The phagocyte NOX2 NADPH oxidase in microbial killing and cell signaling
Open accessAbstract
The phagocyte NADPH oxidase possesses a transmembrane electron transferase comprised of gp91phox (aka NOX2) and p22phox and two multicomponent cytosolic complexes, which in stimulated phagocytes translocate to assemble a functional enzyme complex at plasma or phagosomal membranes. The NOX2-centered NADPH oxidase shuttles electrons from cytoplasmic NADPH to molecular oxygen in phagosomes or the extracellular space to produce oxidants that support optimal antimicrobial activity by phagocytes. Additionally, NOX2-generated oxidants have been implicated in both autocrine and paracrine signaling in a variety of biological contexts. However, when interpreting experimental results, investigators must recognize the complexity inherent in the biochemistry of oxidant-mediated attack of microbial targets and the technical limitations of the probes currently used to detect intracellular oxidants.
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After activation, neutrophils produce more O2•− compared to monocytes and macrophages.
“After activation, neutrophils produce more O2•− compared to monocytes and macrophages [178].”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [178]
In neutrophils, H2O2 generation in phagosomes activates myeloperoxidase, catalysing production of HOCl, which is oxidant and antimicrobial and contributes greatly to lysis of microbes.
“In neutrophils, H2O2 generation in phagosomes activates the enzyme myeloperoxidase, catalysing the production of HOCl, which is oxidant and antimicrobial, and contributes greatly to the lysis of microbes [178].”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [178]
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The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology
Bedard, K., & Krause, K.-H. (2007) · Physiological Reviews · doi:10.1152/physrev.00044.2005 · Cited by 6,989 · see citing works
Rioux, J. D., Xavier, R. J., Taylor, K. D., Silverberg, M. S., Goyette, P., Huett, A., Green, T., Kuballa, P., Barmada, M. M., Datta, L. W., et al. (2007) · Nature Genetics · doi:10.1038/ng2032 · Cited by 1,769 · see citing works
Bcl-2 inhibition of neural death: decreased generation of reactive oxygen species
Kane, D. J., Sarafian, T. A., Anton, R., Hahn, H., Gralla, E. B., Valentine, J. S., Örd, T., & Bredesen, D. E. (1993) · Science · doi:10.1126/science.8235659 · Cited by 1,671 · see citing works
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 · see citing works
Thiol chemistry and specificity in redox signaling
Winterbourn, C. C., & Hampton, M. B. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.05.004 · Cited by 1,226 · see citing works
Superoxide dismutases and superoxide reductases
Sheng, Y., Abreu, I. A., Cabelli, D. E., Maroney, M. J., Miller, A.-F., Teixeira, M., & Valentine, J. S. (2014) · Chemical Reviews · doi:10.1021/cr4005296 · Cited by 1,081 · see citing works
The basics of thiols and cysteines in redox biology and chemistry
Poole, L. B. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.11.013 · Cited by 1,031 · see citing works
Redox Regulation of NLRP3 Inflammasomes: ROS as Trigger or Effector?
Abais, J. M., Xia, M., Zhang, Y., Boini, K. M., & Li, P. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.5994 · Cited by 936 · see citing works
BABIOR, B. M., Lambeth, J. D., & Nauseef, W. M. (2002) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2642 · Cited by 911 · see citing works
Self-citationReactive Oxygen Species and Neutrophil Function
Winterbourn, C. C., Kettle, A. J., & Hampton, M. B. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014442 · Cited by 885 · see citing works
Wardman, P. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.06.026 · Cited by 863 · see citing works
Unraveling the biological roles of reactive oxygen species
Murphy, M. P., Holmgren, A., Larsson, N.-G., Halliwell, B., Chang, C. J., Kalyanaraman, B., Rhee, S. G., Thornalley, P. J., Partridge, L., Gems, D., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.03.010 · Cited by 836 · see citing works
How human neutrophils kill and degrade microbes: an integrated view
Nauseef, W. M. (2007) · Immunological Reviews · doi:10.1111/j.1600-065x.2007.00550.x · Cited by 756 · see citing works
Self-citationWoo, H. A., Yim, S. H., Shin, D. H., Kang, D., Yu, D., & Rhee, S. G. (2010) · Cell · doi:10.1016/j.cell.2010.01.009 · Cited by 613 · see citing works
The PX domains of p47phox and p40phox bind to lipid products of PI(3)K
Kanai, F., Liu, H., Field, S. J., Akbary, H., Matsuo, T., Brown, G. E., Cantley, L. C., & Yaffe, M. B. (2001) · Nature Cell Biology · doi:10.1038/35083070 · Cited by 611 · see citing works
Residual NADPH Oxidase and Survival in Chronic Granulomatous Disease
Kuhns, D. B., Alvord, W. G., Heller, T., Feld, J. J., Pike, K. M., Marciano, B. E., Uzel, G., DeRavin, S. S., Priel, D. A. L., Soule, B. P., et al. (2010) · New England Journal of Medicine · doi:10.1056/nejmoa1007097 · Cited by 568 · see citing works
Nox enzymes and new thinking on reactive oxygen: A double-edged sword revisited
Lambeth, J. D., & Neish, A. S. (2014) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-012513-104651 · Cited by 495 · see citing works
