NOX enzymes and the biology of reactive oxygen

Superoxide Dismutase

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

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Cell transformation by the superoxide-generating oxidase Mox1

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Superoxide and hydrogen peroxide in relation to mammalian cell proliferation

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

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Reversible Inactivation of the Tumor Suppressor PTEN by H2O2

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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

The AMP-Activated Protein Kinase Plays a Role in Antioxidant Defense and Regulation of Vascular Inflammation

Jansen, T., Kvandová, M., Daiber, A., Stamm, P., Frenis, K., Schulz, E., Münzel, T., & Kröller-Schön, S. (2020) · Antioxidants · doi:10.3390/antiox9060525 · Cited by 68

Chemical physiology of oxidative stress-activated TRPM2 and TRPC5 channels

Yamamoto, S., Takahashi, N., & Mori, Y. (2010) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2010.05.005 · Cited by 67

Pre‐clinical evidence of a dual NADPH oxidase 1/4 inhibitor (setanaxib) in liver, kidney and lung fibrosis

Thannickal, V. J., Jandeleit‐Dahm, K., Szyndralewiez, C., & Török, N. J. (2023) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.17649 · Cited by 65

Identification of the Binding Site for the Regulatory Calcium-Binding Domain in the Catalytic Domain of NOX5

Tirone, F., Radu, L., Craescu, C. T., & Cox, J. A. (2010) · Biochemistry · doi:10.1021/bi901846y · Cited by 63

NADPH Oxidase and Guanylate Binding Protein 5 Restrict Survival of Avirulent Type III Strains of Toxoplasma gondii in Naive Macrophages

Matta, S. K., Patten, K., Wang, Q., Kim, B.-H., MacMicking, J. D., & Sibley, L. D. (2018) · mBio · doi:10.1128/mbio.01393-18 · Cited by 52

The intestinal microbiota are necessary for stressor-induced enhancement of splenic macrophage microbicidal activity

Allen, R. G., Lafuse, W. P., Galley, J. D., Ali, M. M., Ahmer, B. M. M., & Bailey, M. T. (2012) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2011.11.002 · Cited by 55

Positive regulation of NADPH oxidase 5 by proinflammatory-related mechanisms in human aortic smooth muscle cells

Manea, A., Manea, S. A., Florea, I. C., Luca, C. M., & Raicu, M. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.02.018 · Cited by 52

Nox-derived ROS are acutely activated in pressure overload pulmonary hypertension: indications for a seminal role for mitochondrial Nox4

Frazziano, G., Al Ghouleh, I., Baust, J., Shiva, S., Champion, H. C., & Pagano, P. J. (2014) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00977.2012 · Cited by 51

Nadph oxidase 4 is required for the generation of macrophage migration inhibitory factor and host defense against toxoplasma gondii infection

Kim, J. H., Lee, J., Bae, S.-J., Kim, Y., Park, B.-J., Choi, J.-W., Kwon, J., Cha, G.-H., Yoo, H. J., Jo, E.-K., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-06610-4 · Cited by 45

The mitochondrial reactive oxygen species regulator p66Shc controls PDGF-induced signaling and migration through protein tyrosine phosphatase oxidation

Frijhoff, J., Dagnell, M., Augsten, M., Beltrami, E., Giorgio, M., & Östman, A. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.12.022 · Cited by 43

TNFα-induced lysosomal membrane permeability (LMP) is downstream of MOMP and triggered by caspase-mediated p75 cleavage and ROS formation

Huai, J., Vögtle, F.-N., Jöckel, L., Li, Y., Kiefer, T., Ricci, J.-E., & Borner, C. (2013) · Journal of Cell Science · doi:10.1242/jcs.129999 · Cited by 43

Arginase 2 and nitric oxide synthase: Pathways associated with the pathogenesis of thyroid tumors

Sousa, M. S. A., Latini, F. R. M., Monteiro, H. P., & Cerutti, J. M. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.06.006 · Cited by 39

Application of Antioxidant Compounds in Bone Defect Repair

Wang, J., Zhang, Y., Tang, Q., Zhang, Y., Yin, Y., & Chen, L. (2024) · Antioxidants · doi:10.3390/antiox13070789 · Cited by 39

Diabetes-induced oxidative stress mediates upregulation of RhoA/Rho kinase pathway and hypercontractility of gastric smooth muscle

Mahavadi, S., Sriwai, W., Manion, O., Grider, J. R., & Murthy, K. S. (2017) · PLoS ONE · doi:10.1371/journal.pone.0178574 · Cited by 31

Screening Assay for Metal-Catalyzed Oxidation Inhibitors Using Liquid Chromatography−Mass Spectrometry with an N-Terminal β-Amyloid Peptide

Inoue, K., Nakagawa, A., Hino, T., & Oka, H. (2009) · Analytical Chemistry · doi:10.1021/ac802162n · Cited by 32

Endothelial NADPH oxidase 2: when does it matter in atherosclerosis?

Haendeler, J., Eckers, A., Lukosz, M., Unfried, K., & Altschmied, J. (2012) · Cardiovascular Research · doi:10.1093/cvr/cvs106 · Cited by 15

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)