NOX enzymes and the biology of reactive oxygen
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In non-phagocytic cells, NADP oxidase is represented by NOX (non-phagocytic NADPH oxidase), enzymes producing small constitutive pulses of O2•−, which are key players in cell signalling.
“In the rest of the non-phagocytic cells, NADP oxidase is represented by NOX (non-phagocytic NADPH oxidase), enzymes producing small constitutive pulses of O2•−, which are key players in cell signalling [30], Figure 12.”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [30]
No off-target effects were detected against a panel of 135 enzymes, including XO and eNOS, for GKT-136901.
“No off-target effects were detected against a panel of 135 enzymes, including XO and eNOS (545).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [545]
GKT-136901 was first characterized as a selective NOX1 and NOX4 inhibitor, although it can also inhibit NOX2 at higher concentrations.
“GKT-136901 was first characterized as a selective NOX1 and NOX4 inhibitor, although it can also inhibit NOX 2 at higher concentrations (545).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [545]
Cites
McCord, J. M., & Fridovich, I. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63504-5 · Cited by 12,952 · see citing works
Production of large amounts of hydrogen peroxide by human tumor cells.
Szatrowski, T. P., & Nathan, C. (1991) · PubMed · Cited by 2,504 · see citing works
Cell transformation by the superoxide-generating oxidase Mox1
Suh, Y.-A., Arnold, R. S., Lassegue, B., Shi, J., Xu, X., Sorescu, D., Chung, A. B., Griendling, K. K., & Lambeth, J. D. (1999) · Nature · doi:10.1038/43459 · Cited by 1,480 · see citing works
Self-citationSuperoxide 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 1,166 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Lee, S.-R., Kwon, K.-S., Kim, S.-R., & Rhee, S. G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.25.15366 · Cited by 969 · see citing works
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 · see citing works
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
Self-citationSuperoxide Production and Expression of Nox Family Proteins in Human Atherosclerosis
Sorescu, D., Weiss, D., Lassègue, B., Clempus, R. E., Szöcs, K., Sorescu, G. P., Valppu, L., Quinn, M. T., Lambeth, J. D., Vega, J. D., et al. (2002) · Circulation · doi:10.1161/01.cir.0000012917.74432.66 · Cited by 847 · see citing works
Self-citationIdentification 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 · see citing works
Lassègue, B., Sorescu, D., Szöcs, K., Yin, Q., Akers, M., Zhang, Y., Grant, S. L., Lambeth, J. D., & Griendling, K. K. (2001) · Circulation Research · doi:10.1161/hh0901.090299 · Cited by 839 · see citing works
Self-citationHomologs 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 · see citing works
Self-citationThe 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 773 · 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
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 · see citing works
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 · see citing works
Distinct Subcellular Localizations of Nox1 and Nox4 in Vascular Smooth Muscle Cells
Hilenski, L. L., Clempus, R. E., Quinn, M. T., Lambeth, J. D., & Griendling, K. K. (2004) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/01.atv.0000112024.13727.2c · Cited by 573 · see citing works
Self-citationA 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 · see citing works
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 · see citing works
Self-citationDual 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 505 · see citing works
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 · see citing works
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 · see citing works
Self-citationHydrogen 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 · see citing works
Self-citationInactivating 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 481 · see citing works
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 · see citing works
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 444 · see citing works
Self-citationMolecular 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 · see citing works