Priming of the neutrophil respiratory burst: role in host defense and inflammation
Benna, J. E., Hurtado-Nédelec, M., Marzaioli, V., Marie, J., Gougerot‐Pocidalo, M., & Dang, P. M. (2016) · Immunological Reviews · doi:10.1111/imr.12447 · Cited by 481 · see citing works
Redox Reactions and Microbial Killing in the Neutrophil Phagosome
Winterbourn, C. C., & Kettle, A. J. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4827 · Cited by 468 · see citing works
The Biological Chemistry of Hydrogen Peroxide
Winterbourn, C. C. (2013) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-405881-1.00001-x · Cited by 459 · see citing works
Winterbourn, C. C. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.05.004 · Cited by 420 · see citing works
Common Severe Infections in Chronic Granulomatous Disease
Marciano, B. E., Spalding, C. D., Fitzgerald, A., Mann, D. L., Brown, T., Osgood, S., Yockey, L., Darnell, D. N., Barnhart, L. A., Daub, J., et al. (2014) · Clinical Infectious Diseases · doi:10.1093/cid/ciu1154 · Cited by 419 · see citing works
Matute, J. D., Arias, A. A., Wright, N. A. M., Wrobel, I. T., Waterhouse, C. C. M., Li, X. J., Marchal, C. C., Stull, N. D., Lewis, D. B., Steele, M., et al. (2009) · Blood · doi:10.1182/blood-2009-07-231498 · Cited by 417 · see citing works
Self-citationHeyworth, P. G., Curnutte, J. T., Nauseef, W. M., Volpp, B. D., Pearson, D. W., Rosen, H., & Clark, R. A. (1991) · Journal of Clinical Investigation · doi:10.1172/jci114993 · Cited by 373 · see citing works
Self-citationHolland, S. M. (2012) · Hematology/Oncology Clinics of North America · doi:10.1016/j.hoc.2012.11.002 · Cited by 345 · see citing works
A Mammalian H + Channel Generated Through Alternative Splicing of the NADPH Oxidase Homolog NOH-1
Bánfi, B., Maturana, A. D., Jaconi, S., Arnaudeau, S., Laforge, T., Sinha, B. N. M., Ligeti, E., Demaurex, N., & Krause, K. (2000) · Science · doi:10.1126/science.287.5450.138 · Cited by 309 · see citing works
Forman, H. J., Augusto, O., Brigelius‐Flohé, R., Dennery, P. A., Kalyanaraman, B., Ischiropoulos, H., Mann, G. E., Radí, R., Roberts, L. J., Viña, J., et al. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.10.504 · Cited by 303 · see citing works
Superoxide dismutase 1 regulates caspase-1 and endotoxic shock
Meissner, F., Molawi, K., & Zychlinsky, A. (2008) · Nature Immunology · doi:10.1038/ni.1633 · Cited by 302 · see citing works
Peculiarities of cell death mechanisms in neutrophils
Geering, B., & Simon, H.-U. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.75 · Cited by 301 · see citing works
Redox regulation in metabolic programming and inflammation
Griffiths, H. R., Gao, D., & Pararasa, C. (2017) · Redox Biology · doi:10.1016/j.redox.2017.01.023 · Cited by 284 · see citing works
Myeloperoxidase in human neutrophil host defence
Nauseef, W. M. (2014) · Cellular Microbiology · doi:10.1111/cmi.12312 · Cited by 276 · see citing works
Self-citationVestibular defects in head-tilt mice result from mutations in Nox3 , encoding an NADPH oxidasePreprint
Paffenholz, R., Bergstrom, R. A., Pasutto, F., Wabnitz, P., Munroe, R. J., Jagla, W., Heinzmann, U., Marquardt, A., Bareiss, A., Laufs, J., et al. (2004) · Genes & Development · doi:10.1101/gad.1172504 · Cited by 269 · see citing works
van de Veerdonk, F. L., Smeekens, S. P., Joosten, L. A. B., Kullberg, B. J., Dinarello, C. A., van der Meer, J. W. M., & Netea, M. G. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914795107 · Cited by 248 · see citing works
Abuaita, B. H., Schultz, T. L., & O’Riordan, M. X. (2018) · Cell Host & Microbe · doi:10.1016/j.chom.2018.10.005 · Cited by 223 · see citing works
Stöcker, S., Laer, K. V., Mijušković, A., & Dick, T. P. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7162 · Cited by 219 · see citing works
Signaling Components of Redox Active Endosomes: The Redoxosomes
Oakley, F. D., Abbott, D., Li, Q., & Engelhardt, J. F. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2363 · Cited by 209 · see citing works
Biological Production, Detection, and Fate of Hydrogen Peroxide
Winterbourn, C. C. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7425 · Cited by 197 · see citing works
Chemaly, A. E., Okochi, Y., Sasaki, M., Arnaudeau, S., Okamura, Y., & Demaurex, N. (2009) · The Journal of Experimental Medicine · doi:10.1084/jem.20091837 · Cited by 189 · see citing works
Hoffmann, M. H., & Griffiths, H. R. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.03.016 · Cited by 187 · see citing works
Jacob, C. O., Eisenstein, M., Dinauer, M. C., Ming, W., Liu, Q., John, S. K., Quismorio, F. P., Reiff, A. O., Myones, B. L., Kaufman, K. M., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1113251108 · Cited by 184 · see citing works
Determinants of the Phagosomal pH in Neutrophils
Jankowski, A. W., Scott, C. C., & Grinstein, S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110059200 · Cited by 181 · see citing works
X-linked carriers of chronic granulomatous disease: Illness, lyonization, and stability
Marciano, B. E., Zerbe, C. S., Falcone, E. L., Ding, L., Ravin, S. S. D., Daub, J. R., Kreuzburg, S., Yockey, L., Hunsberger, S., Foruraghi, L., et al. (2017) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2017.04.035 · Cited by 181 · see citing works
