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ROS production in phagocytes: why, when, and where?
Abstract
In the phagocytosis field, ROS production by the phagocyte NOX has been associated with pathogen killing for the last 50 years. Since the discovery of nonphagocyte NOX, numerous other roles for ROS production have been identified. Oxidative stress and ROS-mediated signaling have received much attention in recent years. Much lower concentrations of ROS may be required for signaling compared with microbial killing. Based on the discoveries in nonphagocytic cells, it became logical to look for ROS functions distinct from pathogen killing, even in phagocytes. ROS are now linked to various forms of cell death, to chemotaxis, and to numerous modifications of cellular processes, including the NOX itself. ROS functions are clearly concentration-dependent over a wide range of concentrations. How much is required for which function? Which species are required for how much time? Is ROS signaling only a side effect of bactericidal ROS production? One major obstacle to answer these questions is the difficulty of reliable quantitative ROS detection. Signal transduction often takes place on a subcellular scale over periods of seconds or minutes, so the detection methods need to provide appropriate time and space resolution. We present examples of local ROS production, decreased degradation, signaling events, and potentially ROS-sensitive functions. We attempt to illustrate the current limitations for quantitative spatiotemporal ROS detection and point out directions for ongoing development. Probes for localized ROS detection and for combined detection of ROS, together with protein localization or other cellular parameters, are constantly improved.
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“Alongside the ability of O2•− to induce lysis of bacteria in the phagosome through oxidative damage to bacterial biomolecules, defence against pathogens is also triggered by various non-oxidative means, such as autophagy, receptor signalling, extracellular trap formation and instruction of lymphocyte responses [171].”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [171]
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Cites
1 retracted
RETRACTED: Activation and silencing of matrix metalloproteinases
Fu, X., Parks, W. C., & Heinecke, J. W. (2007) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2007.06.005 · Cited by 87
RetractedFree Radicals in the Physiological Control of Cell Function
Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855
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
Novel cell death program leads to neutrophil extracellular traps
Fuchs, T. A., Abed, U., Goosmann, C., Hurwitz, R., Schulze, I., Wahn, V., Weinrauch, Y., Brinkmann, V., & Zychlinsky, A. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200606027 · Cited by 3,197
A Common Mechanism of Cellular Death Induced by Bactericidal Antibiotics
Kohanski, M. A., Dwyer, D. J., Hayete, B., Lawrence, C. A., & Collins, J. J. (2007) · Cell · doi:10.1016/j.cell.2007.06.049 · Cited by 2,982
Myeloperoxidase: friend and foe
Klebanoff, S. J. (2005) · Journal of Leukocyte Biology · doi:10.1189/jlb.1204697 · Cited by 2,282
Neutrophil elastase and myeloperoxidase regulate the formation of neutrophil extracellular traps
Papayannopoulos, V., Metzler, K. D., Hakkim, A., & Zychlinsky, A. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201006052 · Cited by 2,103
Fluorescence probes used for detection of reactive oxygen species
Gomes, A., Fernandes, E., & Lima, J. L. F. C. (2005) · Journal of Biochemical and Biophysical Methods · doi:10.1016/j.jbbm.2005.10.003 · Cited by 1,844
Segal, A. W. (2005) · Annual Review of Immunology · doi:10.1146/annurev.immunol.23.021704.115653 · Cited by 1,783
Zhou, M., Diwu, Z. J., Panchuk-Voloshina, N., & Haugland, R. P. (1997) · Analytical Biochemistry · doi:10.1006/abio.1997.2391 · Cited by 1,400
Superoxide Anion Radical (O·̄2), Superoxide Dismutases, and Related Matters
Fridovich, I. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.30.18515 · Cited by 1,337
Setsukinai, K.-I., Urano, Y., Kakinuma, K., Majima, H. J., & Nagano, T. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209264200 · Cited by 1,301
Genetically encoded fluorescent indicator for intracellular hydrogen peroxide
Belousov, V. V., Fradkov, A. F., Lukyanov, K. A., Staroverov, D. B., Shakhbazov, K., Terskikh, A. V., & Lukyanov, S. (2006) · Nature Methods · doi:10.1038/nmeth866 · Cited by 1,286
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
Nitric oxide and superoxide in inflammation and immune regulation.
