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

Novel isoforms of NADPH-oxidase in cerebral vascular control

Miller, A. A., Drummond, G. R., & Sobey, C. G. (2006) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2006.02.005 · Cited by 110

Oxidative Stress Causes Mineralocorticoid Receptor Activation in Rat Cardiomyocytes

Nagase, M., Ayuzawa, N., Kawarazaki, W., Ishizawa, K., Ueda, K., Yoshida, S., & Fujita, T. (2012) · Hypertension · doi:10.1161/hypertensionaha.111.185520 · Cited by 110

Proinflammatory Cytokine IL-1β Stimulates IL-8 Synthesis in Mast Cells via a Leukotriene B4 Receptor 2-Linked Pathway, Contributing to Angiogenesis

Kim, G.-Y., Lee, J.-W., Ryu, H.-C., Wei, J.-D., Seong, C., & Kim, J. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0901735 · Cited by 109

Nox2, Ca 2+ , and Protein Kinase C Play a Role in Angiotensin II-Induced Free Radical Production in Nucleus Tractus Solitarius

Wang, G., Anrather, J., Glass, M. J., Tarsitano, M., Zhou, P., Frys, K. A., Pickel, V. M., & Iadecola, C. (2006) · Hypertension · doi:10.1161/01.hyp.0000236647.55200.07 · Cited by 109

Determinants of Ion-Transporter Cancer Cell Death

Park, S.-H., Park, S., Howe, E. N. W., Hyun, J. Y., Chen, L., Hwang, I., Vargas‐Zúñiga, G. I., Busschaert, N., Gale, P. A., Sessler, J. L., et al. (2019) · Chem · doi:10.1016/j.chempr.2019.05.001 · Cited by 109

Impaired OXPHOS Complex III in Breast Cancer

Owens, K. M., Kulawiec, M., Desouki, M., Vanniarajan, A., & Singh, K. K. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023846 · Cited by 109

Nox1 Redox Signaling Mediates Oncogenic Ras-induced Disruption of Stress Fibers and Focal Adhesions by Down-regulating Rho

Shinohara, M., Shang, W.-H., Kubodera, M., Harada, S., Mitsushita, J., Kato, M., Miyazaki, H., Sumimoto, H., & Kamata, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609450200 · Cited by 108

NADPH oxidase‐derived superoxide Anion‐induced apoptosis is mediated via the JNK‐dependent activation of NF‐κB in cardiomyocytes exposed to high glucose

Tsai, K.-H., Wang, W., Lin, C., Pai, P., Lai, T.-Y., Tsai, C., & Kuo, W. (2011) · Journal of Cellular Physiology · doi:10.1002/jcp.22847 · Cited by 108

Abiotic and Biotic Stress Response Crosstalk in Plants

Fraire-Velázquez, S., Rodríguez-Guerra, R., & Sánchez-Calderón, L. (2011) · InTech eBooks · doi:10.5772/23217 · Cited by 108

Berberine inhibits NADPH oxidase mediated superoxide anion production in macrophagesThis article is one of a selection of papers published in a Special Issue on Oxidative Stress in Health and Disease.

Sarna, L. K., Wu, N., Hwang, S., Siow, Y. L., & Karmin, O. (2010) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y09-136 · Cited by 108

Mitochondrial damage mediated by ROS incurs bronchial epithelial cell apoptosis upon ambient PM2.5 exposure

Jin, X., Xue, B., Zhou, Q., Su, R., & Li, Z. (2018) · The Journal of Toxicological Sciences · doi:10.2131/jts.43.101 · Cited by 107

Reactive oxygen species and NADPH oxidase 4 involvement in osteoarthritis

Drevet, S., Gavazzi, G., Grange, L., Dupuy, C., & Lardy, B. (2018) · Experimental Gerontology · doi:10.1016/j.exger.2018.07.007 · Cited by 107

