The DOI matches its Crossref record; 94 of the 94 references it cites were found in a registry or an index.
Lipopolysaccharide Induces Rac1-dependent Reactive Oxygen Species Formation and Coordinates Tumor Necrosis Factor-α Secretion through IKK Regulation of NF-κB
Open accessAbstract
Reactive oxygen species (ROS) are important second messengers generated in response to many types of environmental stress. In this setting, changes in intracellular ROS can activate signal transduction pathways that influence how cells react to their environment. In sepsis, a dynamic proinflammatory cellular response to bacterial toxins (e.g. lipopolysaccharide or LPS) leads to widespread organ damage and death. The present study demonstrates for the first time that the activation of Rac1 (a GTP-binding protein), and the subsequent production of ROS, constitutes a major pathway involved in NFkappaB-mediated tumor necrosis factor-alpha (TNFalpha) secretion following LPS challenge in macrophages. Expression of a dominant negative mutant of Rac1 (N17Rac1) reduced Rac1 activation, ROS formation, NFkappaB activation, and TNFalpha secretion following LPS stimulation. In contrast, expression of a dominant active form of Rac1 (V12Rac1) mimicked these effects in the absence of LPS stimulation. IKKalpha and IKKbeta were both required downstream modulators of LPS-activated Rac1, since the expression of either of the IKK dominant mutants (IKKalphaKM or IKKbetaKA) drastically reduced NFkappaB-dependent TNFalpha secretion. Moreover, studies using CD14 blocking antibodies suggest that Rac1 induces TNFalpha secretion through a pathway independent of CD14. However, a maximum therapeutic inhibition of LPS-induced TNFalpha secretion occurred when both CD14 and Rac1 pathways were inhibited. Our results suggest that targeting both Rac1- and CD14-dependent pathways could be a useful therapeutic strategy for attenuating the proinflammatory cytokine response during the course of sepsis.
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
“In the NF-κB system (e.g. [2020-2024]) (Fig 8), NF-κB is normally held inactive in the cytoplasm by binding to an inhibitor IκB (often IκBα). Pro-inflammatory cytokines such as TNF-α, LPS [2025-2030] and IL-1 [2031] act by binding to receptors at the cell surface and initiating signalling pathways that lead to the activation of a particular kinase, IκB kinase or IKK. This kinase phosphorylates the”
From Iron behaving badly: inappropriate iron chelation as a major contributor to the aetiology of vascular and other progressive inflammatory and degenerative diseases (2009) · cites this paper as [2026]
Citations
Cites
CD14, a Receptor for Complexes of Lipopolysaccharide (LPS) and LPS Binding Protein
Wright, S. D., Ramos, R., Tobias, P. S., Ulevitch, R. J., & Mathison, J. C. (1990) · Science · doi:10.1126/science.1698311 · Cited by 3,996
Phylogenetic Perspectives in Innate Immunity
Hoffmann, J. A., Kafatos, F. C., Janeway, C. A., & Ezekowitz, R. A. B. (1999) · Science · doi:10.1126/science.284.5418.1313 · Cited by 2,524
Andrews, N. C., & Faller, D. V. (1991) · Nucleic Acids Research · doi:10.1093/nar/19.9.2499 · Cited by 2,337
Ozinsky, A., Underhill, D. M., Fontenot, J. D., Hajjar, A. M., Smith, K. D., Wilson, C. B., Schroeder, L. A., & Aderem, A. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.250476497 · Cited by 2,086
A family of human receptors structurally related to Drosophila Toll.
Rock, F., Hardiman, G., Timans, J., Kastelein, R., & Bazan, J. (1998) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.95.2.588 · Cited by 2,009
Zandi, E., Rothwarf, D. M., Delhase, M., Hayakawa, M., & Karin, M. (1997) · Cell · doi:10.1016/s0092-8674(00)80406-7 · Cited by 1,814
Self-citationMyD88 is an adaptor protein in the hToll/IL-1 receptor family signaling pathways.
