Mapping sites of interaction of p47-phox and flavocytochrome b with random-sequence peptide phage display libraries.
Open accessAbstract
During assembly of the phagocyte NADPH oxidase, cytosolic p47-phox translocates to the plasma membrane and binds to flavocytochrome b, and binding domains for p47-phox have been identified on the C-terminal tails of both flavocytochrome b subunits. In the present report, we further examine the interaction of these two oxidase components by using random-sequence peptide phage display library analysis. Screening p47-phox with the peptide libraries identified five potential sites of interaction with flavocytochrome b, including three previously reported regions of interaction and two additional regions of interaction of p47-phox with gp91-phox and p22-phox. The additional sites were mapped to a domain on the first predicted cytosolic loop of gp91-phox encompassing residues S86TRVRRQL93 and to a domain near the cytosolic C-terminal tail of gp91-phox encompassing residues F450EWFADLL457. The mapping also confirmed a previously reported binding domain on gp91-phox (E554SGPRGVHFIF564) and putative Src homology 3 domain binding sites on p22-phox (P156PRPP160 and G177GPPGGP183). To demonstrate that the additional regions identified were biologically significant, peptides mimicking the gp91-phox sequences F77LRGSSACCSTRVRRQL93 and E451WFADLLQLLESQ463 were synthesized and assayed for their ability to inhibit NADPH oxidase activity. These peptides had EC50 values of 1 microM and 230 microM, respectively, and inhibited activation when added prior to assembly but did not affect activity of the preassembled oxidase. Our data demonstrate the usefulness of phage display library analysis for the identification of biologically relevant sites of protein-protein interaction and show that the binding of p47-phox to flavocytochrome b involves multiple binding sites along the C-terminal tails of both gp91- and p22-phox and other regions of gp91-phox nearer to the N terminus.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
NOX2 docking sequence-tat (NOX2ds-tat) is the first isoform-specific NOX inhibitor, a peptide based on the sequence of the B-loop of NOX2.
“NOX2 docking sequence-tat (NOX2ds-tat), the first isoform-specific NOX inhibitor, is a peptide based on the sequence of the B-loop of NOX2 (199, 218, 782).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [218]
Cites
Molecular cloning: A laboratory manual
Deininger, P. L. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90595-z · Cited by 84,684 · see citing works
Searching for Peptide Ligands with an Epitope Library
Scott, J. K., & Smith, G. P. (1990) · Science · doi:10.1126/science.1696028 · Cited by 2,087 · see citing works
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 · see citing works
Peptides on phage: a vast library of peptides for identifying ligands.
Cwirla, S. E., Peters, E. A., Barrett, R. W., & Dower, W. J. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.16.6378 · Cited by 930 · see citing works
Random Peptide Libraries: a Source of Specific Protein Binding Molecules
Devlin, J. J., Panganiban, L. C., & Devlin, P. E. (1990) · Science · doi:10.1126/science.2143033 · Cited by 923 · see citing works
[15] Libraries of peptides and proteins displayed on filamentous phage
Smith, G. P., & Scott, J. K. (1993) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(93)17065-d · Cited by 776 · see citing works
Mammalian Membrane-bound Adenylyl Cyclases
Taussig, R., & Gilman, A. G. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.1.1 · Cited by 719 · see citing works
Regulation of Phagocyte Oxygen Radical Production by the GTP-Binding Protein Rac 2
Knaus, U. G., Heyworth, P. G., Evans, T., Curnutte, J. T., & Bokoch, G. (1991) · Science · doi:10.1126/science.1660188 · Cited by 673 · see citing works
The respiratory burst oxidase.
