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

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Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor

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

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The Neutrophil NADPH Oxidase

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Glycolysis regulates the expansion of myeloid-derived suppressor cells in tumor-bearing hosts through prevention of ROS-mediated apoptosis

Jian, S.-L., Chen, W., Su, Y., Su, Y., Chuang, T., Hsu, S., & Huang, L. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.192 · Cited by 187

Neutrophils from p40phox−/− mice exhibit severe defects in NADPH oxidase regulation and oxidant-dependent bacterial killing

Ellson, C. D., Davidson, K., Ferguson, G., O'Connor, R. P., Stephens, L., & Hawkins, P. T. (2006) · The Journal of Experimental Medicine · doi:10.1084/jem.20052069 · Cited by 186

Regulation of myocardial growth and death by NADPH oxidase

Maejima, Y., Kuroda, J., Matsushima, S., Ago, T., & Sadoshima, J. (2011) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2010.12.018 · Cited by 185

CO–metal interaction: vital signaling from a lethal gas

Boczkowski, J., Poderoso, J. J., & Motterlini, R. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.09.001 · Cited by 185

Redefining the major contributors to superoxide production in contracting skeletal muscle. The role of NAD(P)H oxidases

Sakellariou, G. K., Jackson, M. J., & Vasilaki, A. (2014) · Free Radical Research · doi:10.3109/10715762.2013.830718 · Cited by 184

Regulation of Late G1/S Phase Transition and APCCdh1by Reactive Oxygen Species

Havens, C. G., Ho, A. L., Yoshioka, N., & Dowdy, S. F. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00303-06 · Cited by 184

NADPH oxidases in cardiovascular disease: insights from in vivo models and clinical studies

Sirker, A. A., Zhang, M., & Shah, A. M. (2011) · Basic Research in Cardiology · doi:10.1007/s00395-011-0190-z · Cited by 184

SLAM is a microbial sensor that regulates bacterial phagosome functions in macrophages

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Pathogen Recognition and Activation of the Innate Immune Response in Zebrafish

van der Vaart, M., Spaink, H. P., & Meijer, A. H. (2012) · Advances in Hematology · doi:10.1155/2012/159807 · Cited by 184

Abiotic Stress Response in Plants - Physiological, Biochemical and Genetic Perspectives

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Use and abuse of exogenous H2O2 in studies of signal transduction

Forman, H. J. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.01.011 · Cited by 183

The expanding role of NADPH oxidases in health and disease: no longer just agents of death and destruction

Quinn, M. T., Ammons, M. C. B., & DeLeo, F. R. (2006) · Clinical Science · doi:10.1042/cs20060059 · Cited by 183

New Insights Into Molecular Mechanisms of Diabetic Kidney Disease

Badal, S. S., & Danesh, F. R. (2014) · American Journal of Kidney Diseases · doi:10.1053/j.ajkd.2013.10.047 · Cited by 183

Regulation of Apical Dominance in Aspergillus nidulans Hyphae by Reactive Oxygen Species

Semighini, C. P., & Harris, S. D. (2008) · Genetics · doi:10.1534/genetics.108.089318 · Cited by 183

NADPH Oxidases: The Vital Performers and Center Hubs during Plant Growth and Signaling

Hu, C., Wang, P., Zhang, P., Nie, X.-M., Li, B., Li, T., Liu, W., Li, W., & Chen, K. (2020) · Cells · doi:10.3390/cells9020437 · Cited by 183

The role of NADPH oxidases in infectious and inflammatory diseases

Taylor, J. P., & Tse, H. M. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102159 · Cited by 185

Mitochondrial Pathways, Permeability Transition Pore, and Redox Signaling in Cardioprotection: Therapeutic Implications

Penna, C. R. R., Perrelli, M.-G., & Pagliaro, P. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4459 · Cited by 182

Effects of spaceflight on innate immune function and antioxidant gene expression

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A p67Phox-Like Regulator Is Recruited to Control Hyphal Branching in a Fungal–Grass Mutualistic Symbiosis

Takemoto, D., Tanaka, A., & Scott, B. (2006) · The Plant Cell · doi:10.1105/tpc.106.046169 · Cited by 182

The arachidonic acid‐binding protein S100A8/A9 promotes NADPH oxidase activation by interaction with p67 phox and Rac‐2

