxygen Radical Generation in the Arterial Wall

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 3× · see citing works

Stimulatory Autoantibodies to the PDGF Receptor in Systemic Sclerosis

Svegliati, S., Santillo, M., Bevilacqua, F., Luchetti, M. M., Spadoni, T., Mancini, M., Fraticelli, P., Sambo, P., Funaro, A., Kazlauskas, A., et al. (2006) · New England Journal of Medicine · doi:10.1056/nejmoa052955 · Cited by 581 · see citing works

Endothelin-1 is an autocrine/paracrine factor in the mechanism of angiotensin II-induced hypertrophy in cultured rat cardiomyocytes.

Ito, H., Hirata, Y., Adachi, S., Tanaka, M., Tsujino, M., Koike, A., Nogami, A., Murumo, F., & Hiroe, M. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116579 · Cited by 574 · 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

Role of p47 phox in Vascular Oxidative Stress and Hypertension Caused by Angiotensin II

Landmesser, U., Cai, H. “., Dikalov, S., McCann, L. A., Hwang, J., Jo, H., Holland, S. M., & Harrison, D. G. (2002) · Hypertension · doi:10.1161/01.hyp.0000032100.23772.98 · Cited by 572 · see citing works

X-ROS Signaling: Rapid Mechano-Chemo Transduction in Heart

Prosser, B. L., Ward, C. W., & Lederer, W. J. (2011) · Science · doi:10.1126/science.1202768 · Cited by 564 · see citing works

Angiotensin II, NADPH Oxidase, and Redox Signaling in the Vasculature

Cat, A. N. D., Montezano, A. C. I., Burger, D. E., & Touyz, R. M. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4641 · Cited by 469 · see citing works

Role of xanthine oxidoreductase and NAD(P)H oxidase in endothelial superoxide production in response to oscillatory shear stress

McNally, J. S., Davis, M. E., Giddens, D. P., Saha, A., Hwang, J., Dikalov, S., Jo, H., & Harrison, D. G. (2003) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00515.2003 · Cited by 461 · see citing works

NADPH oxidase-4 mediates protection against chronic load-induced stress in mouse hearts by enhancing angiogenesis

Zhang, M., Brewer, A. C., Schröder, K., Santos, C. X. C., Grieve, D., Wang, M., Anilkumar, N. P., Yu, B., Dong, X., Walker, S. J., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009700107 · Cited by 447 · 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

Contrasting Roles of NADPH Oxidase Isoforms in Pressure-Overload Versus Angiotensin II–Induced Cardiac Hypertrophy

Byrne, J., Grieve, D., Bendall, J. K., Li, J., Gove, C. D., Lambeth, J. D., Cave, A. C., & Shah, A. M. (2003) · Circulation Research · doi:10.1161/01.res.0000099504.30207.f5 · Cited by 411 · see citing works

The glycoprotein encoded by the X-linked chronic granulomatous disease locus is a component of the neutrophil cytochrome b complex

Dinauer, M. C., Orkin, S. H., Brown, R., Jesaitis, A. J., & Parkos, C. A. (1987) · Nature · doi:10.1038/327717a0 · Cited by 407 · see citing works

Angiotensin II and Vascular Injury

Montezano, A. C. I., Cat, A. N. D., Rios, F. J. O., & Touyz, R. M. (2014) · Current Hypertension Reports · doi:10.1007/s11906-014-0431-2 · Cited by 404 · see citing works

Intracellular Localization and Preassembly of the NADPH Oxidase Complex in Cultured Endothelial Cells

Li, J., & Shah, A. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110073200 · Cited by 395 · see citing works

Novel cytochrome b system in phagocytic vacuoles of human granulocytes

Segal, A. W., & Jones, O. T. G. (1978) · Nature · doi:10.1038/276515a0 · Cited by 357 · see citing works

Role of NADPH Oxidase in the Vascular Hypertrophic and Oxidative Stress Response to Angiotensin II in Mice

Wang, H. D., Xu, S., Johns, D. G., Du, Y., Quinn, M. T., Cayatte, A. J., & Cohen, R. A. (2001) · Circulation Research · doi:10.1161/hh0901.089987 · Cited by 342 · see citing works

Comparative Effect of ACE Inhibition and Angiotensin II Type 1 Receptor Antagonism on Bioavailability of Nitric Oxide in Patients With Coronary Artery Disease

Hornig, B., Landmesser, U., Kohler, C., Ahlersmann, D., Spiekermann, S., Christoph, A., Tatge, H., & Drexler, H. (2001) · Circulation · doi:10.1161/01.cir.103.6.799 · Cited by 341 · see citing works

Heart Physiology: From Cell to Circulation

Opie, L. H. (1998) · Cited by 339 · see citing works

Endothelial Nox4 NADPH Oxidase Enhances Vasodilatation and Reduces Blood Pressure In Vivo

Ray, R., Murdoch, C. E., Wang, M., Santos, C. X. C., Zhang, M., Alom-Ruiz, S. P., Anilkumar, N. P., Ouattara, A., Cave, A. C., Walker, S. J., et al. (2011) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.110.219238 · Cited by 325 · see citing works

Investigation Into the Sources of Superoxide in Human Blood Vessels

Berry, C., Hamilton, C., Brosnan, M. J., Magill, F. G., Berg, G. A., McMurray, J. J. V., & Dominiczak, A. F. (2000) · Circulation · doi:10.1161/01.cir.101.18.2206 · Cited by 305 · see citing works

Role of NAD(P)H oxidase on vascular alterations in angiotensin II-infused mice

Virdis, A., Neves, M. F., Amiri, F., Touyz, R. M., & Schiffrin, E. L. (2004) · Journal of Hypertension · doi:10.1097/00004872-200403000-00016 · Cited by 244 · see citing works

Redox Signaling, Vascular Function, and Hypertension

Lee, M. Y., & Griendling, K. K. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1986 · Cited by 241 · see citing works

Differential regulation of dual NADPH oxidases/peroxidases, Duox1 and Duox2, by Th1 and Th2 cytokines in respiratory tract epithelium

Harper, R. W., Xu, C., Eiserich, J. P., Chen, Y., Kao, C., Thai, P., Setiadi, H., & Wu, R. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.08.002 · Cited by 231 · see citing works