Medzhitov, R., Preston-Hurlburt, P., Kopp, E., Stadlen, A., Chen, C.-Q., Ghosh, S., & Janeway, C. (1998) · Molecules and Cells · doi:10.1016/s1097-2765(00)80136-7 · Cited by 1,783
Aruoma, O. I., Halliwell, B. B., Hoey, B. M., & Butler, J. (1989) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(89)90066-x · Cited by 1,774
Structure and Function of Lipopolysaccharide Binding Protein
Schumann, R. R., Leong, S. R., Flaggs, G., Gray, P. W., Wright, S. D., Mathison, J. C., Tobias, P. S., & Ulevitch, R. J. (1990) · Science · doi:10.1126/science.2402637 · Cited by 1,672
Ziegler, E. J., Fisher, C. J., Sprung, C. L., Straube, R., SADOFF, J. C., Foulke, G. E., Wortel, C. H., Fink, M. P., Dellinger, R. P., Teng, N. N. H., et al. (1991) · New England Journal of Medicine · doi:10.1056/nejm199102143240701 · Cited by 1,618
Research works printed but not linked: 4
- Morrison, 1978, Am. J. Pathol., 93, 526
- Peppelenbosch, 1999, Blood, 93, 4011, 10.1182/blood.V93.11.4011 · DOI
- Shi, 2000, Ann. Clin. Lab. Sci., 30, 209
- Ingalls, 1998, Prog. Clin. Biol. Res., 397, 107
Cited by
Sorted by citations
NF-κB activation by reactive oxygen species: Fifteen years later
Gloire, G., Legrand-Poels, S., & Piette, J. G. (2006) · Biochemical Pharmacology · doi:10.1016/j.bcp.2006.04.011 · Cited by 1,561
Liu, B., & Hong, J.-S. (2003) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.102.035048 · Cited by 1,095
Nrf2 is a critical regulator of the innate immune response and survival during experimental sepsis
Thimmulappa, R. K. (2006) · Journal of Clinical Investigation · doi:10.1172/jci25790 · Cited by 1,028
Reactive Oxygen Species: Drivers of Physiological and Pathological Processes
Checa, J., & Aran, J. M. (2020) · Journal of Inflammation Research · doi:10.2147/jir.s275595 · Cited by 1,068
Reactive oxygen species and cell signaling: Respiratory burst in macrophage signaling
Forman, H. J., & Torres, M. (2002) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.2206007 · Cited by 891
Azad, M. B., Chen, Y., & Gibson, S. B. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2270 · Cited by 764
Paik, Y.-H., Schwabe, R. F., Bataller, R., Russo, M. P., Jobin, C., & Brenner, D. A. (2003) · Hepatology · doi:10.1053/jhep.2003.50182 · Cited by 651
Sivandzade, F., Prasad, S., Bhalerao, A., & Cucullo, L. (2019) · Redox Biology · doi:10.1016/j.redox.2018.11.017 · Cited by 639
Park, H. S., Jung, H. Y., Park, E. Y., Kim, J., Lee, W. J., & Bae, Y. S. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.173.6.3589 · Cited by 635
NADPH Oxidases in Cardiovascular Health and Disease
Cave, A. C., Brewer, A. C., Narayanapanicker, A., Ray, R., Grieve, D. J., Walker, S., & Shah, A. M. (2006) · Antioxidants & Redox Signaling · doi:10.1089/ars.2006.8.691 · Cited by 630
CD14 and Toll-Like Receptors 2 and 4 Are Required for Fibrillar Aβ-Stimulated Microglial Activation
Reed-Geaghan, E. G., Savage, J. C., Hise, A. G., & Landreth, G. E. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.3158-09.2009 · Cited by 591
Qin, L., Liu, Y., Wang, T., Wei, S.-J., Block, M. L., Wilson, B., Liu, B., & Hong, J.-S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307657200 · Cited by 574
Kell, D. B. (2009) · BMC Medical Genomics · doi:10.1186/1755-8794-2-2 · Cited by 554
Hsu, H.-Y., & Wen, M.-H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111883200 · Cited by 519
Kabe, Y., Ando, K., Hirao, S., Yoshida, M., & Handa, H. (2005) · Antioxidants & Redox Signaling · doi:10.1089/ars.2005.7.395 · Cited by 585