Chanock, S. J., Benna, J. E., Smith, R. M., & BABIOR, B. M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31418-7 · Cited by 595 · see citing works
Parkos, C. A., Allen, R. A., Cochrane, C. G., & Jesaitis, A. J. (1987) · Journal of Clinical Investigation · doi:10.1172/jci113128 · Cited by 455 · see citing works
Self-citationClark, R. A., Volpp, B. D., Leidal, K. G., & Nauseef, W. M. (1990) · Journal of Clinical Investigation · doi:10.1172/jci114496 · Cited by 431 · see citing works
Two cytosolic neutrophil oxidase components absent in autosomal chronic granulomatous disease
Volpp, B. D., Nauseef, W. M., & Clark, R. A. (1988) · Science · doi:10.1126/science.2848318 · Cited by 407 · see citing works
Cytochrome b 558 : the Flavin-Binding Component of the Phagocyte NADPH Oxidase
Rotrosen, D., Yeung, C. L., Leto, T. L., Malech, H. L., & Kwong, C. H. (1992) · Science · doi:10.1126/science.1318579 · Cited by 378 · see citing works
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 373 · see citing works
Segal, A. W., West, I., Wientjes, F. B., Nugent, J. H. A., Chavan, A. J., Haley, B. E., Garcia, R. C., Rosen, H., & Scrace, G. (1992) · Biochemical Journal · doi:10.1042/bj2840781 · Cited by 347 · see citing works
Substrate Phage: Selection of Protease Substrates by Monovalent Phage Display
Matthews, D. J., & Wells, J. A. (1993) · Science · doi:10.1126/science.8493554 · Cited by 344 · see citing works
Two Forms of Autosomal Chronic Granulomatous Disease Lack Distinct Neutrophil Cytosol Factors
Nunoi, H., Rotrosen, D., Gallin, J. I., & Malech, H. L. (1988) · Science · doi:10.1126/science.2848319 · Cited by 331 · see citing works
Quinn, M. T., Evans, T., Loetterle, L. R., Jesaitis, A. J., & Bokoch, G. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36882-6 · Cited by 311 · see citing works
Self-citationIsolation of a highly specific ligand for the alpha 5 beta 1 integrin from a phage display library
Koivunen, E., Wang, B., & Ruoslahti, E. I. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.124.3.373 · Cited by 308 · see citing works
Assembly of the phagocyte NADPH oxidase: binding of Src homology 3 domains to proline-rich targets.
Leto, T. L., Adams, A. G., & de Mendez, I. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.22.10650 · Cited by 298 · see citing works
Role of Src homology 3 domains in assembly and activation of the phagocyte NADPH oxidase.
Sumimoto, H., Kage, Y., Nunoi, H., Sasaki, H., Nose, T., Fukumaki, Y., Ohno, M., Minakami, S., & Takeshige, K. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.12.5345 · Cited by 296 · see citing works
The Human Neutrophil Respiratory Burst Oxidase
Clark, R. A. (1990) · The Journal of Infectious Diseases · doi:10.1093/infdis/161.6.1140 · Cited by 222 · see citing works
Activation of neutrophil leukocytes: chemoattractant receptors and respiratory burst 1
Baggiolini, M., Boula, F., Badwey, J. A., & Curnutte, J. T. (1993) · The FASEB Journal · doi:10.1096/fasebj.7.11.8396540 · Cited by 181 · see citing works
Sparks, A. B., Quilliam, L. A., Thorn, J. M., Der, C. J., & Kay, B. K. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)51013-4 · Cited by 163 · see citing works
Finan, P. M., Shimizu, Y., Gout, I. T., Hsuan, J. J., Truong, O., Butcher, C., Bennett, P., Waterfield, M. D., & Kellie, S. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36710-8 · Cited by 160 · see citing works
The Respiratory Burst Oxidase and the Molecular Genetics of Chronic Granulomatous Disease
Dinauer, M. C., & Newburger, P. E. (1993) · Critical Reviews in Clinical Laboratory Sciences · doi:10.3109/10408369309082591 · Cited by 129 · see citing works
Leto, T. L., Garrett, M. C., Fujii, H., & Nunoi, H. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55064-x · Cited by 120 · see citing works
Identification of a Src SH3 domain binding motif by screening a random phage display library.