Dual oxidase in mucosal immunity and host–microbe homeostasis

Bae, Y. S., Choi, M. K., & Lee, W. (2010) · Trends in Immunology · doi:10.1016/j.it.2010.05.003 · Cited by 213 · see citing works

NADPH oxidases in lung biology and pathology: Host defense enzymes, and more

van der Vliet, A. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.11.016 · Cited by 201 · see citing works

Hydrogen Peroxide, an Endogenous Endothelium-Derived Hyperpolarizing Factor, Plays an Important Role in Coronary Autoregulation In Vivo

Yada, T., Shimokawa, H., Hiramatsu, O., Kajita, T., Shigeto, F., Goto, M., Ogasawara, Y., & Kajiya, F. (2003) · Circulation · doi:10.1161/01.cir.0000050145.25589.65 · Cited by 188 · see citing works

NADPH oxidases in cardiovascular disease: insights from in vivo models and clinical studies

Sirker, A. A., Zhang, M., & Shah, A. M. (2011) · Basic Research in Cardiology · doi:10.1007/s00395-011-0190-z · Cited by 180 · see citing works

Upregulation of nox1 in vascular smooth muscle leads to impaired endothelium-dependent relaxation via enos uncoupling

Dikalova, A. E., Góngora, M. C., Harrison, D. G., Lambeth, J. D., Dikalov, S., & Griendling, K. K. (2010) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00242.2010 · Cited by 179 · see citing works

Platelet-derived Growth Factor and Reactive Oxygen Species (ROS) Regulate Ras Protein Levels in Primary Human Fibroblasts via ERK1/2

Svegliati, S., Cancello, R., Sambo, P., Luchetti, M. M., Paroncini, P., Orlandini, G., Discepoli, G., Paternò, R., Santillo, M., Cuozzo, C., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502851200 · Cited by 173 · see citing works

Effect of the Angiotensin II Type 1 Receptor Blocker Candesartan on Endothelial Function in Patients With Essential Hypertension

Ghiadoni, L., Virdis, A., Magagna, A., Taddei, S., & Salvetti, A. (2000) · Hypertension · doi:10.1161/01.hyp.35.1.501 · Cited by 171 · see citing works

Nox5 mediates PDGF-induced proliferation in human aortic smooth muscle cells

Jay, D. B., Papaharalambus, C. A., Seidel-Rogol, B., Dikalova, A. E., Lassègue, B., & Griendling, K. K. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.04.024 · Cited by 166 · see citing works

Regulation of cell proliferation by NADPH oxidase-mediated signaling: Potential roles in tissue repair, regenerative medicine and tissue engineering

Chan, E. C., Jiang, F., Peshavariya, H., & Dusting, G. J. (2009) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2009.02.005 · Cited by 162 · 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

p47phox Associates With the Cytoskeleton Through Cortactin in Human Vascular Smooth Muscle Cells

Touyz, R. M., Yao, G., Quinn, M. T., Pagano, P. J., & Schiffrin, E. L. (2004) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000154141.66879.98 · Cited by 154 · see citing works

Role of endothelial Nox2 NADPH oxidase in angiotensin II-induced hypertension and vasomotor dysfunction

Murdoch, C. E., Alom-Ruiz, S. P., Wang, M., Zhang, M., Walker, S., Yu, B., Brewer, A. C., & Shah, A. M. (2011) · Basic Research in Cardiology · doi:10.1007/s00395-011-0179-7 · Cited by 152 · see citing works

The Nox Family of NADPH Oxidases: Friend or Foe of the Vascular System?

Takac, I., Schröder, K., & Brandes, R. P. (2011) · Current Hypertension Reports · doi:10.1007/s11906-011-0238-3 · Cited by 142 · see citing works

Nox2 B-loop peptide, Nox2ds, specifically inhibits the NADPH oxidase Nox2

Csányi, G., Cifuentes-Pagano, E., Al Ghouleh, I., Ranayhossaini, D. J., Egaña, L., Lopes, L. R., Jackson, H. M., Kelley, E. E., & Pagano, P. J. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.04.025 · Cited by 131 · see citing works

Dual oxidases

Donkó, Á., Péterfi, Z., Sum, A., Leto, T. L., & Geiszt, M. (2005) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2005.1767 · Cited by 131 · see citing works

Detection of superoxide anion released extracellularly by endothelial cells using cytochrome c reduction, ESR, fluorescence and lucigenin-enhanced chemiluminescence techniques

Barbacanne, M.-A., Souchard, J., Darblade, B., Iliou, J., Nepveu, F., Pipy, B., Bayard, F., & Arnal, J. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00336-1 · Cited by 121 · see citing works

Role of oxidants on calcium and sodium movement in healthy and diseased cardiac myocytes

Sag, C. M., Wagner, S., & Maier, L. S. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.05.035 · Cited by 107 · see citing works

Paradoxical Activation of Endothelial Nitric Oxide Synthase by NADPH Oxidase

Zhang, Q., Malik, P., Pandey, D., Gupta, S. A., Jagnandan, D., de Chantemèle, E. J. B., Bánfi, B., Marrero, M. B., Rudic, R. D., Stepp, D. W., et al. (2008) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.108.168278 · Cited by 107 · see citing works

A crosstalk between chromatin remodeling and histone H3K4 methyltransferase complexes in endothelial cells regulates angiotensin II-induced cardiac hypertrophy

Weng, X., Yu, L., Liang, P., Li, L., Dai, X. J., Zhou, B., Wu, X., Xu, H., Fang, M., Chen, Q., et al. (2015) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2015.02.010 · Cited by 93 · see citing works

Protection of Human Endothelial Cells From Oxidative Stress

Cuda, G., Paternò, R., Ceravolo, R., Candigliota, M., Perrotti, N., Perticone, F., Faniello, M. C., Schepis, F., Ruocco, A., Mele, E., et al. (2002) · Circulation · doi:10.1161/hc0802.104324 · Cited by 92 · see citing works

NADPH Oxidase-Mediated Oxidative Stress: Genetic Studies of the p22 phox Gene in Hypertension

Zalba, G., José, G. S., Moreno, M. U., Fortuño, A., & Dı́ez, J. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.1327 · Cited by 85 · see citing works

Reactive oxygen species-mediated regulation of the Na+–H+ exchanger 1 gene expression connects intracellular redox status with cells' sensitivity to death triggers

Akram, S., Teong, H. F. C., Fliegel, L., Pervaiz, S., & Clément, M.-V. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401775 · Cited by 85 · see citing works

