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

The role of Cu/Zn-SOD and Mn-SOD in the immune response to oxidative stress and pathogen challenge in the clam Meretrix meretrix

Lu, X., Wang, C., & Liu, B. (2014) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2014.10.027 · Cited by 150

Reversible inactivation of deubiquitinases by reactive oxygen species in vitro and in cells

Lee, J., Baek, K., Soetandyo, N., & Ye, Y. (2013) · Nature Communications · doi:10.1038/ncomms2532 · Cited by 149

Connecting the “Dots”: From Free Radical Lipid Autoxidation to Cell Pathology and Disease

Foret, M. K., Lincoln, R., Carmo, S. D., Cuello, A. C., & Cosa, G. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.0c00761 · Cited by 150

In-situ production of singlet oxygen by dioxygen activation on iron phosphide for advanced oxidation processes

Zheng, N., He, X. S., Hu, R., Wang, R., Zhou, Q., Lian, Y., & Hu, Z. (2022) · Applied Catalysis B: Environmental · doi:10.1016/j.apcatb.2022.121157 · Cited by 150

Effects of domestic cooking process on the chemical and biological properties of dietary phytochemicals

Zhao, C., Liu, Y., Lai, S., Cao, H., Guan, Y., Cheang, W. S., Liu, B., Zhao, K., Miao, S., Rivière, C., et al. (2019) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2019.01.004 · Cited by 149

SUMO: regulating the regulator.

Bossis, G., & Melchior, F. (2006) · Cell Division · doi:10.1186/1747-1028-1-13 · Cited by 149

Extracellular matrix stimulates reactive oxygen species production and increases pancreatic cancer cell survival through 5-lipoxygenase and NADPH oxidase

Edderkaoui, M., Hong, P., Vaquero, E. C., Lee, J. K., Fischer, L., Friess, H., Büchler, M. W., Lerch, M. M., Pandol, S. J., & Gukovskaya, A. S. (2005) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00197.2005 · Cited by 149

Cutting Edge: MyD88 Controls Phagocyte NADPH Oxidase Function and Killing of Gram-Negative Bacteria

Laroux, F. S., Ros, X. R., Wetzler, L. M., Engel, P., & Terhorst, C. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.9.5596 · Cited by 149

Repression of Sestrin Family Genes Contributes to Oncogenic Ras-Induced Reactive Oxygen Species Up-regulation and Genetic Instability

Kopnin, P., Agapova, L. S., Kopnin, B. P., & Chumakov, P. M. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-2466 · Cited by 149

Extracellular haem peroxidases mediate M n( II ) oxidation in a marine R oseobacter bacterium via superoxide production

Andeer, P. F., Learman, D. R., McIlvin, M. R., Dunn, J. A., & Hansel, C. M. (2015) · Environmental Microbiology · doi:10.1111/1462-2920.12893 · Cited by 148

The Rho-kinase inhibitor, fasudil, attenuates diabetic nephropathy in streptozotocin-induced diabetic rats

Gojo, A., Utsunomiya, K., Taniguchi, K., Yokota, T., Ishizawa, S., Kanazawa, Y., Kurata, H., & Tajima, N. (2007) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2007.04.011 · Cited by 148

Microglial polarization: novel therapeutic mechanism against Alzheimer’s disease

Yao, K., & Zu, H. (2019) · Inflammopharmacology · doi:10.1007/s10787-019-00613-5 · Cited by 150

Involvement of the Nicotinamide Adenosine Dinucleotide Phosphate Oxidase Isoform Nox2 in Cardiac Contractile Dysfunction Occurring in Response to Pressure Overload

Grieve, D., Byrne, J., Siva, A., Layland, J., Johar, S., Cave, A. C., & Shah, A. M. (2006) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2005.09.051 · Cited by 148

NADPH oxidases: key modulators in aging and age-related cardiovascular diseases?