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 · see citing works
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 · see citing works
Self-citationLambeth, 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 · see citing works
Self-citationEvidence 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 · see citing works
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 332 · see citing works
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 314 · see citing works
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 · see citing works
Geiszt, M., Lekstrom, K., Witta, J., & Leto, T. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301289200 · Cited by 280 · see citing works
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 · see citing works
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 269 · see citing works
Singlet oxygen production by biological systems
Kanofsky, J. R. (1989) · Chemico-Biological Interactions · doi:10.1016/0009-2797(89)90059-8 · Cited by 259 · see citing works
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 259 · see citing works
Self-citationKoga, 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 · see citing works
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 · see citing works
Self-citationAgo, 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 · see citing works
Cheng, G., & Lambeth, J. D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m305968200 · Cited by 209 · see citing works
Self-citationThe 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 204 · see citing works
Self-citationGeiszt, 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 201 · see citing works
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 · see citing works
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 · see citing works
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 178 · see citing works
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 · see citing works
Eklund, E. A., Jalava, A., & Kakar, R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.22.13957 · Cited by 176 · see citing works
Roos, D., & Winterbourn, C. C. (2002) · Science · doi:10.1126/science.1071271 · Cited by 170 · see citing works
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 · see citing works
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 · see citing works
Fu, X., Kassim, S. Y., Parks, W. C., & Heinecke, J. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304739200 · Cited by 152 · see citing works
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 · see citing works
The NADPH oxidase and chronic granulomatous disease
Segal, A. W. (1996) · Molecular Medicine Today · doi:10.1016/1357-4310(96)88723-5 · Cited by 128 · see citing works
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 · see citing works
Chamulitrat, W., Schmidt, R., Tomakidi, P., Stremmel, W., Chunglok, W., Kawahara, T., & Rokutan, K. (2003) · Oncogene · doi:10.1038/sj.onc.1206654 · Cited by 108 · see citing works
NADPH Oxidase Is Involved in Prostaglandin F2α-induced Hypertrophy of Vascular Smooth Muscle Cells
Katsuyama, M., Fan, C., & Yabe-Nishimura, C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111634200 · Cited by 95 · see citing works
Teshima, S., Rokutan, K., Nikawa, T., & Kishi, K. (1998) · Gastroenterology · doi:10.1016/s0016-5085(98)70090-3 · Cited by 90 · see citing works
Perner, A., Andresen, L. O., Pedersen, G., & Rask-Madsen, J. (2003) · Gut · doi:10.1136/gut.52.2.231 · Cited by 72 · see citing works
Role of NADPH Oxidases in the Control of Vascular Gene Expression
Brandes, R. (2003) · Antioxidants and Redox Signaling · doi:10.1089/152308603770380115 · Cited by 71 · see citing works
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 · see citing works
Catalytic Antibody Bridges Innate and Adaptive Immunity
Nathan, C. (2002) · Science · doi:10.1126/science.1080005 · Cited by 32 · see citing works
Yaffe, M. B. (2002) · Structure · doi:10.1016/s0969-2126(02)00860-2 · Cited by 18 · see citing works
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Bedard, K., & Krause, K.-H. (2007) · Physiological Reviews · doi:10.1152/physrev.00044.2005 · Cited by 6,989 · see citing works
