The DOI matches its Crossref record; 66 of the 67 references it cites were found in a registry or an index.
Reactive Oxygen Species and Cell Signaling: Respiratory Burst in Macrophage Signaling
Abstract
Phagocytes such as neutrophils and macrophages produce reactive oxygen species (ROS) during phagocytosis or stimulation with a wide variety of agents through activation of nicotinamide adenine dinucleotide phosphate reduced (NADPH) oxidase that is assembled at the plasma membrane from resident plasma membrane and cytosolic protein components. One of the subunits of the phagocyte NADPH oxidase is now recognized as a member of a family of NADPH oxidases, or NOX, present in cells other than phagocytes. Physiologic generation of ROS has been implicated in a variety of physiologic responses from transcriptional activation to cell proliferation and apoptosis. The increase in superoxide and hydrogen peroxide (H2O2) that results from stimulation of the NADPH oxidase is transient, in part due to the presence of the antioxidant enzymes, which return their concentrations to the prestimulation steady state level. Thus, the antioxidant enzymes may function in the “turn-off” phase of signal transduction by ROS. During its transient elevation, H2O2 may act as a modifier of key signaling enzymes through reversible oxidation of critical thiols. The rapid reaction of thiols with H2O2 when in their unprotonated state would provide a potential mechanism for the specificity that is necessary for physiologic cell signaling.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
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?
In the citing paper
“The oxidative burst in phagocytes is commonly associated with bacterial killing, but in the case of alveolar macrophages, they typically produce lower levels of ROS than neutrophils and may require their activation to exhibit their bactericidal properties.”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [101]
In the citing paper
“Instead, their transient oxidative burst regulates the inflammatory response by inducing cytokine synthesis for redox signaling, resulting in an influx of activated neutrophils and macrophages [101].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [101]
Citations
Cites
Free Radicals in the Physiological Control of Cell Function
Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855
Schafer, F. Q., & Buettner, G. R. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00480-4 · Cited by 4,587
Mitogen-Activated Protein (MAP) Kinase Pathways: Regulation and Physiological Functions*
Pearson, G. W., Robinson, F. L., Gibson, T. B., Xu, B.-E., Karandikar, M. S., Berman, K. S., & Cobb, M. H. (2001) · Endocrine Reviews · doi:10.1210/edrv.22.2.0428 · Cited by 4,111
AP-1 as a regulator of cell life and death
Shaulian, E., & Karin, M. (2002) · Nature Cell Biology · doi:10.1038/ncb0502-e131 · Cited by 2,961
Reactive oxygen species in cell signaling
Thannickal, V. J., & Fanburg, B. L. (2000) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.2000.279.6.l1005 · Cited by 2,950
Babior, B. M., Kipnes, R. S., & Curnutte, J. T. (1973) · Journal of Clinical Investigation · doi:10.1172/jci107236 · Cited by 2,931
NAD(P)H Oxidase: Role in Cardiovascular Biology and Disease
Griendling, K. K., Sorescu, D., & Ushio-Fukai, M. (2000) · Circulation Research · doi:10.1161/01.res.86.5.494 · Cited by 2,886
Mammalian thioredoxin is a direct inhibitor of apoptosis signal‐regulating kinase (ASK) 1
Saitoh, M., Nishitoh, H., Fujii, M., Takeda, K., Tobiume, K., Sawada, Y., Kawabata, M., Miyazono, K., & Ichijo, H. (1998) · The EMBO Journal · doi:10.1093/emboj/17.9.2596 · Cited by 2,377
Mitogenic Signaling Mediated by Oxidants in Ras-Transformed Fibroblasts
Irani, K., Xia, Y., Zweier, J. L., Sollott, S. J., Der, C. J., Fearon, E. R., Sundaresan, M., Finkel, T., & Goldschmidt-Clermont, P. J. (1997) · Science · doi:10.1126/science.275.5306.1649 · Cited by 1,588
Redox Regulation of Fos and Jun DNA-Binding Activity in Vitro
Abate, C., Patel, L., Rauscher, F. J., & Curran, T. (1990) · Science · doi:10.1126/science.2118682 · Cited by 1,573
Flagged first, then by citations
1 of the 67 references couldn’t be matched to a known paper.