Selective Recapitulation of Conserved and Nonconserved Regions of Putative NOXA1 Protein Activation Domain Confers Isoform-specific Inhibition of Nox1 Oxidase and Attenuation of Endothelial Cell Migration

Ranayhossaini, D., Rodriguez, A. I., Sahoo, S., Chen, B. B., Mallampalli, R. K., Kelley, E. E., Csányi, G., Gladwin, M. T., Romero, G. G., & Pagano, P. J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.521344 · Cited by 82 · see citing works

Vascular smooth muscle cell NAD(P)H oxidase activity during the development of hypertension: Effect of angiotensin II and role of insulinlike growth factor-1 receptor transactivation

Cruzado, M., Risler, N., Miatello, R. M., Yao, G., Schiffrin, E. L., & Touyz, R. M. (2005) · American Journal of Hypertension · doi:10.1016/j.amjhyper.2004.09.001 · Cited by 81 · see citing works

Epidermal growth factor receptor transactivation by endogenous vasoactive peptides contributes to hyperproliferation of vascular smooth muscle cells of SHR

Li, Y., Lévesque, L.-O., & Anand‐Srivastava, M. B. (2010) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00526.2010 · Cited by 71 · see citing works

Oxidative stress and the pathogenesis of scleroderma: the Murrell’s hypothesis revisited

Gabrielli, A., Svegliati, S., Moroncini, G., Pomponio, G., Santillo, M., & Avvedimento, E. V. (2008) · Seminars in Immunopathology · doi:10.1007/s00281-008-0125-4 · Cited by 69 · see citing works

X-ROS signalling is enhanced and graded by cyclic cardiomyocyte stretch

Prosser, B. L., Ward, C. W., & Lederer, W. J. (2013) · Cardiovascular Research · doi:10.1093/cvr/cvt066 · Cited by 68 · see citing works

Physiology and Pathophysiology of the DUOXes

Ris‐Stalpers, C. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1563 · Cited by 67 · see citing works

Early and Late Events Induced by PolyQ-expanded Proteins

Bertoni, A., Giuliano, P., Galgani, M., Rotoli, D., Ulianich, L., Adornetto, A., Santillo, M. R., Porcellini, A., & Avvedimento, V. E. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.156521 · Cited by 66 · see citing works

NADPH Oxidase and the Cardiovascular Toxicity Associated with Smoking

Kim, M., Han, C.-H., & Lee, M. (2014) · Toxicological Research · doi:10.5487/tr.2014.30.3.149 · Cited by 65 · see citing works

Opposing functions of Ki- and Ha-Ras genes in the regulation of redox signals

Santillo, M., Mondola, P., Serù, R., Annella, T., Cassano, S., Ciullo, I., Tecce, M. F., Iacomino, G., Damiano, S., Cuda, G., et al. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00159-2 · Cited by 62 · see citing works

Inhibition of Ras/ERK1/2 signaling protects against postischemic renal injury

Sabbatini, M., Santillo, M., Pisani, A., Paternò, R., Uccello, F., Serù, R., Matrone, G., Spagnuolo, G., Andreucci, M., Serio, V., et al. (2006) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00304.2005 · Cited by 56 · see citing works

NADPH Oxidase 4 Regulates Cardiomyocyte Differentiation via Redox Activation of c-Jun Protein and the cis-Regulation of GATA-4 Gene Transcription

Murray, T. V., Smyrnias, I., Shah, A. M., & Brewer, A. C. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.439844 · Cited by 53 · see citing works

Blood pressure regulation XI: overview and future research directions

Raven, P. B., & Chapleau, M. W. (2014) · European Journal of Applied Physiology · doi:10.1007/s00421-014-2823-z · Cited by 47 · see citing works

HaRas activates the NADPH oxidase complex in human neuroblastoma cells via extracellular signal‐regulated kinase 1/2 pathway

Serù, R., Mondola, P., Damiano, S., Svegliati, S., Agnese, S., Avvedimento, E. V., & Santillo, M. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02754.x · Cited by 46 · see citing works

T cell activation induces CuZn superoxide dismutase (SOD)-1 intracellular re-localization, production and secretion

Terrazzano, G., Rubino, V., Damiano, S., Sasso, A., Petrozziello, T., Ucci, V., Palatucci, A. T., Giovazzino, A., Santillo, M., Felice, B. D., et al. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.10.020 · Cited by 39 · see citing works

Reactive Oxygen Species Regulate the Levels of Dual Oxidase (Duox1-2) in Human Neuroblastoma Cells

Damiano, S., Fusco, R., Morano, A., Mizio, M. D., Paternò, R., Rosa, A. D., Spinelli, R., Amente, S., Frunzio, R., Mondola, P., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0034405 · Cited by 39 · see citing works

Cu,Zn superoxide dismutase increases intracellular calcium levels via a phospholipase C–protein kinase C pathway in SK-N-BE neuroblastoma cells

Mondola, P., Santillo, M., Serù, R., Damiano, S., Alvino, C. G., Ruggiero, G., Formisano, P., Terrazzano, G., Secondo, A., & Annunziato, L. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.09.131 · Cited by 35 · see citing works

Reactive Oxygen Species, Ki-Ras, and Mitochondrial Superoxide Dismutase Cooperate in Nerve Growth Factor-induced Differentiation of PC12 Cells

Cassano, S., Agnese, S., D'Amato, V., Papale, M., Garbi, C., Castagnola, P., Ruocco, M. R., Castellano, I., Vendittis, E. D., Santillo, M., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.098525 · Cited by 33 · see citing works

Pulmonary Endothelial Cell NOX

Damico, R. L., Zulueta, J. J., & Hassoun, P. M. (2012) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2010-0331rt · Cited by 33 · see citing works

Dual oxidase 2 generated reactive oxygen species selectively mediate the induction of mucins by epidermal growth factor in enterocytes

Damiano, S., Morano, A., Ucci, V., Accetta, R., Mondola, P., Paternò, R., Avvedimento, V. E., & Santillo, M. (2015) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2014.12.014 · Cited by 29 · see citing works

Cu–Zn superoxide dismutase activates muscarinic acetylcholine M1 receptor pathway in neuroblastoma cells

Damiano, S., Petrozziello, T., Ucci, V., Amente, S., Santillo, M., & Mondola, P. (2012) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2012.11.001 · Cited by 29 · see citing works