Cheadle, C., Ivashchenko, Y., South, V., Searfoss, G. H., French, S., Howk, R. S., Ricca, G. A., & Jaye, M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)51043-2 · Cited by 119 · see citing works
Leusen, J. H. W., Bolscher, B. G. J. M., Hilarius, P. M., Weening, R. S., Kaulfersch, W., Seger, R. A., Roos, D., & Verhoeven, A. J. (1994) · The Journal of Experimental Medicine · doi:10.1084/jem.180.6.2329 · Cited by 111 · see citing works
Leusen, J. H. W., de Boer, M., Bolscher, B. G. J. M., Hilarius, P. M., Weening, R. S., Ochs, H. D., Roos, D., & Verhoeven, A. J. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117207 · Cited by 108 · see citing works
Yayon, A., Aviezer, D., Safran, M., Gross, J. L., Heldman, Y., Cabilly, S., Givol, D., & Katchalski‐Katzir, E. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.22.10643 · Cited by 105 · see citing works
Molecular basis of oxidative damage by leukocytes
Dratz, E. A., & Jesaitis, A. J. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90132-e · Cited by 92 · see citing works
Self-citationQuinn, M. T., Parkos, C. A., & Jesaitis, A. J. (1989) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(89)90458-6 · Cited by 90 · see citing works
Self-citationKleinberg, M. E., Malech, H. L., & Rotrosen, D. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55436-3 · Cited by 87 · see citing works
Nakanishi, A., Imajoh‐Ohmi, S., Fujinawa, T., Kikuchi, H., & Kanegasaki, S. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41742-5 · Cited by 79 · see citing works
Hoess, R. H., Mack, A. J., Walton, H. L., & Reilly, T. M. (1994) · The Journal of Immunology · doi:10.4049/jimmunol.153.2.724 · Cited by 63 · see citing works
Functional domain in an arginine-rich carboxyl-terminal region of p47phox.
Nauseef, W. M., McCormick, S. J., Renee, J., Leidal, K. G., & Clark, R. A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49511-2 · Cited by 62 · see citing works
Fujita, I., Takeshige, K., & Minakami, S. (1987) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(87)90048-6 · Cited by 58 · see citing works
Joseph, G., Gorzalczany, Y., Koshkin, V., & Pick, E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)62008-9 · Cited by 57 · see citing works
Yu, L., Takeshige, K., Nunoi, H., & Minakami, S. (1993) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(93)90111-2 · Cited by 5 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
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
BABIOR, B. M. (1999) · Blood · doi:10.1182/blood.v93.5.1464 · Cited by 2,147 · see citing works
NADPH oxidases: An overview from structure to innate immunity-associated pathologies
Panday, A., Sahoo, M. K., Osorio, D., & Batra, S. (2015) · Cellular & Molecular Immunology · doi:10.1038/cmi.2014.89 · Cited by 944 · see citing works
Combating oxidative stress in vascular disease: NADPH oxidases as therapeutic targets
Drummond, G. R., Selemidis, S., Griendling, K. K., & Sobey, C. G. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3403 · Cited by 899 · see citing works
Genetic, Biochemical, and Clinical Features of Chronic Granulomatous Disease
Segal, B. H., Leto, T. L., Gallin, J. I., Malech, H. L., & Holland, S. M. (2000) · Medicine · doi:10.1097/00005792-200005000-00004 · Cited by 877 · see citing works
Functional analysis of Nox4 reveals unique characteristics compared to other NADPH oxidases
Martyn, K. D., Frederick, L. M., von Loehneysen, K., Dinauer, M. C., & Knaus, U. G. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2005.03.023 · Cited by 783 · see citing works
The superoxide-generating NADPH oxidase: structural aspects and activation mechanism
Vignais, P. V. (2002) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-002-8520-9 · Cited by 773 · see citing works
NADPH Oxidases (NOX): An Overview from Discovery, Molecular Mechanisms to Physiology and Pathology
Vermot, A., Petit-Härtlein, I., Smith, S. M. E., & Fieschi, F. (2021) · Antioxidants · doi:10.3390/antiox10060890 · Cited by 766 · see citing works