NADPH oxidase regulates paraquat and maneb-induced dopaminergic neurodegeneration through ferroptosis

Hou, L., Huang, R., Sun, F., Zhang, L., & Wang, Q. (2019) · Toxicology · doi:10.1016/j.tox.2019.02.011 · Cited by 107

Andrographolide inhibits TNFα-induced ICAM-1 expression via suppression of NADPH oxidase activation and induction of HO-1 and GCLM expression through the PI3K/Akt/Nrf2 and PI3K/Akt/AP-1 pathways in human endothelial cells

Lu, C., Yang, Y., Li, C., Liu, K., Lii, C., & Chen, H. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.06.024 · Cited by 107

Idh1 protects murine hepatocytes from endotoxin-induced oxidative stress by regulating the intracellular NADP+/NADPH ratio

Itsumi, M., Inoue, S., Elia, A., Murakami, K., Sasaki, M., Lind, E. F., Brenner, D., Harris, I. S., Chio, I. I. C., Afzal, S., et al. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.38 · Cited by 107

Reactive Oxygen Generated by NADPH Oxidase 1 (Nox1) Contributes to Cell Invasion by Regulating Matrix Metalloprotease-9 Production and Cell Migration

Shinohara, M., Adachi, Y., Mitsushita, J., Kuwabara, M., Nagasawa, A., Harada, S., Furuta, S., Zhang, Y., Seheli, K., Miyazaki, H., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.071779 · Cited by 107

Downstream Targets and Intracellular Compartmentalization in Nox Signaling

Chen, K., Craige, S. M., & Keaney, J. F. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2594 · Cited by 106

Redox Signaling in Neurotransmission and Cognition During Aging

Kumar, A., Yegla, B., & Foster, T. C. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7111 · Cited by 106

Versatile Histochemical Approach to Detection of Hydrogen Peroxide in Cells and Tissues Based on Puromycin Staining

Chung, C. Y., Timblin, G. A., Saijo, K., & Chang, C. J. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b02279 · Cited by 106

Reactive oxygen species produced by altered tumor metabolism impacts cancer stem cell maintenance

Tuy, K., Rickenbacker, L., & Hjelmeland, A. B. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101953 · Cited by 107

Singlet Oxygen Generation by Cyclometalated Complexes and Applications

Ashen‐Garry, D., & Selke, M. (2013) · Photochemistry and Photobiology · doi:10.1111/php.12211 · Cited by 106

Current methods in quantifying ROS and oxidative damage in Caenorhabditis elegans and other model organism of aging

Labuschagne, C. F., & Brenkman, A. B. (2013) · Ageing Research Reviews · doi:10.1016/j.arr.2013.09.003 · Cited by 106

Redox signalling involving NADPH oxidase-derived reactive oxygen species

Dworakowski, R., Anilkumar, N., Zhang, M., & Shah, A. M. (2006) · Biochemical Society Transactions · doi:10.1042/bst0340960 · Cited by 105

Requirement of FADD, NEMO, and BAX/BAK for Aberrant Mitochondrial Function in Tumor Necrosis Factor Alpha-Induced Necrosis

Irrinki, K. M., Mallilankaraman, K. B., Thapa, R. J., Chandramoorthy, H. C. K., Smith, F. J., Jog, N. R., Gandhirajan, R. K., Kelsen, S. G., Houser, S. R., May, M. J., et al. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05303-11 · Cited by 105

ROS signalling between endothelial cells and cardiac cells

Zhang, M., & Shah, A. M. (2014) · Cardiovascular Research · doi:10.1093/cvr/cvu050 · Cited by 105

Novel iron oxide–cerium oxide core–shell nanoparticles as a potential theranostic material for ROS related inflammatory diseases

Wu, Y., Yang, Y., Zhao, W., Xu, Z. P., Little, P. J., Whittaker, A. K., Zhang, R., & Ta, H. T. (2018) · Journal of Materials Chemistry B · doi:10.1039/c8tb00022k · Cited by 105

