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

Regulatory Mechanisms and Novel Therapeutic Targeting Strategies for Protein Tyrosine Phosphatases

Yu, Z.-H., & Zhang, Z. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00105 · Cited by 131

Interferon-γ activates transcription of NADPH oxidase 1 gene and upregulates production of superoxide anion by human large intestinal epithelial cells

Kuwano, Y., Kawahara, T., Yamamoto, H., Teshima-Kondo, S., Tominaga, K., Masuda, K., Kishi, K., Morita, K., & Rokutan, K. (2005) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00135.2005 · Cited by 131

Cellular Respiration: The Nexus of Stress, Condition, and Ornamentation

Hill, G. E. (2014) · Integrative and Comparative Biology · doi:10.1093/icb/icu029 · Cited by 130

The H+-ATP synthase: A gate to ROS-mediated cell death or cell survival

Martínez‐Reyes, I., & Cuezva, J. M. (2014) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2014.03.010 · Cited by 130

Oxidative Stress and Redox Modulation Potential in Type 1 Diabetes

Delmastro-Greenwood, M. M., & Piganelli, J. D. (2011) · Clinical and Developmental Immunology · doi:10.1155/2011/593863 · Cited by 130

From birth to death: A role for reactive oxygen species in neuronal development

Wilson, C., Muñoz-Palma, E., & González-Billault, C. E. (2017) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2017.09.012 · Cited by 131

Lanthanide-based luminescent probes for selective time-gated detection of hydrogen peroxide in water and in living cells

Lippert, A. R., Gschneidtner, T. A., & Chang, C. J. (2010) · Chemical Communications · doi:10.1039/c0cc01560a · Cited by 129

Macrophage Glucose-6-Phosphate Dehydrogenase Stimulates Proinflammatory Responses with Oxidative Stress

Ham, M., Lee, J., Choi, A. H., Jang, H., Choi, G., Park, J., Kozuka, C., Sears, D. D., Masuzaki, H., & Kim, J. B. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01260-12 · Cited by 129

Modulation of cardiac ryanodine receptor activity by ROS and RNS

Donoso, P. (2010) · Frontiers in bioscience · doi:10.2741/3705 · Cited by 129

Role of a novel bile acid receptor TGR5 in the development of oesophageal adenocarcinoma

Hong, J., Behar, J., Wands, J. R., Resnick, M. B., Wang, L., DeLellis, R. A., Lambeth, D. J., Souza, R. F., Spechler, S. J., & Cao, W. (2009) · Gut · doi:10.1136/gut.2009.188375 · Cited by 129

The Role of Autophagy in Sepsis: Protection and Injury to Organs

Yin, X., Xin, H., Mao, S., Wu, G., & Guo, L. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.01071 · Cited by 128

Spontaneous and aging-dependent development of arthritis in NADPH oxidase 2 deficiency through altered differentiation of CD11b+ and Th/Treg cells

Lee, K., Won, H. Y., Bae, M. A., Hong, J., & Hwang, E. S. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1012645108 · Cited by 127

Novel Nox inhibitor of oxLDL-induced reactive oxygen species formation in human endothelial cells

Stielow, C., Catar, R. A., Müller, G. M., Wingler, K., Scheurer, P., Schmidt, H. H. H. W., & Morawietz, H. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.03.114 · Cited by 127

Functional characterization of Rho GTPases in Aspergillus niger uncovers conserved and diverged roles of Rho proteins within filamentous fungi

Kwon, M. J., Arentshorst, M., Roos, E. D., van den Hondel, C. A. M. J. J., Meyer, V., & Ram, A. F. J. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07524.x · Cited by 127

Redox signaling: Potential arbitrator of autophagy and apoptosis in therapeutic response

Zhang, L., Wang, K., Lei, Y., Li, Q., Nice, E. C., & Huang, C. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.08.030 · Cited by 127

Stress Response and Pathogenicity of the Necrotrophic Fungal Pathogen Alternaria alternata

Chung, K.-R. (2012) · Scientifica · doi:10.6064/2012/635431 · Cited by 127

Sensing of redox status by TRP channels

Ogawa, N., Kurokawa, T., & Mori, Y. (2016) · Cell Calcium · doi:10.1016/j.ceca.2016.02.009 · Cited by 126