Research works printed but not linked: 4
- 2000, Mutat Res, 448, 179
- 2001, Endocr Rev, 22, 153
- 1996, J Biol Chem, 271, 4138, 10.1074/jbc.271.8.4138 · DOI
- 1996, Int J Pediatr Hematol Oncol, 3, 387
Cited by
Sorted by citations
Items 501–600 of 892
Mathews, M., Wißfeld, J., Flitsch, L. J., Shahraz, A., Semkova, V., Breitkreuz, Y., Neumann, H., & Brüstle, O. (2022) · Stem Cell Reviews and Reports · doi:10.1007/s12015-022-10433-w · Cited by 20
Biogenic selenium nanoparticles: trace element with promising anti-toxoplasma effect
Arafa, F. M., Mogahed, N. M. F. H., Eltarahony, M. M., & Diab, R. G. (2023) · Pathogens and Global Health · doi:10.1080/20477724.2023.2186079 · Cited by 21
Yang, S., Yang, Y., Yu, P., Yang, J., Jiang, X., Villar-Davila, V., Sibley, D. R., José, P. A., & Zeng, C. (2015) · Free Radical Research · doi:10.3109/10715762.2015.1006215 · Cited by 21
León-Rodríguez, L., Álvarez, A. L., Blanco-Méndez, J., Lamas, J., & Leiro, J. M. (2012) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2012.10.029 · Cited by 21
Allimuthu, D., Dash, T. K., Konkimalla, V. B., & Chakrapani, H. (2011) · MedChemComm · doi:10.1039/c1md00234a · Cited by 21
Clotrimazole enhances lysis of human erythrocytes induced by t-BHP
Lisovskaya, I. L., Shcherbachenko, I. M., Volkova, R. I., & Иноятович, А. Ф. (2009) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2009.04.003 · Cited by 21
Tepel, M. (2003) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfg201 · Cited by 21
Telomeric DNA induces p53-dependent reactive oxygen species and protects against oxidative damage
Lee, M. S., Yaar, M., Eller, M. S., Rünger, T. M., Gao, Y. J., & Gilchrest, B. A. (2009) · Journal of Dermatological Science · doi:10.1016/j.jdermsci.2009.08.008 · Cited by 21
Lim, D., Choi, H.-J., Park, S., Kim, H., Yu, G., Kim, J., & Park, W. (2020) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2020/2837853 · Cited by 21
A potential therapeutic effect of CYP2C8 overexpression on anti-TNF-α activity
LIU, W., Wang, B., Ding, H., Wang, D. W., & Zeng, H. (2014) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2014.1844 · Cited by 22
Gould, N. S., Min, E., & Day, B. J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025704 · Cited by 21
Yang, X. Z., Yuan, L., Chen, J., Xiong, C., & Ruan, J. (2013) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2013.10.061 · Cited by 20
Chung, D., Thammahong, A., Shepardson, K. M., Blosser, S. J., & Cramer, R. A. (2014) · Molecular Microbiology · doi:10.1111/mmi.12626 · Cited by 21
Differential Expression of Mycothiol Pathway Genes: Are they Affected by Antituberculosis Drugs?
