The DOI matches its Crossref record; 53 of the 53 references it cites were found in a registry or an index.
Functional analysis of Nox4 reveals unique characteristics compared to other NADPH oxidases
Abstract
Reactive oxygen species (ROS) are important signal transduction molecules in ligand-induced signaling, regulation of cell growth, differentiation, apoptosis and motility. Recently NADPH oxidases (Nox) homologous to Nox2 (gp91phox) of phagocyte cytochrome b558 have been identified, which are an enzymatic source for ROS generation in epithelial cells. This study was undertaken to delineate the requirements for ROS generation by Nox4. Nox4, in contrast to other Nox proteins, produces large amounts of hydrogen peroxide constitutively. Known cytosolic oxidase proteins or the GTPase Rac are not required for this activity. Nox4 associates with the protein p22phox on internal membranes, where ROS generation occurs. Knockdown and gene transfection studies confirmed that Nox4 requires p22phox for ROS generation. Mutational analysis revealed structural requirements affecting expression of the p22phox protein and Nox activity. Mechanistic insight into ROS regulation is significant for understanding fundamental cell biology and pathophysiological conditions.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“NOX4 is distinct from NOX2 in its ability to generate directly both O2•− and H2O2 (25).”
From Skeletal muscle NOX4 is required for adaptive responses that prevent insulin resistance (2021) · cites this paper as [25]
Citations
Cites
Free Radicals in the Physiological Control of Cell Function
Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855
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
PDZ Domains and the Organization of Supramolecular Complexes
Sheng, M., & Sala, C. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1 · Cited by 1,211
Reactive Oxygen Species as Intracellular Messengers During Cell Growth and Differentiation
Sauer, H., Wartenberg, M., & Hescheler, J. (2001) · Cellular Physiology and Biochemistry · doi:10.1159/000047804 · Cited by 1,118
Vascular NAD(P)H oxidases: specific features, expression, and regulation
Lassegue, B. P., & Clempus, R. E. (2003) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00758.2002 · Cited by 1,026
Identification of Renox, an NAD(P)H oxidase in kidney
Geiszt, M., Kopp, J. B., Várnai, P., & Leto, T. L. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.130135897 · Cited by 840
Homologs of gp91 phox : cloning and tissue expression of Nox3, Nox4, and Nox5
Cheng, G., Cao, Z., Xu, X., Meir, E. G. V., & Lambeth, J. D. (2001) · Gene · doi:10.1016/s0378-1119(01)00449-8 · Cited by 820
The superoxide-generating NADPH oxidase: structural aspects and activation mechanism
Vignais, P. V. (2002) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-002-8520-9 · Cited by 799
Planat‐Benard, V., Bohl, B. P., & Bokoch, G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.19.13198 · Cited by 754
Frangioni, J. V., Beahm, P. H., Shifrin, V. I., Jost, C. A., & Neel, B. G. (1992) · Cell · doi:10.1016/0092-8674(92)90190-n · Cited by 596
Flagged first, then by citations
Research works printed but not linked: 1
- Nimnual, 2003, Nature, 5, 236
Cited by
Sorted by citations
Items 401–500 of 782
Hypoxia and Reactive Oxygen Species as Modulators of Endoplasmic Reticulum and Golgi Homeostasis
Mennerich, D., Kellokumpu, S., & Kietzmann, T. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7523 · Cited by 49
Nox4 B-loop Creates an Interface between the Transmembrane and Dehydrogenase Domains
Jackson, H. M., Kawahara, T., Nisimoto, Y., Smith, S. M. E., & Lambeth, J. D. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.084939 · Cited by 51
NADPH oxidase 4 promotes cardiac microvascular angiogenesis after hypoxia/reoxygenation in vitro
Wang, J., Hong, Z., Zeng, C., Yu, Q., & Wang, H. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.01.027 · Cited by 48