Sahoo, S., Meijles, D. N., & Pagano, P. J. (2016) · Clinical Science · doi:10.1042/cs20150087 · Cited by 147

Rosmarinic acid inhibits the formation of reactive oxygen and nitrogen species in RAW264.7 macrophages

Qiao, S., Li, W., Tsubouchi, R., Haneda, M., Murakami, K., Takeuchi, F., Nisimoto, Y., & Yoshino, M. (2005) · Free Radical Research · doi:10.1080/10715760500231836 · Cited by 147

Insulin infusion in acute illness

Dandona, P. (2005) · Journal of Clinical Investigation · doi:10.1172/jci26045 · Cited by 147

NOX5 is expressed at the plasma membrane and generates superoxide in response to protein kinase C activation

SERRANDER, L., JAQUET, V, BEDARD, K., PLASTRE, O., HARTLEY, O., ARNAUDEAU, S., DEMAUREX, N., SCHLEGEL, W., & KRAUSE, K. (2007) · Biochimie · doi:10.1016/j.biochi.2007.05.004 · Cited by 146

Fungal antioxidant pathways promote survival against neutrophils during infection

Leal, S. M., Vareechon, C., Cowden, S., Cobb, B. A., Latgé, J.-P., Momany, M., & Pearlman, E. (2012) · Journal of Clinical Investigation · doi:10.1172/jci63239 · Cited by 146

Ce-Duox1/BLI-3 Generates Reactive Oxygen Species as a Protective Innate Immune Mechanism in Caenorhabditis elegans

Chávez, V., Mohri‐Shiomi, A., & Garsin, D. A. (2009) · Infection and Immunity · doi:10.1128/iai.00627-09 · Cited by 146

Bacillus amyloliquefaciens SC06 alleviates the oxidative stress of IPEC-1 via modulating Nrf2/Keap1 signaling pathway and decreasing ROS production

Wang, Y., Wu, Y., Wang, Y., Fu, A., Gong, L., Li, W., & Li, Y. (2016) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-016-8032-4 · Cited by 146

The Role of Peroxiredoxins in the Transduction of H 2 O 2 Signals

Rhee, S. G., Woo, H. A., & Kang, D. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7167 · Cited by 146

From Flies to Men: ROS and the NADPH Oxidase in Phagocytes

Moghadam, Z. M., Henneke, P., & Kolter, J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.628991 · Cited by 146

The receptor-like cytoplasmic kinase RIPK regulates broad-spectrum ROS signaling in multiple layers of plant immune system

Li, P., Zhao, L., Qi, F., Htwe, N. M. P. S., Li, Q., Zhang, D., Lin, F., Shang‐Guan, K., & Liang, Y. (2021) · Molecular Plant · doi:10.1016/j.molp.2021.06.010 · Cited by 146

Oxidative Stress in Age-Related Neurodegenerative Diseases: An Overview of Recent Tools and Findings

Korovesis, D., Rubio‐Tomás, T., & Tavernarakis, N. (2023) · Antioxidants · doi:10.3390/antiox12010131 · Cited by 146

Redox modifier genes in amyotrophic lateral sclerosis in mice

Marden, J. J., Harraz, M. M., Williams, A. J., Nelson, K., Luo, M., Paulson, H., & Engelhardt, J. F. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31265 · Cited by 145

The role of the microglia in acute CNS injury

Kawabori, M., & Yenari, M. A. (2014) · Metabolic Brain Disease · doi:10.1007/s11011-014-9531-6 · Cited by 145

Reduction–oxidation (redox) system in radiation-induced normal tissue injury: molecular mechanisms and implications in radiation therapeutics

Yahyapour, R., Motevaseli, E., Rezaeyan, A., Abdollahi, H., Farhood, B., Cheki, M., Rezapoor, S., Shabeeb, D., Musa, A. E., Najafi, M., et al. (2018) · Clinical & Translational Oncology · doi:10.1007/s12094-017-1828-6 · Cited by 145

Helicobacter pylori lipopolysaccharide activates Rac1 and transcription of NADPH oxidase Nox1 and its organizer NOXO1 in guinea pig gastric mucosal cells