Guzik, T. J., Korbut, R., & Adamek-Guzik, T. (2003) · PubMed · Cited by 1,096
Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes
Hamanaka, R. B., & Chandel, N. S. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.04.002 · Cited by 1,011
Sublethal Antibiotic Treatment Leads to Multidrug Resistance via Radical-Induced Mutagenesis
Kohanski, M. A., DePristo, M. A., & Collins, J. J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.01.003 · Cited by 985
Borregaard, N., Heiple, J. M., Simons, E. R., & Clark, R. A. (1983) · The Journal of Cell Biology · doi:10.1083/jcb.97.1.52 · Cited by 920
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
Lippert, A. R., de Bittner, G. C. V., & Chang, C. J. (2011) · Accounts of Chemical Research · doi:10.1021/ar200126t · Cited by 809
Metzler, K. D., Fuchs, T. A., Nauseef, W. M., Reumaux, D., Roesler, J., Schulze, I., Wahn, V., Papayannopoulos, V., & Zychlinsky, A. (2010) · Blood · doi:10.1182/blood-2010-06-290171 · Cited by 802
Intravascular Neutrophil Extracellular Traps Capture Bacteria from the Bloodstream during Sepsis
McDonald, B., Urrutia, R., Yipp, B. G., Jenne, C. N., & Kubes, P. (2012) · Cell Host & Microbe · doi:10.1016/j.chom.2012.06.011 · Cited by 799
Advances in fluorescent protein technology
Shaner, N. C., Patterson, G. H., & Davidson, M. W. (2007) · Journal of Cell Science · doi:10.1242/jcs.005801 · Cited by 789
Reactive oxygen and nitrogen species as signaling molecules regulating neutrophil function
Fialkow, L., Wang, Y., & Downey, G. P. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.09.030 · Cited by 723
Superoxide flashes in single mitochondria
Wang, W., Fang, H., Groom, L., Cheng, A., Zhang, W., Liu, J., Wang, X., Li, K., Han, P., Zheng, M., et al. (2008) · Cell · doi:10.1016/j.cell.2008.06.017 · Cited by 715
Free radicals and antioxidants – quo vadis?
Halliwell, B. (2011) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2010.12.002 · Cited by 706
Redox Redux: Revisiting PTPs and the Control of Cell Signaling
Tonks, N. K. (2005) · Cell · doi:10.1016/j.cell.2005.05.016 · Cited by 702
Protein kinase C signaling and oxidative stress
Gopalakrishna, R., & Jaken, S. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00221-5 · Cited by 701 · cited 1×
“that PKC activity can be modulated by H2O2 [23].”
BackgroundMyeloperoxidase: a front-line defender against phagocytosed microorganisms
Klebanoff, S. J., Kettle, A. J., Rosen, H., Winterbourn, C. C., & Nauseef, W. M. (2012) · Journal of Leukocyte Biology · doi:10.1189/jlb.0712349 · Cited by 679
Role of peroxisomes in ros/rns-metabolism: Implications for human disease
Fransen, M., Nordgren, M., Wang, B., & Apanasets, O. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.12.001 · Cited by 644
Modeling the Reactions of Superoxide and Myeloperoxidase in the Neutrophil Phagosome
Winterbourn, C. C., Hampton, M. B., Livesey, J. H., & Kettle, A. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605898200 · Cited by 633
The Molecular Probes handbook. A guide to fluorescent probes and labeling technologies
Wiederschain, G. Y. (2011) · Biochemistry (Moscow) · doi:10.1134/s0006297911110101 · Cited by 632
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
Coxon, A., Rieu, P., Barkalow, F. J., Askari, S., Sharpe, A. H., von Andrian, U. H., Arnaout, M. A., & Mayadas, T. N. (1996) · Immunity · doi:10.1016/s1074-7613(00)80278-2 · Cited by 627
Reactive oxygen and mechanisms of inflammatory liver injury: Present concepts
Jaeschke, H. (2011) · Journal of Gastroenterology and Hepatology · doi:10.1111/j.1440-1746.2010.06592.x · Cited by 599
Activation and assembly of the NADPH oxidase: a structural perspective
Groemping, Y., & Rittinger, K. (2005) · Biochemical Journal · doi:10.1042/bj20041835 · Cited by 592
An Endonuclease Allows Streptococcus pneumoniae to Escape from Neutrophil Extracellular Traps
Beiter, K., Wartha, F., Albiger, B., Normark, S. J., Zychlinsky, A., & Henriques‐Normark, B. (2006) · Current Biology · doi:10.1016/j.cub.2006.01.056 · Cited by 588
Inducible nitric oxide synthase in human diseases
Kröncke, K.-D., Fehsel, K., & Kolb‐Bachofen, V. (1998) · Clinical & Experimental Immunology · doi:10.1046/j.1365-2249.1998.00648.x · Cited by 585
Koide, Y., Urano, Y., Hanaoka, K., Terai, T., & Nagano, T. (2011) · Journal of the American Chemical Society · doi:10.1021/ja111470n · Cited by 576
Chen, X., Zhong, Z., Xu, Z., Chen, L., & Wang, Y. (2010) · Free Radical Research · doi:10.3109/10715761003709802 · Cited by 548
Fluorescent Protein-Based Redox Probes
Meyer, A. J., & Dick, T. P. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2948 · Cited by 542
Dickinson, B. C., Huynh, C., & Chang, C. J. (2010) · Journal of the American Chemical Society · doi:10.1021/ja1014103 · Cited by 520
Regulation of Nox and Duox enzymatic activity and expression
Lambeth, J. D., Kawahara, T., & Diebold, B. A. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.03.028 · Cited by 510