Li, W. G., Gavrila, D., Liu, X., Wang, L., Gunnlaugsson, S. T., Stoll, L. L., McCormick, M. L., Sigmund, C. D., Tang, C., & Weintraub, N. L. (2004) · Circulation · doi:10.1161/01.cir.0000127956.43874.f2 · Cited by 499
Reactive Oxygen Species in Macrophages: Sources and Targets
Canton, M., Sánchez‐Rodríguez, R., Spera, I., Venegas, F. C., Favia, M., Viola, A., & Castegna, A. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.734229 · Cited by 490
Redox regulation of glial inflammatory response to lipopolysaccharide and interferonγ
Pawate, S., Shen, Q., Fan, F., & Bhat, N. R. (2004) · Journal of Neuroscience Research · doi:10.1002/jnr.20180 · Cited by 428
Antioxidant and prooxidant mechanisms in the regulation of redox(y)-sensitive transcription factors
Haddad, J. J. (2002) · Cellular Signalling · doi:10.1016/s0898-6568(02)00053-0 · Cited by 430
NADPH Oxidase-Dependent Signaling in Endothelial Cells: Role in Physiology and Pathophysiology
Frey, R. S., Ushio‐Fukai, M., & Malik, A. B. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2220 · Cited by 432
Eicosapentaenoic Acid Prevents LPS-Induced TNF-α Expression by Preventing NF-κB Activation
Zhao, Y., Joshi-Barve, S., Barve, S., & Chen, L. H. (2004) · Journal of the American College of Nutrition · doi:10.1080/07315724.2004.10719345 · Cited by 405
Starkey, M., Hickman, J. H., Luyan, Z., Zhang, N., Long, S. D., Hinz, A. J., Palacios, S., Manoil, C., Kirisits, M. J., Starner, T. D., et al. (2009) · Journal of Bacteriology · doi:10.1128/jb.00119-09 · Cited by 392
Evidence that reactive oxygen species do not mediate NF‐κB activation
Hayakawa, M., Miyashita, H., Sakamoto, I., Kitagawa, M., Tanaka, H., Yasuda, H., Karin, M., & Kikugawa, K. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg332 · Cited by 384
Liver ischemia/reperfusion injury: Processes in inflammatory networks—A review
Abu‐Amara, M., Yang, S. Y., Tapuria, N., Fuller, B. J., Davidson, B. R., & Seifalian, A. M. (2010) · Liver Transplantation · doi:10.1002/lt.22117 · Cited by 368
Cuadrado, A., Martín‐Moldes, Z., Ye, J., & Lastres‐Becker, I. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.540633 · Cited by 330
Immune cells: free radicals and antioxidants in sepsis
Víctor, V. M., Rocha, M., & la Fuente, M. D. (2004) · International Immunopharmacology · doi:10.1016/j.intimp.2004.01.020 · Cited by 319
Redox-Sensitive Kinases of the Nuclear Factor-κB Signaling Pathway
Pantano, C., Reynaert, N. L., van der Vliet, A., & Janssen-Heininger, Y. M. W. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1791 · Cited by 306
Lee, S., Bai, S.-K., Lee, K.-S., Namkoong, S., Na, H. J., Ha, K., Han, J. A., Yim, S. V., Chang, K., Kwon, Y. G., et al. (2003) · PubMed · Cited by 279
Yuan, H., Perry, C. N., Huang, C., Iwai‐Kanai, E., Carreira, R., Glembotski, C. C., & Gottlieb, R. A. (2008) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01051.2008 · Cited by 265
Human Hepatic Stellate Cells Express CCR5 and RANTES to Induce Proliferation and Migration
Schwabe, R. F., Bataller, R., & Brenner, D. A. (2003) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00215.2003 · Cited by 252
Lee, S., Bai, S.-K., Lee, K., Namkoong, S., Na, H.-J., Ha, K., Han, J., Yim, S., Chang, K., Kwon, Y., et al. (2003) · Molecules and Cells · doi:10.1016/s1016-8478(23)13772-1 · Cited by 247