Kawahara, T., Kohjima, M., Kuwano, Y., Mino, H., Teshima-Kondo, S., Takeya, R., Tsunawaki, S., Wada, A., Sumimoto, H., & Rokutan, K. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00319.2004 · Cited by 145

Role of nitric oxide and reactive oxygen species in the pathogenesis of preeclampsia

Matsubara, K., Matsubara, Y., Hyodo, S., Katayama, T., & Ito, M. (2010) · Journal of obstetrics and gynaecology research · doi:10.1111/j.1447-0756.2009.01128.x · Cited by 144

Regulation of the Phagocyte NADPH Oxidase by Rac GTPase

Bokoch, G., & Zhao, T. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1533 · Cited by 144

Crossroads of PI3K and Rac pathways

Campa, C. C., Ciraolo, E., Ghigo, A., Germena, G., & Hirsch, E. (2015) · Small GTPases · doi:10.4161/21541248.2014.989789 · Cited by 143

Reactive Oxygen Species-Activated Akt/ASK1/p38 Signaling Pathway in Nickel Compound-Induced Apoptosis in BEAS 2B Cells

Pan, J., Chang, Q., Wang, X., Son, Y., Zhang, Z., Chen, G., Luo, J., Bi, Y., Chen, F., & Shi, X. (2010) · Chemical Research in Toxicology · doi:10.1021/tx9003193 · Cited by 143

NADPH oxidase signaling and cardiac myocyte function

Akki, A. S., Zhang, M., Murdoch, C. E., Brewer, A. C., & Shah, A. M. (2009) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2009.04.004 · Cited by 143

Atherogenic dyslipidemia and oxidative stress: a new look

Rizzo, M., Kotur‐Stevuljević, J., Berneis, K. K., Spinas, G. A., Rini, G. B., Jelić‐Ivanović, Z., Spasojević‐Kalimanovska, V., & Vekić, J. (2009) · Translational research · doi:10.1016/j.trsl.2009.01.008 · Cited by 143

Immunobiology of Nitric Oxide and Regulation of Inducible Nitric Oxide Synthase

Lee, M. W., Rey, K., Besler, K. J., Wang, C., & Choy, J. C. (2017) · Results and problems in cell differentiation · doi:10.1007/978-3-319-54090-0_8 · Cited by 143

Ras-induced reactive oxygen species promote growth factor–independent proliferation in human CD34+ hematopoietic progenitor cells

Hole, P. S., Pearn, L., Tonks, A. J., James, P. E., Burnett, A. K., Darley, R. L., & Tonks, A. (2009) · Blood · doi:10.1182/blood-2009-06-222869 · Cited by 142

Apocynin improves outcome in experimental stroke with a narrow dose range

Tang, X. N., Cairns, B., Cairns, N., & Yenari, M. A. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.03.090 · Cited by 142

Reactive Oxygen Species Production in the Phagosome: Impact on Antigen Presentation in Dendritic Cells

Kotsias, F., Hoffmann, E., Amigorena, S., & Savina, A. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4557 · Cited by 142

Direct and specific inactivation of protein tyrosine kinases in the Src and FGFR families by reversible cysteine oxidation

Kemble, D. J., & Sun, G. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806117106 · Cited by 142

Airway Epithelial Cell Migration and Wound Repair by ATP-mediated Activation of Dual Oxidase 1

Wesley, U. V., Bove, P. F., Hristova, M., McCarthy, S. M., & van der Vliet, A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606533200 · Cited by 142

Wolbachia and the insect immune system: what reactive oxygen species can tell us about the mechanisms of Wolbachia–host interactions

Zug, R., & Hammerstein, P. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.01201 · Cited by 141

Novel Role of NADPH Oxidase in Angiogenesis and Stem/Progenitor Cell Function

Ushio‐Fukai, M., & Urao, N. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2582 · Cited by 141

Redox amplification of apoptosis by caspase-dependent cleavage of glutaredoxin 1 and S-glutathionylation of Fas