Understanding Reactive Oxygen Species in Bone Regeneration: A Glance at Potential Therapeutics and Bioengineering Applications

Sheppard, A. J., Barfield, A. M., Barton, R. S., & Dong, Y. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2022.836764 · Cited by 105

ROS-mediated platelet generation: a microenvironment-dependent manner for megakaryocyte proliferation, differentiation, and maturation

Chen, S., Su, Y., & Wang, J. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.253 · Cited by 105

Single europium-doped nanoparticles measure temporal pattern of reactive oxygen species production inside cells

Casanova, D., Bouzigues, C., Nguyen, T., Ramodiharilafy, R. O., Bouzhir-Sima, L., Gacoin, T., Boilot, J., Tharaux, P., & Alexandrou, A. (2009) · Nature Nanotechnology · doi:10.1038/nnano.2009.200 · Cited by 105

Antioxidant therapy in multiple sclerosis

Mirshafiey, A., & Mohsenzadegan, M. (2008) · Immunopharmacology and Immunotoxicology · doi:10.1080/08923970802331943 · Cited by 105

Enhanced ROS production by NADPH oxidase is correlated to changes in antioxidant enzyme activity in human heart failure

Borchi, E., Bargelli, V., Stillitano, F., Giordano, C., Sebastiani, M., Nassi, P., d’Amati, G., Cerbai, E., & Nediani, C. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.10.014 · Cited by 105

Complement receptor 3 mediates NADPH oxidase activation and dopaminergic neurodegeneration through a Src-Erk-dependent pathway

Hou, L., Wang, K., Zhang, C., Sun, F., Che, Y., Zhao, X., Zhang, D., Li, H., & Wang, Q. (2018) · Redox Biology · doi:10.1016/j.redox.2017.09.017 · Cited by 104

Apoplastic and Chloroplastic Redox Signaling Networks in Plant Stress Responses

Sierla, M., Rahikainen, M. M., Salojärvi, J., Kangasjärvi, J., & Kangasjärvi, S. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.5016 · Cited by 104

Role of NADPH Oxidase in Endothelial Ischemia/Reperfusion Injury in Humans

Loukogeorgakis, S., van den Berg, J. M., Sofat, R., Nitsch, D., Charakida, M., Haiyee, B., de Groot, E., MacAllister, R. J., Kuijpers, T. W., & Deanfield, J. E. (2010) · Circulation · doi:10.1161/circulationaha.108.814731 · Cited by 104

Magnaporthe oryzae Effector AVR-Pii Helps to Establish Compatibility by Inhibition of the Rice NADP-Malic Enzyme Resulting in Disruption of Oxidative Burst and Host Innate Immunity

Singh, R. P., Dangol, S., Chen, Y., Choi, J., Cho, Y., Lee, J.-E., Choi, M.-O., & Jwa, N. (2016) · Molecules and Cells · doi:10.14348/molcells.2016.0094 · Cited by 104

Role of Oxidants in Mast Cell Activation

Suzuki, Y., Yoshimaru, T., Inoué, T., Niide, O., & Ra, C. (2005) · KARGER eBooks · doi:10.1159/000087569 · Cited by 104

Clues to Neuro-Degeneration in Niemann-Pick Type C Disease from Global Gene Expression Profiling

Reddy, J. V., Ganley, I. G., & Pfeffer, S. R. (2006) · PLoS ONE · doi:10.1371/journal.pone.0000019 · Cited by 104

Overcoming resistance to histone deacetylase inhibitors in human leukemia with the redox modulating compound β-phenylethyl isothiocyanate

Hu, Y., Lu, W., Chen, G., Zhang, H., Jia, Y., Wei, Y., Yang, H., Zhang, W., Fiskus, W. C., Bhalla, K. N., et al. (2010) · Blood · doi:10.1182/blood-2009-11-256354 · Cited by 104