Shiloh, M. U., MacMicking, J. D., Nicholson, S., Brause, J. E., Potter, S. H., Marino, M., Fang, F. C., Dinauer, M. C., & Nathan, C. (1999) · Immunity · doi:10.1016/s1074-7613(00)80004-7 · Cited by 507
The molecular probes handbook : a guide to fluorescent probes and labeling technologies
Spence, M. T. Z., & Johnson, I. D. (2010) · Medical Entomology and Zoology · Cited by 501
Free radicals and phagocytic cells
Rosen, G. M., Pou, S., Ramos, C. L., Cohen, M. S., & Britigan, B. E. (1995) · The FASEB Journal · doi:10.1096/fasebj.9.2.7540156 · Cited by 478
Kenmoku, S., Urano, Y., Kojima, H., & Nagano, T. (2007) · Journal of the American Chemical Society · doi:10.1021/ja068740g · Cited by 462
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
Figueira, T. R., de Barros, M. H., Camargo, A. A., Castilho, R. F., Ferreira, J. C. B., Kowaltowski, A. J., Sluse, F. E., de Souza-Pinto, N. C., & Vercesi, A. E. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4729 · Cited by 429
Electrochemical Monitoring of Single Cell Secretion: Vesicular Exocytosis and Oxidative Stress
Amatore, C. A., Arbault, S., Guille‐Collignon, M., & Lemaître, F. (2008) · Chemical Reviews · doi:10.1021/cr068062g · Cited by 412
de Bittner, G. C. V., Goun, E. A., Bertozzi, C. R., & Chang, C. J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1012864107 · Cited by 407
THE EXTRA RESPIRATION OF PHAGOCYTOSIS
Baldridge, C. W., & Gerard, R. W. (1932) · American Journal of Physiology-Legacy Content · doi:10.1152/ajplegacy.1932.103.1.235 · Cited by 406
Neutrophils in innate host defense against Staphylococcus aureus infections
Rigby, K. M., & DeLeo, F. R. (2012) · Seminars in Immunopathology · doi:10.1007/s00281-011-0295-3 · Cited by 400
A FRET-Based Approach to Ratiometric Fluorescence Detection of Hydrogen Peroxide
Albers, A. E., Okreglak, V., & Chang, C. J. (2006) · Journal of the American Chemical Society · doi:10.1021/ja063308k · Cited by 375
Sikora, A., Zielonka, J., Lopez, M., Joseph, J., & Kalyanaraman, B. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.08.006 · Cited by 361
Phagosome dynamics during phagocytosis by neutrophils
Nordenfelt, P., & Tapper, H. (2011) · Journal of Leukocyte Biology · doi:10.1189/jlb.0810457 · Cited by 350
Parker, H. A., Albrett, A. M., Kettle, A. J., & Winterbourn, C. C. (2011) · Journal of Leukocyte Biology · doi:10.1189/jlb.0711387 · Cited by 349
BABIOR, B. M., Curnutte, J. T., & McMurrich, B. J. (1976) · Journal of Clinical Investigation · doi:10.1172/jci108553 · Cited by 348
Fossati, G., MOULDING, D. A., Spiller, D. G., Moots, R. J., White, M., & Edwards, S. W. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.170.4.1964 · Cited by 348
Involvement of Caspases in Neutrophil Apoptosis: Regulation by Reactive Oxygen Species
Fadeel, B., Åhlin, A., Henter, J., Orrenius, S., & Hampton, M. B. (1998) · Blood · doi:10.1182/blood.v92.12.4808 · Cited by 344
Park, S., You, X., & Imlay, J. A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502051102 · Cited by 342
Kasahara, Y., Iwai, K., Yachie, A., Ohta, K., Konno, A., Seki, H., Miyawaki, T., & Taniguchi, N. (1997) · Blood · doi:10.1182/blood.v89.5.1748 · Cited by 341
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
Srikun, D., Albers, A. E., Nam, C. I., Iavarone, A. T., & Chang, C. J. (2010) · Journal of the American Chemical Society · doi:10.1021/ja100117u · Cited by 311
Evans, T. J., Buttery, L. D. K., Carpenter, A., Springall, D. R., Polak, J. M., & Cohen, J. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.18.9553 · Cited by 311
Neutrophils undergo apoptosis following ingestion of Escherichia coli
Watson, R. W. G., Redmond, H. P., Wang, J. H., Condron, C. M., & Bouchier‐Hayes, D. (1996) · The Journal of Immunology · doi:10.4049/jimmunol.156.10.3986 · Cited by 303
Brown, G. C., & Borutaitė, V. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.02.001 · Cited by 295
Human neutrophil granules and secretory vesicles
Borregaard, N., Lollike, K., Kjeldsen, L., Sengeløv, H., Bastholm, L., Nielsen, M. H., & Bainton, D. F. (1993) · European Journal Of Haematology · doi:10.1111/j.1600-0609.1993.tb00629.x · Cited by 295
Condliffe, A. M. (2005) · Blood · doi:10.1182/blood-2005-03-0944 · Cited by 295
Bright cyan fluorescent protein variants identified by fluorescence lifetime screening
Goedhart, J., van Weeren, L., Hink, M. A., Vischer, N. O. E., Jalink, K., & Gadella, T. W. J. (2010) · Nature Methods · doi:10.1038/nmeth.1415 · Cited by 284
Conus, S., Perozzo, R., Reinheckel, T., Peters, C., Scapozza, L., Yousefi, S., & Simon, H. (2008) · The Journal of Experimental Medicine · doi:10.1084/jem.20072152 · Cited by 277
Regulation and termination of NADPH oxidase activity
DeCoursey, T. E., & Ligeti, E. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5177-1 · Cited by 268
Shepherd, J., Hilderbrand, S. A., Waterman, P. R., Heinecke, J. W., Weissleder, R., & Libby, P. (2007) · Chemistry & Biology · doi:10.1016/j.chembiol.2007.10.005 · Cited by 265
Consequences of Total and Subtotal Myeloperoxidase Deficiency: Risk or Benefit ?
