NOX enzymes and the biology of reactive oxygen

Superoxide Dismutase

McCord, J. M., & Fridovich, I. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63504-5 · Cited by 12,952

Production of large amounts of hydrogen peroxide by human tumor cells.

Szatrowski, T. P., & Nathan, C. (1991) · PubMed · Cited by 2,504

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

Superoxide and hydrogen peroxide in relation to mammalian cell proliferation

Burdon, R. H. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(94)00198-s · Cited by 1,174

Killing activity of neutrophils is mediated through activation of proteases by K+ flux

Reeves, E. P., Lu, H., Jacobs, H. L., Messina, C. G. M., Bolsover, S., Gabella, G., Potma, E. O., Warley, A., Roes, J., & Segal, A. W. (2002) · Nature · doi:10.1038/416291a · Cited by 1,153

Reversible Inactivation of the Tumor Suppressor PTEN by H2O2

Lee, S.-R., Yang, K., Kwon, J., Lee, C., Jeong, W., & Rhee, S. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111899200 · Cited by 1,061

Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo

Meng, T.-C., Fukada, T., & Tonks, N. K. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00445-8 · Cited by 1,040

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

Activation of the NADPH oxidase involves the small GTP-binding protein p21rac1

Abo, A., Pick, E., Hall, A., Totty, N. F., Teahan, C. G., & Segal, A. W. (1991) · Nature · doi:10.1038/353668a0 · Cited by 954

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

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

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

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

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

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

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

A Ca2+-activated NADPH Oxidase in Testis, Spleen, and Lymph Nodes

Bánfi, B., Molnár, G., Maturana, A., Steger, K., Hegedûs, B., Demaurex, N., & Krause, K.-H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103034200 · Cited by 622

The PX domains of p47phox and p40phox bind to lipid products of PI(3)K

Kanai, F., Liu, H., Field, S. J., Akbary, H., Matsuo, T., Brown, G. E., Cantley, L. C., & Yaffe, M. B. (2001) · Nature Cell Biology · doi:10.1038/35083070 · Cited by 611

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

A Novel Superoxide-producing NAD(P)H Oxidase in Kidney

Shiose, A., Kuroda, J., Tsuruya, K., Hirai, M., Hirakata, H., Naito, S., Hattori, M., Sakaki, Y., & Sumimoto, H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007597200 · Cited by 517

Dual oxidases represent novel hydrogen peroxide sources supporting mucosal surface host defense

Geiszt, M., Witta, J., Baff, J., Lekstrom, K. J., & Leto, T. L. (2003) · The FASEB Journal · doi:10.1096/fj.02-1104fje · Cited by 515

The NAD(P)H Oxidase Homolog Nox4 Modulates Insulin-Stimulated Generation of H2O2 and Plays an Integral Role in Insulin Signal Transduction

Mahadev, K., Motoshima, H., Wu, X., Ruddy, J. M., Arnold, R. S., Cheng, G., Lambeth, J. D., & Goldstein, B. J. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.5.1844-1854.2004 · Cited by 513

Inactivating Mutations in the Gene for Thyroid Oxidase 2 (THOX2) and Congenital Hypothyroidism

Moreno, J. C., Bikker, H., Kempers, M. J. E., van Trotsenburg, A. S. P., Baas, F., de Vijlder, J. J. M., Vulsma, T., & Ris‐Stalpers, C. (2002) · New England Journal of Medicine · doi:10.1056/nejmoa012752 · Cited by 496

Two Novel Proteins Activate Superoxide Generation by the NADPH Oxidase NOX1

Bánfi, B., Clark, R. A., Steger, K., & Krause, K.-H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200613200 · Cited by 491

Reactive oxygen generated by Nox1 triggers the angiogenic switch

Arbiser, J. L., Petros, J. A., Klafter, R., Govindajaran, B., McLaughlin, E. R., Brown, L. F., Cohen, C., Moses, M. A., Kilroy, S. M., Arnold, R. S., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.022630199 · Cited by 489

Hydrogen peroxide mediates the cell growth and transformation caused by the mitogenic oxidase Nox1

Arnold, R. S., Shi, J., Murad, E., Whalen, A. M., Sun, C. Q., Polavarapu, R., Parthasarathy, S., Petros, J. A., & Lambeth, J. D. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.101505898 · Cited by 486