The Role of Reactive Oxygen Species in Integrin and Matrix Metalloproteinase Expression and Function

Svineng, G., Ravuri, C. S., Rikardsen, O., Huseby, N., & Winberg, J. (2008) · Connective Tissue Research · doi:10.1080/03008200802143166 · Cited by 126

Oncogenic Ras upregulates NADPH oxidase 1 gene expression through MEK-ERK-dependent phosphorylation of GATA-6

Adachi, Y., Shibai, Y., Mitsushita, J., Shang, W. H., Hirose, K., & Kamata, T. (2008) · Oncogene · doi:10.1038/onc.2008.133 · Cited by 125

Hypoxia and Metabolic Factors That Influence Inflammatory Bowel Disease Pathogenesis

Glover, L. E., & Colgan, S. P. (2011) · Gastroenterology · doi:10.1053/j.gastro.2011.01.056 · Cited by 126

Mechanisms and Potential Therapeutic Applications of Microglial Activation after Brain Injury

Kim, J. Y., Kim, N., & Yenari, M. A. (2014) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.12360 · Cited by 125

Recent advances in ultrathin two-dimensional materials and biomedical applications for reactive oxygen species generation and scavenging

Wang, L., Li, Y., Zhao, L., Qi, Z., Gou, J., Zhang, S., & Zhang, J. Z. (2020) · Nanoscale · doi:10.1039/d0nr05746k · Cited by 125

Neutrophil-mediated oxidative burst and host defense are controlled by a Vav-PLCγ2 signaling axis in mice

Graham, D. B., Robertson, C. M., Bautista, J., Mascarenhas, F., Diacovo, M. J., Montgrain, V., Lam, S. K., Cremasco, V., Dunne, W. M., Faccio, R., et al. (2007) · Journal of Clinical Investigation · doi:10.1172/jci32729 · Cited by 124

Cinnamaldehyde ameliorates LPS-induced cardiac dysfunction via TLR4-NOX4 pathway: The regulation of autophagy and ROS production

Zhao, H., Zhang, M., Zhou, F., Cao, W., Bi, L., Xie, Y., Yang, Q., & Wang, S. (2016) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2016.10.017 · Cited by 124

Redox regulation of the insulin signalling pathway

Lennicke, C., & Cochemé, H. M. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101964 · Cited by 124

Reactive Oxygen Species in Planarian Regeneration: An Upstream Necessity for Correct Patterning and Brain Formation

Pirotte, N., Stevens, A., Fraguas, S., Plusquin, M., Roten, A. V., Belleghem, F. V., Paesen, R., Ameloot, M. M., Cebrià, F., Artois, T., et al. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/392476 · Cited by 124

Enteric Commensal Bacteria Induce Extracellular Signal-regulated Kinase Pathway Signaling via Formyl Peptide Receptor-dependent Redox Modulation of Dual Specific Phosphatase 3

Wentworth, C. C., Alam, A. M., Jones, R. M., Nusrat, A., & Neish, A. S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.268938 · Cited by 124

Oxidative Stress and Growth-Regulating Intracellular Signaling Pathways in Cardiac Myocytes

Sugden, P. H., & Clerk, A. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.2111 · Cited by 124

Reactive oxygen species and the brain in sleep apnea

Wang, Y., Zhang, S. X. L., & Gozal, D. (2010) · Respiratory Physiology & Neurobiology · doi:10.1016/j.resp.2010.09.001 · Cited by 124

The kinase Btk negatively regulates the production of reactive oxygen species and stimulation-induced apoptosis in human neutrophils

Honda, F., Kano, H., Kanegane, H., Nonoyama, S., Kim, E. S., Lee, S., Takagi, M., Mizutani, S., & Morio, T. (2012) · Nature Immunology · doi:10.1038/ni.2234 · Cited by 123

Redox regulation of calcium ion channels: Chemical and physiological aspects

Bogeski, I., Kappl, R., Kummerow, C., Gulaboski, R., Hoth, M., & Niemeyer, B. A. (2011) · Cell Calcium · doi:10.1016/j.ceca.2011.07.006 · Cited by 123