Kutter, D., Devaquet, P., Vanderstocken, G., Paulus, J., Marchal, V., & Gothot, A. (2000) · Acta Haematologica · doi:10.1159/000041062 · Cited by 250
The role of calcium signaling in phagocytosis
Nunes, P., & Demaurex, N. (2010) · Journal of Leukocyte Biology · doi:10.1189/jlb.0110028 · Cited by 248
agr-Dependent Interactions of Staphylococcus aureus USA300 with Human Polymorphonuclear Neutrophils
Pang, Y., Schwartz, J., Thoendel, M., Ackermann, L. W., Horswill, A. R., & Nauseef, W. M. (2010) · Journal of Innate Immunity · doi:10.1159/000319855 · Cited by 247
Chen, X., Lee, K.-A., Ha, E.-M., Lee, K. M., Seo, Y. Y., Choi, H. K., Kim, H. N., Kim, M. J., Cho, C.-S., Lee, S. Y., et al. (2011) · Chemical Communications · doi:10.1039/c1cc10589b · Cited by 246
Involvement of NADPH Oxidase Isoforms and Src Family Kinases in CD95-dependent Hepatocyte Apoptosis
Reinehr, R., Becker, S., Eberle, A., Grether‐Beck, S., & Häussinger, D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414361200 · Cited by 246
Reactive oxygen species in phagocytic leukocytes
Robinson, J. M. (2008) · Histochemistry and Cell Biology · doi:10.1007/s00418-008-0461-4 · Cited by 231
Nanoelectrodes for determination of reactive oxygen and nitrogen species inside murine macrophages
Wang, Y., Noël, J., Velmurugan, J., Nogala, W., Mirkin, M. V., Lu, C., Guille‐Collignon, M., Lemaître, F., & Amatore, C. A. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1201552109 · Cited by 230
Lundqvist, H., & Dahlgren, C. (1996) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(95)02189-2 · Cited by 221
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
Blomgran, R., Zheng, L., & Stendahl, O. I. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.0506359 · Cited by 212
Intracellular generation of superoxide by the phagocyte NADPH oxidase: How, where, and what for?
Bylund, J., Brown, K. L., Movitz, C., Dahlgren, C., & Karlsson, A. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.09.016 · Cited by 201
Chapman, A., Hampton, M. B., Senthilmohan, R., Winterbourn, C. C., & Kettle, A. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m106134200 · Cited by 200
NOX2 Complex–Derived ROS as Immune Regulators
Sareila, O., Kelkka, T., Pizzolla, A., Hultqvist, M. H., & Holmdahl, R. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3635 · Cited by 200
A design of fluorescent probes for superoxide based on a nonredox mechanism
Maeda, H., Yamamoto, K., Nomura, Y., Kohno, I., Hafsi, L., Ueda, N., Yoshida, S., Fukuda, M., Fukuyasu, Y., Yamauchi, Y., et al. (2005) · Journal of the American Chemical Society · doi:10.1021/ja047018k · Cited by 196
Cuéllar-Cruz, M., Briones-Martin-del-Campo, M., Cañas-Villamar, I., Montalvo-Arredondo, J., Riego-Ruiz, L., Castaño, I., & De Las Peñas, A. (2008) · Eukaryotic Cell · doi:10.1128/ec.00011-08 · Cited by 190
The macrophage marches on its phagosome: dynamic assays of phagosome function
Russell, D. G., VanderVen, B. C., Glennie, S. J., Mwandumba, H. C., & Heyderman, R. S. (2009) · Nature reviews. Immunology · doi:10.1038/nri2591 · Cited by 187
Green fluorescent protein based pH indicators for in vivo use: a review
Bizzarri, R., Serresi, M., Luin, S., & Beltram, F. (2008) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-008-2515-9 · Cited by 181
A reversible near-infrared fluorescence probe for reactive oxygen species based on Te–rhodamine
Koide, Y., Kawaguchi, M., Urano, Y., Hanaoka, K., Komatsu, T., Abo, M., Terai, T., & Nagano, T. (2012) · Chemical Communications · doi:10.1039/c2cc18011a · Cited by 177
Theory, Instrumentation, and Applications of Electron Paramagnetic Resonance Oximetry
Ahmad, R., & Kuppusamy, P. (2010) · Chemical Reviews · doi:10.1021/cr900396q · Cited by 174
Kielland, A., Blom, T., Nandakumar, K. S., Holmdahl, R., Blomhoff, R., & Carlsen, H. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.06.013 · Cited by 173