Sarath, T. S., Waghe, P., Gupta, P., Choudhury, S., Kannan, K., Pillai, A. H., Harikumar, S. K., Mishra, S. K., & Sarkar, S. N. (2014) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2014.08.032 · Cited by 48
Egea, G., Jiménez‐Altayó, F., & Campuzano, V. (2020) · Antioxidants · doi:10.3390/antiox9101013 · Cited by 52
Human platelet lysate‐derived extracellular vesicles enhance angiogenesis through miR ‐126
Bordin, A., Chirivì, M., Pagano, F., Milan, M., Iuliano, M., Scaccia, E., Fortunato, O., Mangino, G., Dhori, X., Marinis, E. D., et al. (2022) · Cell Proliferation · doi:10.1111/cpr.13312 · Cited by 48
Wang, Y., Wang, Y., Liu, D., Wang, W., Zhao, H., Wang, M., & Yin, H. (2015) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2015.02.012 · Cited by 46
Siani, A., & Tirelli, N. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5724 · Cited by 45
Nox-4 and progressive kidney disease
Thallas‐Bonke, V., Jandeleit-Dahm, K. A. M., & Cooper, M. E. (2014) · Current Opinion in Nephrology & Hypertension · doi:10.1097/mnh.0000000000000082 · Cited by 46
Thick Ascending Limb Sodium Transport in the Pathogenesis of Hypertension
Gonzalez‐Vicente, A., Sáez, F., Monzon, C. M., Asirwatham, J., & Garvin, J. L. (2018) · Physiological Reviews · doi:10.1152/physrev.00055.2017 · Cited by 46
NADPH Oxidase 4 Regulates Inflammation in Ischemic Heart Failure: Role of Soluble Epoxide Hydrolase
Stevenson, M., Canugovi, C., Vendrov, A. E., Hayami, T., Bowles, D. E., Krause, K., Madamanchi, N. R., & Runge, M. S. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7548 · Cited by 46
Wang, F., Wang, H., Liu, X., Yu, H., Huang, X., Huang, W. Y., & Wang, G. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.16287 · Cited by 45
Harel, S., Mayaki, D., Sánchez, V., & Hussain, S. N. A. (2017) · Vascular Pharmacology · doi:10.1016/j.vph.2017.03.002 · Cited by 44
Chenevier‐Gobeaux, C., Lemaréchal, H., Bonnefont‐Rousselot, D., Poiraudeau, S., Ekindjian, O. G., & Borderie, D. (2006) · Inflammation Research · doi:10.1007/s00011-006-6036-8 · Cited by 47
Faraci, F. M. (2006) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000238355.56172.b3 · Cited by 45
NOX, NOX Who is There? The Contribution of NADPH Oxidase One to Beta Cell Dysfunction
Taylor, D. (2013) · Frontiers in Endocrinology · doi:10.3389/fendo.2013.00040 · Cited by 46
Liu, G. C., Fang, F., Zhou, J., Koulajian, K., Yang, S., Lam, L., Reich, H. N., John, R., Herzenberg, A. M., Giacca, A., et al. (2012) · Diabetologia · doi:10.1007/s00125-012-2586-1 · Cited by 44
Nox enzymes in allergic airway inflammation
van der Vliet, A. (2011) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.03.004 · Cited by 47
Chen, F., Haigh, S., Yu, Y., Benson, T. W., Wang, Y., Li, X., Dou, H., Bagi, Z. A., Verin, A. D., Stepp, D. W., et al. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.09.019 · Cited by 44
The Role of NOX4 and TRX2 in Angiogenesis and Their Potential Cross-Talk
Chen, C., Li, L., Zhou, H. J., & Wang, M. (2017) · Antioxidants · doi:10.3390/antiox6020042 · Cited by 43
Circadian Clock Control of Nox4 and Reactive Oxygen Species in the Vasculature
Anea, C. B., Zhang, M., Chen, F., Ali, M. I., Hart, C. M., Stepp, D. W., Kovalenkov, Y. O., Merloiu, A. M., Pati, P., Fulton, D. J., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0078626 · Cited by 43
Inhibitory Action of NoxA1 on Dual Oxidase Activity in Airway Cells
Pacquelet, S., Lehmann, M. D., Luxen, S., Regazzoni, K., Frausto, M., Noack, D., & Knaus, U. G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709108200 · Cited by 43
Self-citationKim, H. J., Magesh, V., Lee, J., Kim, S. Y., Knaus, U. G., & Lee, K. (2015) · Oncotarget · doi:10.18632/oncotarget.3843 · Cited by 44
Self-citationCIKS (Act1 or TRAF3IP2) mediates high glucose-induced endothelial dysfunction
Venkatesan, B. A., Valente, A. J., Das, N. A., Carpenter, A. J., Yoshida, T., Delafontaine, J.-L., Siebenlist, U. K., & Chandrasekar, B. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.10.009 · Cited by 43
The 1027th target candidate in stroke: Will NADPH oxidase hold up?