Hayward, D., Wiid, I. J. F., & van Helden, P. D. (2004) · IUBMB Life · doi:10.1080/15216540410001674012 · Cited by 20
Shi, Q., Boots, A. W., Maas, L. M., Veith, C., van Kuijk, K., Haenen, G. R. M. M., Godschalk, R., & van Schooten, F. (2017) · Toxicology · doi:10.1016/j.tox.2017.02.013 · Cited by 21
Lee, Y.-H., Seo, D.-S., Lee, M. J., & Cha, H.-G. (2019) · Journal of Toxicologic Pathology · doi:10.1293/tox.2019-0049 · Cited by 20
Therapeutic Potential of Reactive Oxygen Species: State of the Art and Recent Advances
Graceffa, V. (2020) · SLAS TECHNOLOGY · doi:10.1177/2472630320977450 · Cited by 20
Srisook, K., Kim, C., & Cha, Y. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)96035-7 · Cited by 20
Liu, Y. X., Karsai, Á., Anderson, D. S., Silva, R. M., Uyeminami, D. L., Winkle, L. S. V., Pinkerton, K. E., & Liu, G.-Y. (2015) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5b07656 · Cited by 20
Fisher, A. B., & Zhang, Q. (2006) · Elsevier eBooks · doi:10.1016/b0-12-370879-6/00252-0 · Cited by 20
Spatially-resolved intracellular sensing of hydrogen peroxide in living cells
Warren, E. A. K., Netterfield, T. S., Sarkar, S., Kemp, M. L., & Payne, C. K. (2015) · Scientific Reports · doi:10.1038/srep16929 · Cited by 19
Hydrogel/nanoparticles-mediated cooperative combination of antiangiogenesis and immunotherapy
Yang, A., Sheng, S., Bai, Y., Xing, G., Yu, X., Zhu, D., Mei, L., Dong, X., & Lv, F. (2022) · Acta Biomaterialia · doi:10.1016/j.actbio.2022.09.060 · Cited by 19
Mishra, A., Lelieveld, S., Pöschl, U., & Berkemeier, T. (2023) · Environmental Science & Technology · doi:10.1021/acs.est.3c03556 · Cited by 19
Manipulations of metallothionein gene dose accelerate the response to Listeria monocytogenes
Emeny, R. T., Marusov, G., Lawrence, D. A., Pedersen-Lane, J., Yin, X., & Lynes, M. A. (2009) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2009.06.018 · Cited by 19
Significance and Traditional Medicinal Properties ofSchleichera oleosa
Meshram, N., Ojha, M., Singh, A., Alexander, A., Ajazuddin, M., & Sharma, M. K. (2015) · Asian Journal of Pharmaceutical Research · doi:10.5958/2231-5691.2015.00009.x · Cited by 19
Pieper, R., Zhang, Q., Clark, D. J., Parmar, P. P., Alami, H., Suh, M., Kuntumalla, S., Braisted, J. C., Huang, S., & Tzipori, S. R. (2013) · PLoS ONE · doi:10.1371/journal.pone.0066462 · Cited by 19
TLR2 activation induces antioxidant defence in human monocyte-macrophage cell line models
Karwaciak, I., Gorzkiewicz, M., Bartosz, G., & Pułaski, Ł. (2017) · Oncotarget · doi:10.18632/oncotarget.17342 · Cited by 19
Kim, T., Li, D., Terasaka, T., Nicholas, D., Knight, V. S., Yang, J. J., & Lawson, M. A. (2019) · Endocrinology · doi:10.1210/en.2019-00283 · Cited by 19
Guzzetti, E., Salaberry, E., Ferriol, P., Díaz, J. A., Tejada, S., Faggio, C., & Sureda, A. (2019) · Marine Environmental Research · doi:10.1016/j.marenvres.2019.104763 · Cited by 19
Effects of 2-Methyl-1,4-naphtoquinone (Menadione) on Cellular Signaling in RBL-2H3 Cells
Kawamura, F., Hirashima, N., Furuno, T., & Nakanishi, M. (2006) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.29.605 · Cited by 19
A Novel Class of Cytochrome P450 Reductase Redox Cyclers: Cationic Manganoporphyrins
Day, B. J., & Kariya, C. T. (2005) · Toxicological Sciences · doi:10.1093/toxsci/kfi108 · Cited by 19
The role of oxidative stress-related genes in idiopathic pulmonary fibrosis
Zhao, W., Bai, B., Li, H., Feng, Y., Sun, J., Yang, F., Zheng, P., & Zhang, G. (2025) · Scientific Reports · doi:10.1038/s41598-025-89770-y · Cited by 27