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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 · see citing works
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Balaban, R. S., Nemoto, S., & Finkel, T. (2005) · Cell · doi:10.1016/j.cell.2005.02.001 · Cited by 4,388 · see citing works
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 · see citing works
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Forman, H. J., & Zhang, H. (2021) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00233-1 · Cited by 2,900 · see citing works
Reconciling the chemistry and biology of reactive oxygen species
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West, A. P., Brodsky, I. E., Rahner, C., Woo, D. K., Erdjument-Bromage, H., Tempst, P., Walsh, M. C., Choi, Y., Shadel, G. S., & Ghosh, S. (2011) · Nature · doi:10.1038/nature09973 · Cited by 1,659 · see citing works
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Simpson, D. S. A., & Oliver, P. L. (2020) · Antioxidants · doi:10.3390/antiox9080743 · Cited by 1,044 · see citing works
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Gutscher, M., Pauleau, A.-L., Marty, L., Brach, T., Wabnitz, G. H., Samstag, Y., Meyer, A. J., & Dick, T. P. (2008) · Nature Methods · doi:10.1038/nmeth.1212 · Cited by 894 · see citing works
Bulua, A. C., Simon, A., Maddipati, R., Pelletier, M., Park, H., Kim, K.-Y., Sack, M. N., Kastner, D. L., & Siegel, R. M. (2011) · Journal of Experimental Medicine · doi:10.1084/jem.20102049 · Cited by 860 · see citing works
NADPH oxidase-4 mediates myofibroblast activation and fibrogenic responses to lung injury
Hecker, L., Vittal, R., Jones, T., Jagirdar, R., Luckhardt, T. R., Horowitz, J. C., Pennathur, S., Martinez, F. J., & Thannickal, V. J. (2009) · Nature Medicine · doi:10.1038/nm.2005 · Cited by 852 · see citing works
Cruz, C. M., Rinna, A., Forman, H. J., Ventura, A. L. M., Persechini, P. M., & Ojcius, D. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608083200 · Cited by 786 · see citing works
Redox-based regulation of signal transduction: principles, pitfalls, and promises
Janssen-Heininger, Y. M. W., Mossman, B. T., Heintz, N. H., Forman, H. J., Kalyanaraman, B., Finkel, T., Stamler, J. S., Rhee, S. G., & van der Vliet, A. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.03.011 · Cited by 784 · see citing works
Neutrophils to the ROScue: Mechanisms of NADPH oxidase activation and bacterial resistance
Nguyen, G. T., Green, E. R., & Mecsas, J. (2017) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2017.00373 · Cited by 741 · see citing works
NADPH Oxidases (NOX): An Overview from Discovery, Molecular Mechanisms to Physiology and Pathology
Vermot, A., Petit-Härtlein, I., Smith, S. M. E., & Fieschi, F. (2021) · Antioxidants · doi:10.3390/antiox10060890 · Cited by 766 · see citing works
Dual-specificity phosphatases: critical regulators with diverse cellular targets
Patterson, K. I., Brummer, T., O'brien, P. M., & Daly, R. J. (2009) · Biochemical Journal · doi:10.1042/bj20082234 · Cited by 744 · see citing works
Reactive oxygen species (ROS) in macrophage activation and function in diabetes
Rendra, E., Riabov, V., Mossel, D. M., Sevastyanova, T., Harmsen, M. C., & Kzhyshkowska, J. (2019) · Immunobiology · doi:10.1016/j.imbio.2018.11.010 · Cited by 636 · see citing works
Jones, D. P., & Sies, H. (2015) · Antioxidants & Redox Signaling · doi:10.1089/ars.2015.6247 · Cited by 647 · see citing works
Reactive Oxygen Species in the Regulation of Synaptic Plasticity and Memory
Massaad, C. A., & Klann, E. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3208 · Cited by 635 · see citing works
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 · see citing works
Kwon, J., Lee, S.-R., Yang, K.-S., Ahn, Y., Kim, Y. J., Stadtman, E. R., & Rhee, S. G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407396101 · Cited by 631 · see citing works
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 · see citing works
Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides
Rhee, S. G., Woo, H. A., Kil, I. S., & Bae, S. H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r111.283432 · Cited by 603 · see citing works
Linking oxidative stress to inflammation: Toll-like receptors
