Cited by 301Neutrophil, Myeloperoxidase and Oxidative MechanismsRedox biology and oxidative stressNitric Oxide and Endothelin Effects

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p40 phox , a third cytosolic component of the activation complex of the NADPH oxidase to contain src homology 3 domains

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Wientjes, F B, Hsuan, J J, Totty, N F, Segal, A W·1993·Biochemical Journal

DOI 10.1042/bj2960557PMC PMC1137734

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Abstract

The NADPH oxidase generates superoxide in phagocytic cells. It is important for immunity and its deficiency leads to chronic granulomatous disease (CGD). It consists of a membrane-bound flavocytochrome b that lies dormant until activated by the translocation to the plasma membrane of cytosolic proteins, p47phox (phox for phagocyte oxidase), p67phox and p21rac, a small GTP-binding protein. We show here that a novel component, p40phox, forms an activation complex with p47phox and p67phox with which it translocates to the membrane to associate with the flavocytochrome b. cDNA cloning and amino acid analysis revealed that p40phox has an src homology 3 (SH3) domain and a large region of sequence similarity with the N-terminus of p47phox. The primary association of p40phox appears to be with p67phox, and it is present in reduced amounts in patients with CGD lacking p67phox.

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DNA sequencing with chain-terminating inhibitors
Sanger, F., Nicklen, S., & Coulson, A. R. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.12.5463 · Cited by 68,572
Improved tools for biological sequence comparison.
Pearson, W. R., & Lipman, D. J. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.8.2444 · Cited by 11,227
An analysis of 5'-noncoding sequences from 699 vertebrate messenger RNAs
Kozak, M. (1987) · Nucleic Acids Research · doi:10.1093/nar/15.20.8125 · Cited by 5,090
Progressive sequence alignment as a prerequisitetto correct phylogenetic trees
Feng, D.-F., & Doolittle, R. F. (1987) · Journal of Molecular Evolution · doi:10.1007/bf02603120 · Cited by 1,883
Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation
Egan, S. E., Giddings, B. W., Brooks, M. W., Buday, L., Sizeland, A. M., & Weinberg, R. A. (1993) · Nature · doi:10.1038/363045a0 · Cited by 1,200
Identification of a Ten-Amino Acid Proline-Rich SH3 Binding Site
Ren, R., Mayer, B. J., Cicchetti, P., & Baltimore, D. (1993) · Science · doi:10.1126/science.8438166 · Cited by 1,191
Activation of the NADPH oxidase involves the small GTP-binding protein p21rac1
Abo, A., Pick, E., Hall, A., Totty, N. F., Teahan, C. G., & Segal, A. W. (1991) · Nature · doi:10.1038/353668a0 · Cited by 954
Self-citation
The biochemical basis of the NADPH oxidase of phagocytes
Segal, A. W., & Abo, A. (1993) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(93)90051-n · Cited by 622
Self-citation
The superoxide‐generating oxidase of phagocytic cells
Morel, F., Doussière, J., & Vignais, P. V. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb16312.x · Cited by 565
How receptors turn Ras on
McCormick, F. (1993) · Nature · doi:10.1038/363015a0 · Cited by 408

Show all 27 references

Research works printed but not linked: 5

Abo, A., Webb, M. R., Grogan, A. and Segal, A. W. (1994) Biochem J., in the press
Gullick, W. J. (1988) in Methods in Molecular Biology, New Protein Techniques (Walker, J. M., ed.), vol. 3, pp. 341-354, The Humana Press, Clifton, NJ, U.S.A. Heyworth, P. G., Shrimpton, C. F. and Segal, A. W. (1989) Biochem. J. 260, 243-248
Heyworth, P. G., Curnutte, J. T., Nauseef, W. M., Volpp, B. D., Pearson, D. W., Rosen, H. and Clark, R. A. (1991) J. Clin. Invest. 87, 352-356
Pearson, W. R. and Lipman, D. J. (1988) Proc. Natl. Acad. Sci. U.S.A. 85, 2444-2448
Sanger, F., Nicklen, S. and Coulson, A. R. (1977) Proc. Natl. Acad. Sci. U.S.A. 74, 5463-5467

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Authors: Wientjes, F. B., Hsuan, J. J., Totty, N. F., & Segal, A. W.
Affiliations: University College London (GB)
Ludwig Cancer Research (GB)
ORCID: Hsuan, J J
Segal, A W
Venue: Biochemical Journal
Publisher: Portland Press Ltd.
Published: 1993-12-15
Volume: 296
Issue: 3
Pages: 557-561
ISSN: 0264-6021 (ISSN-L)
1470-8728
DOI: 10.1042/bj2960557
PMC: PMC1137734
OpenAlex: W1727958888
Cited by: 301
References: 27
Citations by year: 2026: 3 · 2025: 3 · 2024: 3 · 2023: 9 · 2022: 4 · 2021: 7 · 2020: 3 · 2019: 6 · 2018: 3 · 2017: 6 · 2016: 6 · 2015: 6 · 2014: 11 · 2013: 11 · 2012: 2
FWCI: 6.94
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Biochemical Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Wellcome Trust
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: p40phox, NADPH oxidase, superoxide production, chronic granulomatous disease, p47phox, p67phox, Src homology 3 domain, membrane translocation, phagocytes, G proteins
MeSH terms: Amino Acid Sequence, Base Sequence, Biological Transport, Cell Membrane, Cloning, Molecular, Enzyme Activation, Granulomatous Disease, Chronic, Humans, Molecular Sequence Data, NADH, NADPH Oxidoreductases, Neutrophils, Phosphoproteins, Genes, src, Sequence Homology, Amino Acid, DNA, Complementary, NADPH Oxidases

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p40 phox , a third cytosolic component of the activation complex of the NADPH oxidase to contain src homology 3 domains

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