Purification of a Novel Flavoprotein Involved in the Thyroid NADPH Oxidase

Dupuy, C., Ohayon, R., Valent, A., Noël‐Hudson, M., Dème, D., & Virion, A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.52.37265 · Cited by 464

Upregulation of Nox-Based NAD(P)H Oxidases in Restenosis After Carotid Injury

Szöcs, K., Lassegue, B. P., Sorescu, D., Hilenski, L. L., Valppu, L., Couse, T. L., Wilcox, J. N., Quinn, M. T., Lambeth, J. D., & Griendling, K. K. (2002) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/hq0102.102189 · Cited by 443

Molecular Basis of Phosphorylation-Induced Activation of the NADPH Oxidase

Groemping, Y., Lapouge, K., Smerdon, S. J., & Rittinger, K. (2003) · Cell · doi:10.1016/s0092-8674(03)00314-3 · Cited by 408

Novel Human Homologues of p47 and p67 Participate in Activation of Superoxide-producing NADPH Oxidases

Takeya, R., Ueno, N., Kami, K., Taura, M., Kohjima, M., Izaki, T., Nunoi, H., & Sumimoto, H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212856200 · Cited by 380

Tyrosine cross-linking of extracellular matrix is catalyzed by Duox, a multidomain oxidase/peroxidase with homology to the phagocyte oxidase subunit gp91 phox

Edens, W. A., Sharling, L., Cheng, G., Shapira, R., Kinkade, J. M., Lee, T., Edens, H. A., Tang, X., Sullards, C., Flaherty, D. B., et al. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200103132 · Cited by 375

Novel homologs of gp91phox

Lambeth, J. D., Cheng, G., Arnold, R. S., & Edens, W. A. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01658-3 · Cited by 355

Evidence for Antibody-Catalyzed Ozone Formation in Bacterial Killing and Inflammation

Wentworth, P., McDunn, J. E., Wentworth, A. D., Takeuchi, C., Nieva, J. J., Jones, T., Bautista, C., Ruedi, J. M., Gutierrez, A., Janda, K. D., et al. (2002) · Science · doi:10.1126/science.1077642 · Cited by 349

Pulsatile Versus Oscillatory Shear Stress Regulates NADPH Oxidase Subunit Expression

Hwang, J., Ing, M. H., Salazar, A. M., Lassegue, B. P., Griendling, K. K., Navab, M., Sevanian, A., & Hsiai, T. K. (2003) · Circulation Research · doi:10.1161/01.res.0000104087.29395.66 · Cited by 339

Structure of the TPR Domain of p67phox in Complex with Rac·GTP

Lapouge, K., Smith, S. J. M., Walker, P. A., Gamblin, S. J., Smerdon, S. J., & Rittinger, K. (2000) · Molecular Cell · doi:10.1016/s1097-2765(05)00091-2 · Cited by 311

X-ray crystal structure of canine myeloperoxidase at 3 Å resolution

Zeng, J., & Fenna, R. E. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90133-5 · Cited by 310

Proteins Homologous to p47 and p67 Support Superoxide Production by NAD(P)H Oxidase 1 in Colon Epithelial Cells

Geiszt, M., Lekstrom, K., Witta, J., & Leto, T. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301289200 · Cited by 280

Lifespan Extension and Rescue of Spongiform Encephalopathy in Superoxide Dismutase 2 Nullizygous Mice Treated with Superoxide Dismutase–Catalase Mimetics

Melov, S., Doctrow, S. R., Schneider, J. A., Haberson, J., Patel, M., Coskun, P. E., Huffman, K. D., Wallace, D. C., & Malfroy, B. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-21-08348.2001 · Cited by 277

Upregulation of the vascular NAD(P)H-oxidase isoforms Nox1 and Nox4 by the renin-angiotensin system in vitro and in vivo

Wingler, K., Wünsch, S., Kreutz, R. H., Rothermund, L., Paul, M., & Schmidt, H. H. H. W. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00727-4 · Cited by 273

NOX5 NAD(P)H oxidase regulates growth and apoptosis in DU 145 prostate cancer cells