Cortez, D. M., Feldman, M. D., Mummidi, S., Valente, A. J., Steffensen, B., Vincenti, M. P., Barnes, J. L., & Chandrasekar, B. (2007) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00928.2007 · Cited by 238
The lipopolysaccharide Parkinson’s disease animal model: mechanistic studies and drug discovery
Dutta, G., Zhang, P., & Liu, B. (2008) · Fundamental & Clinical Pharmacology · doi:10.1111/j.1472-8206.2008.00616.x · Cited by 235
Theiss, A. L., Simmons, J. G., Jobin, C., & Lund, P. K. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505291200 · Cited by 233
Role of glycogen synthase kinase-3 in TNF-α-induced NF-κB activation and apoptosis in hepatocytes
Schwabe, R. F., & Brenner, D. A. (2002) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00016.2002 · Cited by 229
Li, Q., Harraz, M. M., Zhou, W., Zhang, L. N., Ding, W., Zhang, Y., Eggleston, T., Yeaman, C. A., Bánfi, B., & Engelhardt, J. F. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.26.1.140-154.2006 · Cited by 233
Self-citationTan, P., Sagoo, P., Chan, C. C. W., Yates, J., Campbell, J., Beutelspacher, S. C., Foxwell, B. M. J., Lombardi, G., & George, A. J. T. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.12.7633 · Cited by 224
Li, Q., & Engelhardt, J. F. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511153200 · Cited by 219
Self-citationRole of reactive oxygen species in LPS‐induced production of prostaglandin E2in microglia
Wang, T., Qin, L., Liu, B., Liu, Y., Wilson, B. C., Eling, T. E., Langenbach, R. I., Taniura, S., & Hong, J. (2004) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02242.x · Cited by 220
Resolution of inflammation: Mechanisms and opportunity for drug development
Alessandri, A. L., Sousa, L. P., Lucas, C. D., Rossi, A. G., Pinho, V., & Teixeira, M. M. (2013) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2013.04.006 · Cited by 219
Qi, S., Xin, Y., Guo, Y., Diao, Y., Kou, X., Luo, L., & Yin, Z. (2011) · International Immunopharmacology · doi:10.1016/j.intimp.2011.12.001 · Cited by 215
Miller, F. J., Filali, M. S., Huss, G. J., Stanić, B., Chamseddine, A., Barna, T. J., & Lamb, F. S. (2007) · Circulation Research · doi:10.1161/circresaha.107.151076 · Cited by 215
Haemophilus influenzae Forms Biofilms on Airway Epithelia
Starner, T. D., Zhang, N., Kim, G., Apicella, M. A., & McCray, P. B. (2006) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200509-1459oc · Cited by 207
Self-citationPatel, D. N., King, C. A., Bailey, S. R., Holt, J. W., Venkatachalam, K., Agrawal, A. C., Valente, A. J., & Chandrasekar, B. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703250200 · Cited by 199
Oxidative parameters and mortality in sepsis induced by cecal ligation and perforation
Ritter, C., Andrades, M. É., da Frota, M. L. C., Bonatto, F., Pinho, R. A., Polydoro, M., Klamt, F., Pinheiro, C. T. S., Menna‐Barreto, S. S., Moreira, J. C. F., et al. (2003) · Intensive Care Medicine · doi:10.1007/s00134-003-1789-9 · Cited by 195
Syrovets, T., Büchele, B., Krauss, C., Laumonnier, Y., & Simmet, T. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.1.498 · Cited by 196
Luo, J., Wang, Y., Fu, W., Wu, J., & Chen, A. F. (2004) · Circulation · doi:10.1161/01.cir.0000137969.87365.05 · Cited by 187
Fan, C., Li, Q., Ross, D., & Engelhardt, J. F. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m206718200 · Cited by 183
Self-citationDevelopment of cystic fibrosis and noncystic fibrosis airway cell lines
