Cited by 188Neutrophil, Myeloperoxidase and Oxidative MechanismsRedox biology and oxidative stressNitric Oxide and Endothelin Effects

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The phagocyte NOX2 NADPH oxidase in microbial killing and cell signaling

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Nauseef, William M·2019·Current Opinion in Immunology

DOI 10.1016/j.coi.2019.05.006PMC PMC6800624

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Abstract

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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Bedard, K., & Krause, K.-H. (2007) · Physiological Reviews · doi:10.1152/physrev.00044.2005 · Cited by 6,989
Genome-wide association study identifies new susceptibility loci for Crohn disease and implicates autophagy in disease pathogenesis
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
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
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
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
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
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
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
Reactive 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 931
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
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Wardman, P. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.06.026 · Cited by 875
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
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
Self-citation
Inactivation of Peroxiredoxin I by Phosphorylation Allows Localized H2O2 Accumulation for Cell Signaling
Woo, 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 632
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
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
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 516
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
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 490
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
A new genetic subgroup of chronic granulomatous disease with autosomal recessive mutations in p40phox and selective defects in neutrophil NADPH oxidase activity
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 430
Self-citation
The challenges of using fluorescent probes to detect and quantify specific reactive oxygen species in living cells
Winterbourn, C. C. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.05.004 · Cited by 429
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 424
Neutrophil nicotinamide adenine dinucleotide phosphate oxidase assembly. Translocation of p47-phox and p67-phox requires interaction between p47-phox and cytochrome b558.
Heyworth, 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 381
Self-citation
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Holland, S. M. (2012) · Hematology/Oncology Clinics of North America · doi:10.1016/j.hoc.2012.11.002 · Cited by 356
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 314
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
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 308
Even free radicals should follow some rules: A Guide to free radical research terminology and methodology
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
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 287
Vestibular 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 285
Myeloperoxidase in human neutrophil host defence
Nauseef, W. M. (2014) · Cellular Microbiology · doi:10.1111/cmi.12312 · Cited by 283
Self-citation
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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
Mitochondria-derived vesicles deliver antimicrobial reactive oxygen species to control phagosome-localized staphylococcus aureus
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
The Conundrum of Hydrogen Peroxide Signaling and the Emerging Role of Peroxiredoxins as Redox Relay Hubs
Stöcker, S., Laer, K. V., Mijušković, A., & Dick, T. P. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7162 · Cited by 219
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Oakley, F. D., Abbott, D., Li, Q., & Engelhardt, J. F. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2363 · Cited by 217
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Winterbourn, C. C. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7425 · Cited by 204
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Hoffmann, M. H., & Griffiths, H. R. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.03.016 · Cited by 193
VSOP/Hv1 proton channels sustain calcium entry, neutrophil migration, and superoxide production by limiting cell depolarization and acidification
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
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 186
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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 183
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
Superoxide modulates the activity of myeloperoxidase and optimizes the production of hypochlorous acid
Kettle, A. J., & Winterbourn, C. C. (1988) · Biochemical Journal · doi:10.1042/bj2520529 · Cited by 177
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
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Burkitt, M. J., & Wardman, P. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.4578 · Cited by 155
The cytosolic components of the respiratory burst oxidase exist as a M(r) approximately 240,000 complex that acquires a membrane-binding site during activation of the oxidase in a cell-free system.
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
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 146
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
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 142
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
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
A homozygous loss-of-function mutation leading to CYBC1 deficiency causes chronic granulomatous disease
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 111
Evidence for a direct link between PAD4-mediated citrullination and the oxidative burst in human neutrophils
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 107
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Kettle, A. J., Anderson, R. F., Hampton, M. B., & Winterbourn, C. C. (2007) · Biochemistry · doi:10.1021/bi602587k · Cited by 99
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
Phagocyte NADPH oxidase and specific immunity
Cachat, J., Deffert, C., Hugues, S., & Krause, K. (2015) · Clinical Science · doi:10.1042/cs20140635 · Cited by 89
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
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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 84
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 83
Alkalinity of Neutrophil Phagocytic Vacuoles Is Modulated by HVCN1 and Has Consequences for Myeloperoxidase Activity
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
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 78
Evidence for a readily dissociable complex of p47phox and p67phox in cytosol of unstimulated human neutrophils.
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
Self-citation
Defective 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
Eros is a novel transmembrane protein that controls the phagocyte respiratory burst and is essential for innate immunity
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 69
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
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
Haploinsufficiency of NADPH Oxidase Subunit Neutrophil Cytosolic Factor 2 Is Sufficient to Accelerate Full‐Blown Lupus in NZM 2328 Mice
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 59
Hyperinflammation of chronic granulomatous disease is abolished by NOX2 reconstitution in macrophages and dendritic cells
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
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Davies, M. J. (2017) · CRC Press eBooks · doi:10.1201/9781315154831 · Cited by 57
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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
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DeCoursey, T. E. (2016) · Immunological Reviews · doi:10.1111/imr.12437 · Cited by 54
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Breitenbach, M., Rinnerthaler, M., Weber, M., Breitenbach‐Koller, H., Karl, T. R., Cullen, P. J., Basu, S., Haskova, D., & Hašek, J. (2018) · Wiener Medizinische Wochenschrift · doi:10.1007/s10354-018-0640-4 · Cited by 53
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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 52
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
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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
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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
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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 45
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Lindskog, C., Asplund, A., Catrina, A. I., Nielsen, S., & Rützler, M. R. (2016) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155416641028 · Cited by 42
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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
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Nauseef, W. M., & Clark, R. A. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9424-3_1 · Cited by 22
Self-citation
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McLetchie, S., Volpp, B. D., Dinauer, M. C., & Blum, J. S. (2015) · Immunology · doi:10.1111/imm.12530 · Cited by 19
The p47phox PX Domain
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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)
DOI: 10.1016/j.coi.2019.05.006
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
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
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 (medical) › 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

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The phagocyte NOX2 NADPH oxidase in microbial killing and cell signaling

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