Radermacher, K. A., Wingler, K., Kleikers, P. W. M., Altenhöfer, S., Hermans, J. J. R., Kleinschnitz, C., & Schmidt, H. H. H. W. (2012) · Experimental & Translational Stroke Medicine · doi:10.1186/2040-7378-4-11 · Cited by 43
Zhang, G., Zhang, F., Muh, R., Yi, F., Chalupsky, K., Cai, H., & Li, P.-L. (2007) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00632.2006 · Cited by 42
Álvarez, L., Kovačič, L., Rodríguez, J., Gosemann, J., Kubica, M., Pîrcălăbioru, G. G., Friedmacher, F., Cean, A., Ghișe, A. D., Sărăndan, M., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1605443113 · Cited by 42
Self-citationRegulation of Smooth Muscle Cell Proliferation by NADPH Oxidases in Pulmonary Hypertension
Huetsch, J., Suresh, K. S., & Shimoda, L. A. (2019) · Antioxidants · doi:10.3390/antiox8030056 · Cited by 45
Zhang, A., Jia, Z., Wang, N., Tidwell, T. J., & Yang, T. (2011) · Kidney International · doi:10.1038/ki.2011.29 · Cited by 42
Yang, C., Chen, Z., Wong, S. L., Liu, J., Liang, Y. T., Lau, C. W., Lee, H. K., Huang, Y., & Tsang, S. Y. (2012) · Cardiovascular Research · doi:10.1093/cvr/cvs370 · Cited by 41
Nox4-dependent H2O2 production contributes to chronic glutamate toxicity in primary cortical neurons
Ha, J. S., Lee, J. E., Lee, J.-R., Lee, C.-S., Maeng, J.-S., Bae, Y. S., Kwon, K., & Park, S. S. (2010) · Experimental Cell Research · doi:10.1016/j.yexcr.2010.03.021 · Cited by 43
Park, J.-M., Do, V. Q., Seo, Y.-S., Kim, H. J., Nam, J. H., Yin, M. Z., Kim, H. J., Kim, S. J., Griendling, K. K., & Lee, M.-Y. (2022) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.121.317239 · Cited by 42
Ortiz, C., Caja, L., Sancho, P., Bertrán, E., & Fabregat, I. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2008.02.015 · Cited by 41
Nox-2 up-regulation and platelet activation: Novel insights
Pastori, D., Pignatelli, P., Carnevale, R., & Violi, F. (2015) · Prostaglandins & Other Lipid Mediators · doi:10.1016/j.prostaglandins.2015.03.010 · Cited by 42
Long-Term Cyclic Strain Downregulates Endothelial Nox4
Goettsch, C., Göettsch, W., Arsov, A., Hofbauer, L. C., Bornstein, S. R., & Morawietz, H. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2561 · Cited by 41
Redox Modifier Genes and Pathways in Amyotrophic Lateral Sclerosis
Carter, B. J., Anklesaria, P. N., Choi, S. H., & Engelhardt, J. F. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2414 · Cited by 42
Quinone compounds regulate the level of ROS production by the NADPH oxidase Nox4
Nguyen, M. V. C., Lardy, B., Rousset, F., Hazane‐Puch, F., Zhang, L., Trocmé, C., Serrander, L., Krause, K., & Morel, F. (2013) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.03.023 · Cited by 43
Wang, P., Tang, F., Li, R., Zhang, H., Chen, S., Liu, P., & Huang, H. (2007) · Pharmacological Research · doi:10.1016/j.phrs.2007.01.016 · Cited by 40
Dosoki, H., Stegemann, A., Taha, M., Schnittler, H., Luger, T. A., Schröder, K., Distler, J. H. W., Kerkhoff, C., & Böhm, M. (2017) · Experimental Dermatology · doi:10.1111/exd.13180 · Cited by 39
NOX2 is the primary source of angiotensin II-induced superoxide in the macula densa
Fu, Y., Zhang, R., Lu, D., Liu, H., Chandrashekar, K., Juncos, L. A., & Liu, R. (2010) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00762.2009 · Cited by 39