Fatima, N., Upadhyay, T. K., Ahmad, F., Arshad, M., Kamal, M. A., Sharma, D., & Sharma, R. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.118851 · Cited by 20
Yu, Y., Wang, J., Wang, X., Gu, P., Lei, Z., Tang, R., Wei, C., Xu, L., Wang, C., Chen, Y., et al. (2021) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0009696 · Cited by 19
Ni, J., Zhou, H., Gu, J., Liu, X., Chen, J., Yi, X., & Yang, K. (2022) · Nano Research · doi:10.1007/s12274-022-4369-4 · Cited by 18
Sukul, T., Kari, Z. A., Téllez‐Isaías, G., & Ghosh, K. (2023) · Animals · doi:10.3390/ani13162631 · Cited by 18
Marasinghe, C. K., Yoon, S., & Je, J. (2023) · Process Biochemistry · doi:10.1016/j.procbio.2023.10.004 · Cited by 18
Khodade, V. S., Allimuthu, D., & Chakrapani, H. (2012) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2012.04.009 · Cited by 18
The role of nitrite ion in phagocyte function—perspectives and puzzles
Cape, J. L., & Hurst, J. K. (2009) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2009.01.010 · Cited by 18
Abbas, K., Hardy, M., Poulhès, F., Karoui, H., Tordo, P., Ouari, O., & Peyrot, F. (2015) · Free Radical Research · doi:10.3109/10715762.2015.1045504 · Cited by 18
Tumor-Induced Immune Suppression
Gabrilovich, D. I., & Hurwitz, A. A. (2007) · Springer eBooks · doi:10.1007/978-0-387-69118-3 · Cited by 18
Role of gp91phox in hepatic macrophage programming and alcoholic liver disease
Wang, M., Frasch, S. C., Li, G., Feng, D., Gao, B., Xu, L., Ir, D., Frank, D. N., Bratton, D. L., & Ju, C. (2017) · Hepatology Communications · doi:10.1002/hep4.1078 · Cited by 19
García-Pérez, P., Losada‐Barreiro, S., Bravo‐Díaz, C., & Gallego, P. P. F. (2020) · Plants · doi:10.3390/plants9081012 · Cited by 18
Burns, T. A., Westerman, T. L., Nuovo, G. J., Watts, M. R., Pettigrew, A., Yin, C., & Belknap, J. K. (2011) · Journal of Veterinary Internal Medicine · doi:10.1111/j.1939-1676.2011.0706.x · Cited by 19
Shojaee, M., Wood, K. B., Moore, L. K., & Bashur, C. A. (2017) · Acta Biomaterialia · doi:10.1016/j.actbio.2017.10.006 · Cited by 18
Khan, N., Ghousunnissa, S., Jegadeeswaran, S. M., Thiagarajan, D., Hasnain, S. E., & Mukhopadhyay, S. (2007) · International Immunology · doi:10.1093/intimm/dxm012 · Cited by 18
Setubal, S., Pontes, A., Furtado, J., Kayano, A. M., STABELI, R., & Zuliani, J. P. (2011) · The Journal of venomous animals and toxins including tropical diseases · doi:10.1590/s1678-91992011000400010 · Cited by 18
Erukainure, O. L., Mesaik, M. A., Muhammad, A. I., Chukwuma, C. I., Manhas, N., Singh, P., Aremu, O. S., & Islam, M. S. (2016) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2016.09.002 · Cited by 17
Herrou, J., Czyż, D. M., Willett, J. W., Kim, H., Chhor, G., Babnigg, G., Kim, Y., & Crosson, S. (2016) · Journal of Bacteriology · doi:10.1128/jb.00982-15 · Cited by 16
Theodosis‐Nobelos, P., Athanasekou, C. P., & Rekka, E. A. (2017) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2017.09.054 · Cited by 17
Approaches to Investigating the Protein Interactome of PTEN
Smith, S. L., Pitt, A. R., & Spickett, C. M. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00570 · Cited by 16
Zhang, Y., Zheng, D., Li, C., Pan, P., Zeng, S., Pan, T. S., & Zhang, X. (2021) · Small Methods · doi:10.1002/smtd.202100951 · Cited by 17
Brazão, V., Colato, R. P., Santello, F. H., Duarte, A., Goulart, A., Sampaio, P. A., da Silva, C. B. P., Tirapelli, C. R., da Costa, R. M., Tostes, R. C., et al. (2022) · Experimental Gerontology · doi:10.1016/j.exger.2022.111895 · Cited by 17