Diesel exhaust particles induce matrix metalloprotease-1 in human lung epithelial cells via a NADP(H) oxidase/NOX4 redox-dependent mechanism

Amara, N., Bachoual, R., Desmard, M., Gołda, S., Guichard, C., Lanone, S., Aubier, M., Ogier‐Denis, É., & Boczkowski, J. (2007) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00445.2006 · Cited by 104

Advanced glycation end-products induce injury to pancreatic beta cells through oxidative stress

Lin, N., Zhang, H., & Su, Q. (2012) · Diabetes & Metabolism · doi:10.1016/j.diabet.2012.01.003 · Cited by 103

Post-treatment with an ultra-low dose of NADPH oxidase inhibitor diphenyleneiodonium attenuates disease progression in multiple Parkinson’s disease models

Wang, Q., Li, Q., Chen, S., Chu, C., Wilson, B. C., Oyarzabal, E. A., Ali, S. F., Robinson, B. L., Rao, D. B., & Hong, J. (2015) · Brain · doi:10.1093/brain/awv034 · Cited by 103

Reactivation of oxidized PTP1B and PTEN by thioredoxin 1

Schwertassek, U., Haque, A., Krishnan, N., Greiner, R., Weingarten, L., Dick, T. P., & Tonks, N. K. (2014) · FEBS Journal · doi:10.1111/febs.12898 · Cited by 104

A sensitive electrochemical nonenzymatic biosensor for the detection of H2O2 released from living cells based on ultrathin concave Ag nanosheets

Ma, B., Kong, C., Hu, X., Liu, K., Huang, Q., Lv, J., Lu, W., Zhang, X., Yang, Z., & Yang, S. X. (2018) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2018.01.041 · Cited by 103

Primary immunodeficiencies reveal the essential role of tissue neutrophils in periodontitis

Silva, L. M., Brenchley, L., & Moutsopoulos, N. M. (2018) · Immunological Reviews · doi:10.1111/imr.12724 · Cited by 103

Activation of microglia with zymosan promotes excitatory amino acid release via volume‐regulated anion channels: the role of NADPH oxidases

Harrigan, T. J., Abdullaev, I. F., Jourd’heuil, D., & Mongin, A. A. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05553.x · Cited by 103

Respiratory Syncytial Virus Infection: Mechanisms of Redox Control and Novel Therapeutic Opportunities

Garofalo, R. P., Kolli, D., & Casola, A. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4307 · Cited by 103

HaCaT Keratinocytes Overexpressing the S100 Proteins S100A8 and S100A9 Show Increased NADPH Oxidase and NF-κB Activities

Benedyk‐Machaczka, M., Sopalla, C., Nacken, W. K. F., Bode, G., Melkonyan, H., Bánfi, B., & Kerkhoff, C. (2007) · Journal of Investigative Dermatology · doi:10.1038/sj.jid.5700820 · Cited by 103

Redox Regulation of Interleukin-4 Signaling

Sharma, P., Chakraborty, R., Wang, L., Min, B., Tremblay, M. L., Kawahara, T., Lambeth, J. D., & Haque, S. J. (2008) · Immunity · doi:10.1016/j.immuni.2008.07.019 · Cited by 103

NADPH Oxidases in the Gastrointestinal Tract: A Potential Role of Nox1 in Innate Immune Response and Carcinogenesis

Rokutan, K., Kawahara, T., Kuwano, Y., Tominaga, K., Sekiyama, A., & Teshima-Kondo, S. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1573 · Cited by 105

Reactive Oxygen Species Generation Is Involved in Epidermal Growth Factor Receptor Transactivation through the Transient Oxidization of Src Homology 2-Containing Tyrosine Phosphatase in Endothelin-1 Signaling Pathway in Rat Cardiac Fibroblasts