Gill, R., Tsung, A., & Billiar, T. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.01.006 · Cited by 553 · see citing works
Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation
Tejero, J., Shiva, S., & Gladwin, M. T. (2019) · Physiological Reviews · doi:10.1152/physrev.00036.2017 · Cited by 541 · see citing works
Nox enzymes and new thinking on reactive oxygen: A double-edged sword revisited
Lambeth, J. D., & Neish, A. S. (2014) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-012513-104651 · Cited by 495 · see citing works
Self-citationShields, H. J., Traa, A., & Van Raamsdonk, J. M. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.628157 · Cited by 478 · see citing works
Quinn, M. T., & Gauss, K. A. (2004) · Journal of Leukocyte Biology · doi:10.1189/jlb.0404216 · Cited by 480 · see citing works
Redox Reactions and Microbial Killing in the Neutrophil Phagosome
Winterbourn, C. C., & Kettle, A. J. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4827 · Cited by 468 · see citing works
Nox1 Is Involved in Angiotensin II–Mediated Hypertension: A Study in Nox1-Deficient Mice
Matsuno, K., Yamada, H., Iwata, K., Jin, D., Katsuyama, M., Matsuki, M., Takai, S., Yamanishi, K., Miyazaki, M., Matsubara, H., et al. (2005) · Circulation · doi:10.1161/circulationaha.105.573709 · Cited by 470 · see citing works
T cells express a phagocyte-type NADPH oxidase that is activated after T cell receptor stimulation
Jackson, S. H., Devadas, S., Kwon, J., Pinto, L. A., & Williams, M. S. (2004) · Nature Immunology · doi:10.1038/ni1096 · Cited by 457 · see citing works
Torti, S. V., Manz, D. H., Paul, B. T., Blanchette-Farra, N., & Torti, F. M. (2018) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-082117-051732 · Cited by 426 · see citing works
Reynaert, N. L., van der Vliet, A., Guala, A. S., McGovern, T., Hristova, M., Pantano, C., Heintz, N. H., Heim, J., Ho, Y.-S., Matthews, D. E., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603290103 · Cited by 442 · see citing works
Oxidative Stress, Chronic Disease, and Muscle Wasting
Moylan, J. S., & Reid, M. B. (2007) · Muscle & Nerve · doi:10.1002/mus.20743 · Cited by 416 · see citing works
Mitochondria in innate immune signaling
Banoth, B., & Cassel, S. L. (2018) · Translational Research · doi:10.1016/j.trsl.2018.07.014 · Cited by 410 · see citing works
Bubici, C., Papa, S., Dean, K., & Franzoso, G. (2006) · Oncogene · doi:10.1038/sj.onc.1209936 · Cited by 399 · see citing works
Rigoulet, M., Yoboue, E. D., & Devin, A. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3363 · Cited by 394 · see citing works
Espey, M. G. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.10.554 · Cited by 396 · see citing works
Rhee, S. G., Yang, K.-S., Kang, S. W., Woo, H. A., & Chang, T.-S. (2005) · Antioxidants & Redox Signaling · doi:10.1089/ars.2005.7.619 · Cited by 376 · see citing works
Dikalov, S. I., & Nazarewicz, R. R. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4604 · Cited by 356 · see citing works
Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity
Andrés, C. M. C., Pérez de la Lastra, J. M., Andrés Juan, C., Plou, F. J., & Pérez-Lebeña, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24031841 · Cited by 342 · see citing works
Reactive Oxygen Species Regulate T Cell Immune Response in the Tumor Microenvironment
Chen, X., Song, M., Zhang, B., & Zhang, Y. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/1580967 · Cited by 326 · see citing works
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 · see citing works
DNA damage induces reactive oxygen species generation through the H2AX-Nox1/Rac1 pathway
Kang, M. A., So, E.-Y., Simons, A. L., Spitz, D. R., & Ouchi, T. (2012) · Cell Death & Disease · doi:10.1038/cddis.2011.134 · Cited by 311 · see citing works
Beckhauser, T. F., Francis-Oliveira, J., & De Pasquale, R. (2016) · Journal of Experimental Neuroscience · doi:10.4137/jen.s39887 · Cited by 301 · see citing works
Vallet, P., Charnay, Y., Steger, K., Ogier-Denis, E., Kovari, E., Herrmann, F., Michel, J.-P., & Szanto, I. (2005) · Neuroscience · doi:10.1016/j.neuroscience.2004.12.038 · Cited by 291 · see citing works
The superoxide‐producing NAD(P)H oxidase Nox4 in the nucleus of human vascular endothelial cells