Kessler, S. M., Lederer, E., Laggai, S., Golob‐Schwarzl, N., Hosseini, K., Petzold, J., Schweiger, C., Reihs, R., Keil, M., Hoffmann, J., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.21116 · Cited by 39
Bridged tetrahydroisoquinolines as selective NADPH oxidase 2 (Nox2) inhibitors
Cifuentes-Pagano, E., Saha, J., Csányi, G., Ghouleh, I. A., Sahoo, S., Rodriguez, A. I., Wipf, P., Pagano, P. J., & Skoda, E. M. (2013) · MedChemComm · doi:10.1039/c3md00061c · Cited by 39
NADPH oxidase: recent evidence for its role in erectile dysfunction
Jin, L., & Burnett, A. L. “. (2008) · Asian Journal of Andrology · doi:10.1111/j.1745-7262.2008.00371.x · Cited by 37
Inhibition of human vascular nadph oxidase by apocynin derived oligophenols
Mora-Pale, M., Weïwer, M., Yu, J., Linhardt, R. J., & Dordick, J. S. (2009) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2009.05.061 · Cited by 36
NADPH Oxidases: Molecular Understanding Finally Reaching the Clinical Level?
Guzik, T. J., & Griendling, K. K. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2615 · Cited by 38
Adenosine A2A receptor signaling regulation of cardiac NADPH oxidase activity
Ribé, D., Sawbridge, D., Thakur, S., Hussey, M. J., Ledent, C. A., Kitchen, I., Hourani, S. M. O., & Li, J. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.12.035 · Cited by 38
Barangi, S., Hayes, A. W., & Karimi, G. (2017) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2017.1379000 · Cited by 40
Adventitial Fibroblast Nox4 Expression and ROS Signaling in Pulmonary Arterial Hypertension
Barman, S. A., & Fulton, D. J. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-63245-2_1 · Cited by 39
Zana, M., Péterfi, Z., Kovács, H. A., Tóth, Z., Enyedi, B., Morel, F., Paclet, M., Donkó, Á., Morand, S. C., Leto, T. L., et al. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.12.031 · Cited by 39
Szekeres, F. L. M., Walum, E., Wikström, P., & Arner, A. (2021) · Scientific Reports · doi:10.1038/s41598-021-91575-8 · Cited by 40
Role of NADPH oxidase in the regulation of autophagy in cardiomyocytes
Sciarretta, S., Yee, D., Ammann, P. B., Nagarajan, N., Volpe, M., Frati, G., & Sadoshima, J. (2014) · Clinical Science · doi:10.1042/cs20140336 · Cited by 36
Redox signaling at invasive microdomains in cancer cells
Díaz, B., & Courtneidge, S. A. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.09.016 · Cited by 38
Association between NADPH oxidase (NOX) and lung cancer: a systematic review and meta-analysis
Han, M., Zhang, T., Yang, L., Wang, Z., Ruan, J., & Chang, X. (2016) · Journal of Thoracic Disease · doi:10.21037/jtd.2016.06.31 · Cited by 41
NADPH oxidase 4 is dispensable for skin myofibroblast differentiation and wound healing
Siedlar, A. M., Seredenina, T. S., Faivre, A., Cambet, Y., Stasia, M. J., André‐Lévigne, D., Bochaton‐Piallat, M., Pittet-Cuenod, B. M., de Seigneux, S., Krause, K., et al. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102609 · Cited by 36
Hydrogen peroxide-producing NADPH oxidases and the promotion of migratory phenotypes in cancer
Meitzler, J. L., Konaté, M. M., & Doroshow, J. H. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.108076 · Cited by 37