Zabner, J., Karp, P., Seiler, M. P., Phillips, S. L., Mitchell, C. J., Saavedra, M., Welsh, M. J., & Klingelhutz, A. J. (2003) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00355.2002 · Cited by 178
Kamata, H., Manabe, T., Oka, S., Kamata, K., & Hirata, H. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02712-6 · Cited by 179
Lehman, S. E., Morris, A. S., Mueller, P. S., Salem, A. K., Grassian, V. H., & Larsen, S. C. (2015) · Environmental Science Nano · doi:10.1039/c5en00179j · Cited by 173
Anandamide induces necrosis in primary hepatic stellate cells†‡
Siegmund, S., Uchinami, H., Osawa, Y., Brenner, D. A., & Schwabe, R. F. (2005) · Hepatology · doi:10.1002/hep.20667 · Cited by 171
Signaling Role of Intracellular Iron in NF-κB Activation
Xiong, S., She, H., Takeuchi, H., Han, B., Engelhardt, J. F., Barton, C. H., Zandi, E., Giulivi, C., & Tsukamoto, H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210905200 · Cited by 161
Self-citationOxidative Stress and Microglial Cells in Parkinson's Disease
Peterson, L. J., & Flood, P. M. (2012) · Mediators of Inflammation · doi:10.1155/2012/401264 · Cited by 167
Simón, F., & Fernández, R. (2009) · Journal of Hypertension · doi:10.1097/hjh.0b013e328329e31c · Cited by 167
Suzuki, Y., Ohgami, K., Shiratori, K., Jin, X.-H., Ilieva, I. B., Koyama, Y., Yazawa, K., Yoshida, K., Kase, S., & Ohno, S. (2005) · Experimental Eye Research · doi:10.1016/j.exer.2005.06.023 · Cited by 158
Dogra, C., Changotra, H., Mohan, S., & Kumar, A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511131200 · Cited by 159
James, M. A., Lee, J. H., & Klingelhutz, A. (2006) · Journal of Virology · doi:10.1128/jvi.01942-05 · Cited by 162
Chin, C. L., Manzel, L. J., Lehman, E. E., Humlicek, A. L., Shi, L., Starner, T. D., Denning, G. M., Murphy, T. F., Sethi, S., & Look, D. C. (2005) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200412-1687oc · Cited by 151
Anti-inflammatory effects of hydroxycinnamic acid derivatives
Nagasaka, R., Chotimarkorn, C., Shafiqul, I. M., Hori, M., Ozaki, H., & Ushio, H. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.04.178 · Cited by 149
Horwood, N. J., Mahon, T., McDaid, J., Campbell, J., Mano, H., Brennan, F. M., Webster, D., & Foxwell, B. M. J. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20021845 · Cited by 145
Oxidative Stress Contributes to Lung Injury and Barrier Dysfunction via Microtubule Destabilization
Kratzer, E., Tian, Y., Sarich, N. A., Wu, T., Meliton, A. Y., Leff, A. R., & Birukova, A. A. (2012) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2012-0161oc · Cited by 142
Awareness and current knowledge of Parkinson’s disease: a neurodegenerative disorder
Khan, A. U., Akram, M., Daniyal, M., & Zainab, R. (2018) · International Journal of Neuroscience · doi:10.1080/00207454.2018.1486837 · Cited by 151
Schwabe, R. F., Uchinami, H., Qian, T., Bennett, B. L., Lemasters, J. J., & Brenner, D. A. (2004) · The FASEB Journal · doi:10.1096/fj.03-0771fje · Cited by 141
Discovery and Validation of a New Class of Small Molecule Toll-Like Receptor 4 (TLR4) Inhibitors
Neal, M. D., Jia, H., Eyer, B. R., Good, M. L., Guerriero, C. J., Sodhi, C. P., Afrazi, A., Prindle, T., Ma, C., Branca, M. F., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0065779 · Cited by 137
Kizaki, T., Suzuki, K., Hitomi, Y., Taniguchi, N., Saitoh, D., Watanabe, K., Onoé, K., Day, N. K. B., Good, R. A., & Ohno, H. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.142206299 · Cited by 136