Brar, S. S., Corbin, Z. A., Kennedy, T. P., Hemendinger, R. A., Thornton, L., Bommarius, B., Arnold, R. S., Whorton, A. R., Sturrock, A., Huecksteadt, T. P., et al. (2003) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00525.2002 · Cited by 262

Singlet oxygen production by biological systems

Kanofsky, J. R. (1989) · Chemico-Biological Interactions · doi:10.1016/0009-2797(89)90059-8 · Cited by 259

Tetratricopeptide Repeat (TPR) Motifs of p67 Participate in Interaction with the Small GTPase Rac and Activation of the Phagocyte NADPH Oxidase

Koga, H., Terasawa, H., Nunoi, H., Takeshige, K., Inagaki, F., & Sumimoto, H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.35.25051 · Cited by 244

Regulation of the Neutrophil Respiratory Burst Oxidase

Han, C., Freeman, J. L. R., Lee, T., Motalebi, S. A., & Lambeth, J. D. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.27.16663 · Cited by 229

Phosphorylation of p47 phox directs phox homology domain from SH3 domain toward phosphoinositides, leading to phagocyte NADPH oxidase activation

Ago, T., Kuribayashi, F., Hiroaki, H., Takeya, R., Ito, T., Kohda, D., & Sumimoto, H. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0735712100 · Cited by 217

NOXO1, Regulation of Lipid Binding, Localization, and Activation of Nox1 by the Phox Homology (PX) Domain

Cheng, G., & Lambeth, J. D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m305968200 · Cited by 211

The p67 Activation Domain Regulates Electron Flow from NADPH to Flavin in Flavocytochromeb 558

Nisimoto, Y., Motalebi, S. A., Han, C., & Lambeth, J. D. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.33.22999 · Cited by 211

NAD(P)H Oxidase 1, a Product of Differentiated Colon Epithelial Cells, Can Partially Replace Glycoprotein 91 phox in the Regulated Production of Superoxide by Phagocytes

Geiszt, M., Lekstrom, K. J., Brenner, S., Hewitt, S. M., Dana, R., Malech, H. L., & Leto, T. L. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.171.1.299 · Cited by 207

An NAD(P)H oxidase regulates growth and transcription in melanoma cells

Brar, S. S., Kennedy, T. P., Sturrock, A., Huecksteadt, T. P., Quinn, M. T., Whorton, A. R., & Hoidal, J. R. (2002) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00496.2001 · Cited by 183

Type IHelicobacter pyloriLipopolysaccharide Stimulates Toll-Like Receptor 4 and Activates Mitogen Oxidase 1 in Gastric Pit Cells

Kawahara, T., Teshima, S., Oka, A., Sugiyama, T., Kishi, K., & Rokutan, K. (2001) · Infection and Immunity · doi:10.1128/iai.69.7.4382-4389.2001 · Cited by 181

Modulation of p47 PHOX activity by site-specific phosphorylation: Akt-dependent activation of the NADPH oxidase

Hoyal, C. R., Gutierrez, A., Young, B. M., Catz, S. D., Lin, J.-H., Tsichlis, P. N., & BABIOR, B. M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1031526100 · Cited by 179

Activation of the Leukocyte NADPH Oxidase by Phorbol Ester Requires the Phosphorylation of p47 on Serine 303 or 304

Inanami, O., Johnson, J. L., McAdara, J. K., Benna, J. E., Faust, L. R., Newburger, P. E., & BABIOR, B. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.16.9539 · Cited by 176

PU.1, Interferon Regulatory Factor 1, and Interferon Consensus Sequence-binding Protein Cooperate to Increase gp91 Expression

Eklund, E. A., Jalava, A., & Kakar, R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.22.13957 · Cited by 176

Lethal Weapons

Roos, D., & Winterbourn, C. C. (2002) · Science · doi:10.1126/science.1071271 · Cited by 170

Solution structure of the PX domain, a target of the SH3 domain.