Regulation of Reactive Oxygen Species Generation in Cell Signaling
Bae, Y. S., Oh, H., Rhee, S. G., & Yoo, Y. D. (2011) · Molecules and Cells · doi:10.1007/s10059-011-0276-3 · Cited by 660 · see citing works
Rey, F. E., Cifuentes-Pagano, E., Kiarash, A., Quinn, M. T., & Pagano, P. J. (2001) · Circulation Research · doi:10.1161/hh1701.096037 · Cited by 606 · see citing works
Self-citationKeller, T., Damude, H. G., Werner, D., Doerner, P. W., Dixon, R. A., & Lamb, C. J. (1998) · The Plant Cell · doi:10.1105/tpc.10.2.255 · Cited by 604 · see citing works
Activation and assembly of the NADPH oxidase: a structural perspective
Groemping, Y., & Rittinger, K. (2005) · Biochemical Journal · doi:10.1042/bj20041835 · Cited by 559 · see citing works
Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation
Tejero, J., Shiva, S., & Gladwin, M. T. (2019) · Physiological Reviews · doi:10.1152/physrev.00036.2017 · Cited by 541 · see citing works
Assembly of the phagocyte NADPH oxidase: molecular interaction of oxidase proteins
DeLeo, F. R., & Quinn, M. T. (1996) · Journal of Leukocyte Biology · doi:10.1002/jlb.60.6.677 · Cited by 526 · see citing works
Self-citationThe NADPH oxidase of professional phagocytes—prototype of the NOX electron transport chain systems
Cross, A. R., & Segal, A. W. (2004) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2004.03.008 · Cited by 489 · see citing works
Quinn, M. T., & Gauss, K. A. (2004) · Journal of Leukocyte Biology · doi:10.1189/jlb.0404216 · Cited by 480 · see citing works
Self-citationTanaka, A., Christensen, M. J., Takemoto, D., Park, P., & Scott, B. (2006) · The Plant Cell · doi:10.1105/tpc.105.039263 · Cited by 468 · see citing works
Assembly of the phagocyte NADPH oxidase
Nauseef, W. M. (2004) · Histochemistry and Cell Biology · doi:10.1007/s00418-004-0679-8 · Cited by 427 · see citing works
NOX Activation by Subunit Interaction and Underlying Mechanisms in Disease
Rastogi, R., Geng, X., Li, F., & Ding, Y. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2016.00301 · Cited by 249 · see citing works
Selemidis, S., Sobey, C. G., Wingler, K., Schmidt, H. H. H. W., & Drummond, G. R. (2008) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2008.08.005 · Cited by 241 · see citing works
Nox enzymes as novel targets for drug development
Lambeth, J. D., Krause, K.-H., & Clark, R. A. (2008) · Seminars in Immunopathology · doi:10.1007/s00281-008-0123-6 · Cited by 212 · see citing works
Diatchuk, V., Lotan, O., Koshkin, V., Wikstroem, P., & Pick, E. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.20.13292 · Cited by 195 · see citing works
Liu, J., Yang, F., Yang, X.-P., Jankowski, M. A., & Pagano, P. J. (2003) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000066684.37829.16 · Cited by 186 · see citing works
Chan, E. C., Jiang, F., Peshavariya, H., & Dusting, G. J. (2009) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2009.02.005 · Cited by 162 · see citing works
Koshkin, V., Lotan, O., & Pick, E. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.48.30326 · Cited by 158 · see citing works
Regulation of NADPH oxidases in skeletal muscle
Ferreira, L. F., & Laitano, O. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.05.011 · Cited by 150 · see citing works
NADPH Oxidase Inhibitors: New Antihypertensive Agents?
Williams, H. C., & Griendling, K. K. (2007) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0b013e318063e820 · Cited by 146 · see citing works
Identification of Structural Elements in Nox1 and Nox4 Controlling Localization and Activity
Helmcke, I., Heumüller, S., Tikkanen, R., Schröder, K., & Brandes, R. P. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2383 · Cited by 145 · see citing works
Jacobson, G. M., Dourron, H. M., Liu, J., Carretero, O. A., Reddy, D. J., Andrzejewski, T., & Pagano, P. J. (2003) · Circulation Research · doi:10.1161/01.res.0000063423.94645.8a · Cited by 144 · see citing works
