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

Free Radicals in the Physiological Control of Cell Function

Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855

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

PDZ Domains and the Organization of Supramolecular Complexes

Sheng, M., & Sala, C. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1 · Cited by 1,211

Reactive Oxygen Species as Intracellular Messengers During Cell Growth and Differentiation

Sauer, H., Wartenberg, M., & Hescheler, J. (2001) · Cellular Physiology and Biochemistry · doi:10.1159/000047804 · Cited by 1,118

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 1,026

Identification of Renox, an NAD(P)H oxidase in kidney

Geiszt, M., Kopp, J. B., Várnai, P., & Leto, T. L. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.130135897 · Cited by 840

Homologs of gp91 phox : cloning and tissue expression of Nox3, Nox4, and Nox5

Cheng, G., Cao, Z., Xu, X., Meir, E. G. V., & Lambeth, J. D. (2001) · Gene · doi:10.1016/s0378-1119(01)00449-8 · Cited by 820

The superoxide-generating NADPH oxidase: structural aspects and activation mechanism

Vignais, P. V. (2002) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-002-8520-9 · Cited by 799

Characterization of Rac and Cdc42 Activation in Chemoattractant-stimulated Human Neutrophils Using a Novel Assay for Active GTPases

Planat‐Benard, V., Bohl, B. P., & Bokoch, G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.19.13198 · Cited by 754

The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence

Frangioni, J. V., Beahm, P. H., Shifrin, V. I., Jost, C. A., & Neel, B. G. (1992) · Cell · doi:10.1016/0092-8674(92)90190-n · Cited by 596

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

Reactive Oxygen Species in Inflammation and Tissue Injury

Mittal, M., Siddiqui, M. R., Tran, K., Reddy, S. P., & Malik, A. B. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.5149 · Cited by 4,897

Protein tyrosine phosphatases: from genes, to function, to disease

Tonks, N. K. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2039 · Cited by 1,712

Physiology of cell volume regulation in vertebrates

Hoffmann, E. K., Lambert, I. H., & Pedersen, S. F. (2009) · Physiological Reviews · doi:10.1152/physrev.00037.2007 · Cited by 1,441

Uric Acid: The Oxidant-Antioxidant Paradox

Sautin, Y. Y., & Johnson, R. J. (2008) · Nucleosides Nucleotides & Nucleic Acids · doi:10.1080/15257770802138558 · Cited by 1,029

NADPH oxidases: An overview from structure to innate immunity-associated pathologies

Panday, A., Sahoo, M. K., Osorio, D., & Batra, S. (2015) · Cellular & Molecular Immunology · doi:10.1038/cmi.2014.89 · Cited by 944

Adverse effects of the classic antioxidant uric acid in adipocytes: NADPH oxidase-mediated oxidative/nitrosative stress

Sautin, Y. Y., Nakagawa, T., Zharikov, S. I., & Johnson, R. J. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00600.2006 · Cited by 799

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

NADPH oxidase 4 (Nox4) is a major source of oxidative stress in the failing heart

Kuroda, J., Ago, T., Matsushima, S., Zhai, P., Schneider, M. D., & Sadoshima, J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002178107 · Cited by 772

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 780

Structure, regulation and evolution of Nox‐family NADPH oxidases that produce reactive oxygen species

Sumimoto, H. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06488.x · Cited by 740

Nox family NADPH oxidases: Molecular mechanisms of activation

Brandes, R. P., Weißmann, N., & Schröder, K. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.07.046 · Cited by 691

Diabetes and Kidney Disease: Role of Oxidative Stress

Jha, J. C., Banal, C., Chow, B. S. M., Cooper, M. E., & Jandeleit-Dahm, K. (2016) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6664 · Cited by 660

Regulation of Reactive Oxygen Species Generation in Cell Signaling

Bae, Y. S., Oh, H., Rhee, S. G., & Yoo, Y. D. (2011) · Molecules and Cells · doi:10.1007/s10059-011-0276-3 · Cited by 675

The double-edged roles of ROS in cancer prevention and therapy

Wang, Y., Qi, H., Liu, Y., Duan, C., Liu, X., Xia, T., Chen, D., Piao, H., & Liu, H. (2021) · Theranostics · doi:10.7150/thno.56747 · Cited by 657