Hiroaki, H., Ago, T., Ito, T., Sumimoto, H., & Kohda, D. (2001) · Nature Structural Biology · doi:10.1038/88591 · Cited by 169

Antibacterial activity of hydrogen peroxide and the lactoperoxidase-hydrogen peroxide-thiocyanate system against oral streptococci

Thomas, E. L., Milligan, T. W., Joyner, R. E., & Jefferson, M. M. (1994) · Infection and Immunity · doi:10.1128/iai.62.2.529-535.1994 · Cited by 155

Hypochlorous Acid Generated by Myeloperoxidase Modifies Adjacent Tryptophan and Glycine Residues in the Catalytic Domain of Matrix Metalloproteinase-7 (Matrilysin)

Fu, X., Kassim, S. Y., Parks, W. C., & Heinecke, J. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304739200 · Cited by 152

A Novel Assay System Implicates PtdIns(3,4)P2, PtdIns(3)P, and PKCδ in Intracellular Production of Reactive Oxygen Species by the NADPH Oxidase

Brown, G. E., Stewart, M. Q., Liu, H., Ha, V.-L., & Yaffe, M. B. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00005-4 · Cited by 139

The NADPH oxidase and chronic granulomatous disease

Segal, A. W. (1996) · Molecular Medicine Today · doi:10.1016/1357-4310(96)88723-5 · Cited by 130

The p40 and p47 PX Domains of NADPH Oxidase Target Cell Membranes via Direct and Indirect Recruitment by Phosphoinositides

Zhan, Y., Virbasius, J. V., Song, X., Pomerleau, D. P., & Zhou, G. W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109520200 · Cited by 115

Association of gp91phox homolog Nox1 with anchorage-independent growth and MAP kinase-activation of transformed human keratinocytes

Chamulitrat, W., Schmidt, R., Tomakidi, P., Stremmel, W., Chunglok, W., Kawahara, T., & Rokutan, K. (2003) · Oncogene · doi:10.1038/sj.onc.1206654 · Cited by 109

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

Guinea pig gastric mucosal cells produce abundant superoxide anion through an NADPH oxidase-like system

Teshima, S., Rokutan, K., Nikawa, T., & Kishi, K. (1998) · Gastroenterology · doi:10.1016/s0016-5085(98)70090-3 · Cited by 90

Superoxide production and expression of NAD(P)H oxidases by transformed and primary human colonic epithelial cells

Perner, A., Andresen, L. O., Pedersen, G., & Rask-Madsen, J. (2003) · Gut · doi:10.1136/gut.52.2.231 · Cited by 72

Role of NADPH Oxidases in the Control of Vascular Gene Expression

Brandes, R. P. (2003) · Antioxidants and Redox Signaling · doi:10.1089/152308603770380115 · Cited by 67

Regulation of growth and apoptosis of cultured guinea pig gastric mucosal cells by mitogenic oxidase 1

Teshima, S., Kutsumi, H., Kawahara, T., Kishi, K., & Rokutan, K. (2000) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.2000.279.6.g1169 · Cited by 63

Catalytic Antibody Bridges Innate and Adaptive Immunity

Nathan, C. (2002) · Science · doi:10.1126/science.1080005 · Cited by 32

The p47phox PX Domain

Yaffe, M. B. (2002) · Structure · doi:10.1016/s0969-2126(02)00860-2 · Cited by 19

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

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

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

Mitochondria, Oxidants, and Aging

Balaban, R. S., Nemoto, S., & Finkel, T. (2005) · Cell · doi:10.1016/j.cell.2005.02.001 · Cited by 4,388

Crosstalk of reactive oxygen species and NF-κB signaling

Morgan, M. J., & Liu, Z.-G. (2011) · Cell Research · doi:10.1038/cr.2010.178 · Cited by 3,505

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

The Nox Family of NAD(P)H Oxidases: Host Defense and Beyond

Geiszt, M., & Leto, T. L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.r400024200 · Cited by 464

Novel homologs of gp91phox

Lambeth, J. D., Cheng, G., Arnold, R. S., & Edens, W. A. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01658-3 · Cited by 355

Les Nox/Duox : une nouvelle famille de NADPH oxydases

Guichard, C., Pédruzzi, E., Fay, M., Mkaddem, S. B., Coant, N., Bleiberg-Daniel, F., & Ogier‐Denis, É. (2006) · médecine/sciences · doi:10.1051/medsci/20062211953 · Cited by 94

The Role of Reactive Oxygen Species

Cope, A. P. (2013)