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Redox regulation of protein kinases

Truong, T. H., & Carroll, K. S. (2013) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.790873 · Cited by 182

Mitochondria contribute to LPS-induced MAPK activation via uncoupling protein UCP2 in macrophages

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Superoxide production by NAD(P)H oxidase and mitochondria is increased in genetically obese and hyperglycemic rat heart and aorta before the development of cardiac dysfunction. The role of glucose-6-phosphate dehydrogenase-derived NADPH

Serpillon, S., Floyd, B. C., Gupte, R. S., George, S., Kozicky, M., Neito, V., Recchia, F. A., Stanley, W. C., Wolin, M. S., & Gupte, S. A. (2009) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01142.2008 · Cited by 181

AMPK, metabolism, and vascular function

Rodríguez, C., Muñoz, M., Contreras, C., & Prieto, D. (2021) · FEBS Journal · doi:10.1111/febs.15863 · Cited by 181

Exercise-induced hormesis and skeletal muscle health

Ji, L. L., Kang, C., & Zhang, Y. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.02.025 · Cited by 182

Oxidative stress in granulosa cells contributes to poor oocyte quality and IVF-ET outcomes in women with polycystic ovary syndrome

Lai, Q., Xiang, W., Li, Q., Zhang, H., Li, Y., Zhu, G., Xiong, C., & Jin, L. (2017) · Frontiers of Medicine · doi:10.1007/s11684-017-0575-y · Cited by 180

Neutrophil hyperactivation correlates with Alzheimer's disease progression

Dong, Y., Lagarde, J., Xicota, L., Corne, H., Chantran, Y., Chaigneau, T., Crestani, B., Bottlaender, M., Potier, M., Aucouturier, P., et al. (2018) · Annals of Neurology · doi:10.1002/ana.25159 · Cited by 180

Cathelicidin LL-37 induces the generation of reactive oxygen species and release of human α-defensins from neutrophils

Zheng, Y., Niyonsaba, F., Ushio, H., Nagaoka, I., Ikeda, S., Okumura, K., & Ogawa, H. (2007) · British Journal of Dermatology · doi:10.1111/j.1365-2133.2007.08196.x · Cited by 179

Structure and Function of the PB1 Domain, a Protein Interaction Module Conserved in Animals, Fungi, Amoebas, and Plants

Sumimoto, H., Kamakura, S., & Ito, T. (2007) · Science s STKE · doi:10.1126/stke.4012007re6 · Cited by 179

Redox Regulation of Protein Tyrosine Phosphatases: Structural and Chemical Aspects

Tanner, J. J., Parsons, Z. D., Cummings, A. H., Zhou, H., & Gates, K. S. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3611 · Cited by 178

NOX4 mediates hypoxia-induced proliferation of human pulmonary artery smooth muscle cells: the role of autocrine production of transforming growth factor-β1 and insulin-like growth factor binding protein-3

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

Prolonged Production of Reactive Oxygen Species in Response to B Cell Receptor Stimulation Promotes B Cell Activation and Proliferation

Wheeler, M. L., & DeFranco, A. L. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1201433 · Cited by 175

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

NADPH Oxidase 2 Interaction with TLR2 Is Required for Efficient Innate Immune Responses to Mycobacteria via Cathelicidin Expression

Yang, C., Shin, D., Kim, K.-H., Lee, Z.-W., Lee, C., Park, S. G., Bae, Y. S., & Jo, E. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0802217 · Cited by 175

Chronic Inflammatory Disorders and Their Redox Control: From Molecular Mechanisms to Therapeutic Opportunities

Chiurchiù, V., & Maccarrone, M. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3547 · Cited by 175

Mitochondrial function, ornamentation, and immunocompetence

Koch, R. E., Josefson, C. C., & Hill, G. E. (2016) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12291 · Cited by 176

NADPH oxidases as a source of oxidative stress and molecular target in ischemia/reperfusion injury

Kleikers, P. W. M., Wingler, K., Hermans, J. J. R., Diebold, I., Altenhöfer, S., Radermacher, K. A., Janssen, B. J., Görlach, A., & Schmidt, H. H. H. W. (2012) · Journal of Molecular Medicine · doi:10.1007/s00109-012-0963-3 · Cited by 173