NADPH Oxidases in Cardiovascular Health and Disease

Cave, A. C., Brewer, A. C., Narayanapanicker, A., Ray, R., Grieve, D. J., Walker, S., & Shah, A. M. (2006) · Antioxidants & Redox Signaling · doi:10.1089/ars.2006.8.691 · Cited by 630

NOX4 activity is determined by mRNA levels and reveals a unique pattern of ROS generation

Serrander, L., Cartier, L., Bedard, K., Banfi, B., Lardy, B., Plastre, O., Sienkiewicz, A., Fórró, L., Schlegel, W., & Krause, K.-H. (2007) · Biochemical Journal · doi:10.1042/bj20061903 · Cited by 627

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

NADPH Oxidases: Functions and Pathologies in the Vasculature

Lassègue, B., & Griendling, K. K. (2010) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/atvbaha.108.181610 · Cited by 592

NADPH Oxidase-Mediated Redox Signaling: Roles in Cellular Stress Response, Stress Tolerance, and Tissue Repair

Jiang, F., Zhang, Y., & Dusting, G. J. (2011) · Pharmacological Reviews · doi:10.1124/pr.110.002980 · Cited by 585

Mechanisms and Implications of Reactive Oxygen Species Generation During the Unfolded Protein Response: Roles of Endoplasmic Reticulum Oxidoreductases, Mitochondrial Electron Transport, and NADPH Oxidase

Santos, C. X. C., Tanaka, L. Y., Wosniak, J., & Laurindo, F. R. M. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2625 · Cited by 572

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

Positive and Negative Regulation of Insulin Signaling by Reactive Oxygen and Nitrogen Species

Bashan, N., Kovsan, J., Kachko, I., Ovadia, H., & Rudich, A. (2009) · Physiological Reviews · doi:10.1152/physrev.00014.2008 · Cited by 542

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

The E-loop Is Involved in Hydrogen Peroxide Formation by the NADPH Oxidase Nox4

Takac, I., Schröder, K., Zhang, L., Lardy, B., Anilkumar, N. P., Lambeth, J. D., Shah, A. M., Morel, F., & Brandes, R. P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.192138 · Cited by 539

Regulation of NADPH Oxidases

Hordijk, P. L. (2006) · Circulation Research · doi:10.1161/01.res.0000204727.46710.5e · Cited by 534

Oxidative Stress in Liver Pathophysiology and Disease

Allameh, A., Niayesh‐Mehr, R., Aliarab, A., Sebastiani, G., & Pantopoulos, K. (2023) · Antioxidants · doi:10.3390/antiox12091653 · Cited by 606

TNF-Induced Activation of the Nox1 NADPH Oxidase and Its Role in the Induction of Necrotic Cell Death

Kim, Y., Morgan, M. J., Choksi, S., & Liu, Z.-G. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.04.021 · Cited by 523

Upregulation of Nox4 by Hypertrophic Stimuli Promotes Apoptosis and Mitochondrial Dysfunction in Cardiac Myocytes

Ago, T., Kuroda, J., Pain, J., Fu, C., Li, H., & Sadoshima, J. (2010) · Circulation Research · doi:10.1161/circresaha.109.213116 · Cited by 506

Regulation of Nox and Duox enzymatic activity and expression

Lambeth, J. D., Kawahara, T., & Diebold, B. A. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.03.028 · Cited by 510

Nox4 NAD(P)H Oxidase Mediates Hypertrophy and Fibronectin Expression in the Diabetic Kidney

Gorin, Y. C., Block, K. L., Hernandez, J., Bhandari, B., Wagner, B., Barnes, J. L., & Abboud, H. E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502412200 · Cited by 496

Subcellular localization of Nox4 and regulation in diabetes

Block, K. L., Gorin, Y. C., & Abboud, H. E. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906805106 · Cited by 484

Regulation of ROS signal transduction by NADPH oxidase 4 localization

Chen, K., Kirber, M. T., Xiao, H. Q., Yang, Y., & Keaney, J. F. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200709049 · Cited by 480

Mitochondrial Function, Biology, and Role in Disease

Murphy, E., Ardehali, H., Balaban, R. S., Lisa, F. D., Dorn, G. W., Kitsis, R. N., Otsu, K., Ping, P., Rizzuto, R., Sack, M. N., et al. (2016) · Circulation Research · doi:10.1161/res.0000000000000104 · Cited by 476