Cigarette Smoke Condensate Causes a Decrease of the Gene Expression of Cu–Zn Superoxide Dismutase, Mn Superoxide Dismutase, Glutathione Peroxidase, Catalase, and Free Radical-Induced Cell Injury in SH-SY5Y Human Neuroblastoma Cells

Russo, M., Cocco, S., Secondo, A., Adornetto, A., Bassi, A., Nunziata, A., Polichetti, G., Felice, B. D., Damiano, S., Serù, R., et al. (2009) · Neurotoxicity Research · doi:10.1007/s12640-009-9138-6 · Cited by 28 · see citing works

Evidence of calcium‐ and SNARE‐dependent release of CuZn superoxide dismutase from rat pituitary GH3 cells and synaptosomes in response to depolarization

Santillo, M., Secondo, A., Serù, R., Damiano, S., Garbi, C., Taverna, E., Rosa, P., Giovedı̀, S., Benfenati, F., & Mondola, P. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04538.x · Cited by 27 · see citing works

Signal Transduction Mechanisms

(1994) · The Journal of Physiology · doi:10.1113/jphysiol.1994.sp020216 · Cited by 24 · see citing works

Farnesyl transferase inhibitors induce neuroprotection by inhibiting Ha‐Ras signalling pathway

Ruocco, A., Santillo, M., Cicale, M., Serù, R., Cuda, G., Anrather, J., Iadecola, C., Postiglione, A., Avvedimento, E. V., & Paternò, R. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2007.05935.x · Cited by 24 · see citing works

Regulation of Angiotensin II receptor signaling by cysteine modification of NF-κB

Nishida, M., Kitajima, N., Saiki, S., Nakaya, M., & Kurose, H. (2010) · Nitric Oxide · doi:10.1016/j.niox.2010.10.003 · Cited by 24 · see citing works

Blood pressure regulation

Wilson, F. (1981) · Springer eBooks · doi:10.1007/978-94-011-6241-8_14 · Cited by 18 · see citing works

The Cu–Zn superoxide dismutase (SOD1) inhibits ERK phosphorylation by muscarinic receptor modulation in rat pituitary GH3 cells

Secondo, A., Mizio, M. D., Zirpoli, L., Santillo, M., & Mondola, P. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.08.110 · Cited by 17 · see citing works

Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging

Jomova, K., Raptova, R., Alomar, S. Y., Alwasel, S. H., Nepovimova, E., Kuca, K., & Valko, M. (2023) · Archives of Toxicology · doi:10.1007/s00204-023-03562-9 · Cited by 2,638 · see citing works

Angiotensin II Signal Transduction: An Update on Mechanisms of Physiology and Pathophysiology

Forrester, S. J., Booz, G. W., Sigmund, C. D., Coffman, T. M., Kawai, T., Rizzo, V., Scalia, R. G., & Eguchi, S. (2018) · Physiological Reviews · doi:10.1152/physrev.00038.2017 · Cited by 1,106 · see citing works

Oxidative Stress in Cardiovascular Diseases: Still a Therapeutic Target?

Senoner, T., & Dichtl, W. (2019) · Nutrients · doi:10.3390/nu11092090 · Cited by 880 · see citing works

Oxidative Stress in Cardiovascular Diseases

Dubois‐Deruy, E., Peugnet, V., Turkieh, A., & Pinet, F. (2020) · Antioxidants · doi:10.3390/antiox9090864 · Cited by 667 · see citing works

Oxidative Stress-Induced Endothelial Dysfunction in Cardiovascular Diseases

Shaito, A. A., Aramouni, K., Assaf, R., Parenti, A., Orekhov, A. N., EL‐Yazbi, A. F., Pintus, G., & Eid, A. H. (2022) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2703105 · Cited by 427 · see citing works

NADPH Oxidases: From Molecular Mechanisms to Current Inhibitors

Cipriano, A., Viviano, M., Feoli, A., Milite, C., Sarno, G., Castellano, S., & Sbardella, G. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00770 · Cited by 190 · see citing works

Reactive Oxygen Species Scavenging Nanomedicine for the Treatment of Ischemic Heart Disease

Zhang, Z., Dalan, R., Hu, Z., Wang, J., Chew, N., Poh, K. K., Tan, R., Soong, T. W., Dai, Y., Ye, L., et al. (2022) · Advanced Materials · doi:10.1002/adma.202202169 · Cited by 174 · see citing works

The Cu, Zn Superoxide Dismutase: Not Only a Dismutase Enzyme

Mondola, P., Damiano, S., Sasso, A., & Santillo, M. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2016.00594 · Cited by 166 · see citing works

Mitochondria in endothelial cells: Sensors and integrators of environmental cues

Caja, S., & Enrı́quez, J. A. (2017) · Redox Biology · doi:10.1016/j.redox.2017.04.021 · Cited by 150 · see citing works

Lipid Peroxidation in Atherosclerotic Cardiovascular Diseases

Gianazza, E., Brioschi, M., Fernandez, A. M., Casalnuovo, F., Altomare, A., Aldini, G., & Banfi, C. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7955 · Cited by 158 · see citing works

Therapeutic Options Targeting Oxidative Stress, Mitochondrial Dysfunction and Inflammation to Hinder the Progression of Vascular Complications of Diabetes

Teodoro, J. S., Nunes, S., Rolo, A. P., Reis, F., & Palmeira, C. M. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2018.01857 · Cited by 149 · see citing works

NADPH oxidase family proteins: signaling dynamics to disease management

Begum, R., Thota, S., Abdulkadir, A. S., Kaur, G., Bagam, P., & Batra, S. (2022) · Cellular and Molecular Immunology · doi:10.1038/s41423-022-00858-1 · Cited by 148 · see citing works

Aging: Molecular Pathways and Implications on the Cardiovascular System

de Almeida, A. J. P. O., Ribeiro, T. P., & de Medeiros, I. A. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/7941563 · Cited by 117 · see citing works

NADPH oxidase in the vasculature: Expression, regulation and signalling pathways; role in normal cardiovascular physiology and its dysregulation in hypertension

Knock, G. A. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.09.029 · Cited by 108 · see citing works

Dual Role of Reactive Oxygen Species in Muscle Function: Can Antioxidant Dietary Supplements Counteract Age-Related Sarcopenia?