An Overview of Oxidative Stress and Antioxidant Defensive System

Noori, S. (2012) · Journal of Clinical & Cellular Immunology · doi:10.4172/scientificreports.413 · Cited by 123

The gut microbiota engages different signaling pathways to induce Duox2 expression in the ileum and colon epithelium

Sommer, F., & Bäckhed, F. (2014) · Mucosal Immunology · doi:10.1038/mi.2014.74 · Cited by 123

Comparison of select innate immune mechanisms of fish and mammals

Plouffe, D. A., Hanington, P. C., Walsh, J. G., Wilson, E. C., & Belosevic, M. (2005) · Xenotransplantation · doi:10.1111/j.1399-3089.2005.00227.x · Cited by 123

Lymphocytic microparticles inhibit angiogenesis by stimulating oxidative stress and negatively regulating VEGF-induced pathways

Yang, C., Mwaikambo, B. R., Zhu, T., Gagnon, C., Lafleur, J., Seshadri, S., Lachapelle, P., Lavoie, J., Chemtob, S., & Hardy, P. (2007) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00432.2007 · Cited by 123

Hyperoxia sensing: From molecular mechanisms to significance in disease

Gore, A., Muralidhar, M., Espey, M. G., Degenhardt, K., & Mantell, L. L. (2010) · Journal of Immunotoxicology · doi:10.3109/1547691x.2010.492254 · Cited by 123

Evolving Concepts of Oxidative Stress and Reactive Oxygen Species in Cardiovascular Disease

Chen, K., & Keaney, J. F. (2012) · Current Atherosclerosis Reports · doi:10.1007/s11883-012-0266-8 · Cited by 122

Regulation of NAD(P)H oxidases by AMPK in cardiovascular systems

Song, P., & Zou, M. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.01.025 · Cited by 122

Redox-sensitive nanoscale drug delivery systems for cancer treatment

Mirhadi, E., Mashreghi, M., Maleki, M. F., Alavizadeh, S. H., Arabi, L., Badiee, A., & Jaafari, M. R. (2020) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2020.119882 · Cited by 122

Redox-Dependent Expression of Cyclin D1 and Cell Proliferation by Nox1 in Mouse Lung Epithelial Cells

Ranjan, P., Anathy, V., Burch, P. M., Weirather, K., Lambeth, J. D., & Heintz, N. H. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1447 · Cited by 122

Facilitative functionalization of cyanine dye by an on–off–on fluorescent switch for imaging of H2O2 oxidative stress and thiols reducing repair in cells and tissues

Yu, F., Li, P., Song, P., Wang, B., Zhao, J., & Han, K. (2012) · Chemical Communications · doi:10.1039/c2cc30985h · Cited by 121

Eukaryotic copper-only superoxide dismutases (SODs): A new class of SOD enzymes and SOD-like protein domains

Robinett, N. G., Peterson, R. L., & Culotta, V. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.tm117.000182 · Cited by 123

Phagocytosis-Coupled Activation of the Superoxide-Producing Phagocyte Oxidase, a Member of the NADPH Oxidase (Nox) Family

Minakami, R., & Sumimotoa, H. (2006) · International Journal of Hematology · doi:10.1532/ijh97.06133 · Cited by 121

Curcumin ameliorated diabetic neuropathy partially by inhibition of NADPH oxidase mediating oxidative stress in the spinal cord

Zhao, W., Zhang, B., Liao, M., Zhang, W., He, W., Wang, H., & Yang, C. (2013) · Neuroscience Letters · doi:10.1016/j.neulet.2013.12.019 · Cited by 121

Trimetazidine prevents macrophage-mediated septic myocardial dysfunction via activation of the histone deacetylase sirtuin 1

Chen, J., Lai, J., Yang, L., Ruan, G., Chaugai, S., Ning, Q., Chen, C., & Wang, D. W. (2016) · British Journal of Pharmacology · doi:10.1111/bph.13386 · Cited by 120

The Tumor Microenvironment: Characterization, Redox Considerations, and Novel Approaches for Reactive Oxygen Species-Targeted Gene Therapy