Fuller-Espie, S. L., Bearoff, F. M., & Minutillo, M. A. (2011) · Pedobiologia · doi:10.1016/j.pedobi.2011.09.009 · Cited by 23
Koike, A., Minamiguchi, I., Fujimori, K., & Amano, F. (2015) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b14-00405 · Cited by 17
Méndez‐Samperio, P., Pérez, A., & Alba, L. (2010) · Archives of Medical Research · doi:10.1016/j.arcmed.2010.10.009 · Cited by 17
Protein modification as oxidative stress marker in normal and pathological human seminal plasma
Piomboni, P., Stendardi, A., Gambera, L., Tatone, C., Coppola, L., Leo, V. D., & Focarelli, R. (2012) · Redox Report · doi:10.1179/1351000212y.0000000014 · Cited by 17
Role of NO in Enhancing the Expression of HO‐1 in LPS‐Stimulated Macrophages
Srisook, K., Kim, C., & Cha, Y. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)96031-x · Cited by 17
Leite, D. F. P., Echevarria‐Lima, J., Calixto, J. Β., & Rumjanek, V. M. (2006) · Biochemical Pharmacology · doi:10.1016/j.bcp.2006.11.005 · Cited by 17
Potentiation by cigarette smoke of macrophage function against Leishmania donovani infection
Maity, P. C., Bhattacharjee, S., Majumdar, S., & Sil, A. K. (2009) · Inflammation Research · doi:10.1007/s00011-008-8151-1 · Cited by 17
Курилова, Л. С., Krutetskaya, Z. I., Lebedev, O. E., & Антонов, В. Г. (2008) · Cell and Tissue Biology · doi:10.1134/s1990519x08030139 · Cited by 17
Chen, Q., Wang, J., Li, N., Cai, H., & Lu, Y.-Y. (2025) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2025.104924 · Cited by 18
Attenuating Fibrotic Markers of Patient-Derived Dermal Fibroblasts by Thiolated Lignin Composites
Belgodere, J. A., Son, D., Jeon, B., Choe, J., Guidry, A. C., Bao, A. X., Zamin, S. A., Parikh, U. M., Balaji, S., Kim, M., et al. (2021) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.1c00427 · Cited by 16
Némethová, M., Danielisová, V., Gottlieb, M., Kravčuková, P., & Bürda, J. (2010) · PubMed · Cited by 16
Boucher, C. E., Theron, C. W., Hitzeroth, A. C., & Bragg, R. R. (2014) · Veterinary Immunology and Immunopathology · doi:10.1016/j.vetimm.2013.12.004 · Cited by 16
Mechanisms involved in apoptosis of carp leukocytes upon in vitro and in vivo immunostimulation
Kepka, M., Kemenade, B. M. L. V.-V., Homa, J., & Chadzińska, M. (2014) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2014.05.041 · Cited by 16
Nutrients and Immunometabolism: Role of Macrophage NLRP3
Larson, K., Alvine, T., Wu, D., Kalupahana, N. S., Moustaïd‐Moussa, N., & Roemmich, J. N. (2020) · Journal of Nutrition · doi:10.1093/jn/nxaa085 · Cited by 16
The Gut Microbiome, Seleno-Compounds, and Acute Myocardial Infarction
Chiu, F., Tsai, C., Huang, P., Shih, C., Tsai, M., Hwang, J., Wang, Y., Chuang, E. Y.-Y., Tsai, C., & Chang, S. (2022) · Journal of Clinical Medicine · doi:10.3390/jcm11051462 · Cited by 16
Yang, K., Zhao, S., Liu, Y. H., Hu, E., & Liu, B. X. (2009) · Chemotherapy · doi:10.1159/000235730 · Cited by 16
Virus infection drives IL-2 antibody complexes into pro-inflammatory agonists in mice
Lee, W. W. L., Teo, T., Lum, F., Andiappan, A. K., Amrun, S. N., Rénia, L., Rötzschke, O., & Ng, L. F. P. (2016) · Scientific Reports · doi:10.1038/srep37603 · Cited by 16
Lipid Peroxidation in Human Spermatozoa from Men with Genitourinary Infections
Cosci, I., Moretti, E., & Collodel, G. (2008) · Systems Biology in Reproductive Medicine · doi:10.1080/19396360801947722 · Cited by 16
Radwan, M., Miller, I., Grunert, T., Marchetti‐Deschmann, M., Vogl, C., O'Donoghue, N. M., Dunn, M. J., Kolbe, T., Allmaier, G. M., Gemeiner, M., et al. (2008) · PROTEOMICS · doi:10.1002/pmic.200800260 · Cited by 16
