The DOI matches its Crossref record; 63 of the 63 references it cites were found in a registry or an index.
NADPH oxidase
Abstract
NADPH oxidase is an enzyme that catalyzes the production of superoxide from oxygen and NADPH. It is a complex enzyme consisting of two membrane-bound components and three components in the cytosol, plus rac 1 or rac 2. Activation of the oxidase involves the phosphorylation of one of the cytosolic components. Recent crystallography data indicate that the tail of this cytosolic component lies in a groove between two Src homology 3 domains and, when phosphorylated, the tail leaves the groove and is replaced by the tail of one of the membrane-bound components. Chronic granulomatous disease is an inherited immune deficiency caused by the absence of one of the components of the oxidase. The most important recent advances in the field have been the crystallographic analysis of the oxidase and the use of antifungal agents in the prophylaxis of chronic granulomatous disease.
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“NADPH oxidase in phagocytic cells produces large amounts of O2•− in defence against pathogens and other aggressors [29].”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [29]
In the citing paper
“Hydrogen peroxide can then also be reduced by transition metal ions generating the hydroxyl radical (HO°), one of the strongest oxidizing agents that can rapidly react with polyunsaturated fatty acids, resulting the production of peroxyl radicals (ROO•).”
From Antioxidant and Anti-Inflammatory Activities of Essential Oils: A Short Review (2010) · cites this paper as [18]
In the citing paper
“Essential oils are complex mixtures isolated from aromatic plants which may possess antioxidant and anti-inflammatory activities of interest in thye food and cosmetic industries as well as in the human health field.”
From Antioxidant and Anti-Inflammatory Activities of Essential Oils: A Short Review (2010) · cites this paper as [18]
In the citing paper
“Phagocytosis of bacteria, which occurs during inflammation, is accompanied by a dramatic increase in oxygen consumption resulting in the formation of superoxide anion radical (O2•-) which is quickly converted to hydrogen peroxide (H2O2), spontaneously, or by the enzyme superoxide dismutase.”
From Antioxidant and Anti-Inflammatory Activities of Essential Oils: A Short Review (2010) · cites this paper as [18]
In the citing paper
“Peroxide hydrogen can also oxidise halide ions (Cl-) to hypochlorous acid (HOCl), which is a strong oxidant that can react with amines producing chloramines, some of them being very toxic [18,19,20,21,22].”
From Antioxidant and Anti-Inflammatory Activities of Essential Oils: A Short Review (2010) · cites this paper as [18]
Citations
Cites
BABIOR, B. M. (1999) · Blood · doi:10.1182/blood.v93.5.1464 · Cited by 2,147
Self-citationFridovich, I. (1975) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.44.070175.001051 · Cited by 1,753
Cell transformation by the superoxide-generating oxidase Mox1
Suh, Y.-A., Arnold, R. S., Lassegue, B., Shi, J., Xu, X., Sorescu, D., Chung, A. B., Griendling, K. K., & Lambeth, J. D. (1999) · Nature · doi:10.1038/43459 · Cited by 1,480
Superoxide Production and Expression of Nox Family Proteins in Human Atherosclerosis
Sorescu, D., Weiss, D., Lassègue, B., Clempus, R. E., Szöcs, K., Sorescu, G. P., Valppu, L., Quinn, M. T., Lambeth, J. D., Vega, J. D., et al. (2002) · Circulation · doi:10.1161/01.cir.0000012917.74432.66 · Cited by 847
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
Antibody to Interleukin-5 Inhibits Helminth-Induced Eosinophilia in Mice
Coffman, R. L., Seymour, B. W. P., Hudak, S. A., Jackson, J., & Rennick, D. M. (1989) · Science · doi:10.1126/science.2787531 · Cited by 634
Superoxide and peroxynitrite inactivate aconitases, but nitric oxide does not.
Hausladen, A., & Fridovich, I. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43893-8 · Cited by 585
Superoxide sensitivity of the Escherichia coli aconitase.