Kettle, A. J., & Winterbourn, C. C. (1988) · Biochemical Journal · doi:10.1042/bj2520529 · Cited by 177 · see citing works
Cytokine production by human neutrophils: Revisiting the “dark side of the moon”
Tamassia, N., Bianchetto-Aguilera, F. M., Arruda-Silva, F., Gardiman, E., Gasperini, S., Calzetti, F., & Cassatella, M. A. (2018) · European Journal of Clinical Investigation · doi:10.1111/eci.12952 · Cited by 160 · see citing works
Burkitt, M. J., & Wardman, P. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.4578 · Cited by 154 · see citing works
Park, J. W., Ma, M., Ruedi, J. M., Smith, R. M., & BABIOR, B. M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41929-1 · Cited by 148 · see citing works
The Role of Peroxiredoxins in the Transduction of H 2 O 2 Signals
Rhee, S. G., Woo, H. A., & Kang, D. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7167 · Cited by 143 · see citing works
ROS and glutathionylation balance cytoskeletal dynamics in neutrophil extracellular trap formation
Stojkov, D., Amini, P., Oberson, K., Sokollik, C., Duppenthaler, A., Simon, H.-U., & Yousefi, S. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201611168 · Cited by 142 · see citing works
Inherited p40phox deficiency differs from classic chronic granulomatous disease
van de Geer, A., Nieto-Patlán, A., Kuhns, D. B., Tool, A. T. J., Arias, A. A., Bouaziz, M., de Boer, M., Franco, J. L., Gazendam, R. P., van Hamme, J. L., et al. (2018) · Journal of Clinical Investigation · doi:10.1172/jci97116 · Cited by 140 · see citing works
Voltage-gated proton channel is expressed on phagosomes
Okochi, Y., Sasaki, M., Iwasaki, H., & Okamura, Y. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.03.036 · Cited by 129 · see citing works
Fluorescent proteins such as eGFP lead to catalytic oxidative stress in cells
Ganini, D., Leinisch, F., Kumar, A., Jiang, J., Tokar, E. J., Malone, C. C., Petrovich, R. M., & Mason, R. P. (2017) · Redox Biology · doi:10.1016/j.redox.2017.03.002 · Cited by 124 · see citing works
Arnadottir, G. A., Norddahl, G. L., Guðmundsdóttir, S., Agustsdottir, A. B., Sigurðsson, S., Jensson, B. Ö., Bjarnadóttir, K., Theódórs, F., Benónísdóttir, S., Ivarsdottir, E. V., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-06964-x · Cited by 109 · see citing works
Zhou, Y., An, L., Chaerkady, R., Mittereder, N., Clarke, L., Cohen, T. S., Chen, B., Hess, S. Y., Sims, G. P., & Mustelin, T. (2018) · Scientific Reports · doi:10.1038/s41598-018-33385-z · Cited by 101 · see citing works
Reactions of Superoxide with Myeloperoxidase
Kettle, A. J., Anderson, R. F., Hampton, M. B., & Winterbourn, C. C. (2007) · Biochemistry · doi:10.1021/bi602587k · Cited by 99 · see citing works
Isolation of a Complex of Respiratory Burst Oxidase Components from Resting Neutrophil Cytosol
Park, J., Benna, J. E., Scott, K. E., Christensen, B. L., Chanock, S. J., & BABIOR, B. M. (1994) · Biochemistry · doi:10.1021/bi00176a021 · Cited by 93 · see citing works
EROS/CYBC1 mutations: Decreased NADPH oxidase function and chronic granulomatous disease
Thomas, D., Charbonnier, L., Schejtman, A., Al‐Dhekri, H., Coomber, E. L., Dufficy, E. R., Beenken, A. E., Lee, J. C., Clare, S., Speak, A. O., et al. (2018) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2018.09.019 · Cited by 89 · see citing works
Phagocyte NADPH oxidase and specific immunity
Cachat, J., Deffert, C., Hugues, S., & Krause, K. (2015) · Clinical Science · doi:10.1042/cs20140635 · Cited by 85 · see citing works
Han, W., Li, H., Cai, J., Gleaves, L. A., Polosukhin, V. V., Segal, B. H., Yull, F. E., & Blackwell, T. S. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1201809 · Cited by 83 · see citing works
NADPH oxidase activation regulates apoptotic neutrophil clearance by murine macrophages
Bagaitkar, J., Huang, J., Zeng, M. Y., Pech, N. K., Monlish, D. A., Perez‐Zapata, L. J., Miralda, I., Schuettpelz, L. G., & Dinauer, M. C. (2018) · Blood · doi:10.1182/blood-2017-09-809004 · Cited by 82 · see citing works
Levine, A. P., Duchen, M. R., de Villiers, S., Rich, P. R., & Segal, A. W. (2015) · PLoS ONE · doi:10.1371/journal.pone.0125906 · Cited by 81 · see citing works
AQP8 transports NOX2-generated H2O2 across the plasma membrane to promote signaling in B cells
Bertolotti, M., Farinelli, G., Galli, M., Aiuti, A., & Sitia, R. (2016) · Journal of Leukocyte Biology · doi:10.1189/jlb.2ab0116-045r · Cited by 75 · see citing works
Iyer, S. S., Pearson, D. W., Nauseef, W. M., & Clark, R. A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31804-5 · Cited by 69 · see citing works
Self-citationDefective macrophage function in aquaporin‐3 deficiency
Zhu, N., Feng, X., He, C., Gao, H., Yang, L., Ma, Q., Guo, L., Qiao, Y., Yang, H., & Ma, T. (2011) · The FASEB Journal · doi:10.1096/fj.11-182808 · Cited by 69 · see citing works
Thomas, D., Clare, S., Sowerby, J. M., Pardo, M., Juss, J. K., Goulding, D., van der Weyden, L., Storisteanu, D. M. L., Prakash, A., Espéli, M., et al. (2017) · The Journal of Experimental Medicine · doi:10.1084/jem.20161382 · Cited by 68 · see citing works
Association of NOX2 subunits genetic variants with autoimmune diseases