NADPH Oxidases in Vascular Pathology

Konior, A., Schramm‐Luc, A., Cześnikiewicz‐Guzik, M., & Guzik, T. J. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5607 · Cited by 464

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 452

Myofibroblast differentiation during fibrosis: role of NAD(P)H oxidases

Barnes, J. L., & Gorin, Y. C. (2011) · Kidney International · doi:10.1038/ki.2010.516 · Cited by 438

NADPH oxidase in brain injury and neurodegenerative disorders

Ma, M. W., Wang, J., Zhang, Q., Wang, R., Dhandapani, K. M., Vadlamudi, R. K., & Brann, D. W. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0150-7 · Cited by 432

Poldip2, a Novel Regulator of Nox4 and Cytoskeletal Integrity in Vascular Smooth Muscle Cells

Lyle, A. N., Deshpande, N. N., Taniyama, Y., Seidel-Rogol, B., Pounkova, L., Du, P., Papaharalambus, C., Lassègue, B., & Griendling, K. K. (2009) · Circulation Research · doi:10.1161/circresaha.109.193722 · Cited by 428

Transforming growth factor-β1 induces Nox4 NAD(P)H oxidase and reactive oxygen species-dependent proliferation in human pulmonary artery smooth muscle cells

Sturrock, A., Cahill, B., Norman, K., Huecksteadt, T. P., Hill, K., Sanders, K., Karwande, S. V., Stringham, J. C., Bull, D. A., Gleich, M., et al. (2006) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00269.2005 · Cited by 402

RBOH-Dependent ROS Synthesis and ROS Scavenging by Plant Specialized Metabolites To Modulate Plant Development and Stress Responses

Chapman, J. M., Mühlemann, J. K., Gayomba, S. R., & Muday, G. K. (2019) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.9b00028 · Cited by 396

Reactive oxygen species and oxidative stress in osteoclastogenesis, skeletal aging and bone diseases

Callaway, D. A., & Jiang, J. X. (2015) · Journal of Bone and Mineral Metabolism · doi:10.1007/s00774-015-0656-4 · Cited by 393

Localizing NADPH Oxidase–Derived ROS

Ushio‐Fukai, M. (2006) · Science s STKE · doi:10.1126/stke.3492006re8 · Cited by 397

Distinct roles of Nox1 and Nox4 in basal and angiotensin II-stimulated superoxide and hydrogen peroxide production

Dikalov, S., Dikalova, A., Bikineyeva, A. T., Schmidt, H. H. H. W., Harrison, D. G., & Griendling, K. K. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.08.013 · Cited by 391

NADPH oxidases and angiotensin II receptor signaling

Garrido, A. M., & Griendling, K. K. (2008) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2008.11.003 · Cited by 391

The Role of NADPH Oxidases and Oxidative Stress in Neurodegenerative Disorders

Tarafdar, A., & Pula, G. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19123824 · Cited by 373

The NOX toolbox: validating the role of NADPH oxidases in physiology and disease

Altenhöfer, S., Kleikers, P. W. M., Radermacher, K. A., Scheurer, P., Rob Hermans, J. J., Schiffers, P., Ho, H., Wingler, K., & Schmidt, H. H. H. W. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1010-9 · Cited by 371

Compartmentalization of Redox Signaling Through NADPH Oxidase–Derived ROS

Ushio‐Fukai, M. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2333 · Cited by 375

NADPH Oxidases of the Brain: Distribution, Regulation, and Function

Infanger, D. W., Sharma, R. V., & Davisson, R. L. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1583 · Cited by 365

Reactive oxygen species signaling in vascular smooth muscle cells

Clempus, R. E., & Griendling, K. K. (2006) · Cardiovascular Research · doi:10.1016/j.cardiores.2006.02.033 · Cited by 362

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

Targeting and Regulation of Reactive Oxygen Species Generation by Nox Family NADPH Oxidases

Leto, T. L., Morand, S. C., Hurt, D. E., & Ueyama, T. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2637 · Cited by 347

NADPH oxidase-dependent redox signalling in cardiac hypertrophy, remodelling and failure