Zhang, Y., Liu, S.-W., Li, D., He, C., Wang, D., Wei, M., Zheng, S., & Li, J. (2023) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2023.113452 · Cited by 16
In vivo and in vitro anti-inflammatory properties of Achyrocline alata (Kunth) DC
Toffoli-Kadri, M. C., Carollo, C. A., Lourenço, L. D., Felipe, J. L., Néspoli, J. H. B., Wollf, L. G. C., Resende, G. M. S., de Lima, J. R., Franco, V. N. P., Vieira, M. D. C., et al. (2014) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2014.03.008 · Cited by 15
Silvestre, F., Danielski, L. G., Michels, M., Florentino, D., Vieira, A., Souza, L. R., Cardoso, L. C., Schraiber, R., Rezin, G., Vuolo, F., et al. (2014) · Neurotoxicity research · doi:10.1007/s12640-014-9475-y · Cited by 17
Li, L., Zhang, C., Wang, P., Wang, A., Zhou, J., Chen, G., Xu, J., Yang, Y. A., Zhao, Y., Zhang, S., et al. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.8b04292 · Cited by 16
Guenaou, I., Hmimid, F., Lahlou, F. A., Errami, A., Irahal, I. N., Fahde, S., Ouafik, L., & Bourhim, N. (2020) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2020.108899 · Cited by 15
Laaf, E., Benstoem, C., Rossaint, R., Wendt, S., Fitzner, C., Moza, A. K., Zayat, R., Hill, A., Heyland, D. K., Schomburg, L., et al. (2021) · Journal of Parenteral and Enteral Nutrition · doi:10.1002/jpen.2309 · Cited by 15
Madubunyi, I. I., & Ode, J. O. (2011) · Comparative Clinical Pathology · doi:10.1007/s00580-011-1328-y · Cited by 15
Plasma of pregnant and preeclamptic women activates monocytes in vitro
Faas, M. M., Donker, R. B., van Pampus, M. G., Huls, A. M. F., Salomons, J., de Vos, P., & Aarnoudse, J. G. (2008) · American Journal of Obstetrics and Gynecology · doi:10.1016/j.ajog.2007.12.013 · Cited by 15
Muhammad, F., Qi, W., Wang, A., Gu, J., Du, J., & Zhu, G. (2014) · Journal of Materials Chemistry B · doi:10.1039/c4tb01709a · Cited by 15
Scanning Electrochemical Microscopy Imaging during Respiratory Burst in Human Cell
Kikuchi, H., Prasad, A., Matsuoka, R., Aoyagi, S., Matsue, T., & Kasai, S. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2016.00025 · Cited by 15
Macrophage Bactericidal Assays
Aribi, M. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-7837-3_14 · Cited by 15
Polyacrylamide Hydrogels Produce Hydrogen Peroxide from Osmotic Swelling in Aqueous Media
Parameswar, A. V., Fitch, K. R., Bull, D. S., Duke, V. R., & Goodwin, A. P. (2018) · Biomacromolecules · doi:10.1021/acs.biomac.8b00743 · Cited by 15
Shen, B., Wei, K., Ding, Y., & Zhang, J. (2020) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2020.04.056 · Cited by 15
Quek, J. Y., Dabare, P. R. L., Bright, R., Postma, A., & Vasilev, K. A. (2021) · Materials Today Chemistry · doi:10.1016/j.mtchem.2021.100444 · Cited by 15
Hui, B., Xia, W., Li, J., Wang, L., Ai, J., & Geng, M. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03698.x · Cited by 15
Yang, X., Pan, Y., Zhang, J., Yang, Y., Xiong, M., Shi, F., Li, N., & Jin, Y. (2022) · Environmental Toxicology · doi:10.1002/tox.23596 · Cited by 14
Access and utilization of host-derived iron by Leishmania parasites
Goto, Y., Ito, T., Ghosh, S., & Mukherjee, B. (2023) · The Journal of Biochemistry · doi:10.1093/jb/mvad082 · Cited by 14
Regulation of dual oxidase hydrogen peroxide synthesis results in an epithelial respiratory burst
Conner, G. E. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101931 · Cited by 14
Saputri, R. K., Setiawan, B., Nugrahenny, D., Kania, N., Wahyuni, E. S., & Widodo, M. A. (2014) · PubMed Central · Cited by 14