Unraveling mitochondria‐targeting reactive oxygen species modulation and their implementations in cancer therapy by nanomaterials

Peng, H., Yao, F., Zhao, J., Zhang, W., Chen, L., Wang, X., Yang, P., Tang, J., & Chi, Y. (2023) · Exploration · doi:10.1002/exp.20220115 · Cited by 173

Regulation of cell proliferation by NADPH oxidase-mediated signaling: Potential roles in tissue repair, regenerative medicine and tissue engineering

Chan, E. C., Jiang, F., Peshavariya, H., & Dusting, G. J. (2009) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2009.02.005 · Cited by 172

Medicinal plant activity onHelicobacter pylorirelated diseases

Wang, Y.-C. (2014) · World Journal of Gastroenterology · doi:10.3748/wjg.v20.i30.10368 · Cited by 172

On the Relation of Oxidative Stress to Neuroinflammation: Lessons Learned from the G93A-SOD1 Mouse Model of Amyotrophic Lateral Sclerosis

Hensley, K., Mhatre, M., Mou, S., Pye, Q. N., Stewart, C. A., West, M. S., & Williamson, K. S. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.2075 · Cited by 172

Nox1 is over‐expressed in human colon cancers and correlates with activating mutations in K‐Ras

Laurent, E., McCoy, J. W., Macina, R. A., Liu, W., Cheng, G., Robine, S., Papkoff, J., & Lambeth, J. D. (2008) · International Journal of Cancer · doi:10.1002/ijc.23423 · Cited by 170

Nox4 regulates Nrf2 and glutathione redox in cardiomyocytes in vivo

Brewer, A. C., Murray, T. V., Arno, M. J., Zhang, M., Anilkumar, N. P., Mann, G. E., & Shah, A. M. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.04.022 · Cited by 170

The roles of NADPH oxidase and phospholipases A2in oxidative and inflammatory responses in neurodegenerative diseases

Sun, G. Y., Horrocks, L. A., & Farooqui, A. A. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04670.x · Cited by 170

Update on Inflammatory Biomarkers and Treatments in Ischemic Stroke

Bonaventura, A., Liberale, L., Vecchié, A., Casula, M., Carbone, F., Dallegri, F., & Montecucco, F. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17121967 · Cited by 170

NADPH oxidases in oxidant production by microglia: activating receptors, pharmacology and association with disease

Haslund‐Vinding, J., McBean, G., Jaquet, V, & Vilhardt, F. (2017) · British Journal of Pharmacology · doi:10.1111/bph.13425 · Cited by 169

Autophagy Protein Rubicon Mediates Phagocytic NADPH Oxidase Activation in Response to Microbial Infection or TLR Stimulation

Yang, C., Lee, J., Rodgers, M. A., Min, C., Lee, J., Kim, H. J., Lee, K.-H., Kim, C., Oh, B., Zandi, E., et al. (2012) · Cell Host & Microbe · doi:10.1016/j.chom.2012.01.018 · Cited by 169

NADPH oxidase-derived reactive oxygen species: involvement in vascular physiology and pathology

Manea, A. (2010) · Cell and Tissue Research · doi:10.1007/s00441-010-1060-y · Cited by 169

NADPH Oxidase-Derived Overproduction of Reactive Oxygen Species Impairs Postischemic Neovascularization in Mice with Type 1 Diabetes

Ebrahimian, T. G., Heymes, C., Broquères-You, D., Blanc‐Brude, O., Mees, B., Waeckel, L., Duriez, M., Vilar, J., Brandes, R. P., Levy, B. I., et al. (2006) · American Journal Of Pathology · doi:10.2353/ajpath.2006.060042 · Cited by 168

Hepatocyte nicotinamide adenine dinucleotide phosphate reduced oxidase 4 regulates stress signaling, fibrosis, and insulin sensitivity during development of steatohepatitis in mice

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

Environmental Exposures and Autoimmune Diseases: Contribution of Gut Microbiome

Khan, M. F., & Wang, H. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2019.03094 · Cited by 167

T Cell Receptor Stimulation, Reactive Oxygen Species, and Cell Signaling

Williams, M. S., & Kwon, J. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.05.029 · Cited by 167