Zhong, J., Olsson, L. M., Urbonaviciute, V., Yang, M., Bäckdahl, L., & Holmdahl, R. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.03.005 · Cited by 63 · see citing works
Dysregulation of innate immune receptors on neutrophils in chronic granulomatous disease
Hartl, D., Lehmann, N., Hoffmann, F., Jansson, A. F., Hector, A., Notheis, G., Roos, D., Belohradsky, B. H., & Wintergerst, U. (2008) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2007.10.037 · Cited by 59 · see citing works
Jacob, C. O., Yu, N., Yoo, D., Perez‐Zapata, L. J., Barbu, E. A., Kaplan, M. J., Purmalek, M. M., Pingel, J. T., Idol, R. A., & Dinauer, M. C. (2017) · Arthritis & Rheumatology · doi:10.1002/art.40141 · Cited by 58 · see citing works
Deffert, C., Carnésecchi, S., Yuan, H., Rougemont, A., Kelkka, T., Holmdahl, R., Krause, K., & Schäppi, M. G. (2012) · The Journal of Pathology · doi:10.1002/path.4061 · Cited by 57 · see citing works
Hydrogen Peroxide Metabolism in Health and Disease
Davies, M. J. (2017) · CRC Press eBooks · doi:10.1201/9781315154831 · Cited by 55 · see citing works
Gabelloni, M. L., Sabbione, F., Jancic, C. C., Bass, J. I. F., Keitelman, I. A., Iula, L., Oleastro, M., Geffner, J. R., & Trevani, A. S. (2013) · European Journal of Immunology · doi:10.1002/eji.201243089 · Cited by 54 · see citing works
DeCoursey, T. E. (2016) · Immunological Reviews · doi:10.1111/imr.12437 · Cited by 54 · see citing works
Cutting Edge: NADPH Oxidase Modulates MHC Class II Antigen Presentation by B Cells
Crotzer, V. L., Matute, J. D., Arias, A. A., Zhao, H., Quilliam, L. A., Dinauer, M. C., & Blum, J. S. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1103080 · Cited by 51 · see citing works
The defense and signaling role of NADPH oxidases in eukaryotic cells
Breitenbach, M., Rinnerthaler, M., Weber, M., Breitenbach‐Koller, H., Karl, T., Cullen, P. J., Basu, S., Haskova, D., & Hašek, J. (2018) · Wiener Medizinische Wochenschrift · doi:10.1007/s10354-018-0640-4 · Cited by 51 · see citing works
Hydrogen Peroxide As an Immunological Transmitter Regulating Autoreactive T Cells
Holmdahl, R., Sareila, O., Pizzolla, A., Winter, S., Hagert, C., Jaakkola, N., Kelkka, T., Olsson, L. M., Wing, K., & Bäckdahl, L. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4734 · Cited by 50 · see citing works
Regulation of phagocyte NADPH oxidase by hydrogen peroxide through a Ca2+/c-Abl signaling pathway
Jamali, A. E., Valente, A. J., & Clark, R. A. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.12.018 · Cited by 47 · see citing works
Albrett, A. M., Ashby, L. V., Dickerhof, N., Kettle, A. J., & Winterbourn, C. C. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.004789 · Cited by 47 · see citing works
Iversen, M. B., Gottfredsen, R. H., Larsen, U. G., Enghild, J. J., Prætorius, J., Borregaard, N., & Petersen, S. V. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.07.004 · Cited by 43 · see citing works
A Systematic Characterization of Aquaporin-9 Expression in Human Normal and Pathological Tissues
Lindskog, C., Asplund, A., Catrina, A. I., Nielsen, S., & Rützler, M. R. (2016) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155416641028 · Cited by 42 · see citing works
Redox-Sensitive Innate Immune Pathways During Macrophage Activation in Type 1 Diabetes
Burg, A. R., & Tse, H. M. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7243 · Cited by 38 · see citing works
The Phagocyte Oxidase Controls Tolerance to Mycobacterium tuberculosis Infection
Olive, A. J., Smith, C. M., Kiritsy, M. C., & Sassetti, C. M. (2018) · The Journal of Immunology · doi:10.4049/jimmunol.1800202 · Cited by 35 · see citing works
Ziegler, C., Bouchab, L., Tramier, M., Christiane, D. D., Fieschi, F., Dupré‐Crochet, S., Mérola, F., Nüße, O., & Erard, M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006864 · Cited by 35 · see citing works
Intersecting Stories of the Phagocyte NADPH Oxidase and Chronic Granulomatous Disease
Nauseef, W. M., & Clark, R. A. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9424-3_1 · Cited by 22 · see citing works
Self-citationHyper‐responsive Toll‐like receptor 7 and 9 activation in NADPH oxidase‐deficient B lymphoblasts
McLetchie, S., Volpp, B. D., Dinauer, M. C., & Blum, J. S. (2015) · Immunology · doi:10.1111/imm.12530 · Cited by 19 · see citing works
Yaffe, M. B. (2002) · Structure · doi:10.1016/s0969-2126(02)00860-2 · Cited by 18 · see citing works
Fang, M. M., Barman, P. K., Thiruppathi, M., Mirza, R. E., McKinney, R. D., Deng, J., Christman, J. W., Du, X., Fukai, T., Ennis, W. J., et al. (2018) · The Journal of Immunology · doi:10.4049/jimmunol.1800252 · Cited by 17 · see citing works
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- [42]Forbes LV, Kettle AJ: Myeloperoxidase: Unleashing the Power of Hydrogen Peroxide In Hydrogen Peroxide Metabolism in Health and Disease. Edited by Vissers MCM, Hampton MB, Kettle AJ: CRC Press; 2018: 281– 304. [Packer L, Cadenas E (Series Editor): Oxidative Stress and Disease
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The superoxide radical switch in the biology of nitric oxide and peroxynitrite
Piacenza, L., Zeida, A., Trujillo, M., & Radí, R. (2022) · Physiological Reviews · doi:10.1152/physrev.00005.2022 · Cited by 204 · see citing works