Suh, C.-I., Stull, N. D., Li, X. J., Tian, W., Price, M. O., Grinstein, S., Yaffe, M. B., Atkinson, S. J., & Dinauer, M. C. (2006) · The Journal of Experimental Medicine · doi:10.1084/jem.20052085 · Cited by 141 · see citing works
Nox2 B-loop peptide, Nox2ds, specifically inhibits the NADPH oxidase Nox2
Csányi, G., Cifuentes-Pagano, E., Al Ghouleh, I., Ranayhossaini, D. J., Egaña, L., Lopes, L. R., Jackson, H. M., Kelley, E. E., & Pagano, P. J. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.04.025 · Cited by 131 · see citing works
The NADPH Oxidase Family and its Inhibitors
Kleniewska, P., Piechota-Polańczyk, A., Skibska, B., & Gorąca, A. (2012) · Archivum Immunologiae et Therapiae Experimentalis · doi:10.1007/s00005-012-0176-z · Cited by 126 · see citing works
Structural Insights into Nox4 and Nox2: Motifs Involved in Function and Cellular Localization
von Löhneysen, K., Noack, D., Wood, M. R., Friedman, J. S., & Knaus, U. G. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01393-09 · Cited by 124 · see citing works
DeLeo, F. R., Ulman, K. V., Davis, A. R., Jutila, K. L., & Quinn, M. T. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.29.17013 · Cited by 123 · see citing works
Self-citationSelection of biologically active peptides by phage display of random peptide libraries
Cortese, R. (1996) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(96)80072-3 · Cited by 120 · see citing works
Interactions between the components of the human nadph oxidase: intrigues in the phox family
Leusen, J. H. W., Verhoeven, A. J., & Roos, D. (1996) · Journal of Laboratory and Clinical Medicine · doi:10.1016/s0022-2143(96)90043-8 · Cited by 118 · see citing works
Wu, H., Chang, D.-K., & Huang, C.-T. (2006) · Cited by 118 · see citing works
Gómez, I., Oltean, D. I., Gill, S. S., Bravo, A., & Soberón, M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103007200 · Cited by 108 · see citing works
Swain, S. D., Helgerson, S. L., Davis, A. R., Nelson, L. K., & Quinn, M. T. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.47.29502 · Cited by 105 · see citing works
Self-citationNADPH 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
NADPH oxidases: Current aspects and tools
Schröder, K. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101512 · Cited by 105 · see citing works
A Domain of p47phox That Interacts with Human Neutrophil Flavocytochrome b558
DeLeo, F. R., Nauseef, W. M., Jesaitis, A. J., Burritt, J. B., Clark, R. A., & Quinn, M. T. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.44.26246 · Cited by 100 · see citing works
Self-citationNADPH Oxidases as Regulators of Tumor Angiogenesis: Current and Emerging Concepts
Coso, S., Harrison, I., Harrison, C. B., Vinh, A., Sobey, C. G., Drummond, G. R., Williams, E. D., & Selemidis, S. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4489 · Cited by 99 · see citing works
Allen, L. H., DeLeo, F. R., Gallois, A., Toyoshima, S., Suzuki, K., & Nauseef, W. M. (1999) · Blood · doi:10.1182/blood.v93.10.3521.410k21_3521_3530 · Cited by 96 · see citing works
Self-citationDahan, I. M., Issaeva, I., Gorzalczany, Y., Sigal, N., Hirshberg, M., & Pick, E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109778200 · Cited by 94 · see citing works
NADPH oxidase inhibitors: a decade of discovery from Nox2ds to HTS
Cifuentes-Pagano, E., Csányi, G., & Pagano, P. J. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1009-2 · Cited by 92 · see citing works
The NADPH Oxidase Family and Its Inhibitors
Chocry, M., & Leloup, L. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7915 · Cited by 89 · see citing works
Targeting reactive oxygen species in hypertension
Cifuentes-Pagano, E., & Pagano, P. J. (2006) · Current Opinion in Nephrology & Hypertension · doi:10.1097/01.mnh.0000214776.19233.68 · Cited by 88 · see citing works
The NADPH‐Dependent Oxidase of Phagocytes
Nauseef, W. M. (1999) · Proceedings of the Association of American Physicians · doi:10.1111/paa.1999.111.5.373 · Cited by 88 · see citing works