Kuroda, J., Nakagawa, K., Yamasaki, T., Nakamura, K., Takeya, R., Kuribayashi, F., Imajoh‐Ohmi, S., Igarashi, K., Shibata, Y., Sueishi, K., et al. (2005) · Genes to Cells · doi:10.1111/j.1365-2443.2005.00907.x · Cited by 275 · see citing works
Geng, J., Sun, X., Wang, P., Zhang, S., Wang, X., Wu, H., Hong, L., Xie, C., Li, X., Zhao, H., et al. (2015) · Nature Immunology · doi:10.1038/ni.3268 · Cited by 264 · see citing works
Meissner, F., Seger, R. A., Moshous, D., Fischer, A., Reichenbach, J., & Zychlinsky, A. (2010) · Blood · doi:10.1182/blood-2010-01-264218 · Cited by 269 · see citing works
T cells and reactive oxygen species
Belikov, A. V., Schraven, B., & Simeoni, L. (2015) · Journal of Biomedical Science · doi:10.1186/s12929-015-0194-3 · Cited by 264 · see citing works
Reactive oxygen species and insulin resistance: the good, the bad and the ugly
Tiganis, T. (2011) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2010.11.006 · Cited by 256 · see citing works
NOX5 variants are functionally active in endothelial cells
BelAiba, R. S., Djordjevic, T., Petry, A., Diemer, K., Bonello, S., Banfi, B., Hess, J., Pogrebniak, A., Bickel, C., & Görlach, A. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.10.054 · Cited by 255 · see citing works
Dual Oxidase-2 Has an Intrinsic Ca2+-dependent H2O2-generating Activity
Ameziane-El-Hassani, R., Morand, S., Boucher, J.-L., Frapart, Y.-M., Apostolou, D., Agnandji, D., Gnidehou, S., Ohayon, R., Noël-Hudson, M.-S., Francon, J., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500516200 · Cited by 248 · see citing works
Park, L., Anrather, J., Zhou, P., Frys, K., Pitstick, R., Younkin, S., Carlson, G. A., & Iadecola, C. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.5207-04.2005 · Cited by 244 · see citing works
Diaz, B., Shani, G., Pass, I., Anderson, D., Quintavalle, M., & Courtneidge, S. A. (2009) · Science Signaling · doi:10.1126/scisignal.2000368 · Cited by 242 · see citing works
Nrros negatively regulates reactive oxygen species during host defence and autoimmunity
Noubade, R., Wong, K., Ota, N., Rutz, S., Eidenschenk, C., Valdez, P. A., Ding, J., Peng, I., Sebrell, A., Caplazi, P., et al. (2014) · Nature · doi:10.1038/nature13152 · Cited by 246 · see citing works
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 · see citing works
Oxidative stress in chronic venous leg ulcers
Wlaschek, M., & Scharffetter‐Kochanek, K. (2005) · Wound Repair and Regeneration · doi:10.1111/j.1067-1927.2005.00065.x · Cited by 241 · see citing works
Radical medicine: treating ageing to cure disease
Finkel, T. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1763 · Cited by 234 · see citing works
Redox activation of Nrf2 & NF-κB: A double end sword?
Buelna-Chontal, M., & Zazueta, C. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.08.007 · Cited by 239 · see citing works
Wilson, C., & González-Billault, C. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00381 · Cited by 238 · see citing works
Mechanisms of Statin-mediated Inhibition of Small G-protein Function
Cordle, A., Koenigsknecht-Talboo, J., Wilkinson, B., Limpert, A., & Landreth, G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505268200 · Cited by 235 · see citing works
Chen, Y., Okano, K., Maeda, T., Chauhan, V., Golczak, M., Maeda, A., & Palczewski, K. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.315432 · Cited by 229 · see citing works
McAllister, S. D., Murase, R., Christian, R. T., Lau, D., Zielinski, A. J., Allison, J., Almanza, C., Pakdel, A., Lee, J., Limbad, C., et al. (2011) · Breast Cancer Research and Treatment · doi:10.1007/s10549-010-1177-4 · Cited by 229 · see citing works
Neutrophils: important contributors to tumor progression and metastasis
Swierczak, A., Mouchemore, K. A., Hamilton, J. A., & Anderson, R. L. (2015) · Cancer and Metastasis Reviews · doi:10.1007/s10555-015-9594-9 · Cited by 220 · see citing works
Li, Q., & Engelhardt, J. F. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511153200 · Cited by 219 · see citing works
Nox enzymes as novel targets for drug development
Lambeth, J. D., Krause, K.-H., & Clark, R. A. (2008) · Seminars in Immunopathology · doi:10.1007/s00281-008-0123-6 · Cited by 212 · see citing works
Self-citationNovel Mechanism of Activation of NADPH Oxidase 5