Innate immunity and gut–microbe mutualism in Drosophila

Ryu, J.-H., Ha, E.-M., & Lee, W. (2009) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2009.11.010 · Cited by 166

Human Urotensin II Is a Novel Activator of NADPH Oxidase in Human Pulmonary Artery Smooth Muscle Cells

Djordjevic, T., BelAiba, R. S., Bonello, S., Pfeilschifter, J. M., Hess, J., & Görlach, A. (2004) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000154279.98244.eb · Cited by 165

Redox signaling in cardiovascular pathophysiology: A focus on hydrogen peroxide and vascular smooth muscle cells

Byon, C. H., Heath, J. M., & Chen, Y. (2016) · Redox Biology · doi:10.1016/j.redox.2016.08.015 · Cited by 166

Preparation and use of MitoPY1 for imaging hydrogen peroxide in mitochondria of live cells

Dickinson, B. C., Lin, V., & Chang, C. J. (2013) · Nature Protocols · doi:10.1038/nprot.2013.064 · Cited by 164

Molecular and Histopathological Changes Associated with Keratoconus

Khaled, M. L., Helwa, I., Drewry, M. D., Seremwe, M., Estes, A. J., & Liu, Y. (2017) · BioMed Research International · doi:10.1155/2017/7803029 · Cited by 164

A Novel Human AlkB Homologue, ALKBH8, Contributes to Human Bladder Cancer Progression

Shimada, K., Nakamura, M., Anai, S., Velasco, M. A. D., Tanaka, M., Tsujikawa, K., Ouji, Y., & Konishi, N. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-3530 · Cited by 164

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

A two-photon fluorescent probe for ratiometric imaging of hydrogen peroxide in live tissue

Chung, C., Srikun, D., Lim, C. S., Chang, C. J., & Cho, B. R. (2011) · Chemical Communications · doi:10.1039/c1cc13583j · Cited by 163

Gene Therapy of Chronic Granulomatous Disease: The Engraftment Dilemma

Grez, M., Reichenbach, J., Schwäble, J., Seger, R. A., Dinauer, M. C., & Thrasher, A. J. (2010) · Molecular Therapy · doi:10.1038/mt.2010.232 · Cited by 163

Role of reactive oxygen species in fungal cellular differentiations

Scott, B., & Eaton, C. J. (2008) · Current Opinion in Microbiology · doi:10.1016/j.mib.2008.10.008 · Cited by 163

Roles of TRPM2 in oxidative stress

Takahashi, N., Kozai, D., Kobayashi, R., Ebert, M., & Mori, Y. (2011) · Cell Calcium · doi:10.1016/j.ceca.2011.04.006 · Cited by 163

Honey: An Advanced Antimicrobial and Wound Healing Biomaterial for Tissue Engineering Applications

Mieles, J. Y., Vyas, C., Aslan, E., Humphreys, G. J., Diver, C., & Bártolo, P. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14081663 · Cited by 162

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

Redox Control of the Survival of Healthy and Diseased Cells

Zhang, Y., Du, Y., Le, W., Wang, K., Kieffer, N., & Zhang, J. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3685 · Cited by 161

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

Fragile X syndrome

McLennan, Y., Polussa, J., Tassone, F., & Hagerman, R. (2011) · Current Genomics · doi:10.2174/138920211795677886 · Cited by 160

Cysteine S-Nitrosylation Protects Protein-tyrosine Phosphatase 1B against Oxidation-induced Permanent Inactivation

Chen, Y.-Y., Chu, H., Pan, K., Teng, C.-H., Wang, D.-L., Wang, A. H. ‐., Khoo, K., & Meng, T. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805287200 · Cited by 160

Bcr-Abl-mediated redox regulation of the PI3K/AKT pathway

Naughton, R., Quiney, C., Turner, S. D., & Cotter, T. G. (2009) · Leukemia · doi:10.1038/leu.2009.49 · Cited by 160

Taurine protects dopaminergic neurons in a mouse Parkinson’s disease model through inhibition of microglial M1 polarization

Che, Y., Hou, L., Sun, F., Zhang, C., Liu, X., Piao, F., Zhang, D., Li, H., & Wang, Q. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0468-2 · Cited by 160

The Influence of Reactive Oxygen Species in the Immune System and Pathogenesis of Multiple Sclerosis