Policastro, L. L., Ibañez, I. L., Notcovich, C., Duran, H. A., & Podhajcer, O. L. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4367 · Cited by 120

Lipid Rafts and Caveolin-1 Coordinate Interleukin-1β (IL-1β)-dependent Activation of NFκB by Controlling Endocytosis of Nox2 and IL-1β Receptor 1 from the Plasma Membrane

Oakley, F. D., Smith, R. L., & Engelhardt, J. F. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.042127 · Cited by 120

Innovation in the Treatment of Uremia: Proceedings from the Cleveland Clinic Workshop: Uremic Toxicity, Oxidative Stress, and Hemodialysis as Renal Replacement Therapy

Himmelfarb, J. (2009) · Seminars in Dialysis · doi:10.1111/j.1525-139x.2009.00659.x · Cited by 120

Reactive oxygen and nitrogen species and innate immune response

Al‐Shehri, S. S. (2020) · Biochimie · doi:10.1016/j.biochi.2020.11.022 · Cited by 120

Ebselen and Congeners Inhibit NADPH Oxidase 2-Dependent Superoxide Generation by Interrupting the Binding of Regulatory Subunits

Smith, S. M. E., Min, J., Ganesh, T., Diebold, B. A., Kawahara, T., Zhu, Y., McCoy, J. W., Sun, A., Snyder, J. P., Fu, H., et al. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.04.015 · Cited by 120

Mechanisms of Control of Mycobacterium tuberculosis by NK Cells: Role of Glutathione

Allen, M., Bailey, C., Cahatol, I., Dodge, L., Yim, J., Kassissa, C., Luong, J., Kasko, S., Pandya, S., & Venketaraman, V. (2015) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00508 · Cited by 119

Angiotensin II Triggers Peripheral Macrophage-to-Sensory Neuron Redox Crosstalk to Elicit Pain

Shepherd, A. J., Copits, B. A., Mickle, A. D., Karlsson, P., Kadunganattil, S., Haroutounian, S., Tadinada, S. M., de Kloet, A. D., Valtcheva, M. V., McIlvried, L. A., et al. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.3542-17.2018 · Cited by 119

The Role of Hydrogen Peroxide and Peroxiredoxins throughout the Cell Cycle

Heo, S., Kim, S., & Kang, D. (2020) · Antioxidants · doi:10.3390/antiox9040280 · Cited by 120

Emerging factors affecting peri‐implant bone metabolism

Ínsua, Á., Galindo‐Moreno, P., Miron, R. J., Wang, H., & Monje, A. (2023) · Periodontology 2000 · doi:10.1111/prd.12532 · Cited by 119

Expression of Amyotrophic Lateral Sclerosis-linked SOD1 Mutant Increases the Neurotoxic Potential of Microglia via TLR2

Liu, Y., Hao, W., Dawson, A., Liu, S., & Fassbender, K. C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804446200 · Cited by 119

Interplay between enterobactin, myeloperoxidase and lipocalin 2 regulates E. coli survival in the inflamed gut

Singh, V., Yeoh, B. S., Xiao, X., Kumar, M., Bachman, M. A., Borregaard, N., Joe, B., & Vijay–Kumar, M. (2015) · Nature Communications · doi:10.1038/ncomms8113 · Cited by 119

Cytosolic NADPH may regulate differences in basal Nox oxidase-derived superoxide generation in bovine coronary and pulmonary arteries

Gupte, S. A., Kaminski, P. M., Floyd, B. C., Agarwal, R., Ali, N., Ahmad, M., Edwards, J. G., & Wolin, M. S. (2004) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00629.2004 · Cited by 118

Ibuprofen attenuates oxidative damage through NOX2 inhibition in Alzheimer's disease

Wilkinson, B. L., Cramer, P. E., Varvel, N. H., Reed-Geaghan, E. G., Jiang, Q., Szabo, A., Herrup, K., Lamb, B. T., & Landreth, G. E. (2010) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.06.014 · Cited by 118

Upregulation of xCT by KSHV-Encoded microRNAs Facilitates KSHV Dissemination and Persistence in an Environment of Oxidative Stress