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 177 · see citing works
NOX Dependent ROS Generation and Cell Metabolism
Cimmino, T. P., Ammendola, R., Cattaneo, F., & Esposito, G. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032086 · Cited by 164 · see citing works
Inducible antibacterial responses in macrophages
Sweet, M. J., Ramnath, D., Singhal, A., & Kapétanovic, R. (2024) · Nature reviews. Immunology · doi:10.1038/s41577-024-01080-y · Cited by 163 · see citing works
Energetic dysfunction in sepsis: a narrative review
Préau, S., Vodovar, D., Jung, B., Lancel, S., Zafrani, L., Flatres, A., Oualha, M., Voiriot, G., Jouan, Y., Joffre, J., et al. (2021) · Annals of Intensive Care · doi:10.1186/s13613-021-00893-7 · Cited by 156 · see citing works
From Flies to Men: ROS and the NADPH Oxidase in Phagocytes
Moghadam, Z. M., Henneke, P., & Kolter, J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.628991 · Cited by 136 · see citing works
Standing on the shoulders of mice
Medetgul-Ernar, K., & Davis, M. M. (2022) · Immunity · doi:10.1016/j.immuni.2022.07.008 · Cited by 119 · see citing works
Triple threat: how diabetes results in worsened bacterial infections
Darwitz, B. P., Genito, C. J., & Thurlow, L. R. (2024) · Infection and Immunity · doi:10.1128/iai.00509-23 · Cited by 122 · see citing works
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 104 · see citing works
The Role of HDAC6 in Autophagy and NLRP3 Inflammasome
Chang, P., Li, H., Hu, H., Li, Y., & Wang, T. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.763831 · Cited by 101 · see citing works
Rugaie, O. A., Jabir, M. S., Mohammed, M. K., Abbas, R., Ahmed, D., Sulaiman, G., Mohammed, S. A. A., Khan, R. A., Al-Regaiey, K. A., Alsharidah, M., et al. (2022) · Scientific Reports · doi:10.1038/s41598-022-22193-1 · Cited by 94 · see citing works
Unlocking the power of NOX2: A comprehensive review on its role in immune regulation
Bode, K., Hauri-Hohl, M. M., Jaquet, V., & Weyd, H. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102795 · Cited by 94 · see citing works
Redox regulation of macrophages
Tran, N., & Mills, E. L. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103123 · Cited by 97 · see citing works
Biological chemistry of superoxide radicals
Winterbourn, C. C. (2020) · ChemTexts · doi:10.1007/s40828-019-0101-8 · Cited by 89 · see citing works
Human neutrophils ≠ murine neutrophils: Does it matter?
Nauseef, W. M. (2022) · Immunological Reviews · doi:10.1111/imr.13154 · Cited by 84 · see citing works
Self-citationAnti-Inflammatory Neutrophil Functions in the Resolution of Inflammation and Tissue Repair
Loh, W., & Vermeren, S. (2022) · Cells · doi:10.3390/cells11244076 · Cited by 87 · see citing works
Neutrophils and the Systemic Inflammatory Response Syndrome (SIRS)
Sikora, J. P., Karawani, J., & Sobczak, J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241713469 · Cited by 87 · see citing works
A guide to membrane atg8ylation and autophagy with reflections on immunity
Deretic, V. P., & Lazarou, M. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202203083 · Cited by 78 · see citing works
Interactions Between Neutrophils and Periodontal Pathogens in Late-Onset Periodontitis
Jiang, Q., Zhao, Y., Shui, Y., Zhou, X., Cheng, L., Ren, B., Chen, Z., & Li, M. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.627328 · Cited by 76 · see citing works
Uriarte, S. M., & Hajishengallis, G. (2022) · Immunological Reviews · doi:10.1111/imr.13152 · Cited by 71 · see citing works
Modulating Nitric Oxide: Implications for Cytotoxicity and Cytoprotection
Belenichev, I. F., Popazova, O., Bukhtiyarova, N. V., Savchenko, D., Oksenych, V., & Kamyshnyi, O. (2024) · Antioxidants · doi:10.3390/antiox13050504 · Cited by 80 · see citing works
Determinants of Phagosomal pH During Host-Pathogen Interactions
Westman, J., & Grinstein, S. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.624958 · Cited by 65 · see citing works
Oxidants in Physiological Processes
Knaus, U. G. (2020) · Handbook of experimental pharmacology · doi:10.1007/164_2020_380 · Cited by 63 · see citing works
Neutrophil dysfunction in the pathogenesis of cystic fibrosis
Wang, G., & Nauseef, W. M. (2022) · Blood · doi:10.1182/blood.2021014699 · Cited by 58 · see citing works
Self-citationNeutrophils in host defense, healing, and hypersensitivity: Dynamic cells within a dynamic host
Siwicki, M. R., & Kubes, P. (2023) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2022.12.004 · Cited by 57 · see citing works
Beyond the Extra Respiration of Phagocytosis: NADPH Oxidase 2 in Adaptive Immunity and Inflammation
Mortimer, P. M., McIntyre, S., & Thomas, D. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.733918 · Cited by 57 · see citing works
Possible Beneficial Effects of N-Acetylcysteine for Treatment of Triple-Negative Breast Cancer
Kwon, Y. (2021) · Antioxidants · doi:10.3390/antiox10020169 · Cited by 55 · see citing works
Neutrophil heterogeneity and plasticity: unveiling the multifaceted roles in health and disease
He, W., Yan, L., Hu, D., Hao, J., Liou, Y., & Luo, G. (2025) · MedComm · doi:10.1002/mco2.70063 · Cited by 55 · see citing works
Periodontal Pathogens’ strategies disarm neutrophils to promote dysregulated inflammation