Tavassolifar, M. J., Vodjgani, M., Salehi, Z., & Izad, M. H. (2020) · Autoimmune Diseases · doi:10.1155/2020/5793817 · Cited by 160

Quantitative phosphoproteomic analysis reveals common regulatory mechanisms between effector‐ and PAMP‐triggered immunity in plants

Kadota, Y., Liebrand, T. W. H., Goto, Y., Sklenář, J., Derbyshire, P., Menke, F. L. H., Torres, M. Á. M., Molina, A., Zipfel, C., Coaker, G., et al. (2018) · New Phytologist · doi:10.1111/nph.15523 · Cited by 159

Genetics and immunopathology of chronic granulomatous disease

Stasia, M. J., & Li, X. J. (2008) · Seminars in Immunopathology · doi:10.1007/s00281-008-0121-8 · Cited by 159

Protein Tyrosine Phosphorylation and Protein Tyrosine Nitration in Redox Signaling

Monteiro, H. P., Arai, R. J., & Travassos, L. R. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1853 · Cited by 158

Reactive oxygen and nitrogen species in normal physiological processes

Pourová, J., Kottová, M., Vopršalová, M., & Pour, M. (2009) · Acta Physiologica · doi:10.1111/j.1748-1716.2009.02039.x · Cited by 158

The Angiotensin-Converting Enzyme 2/Angiotensin (1–7)/Mas Axis Protects Against Lung Fibroblast Migration and Lung Fibrosis by Inhibiting the NOX4-Derived ROS-Mediated RhoA/Rho Kinase Pathway

Meng, Y., Li, T., Zhou, G.-S., Chen, Y., Yu, C., Pang, M.-X., Li, W., Li, Y., Zhang, W., & Li, X. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5818 · Cited by 157

NADPH Oxidase Promotes Pancreatic Cancer Cell Survival via Inhibiting JAK2 Dephosphorylation by Tyrosine Phosphatases

Lee, J. K., Edderkaoui, M., Truong, P. A., Ohno, I., Jang, K., Berti, A., Pandol, S. J., & Gukovskaya, A. S. (2007) · Gastroenterology · doi:10.1053/j.gastro.2007.08.022 · Cited by 157

Amyotrophic Lateral Sclerosis: From Current Developments in the Laboratory to Clinical Implications

Cozzolino, M., Ferri, A., & Teresa Carrì, M. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1760 · Cited by 156

Reactive Oxygen Species Derived from NOX1/NADPH Oxidase Enhance Inflammatory Pain

Ibi, M., Matsuno, K., Shiba, D., Katsuyama, M., Iwata, K., Kakehi, T., Nakagawa, T., Sango, K., Shirai, Y., Yokoyama, T., et al. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.1857-08.2008 · Cited by 156

Conformation-Sensing Antibodies Stabilize the Oxidized Form of PTP1B and Inhibit Its Phosphatase Activity

Haque, A., Andersen, J. N., Salmeen, A. E., Barford, D., & Tonks, N. K. (2011) · Cell · doi:10.1016/j.cell.2011.08.036 · Cited by 158

Silencing of DUOX NADPH Oxidases by Promoter Hypermethylation in Lung Cancer

Luxen, S., Belinsky, S. A., & Knaus, U. G. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-5782 · Cited by 156

Reactive oxygen species-responsive drug delivery systems for the treatment of neurodegenerative diseases

Ballance, W. C., Qin, E. C., Chung, H. J., Gillette, M. U., & Kong, H. (2019) · Biomaterials · doi:10.1016/j.biomaterials.2019.119292 · Cited by 156

NOX Enzymes and Pulmonary Disease

Griffith, B. D., Pendyala, S., Hecker, L., Lee, P. J., Natarajan, V., & Thannickal, V. J. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2599 · Cited by 156

Pulmonary Neuroendocrine Cell System in Pediatric Lung Disease—Recent Advances

Cutz, E., Yeger, H., & Pan, J. (2006) · Pediatric and Developmental Pathology · doi:10.2350/07-04-0267 · Cited by 156

Redox Regulation of Transient Receptor Potential Channels

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Myotube depolarization generates reactive oxygen species through NAD(P)H oxidase; ROS‐elicited Ca2+ stimulates ERK, CREB, early genes

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