Lardy, B., Bof, M., Aubry, L., Paclet, M. H., Morel, F., Satre, M., & Klein, G. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2005.02.004 · Cited by 83 · see citing works
The Quest for Selective Nox Inhibitors and Therapeutics: Challenges, Triumphs and Pitfalls
Cifuentes-Pagano, E., Meijles, D. N., & Pagano, P. J. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5620 · Cited by 84 · see citing works
Cell-Specific Peptide Binding by Human Neutrophils
Mazzucchelli, L., Burritt, J. B., Jesaitis, A. J., Nusrat, A., Liang, T. W., Gewirtz, A. T., Schnell, F. J., & Parkos, C. A. (1999) · Blood · doi:10.1182/blood.v93.5.1738 · Cited by 78 · see citing works
Self-citationGorzalczany, Y., Alloul, N., Sigal, N., Weinbaum, C., & Pick, E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202114200 · Cited by 77 · see citing works
Effects of angiotensin II on the cerebral circulation: role of oxidative stress
Silva, T. M. D., & Faraci, F. M. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2012.00484 · Cited by 75 · see citing works
From peptides to drugs via phage display
Kay, B. K., Kurakin, A. V., & Hyde‐DeRuyscher, R. (1998) · Drug Discovery Today · doi:10.1016/s1359-6446(98)01220-3 · Cited by 75 · see citing works
Roos, D. (1996) · Frontiers in bioscience · doi:10.2741/a117 · Cited by 75 · see citing works
Phage Display Epitope Mapping of Human Neutrophil Flavocytochromeb 558
Burritt, J. B., DeLeo, F. R., McDonald, C., Prigge, J. R., Dinauer, M. C., Nakamura, M., Nauseef, W. M., & Jesaitis, A. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006236200 · Cited by 72 · see citing works
Self-citationNADPH Oxidase as a Therapeutic Target for Oxalate Induced Injury in Kidneys
Joshi, S. K., Peck, A. B., & Khan, S. R. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/462361 · Cited by 69 · see citing works
X-CGDbase: a database of X-CGD-causing mutations
Roosl, D., Curnutte, J. T., Hossle, J. P., Lau, Y., Ariga, T., Nunoi, H., Dinauer, M. C., Gahr, M. L., Segal, A. W., Newburger, P. E., et al. (1996) · Immunology Today · doi:10.1016/s0167-5699(96)80905-4 · Cited by 66 · see citing works
Boslett, J., Hemann, C., Christofi, F. L., & Zweier, J. L. (2018) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00139.2017 · Cited by 65 · see citing works
Yu, J., Weïwer, M., Linhardt, R. J., & Dordick, J. S. (2008) · Current Vascular Pharmacology · doi:10.2174/157016108784911984 · Cited by 62 · see citing works
Derochette, S., Franck, T. J., Mouithys-Mickalad, A. A., Ceusters, J. D., Deby-Dupont, G. P., Lejeune, J., Neven, P., & Serteyn, D. (2013) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2013.09.011 · Cited by 57 · see citing works
NADPH Oxidases as Novel Pharmacologic Targets against Influenza A Virus Infection
Vlahos, R., & Selemidis, S. (2014) · Molecular Pharmacology · doi:10.1124/mol.114.095216 · Cited by 57 · see citing works
The NOX1/4 Inhibitor GKT136901 as Selective and Direct Scavenger of Peroxynitrite
Schildknecht, S., Weber, A., Gerding, H., Pape, R., Robotta, M., Drescher, M., Marquardt, A., Daiber, A., Ferger, B., & Leist, M. (2013) · Current Medicinal Chemistry · doi:10.2174/09298673113209990179 · Cited by 55 · see citing works
Peptide-based inhibitors of the phagocyte NADPH oxidase
Benna, J. E., Dang, P. M., & Périanin, A. (2010) · Biochemical Pharmacology · doi:10.1016/j.bcp.2010.05.020 · Cited by 55 · see citing works
Nox Inhibitors & Therapies: Rational Design of Peptidic and Small Molecule Inhibitors
Cifuentes-Pagano, E., Meijles, D. N., & Pagano, P. J. (2015) · Current Pharmaceutical Design · doi:10.2174/1381612821666151029112013 · Cited by 55 · see citing works
Antibody Imprint of a Membrane Protein Surface
Burritt, J. B., Busse, S. C., Gizachew, D., Siemsen, D. W., Quinn, M. T., Bond, C. W., Dratz, E. A., & Jesaitis, A. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.38.24847 · Cited by 55 · see citing works