Gardner, P. R., & Fridovich, I. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55001-8 · Cited by 514
Reactive oxygen generated by Nox1 triggers the angiogenic switch
Arbiser, J. L., Petros, J. A., Klafter, R., Govindajaran, B., McLaughlin, E. R., Brown, L. F., Cohen, C., Moses, M. A., Kilroy, S. M., Arnold, R. S., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.022630199 · Cited by 489
Upregulation of Nox-Based NAD(P)H Oxidases in Restenosis After Carotid Injury
Szöcs, K., Lassegue, B. P., Sorescu, D., Hilenski, L. L., Valppu, L., Couse, T. L., Wilcox, J. N., Quinn, M. T., Lambeth, J. D., & Griendling, K. K. (2002) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/hq0102.102189 · Cited by 443
Mutations in the X-linked and autosomal recessive forms of chronic granulomatous disease
Roos, D., de Boer, M., Kuribayashi, F., Meischl, C., Weening, R. S., Segal, A. W., Åhlin, A., Német, K., Hossle, J. P., Bernatowska, E. A., et al. (1996) · Blood · doi:10.1182/blood.v87.5.1663.1663 · Cited by 423
Molecular Basis of Phosphorylation-Induced Activation of the NADPH Oxidase
Groemping, Y., Lapouge, K., Smerdon, S. J., & Rittinger, K. (2003) · Cell · doi:10.1016/s0092-8674(03)00314-3 · Cited by 408
Itraconazole to Prevent Fungal Infections in Chronic Granulomatous Disease
Gallin, J. I., Alling, D. W., Malech, H. L., WESLEY, R. A., Koziol, D. E., Marciano, B. E., Eisenstein, E. M., Turner, M. L. C., DeCarlo, E. S., Starling, J. M., et al. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa021931 · Cited by 394
Defective Superoxide Production by Granulocytes from Patients with Chronic Granulomatous Disease
Curnutte, J. T., Whitten, D. M., & BABIOR, B. M. (1974) · New England Journal of Medicine · doi:10.1056/nejm197403142901104 · Cited by 364
Self-citationBrominating Oxidants Generated by Human Eosinophils
Weiss, S. J., Test, S. T., Eckmann, C. M., Roos, D., & REGIANI, S. R. (1986) · Science · doi:10.1126/science.3018933 · Cited by 360
Evidence for Antibody-Catalyzed Ozone Formation in Bacterial Killing and Inflammation
Wentworth, P., McDunn, J. E., Wentworth, A. D., Takeuchi, C., Nieva, J. J., Jones, T., Bautista, C., Ruedi, J. M., Gutierrez, A., Janda, K. D., et al. (2002) · Science · doi:10.1126/science.1077642 · Cited by 349
Self-citationDinauer, M. C., Pierce, E. A., Bruns, G. A. P., Curnutte, J. T., & Orkin, S. H. (1990) · Journal of Clinical Investigation · doi:10.1172/jci114898 · Cited by 334
The Crystal Structure of the PX Domain from p40phox Bound to Phosphatidylinositol 3-Phosphate
Bravo, J., Karathanassis, D., Pacold, C. M., Pacold, M. E., Ellson, C. D., Anderson, K. E., Butler, P. J. G., Lavenir, I., Perišić, O., Hawkins, P. T., et al. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00372-0 · Cited by 284
Superoxide sensitivity of the Escherichia coli 6-phosphogluconate dehydratase
Gardner, P. R., & Fridovich, I. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)52319-x · Cited by 264
Steinbeck, M. J., Khan, A. U., & Karnovsky, M. J. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42228-4 · Cited by 258
Clark, R. A., Malech, H. L., Gallin, J. I., Nunoi, H., Volpp, B. D., Pearson, D. W., Nauseef, W. M., & Curnutte, J. T. (1989) · New England Journal of Medicine · doi:10.1056/nejm198909073211005 · Cited by 244
Mechanism for Phosphorylation-induced Activation of the Phagocyte NADPH Oxidase Protein p47
Ago, T., Nunoi, H., Ito, T., & Sumimoto, H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.47.33644 · Cited by 238
Investigating antibody-catalyzed ozone generation by human neutrophils
BABIOR, B. M., Takeuchi, C., Ruedi, J. M., Gutierrez, A., & Wentworth, P. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0530251100 · Cited by 211
Self-citationJohnston, R. B., & Newman, S. L. (1977) · Pediatric Clinics of North America · doi:10.1016/s0031-3955(16)33424-1 · Cited by 206
Hoyal, C. R., Gutierrez, A., Young, B. M., Catz, S. D., Lin, J.-H., Tsichlis, P. N., & BABIOR, B. M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1031526100 · Cited by 179
Self-citationInanami, O., Johnson, J. L., McAdara, J. K., Benna, J. E., Faust, L. R., Newburger, P. E., & BABIOR, B. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.16.9539 · Cited by 176