Miralda, I., & Uriarte, S. M. (2020) · Molecular Oral Microbiology · doi:10.1111/omi.12321 · Cited by 52 · see citing works
Pathophysiology of reactive oxygen species (ROS)
de la Lastra, J. M. P., Andrés, C. M. C., Munguira, E. B., Juan, C. A., & Pérez‐Lebeña, E. (2026) · Archives of Toxicology · doi:10.1007/s00204-025-04276-w · Cited by 54 · see citing works
Nox, Nox, Are You There? The Role of NADPH Oxidases in the Peripheral Nervous System
Eid, S., Savelieff, M. G., Eid, A. A., & Feldman, E. L. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2021.0135 · Cited by 50 · see citing works
Cell intrinsic functions of neutrophils and their manipulation by pathogens
Allen, L. H., & Criss, A. K. (2019) · Current Opinion in Immunology · doi:10.1016/j.coi.2019.05.004 · Cited by 47 · see citing works
Beyond bacterial killing: NADPH oxidase 2 is an immunomodulator
Trevelin, S. C., Shah, A. M., & Lombardi, G. (2020) · Immunology Letters · doi:10.1016/j.imlet.2020.02.009 · Cited by 47 · see citing works
Salmonid Antibacterial Immunity: An Aquaculture Perspective
Semple, S. L., & Dixon, B. (2020) · Biology · doi:10.3390/biology9100331 · Cited by 47 · see citing works
Cabrera-Serrano, A. J., Sánchez-Maldonado, J. M., González-Olmedo, C., Carretero-Fernández, M., Díaz-Beltrán, L., Gutiérrez-Bautista, J. F., García-Verdejo, F., Gálvez-Montosa, F., López-López, J. A., García-Martín, P., et al. (2025) · Antioxidants · doi:10.3390/antiox14030264 · Cited by 36 · see citing works
Immunomodulatory effects of 4-hydroxynonenal
Ioannidis, M., Tjepkema, J., Uitbeijerse, M. R. P., & van den Bogaart, G. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103719 · Cited by 44 · see citing works
Superoxide: The enigmatic chemical chameleon in neutrophil biology
Kettle, A. J., Ashby, L. V., Winterbourn, C. C., & Dickerhof, N. (2023) · Immunological Reviews · doi:10.1111/imr.13183 · Cited by 40 · see citing works
Fujii, J., & Osaki, T. (2023) · Molecules · doi:10.3390/molecules28020814 · Cited by 42 · see citing works
Microbes and the fate of neutrophils
Kobayashi, S. D., DeLeo, F. R., & Quinn, M. T. (2022) · Immunological Reviews · doi:10.1111/imr.13163 · Cited by 43 · see citing works
Insights into Alkaline Phosphatase Anti-Inflammatory Mechanisms
Balabanova, L., Bondarev, G., Seitkalieva, A. V., Son, O. M., & Tekutyeva, L. (2024) · Biomedicines · doi:10.3390/biomedicines12112502 · Cited by 37 · see citing works
The NADPH Oxidase and the Phagosome
Valenta, H., Erard, M., Dupré‐Crochet, S., & Nüβe, O. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-40406-2_9 · Cited by 36 · see citing works
Reverte, M., Eren, R. O., Jha, B., Desponds, C., Snäkä, T., Prével, F., Isorce, N., Lye, L., Owens, K. L., Lopes, U. G., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009422 · Cited by 36 · see citing works
Roth, M., Jaquet, V., Lemeille, S., Bonetti, E.-J., Cambet, Y., François, P., & Krause, K. (2022) · Antioxidants · doi:10.3390/antiox11040655 · Cited by 35 · see citing works
Zhou, Y., & Bréchard, S. (2022) · Cells · doi:10.3390/cells11203318 · Cited by 33 · see citing works
Urban, C. F., & Backman, E. (2020) · Current Opinion in Microbiology · doi:10.1016/j.mib.2020.09.011 · Cited by 32 · see citing works
Mitochondrial Ca2+ Signaling Is an Electrometabolic Switch to Fuel Phagosome Killing
Seegren, P. V., Downs, T. K., Stremska, M. E., Harper, L. R., Cao, R., Olson, R. J., Upchurch, C. M., Doyle, C. A., Kennedy, J. A., Stipes, E. J., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108411 · Cited by 32 · see citing works
Phagocytosis: Phenotypically Simple Yet a Mechanistically Complex Process
Kumar, V. (2020) · International Reviews of Immunology · doi:10.1080/08830185.2020.1732958 · Cited by 31 · see citing works
Suleimanov, S. K., Efremov, Y. M., Klyucherev, T. O., Salimov, E. L., Ragimov, A. A., Timashev, P. S., & Vlasova, I. I. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25031860 · Cited by 30 · see citing works
How Do Polyphenol-Rich Foods Prevent Oxidative Stress and Maintain Gut Health?
Jawhara, S. (2024) · Microorganisms · doi:10.3390/microorganisms12081570 · Cited by 33 · see citing works
Rugaie, O. A., Jabir, M. S., Kadhim, R. J., Karsh, E. H., Sulaiman, G. M., Mohammed, S. A. A., Khan, R. A., & Mohammed, H. A. (2021) · Microorganisms · doi:10.3390/microorganisms9010101 · Cited by 30 · see citing works
Wan, Y., Zhang, W., Huang, C., Jian, J., Zhang, Y., Liu, Q., Chen, P., & Zhu, X. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.109321 · Cited by 29 · see citing works
Phagocytosis via complement receptor 3 enables microbes to evade killing by neutrophils
Smirnov, A., Daily, K. P., Gray, M. C., Ragland, S. A., Werner, L. M., Johnson, M. B., Eby, J. C., Hewlett, E. L., Taylor, R. P., & Criss, A. K. (2023) · Journal of Leukocyte Biology · doi:10.1093/jleuko/qiad028 · Cited by 29 · see citing works
Song, Z., Bhattacharya, S., Huang, G., Greenberg, Z. J., Yang, W., Bagaitkar, J., Schuettpelz, L. G., & Dinauer, M. C. (2022) · Blood Advances · doi:10.1182/bloodadvances.2022007652 · Cited by 26 · see citing works
Cross-Talk of NADPH Oxidases and Inflammation in Obesity
Morawietz, H., Brendel, H., Diaba‐Nuhoho, P., Catar, R. A., Perakakis, N., Wolfrum, C., & Bornstein, S. R. (2023) · Antioxidants · doi:10.3390/antiox12081589 · Cited by 29 · see citing works