Chen, C., Cheng, T., Lin, H., Shih, N., Chen, Y., Chen, Y.-S., Cheng, C., Lian, W., Meng, T., Chiu, W., et al. (2006) · Molecular Pharmacology · doi:10.1124/mol.105.017558 · Cited by 103

Methyl Jasmonate: Putative Mechanisms of Action on Cancer Cells Cycle, Metabolism, and Apoptosis

Cesari, I. M., Carvalho, É., Rodrigues, M. F., Mendonça, B. D. S., Amoêdo, N. D., & Rumjanek, F. D. (2014) · International Journal of Cell Biology · doi:10.1155/2014/572097 · Cited by 102

NADPH oxidase 1 supports proliferation of colon cancer cells by modulating reactive oxygen species-dependent signal transduction

Juhasz, A. N., Markel, S., Gaur, S., Liu, H., Lu, J., Jiang, G., Wu, X., Antony, S., Wu, Y., Melillo, G., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.768283 · Cited by 101

Green Synthesis of Silver Nanoparticles by the Cyanobacteria Synechocystis sp.: Characterization, Antimicrobial and Diabetic Wound-Healing Actions

Younis, N. S., Mohamed, M. E., & Semary, N. A. H. E. (2022) · Marine Drugs · doi:10.3390/md20010056 · Cited by 102

Lipid Rafts and Oxidative Stress–Induced Cell Death

Morgan, M. J., Kim, Y., & Liu, Z.-G. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1658 · Cited by 101

Malaria circumsporozoite protein inhibits the respiratory burst in Kupffer cells

Усынин, И. Ф., Klotz, C., & Frevert, U. (2007) · Cellular Microbiology · doi:10.1111/j.1462-5822.2007.00982.x · Cited by 101

Nox enzymes and oxidative stress in the immunopathology of the gastrointestinal tract

Rokutan, K., Kawahara, T., Kuwano, Y., Tominaga, K., Nishida, K., & Teshima-Kondo, S. (2008) · Seminars in Immunopathology · doi:10.1007/s00281-008-0124-5 · Cited by 101

Process of aerenchyma formation and reactive oxygen species induced by waterlogging in wheat seminal roots

Xu, Q., Yang, L., Zhou, Z., Mei, F., Qu, L., & Zhou, G. S. (2013) · Planta · doi:10.1007/s00425-013-1947-4 · Cited by 101

Plant Defence: Biological Control

Mérillon, J., & Ramawat, K. G. (2011) · Springer eBooks · doi:10.1007/978-94-007-1933-0 · Cited by 101

Inactivation of NADPH oxidase organizer 1 Results in Severe Imbalance

Kiss, P. J., Knisz, J., Zhang, Y., Baltrušaitis, J., Sigmund, C. D., Thalmann, R., Smith, R. J., Verpy, E., & Bánfi, B. (2006) · Current Biology · doi:10.1016/j.cub.2005.12.025 · Cited by 101

Modulation of microglial pro-inflammatory and neurotoxic activity for the treatment of Parkinson’s disease

Liu, B. (2006) · The AAPS Journal · doi:10.1208/aapsj080369 · Cited by 100

Heart Failure and Mitochondrial Dysfunction

Knowlton, A. A., Chen, L., & Malik, Z. A. (2013) · Journal of Cardiovascular Pharmacology · doi:10.1097/01.fjc.0000432861.55968.a6 · Cited by 100

Targeting glycogen synthase kinase-3 for oxidative stress and neuroinflammation: Opportunities, challenges and future directions for cerebral stroke management

Rana, A. K., & Singh, D. (2018) · Neuropharmacology · doi:10.1016/j.neuropharm.2018.07.006 · Cited by 101

A tandem activity-based sensing and labeling strategy enables imaging of transcellular hydrogen peroxide signaling

Iwashita, H., Castillo, E., Messina, M. S., Swanson, R. A., & Chang, C. J. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2018513118 · Cited by 100