Lee, C. F., Qiao, M., Schröder, K., Zhao, Q. D., & Asmis, R. (2010) · Circulation Research · doi:10.1161/circresaha.109.215392 · Cited by 171
Nitrosative and oxidative stress responses in fungal pathogenicity
Brown, A. J. P., Haynes, K., & Quinn, J. (2009) · Current Opinion in Microbiology · doi:10.1016/j.mib.2009.06.007 · Cited by 167
Genetics and immunopathology of chronic granulomatous disease
Stasia, M. J., & Li, X. J. (2008) · Seminars in Immunopathology · doi:10.1007/s00281-008-0121-8 · Cited by 159
Exploring real-time in vivo redox biology of developing and aging Caenorhabditis elegans
Back, P., Vos, W. H. D., Depuydt, G., Matthijssens, F., Vanfleteren, J. R., & Braeckman, B. P. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.11.037 · Cited by 155
Detection of reactive oxygen species derived from the family of NOX NADPH oxidases
Maghzal, G. J., Krause, K., Stocker, R., & Jaquet, V. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.09.002 · Cited by 154
Venton, B. J., Michael, D. J., & Wightman, R. M. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01527.x · Cited by 152
Bioimaging Probes for Reactive Oxygen Species and Reactive Nitrogen Species
Nagano, T. (2009) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.r09-66 · Cited by 143
Palazzolo-Ballance, A. M., Reniere, M. L., Braughton, K. R., Sturdevant, D. E., Otto, M., Kreiswirth, B. N., Skaar, E. P., & DeLeo, F. R. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.1.500 · Cited by 142
Arroyo, A., Modrianský, M., Serinkan, F. B., Bello, R. I., Matsura, T., Jiang, J., Tyurin, V. A., Tyurina, Y. Y., Fadeel, B., & Kagan, V. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204513200 · Cited by 138
Schwarzländer, M., Logan, D. C., Fricker, M. D., & Sweetlove, L. J. (2011) · Biochemical Journal · doi:10.1042/bj20110883 · Cited by 138
PtdIns3P binding to the PX domain of p40phox is a physiological signal in NADPH oxidase activation
Ellson, C. D., Davidson, K., Anderson, K. E., Stephens, L., & Hawkins, P. T. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601346 · Cited by 135
Myeloperoxidase Inactivates TIMP-1 by Oxidizing Its N-terminal Cysteine Residue
Wang, Y., Rosen, H., Madtes, D. K., Shao, B., Martin, T. R., Heinecke, J. W., & Fu, X. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704894200 · Cited by 132
Singlet oxygen is essential for neutrophil extracellular trap formation
Nishinaka‐Arai, Y., Arai, T., Adachi, S., Takaori‐Kondo, A., & Yamashita, K. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.08.052 · Cited by 124
Park, D., Baek, K., Kim, J.-R., Lee, J. J., Ryu, S.-H., Chin, B.-R., & Baek, S. (2009) · Experimental & Molecular Medicine · doi:10.3858/emm.2009.41.3.020 · Cited by 121
Jirapongsananuruk, O., Malech, H. L., Kuhns, D. B., Niemela, J. E., Brown, M. R., Anderson-Cohen, M., & Fleisher, T. A. (2003) · Journal of Allergy and Clinical Immunology · doi:10.1067/mai.2003.58 · Cited by 112
Xu, K., Liu, X., Tang, B., Yang, G., Yang, Y., & An, L. (2007) · Chemistry – A European Journal · doi:10.1002/chem.200600497 · Cited by 105
Casanova, D., Bouzigues, C., Nguyen, T., Ramodiharilafy, R. O., Bouzhir-Sima, L., Gacoin, T., Boilot, J., Tharaux, P., & Alexandrou, A. (2009) · Nature Nanotechnology · doi:10.1038/nnano.2009.200 · Cited by 105
Zhang, Z., Zheng, Y. Q., Hang, W., Yan, X., & Zhao, Y. (2011) · Talanta · doi:10.1016/j.talanta.2011.04.078 · Cited by 102
Steinckwich, N., Schenten, V., Melchior, C., Bréchard, S., & Tschirhart, E. J. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1001338 · Cited by 102
Neutrophil dysfunction in a family with a SAPHO syndrome–like phenotype
Ferguson, P. J., Lokuta, M. A., El‐Shanti, H., Muhle, L., Bing, X., & Anna Huttenlocher, A. (2008) · Arthritis & Rheumatism · doi:10.1002/art.23942 · Cited by 100
Nanoencapsulation Method for High Selectivity Sensing of Hydrogen Peroxide inside Live Cells