Dagah, O. M. A., Silaa, B. B., Zhu, M., Pan, Q., Qi, L., Liu, X., Liu, Y., Peng, W., Ullah, Z., Yudas, A. F., et al. (2024) · Antioxidants · doi:10.3390/antiox13050545 · Cited by 28 · see citing works
Gupta, K. D., Ramnath, D., von Pein, J. B., Curson, J. E. B., Wang, Y., Abrol, R., Kakkanat, A., Moradi, S. V., Gunther, K. S., Murthy, A. M. V., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2212813120 · Cited by 25 · see citing works
Self-citationDu, L. Y., Keerthisinghe, P., Rolland, L., Sung, Y. J., Darroch, H., Linnerz, T., Ashimbayeva, E., Grant, M. J., Kakadia, P. M., Ramachandran, A., et al. (2025) · Science Immunology · doi:10.1126/sciimmunol.adn3080 · Cited by 23 · see citing works
Li, L.-J., Mao, R., Yuan, S.-L., Xie, Q.-Q., Meng, J., Gu, Y., Tan, S.-Y., Xu, X.-Q., Gao, C.-J., Liu, H., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-49549-7 · Cited by 24 · see citing works
Casella, A. C., Prolo, C., Pereyra, J., Ríos, N., Piacenza, L., Radí, R., & Álvarez, M. N. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.12.024 · Cited by 22 · see citing works
Extracellular Vesicles from Candida haemulonii var. vulnera Modulate Macrophage Oxidative Burst
Oliveira, B. T. M., Dourado, T. M. H., dos Santos, P. W. D. S., Bitencourt, T. A., Tirapelli, C. R., Colombo, A. L., & Almeida, F. B. D. R. (2023) · Journal of Fungi · doi:10.3390/jof9050562 · Cited by 20 · see citing works
Ahmad, F., Ahmad, S., Srivastav, A. K., Upadhyay, T. K., Husain, A., Khubaib, M., Kang, S., Park, M. N., Kim, B., & Sharma, R. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.136520 · Cited by 21 · see citing works
Oxidative Stress in Antigen Processing and Presentation
Chang, Q., Zhang, Y., Liu, X., Miao, P., Pu, W., Liu, S., Zhang, J., Yuan, T., Shen, G., & Xie, N. (2025) · MedComm – Oncology · doi:10.1002/mog2.70020 · Cited by 21 · see citing works
Novel and Converging Ways of NOX2 and SOD3 in Trafficking and Redox Signaling in Macrophages
Petersen, S. V., Poulsen, N. B., Matthiesen, C. L., & Vilhardt, F. (2021) · Antioxidants · doi:10.3390/antiox10020172 · Cited by 21 · see citing works
Tlili, A., Pintard, C., Hurtado-Nédelec, M., Liu, D., Marzaioli, V., Thiéblemont, N., Dang, P. M., & Benna, J. E. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2209184120 · Cited by 21 · see citing works
Impact of CFTR Modulators on the Impaired Function of Phagocytes in Cystic Fibrosis Lung Disease
Meoli, A., Eickmeier, O., Pisi, G., Fainardi, V., Zielen, S., & Esposito, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012421 · Cited by 21 · see citing works
Gastrointestinal redox homeostasis in ageing
Homolak, J. (2023) · Biogerontology · doi:10.1007/s10522-023-10049-8 · Cited by 20 · see citing works
Belambri, S. A., Marzaioli, V., Hurtado-Nédelec, M., Pintard, C., Liang, S., Liu, Y., Boussetta, T., Gougerot‐Pocidalo, M., Ye, R. D., Dang, P. M., et al. (2022) · Blood · doi:10.1182/blood.2021011134 · Cited by 19 · see citing works
Königstorfer, A., Ashby, L. V., Bollar, G. E., Billiot, C. E., Gray, M. J., Jakob, U., Hampton, M. B., & Winterbourn, C. C. (2020) · Pathogens and Disease · doi:10.1093/femspd/ftaa079 · Cited by 19 · see citing works
Carriere, V. M., Rodrigues, J. P., Tan, C., Arumugam, P. U., & Poh, S. (2021) · Sensors · doi:10.3390/s21165607 · Cited by 18 · see citing works
Emerging Concepts in Defective Macrophage Phagocytosis in Cystic Fibrosis
Jaganathan, D., Bruscia, E. M., & Kopp, B. T. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23147750 · Cited by 18 · see citing works
NADPH Oxidase 3: Beyond the Inner Ear
Herb, M. (2024) · Antioxidants · doi:10.3390/antiox13020219 · Cited by 18 · see citing works
Kim, J. Y., Kim, J., Kim, Y., & Seo, J. H. (2022) · Antioxidants · doi:10.3390/antiox11051031 · Cited by 17 · see citing works
Inhibition of NADPH Oxidase (NOX) 2 Mitigates Colitis in Mice with Impaired Macrophage AMPK Function
Banskota, S., Wang, H.-Q., Kwon, Y. H., Gautam, J., Haq, S., Grondin, J., Steinberg, G., & Khan, W. (2023) · Biomedicines · doi:10.3390/biomedicines11051443 · Cited by 18 · see citing works
Miralda, I., Vashishta, A., Rogers, M. N., Rouchka, E. C., Li, X., Waigel, S. J., Lamont, R. J., & Uriarte, S. M. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00497 · Cited by 17 · see citing works
Abdelbaset‐Ismail, A., Ciechanowicz, A. K., Bujko, K., Ratajczak, J., Kucia, M., & Ratajczak, M. Z. (2022) · Stem Cell Reviews and Reports · doi:10.1007/s12015-022-10481-2 · Cited by 17 · see citing works
Lactoferrin modified by hypohalous acids: Partial loss in activation of human neutrophils
Grigorieva, D. V., Gorudko, I. V., Грудинина, Н. А., Panasenko, O. M., Semak, I. V., Av, S., & Timoshenko, A. V. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.11.165 · Cited by 15 · see citing works
Ischemia/reperfusion-associated oxidative stress is an aggravating factor for pressure ulcers
Murata, E., & Fujii, J. (2025) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.25-28 · Cited by 15 · see citing works
He, W., Xu, T., Wang, M., Ni, N., Su, Y., & Fan, X. (2025) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2025.09.040 · Cited by 19 · see citing works