Fe3+ Reducing Power as the Most Common Assay for Understanding the Biological Functions of Antioxidants

Gülçın, İ., & Alwasel, S. H. (2025) · Processes · doi:10.3390/pr13051296 · Cited by 100

Evidence for a Superoxide Permeability Pathway in Endosomal Membranes

Mumbengegwi, D. R., Li, Q., Li, C., Bear, C. E., & Engelhardt, J. F. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.02038-07 · Cited by 100

Neferine ameliorates cardiomyoblast apoptosis induced by doxorubicin: possible role in modulating NADPH oxidase/ROS-mediated NFκB redox signaling cascade

Priya, L. B., Baskaran, R., Huang, C., & Padma, V. V. (2017) · Scientific Reports · doi:10.1038/s41598-017-12060-9 · Cited by 100

The Future Challenge of Reactive Oxygen Species (ROS) in Hypertension: From Bench to Bed Side

Togliatto, G., Lombardo, G., & Brizzi, M. F. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18091988 · Cited by 99

Quercetin attenuates zymosan-induced arthritis in mice

Guazelli, C. F. S., Staurengo‐Ferrari, L., Zarpelon, A. C., Pinho-Ribeiro, F. A., Ruiz-Miyazawa, K. W., Vicentini, F. T. M. C., Vignoli, J. A., Camilios‐Neto, D., Georgetti, S. R., Baracat, M. M., et al. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.03.057 · Cited by 99

Proton leak regulates mitochondrial reactive oxygen species generation in endothelial cell activation and inflammation - A novel concept

Nanayakkara, G., Wang, H., & Yang, X. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.12.002 · Cited by 100

Engineering nanoparticles to overcome immunological barriers for enhanced drug delivery

Malachowski, T., & Hassel, A. (2020) · Engineered Regeneration · doi:10.1016/j.engreg.2020.06.001 · Cited by 99

Engineering Single‐Atom Nanozymes for Catalytic Biomedical Applications

Zhu, Y., Liao, Y., Zou, J., Cheng, J., Pan, Y., Lin, L., & Chen, X. S. (2023) · Small · doi:10.1002/smll.202300750 · Cited by 100

The reproductive and transgenerational toxicity of microplastics and nanoplastics: A threat to mammalian fertility in both sexes

He, Y., & Yin, R. (2023) · Journal of Applied Toxicology · doi:10.1002/jat.4510 · Cited by 100

NOX2 As a Target for Drug Development: Indications, Possible Complications, and Progress

Diebold, B. A., Smith, S. M., Yang, L., & Lambeth, J. D. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.5862 · Cited by 99

Enhanced expression of NADPH oxidase Nox4 in human gliomas and its roles in cell proliferation and survival

Shono, T., Yokoyama, N., Uesaka, T., Kuroda, J., Takeya, R., Yamasaki, T., Amano, T., Mizoguchi, M., Suzuki, S. O., Niiro, H., et al. (2008) · International Journal of Cancer · doi:10.1002/ijc.23569 · Cited by 99

In vitro anti-inflammatory effect of apigenin in the Helicobacter pylori-infected gastric adenocarcinoma cells

Wang, Y.-C., & Huang, K.-M. (2012) · Food and Chemical Toxicology · doi:10.1016/j.fct.2012.12.018 · Cited by 99

Mechanisms of Peroxynitrite Interactions with Heme Proteins

Su, J., & Groves, J. T. (2010) · Inorganic Chemistry · doi:10.1021/ic902157z · Cited by 99

Methionine sulfoxide reductase A down-regulation in human breast cancer cells results in a more aggressive phenotype

Luca, A. D., Sanna, F., Sallese, M., Ruggiero, C., Grossi, M., Sacchetta, P., Rossi, C., Laurenzi, V. D., Ilio, C. D., & Favaloro, B. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1010171107 · Cited by 99