Hypoxia-inducible factor-1 mediates pancreatic β-cell dysfunction by intermittent hypoxia
Wang, N., Shi, X., Khan, S. A., Wang, B. L., Semenza, G. L., Prabhakar, N. R., & Nanduri, J. (2020) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00309.2020 · Cited by 38
Yan, S., Resta, T. C., & Jernigan, N. L. (2020) · Antioxidants · doi:10.3390/antiox9100999 · Cited by 38
Medikayala, S., Piteo, B., Zhao, X., & Edwards, J. G. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00248.2010 · Cited by 36
Violi, F., & Pignatelli, P. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5790 · Cited by 37
Zhao, Q., Zhang, J., & Wang, H. (2015) · Bioscience Reports · doi:10.1042/bsr20150112 · Cited by 35
Green, D. E., Kang, B., Murphy, T. C., & Hart, C. M. (2012) · Pulmonary Circulation · doi:10.4103/2045-8932.105037 · Cited by 35
The TGF-β/NADPH Oxidases Axis in the Regulation of Liver Cell Biology in Health and Disease
Herranz‐Itúrbide, M., Peñuelas‐Haro, I., Espinosa‐Sotelo, R., Bertrán, E., & Fabregat, I. (2021) · Cells · doi:10.3390/cells10092312 · Cited by 37
Forsythiaside A Regulates Activation of Hepatic Stellate Cells by Inhibiting NOX4‐Dependent ROS
Zhou, M., Zhao, X., Liao, L., Deng, Y., Liu, M., Wang, J., Xue, X., & Li, Y. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/9938392 · Cited by 35
Block, K. L., Ricono, J. M., Lee, D., Bhandari, B., Choudhury, G. G., Abboud, H. E., & Gorin, Y. C. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1497 · Cited by 35
Xie, W., Parker, J. L., & Heaps, C. L. (2012) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01248.2011 · Cited by 35
Impaired Generation of Reactive Oxygen Species in Leprechaunism Through Downregulation of Nox4
Park, H. S., Jin, D., Shin, S. M., Jang, M. K., Longo, N., Park, J. W., Bae, D. S., & Bae, Y. S. (2005) · Diabetes · doi:10.2337/diabetes.54.11.3175 · Cited by 35
Garrido‐Urbani, S., Jemelin, S., Deffert, C., Carnésecchi, S., Basset, O., Szyndralewiez, C., Heitz, F., Page, P., Montet, X., Michalik, L., et al. (2011) · PLoS ONE · doi:10.1371/annotation/a392bbef-b0ec-4c70-b403-74a7bad85178 · Cited by 35
The mechanism of stem cell differentiation into smooth muscle cells
Wang, G., Luo, Z., Xu, Q., & Xiao, Q. (2010) · Thrombosis and Haemostasis · doi:10.1160/th09-11-0794 · Cited by 35
Gao, X., Sun, J., Huang, C., Hu, X., Jiang, N., & Lu, C. (2017) · PubMed Central · Cited by 34
Dec, K., Łukomska, A., Skonieczna‐Żydecka, K., Jakubczyk, K., Tarnowski, M., Lubkowska, A., Baranowska‐Bosiacka, I., Styburski, D., Skórka-Majewicz, M., Maciejewska, D., et al. (2020) · Biomolecules · doi:10.3390/biom10030422 · Cited by 34
Kirsch, M., Kemp‐Harper, B. K., Weißmann, N., Grimminger, F., & Schmidt, H. H. H. W. (2007) · The FASEB Journal · doi:10.1096/fj.06-7526com · Cited by 34
Qin, Z., Hou, X., Weisbrod, R. M., Seta, F., Cohen, R. A., & Tong, X. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.02.019 · Cited by 34
Liu, X., Hao, B., Ma, A., He, J., Liu, X., & Chen, J. (2016) · BioMed Research International · doi:10.1155/2016/2891810 · Cited by 31
Expression of NOX Family Genes and Their Clinical Significance in Colorectal Cancer
