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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In the citing paper
“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
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Cell transformation by the superoxide-generating oxidase Mox1
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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.
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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
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
Cited by
Sorted by citations
Myeloperoxidase: friend and foe
Klebanoff, S. J. (2005) · Journal of Leukocyte Biology · doi:10.1189/jlb.1204697 · Cited by 2,282
Ying, W. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1672 · Cited by 1,494
The role of oxidative stress in neurodegenerative diseases
Kim, G. H., Kim, J. E., Rhie, S. J., & Yoon, S. (2015) · Experimental Neurobiology · doi:10.5607/en.2015.24.4.325 · Cited by 1,355
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 1,202
Hydrogen Peroxide: A Signaling Messenger
Stone, J. R., & Yang, S. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.243 · Cited by 1,194
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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