Jagnandan, D., Church, J. E., Banfi, B., Stuehr, D. J., Marrero, M. B., & Fulton, D. J. R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608966200 · Cited by 210 · see citing works
Dijkhoff, I. M., Drasler, B., Karakocak, B. B., Petri-Fink, A., Valacchi, G., Eeman, M., & Rothen-Rutishauser, B. (2020) · Particle and Fibre Toxicology · doi:10.1186/s12989-020-00366-y · Cited by 202 · see citing works
Valencia, A., & Kochevar, I. E. (2008) · Journal of Investigative Dermatology · doi:10.1038/sj.jid.5700960 · Cited by 194 · see citing works
Gianni, D., Taulet, N., Zhang, H., DerMardirossian, C., Kister, J., Martinez, L., Roush, W. R., Brown, S. J., Bokoch, G. M., & Rosen, H. (2010) · ACS Chemical Biology · doi:10.1021/cb100219n · Cited by 192 · see citing works
Lee, S. B., Bae, I. H., Bae, Y. S., & Um, H.-D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606702200 · Cited by 187 · see citing works
Redox regulation of the hypoxia-inducible factor
Pouysségur, J., & Mechta-Grigoriou, F. (2006) · Biological Chemistry · doi:10.1515/bc.2006.167 · Cited by 186 · see citing works
Handy, D. E., Lubos, E., Yang, Y., Galbraith, J. D., Kelly, N., Zhang, Y.-Y., Leopold, J. A., & Loscalzo, J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900392200 · Cited by 187 · see citing works
Sakellariou, G. K., Jackson, M. J., & Vasilaki, A. (2014) · Free Radical Research · doi:10.3109/10715762.2013.830718 · Cited by 184 · see citing works
Ismail, S., Sturrock, A., Wu, P., Cahill, B., Norman, K., Huecksteadt, T., Sanders, K., Kennedy, T., & Hoidal, J. (2009) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.90488.2008 · Cited by 177 · see citing works
Bettaieb, A., Jiang, J. X., Sasaki, Y., Chao, T.-I., Kiss, Z., Chen, X., Tian, J., Katsuyama, M., Yabe-Nishimura, C., Xi, Y., et al. (2015) · Gastroenterology · doi:10.1053/j.gastro.2015.04.009 · Cited by 167 · see citing works
Haslund‐Vinding, J., McBean, G., Jaquet, V, & Vilhardt, F. (2017) · British Journal of Pharmacology · doi:10.1111/bph.13425 · Cited by 169 · see citing works
Disruption of mitochondrial redox circuitry in oxidative stress
Jones, D. P. (2006) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2006.07.008 · Cited by 176 · see citing works
Nadph oxidase-1 plays a crucial role in hyperoxia-induced acute lung injury in mice
Carnesecchi, S., Deffert, C., Pagano, A., Garrido-Urbani, S., Métrailler-Ruchonnet, I., Schäppi, M., Donati, Y., Matthay, M. A., Krause, K.-H., & Barazzone Argiroffo, C. (2009) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200902-0296oc · Cited by 160 · see citing works
Therapeutic potential of nadph oxidase 1/4 inhibitors
Teixeira, G., Szyndralewiez, C., Molango, S., Carnesecchi, S., Heitz, F., Wiesel, P., & Wood, J. M. (2017) · British Journal of Pharmacology · doi:10.1111/bph.13532 · Cited by 163 · see citing works
Constitutive NADPH-Dependent Electron Transferase Activity of the Nox4 Dehydrogenase Domain
Nisimoto, Y., Jackson, H. M., Ogawa, H., Kawahara, T., & Lambeth, J. D. (2010) · Biochemistry · doi:10.1021/bi9022285 · Cited by 161 · see citing works
Self-citationMcLennan, Y., Polussa, J., Tassone, F., & Hagerman, R. (2011) · Current Genomics · doi:10.2174/138920211795677886 · Cited by 160 · see citing works
- Authors
- Lambeth, J. D.
- Affiliations
- Emory University (US)
- Corresponding author
- Lambeth, J. David
- Venue
- Nature Reviews Immunology
- Published
- 2004-03
- Volume
- 4
- Issue
- 3
- Pages
- 181-189
- ISSN
- 1474-1733 (ISSN-L)
- 1474-1741
- OpenAlex
- W2102619095
- Cited by
- 3,125
- References
- 68
- Citations by year
- 2026: 72 · 2025: 83 · 2024: 79 · 2023: 119 · 2022: 125 · 2021: 131 · 2020: 133 · 2019: 152 · 2018: 122 · 2017: 153 · 2016: 151 · 2015: 150 · 2014: 185 · 2013: 181 · 2012: 173
- FWCI
- 11.09
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature reviews. Immunology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Keywords
- NADPH oxidase, gp91phox, reactive oxygen species, superoxide, phagocytes, innate immunity, signal transduction, extracellular matrix modification, non-phagocytic cells
- MeSH terms
- Animals, Cell Division, Humans, Phagocytes, Signal Transduction, Apoptosis, Reactive Oxygen Species, NADPH Oxidases
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