Cho, S. Y., Kim, J., Eun, H. S., Kang, S. H., Lee, E. S., Kim, S. H., Sung, J. K., Lee, B. S., Jeong, H. Y., & Moon, H. S. (2018) · Digestive Diseases and Sciences · doi:10.1007/s10620-018-5121-5 · Cited by 33
Stock, C. J. W., Michaeloudes, C., Leoni, P., Durham, A. L., Mumby, S. E., Wells, A. U., Chung, K. F., Adcock, I. M., Renzoni, E. A., & Lindahl, G. E. (2019) · BioMed Research International · doi:10.1155/2019/1484736 · Cited by 33
Chen, Z., Sun, X., Chen, Q., Lan, T., Huang, K., Xiao, H., Lin, Z., Yang, Y., Liu, P., & Huang, H. (2019) · British Journal of Pharmacology · doi:10.1111/bph.14853 · Cited by 33
Regulation of Metabolic Processes by Hydrogen Peroxide Generated by NADPH Oxidases
Vilchis‐Landeros, M. M., Matuz‐Mares, D., & Vázquez‐Meza, H. (2020) · Processes · doi:10.3390/pr8111424 · Cited by 33
Protective effect of 4,4'-diaminodiphenylsulfone against paraquat-induced mouse lung injury
Cho, S. C., Rhim, J. H., Choi, H. R., Son, Y. H., Lee, S. J., Song, K.-Y., & Park, S. C. (2011) · Experimental & Molecular Medicine · doi:10.3858/emm.2011.43.9.060 · Cited by 35
Tong, X., & Schröder, K. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.08.026 · Cited by 33
Park, S. J., Chun, Y., Park, K., Kim, S. J., Choi, S.-O., Kim, H.-L., & Park, J. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00463.2008 · Cited by 30
Zheleznova, N. N., Yang, C., & Cowley, A. W. (2016) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00187.2016 · Cited by 32
Regulation of NADPH Oxidases by G Protein-Coupled Receptors
Petry, A., & Görlach, A. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7525 · Cited by 34
Shi, Y., & Hou, S. (2021) · Molecular Medicine Reports · doi:10.3892/mmr.2021.12351 · Cited by 33
Taurine in adipocytes prevents insulin-mediated H2o2 generation and activates Pka and lipolysis
Piña-Zentella, G., de la Rosa-Cuevas, G., Vázquez‐Meza, H., Piña, E., & de Piña, M. Z. (2011) · Amino Acids · doi:10.1007/s00726-011-0919-x · Cited by 33
Mora‐Pale, M., Kwon, S., Linhardt, R. J., & Dordick, J. S. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.12.015 · Cited by 32
Guo, W., Saito, S., Sánchez, C. G., Zhuang, Y., Rosero, R. E. G., Shan, B., Luo, F., & Lasky, J. A. (2017) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00256.2016 · Cited by 32
Zinc homeostasis and redox alterations in obesity
Franco, C., & Canzoniero, L. M. T. (2024) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1273177 · Cited by 31
Cui, W., Matsuno, K., Iwata, K., Ibi, M., Katsuyama, M., Kakehi, T., Sasaki, M., Ikami, K., Zhu, K., & Yabe‐Nishimura, C. (2009) · Journal of Pharmacological Sciences · doi:10.1254/jphs.09148fp · Cited by 32
Statins in Endothelial Signaling and Activation
Jacobson, J. R. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2284 · Cited by 32
Jiang, F., Zhang, G., Hashimoto, I., Kumar, B. S. H., Bortolotto, S., Morrison, W. A., & Dusting, G. J. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00199.x · Cited by 31
Ha, S. Y., Paik, Y., Yang, J. W., Lee, M. J., Bae, H., & Park, C.-K. (2016) · Gut and Liver · doi:10.5009/gnl15543 · Cited by 31
Dayal, S., Baumbach, G. L., Arning, E., Bottiglieri, T., Faraci, F. M., & Lentz, S. R. (2017) · PLoS ONE · doi:10.1371/journal.pone.0175732 · Cited by 32