Kim, G., Lee, Y.-E. K., Xu, H., Philbert, M. A., & Kopelman, R. (2010) · Analytical Chemistry · doi:10.1021/ac9024544 · Cited by 97
Ryan, T. C., Weil, G. J., Newburger, P. E., Haugland, R. P., & Simons, E. R. (1990) · Journal of Immunological Methods · doi:10.1016/0022-1759(90)90052-w · Cited by 95
A novel TNFR1-triggered apoptosis pathway mediated by class IA PI3Ks in neutrophils
Geering, B., Gurzeler, U., Federzoni, E. A., Kaufmann, T., & Simon, H. (2011) · Blood · doi:10.1182/blood-2010-11-322206 · Cited by 93
Regulation of Candida glabrata oxidative stress resistance is adapted to host environment
Roetzer, A., Klopf, E., Gratz, N., Marcet-Houben, M., Hiller, E., Rupp, S., Gabaldón, T., Kovarik, P., & Schüller, C. (2011) · FEBS Letters · doi:10.1016/j.febslet.2010.12.006 · Cited by 90
Amatore, C. A., Arbault, S., Chen, Y., Crozatier, C., Lemaître, F., & Verchier, Y. (2006) · Angewandte Chemie International Edition · doi:10.1002/anie.200600510 · Cited by 90
Yamada, K., Kuppusamy, P., English, S. J., Yoo, J., Irie, A., Subramanian, S., Mitchell, J. B., & Krishna, M. C. (2002) · Acta Radiologica · doi:10.1034/j.1600-0455.2002.430418.x · Cited by 87
Mitochondrial compartmentalization of redox processes
Cardoso, A. R., Chausse, B., da Cunha, F. M., Luévano‐Martínez, L. A., Marazzi, T. B. M., Pessoa, P. S., Queliconi, B. B., & Kowaltowski, A. J. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.03.008 · Cited by 86
Schwartz, J., Leidal, K. G., Femling, J., Weiss, J. P., & Nauseef, W. M. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0804110 · Cited by 86
Casbon, A.-J., Allen, L. H., Dunn, K. W., & Dinauer, M. C. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0803476 · Cited by 85
Maeda, H., Yamamoto, K., Kohno, I., Hafsi, L., Itoh, N., Nakagawa, S., Kanagawa, N., Suzuki, K., & Uno, T. (2007) · Chemistry – A European Journal · doi:10.1002/chem.200600522 · Cited by 85
Amatore, C. A., Arbault, S., Bruce, D., de Oliveira, P., Erard, M., & Vuillaume, M. (2000) · Faraday Discussions · doi:10.1039/b001448f · Cited by 84
Self-citationvan Pelt, L. J., van Zwieten, R., Weening, R. S., Roos, D., Verhoeven, A. J., & Bolscher, B. G. J. M. (1996) · Journal of Immunological Methods · doi:10.1016/0022-1759(96)00024-5 · Cited by 83
Meunier, A., Jouannot, O., Fulcrand, R., Fanget, I., Bretou, M., Karatekin, E., Arbault, S., Guille‐Collignon, M., Darchen, F., Lemaître, F., et al. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201101148 · Cited by 80
[12] In Vivo visualization of oxygen radical-dependent photoemission
Tsuchiya, M., Suematsu, M., & Suzuki, H. (1994) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(94)33015-8 · Cited by 78
Neutrophil direction sensing and superoxide production linked by the GTPase-activating protein GIT2
Mazaki, Y., Hashimoto, S., Tsujimura, T., Morishige, M., Hashimoto, A., Aritake, K., Yamada, A., Nam, J., Kiyonari, H., Nakao, K., et al. (2006) · Nature Immunology · doi:10.1038/ni1349 · Cited by 76
Foyouzi-Youssefi, R., PETERSSON, F., Lew, D. P., Krause, K., & Nüße, O. (1997) · Biochemical Journal · doi:10.1042/bj3220709 · Cited by 75
Self-citationRac regulates PtdInsP3 signaling and the chemotactic compass through a redox-mediated feedback loop
Kuiper, J. W., Sun, C., Magalhães, M. A. O., & Glogauer, M. (2011) · Blood · doi:10.1182/blood-2010-09-310383 · Cited by 72
Xu, K., Liu, X., & Tang, B. (2007) · ChemBioChem · doi:10.1002/cbic.200600392 · Cited by 71
Minimum set of mutations needed to optimize cyan fluorescent proteins for live cell imaging
Erard, M., Fredj, A., Pasquier, H., Beltolngar, D.-B., Bousmah, Y., Derrien, V., Vincent, P., & Mérola, F. (2012) · Molecular BioSystems · doi:10.1039/c2mb25303h · Cited by 69
Self-citationDewitt, S., Laffafian, I., & Hallett, M. B. (2003) · Journal of Cell Science · doi:10.1242/jcs.00499 · Cited by 67