Murdoch, C. E., Zhang, M., Cave, A. C., & Shah, A. M. (2006) · Cardiovascular Research · doi:10.1016/j.cardiores.2006.03.016 · Cited by 344

Molecular evolution of the reactive oxygen-generating NADPH oxidase (Nox/Duox) family of enzymes

Kawahara, T., Quinn, M. T., & Lambeth, J. D. (2007) · BMC Evolutionary Biology · doi:10.1186/1471-2148-7-109 · Cited by 346

Nox4 Is Required for Maintenance of the Differentiated Vascular Smooth Muscle Cell Phenotype

Clempus, R. E., Sorescu, D., Dikalova, A., Pounkova, L., Jo, P. C., Sorescu, G. P., Lassegue, B. P., & Griendling, K. K. (2006) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000251500.94478.18 · Cited by 338

Biological roles for the NOX family NADPH oxidases

Nauseef, W. M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r700045200 · Cited by 331

Oxidative stress and cardiovascular disease: Novel tools give (free) radical insight

Fearon, I. M., & Faux, S. P. (2009) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2009.05.013 · Cited by 334

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 332

Decreased blood pressure in NOX1‐deficient mice

Gavazzi, G., Banfi, B., Deffert, C., Fiette, L., Schappi, M., Herrmann, F., & Krause, K.-H. (2006) · FEBS Letters · doi:10.1016/j.febslet.2005.12.049 · Cited by 321

Redox signaling in cardiac myocytes

Santos, C. X. C., Anilkumar, N. P., Zhang, M., Brewer, A. C., & Shah, A. M. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.01.003 · Cited by 325

Endothelial NADPH oxidases: which NOX to target in vascular disease?

Drummond, G. R., & Sobey, C. G. (2014) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2014.06.012 · Cited by 315

Nox2-Induced Production of Mitochondrial Superoxide in Angiotensin II-Mediated Endothelial Oxidative Stress and Hypertension

Dikalov, S., Nazarewicz, R. R., Bikineyeva, A. T., Hilenski, L. L., Lassegue, B. P., Griendling, K. K., Harrison, D. G., & Dikalova, A. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4918 · Cited by 312

Hydrogen Peroxide as a Cell-Survival Signaling Molecule

Groeger, G., Quiney, C., & Cotter, T. G. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2728 · Cited by 318

Molecular mechanisms underlying chronic inflammation-associated cancers

Wu, Y., Antony, S., Meitzler, J. L., & Doroshow, J. H. (2013) · Cancer Letters · doi:10.1016/j.canlet.2013.08.014 · Cited by 312

Hyperuricemia-Related Diseases and Xanthine Oxidoreductase (XOR) Inhibitors: An Overview

Chen, C., Lü, J.-M., & Yao, Q. C. (2016) · Medical Science Monitor · doi:10.12659/msm.899852 · Cited by 307

Molecular composition and regulation of the Nox family NAD(P)H oxidases

Sumimoto, H., Miyano, K., & Takeya, R. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.08.210 · Cited by 306

Aiding and abetting roles of NOX oxidases in cellular transformation

Block, K. L., & Gorin, Y. C. (2012) · Nature reviews. Cancer · doi:10.1038/nrc3339 · Cited by 308

Direct evidence of a role for Nox2 in superoxide production, reduced nitric oxide bioavailability, and early atherosclerotic plaque formation in ApoE−/−mice

Judkins, C. P., Diep, H., Broughton, B. R. S., Mast, A. E., Hooker, E. U., Miller, A. A., Selemidis, S., Dusting, G. J., Sobey, C. G., & Drummond, G. R. (2010) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00799.2009 · Cited by 299

Role of Oxidative Stress in Reperfusion following Myocardial Ischemia and Its Treatments

Xiang, M., Lu, Y., Xin, L., Gao, J., Shang, C., Jiang, Z., Lin, H., Fang, X., Qu, Y., Wang, Y., et al. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/6614009 · Cited by 309

The NADPH Oxidase Subunit NOX4 Is a New Target Gene of the Hypoxia-inducible Factor-1

Diebold, I., Petry, A., Hess, J., & Görlach, A. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-12-1003 · Cited by 296

NADPH Oxidase 4 Promotes Endothelial Angiogenesis Through Endothelial Nitric Oxide Synthase Activation