Cao, X., Dai, X., Parker, L. M., & Kreulen, D. L. (2007) · Hypertension · doi:10.1161/hypertensionaha.107.089748 · Cited by 32
Liang, X., Wang, Z., Gao, M. Q., Wu, S., Zhang, J., Liu, Q., Yu, Y., Wang, J., & Liu, W. (2019) · BMC Ophthalmology · doi:10.1186/s12886-019-1087-0 · Cited by 30
Ha, C., Bakshi, S., Brahma, M. K., Potter, L., Chang, S. F., Sun, Z., Benavides, G. A., He, L., Umbarkar, P., Zou, L., et al. (2023) · Journal of the American Heart Association · doi:10.1161/jaha.123.029898 · Cited by 29
Miyano, K., Okamoto, S., 山内, 明., Kawai, C., Kajikawa, M., Kiyohara, T., TAMURA, M. N., Taura, M., & Kuribayashi, F. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014723 · Cited by 31
Human iPSC model reveals a central role for NOX4 and oxidative stress in Duchenne cardiomyopathy
Duelen, R., Costamagna, D., Gilbert, G., Waele, L. D., Goemans, N., Desloovere, K., Verfaillie, C. M., Sipido, K. R., Buyse, G., & Sampaolesi, M. (2022) · Stem Cell Reports · doi:10.1016/j.stemcr.2021.12.019 · Cited by 31
Fletcher, N. M., Saed, M. G., Abuanzeh, S., Abu‐Soud, H. M., Al-Hendy, A. A., Diamond, M. P., & Saed, G. M. (2014) · Reproductive Sciences · doi:10.1177/1933719114522552 · Cited by 29
Nrf2 mediates redox adaptation in NOX4-overexpressed non-small cell lung cancer cells
Wu, Q., Yao, B., Li, N., Ma, L., Deng, Y., Yang, Y., Zeng, C., Yang, Z., & Liu, B. (2017) · Experimental Cell Research · doi:10.1016/j.yexcr.2017.02.014 · Cited by 29
Chronic Alcohol Ingestion Changes the Landscape of the Alveolar Epithelium
Downs, C. A., Trac, D. Q., Brewer, E. M., Brown, L. A. S., & Helms, M. N. (2012) · BioMed Research International · doi:10.1155/2013/470217 · Cited by 28
Metadata
- Authors
- Martyn, K. D., Frederick, L. M., von Loehneysen, K., Dinauer, M. C., & Knaus, U. G.
- Affiliations
- Scripps Research Institute (US)
- Indiana University Indianapolis (US)
- Corresponding author
- Knaus, Ulla G.
- Venue
- Cellular Signalling
- Publisher
- Elsevier BV
- Published
- 2006-01
- Volume
- 18
- Issue
- 1
- Pages
- 69-82
- ISSN
- 0898-6568 (ISSN-L)
- OpenAlex
- W1971215115
- Cited by
- 783
- References
- 53
- Citations by year
- 2026: 14 · 2025: 17 · 2024: 20 · 2023: 29 · 2022: 22 · 2021: 18 · 2020: 27 · 2019: 38 · 2018: 32 · 2017: 36 · 2016: 40 · 2015: 44 · 2014: 52 · 2013: 62 · 2012: 50
- FWCI
- 16.75
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Cellular Signalling (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Heart, Lung, and Blood Institute (HL 45635, R01HL045635)
- National Cancer Institute (CA-84138, R01CA084138)
- National Institute of General Medical Sciences (GM 37696, P01GM037696)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Keywords
- NOX4, NADPH oxidase, reactive oxygen species, hydrogen peroxide, p22phox, gp91phox, epithelial cells, protein association, gene knockdown, mutation analysis
- MeSH terms
- NADPH Oxidase 4, Animals, Cell Line, Cell Membrane, Chlorocebus aethiops, Cytosol, DNA Mutational Analysis, Epithelial Cells, Gene Expression Regulation, Humans, Hydrogen Peroxide, Phosphoproteins, Signal Transduction, Reactive Oxygen Species, NADPH Oxidases, COS Cells, rac GTP-Binding Proteins, Membrane Transport Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review