Participation of superoxide in neutrophil activation and cytokine production

Mitra, S., & Abraham, E. H. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2006.06.011 · Cited by 99

Antimicrobial actions of dual oxidases and lactoperoxidase

Sarr, D., Tóth, E., Gingerich, A., & Rada, B. (2018) · Journal of Microbiology · doi:10.1007/s12275-018-7545-1 · Cited by 98

Chapter 14 Cerebral vascular dysregulation in the ischemic brain

(2008) · Handbook of Clinical Neurology · doi:10.1016/s0072-9752(08)01914-3 · Cited by 98

Nitric Oxide, NAD(P)H Oxidase, and Atherosclerosis

Müller, G. M., & Morawietz, H. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2403 · Cited by 98

Genetic Silencing of Nox2 and Nox4 Reveals Differential Roles of These NADPH Oxidase Homologues in the Vasopressor and Dipsogenic Effects of Brain Angiotensin II

Peterson, J. R., Burmeister, M. A., Tian, X., Zhou, Y., Guruju, M. R., Stupinski, J. A., Sharma, R. V., & Davisson, R. L. (2009) · Hypertension · doi:10.1161/hypertensionaha.109.140087 · Cited by 98

Reactive Oxygen Species in Pathogenesis of Atherosclerosis

Goncharov, N. V., Avdonin, P. V., Nadeev, A. D., Zharkikh, I. L., & Jenkins, R. O. (2014) · Current Pharmaceutical Design · doi:10.2174/1381612820666141014142557 · Cited by 99

Pathophysiological Roles of NADPH Oxidase/Nox Family Proteins in the Vascular System - Review and Perspective -

Ago, T., Kuroda, J., Kamouchi, M., Sadoshima, J., & Kitazono, T. (2011) · Circulation Journal · doi:10.1253/circj.cj-11-0388 · Cited by 98

From death receptor to reactive oxygen species and c‐Jun N‐terminal protein kinase: the receptor‐interacting protein 1 odyssey

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Redox Regulation and Its Emerging Roles in Stem Cells and Stem-Like Cancer Cells

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NADPH Oxidase 1 Overexpression Enhances Invasion via Matrix Metalloproteinase-2 and Epithelial–Mesenchymal Transition in Melanoma Cells

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Activation of AMPK Enhances Neutrophil Chemotaxis and Bacterial Killing

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Aquaporin8 regulates cellular development and reactive oxygen species production, a critical component of virulence in Botrytis cinerea

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The balance of powers: Redox regulation of fibrogenic pathways in kidney injury

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TrpA1 Regulates Defecation of Food-Borne Pathogens under the Control of the Duox Pathway

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Biological chemistry of superoxide radicals

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Crosstalk between endoplasmic reticulum stress and oxidative stress: a dynamic duo in multiple myeloma

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The Heart As a Target for Xenobiotic Toxicity: The Cardiac Susceptibility to Oxidative Stress

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Cognitive impairment in humanized APP×PS1 mice is linked to Aβ1–42 and NOX activation

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Mangiferin: A multipotent natural product preventing neurodegeneration in Alzheimer’s and Parkinson’s disease models

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Comparison of gene expression signatures of diamide, H2O2 and menadione exposed Aspergillus nidulans cultures – linking genome-wide transcriptional changes to cellular physiology

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NADPH oxidase 5 (NOX5) interacts with and is regulated by calmodulin

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Microbicidal protein psoriasin is a multifunctional modulator of neutrophil activation

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NOX2 deficiency attenuates markers of adiposopathy and brain injury induced by high-fat diet

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Molecular composition and regulation of the Nox family NAD(P)H oxidases

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The Nox Family of NAD(P)H Oxidases: Host Defense and Beyond

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Novel homologs of gp91phox

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Les Nox/Duox : une nouvelle famille de NADPH oxydases

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The Role of Reactive Oxygen Species

Cope, A. P. (2013)