Anathy, V., Aesif, S. W., Guala, A. S., Havermans, M., Reynaert, N. L., Ho, Y.-S., Budd, R. C., & Janssen-Heininger, Y. M. W. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200807019 · Cited by 141

The role of NOX enzymes in ethanol-induced oxidative stress and apoptosis in mouse embryos

Dong, J., Sulik, K. K., & Chen, S.-Y. (2009) · Toxicology Letters · doi:10.1016/j.toxlet.2009.12.012 · Cited by 141

Reactive Oxygen Species Generated by NADPH Oxidase 2 and 4 Are Required for Chondrogenic Differentiation

Kim, K. S., Choi, H. W., Yoon, H. E., & Kim, I. Y. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.126821 · Cited by 141

Long noncoding RNA SNHG12 integrates a DNA-PK–mediated DNA damage response and vascular senescence

Haemmig, S., Yang, D., Sun, X., Das, D., Ghaffari, S., Molinaro, R., Chen, L., Deng, Y., Freeman, D., Moullan, N., et al. (2020) · Science Translational Medicine · doi:10.1126/scitranslmed.aaw1868 · Cited by 142

Redox biology and gastric carcinogenesis: the role of Helicobacter pylori

Handa, O., Naito, Y., & Yoshikawa, T. (2011) · Redox Report · doi:10.1179/174329211x12968219310756 · Cited by 141

Aging mechanisms in bone

Almeida, M. (2012) · BoneKEy Reports · doi:10.1038/bonekey.2012.102 · Cited by 141

Toll-like receptors: key players in antiviral immunity

Arpaia, N., & Barton, G. M. (2011) · Current Opinion in Virology · doi:10.1016/j.coviro.2011.10.006 · Cited by 140

Recent developments in detection of superoxide radical anion and hydrogen peroxide: Opportunities, challenges, and implications in redox signaling

Kalyanaraman, B., Hardy, M., Podsiadły, R., Cheng, G., & Zielonka, J. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.08.021 · Cited by 140

Direct Involvement of the Small GTPase Rac in Activation of the Superoxide-producing NADPH Oxidase Nox1

Miyano, K., Ueno, N., Takeya, R., & Sumimoto, H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513665200 · Cited by 140

Roles of DUOX-Mediated Hydrogen Peroxide in Metabolism, Host Defense, and Signaling

Deken, X. D., Corvilain, B., Dumont, J. E., & Miot, F. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5602 · Cited by 139

Peptidoglycan: a critical activator of the mammalian immune system during infection and homeostasis

Sorbara, M. T., & Philpott, D. J. (2011) · Immunological Reviews · doi:10.1111/j.1600-065x.2011.01047.x · Cited by 139

Modulating neuroinflammation and oxidative stress to prevent epilepsy and improve outcomes after traumatic brain injury

Eastman, C. L., D’Ambrosio, R., & Ganesh, T. (2019) · Neuropharmacology · doi:10.1016/j.neuropharm.2019.107907 · Cited by 140

AMP-activated protein kinase: A remarkable contributor to preserve a healthy heart against ROS injury

Marino, A., Hausenloy, D. J., Andreadou, I., Horman, S., Bertrand, L., & Beauloye, C. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.02.047 · Cited by 140

AIF suppresses chemical stress‐induced apoptosis and maintains the transformed state of tumor cells

Urbano, A., Lakshmanan, U., Choo, P. H., Kwan, J., Ng, P. Y., Guo, K., Dhakshinamoorthy, S., & Porter, A. G. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600746 · Cited by 139

Suppression of Microglial Inflammatory Activity by Myelin Phagocytosis: Role of p47-PHOX-Mediated Generation of Reactive Oxygen Species

Liu, Y., Hao, W., Letièmbre, M., Walter, S., Kulanga, M., Neumann, H., & Fassbender, K. C. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.2531-06.2006 · Cited by 139

Reactive oxygen species in the neuropathogenesis of hypertension

Peterson, J. R., Sharma, R. V., & Davisson, R. L. (2006) · Current Hypertension Reports · doi:10.1007/s11906-006-0056-1 · Cited by 139