Qin, Z., Freitas, E., Sullivan, R. J., Mohan, S., Bacelieri, R. E., Branch, D., Romano, M., Kearney, P., Oates, J. C., Plaisance‐Bonstaff, K., et al. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1000742 · Cited by 118

Deficits in bioenergetics and impaired immune response in granulocytes from children with autism

Napoli, E., Wong, S., Hertz-Picciotto, I., & Giulivi, C. (2014) · Pediatrics · doi:10.1542/peds.2013-1545 · Cited by 117

Activation of the Nrf2-regulated antioxidant cell response inhibits HEMA-induced oxidative stress and supports cell viability

Gallorini, M., Petzel, C., Bolay, C., Hiller, K., Cataldi, A., Buchalla, W., Krifka, S., & Schweikl, H. (2015) · Biomaterials · doi:10.1016/j.biomaterials.2015.03.047 · Cited by 117

NOX Isoforms and Reactive Oxygen Species in Vascular Health

Touyz, R. M., Briones, A. M., Sedeek, M. H., Burger, D. E., & Montezano, A. C. (2011) · Molecular Interventions · doi:10.1124/mi.11.1.5 · Cited by 117

Sleep fragmentation promotes NADPH oxidase 2-mediated adipose tissue inflammation leading to insulin resistance in mice

Zhang, S. X. L., Khalyfa, A., Wang, Y., Carreras, A., Hakim, F., Neel, B. A., Brady, M., Qiao, Z., Hirotsu, C., & Gozal, D. (2013) · International Journal of Obesity · doi:10.1038/ijo.2013.139 · Cited by 117

Combination of chemotherapy and physical plasma elicits melanoma cell death via upregulation of SLC22A16

Sagwal, S. K., Pasqual-Melo, G., Bodnar, Y., Gandhirajan, R. K., & Bekeschus, S. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-1221-6 · Cited by 117

The Bidirectional Interactions between Resveratrol and Gut Microbiota: An Insight into Oxidative Stress and Inflammatory Bowel Disease Therapy

Hu, Y., Chen, D., Zheng, P., Yu, J., He, J., Mao, X., & Yu, B. (2019) · BioMed Research International · doi:10.1155/2019/5403761 · Cited by 117

The homeostatic role of hydrogen peroxide, superoxide anion and nitric oxide in the vasculature

Costa, T. J. D., Barros, P. R., Arce, C., Santos, J. D., da Silva-Neto, J., Egea, G., Dantas, A. P., Tostes, R. C., & Jiménez‐Altayó, F. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.11.021 · Cited by 117

Oxygen in the evolution of complex life and the price we pay

Thannickal, V. J. (2009) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2008-0360ps · Cited by 116

Superoxide induces Neutrophil Extracellular Trap Formation in a TLR-4 and NOX-Dependent Mechanism

Al‐Khafaji, A. B., Tohme, S. T., Yazdani, H. O., Miller, D., Huang, H., & Tsung, A. (2016) · Molecular Medicine · doi:10.2119/molmed.2016.00054 · Cited by 116

NADPH oxidases in traumatic brain injury – Promising therapeutic targets?

Ma, M. W., Wang, J., Dhandapani, K. M., Wang, R., & Brann, D. W. (2018) · Redox Biology · doi:10.1016/j.redox.2018.03.005 · Cited by 116

When It Comes to an End: Oxidative Stress Crosstalk with Protein Aggregation and Neuroinflammation Induce Neurodegeneration

Michalska, P., & Leon, R. M. (2020) · Antioxidants · doi:10.3390/antiox9080740 · Cited by 119

The Mechanisms and Physiological Relevance of Glycocalyx Degradation in Hepatic Ischemia/Reperfusion Injury

van Golen, R. F., Reiniers, M. J., Vrisekoop, N., Zuurbier, C. J., Olthof, P. B., van Rheenen, J., van Gulik, T. M., Parsons, B. J., & Heger, M. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5751 · Cited by 116

NADPH oxidase-derived reactive oxygen species in the regulation of endothelial phenotype.