Damiano, S., Muscariello, E., Rosa, G. L., Maro, M. D., Mondola, P., & Santillo, M. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20153815 · Cited by 110 · see citing works

Management of oxidative stress and inflammation in cardiovascular diseases: mechanisms and challenges

Donia, T., & Khamis, A. A. (2021) · Environmental Science and Pollution Research · doi:10.1007/s11356-021-14109-9 · Cited by 108 · see citing works

Matrix Metalloproteinases and Arterial Hypertension: Role of Oxidative Stress and Nitric Oxide in Vascular Functional and Structural Alterations

do Prado, A. F., Batista, R. I. M., Tanus-Santos, J. E., & Gerlach, R. F. (2021) · Biomolecules · doi:10.3390/biom11040585 · Cited by 102 · see citing works

mTOR and Aging: An Old Fashioned Dress

Stallone, G., Infante, B., Prisciandaro, C., & Grandaliano, G. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20112774 · Cited by 97 · see citing works

The role of nutraceuticals in prevention and treatment of hypertension: An updated review of the literature

Ghaffari, S., & Roshanravan, N. (2019) · Food Research International · doi:10.1016/j.foodres.2019.108749 · Cited by 91 · see citing works

Dietary supplementation of ginger and turmeric improves reproductive function in hypertensive male rats

Akinyemi, A. J., Adedara, I. A., Thomé, G. R., Morsch, V. M., Rovani, M. T., Mujica, L. K. S., Duarte, T., Duarte, M. M. M. F., Oboh, G., & Schetinger, M. R. C. (2015) · Toxicology Reports · doi:10.1016/j.toxrep.2015.10.001 · Cited by 75 · see citing works

Mineralocorticoid regulation of cell function: the role of rapid signalling and gene transcription pathways

Ong, G. S. Y., & Young, M. J. (2016) · Journal of Molecular Endocrinology · doi:10.1530/jme-15-0318 · Cited by 72 · see citing works

Reactive Oxygen Species Derived from NOX3 and NOX5 Drive Differentiation of Human Oligodendrocytes

Accetta, R., Damiano, S., Morano, A., Mondola, P., Paternò, R., Avvedimento, E. V., & Santillo, M. (2016) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2016.00146 · Cited by 66 · see citing works

Molecular insights of NADPH oxidases and its pathological consequences

Waghela, B. N., Vaidya, F. U., Agrawal, Y., Santra, M. K., Mishra, V., & Pathak, C. (2020) · Cell Biochemistry and Function · doi:10.1002/cbf.3589 · Cited by 59 · see citing works

Metabolism Regulation and Redox State: Insight into the Role of Superoxide Dismutase 1

Damiano, S., Sozio, C., Rosa, G. L., Guida, B., Faraonio, R., Santillo, M., & Mondola, P. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186606 · Cited by 56 · see citing works

ROS-dependent activation of RhoA/Rho-kinase in pulmonary artery: Role of Src-family kinases and ARHGEF1

Mackay, C., Shaifta, Y., Snetkov, V. A., Francois, A. A., Ward, J. P. T., & Knock, G. A. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.06.022 · Cited by 55 · see citing works

The Impact of the Renin-Angiotensin-Aldosterone System on Inflammation, Coagulation, and Atherothrombotic Complications, and to Aggravated COVID-19

Ekholm, M., & Kahan, T. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.640185 · Cited by 56 · see citing works

NADPH Oxidases in Diastolic Dysfunction and Heart Failure with Preserved Ejection Fraction

Teuber, J. P., Essandoh, K., Hummel, S. L., Madamanchi, N. R., & Brody, M. J. (2022) · Antioxidants · doi:10.3390/antiox11091822 · Cited by 52 · see citing works

NADPH oxidases as electrochemical generators to produce ion fluxes and turgor in fungi, plants and humans

Segal, A. W. (2016) · Open Biology · doi:10.1098/rsob.160028 · Cited by 44 · see citing works

ACE2 and the Homolog Collectrin in the Modulation of Nitric Oxide and Oxidative Stress in Blood Pressure Homeostasis and Vascular Injury

Yang, G., Chu, P., Rump, L. C., Le, T. H., & Stegbauer, J. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6950 · Cited by 43 · see citing works

P2Y Purinergic Receptors, Endothelial Dysfunction, and Cardiovascular Diseases

Strassheim, D., Verin, A. D., Batori, R. K., Nijmeh, H., Burns, N., Kovács‐Kása, A., Umapathy, N. S., Kotamarthi, J., Gokhale, Y., Karoor, V., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186855 · Cited by 42 · see citing works

Circulating metabolites of strawberry mediate reductions in vascular inflammation and endothelial dysfunction in db/db mice

Petersen, C., Bharat, D., Cutler, B. R., Gholami, S., Denetso, C., Mueller, J. E., Cho, J. M., Kim, J.-S., Symons, J. D., & Babu, P. V. A. (2018) · International Journal of Cardiology · doi:10.1016/j.ijcard.2018.04.040 · Cited by 36 · see citing works

Role of curcumin in ameliorating hypertension and associated conditions: a mechanistic insight

Joshi, P., Joshi, S., Semwal, D. K., Verma, K., Dwivedi, J., & Sharma, S. K. (2022) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-022-04447-8 · Cited by 35 · see citing works

Genistein Prevents Nitric Oxide Deficiency-Induced Cardiac Dysfunction and Remodeling in Rats

Poasakate, A., Maneesai, P., Rattanakanokchai, S., Bunbupha, S., Tong-un, T., & Pakdeechote, P. (2021) · Antioxidants · doi:10.3390/antiox10020237 · Cited by 33 · see citing works

Diverse biological functions of the renin‐angiotensin system

Rao, A., Bhat, S. A., Shibata, T., Giani, J. F., Rader, F., Bernstein, K. E., & Khan, Z. (2023) · Medicinal Research Reviews · doi:10.1002/med.21996 · Cited by 31 · see citing works

Anti-Inflammatory Effects of Peripheral Dopamine

Moore, S. C., de Castro, P. A. S. V., Yaqub, D., José, P. A., & Armando, I. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241813816 · Cited by 31 · see citing works

Low concentration of rutin treatment might alleviate the cardiotoxicity effect of pirarubicin on cardiomyocytes via activation of PI3K/AKT/mTOR signaling pathway