NADPH oxidases and cardiac remodelling

Nabeebaccus, A., Zhang, M., & Shah, A. M. (2011) · Heart Failure Reviews · doi:10.1007/s10741-010-9186-2 · Cited by 138

The Behavioral Sequelae of Social Defeat Require Microglia and Are Driven by Oxidative Stress in Mice

Lehmann, M. L., Weigel, T. K., Poffenberger, C. N., & Herkenham, M. (2019) · The Journal of Neuroscience · doi:10.1523/jneurosci.0184-19.2019 · Cited by 138

Elevated hydrogen peroxide and decreased catalase and glutathione peroxidase protection are associated with aging sarcopenia

Sullivan, M., & Lewandowski, P. A. (2013) · BMC Geriatrics · doi:10.1186/1471-2318-13-104 · Cited by 138

Combined NADPH and the NOX inhibitor apocynin provides greater anti-inflammatory and neuroprotective effects in a mouse model of stroke

Qin, Y., Li, M., Feng, X., Wang, J., Cao, L., Shen, X.-K., Chen, J., Sun, M., Sheng, R., Han, F., et al. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.01.034 · Cited by 138

Mechanisms of Overcoming Intrinsic Resistance to Gemcitabine in Pancreatic Ductal Adenocarcinoma through the Redox Modulation

Ju, H.-Q., Gocho, T., Aguilar, M., Wu, M., Zhuang, Z.-N., Fu, J., Yanaga, K., Huang, P., & Chiao, P. J. (2015) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-14-0420 · Cited by 137

The effects of dietary flavonoids on the regulation of redox inflammatory networks

Izzi, V. (2012) · Frontiers in bioscience · doi:10.2741/4061 · Cited by 137

Mitocans Revisited: Mitochondrial Targeting as Efficient Anti-Cancer Therapy

Dong, L., Gopalan, V., Holland, O. J., & Neužil, J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21217941 · Cited by 137

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 137

Relationship of electrophilic stress to aging

Zimniak, P. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.05.039 · Cited by 136

H 2 O 2

Rice, M. E. (2011) · The Neuroscientist · doi:10.1177/1073858411404531 · Cited by 136

Mammalian NADPH Oxidases

Buvelot, H., Jaquet, V., & Krause, K. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9424-3_2 · Cited by 136

Mitochondria Are the Source of Hydrogen Peroxide for Dynamic Brain-Cell Signaling

Bao, L., Avshalumov, M. V., Patel, J. C., Lee, C. R., Miller, E. W., Chang, C. J., & Rice, M. E. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.1706-09.2009 · Cited by 136

NAD(P)H Oxidases in Rat Basilar Arterial Endothelial Cells

Ago, T., Kitazono, T., Kuroda, J., Kumai, Y., Kamouchi, M., Ooboshi, H., Wakisaka, M., Kawahara, T., Rokutan, K., Ibayashi, S., et al. (2005) · Stroke · doi:10.1161/01.str.0000163111.05825.0b · Cited by 136

Targeted removal of bioavailable metal as a detoxification strategy for carbon nanotubes

Liu, X., Guo, L., Morris, D., Kane, A. B., & Hurt, R. H. (2008) · Carbon · doi:10.1016/j.carbon.2007.12.018 · Cited by 135

NOX1 Deficiency Protects From Aortic Dissection in Response to Angiotensin II

Gavazzi, G., Deffert, C., Trocme, C., Schäppi, M., Herrmann, F. R., & Krause, K.-H. (2007) · Hypertension · doi:10.1161/hypertensionaha.107.089706 · Cited by 135

STEAP1 Is Associated with the Invasive and Oxidative Stress Phenotype of Ewing Tumors

Grünewald, T. G. P., Diebold, I., Esposito, I., Plehm, S., Hauer, K., Thiel, U., da Silva‐Buttkus, P., Neff, F., Unland, R., Müller‐Tidow, C., et al. (2011) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-11-0524 · Cited by 135