Dworakowski, R., Alom-Ruiz, S. P., & Shah, A. M. (2008) · PubMed · Cited by 116

S-nitrosylation of the zinc finger protein SRG1 regulates plant immunity

Cui, B., Pan, Q., Clarke, D. J., Ochoa-Villarreal, M., Umbreen, S., Yuan, B., Shan, W., Jiang, J., & Loake, G. J. (2018) · Nature Communications · doi:10.1038/s41467-018-06578-3 · Cited by 115

Role of oxidative stress in calcific aortic valve disease and its therapeutic implications

Greenberg, H. Z. E., Zhao, G., Shah, A. M., & Zhang, M. (2021) · Cardiovascular Research · doi:10.1093/cvr/cvab142 · Cited by 115

Risk of Heart Failure in Patients With Nonalcoholic Fatty Liver Disease

Mantovani, A., Byrne, C. D., Benfari, G., Bonapace, S., Simon, T. G., & Targher, G. (2022) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2021.11.007 · Cited by 115

NADPH oxidases regulate cell growth and migration in myeloid cells transformed by oncogenic tyrosine kinases

Reddy, M. M., Fernandes, M. S., Salgia, R., Levine, R. L., Griffin, J. D., & Sattler, M. (2010) · Leukemia · doi:10.1038/leu.2010.263 · Cited by 115

Reactive oxygen species in vascular endothelial cell motility. Roles of NAD(P)H oxidase and Rac1

Moldovan, L., Mythreye, K., Goldschmidt‐Clermont, P. J., & Satterwhite, L. L. (2006) · Cardiovascular Research · doi:10.1016/j.cardiores.2006.05.003 · Cited by 115

Reactive Oxygen Species and Endothelial Activation

Alom-Ruiz, S. P., Anilkumar, N. P., & Shah, A. M. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.2007 · Cited by 115

NADPH Oxidase Activation Is Required in Reactive Oxygen Species Generation and Cell Transformation Induced by Hexavalent Chromium

Wang, X., Son, Y., Chang, Q., Sun, L., Hitron, J. A., Budhraja, A., Zhang, Z., Ke, Z., Chen, F., Luo, J., et al. (2011) · Toxicological Sciences · doi:10.1093/toxsci/kfr180 · Cited by 115

The human Nox4: gene, structure, physiological function and pathological significance

Guo, S., & Chen, X. (2015) · Journal of drug targeting · doi:10.3109/1061186x.2015.1036276 · Cited by 114

Reactive Oxygen Species: The 2-Edged Sword of Osteoarthritis

Ding, L., Wang, W., & Xie, G. (2012) · The American Journal of the Medical Sciences · doi:10.1097/maj.0b013e3182579dc6 · Cited by 114

The emerging role of ROS-generating NADPH oxidase NOX4 in DNA-damage responses

Weyemi, U., & Dupuy, C. (2012) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2012.04.002 · Cited by 114

Redox Imbalance in Idiopathic Pulmonary Fibrosis: A Role for Oxidant Cross-Talk Between NADPH Oxidase Enzymes and Mitochondria

Veith, C., Boots, A. W., Idris, M., van Schooten, F., & van der Vliet, A. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7742 · Cited by 114

Redox regulation of the protein tyrosine phosphatase PTP1B in cancer cells

Lou, Y., Chen, Y., Hsu, S.-F., Chen, R., Lee, C., Khoo, K., Tonks, N. K., & Meng, T. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.06173.x · Cited by 115

Roles and regulation of microglia activity in multiple sclerosis: insights from animal models

Distéfano‐Gagné, F., Bitarafan, S., Lacroix, S., & Gosselin, D. (2023) · Nature reviews. Neuroscience · doi:10.1038/s41583-023-00709-6 · Cited by 115

NOX4 as an oxygen sensor to regulate TASK-1 activity

Lee, Y.-M., Kim, B., Chun, Y., So, I., Choi, H., Kim, M.-S., & Park, J. (2005) · Cellular Signalling · doi:10.1016/j.cellsig.2005.05.025 · Cited by 113