Self-citationStructure and mutational analysis of Rab GDP-dissociation inhibitor
Schalk, I. J., Zeng, K., Wu, S.-K., Stura, E. A., Matteson, J., Huang, M., Tandon, A., Wilson, I. A., & Balch, W. E. (1996) · Nature · doi:10.1038/381042a0 · Cited by 171
Architecture of the p40-p47-p67 Complex in the Resting State of the NADPH Oxidase
Lapouge, K., Smith, S. J., Groemping, Y., & Rittinger, K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112065200 · Cited by 166
Steinbeck, M. J., Khan, A. U., & Karnovsky, M. J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82305-5 · Cited by 158
NADPH Oxidase Activity Is Independent of p47
Freeman, J. L. R., & Lambeth, J. D. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.37.22578 · Cited by 157
Activation of p47 , a Cytosolic Subunit of the Leukocyte NADPH Oxidase
Johnson, J. L., Park, J., Benna, J. E., Faust, L. P., Inanami, O., & BABIOR, B. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.52.35147 · Cited by 151
Self-citationWink, D. A., Nims, R. W., Saavedra, J. E., Utermahlen, W. E., & Ford, P. C. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.14.6604 · Cited by 141
Speert, D. P., Bond, M., Woodman, R. C., & Curnutte, J. T. (1994) · The Journal of Infectious Diseases · doi:10.1093/infdis/170.6.1524 · Cited by 137
Eosinophil Peroxidase Oxidation of Thiocyanate
Arlandson, M. E., Decker, T., Roongta, V. A., Bonilla, L. E., Mayo, K. H., MacPherson, J. C., Hazen, S. L., & Slungaard, A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m004881200 · Cited by 130
Cytochrome b-245 of neutrophils is also present in human monocytes, macrophages and eosinophils
Segal, A. W., Garcia, R. C., Goldstone, H. M. H., Cross, A. R., & Jones, O. T. G. (1981) · Biochemical Journal · doi:10.1042/bj1960363 · Cited by 125
Chang, Y. C., Segal, B. H., Holland, S. M., Miller, G., & Kwon-Chung, K. J. (1998) · Journal of Clinical Investigation · doi:10.1172/jci2301 · Cited by 122
Cytochrome b−245 of the Neutrophil Superoxide-generating System Contains Two Nonidentical Hemes
Cross, A. R., Rae, J., & Curnutte, J. T. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.29.17075 · Cited by 117
Curnutte, J. T., Scott, P., & Mayo, L. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.3.825 · Cited by 117
p40 Down-regulates NADPH Oxidase Activity through Interactions with Its SH3 Domain
Sathyamoorthy, M., de Mendez, I., Adams, A. G., & Leto, T. L. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.14.9141 · Cited by 115
Autosomal recessive chronic granulomatous disease caused by deletion at a dinucleotide repeat.
Casimir, C. M., Bu-Ghanim, H. N., Rodaway, A., Bentley, D. L., Rowe, P. S., & Segal, A. W. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.7.2753 · Cited by 114
Bolscher, B. G. J. M., de Boer, M., de Klein, A., Weening, R. S., & Roos, D. (1991) · Blood · doi:10.1182/blood.v77.11.2482.2482 · Cited by 111
Dinauer, M., & Orkin, S. H. (1992) · Annual Review of Medicine · doi:10.1146/annurev.me.43.020192.001001 · Cited by 100
Clinical Features and Current Management of Chronic Granulomatous Disease
Forrest, C. B., Forehand, J. R., Axtell, R. A., Roberts, R. L., & Johnston, R. B. (1988) · Hematology/Oncology Clinics of North America · doi:10.1016/s0889-8588(18)30619-1 · Cited by 92
Tsunawaki, S., Kagara, S., Yoshikawa, K., Yoshida, L. S., Kuratsuji, T., & Namiki, H. (1996) · The Journal of Experimental Medicine · doi:10.1084/jem.184.3.893 · Cited by 90
The Active N-terminal Region of p67
Grizot, S., Fieschi, F., Dagher, M., & Pebay‐Peyroula, E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100893200 · Cited by 83
Smith, R. M., Curnutte, J. T., & BABIOR, B. M. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94127-x · Cited by 72
Self-citationNewburger, P. E., Skalnik, D. G., Hopkins, P. J., Eklund, E. A., & Curnutte, J. T. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117437 · Cited by 66
The management of chronic granulomatous disease
Fischer, A., Segal, A. W., Seger, R. A., & Weening, R. S. (1993) · European Journal of Pediatrics · doi:10.1007/bf01957525 · Cited by 57