Boronate-Based Fluorescent Probes

Lin, V., Dickinson, B. C., & Chang, C. J. (2013) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-405883-5.00002-8 · Cited by 135

The Bacterial Fermentation Product Butyrate Influences Epithelial Signaling via Reactive Oxygen Species-Mediated Changes in Cullin-1 Neddylation

Kumar, A., Wu, H., Collier-Hyams, L. S., Kwon, Y.-M., Hanson, J. M., & Neish, A. S. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.182.1.538 · Cited by 135

Pro-metastatic signaling by c-Met through RAC-1 and reactive oxygen species (ROS)

Ferraro, D. A., Corso, S., Fasano, E., Panieri, E., Santangelo, R., Borrello, S., Giordano, S., Pani, G., & Galeotti, T. (2006) · Oncogene · doi:10.1038/sj.onc.1209409 · Cited by 135

NoxA activation by the small GTPase RacA is required to maintain a mutualistic symbiotic association between Epichloë festucae and perennial ryegrass

Tanaka, A., Takemoto, D., Hyon, G., Park, P., & Scott, B. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06217.x · Cited by 135

Reactive Oxygen Species: Physiological Roles in the Regulation of Vascular Cells

Vara, D. S., & Pula, G. (2014) · Current Molecular Medicine · doi:10.2174/1566524014666140603114010 · Cited by 135

Role of mitochondria in angiotensin II-induced reactive oxygen species and mitogen-activated protein kinase activation

Zhang, G., LU, X., KIMURA, S., & Nishiyama, A. (2007) · Cardiovascular Research · doi:10.1016/j.cardiores.2007.07.014 · Cited by 134

Production of Reactive Oxygen Species in the Diabetic Heart

Teshima, Y., Takahashi, N., Nishio, S., Saito, S., Kondo, H., Fukui, A., Aoki, K., Yufu, K., Nakagawa, M., & Saikawa, T. (2013) · Circulation Journal · doi:10.1253/circj.cj-13-1187 · Cited by 134

Interplay Between Calcium and Reactive Oxygen/Nitrogen Species: An Essential Paradigm for Vascular Smooth Muscle Signaling

Trebak, M., Ginnan, R. G., Singer, H. A., & Jourd’heuil, D. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2842 · Cited by 134

Redox regulation of lung inflammation: role of NADPH oxidase and NF-κB signalling

Yao, H., Yang, S., Kode, A., Rajendrasozhan, S., Caito, S. W., Adenuga, D., Henry, R. A., Edirisinghe, I., & Rahman, I. (2007) · Biochemical Society Transactions · doi:10.1042/bst0351151 · Cited by 134

Angiotensin II-Dependent Chronic Hypertension and Cardiac Hypertrophy Are Unaffected by gp91phox-Containing NADPH Oxidase

Touyz, R. M., Mercure, C., He, Y., Javeshghani, D., Yao, G., Callera, G. E., Yogi, Á., Lochard, N., & Reudelhuber, T. L. (2005) · Hypertension · doi:10.1161/01.hyp.0000158845.49943.5e · Cited by 134

Inflammation and oxidative stress induced by cigarette smoke in Lewis rat brains

Khanna, A. K., Guo, M., Mehra, M. R., & Royal, W. (2012) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2012.09.006 · Cited by 134

α-Tocopherol Protects Against Oxidative Stress in the Fragile X Knockout Mouse: an Experimental Therapeutic Approach for the Fmr1 Deficiency

de Diego-Otero, Y., Romero-Zerbo, Y., Bekay, R. E., Decara, J., Sanchez, L., Fonseca, F. R.-D., & Arco-Herrera, I. D. (2009) · Neuropsychopharmacology · doi:10.1038/npp.2008.152 · Cited by 133

MicroRNA and ROS Crosstalk in Cardiac and Pulmonary Diseases

Climent, M., Viggiani, G., Chen, Y., Coulis, G., & Castaldi, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21124370 · Cited by 134