Casey, A. M., & Murphy, M. P. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2022.166481 · Cited by 14 · see citing works
Ladik, M., Valenta, H., Erard, M., Vandenabeele, P., & Riquet, F. B. (2023) · Frontiers in Cell Death · doi:10.3389/fceld.2023.1127330 · Cited by 14 · see citing works
Host-directed therapy for bacterial infections -Modulation of the phagolysosome pathway-
Taya, T., Teruyama, F., & Gojo, S. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1227467 · Cited by 14 · see citing works
Wang, Y., Li, D., Zhang, H., Chen, J., Tang, Y., Nie, H., Huo, Z., & Yan, X. (2024) · Aquaculture · doi:10.1016/j.aquaculture.2024.740681 · Cited by 14 · see citing works
Signaling by neutrophil G protein-coupled receptors that regulate the release of superoxide anions
Dahlgren, C., Forsman, H. F., Sundqvist, M., Björkman, L. I., & Mårtensson, J. (2024) · Journal of Leukocyte Biology · doi:10.1093/jleuko/qiae165 · Cited by 13 · see citing works
Effects of Magnetic Nanoparticles on the Functional Activity of Human Monocytes and Dendritic Cells
Donini, M., Pettinella, F., Zanella, G., Gaglio, S. C., Laudanna, C., Jiménez-Carretero, M., Jiménez-López, C., Perduca, M., & Dusi, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24021358 · Cited by 14 · see citing works
Donini, M., Gaglio, S. C., Laudanna, C., Perduca, M., & Dusi, S. (2021) · Molecules · doi:10.3390/molecules26144351 · Cited by 14 · see citing works
Klyucherev, T. O., Yurkanova, M. D., Revokatova, D. P., Chevalier, D. A., Shishkov, V. V., Vlasova, I. I., Kosheleva, N. V., & Timashev, P. S. (2026) · Cells · doi:10.3390/cells15020093 · Cited by 13 · see citing works
Distinct timing of neutrophil spreading and stiffening during phagocytosis
Zak, A., Dupré‐Crochet, S., Hudik, E., Babataheri, A., Barakat, A. I., Nüße, O., & Husson, J. (2022) · Biophysical Journal · doi:10.1016/j.bpj.2022.03.021 · Cited by 13 · see citing works
Xu, S., Chuang, C. Y., Hawkins, C. L., Hägglund, P., & Davies, M. J. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102799 · Cited by 13 · see citing works
De novo DUOX2 expression in neutrophil subsets shapes the pathogenesis of intestinal disease
Singh, A. K., Ainciburu, M., Wynne, K. J., Bhat, S. A., Blanco, A., Tzani, I., Akiba, Y., Lalor, S. J., Kaunitz, J. D., Bourke, B., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2421747122 · Cited by 11 · see citing works
Microglial reprogramming by Hv1 antagonism protects neurons from inflammatory and glutamate toxicity
Hernández-Espinosa, D. R., Gale, J. R., Scrabis, M. G., & Aizenman, E. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.15760 · Cited by 11 · see citing works
Bechor, E., Zahavi, A., Amichay, M., Fradin, T., Federman, A., Berdichevsky, Y., & Pick, E. (2020) · Journal of Leukocyte Biology · doi:10.1002/jlb.4a1219-607r · Cited by 11 · see citing works
Yang, L., Sun, L., & Li, C. (2024) · Aquaculture · doi:10.1016/j.aquaculture.2024.740953 · Cited by 10 · see citing works
Specific signaling by nicotinamide adenine dinucleotide oxidases – Role of their site of action
Schröder, K. (2024) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2024.102461 · Cited by 9 · see citing works
The involvement of HDAC3 in the pathogenesis of lung injury and pulmonary fibrosis
Yu, H., Liu, S., Wang, S., & Gu, X. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1392145 · Cited by 9 · see citing works
Yurkanova, M. D., Kosheleva, N. V., Teplova, A. A., Timashev, P. S., & Vlasova, I. I. (2025) · Free Radical Research · doi:10.1080/10715762.2025.2519528 · Cited by 9 · see citing works
Eosinophils in inflammatory bowel disease pathogenesis: an ROS-centric view
Tomii, T., & Kano, G. (2025) · Frontiers in Allergy · doi:10.3389/falgy.2025.1608202 · Cited by 9 · see citing works
Regulation of Derlin-1-mediated degradation of NADPH oxidase partner p22 by thiol modification
Miyano, K., Okamoto, S., Kajikawa, M., Kiyohara, T., Kawai, C., 山内, 明., & Kuribayashi, F. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102479 · Cited by 9 · see citing works
- Authors
- Nauseef, W. M.
- Affiliations
- University of Iowa (US)
- Corresponding author
- Nauseef, William M
- ORCID
- Nauseef, William M
- Venue
- Current Opinion in Immunology
- Publisher
- Elsevier BV
- Published
- 2019-10
- Volume
- 60
- Pages
- 130-140
- ISSN
- 0952-7915 (ISSN-L)
- PMC
- PMC6800624
- OpenAlex
- W2958386701
- Cited by
- 188
- References
- 85
- Citations by year
- 2026: 33 · 2025: 29 · 2024: 27 · 2023: 34 · 2022: 27 · 2021: 20 · 2020: 16 · 2019: 2
- FWCI
- 1.40
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Current Opinion in Immunology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- U.S. Department of Veterans Affairs
- National Institutes of Health (R01-AI116546, R01-AI132335)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Keywords
- NADPH oxidase, gp91phox, p22phox, phagocytes, reactive oxygen species, phagosome, autocrine signaling, paracrine signaling, electron transfer
- MeSH terms
- NADPH Oxidase 2, Animals, Granulomatous Disease, Chronic, Humans, Hydrogen Peroxide, Neutrophils, Oxidation-Reduction, Phagocytes, Phagocytosis, Phagosomes, Signal Transduction, Oxidants
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 ›
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