Gonzalez‐Dosal, R., Horan, K., Rahbek, S. H., Ichijo, H., Chen, Z. J., Mieyal, J. J., Hartmann, R., & Paludan, S. R. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002250 · Cited by 135
Campbell, J., Ciesielski, C. J., Hunt, A. E., Horwood, N. J., Beech, J. T., Hayes, L. A., Denys, A., Feldmann, M., Brennan, F. M., & Foxwell, B. M. J. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.173.11.6928 · Cited by 135
Ischemia/Reperfusion Injury in Liver Surgery and Transplantation: Pathophysiology
Weigand, K., Brost, S., Steinebrunner, N., Büchler, M. W., Schemmer, P., & Müller, M. (2012) · HPB Surgery · doi:10.1155/2012/176723 · Cited by 139
Wang, T., Liu, B., Zhang, W., Wilson, B. C., & Hong, J. (2004) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.103.059683 · Cited by 133
TRPM2 mediates ischemic kidney injury and oxidant stress through RAC1
Gao, G., Wang, W., Tadagavadi, R. K., Briley, N. E., Love, M. I., Miller, B. A., & Reeves, W. B. (2014) · Journal of Clinical Investigation · doi:10.1172/jci76042 · Cited by 131
Bowen, E. J., Schmidt, T., Firm, C. S., Russo, A. F., & Durham, P. L. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03524.x · Cited by 130
Şanlioğlu, A. D., Dirice, E., Aydın, Ç., Erin, N., Köksoy, S., & Şanlıoğlu, S. (2005) · BMC Cancer · doi:10.1186/1471-2407-5-54 · Cited by 129
Primary Epithelial Cell Models for Cystic Fibrosis Research
Randell, S. H., Fulcher, M. L., O’Neal, W. K., & Olsen, J. C. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-120-8_18 · Cited by 129
Song, M., Kellum, J. A., Kaldas, H., & Fink, M. P. (2004) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.103.056622 · Cited by 128
Denys, A., Udalova, I. A., Smith, C., Williams, L. M., Ciesielski, C. J., Campbell, J., Andrews, C., Kwiatkowski, D. P., & Foxwell, B. M. J. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.168.10.4837 · Cited by 127
Chemoprotection by Phenolic Antioxidants
Ma, Q., & Kinneer, K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m106685200 · Cited by 127
Yang, C., Lee, D., Song, C., An, S., Li, S., Kim, J., Kim, C., Yoo, D. G., Jeon, B. H., Yang, H., et al. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20061849 · Cited by 129
Elks, C. M., Mariappan, N., Haque, M., Guggilam, A., Majid, D. S. A., & Francis, J. (2008) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.90628.2008 · Cited by 122
Zhang, Q., Piao, X., Piao, X., Lu, T., Wang, D., & Kim, S. W. (2010) · Food and Chemical Toxicology · doi:10.1016/j.fct.2010.09.032 · Cited by 122
Endosomal Nox2 Facilitates Redox-Dependent Induction of NF-κB by TNF-α
Li, Q., Spencer, N. Y., Oakley, F. D., Buettner, G. R., & Engelhardt, J. F. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2407 · Cited by 119
Self-citationVaccination in patients with kidney failure: lessons from COVID-19
Babel, N., Hugo, C., & Westhoff, T. H. (2022) · Nature Reviews Nephrology · doi:10.1038/s41581-022-00617-5 · Cited by 119
Kumar, S., Saxena, J., Srivastava, V. K., Kaushik, S., Singh, H., Abo‐EL‐Sooud, K., Abdel‐Daim, M. M., Jyoti, A., & Saluja, R. (2022) · Vaccines · doi:10.3390/vaccines10101575 · Cited by 123
Role of sestrin2 in the regulation of proinflammatory signaling in macrophages
Yang, J. H., Kim, K. M., Kim, M. G., Seo, K. H., Han, J. Y., Ka, S., Park, B., Shin, S. M., Ku, S., Cho, I. J., et al. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.11.002 · Cited by 108
Dysregulation of the Immune Response in Severe Sepsis