Recent advances and contraversies on the role of pulmonary neuroepithelial bodies as airway sensors

Cutz, E., Pan, J., Yeger, H., Domnik, N. J., & Fisher, J. T. (2012) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2012.09.003 · Cited by 132

The Involvement of the Tyrosine Kinase c-Src in the Regulation of Reactive Oxygen Species Generation Mediated by NADPH Oxidase-1

Gianni, D., Bohl, B. P., Courtneidge, S. A., & Bokoch, G. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-02-0138 · Cited by 132

Polarity proteins Bem1 and Cdc24 are components of the filamentous fungal NADPH oxidase complex

Takemoto, D., Kamakura, S., Saikia, S., Becker, Y., Wrenn, R. E., Tanaka, A., Sumimoto, H., & Scott, B. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1017309108 · Cited by 132

Rheumatoid Arthritis: The Role of Reactive Oxygen Species in Disease Development and Therapeutic Strategies

Gelderman, K. A., Hultqvist, M. H., Olsson, L. M., Bauer, K., Pizzolla, A., Olofsson, P., & Holmdahl, R. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1569 · Cited by 132

cAMP-response Element-binding Protein Mediates Acid-induced NADPH Oxidase NOX5-S Expression in Barrett Esophageal Adenocarcinoma Cells

Fu, X., Beer, D. G., Behar, J., Wands, J. R., Lambeth, D. J., & Cao, W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603353200 · Cited by 132

Oxidative Stress and Redox Signaling in the Pathophysiology of Liver Diseases

Mooli, R. G. R., Mukhi, D., & Ramakrishnan, S. K. (2022) · Comprehensive physiology · doi:10.1002/cphy.c200021 · Cited by 134

NADPH-oxidase activation and cognition in Alzheimer disease progression

Ansari, M. A., & Scheff, S. W. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.03.025 · Cited by 131

NADPH oxidase 2-derived reactive oxygen species in the hippocampus might contribute to microglial activation in postoperative cognitive dysfunction in aged mice

Qiu, L., Ji, M., Zhang, H., Yang, J., Sun, X.-R., Tang, H., Wang, J., Liu, W., & Yang, J.-J. (2015) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2015.08.002 · Cited by 131

Fibrillar β-Amyloid-stimulated Intracellular Signaling Cascades Require Vav for Induction of Respiratory Burst and Phagocytosis in Monocytes and Microglia

Wilkinson, B. L., Koenigsknecht-Talboo, J., Grommes, C., Lee, C. Y. D., & Landreth, G. E. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600627200 · Cited by 131

p ‐Cresyl Sulfate Aggravates Cardiac Dysfunction Associated With Chronic Kidney Disease by Enhancing Apoptosis of Cardiomyocytes

Han, H., Zhu, J., Zhu, Z., Ni, J., Du, R., Dai, Y., Chen, Y., Wu, Z., Lu, L., & Zhang, R. (2015) · Journal of the American Heart Association · doi:10.1161/jaha.115.001852 · Cited by 131

Parasitic Worms Stimulate Host NADPH Oxidases to Produce Reactive Oxygen Species That Limit Plant Cell Death and Promote Infection

Siddique, S., Matera, C., Radaković, Z. S., Hasan, M. S., Gutbrod, P., Różańska, E., Sobczak, M., Torres, M. Á. M., & Grundler, F. M. W. (2014) · Science Signaling · doi:10.1126/scisignal.2004777 · Cited by 131

Antibody-induced nonapoptotic cell death in human lymphoma and leukemia cells is mediated through a novel reactive oxygen species-dependent pathway

Honeychurch, J., Alduaij, W., Azizyan, M., Cheadle, E. J., Pelicano, H., Ivanov, A., Huang, P., Cragg, M. S., & Illidge, T. (2012) · Blood · doi:10.1182/blood-2011-12-395541 · Cited by 131

Redox regulation of the actin cytoskeleton and its role in the vascular system

Xu, Q., Huff, L. P., Fujii, M., & Griendling, K. K. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.03.004 · Cited by 132

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)