Fei, J., Sun, Y., Duan, Y., Xia, J., Yu, S., Ouyang, P., Wang, T., & Zhang, G. (2019) · Bioscience Reports · doi:10.1042/bsr20190546 · Cited by 27 · see citing works

Dynamic regulation of NADPH oxidase 5 by intracellular heme levels and cellular chaperones

Sweeny, E. A., Schlanger, S. E., & Stuehr, D. J. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101656 · Cited by 24 · see citing works

Immunomodulatory properties of the lymphatic endothelium in the tumor microenvironment

Viúdez-Pareja, C., Kreft, E. A., & García‐Caballero, M. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1235812 · Cited by 23 · see citing works

An overview of the emerging interface between cardiac metabolism, redox biology and the circadian clock

Garcia, R. A. P., Darley-Usmar, V. M., & Young, M. E. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.02.013 · Cited by 20 · see citing works

Berries and Their Polyphenols as a Potential Therapy for Coronary Microvascular Dysfunction: A Mini-Review

Najjar, R. S., Schwartz, A. M., Wong, B. J., Mehta, P. K., & Feresin, R. G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22073373 · Cited by 20 · see citing works

NADPH Oxidase 3: Beyond the Inner Ear

Herb, M. (2024) · Antioxidants · doi:10.3390/antiox13020219 · Cited by 18 · see citing works

Associations Between Genetic Variants of NADPH Oxidase-Related Genes and Blood Pressure Responses to Dietary Sodium Intervention: The GenSalt Study

Han, X., Hu, Z., Chen, J., Huang, J., Huang, C., Liu, F., Gu, C. C., Yang, X., Hixson, J. E., Lu, X., et al. (2017) · American Journal of Hypertension · doi:10.1093/ajh/hpw200 · Cited by 18 · see citing works

Cardiovascular Disease in Obstructive Sleep Apnea: Putative Contributions of Mineralocorticoid Receptors

Badran, M., Bender, S. B., & Gozal, D. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032245 · Cited by 18 · see citing works

Overview on Interactive Role of Inflammation, Reactive Oxygen Species, and Calcium Signaling in Asthma, COPD, and Pulmonary Hypertension

Truong, L., Zheng, Y., Kandhi, S., & Wang, Y.-X. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-68748-9_9 · Cited by 16 · see citing works

Effect of Mutated Cu, Zn Superoxide Dismutase (SOD1G93A) on Modulation of Transductional Pathway Mediated by M1 Muscarinic Receptor in SK-N-BE and NSC-34 Cells

Damiano, S., Sasso, A., Accetta, R., Monda, M., Luca, B. D., Pavone, L. M., Belfiore, A., Santillo, M., & Mondola, P. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00611 · Cited by 16 · see citing works

Age-Related Changes in Skeletal Muscle Oxygen Utilization

Salvatore, S. S., Zelenski, K. N., & Perkins, R. K. (2022) · Journal of Functional Morphology and Kinesiology · doi:10.3390/jfmk7040087 · Cited by 15 · see citing works

Mitochondrial Integrity Is Critical in Right Heart Failure Development

Müller, M., Donhauser, E., Maske, T., Bischof, C., Dumitrescu, D., Rudolph, V., & Klinke, A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241311108 · Cited by 15 · see citing works

Associations of NADPH oxidase-related genes with blood pressure changes and incident hypertension: The GenSalt Study

Li, H., Han, X., Hu, Z., Huang, J., Chen, J., Hixson, J. E., Rao, D. C., He, J., Gu, D., & Chen, S. (2018) · Journal of Human Hypertension · doi:10.1038/s41371-018-0041-6 · Cited by 15 · see citing works

The NADPH Oxidase Isoform 1 Contributes to Angiotensin II-Mediated DNA Damage in the Kidney

Zimnol, A., Spicker, N., Balhorn, R., Schröder, K., & Schupp, N. (2020) · Antioxidants · doi:10.3390/antiox9070586 · Cited by 16 · see citing works

Exogenous 8‐hydroxydeoxyguanosine ameliorates liver fibrosis through the inhibition of Rac1‐NADPH oxidase signaling

Shin, S. K., Kim, K., Kim, S., Kwon, O. S., Choi, C. S., Jeong, S. H., Kim, Y. S., Kim, J. H., & Chung, M. (2020) · Journal of Gastroenterology and Hepatology · doi:10.1111/jgh.14979 · Cited by 14 · see citing works

Inhibition of NOX1 Mitigates Blood Pressure Increases in Elastin Insufficiency

Troia, A., Knutsen, R. H., Halabi, C. M., Malide, D. A., Yu, Z., Wardlaw-Pickett, A., Kronquist, E. K., Tsang, K. M., Kovács, A. D., Mecham, R. P., et al. (2021) · Function · doi:10.1093/function/zqab015 · Cited by 13 · see citing works

Understanding the causes and implications of endothelial metabolic variation in cardiovascular disease through genome-scale metabolic modeling

McGarrity, S., Halldórsson, H., Palsson, S., Johansson, P. I., & Rolfsson, Ó. (2016) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2016.00010 · Cited by 12 · see citing works

Lancemaside A from Codonopsis lanceolata prevents hypertension by inhibiting NADPH oxidase 2-mediated MAPK signalling and improving NO bioavailability in rats

Shin, Y. K., Han, A. Y., Hsieh, Y.-S., Kwon, S., Kim, J., Lee, K., & Seol, G. H. (2019) · Journal of Pharmacy and Pharmacology · doi:10.1111/jphp.13140 · Cited by 12 · see citing works

Exogenous 8-Hydroxydeoxyguanosine Attenuates PM2.5-Induced Inflammation in Human Bronchial Epithelial Cells by Decreasing NLRP3 Inflammasome Activation

Bang, J., Son, K. H., Heo, H.-R., Park, E., Kwak, H. J., Uhm, K., Chung, M., Kim, Y.-Y., & Lim, H. J. (2023) · Antioxidants · doi:10.3390/antiox12061189 · Cited by 12 · see citing works

Nelumbo nucifera Receptaculum Extract Suppresses Angiotensin II-Induced Cardiomyocyte Hypertrophy

Cho, S., Cho, H. W., Woo, K. W., Jeong, J., Lim, J., Park, S., Seo, M., & Lim, S. (2019) · Molecules · doi:10.3390/molecules24091647 · Cited by 11 · see citing works