Transient Increase in Cyclic AMP Localized to Macrophage Phagosomes
Ballinger, M. N., Welliver, T. P., Straight, S. W., Peters-Golden, M. L., & Swanson, J. A. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013962 · Cited by 14
Thind, T. S., Rampal, G., Agrawal, S. K., Saxena, A. K., & Arora, S. (2010) · Drug and Chemical Toxicology · doi:10.3109/01480540903483433 · Cited by 16
Antioxidant Status and Sex Hormones in Women with Simple Endometrial Hyperplasia
Pejić, S., Todorović, A., Stojiljković, V., Pavlović, I., Gavrilović, L., Popović, N., & Pajović, S. B. (2015) · InTech eBooks · doi:10.5772/60853 · Cited by 14
Effect of physicochemical character differences on the genotoxic potency of kaolin
Kato, T., Toyooka, T., Ibuki, Y., Masuda, S., Watanabe, M., & Totsuka, Y. (2017) · Genes and Environment · doi:10.1186/s41021-017-0075-y · Cited by 14
Benghalem, I., Meziane, W., Hadjidj, Z., Ysmail-Dahlouk, L., Belamri, A., Mouhadjer, K., & Aribi, M. (2017) · Cytokine · doi:10.1016/j.cyto.2017.03.001 · Cited by 15
Wen, Y., Wen, Y., Wen, X., Cao, S., Huang, X., Wu, R. J., Zhao, Q., Liu, M., Huang, Y., Yan, Q., et al. (2017) · Gene · doi:10.1016/j.gene.2017.12.010 · Cited by 14
Yang, H., Kim, J., Chung, G., Lee, J., & Jang, Y. (2006) · Molecular Immunology · doi:10.1016/j.molimm.2006.08.017 · Cited by 14
CD14-dependent alterations in c-Jun expression in the liver after burn injury1
Cho, K., Adamson, L. K., Jeong, J., Crivello, S. D., VanHook, T. G., Palmieri, T. L., & Greenhalgh, D. G. (2004) · Journal of Surgical Research · doi:10.1016/j.jss.2004.07.007 · Cited by 14
Tumurkhuu, G., Koide, N., Dagvadorj, J., Hassan, F., Islam, S., Naiki, Y., Mori, I., Yoshida, T., & Yokochi, T. (2007) · FEMS Immunology & Medical Microbiology · doi:10.1111/j.1574-695x.2006.00203.x · Cited by 15
Metadata
- Authors
- Forman, H. J., & Torres, M.
- Affiliations
- University of Southern California (US)
- Department of Environmental Health Sciences, School of Public Health, University of Alabama at Birmingham, Birmingham, Alabama; and Department of Pediatrics, Children's Hospital Los Angeles Research Institute, Keck School of Medicine, University of Southern California, Los Angeles, California
- ORCID
- Forman, Henry Jay
- Venue
- American Journal of Respiratory and Critical Care Medicine
- Publisher
- Oxford University Press (OUP)
- Published
- 2002-12
- Volume
- 166
- Issue
- Supplement_1
- Pages
- S4-S8
- ISSN
- 1073-449X (ISSN-L)
- 1535-4970
- OpenAlex
- W1874751834
- Cited by
- 891
- References
- 67
- Citations by year
- 2026: 18 · 2025: 21 · 2024: 23 · 2023: 32 · 2022: 47 · 2021: 44 · 2020: 36 · 2019: 31 · 2018: 44 · 2017: 43 · 2016: 50 · 2015: 43 · 2014: 48 · 2013: 45 · 2012: 44
- FWCI
- 2.28
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- American Journal of Respiratory and Critical Care Medicine (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Heart, Lung, and Blood Institute (R01HL037556, HL 37556)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Keywords
- reactive oxygen species, NADPH oxidase, respiratory burst, macrophages, signal transduction, hydrogen peroxide, superoxide, antioxidant enzymes, thioredoxin reductase, thioredoxin, redox signaling, phagocytes
- MeSH terms
- Humans, Hydrogen Peroxide, Macrophages, Oxidation-Reduction, Signal Transduction, Respiratory Burst, Protein Tyrosine Phosphatases, Reactive Oxygen Species, Mitogen-Activated Protein Kinases
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