Lerner, R. A., & Eschenmoser, A. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0730791100 · Cited by 56
Smith, R. M., Connor, J., Chen, L. M., & BABIOR, B. M. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118882 · Cited by 51
Self-citationÅhlin, A., Elinder, G., & Palmblad, J. E. W. (1997) · Blood · doi:10.1182/blood.v89.9.3396 · Cited by 42
Batot, G., Martel, C., Capdeville, N., Wientjes, F. B., & Morel, F. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.208_c.x · Cited by 41
Segal, A. W. (1991) · Clinical & Experimental Allergy · doi:10.1111/j.1365-2222.1991.tb01727.x · Cited by 40
Casimir, C. M., Chetty, M. C., Bohler, M., Garcia, R. C., Fischer, A., Griscelli, C., Johnson, B., & Segal, A. W. (1992) · European Journal of Clinical Investigation · doi:10.1111/j.1365-2362.1992.tb01481.x · Cited by 39
Smith, R. M., Curnutte, J. T., Mayo, L., & BABIOR, B. M. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63848-7 · Cited by 38
Self-citationMolecular analysis in three cases of X91- variant chronic granulomatous disease
Bu-Ghanim, H. N., Segal, A. W., Keep, N. H., & Casimir, C. M. (1995) · Blood · doi:10.1182/blood.v86.9.3575.bloodjournal8693575 · Cited by 38
NADPH Dehydrogenase Activity of p67PHOX, a Cytosolic Subunit of the Leukocyte NADPH Oxidase
Dang, P. M., BABIOR, B. M., & Smith, R. M. (1999) · Biochemistry · doi:10.1021/bi982750f · Cited by 26
Self-citationApplication of bone marrow transplantation in genetic diseases
Rappeport, J. M., Smith, B. R., Parkman, R., & Rosen, F. S. (1983) · Clinics in Haematology · doi:10.1016/s0308-2261(83)80009-5 · Cited by 25
Aspergillosis in Chronic Granulomatous Disease: Therapeutic Considerations
Corrado, M. L. (1980) · Archives of Pediatrics and Adolescent Medicine · doi:10.1001/archpedi.1980.02130230070021 · Cited by 18
Fujii, H. G., Finnegan, M. G., Miki, T., Crouse, B. R., Kakinuma, K., & Johnson, M. K. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)01372-5 · Cited by 14
Fujii, H. G., Finnegan, M. G., & Johnson, M. K. (1999) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a022507 · Cited by 12
Expression and characterization of the flavoprotein domain of gp91phox
Han, C. H., & Lee, M. H. (2000) · Journal of Veterinary Science · doi:10.4142/jvs.2000.1.1.19 · Cited by 4
Flagged first, then by citations
Research works printed but not linked: 2
- Roesler, 1995, Recombination events between the normal p47-phox gene and a highly homologous pseudogene are the main cause of autosomal recessive chronic granulomatous disease, Blood, 86, 260a
- Groemping, 2002, Molecular basis of phosphorylation-induced activation of the NADPH oxidase, Cell, 113, 343, 10.1016/S0092-8674(03)00314-3 · DOI
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Ott, M., Schmidt, M., Schwarzwaelder, K., Stein, S., Siler, U., Koehl, U., Glimm, H., Kühlcke, K., Schilz, A. J., Kunkel, H., et al. (2006) · Nature Medicine · doi:10.1038/nm1393 · Cited by 1,189
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Metadata
- Authors
- Babior, B. M.
- Affiliations
- Scripps Research Institute (US)
- Corresponding author
- Babior, Bernard M
- Venue
- Current Opinion in Immunology
- Publisher
- Elsevier BV
- Published
- 2004-02
- Volume
- 16
- Issue
- 1
- Pages
- 42-47
- ISSN
- 0952-7915 (ISSN-L)
- OpenAlex
- W4242182607
- Cited by
- 705
- References
- 63
- Citations by year
- 2026: 7 · 2025: 8 · 2024: 25 · 2023: 20 · 2022: 28 · 2021: 24 · 2020: 34 · 2019: 22 · 2018: 21 · 2017: 26 · 2016: 29 · 2015: 29 · 2014: 53 · 2013: 40 · 2012: 42
- FWCI
- 2.15
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Current Opinion in Immunology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01ai044434-05)
- National Institute of Allergy and Infectious Diseases (AI44434, R01AI028479, AI-24227, AI28479)
- 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, superoxide production, Rac1, Rac2, Src homology 3 domain, chronic granulomatous disease, antifungal prophylaxis, crystal structure
- MeSH terms
- Granulomatous Disease, Chronic, Humans, Models, Molecular, Crystallography, X-Ray, src Homology Domains, NADPH Oxidases, Protein Subunits
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