Boyle, K. B., Gyori, D., Sindrilaru, A., Scharffetter-Kochanek, K., Taylor, P., Mócsai, A., Stephens, L., & Hawkins, P. (2011) · Journal of Immunology · doi:10.4049/jimmunol.1002268 · Cited by 66
NADPH oxidase is functionally assembled in specific granules during activation of human neutrophils
Vaissière, C., Cabec, V. L., & Maridonneau‐Parini, I. (1999) · Journal of Leukocyte Biology · doi:10.1002/jlb.65.5.629 · Cited by 63
SHIP-1 Increases Early Oxidative Burst and Regulates Phagosome Maturation in Macrophages
Kamen, L. A., Levinsohn, J. L., Cadwallader, A. M., Tridandapani, S., & Swanson, J. A. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.11.7497 · Cited by 63
Fungi sensing environmental stress
Alonso‐Monge, R., Román, E., Arana, D. M., Plá, J., & Nombela, C. (2009) · Clinical Microbiology and Infection · doi:10.1111/j.1469-0691.2008.02690.x · Cited by 62
Anderson, K. E., Chessa, T. A. M., Davidson, K., Henderson, R. B., Walker, S. A., Tolmachova, T., Grys, K., Rausch, O., Seabra, M. C., Tybulewicz, V. L. J., et al. (2010) · Blood · doi:10.1182/blood-2010-03-275602 · Cited by 62
Li, X. J., Marchal, C. C., Stull, N. D., Stahelin, R. V., & Dinauer, M. C. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.164475 · Cited by 59
A critical evaluation of cpYFP as a probe for superoxide
Müller, F. L. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.09.019 · Cited by 55
Allen, L. H., & McCaffrey, R. L. (2007) · Immunological Reviews · doi:10.1111/j.1600-065x.2007.00544.x · Cited by 55
Wang, L., Taneja, R., Razavi, H. M., Law, C., Gillis, C., & Mehta, S. (2012) · Shock · doi:10.1097/shk.0b013e31824dcb5a · Cited by 54
Biochemistry of the Phagosome: The Challenge to Study a Transient Organelle
Nüße, O. (2011) · The Scientific World JOURNAL · doi:10.1100/2011/741046 · Cited by 51
Self-citationPalazzolo, A. M., Suquet, C., Konkel, M. E., & Hurst, J. K. (2005) · Biochemistry · doi:10.1021/bi047342s · Cited by 48
Ohsaki, Y., O'Connor, P. M., Mori, T., Ryan, R. P., Dickinson, B. C., Chang, C. J., Lu, Y., Ito, S., & Cowley, A. W. (2011) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00469.2011 · Cited by 47
Lamb, F. S., Hook, J. S., Hilkin, B. M., Huber, J. N., Volk, A. P. D., & Moreland, J. G. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.306530 · Cited by 46
Kinetic analysis of phagosomal production of reactive oxygen species
Tlili, A., Dupré‐Crochet, S., Erard, M., & Nüße, O. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.11.024 · Cited by 46
Self-citationDu, C., Calderone, R., Richert, J. R., & Li, D. (2005) · Infection and Immunity · doi:10.1128/iai.73.2.865-871.2005 · Cited by 45
The Oxidation State of Phospholipids Controls the Oxidative Burst in Neutrophil Granulocytes
Blüml, S., Rosc, B., Lőrincz, Á. M., Seyerl, M., Kirchberger, S., Oskolkova, O., Bochkov, V. N., Majdic, O., Ligeti, E., & Stöckl, J. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.6.4347 · Cited by 41
Oxygen detection in biological systems
Renger, G., & Hanssum, B. (2009) · Photosynthesis Research · doi:10.1007/s11120-009-9434-2 · Cited by 41
Fujii, H. G., Sato‐Akaba, H., Emoto, M. C., Itoh, K., Ishihara, Y., & Hirata, H. (2012) · Magnetic Resonance Imaging · doi:10.1016/j.mri.2012.06.021 · Cited by 40
Response to “A critical evaluation of cpYFP as a probe for superoxide”
Huang, Z., Zhang, W., Gong, G., Fang, H., Zheng, M., Wang, X., Xu, J., Dirksen, R. T., Sheu, S., Cheng, H., et al. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.08.024 · Cited by 35
Stable accumulation of p67phox at the phagosomal membrane and ROS production within the phagosome
Tlili, A., Erard, M., Faure, M.-C., Baudin, X., Piolot, T., Dupré‐Crochet, S., & Nüße, O. (2011) · Journal of Leukocyte Biology · doi:10.1189/jlb.1210701 · Cited by 34
Self-citationNanoparticle PEBBLE Sensors in Live Cells
Lee, Y.-E. K., & Kopelman, R. (2012) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-391857-4.00021-5 · Cited by 33