Self-citationDavis, A. R., Mascolo, P. L., Bunger, P. L., Sipes, K. M., & Quinn, M. T. (1998) · Journal of Leukocyte Biology · doi:10.1002/jlb.64.1.114 · Cited by 54 · see citing works
Self-citationvon Löhneysen, K., Noack, D., Hayes, P., Friedman, J. S., & Knaus, U. G. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.332494 · Cited by 53 · see citing works
Morozov, G. I., Lotan, O., Joseph, G., Gorzalczany, Y., & Pick, E. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.25.15435 · Cited by 50 · see citing works
Nox4 B-loop Creates an Interface between the Transmembrane and Dehydrogenase Domains
Jackson, H. M., Kawahara, T., Nisimoto, Y., Smith, S. M. E., & Lambeth, J. D. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.084939 · Cited by 49 · see citing works
Phage display mapping for peptide 11 sensitive sequences binding to laminin-1
Kazmin, D. A., Hoyt, T., Taubner, L. M., Teintze, M., & Starkey, J. R. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3680 · Cited by 48 · see citing works
Nishida, S., Yoshida, L. S., Shimoyama, T., Nunoi, H., Kobayashi, T., & Tsunawaki, S. (2004) · Infection and Immunity · doi:10.1128/iai.73.1.235-244.2005 · Cited by 48 · see citing works
Wu, H., Jung, M.-Y., Chiu, C., Chao, T.-T., Lai, S.-C., Jan, J., & Shaio, M. (2003) · Journal of General Virology · doi:10.1099/vir.0.19228-0 · Cited by 46 · see citing works
Li, X. J., Grünwald, D., Mathieu, J., Morel, F., & Stasia, M. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500226200 · Cited by 45 · see citing works
Biberstine-Kinkade, K. J., Yu, L., & Dinauer, M. C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.15.10451 · Cited by 45 · see citing works
Self-citationZhen, L., Yu, L., & Dinauer, M. C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.11.6575 · Cited by 44 · see citing works
Self-citationFunctional Epitope on Human Neutrophil Flavocytochrome b 558
Burritt, J. B., Foubert, T. R., Baniulis, D., Lord, C. I., Taylor, R. M., MILLS, J. S., Baughan, T. D., Roos, D., Parkos, C. A., & Jesaitis, A. J. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.170.12.6082 · Cited by 44 · see citing works
Self-citationLocalization of Nox2 N-terminus using polyclonal antipeptide antibodies
Paclet, M., HENDERSON, L. M., Campion, Y., Morel, F., & Dagher, M. (2004) · Biochemical Journal · doi:10.1042/bj20040954 · Cited by 43 · see citing works
Fang, J., Sheng, R., & Qin, Z. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2021.0040 · Cited by 39 · see citing works
NOX2 is the primary source of angiotensin II-induced superoxide in the macula densa
Fu, Y., Zhang, R., Lu, D., Liu, H., Chandrashekar, K., Juncos, L. A., & Liu, R. (2010) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00762.2009 · Cited by 39 · see citing works
Yu, L., Cross, A. R., Zhen, L., & Dinauer, M. C. (1999) · Blood · doi:10.1182/blood.v94.7.2497.419k11_2497_2504 · Cited by 39 · see citing works
Self-citationRegulation of the Phagocyte Respiratory Burst Oxidase by Protein Interactions
Lambeth, J. D. (2000) · BMB Reports · Cited by 38 · see citing works
Dahan, I. M., & Pick, E. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1007-4 · Cited by 36 · see citing works
Chen, Y., Huang, H., Lin, C., Chen, Y., King, C., & Wu, H. (2007) · Clinical and Vaccine Immunology · doi:10.1128/cvi.00249-06 · Cited by 34 · see citing works
Boltaña, S., Doñate, C., Goetz, F. W., MacKenzie, S. A., & Balasch, J. C. (2008) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2008.11.011 · Cited by 31 · see citing works
Intracellular Expression of Peptide Fusions for Demonstration of Protein Essentiality in Bacteria
Benson, R. E., Gottlin, E. B., Christensen, D. J., & Hamilton, P. T. (2003) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.47.9.2875-2881.2003 · Cited by 31 · see citing works
Dusi, S., Nadalini, K. A., Donini, M., Zentilin, L., Wientjes, F. B., Roos, D., Giacca, M., & Rossi, F. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.161.9.4968 · Cited by 30 · see citing works