Hydroxychloroquine reduces hypertension and soluble fms-like kinase-1 in a N ω-nitro-l-arginine methyl ester-induced preeclampsia rat model

Choi, M., Hwang, J. R., Sung, J., Byun, N., Seok, Y. S., Cho, G. J., Choi, S., Kim, J.-S., Oh, S., & Roh, C. (2022) · Journal of Hypertension · doi:10.1097/hjh.0000000000003279 · Cited by 10 · see citing works

Intermittent high‐intensity exercise for pre‐ to established hypertension: A systematic review and meta‐analysis

Teixeira, J. M. M., Motta‐Santos, D., Milanović, Z., Pereira, R., Krustrup, P., & Póvoas, S. C. A. (2022) · Scandinavian Journal of Medicine and Science in Sports · doi:10.1111/sms.14299 · Cited by 10 · see citing works

Integrated chemical composition, transcriptomics, and network pharmacology to reveal the mechanism of Jia-Wei-Si-Miao-Yong-An Decoction in ACS model rats

Zhao, N., Dang, M., Sun, Y., Ma, Y., Xia, Y., Jin, Q., Yang, X., Gao, Y., Hu, J., & Bai, D. (2025) · Phytomedicine · doi:10.1016/j.phymed.2025.157027 · Cited by 9 · see citing works

Functional interactions between NADPH oxidase 5 and actin

Richter, S. M., Massman, L., Stuehr, D. J., & Sweeny, E. A. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1116833 · Cited by 8 · see citing works

Skin Microhemodynamics and Mechanisms of Its Regulation in Type 2 Diabetes Mellitus

Tikhonova, I. V., Grinevich, A. A., Tankanag, A. V., & Safronova, V. G. (2022) · BIOPHYSICS · doi:10.1134/s0006350922040200 · Cited by 7 · see citing works

Low but not high frequency of intermittent hypoxia suppresses endothelium-dependent, oxidative stress-mediated contractions in carotid arteries of obese mice

Lee, M. Y. K., Ge, G. M., Fung, M. L., Vanhoutte, P. M., Mak, J., & Ip, M. (2018) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00224.2018 · Cited by 7 · see citing works

Role of Mitochondrial ROS for Calcium Alternans in Atrial Myocytes

Oropeza‐Almazán, Y., & Blatter, L. A. (2024) · Biomolecules · doi:10.3390/biom14020144 · Cited by 6 · see citing works

Mangiferin mitigates dexamethasone-induced insulin resistance in rats: insight into vascular dysfunction and hepatic steatosis

Alsaedi, A. Q., Nader, M. A., El-Kashef, D. H., & Abdelmageed, M. E. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1572758 · Cited by 5 · see citing works

The Alleviative Effect of Naringin Against Cardiovascular Dysfunction and Remodeling in Hypertensive Rats by Suppressing the Angiotensin II Pathway

Khamseekaew, J., Iampanichakul, M., Potue, P., Maneesai, P., Tangsucharit, P., Rattanakanokchai, S., & Pakdeechote, P. (2025) · Food Science & Nutrition · doi:10.1002/fsn3.70484 · Cited by 5 · see citing works

Endothelial NOX1 Drives Obesity via Skeletal Muscle Mitochondrial Dysfunction

Huang, K., Huang, Y., Zhang, Y., Zhang, Y., Hatch, N. W., Freed, J. K., & Cai, H. “. (2026) · Circulation Research · doi:10.1161/circresaha.125.326768 · Cited by 4 · see citing works

EGF Receptor Transactivation by Endothelin-1 Increased CHSY-1 Mediated by NADPH Oxidase and Phosphorylation of ERK1/2.

Babaahmadi‐Rezaei, H., Kheirollah, A., Rashidi, M., Seif, F., Niknam, Z., & Zamanpour, M. (2021) · PubMed Central · doi:10.22074/cellj.2021.7392 · Cited by 4 · see citing works

SARS-CoV-2 spike interactions with the renin-angiotensin-aldosterone system -Consequences of adverse reactions of vaccination-Preprint

Lehmann, K. J. (2023) · doi:10.31219/osf.io/27g5h · Cited by 4 · see citing works

NADPH Oxidase 1 Mediates Endothelial Dysfunction and Hypertension in a Murine Model of Obesity

Padgett, C. A., Butcher, J. T., Larion, S., MINTZ, J. D., Fulton, D. J., & Stepp, D. W. (2026) · Antioxidants · doi:10.3390/antiox15010060 · Cited by 3 · see citing works

The role of low-carbohydrate, high-fat diet in modulating autophagy and endoplasmic reticulum stress in aortic endothelial dysfunction of metabolic syndrome animal model

Eldakhakhny, B. M., Bima, A. I. H., Alamoudi, A. A., Alnami, A., El‐khair, S. M. A., Sakr, H. F., Almoghrabi, Y. M., Ghoneim, F. M., Nagib, R. M., & Elsamanoudy, A. Z. (2024) · Frontiers in Nutrition · doi:10.3389/fnut.2024.1467719 · Cited by 3 · see citing works

The role of oxidative stress in the etiology of selected civilization diseases

Koczurkiewicz, P., Gąsiorkiewicz, B., Pękala, E., & Bojdo, P. (2021) · Farmacja Polska · doi:10.32383/farmpol/134797 · Cited by 2 · see citing works

Oxidative Stress in Cardiovascular Diseases

Mahmoud, A. M., & Junejo, R. T. (2024) · Springer eBooks · doi:10.1007/978-3-031-69962-7_3 · Cited by 2 · see citing works

Calcium in hypertension prevention: an exploratory review

Fikri, A. M. (2023) · Nutrire · doi:10.1186/s41110-023-00209-8 · Cited by 2 · see citing works

Oxidative damage in immunoglobulin light chain and transthyretin cardiac amyloidosis – a closer look

Cavallone, E., Mousavi, A. H., Biolè, C., Nangeroni, G., Chinaglia, A., & Bianco, M. (2024) · Redox Experimental Medicine · doi:10.1530/rem-24-0001 · Cited by 2 · see citing works

Commentary: Oxygen regulation of breathing through an olfactory receptor activated by lactate

Santillo, M., & Damiano, S. (2016) · Frontiers in Neuroscience · doi:10.3389/fnins.2016.00213 · Cited by 2 · see citing works