Ostuni, M. A., Gelinotte, M., Bizouarn, T., Baciou, L., & Houée-Levin, C. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.06.021 · Cited by 32
Bézière, N., Frapart, Y., Rockenbauer, A., Boucher, J., Mansuy, D., & Peyrot, F. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.04.035 · Cited by 25
Fredj, A., Pasquier, H., Demachy, I., Jonasson, G., Levy, B. C., Derrien, V., Bousmah, Y., Manoussaris, G., Wien, F., Ridard, J., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0049149 · Cited by 25
Self-citationDetection of Peroxidase/H2O2-Mediated Oxidation with Enhanced Yellow Fluorescent Protein
Tsourkas, A., Newton, G. A., Perez, J. M., Basilion, J. P., & Weissleder, R. (2005) · Analytical Chemistry · doi:10.1021/ac0480747 · Cited by 22
Bernardo, J., Long, H. J., & Simons, E. R. (2009) · Cytometry Part A · doi:10.1002/cyto.a.20827 · Cited by 22
Oxidative modification of ferritin induced by hydrogen peroxide
Yoon, J., An, S. H., Kyeong, I.-G., Lee, M.-S., Kwon, S.-C., & Kang, J. H. (2011) · BMB Reports · doi:10.5483/bmbrep.2011.44.3.165 · Cited by 22
Álvarez, L., Houée‐Levin, C., Mérola, F., Bizouarn, T., Pasquier, H., Baciou, L., Rusconi, F., & Erard, M. (2009) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.2009.00617.x · Cited by 21
Self-citationStress Response in Candida Glabrata : Pieces of a Fragmented Picture
Jandric, Z., & Schüller, C. (2011) · Future Microbiology · doi:10.2217/fmb.11.131 · Cited by 19
amada, K.-I. Y., uppusamy, P. K., nglish, S. E., oo, J. Y., rie, A. I., ubramanian, S. S., itchell, J. B. M., & rishna, M. C. K. (2009) · Cited by 14
Mass Spectrometry-Based Structural Dissection of Fluorescent Proteins
Álvarez, L., Mérola, F., Erard, M., & Rusconi, F. (2009) · Biochemistry · doi:10.1021/bi900327f · Cited by 8
Self-citationKing-Smith (1997) · doi:10.1002/(sici)1097-0169(1997)38:3
Flagged first, then by citations
Research works printed but not linked: 2
- Figueira, 2013, Antioxid. Redox Signal.
- Amatore, 2000, Faraday Discuss.
Cited by
Sorted by citations
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Role of advanced glycation end products in cellular signaling
Ott, C., Jacobs, K., Haucke, E., Navarrete Santos, A., Grune, T., & Simm, A. (2014) · Redox Biology · doi:10.1016/j.redox.2013.12.016 · Cited by 1,150
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Blaser, H., Dostert, C., Mak, T. W., & Brenner, D. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.12.002 · Cited by 1,008
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Metadata
- Authors
- Dupré-Crochet, S., Erard, M., & Nüβe, O.
- Affiliations
- University Paris-Sud , Orsay, France
- Université Paris-Sud (FR)
- Corresponding author
- Nüβe, Oliver
- ORCID
- Erard, Marie
- Venue
- Journal of Leukocyte Biology
- Publisher
- Oxford University Press (OUP)
- Published
- 2013-10-01
- Volume
- 94
- Issue
- 4
- Pages
- 657-670
- ISSN
- 0741-5400 (ISSN-L)
- 1938-3673
- OpenAlex
- W2131917465
- Cited by
- 467
- References
- 166
- Citations by year
- 2026: 26 · 2025: 35 · 2024: 34 · 2023: 35 · 2022: 54 · 2021: 58 · 2020: 47 · 2019: 40 · 2018: 37 · 2017: 32 · 2016: 35 · 2015: 17 · 2014: 16 · 2013: 1
- FWCI
- 2.01
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Leukocyte Biology (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Funders
- Institut National de la Santé et de la Recherche Médicale
- Centre National de la Recherche Scientifique
- University Paris-Sud (GDR2588)
- French Ministry of 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 (medical) › Nitric Oxide and Endothelin Effects
- Keywords
- reactive oxygen species, phagocytes, NADPH oxidase, phagocytosis, oxidative stress, ROS signaling, cell death, chemotaxis, pathogen killing
- MeSH terms
- Animals, Humans, Phagocytes, Phagocytosis, Signal Transduction, Cell Death, Reactive Oxygen Species, Models, Immunological
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