Jesaitis, A. J., Gizachew, D., Dratz, E. A., Siemsen, D. W., Stone, K. C., & Burritt, J. B. (1999) · Protein Science · doi:10.1110/ps.8.4.760 · Cited by 28 · see citing works
Self-citationNOX2β: A Novel Splice Variant of NOX2 That Regulates NADPH Oxidase Activity in Macrophages
Harrison, C. B., Selemidis, S., Guida, E., King, P. T., Sobey, C. G., & Drummond, G. R. (2012) · PLoS ONE · doi:10.1371/journal.pone.0048326 · Cited by 27 · see citing works
Analysis of Human Phagocyte Flavocytochrome b558 by Mass Spectrometry
Taylor, R. M., Baniulis, D., Burritt, J. B., Gripentrog, J. M., Lord, C. I., Riesselman, M. H., Maaty, W. S. A., Bothner, B. B., Angel, T. E., Dratz, E. A., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607354200 · Cited by 27 · see citing works
Self-citationCharacterization of peptide diffusion into electropermeabilized neutrophils
DeLeo, F. R., Jutila, M. A., & Quinn, M. T. (1996) · Journal of Immunological Methods · doi:10.1016/0022-1759(96)00144-5 · Cited by 27 · see citing works
Self-citationOlavarría, V. H., Gallardo, L., Figueroa, J. E., & Mulero, V. (2010) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2010.07.002 · Cited by 25 · see citing works
Kaneda, M., Sakuraba, H., Ohtake, A., Nishida, A., Kiryu, C., & Kakinuma, K. (1999) · Blood · doi:10.1182/blood.v93.6.2098.406k09_2098_2104 · Cited by 25 · see citing works
Towards specific NADPH oxidase inhibition by small synthetic peptides
Benna, J. E., Dang, P. M., & Périanin, A. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1008-3 · Cited by 24 · see citing works
Identification of mutations in seven Chinese patients with X-linked chronic granulomatous disease
Hui, Y., Chan, S. Y., & Lau, Y. (1996) · Blood · doi:10.1182/blood.v88.10.4021.bloodjournal88104021 · Cited by 23 · see citing works
Dahan, I. M., Molshanski-Mor, S., & Pick, E. (2011) · Journal of Leukocyte Biology · doi:10.1189/jlb.1011507 · Cited by 22 · see citing works
Dahan, I. M., Smith, S. M. E., & Pick, E. (2015) · Journal of Leukocyte Biology · doi:10.1189/jlb.4a0315-107r · Cited by 22 · see citing works
Demangel, C., Maroun, R. C., Rouyre, S., Bon, C., Mazié, J. C., & Choumet, V. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01244.x · Cited by 22 · see citing works
Brandes, R. P. (2003) · Circulation Research · doi:10.1161/01.res.0000066880.62205.b0 · Cited by 22 · see citing works
- Authors
- DeLeo, F. R., Yu, L., Burritt, J. B., Loetterle, L. R., Bond, C. W., Jesaitis, A. J., & Quinn, M. T.
- Affiliations
- Montana State University (US)
- University of Washington (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1995-07-18
- Volume
- 92
- Issue
- 15
- Pages
- 7110-7114
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC41481
- OpenAlex
- W2092234562
- Cited by
- 150
- References
- 40
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 2 · 2023: 4 · 2021: 2 · 2020: 3 · 2019: 4 · 2018: 2 · 2017: 2 · 2016: 4 · 2015: 5 · 2014: 3 · 2013: 7 · 2012: 7
- FWCI
- 3.45
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation
- University of Missouri
- National Institutes of Health (5r29ar040929-05)
- National Institute of Allergy and Infectious Diseases (R01AI026711, AI26711)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR40929)
- Office of Experimental Program to Stimulate Competitive Research
- 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
- p47phox, NADPH oxidase, gp91phox, p22phox, protein-protein interaction, binding sites, phage display, Src homology 3 domain, NADPH oxidase inhibitors, phagocytes
- MeSH terms
- NADPH Oxidase 2, Binding Sites, Cytochrome b Group, Humans, Membrane Glycoproteins, NADH, NADPH Oxidoreductases, NADPH Dehydrogenase, Neutrophils, Peptide Fragments, Phosphoproteins, Protein Binding, Gene Library, NADPH Oxidases, Membrane Transport Proteins
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 ›
Are you an author, or do you see a problem with this page? Request a review