Craige, S. M., Chen, K., Pei, Y., Li, C., Huang, X., Chen;, C., Shibata, R., Sato, K., Walsh, K., & Keaney, J. F. (2011) · Circulation · doi:10.1161/circulationaha.111.030775 · Cited by 283

Calcium-Dependent NOX5 Nicotinamide Adenine Dinucleotide Phosphate Oxidase Contributes to Vascular Oxidative Stress in Human Coronary Artery Disease

Guzik, T. J., Chen, W., Gongora, M. C., Guzik, B., Lob, H. E., Mangalat, D., Hoch, N., Dikalov, S., Rudzinski, P., Kapelak, B., et al. (2008) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2008.07.063 · Cited by 281

Nox1-dependent Reactive Oxygen Generation Is Regulated by Rac1

Cheng, G., Diebold, B. A., Hughes, Y., & Lambeth, J. D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512751200 · Cited by 285

Cell Signaling through Protein Kinase C Oxidation and Activation

Cosentino‐Gomes, D., Rocco-Machado, N., & Meyer‐Fernandes, J. R. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms130910697 · Cited by 276

NADPH oxidases in cardiovascular disease

Brandes, R. P., Weißmann, N., & Schröder, K. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.04.030 · Cited by 273

Oxidative Stress in Pulmonary Fibrosis

Otoupalova, E., Smith, S., Cheng, G., & Thannickal, V. J. (2020) · Comprehensive physiology · doi:10.1002/cphy.c190017 · Cited by 312

Role of Nox Family NADPH Oxidases in Host Defense

Leto, T. L., & Geiszt, M. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1549 · Cited by 266

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

Monoamine oxidases as sources of oxidants in the heart

Kaludercic, N., Mialet‐Perez, J., Paolocci, N., Parini, A., & Lisa, F. D. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2013.12.032 · Cited by 253

Oxidases and peroxidases in cardiovascular and lung disease: New concepts in reactive oxygen species signaling

Ghouleh, I. A., Khoo, N. K. H., Knaus, U. G., Griendling, K. K., Touyz, R. M., Thannickal, V. J., Barchowsky, A., Nauseef, W. M., Kelley, E. E., Bauer, P. M., et al. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.06.011 · Cited by 252

VEGF Signaling Through NADPH Oxidase-Derived ROS

Ushio‐Fukai, M. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1556 · Cited by 246

NOX2 and NOX4 Mediate Proliferative Response in Endothelial Cells

Petry, A., Djordjevic, T., Weitnauer, M., Kietzmann, T., Hess, J., & Görlach, A. (2006) · Antioxidants & Redox Signaling · doi:10.1089/ars.2006.8.1473 · Cited by 243

Tks5-Dependent, Nox-Mediated Generation of Reactive Oxygen Species Is Necessary for Invadopodia Formation

Diaz, B., Shani, G., Pass, I., Anderson, D., Quintavalle, M., & Courtneidge, S. A. (2009) · Science Signaling · doi:10.1126/scisignal.2000368 · Cited by 242

NADPH oxidases in the vasculature: Molecular features, roles in disease and pharmacological inhibition

Selemidis, S., Sobey, C. G., Wingler, K., Schmidt, H. H. H. W., & Drummond, G. R. (2008) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2008.08.005 · Cited by 249

Modulation of Vascular Smooth Muscle Signaling by Reactive Oxygen Species

Lyle, A. N., & Griendling, K. K. (2006) · Physiology · doi:10.1152/physiol.00004.2006 · Cited by 247

NADPH oxidase 4 is an oncoprotein localized to mitochondria

Graham, K., Kulawiec, M., Owens, K. M., Li, X., Desouki, M. M., Chandra, D., & Singh, K. K. (2010) · Cancer Biology & Therapy · doi:10.4161/cbt.10.3.12207 · Cited by 240

NADPH oxidases and cancer

Roy, K., Wu, Y., Meitzler, J. L., Juhasz, A. N., Liu, H., Jiang, G., Lu, J., Antony, S., & Doroshow, J. H. (2015) · Clinical Science · doi:10.1042/cs20140542 · Cited by 230