Efectos biológicos protectores del ejercicio en modelos experimentales de tabaquismo: Más allá de la cesación y la abstinencia

Rodríguez‐Núñez, I. (2020) · Revista chilena de enfermedades respiratorias · doi:10.4067/s0717-73482020000100033 · Cited by 1 · see citing works

Pro-oxidants

Khelfi, A. (2024) · Springer eBooks · doi:10.1007/978-3-031-60738-7_4 · Cited by 1 · see citing works

Asymmetric dimethylarginine mediates oxidative stress and atrial remodeling in HL-1 cells

Yu, C., Zhang, M., & Xia, W. T. (2025) · Frontiers in Medicine · doi:10.3389/fmed.2025.1696845 · Cited by 1 · see citing works

Targeting endothelial oxidative stress in hypertension

Liu, J. (2025) · Open Medicine · doi:10.1515/med-2025-1361 · Cited by 1 · see citing works

Glutathione-S-transferase in the context of antioxidant protection against cardiovascular diseases

Khadorych, M. A., Gumanova, N. G., & Vasiliev, D. K. (2025) · Russian Journal of Preventive Medicine · doi:10.17116/profmed202528121124 · Cited by 1 · see citing works

ROS-Mediated Cardiomyocyte Proliferation and Myocardial Regeneration: Mechanisms and Targeted Strategies for Ischemic Heart Disease

Chen, M., Liu, T., Sun, F., Tian, X., Zheng, W., Zhu, Z., & Wang, W. (2026) · Journal of Cardiovascular Development and Disease · doi:10.3390/jcdd13030105 · Cited by 1 · see citing works

Oxidative Stress Monitoring: Needs and Opportunities

Khelfi, A., Mahmoud, A. M., Perrone, S., Marı́n, R., Hussain, F., Fülöp, T., Khalil, A., Pilo, F., Rehman, R., Roumeliotis, S. K., et al. (2024) · Springer eBooks · doi:10.1007/978-3-031-60738-7_22 · Cited by 1 · see citing works

Interferon-stimulated gene 15, a common link of vascular damage in hypertension, obesity and aortic aneurysms

González‐Amor, M., & García‐Redondo, A. B. (2022) · Anales de la Real Academia Nacional de Farmacia · doi:10.53519/analesranf.2022.88.02.04 · Cited by 1 · see citing works

Role of Flavonoids in ROS‐Mediated Cardiovascular Disorders

Chenchula, S., Anitha, K., Garg, A., Ashique, S., Ghanta, M. K., & Mishra, N. (2024) · doi:10.1002/9781394238071.ch12 · Cited by 1 · see citing works

Modulation of miRNA in Oxidative Stress-Induced Cardiac Remodeling

Gupta, S. (2019) · Springer eBooks · doi:10.1007/978-981-13-8946-7_3

Hypotensive Effect of Magnolin on Spontaneously Hypertensive Rats by Reversing Nitric Oxide Synthase Uncoupling

Zhang, H. P., Qin, D., Aletengtuya, Gu, H. Q., Chen, L., & Jiang, M. H. (2022) · Revista Brasileira de Farmacognosia · doi:10.1007/s43450-021-00196-9

Influência do treinamento de força moderado sobre a expressão de marcadores de estresse oxidativo em mulheres idosas

de Oliveira, P. R. C. (2021) · doi:10.11606/d.5.2021.tde-04042022-151952

Caracterização farmacológica de doadores de sulfeto de hidrogênio (H2S) na resposta vasomotora in vitro de anéis de artéria mesentérica de camundongos.

Marques, L. A. D. C. (2020) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.42.2020.tde-05012021-145806

NADPH Oxidases in Zebrafish

Alam, S. M. S., & Suter, D. M. (2023) · Springer eBooks · doi:10.1007/978-3-031-23752-2_29

Age-Induced Endothelial Dysfunction and Intima–Media Thickening

Kozàkovà, M., & Schmidt‐Trucksäss, A. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-15512-3.00029-5

Cell Signaling

Feher, J. (2025) · Elsevier eBooks · doi:10.1016/b978-0-12-820476-4.00017-5

Oxidative Stress and Pathophysiology of Chronic Disease

Balaji, S., Pandian, M. S., Ganesamoorthy, R., Parameswari, R., & Babujanarthanam, R. (2026) · Springer eBooks · doi:10.1007/978-981-96-9670-3_3

F-actin-dependent activation of NADPH oxidase 5 by the vacuolar-type ATPase

Heywood, G. J., Richter, S. M., Paul, A. S., & Sweeny, E. A. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.113546

LPS stimulation reveals male and female dimorphism in human iPSC-derived macrophages

Graney, P. L., Tavakol, D. N., Lock, R. I., Chen, C., Samaritano, M., Sanchez, E., Hachmann, N. P., Pineda‐Rosales, M., Friedman, R., & Vunjak‐Novakovic, G. (2026) · iScience · doi:10.1016/j.isci.2026.117565 · Cited by 1 · see citing works

BindingDB Entry 50020295: NADPH Oxidases: From Molecular Mechanisms to Current Inhibitors.

BindingDB (2024) · UC San Diego · doi:10.7270/q2jm2g3p

Molecular mechanisms of hypertension: role of Nox family NADPH oxidases

Sedeek, M. H., Hébert, R., Kennedy, C., Burns, K. D., & Touyz, R. M. (2009) · Current Opinion in Nephrology & Hypertension · doi:10.1097/mnh.0b013e32832923c3 · Cited by 170 · see citing works

NADPH oxidase in the vasculature: Expression, regulation and signalling pathways; role in normal cardiovascular physiology and its dysregulation in hypertension

Knock, G. A. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.09.029 · Cited by 108 · see citing works

Reactive Oxygen Species, Vascular Noxs, and Hypertension: Focus on Translational and Clinical Research

Montezano, A. C. I., & Touyz, R. M. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5302 · Cited by 275 · see citing works

Up-Regulation of Nox4 Expression in DUSP4-/- hearts Plays a Critical Role in Modulating Cardiovascular Function Under Oxidative Stress

Lamb, J., Angelos, M. G., & Chen, C. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.10.126

Oxidative stress, Noxs, and hypertension: Experimental evidence and clinical controversies

Montezano, A. C. I., & Touyz, R. M. (2012) · Annals of Medicine · doi:10.3109/07853890.2011.653393 · Cited by 194 · see citing works