NADPH oxidase-derived reactive oxygen species in cardiac pathophysiology

Cave, A. C., Grieve, D., Johar, S., Zhang, M., & Shah, A. M. (2005) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2005.1772 · Cited by 113

NADPH Oxidases in Lung Health and Disease

Bernard, K. F., Hecker, L., Luckhardt, T., Cheng, G., & Thannickal, V. J. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5608 · Cited by 112

Redox proteomics analysis to decipher the neurobiology of Alzheimer-like neurodegeneration: overlaps in Down's syndrome and Alzheimer's disease brain

Butterfield, D. A., Domenico, F. D., Swomley, A. M., Head, E., & Marzia Perluigi, A. (2014) · Biochemical Journal · doi:10.1042/bj20140772 · Cited by 112

c-Src–Mediated Phosphorylation of NoxA1 and Tks4 Induces the Reactive Oxygen Species (ROS)–Dependent Formation of Functional Invadopodia in Human Colon Cancer Cells

Gianni, D., Taulet, N., DerMardirossian, C. M., & Bokoch, G. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-08-0685 · Cited by 112

Simvastatin Inhibits Activation of NADPH Oxidase/p38 MAPK Pathway and Enhances Expression of Antioxidant Protein in Parkinson Disease Models

Tong, H., Zhang, X., Meng, X., Lu, L., Mai, D., & Qu, S. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00165 · Cited by 112

Inhibition of NADPH oxidase by apocynin prevents learning and memory deficits in a mouse Parkinson's disease model

Hou, L., Sun, F., Huang, R., Sun, W., Zhang, D., & Wang, Q. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101134 · Cited by 112

NADPH oxidases: redox regulation of cell homeostasis and disease

Kračun, D., Lopes, L. R., Cifuentes-Pagano, E., & Pagano, P. J. (2025) · Physiological Reviews · doi:10.1152/physrev.00034.2023 · Cited by 114

Mutation of the Cyba gene encoding p22phox causes vestibular and immune defects in mice

Nakano, Y., Longo-Guess, C. M., Bergstrom, D. E., Nauseef, W. M., Jones, S. M., & Bánfi, B. (2008) · Journal of Clinical Investigation · doi:10.1172/jci33835 · Cited by 112

Nox1-dependent superoxide production controls colon adenocarcinoma cell migration

Sadok, A., Bourgarel‐Rey, V., Gattacceca, F., Penel, C., Lehmann, M., & Kovacic, H. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2007.10.010 · Cited by 112

Extracellular Superoxide Dismutase Attenuates Lipopolysaccharide-Induced Neutrophilic Inflammation

Bowler, R. P., Nicks, M., Tran, K. C., Tanner, G., Chang, L., Young, S. K., & Worthen, G. S. (2004) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2004-0057oc · Cited by 111

NADPH oxidase 1 plays a critical mediating role in oncogenic Ras-induced vascular endothelial growth factor expression

Komatsu, D., Kato, M., Nakayama, J., Miyagawa, S., & Kamata, T. (2008) · Oncogene · doi:10.1038/onc.2008.102 · Cited by 111

Selective role for superoxide in InsP3 receptor–mediated mitochondrial dysfunction and endothelial apoptosis

Madesh, M., Hawkins, B. J., Milovanova, T. N., Bhanumathy, C. D., Joseph, S. K., RamachandraRao, S. P., Sharma, K., Kurosaki, T., & Fisher, A. B. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200505022 · Cited by 111

Novel p47 phox -Related Organizers Regulate Localized NADPH Oxidase 1 (Nox1) Activity

Gianni, D., Díaz, B., Taulet, N., Fowler, B. J., Courtneidge, S. A., & Bokoch, G. (2009) · Science Signaling · doi:10.1126/scisignal.2000370 · Cited by 110

Functional Analysis of the Trichoderma harzianum nox1 Gene, Encoding an NADPH Oxidase, Relates Production of Reactive Oxygen Species to Specific Biocontrol Activity against Pythium ultimum

Montero-Barrientos, M., Hermosa, R., Cardoza, R. E., Gutiérrez, S., & Monte, E. (2011) · Applied and Environmental Microbiology · doi:10.1128/aem.02486-10 · Cited by 110

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)