Metformin attenuates lung fibrosis development via NOX4 suppression

Sato, N., Takasaka, N., Yoshida, M., Tsubouchi, K., Minagawa, S., Araya, J., Saito, N., Fujita, Y., Kurita, Y., Kobayashi, K., et al. (2016) · Respiratory Research · doi:10.1186/s12931-016-0420-x · Cited by 233

Upregulation of the NADPH oxidase NOX4 by TGF-beta in hepatocytes is required for its pro-apoptotic activity

Carmona‐Cuenca, I., Roncero, C., Sancho, P., Caja, L., Fausto, N., Fernández, M., & Fabregat, I. (2008) · Journal of Hepatology · doi:10.1016/j.jhep.2008.07.021 · Cited by 224

Analysis of dihydroethidium fluorescence for the detection of intracellular and extracellular superoxide produced by NADPH oxidase

Peshavariya, H., Dusting, G. J., & Selemidis, S. (2007) · Free Radical Research · doi:10.1080/10715760701297354 · Cited by 221

Role of NADPH Oxidases in Liver Fibrosis

Paik, Y., Kim, J., Aoyama, T., Minicis, S. D., Bataller, R. A., & Brenner, D. A. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5619 · Cited by 223

Nox4-Derived H2O2 Mediates Endoplasmic Reticulum Signaling through Local Ras Activation

Wu, R. F., Ma, Z., Liu, Z., & Terada, L. S. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01445-09 · Cited by 221

Hydrogen peroxide signaling in vascular endothelial cells

Bretón‐Romero, R., & Lamas, S. (2014) · Redox Biology · doi:10.1016/j.redox.2014.02.005 · Cited by 227

NADPH oxidases: New kids on the block

Geiszt, M. (2006) · Cardiovascular Research · doi:10.1016/j.cardiores.2006.05.004 · Cited by 221

Oxidative stress in atrial fibrillation: An emerging role of NADPH oxidase

Youn, J.-Y., Zhang, J., Zhang, Y., Chen, H., Liu, D., Ping, P., Weiss, J. N., & Cai, H. “. (2013) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2013.04.019 · Cited by 219

Analysis of DHE-derived oxidation products by HPLC in the assessment of superoxide production and NADPH oxidase activity in vascular systems

Fernandes, D. C., Wosniak, J., Pescatore, L. A., Bertoline, M. A., Liberman, M., Laurindo, F. R. M., & Santos, C. X. C. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00188.2006 · Cited by 213

Specificity in reactive oxidant signaling: think globally, act locally

Terada, L. S. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200605036 · Cited by 215

The role of oxidative stress and NADPH oxidase in cerebrovascular disease

Chrissobolis, S., & Faraci, F. M. (2008) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2008.09.003 · Cited by 212

NADPH oxidase activity and function are profoundly greater in cerebral versus systemic arteries

Miller, A. A., Drummond, G. R., Schmidt, H. H. H. W., & Sobey, C. G. (2005) · Circulation Research · doi:10.1161/01.res.0000189301.10217.87 · Cited by 211

Cannabidiol-Induced Apoptosis in Human Leukemia Cells: A Novel Role of Cannabidiol in the Regulation of p22 and Nox4 Expression

McKallip, R. J., Jia, W., Schlomer, J., Warren, J. W., Nagarkatti, P. S., & Nagarkatti, M. (2006) · Molecular Pharmacology · doi:10.1124/mol.106.023937 · Cited by 230

Structural Insights into Nox4 and Nox2: Motifs Involved in Function and Cellular Localization

von Löhneysen, K., Noack, D., Wood, M. R., Friedman, J. S., & Knaus, U. G. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01393-09 · Cited by 127

NOX family: the ROS producer in plasma membrane

Li, L. (2005)

NADPH oxidase 4 function as a hydrogen peroxide sensor

Nisimoto, Y., Ogawa, H., Kadokawa, Y., & Qiao, S. (2018) · The Journal of Biochemistry · doi:10.1093/jb/mvy014 · Cited by 10

Molecular composition and regulation of the Nox family NAD(P)H oxidases

Sumimoto, H., Miyano, K., & Takeya, R. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.08.210 · Cited by 306

Point Mutations in the Proline-rich Region of p22 Are Dominant Inhibitors of Nox1- and Nox2-dependent Reactive Oxygen Generation

Kawahara, T., Ritsick, D., Cheng, G., & Lambeth, J. D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501882200 · Cited by 231