Pinsky, M. R. (2004) · The American Journal of the Medical Sciences · doi:10.1097/00000441-200410000-00005 · Cited by 108
Wen, H., Lei, Y. L., Eun, S.-Y., & Ting, J. P. ‐. (2010) · The Journal of Experimental Medicine · doi:10.1084/jem.20101138 · Cited by 109
Dynein Light Chain LC8 Negatively Regulates NF-κB through the Redox-dependent Interaction with IκBα
Jung, Y., Kim, H., Min, S. H., Rhee, S. G., & Jeong, W. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803072200 · Cited by 109
Chen, X., Zhang, Q., Zhao, R., Ding, X., Tummala, P. E., & Medford, R. M. (2003) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.102.047894 · Cited by 107
McPhillips, K. A., Janssen, W. J., Ghosh, M., Byrne, A. M., Gardai, S. J., Remigio, L. K., Bratton, D. L., Kang, J. L., & Henson, P. M. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.12.8117 · Cited by 106
Nardo, D. D., Nardo, C. M. D., Nguyen, T. U., Hamilton, J. A., & Scholz, G. M. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0901031 · Cited by 106
Yin, J., Kwon, Y., Kim, D., Lee, D., Kim, G., Hu, Y., Ryu, J.-H., & Yoon, J. (2015) · Nature Protocols · doi:10.1038/nprot.2015.109 · Cited by 104
Syeda, F., Grosjean, J., Houliston, R. A., Keogh, R. J., Carter, T. D., Paleolog, E. M., & Wheeler-Jones, C. P. D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m509292200 · Cited by 102
Nitrosative Stress-induced Apoptosis through Inhibition of NF-κB
Marshall, H. E., & Stamler, J. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201638200 · Cited by 101
Hsing, C., Lin, M.-C., Choi, P.-C., Huang, W.-C., Kai, J.-I., Tsai, C., Cheng, Y., Hsieh, C.-Y., Wang, C., Chang, Y.-P., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017598 · Cited by 100
HMG-CoA Reductase Inhibitors Inhibit Inducible Nitric Oxide Synthase Gene Expression in Macrophages
Huang, K., Chen, C., Chen, J.-C., & Lin, W. (2003) · Journal of Biomedical Science · doi:10.1007/bf02256431 · Cited by 96
Murthy, S., Ryan, A. J., He, C., Mallampalli, R. K., & Carter, A. B. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.099655 · Cited by 100
Shaik, S., Combs, C. K., & Ebadi, M. (2006) · Neurochemical Research · doi:10.1007/s11064-005-9233-x · Cited by 104
Escobar, J., Pereda, J., Arduini, A., Sandoval, J., Sabater, L., Aparisi, L., López‐Rodas, G., & Sastre, J. (2009) · Current Pharmaceutical Design · doi:10.2174/138161209789058075 · Cited by 99
Reshef, Y., Rumker, L., Kang, J. B., Nathan, A., Korsunsky, I., Asgari, S., Murray, M. B., Moody, D. B., & Raychaudhuri, S. (2021) · Nature Biotechnology · doi:10.1038/s41587-021-01066-4 · Cited by 93
Li, Q., Spencer, N. Y., Pantazis, N. J., & Engelhardt, J. F. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.279711 · Cited by 94
Self-citation
Metadata
- Authors
- Sanlioglu, S., Williams, C. M., Samavati, L., Butler, N. S., Wang, G., McCray, P. B., Ritchie, T. C., Hunninghake, G. W., Zandi, E., & Engelhardt, J. F.
- Affiliations
- University of Iowa (US)
- USC Norris Comprehensive Cancer Center (US)
- Corresponding author
- Engelhardt, John F.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2001-08
- Volume
- 276
- Issue
- 32
- Pages
- 30188-30198
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2161781385
- Cited by
- 395
- References
- 94
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 5 · 2023: 8 · 2022: 7 · 2021: 10 · 2020: 9 · 2019: 10 · 2018: 12 · 2017: 4 · 2016: 9 · 2015: 13 · 2014: 17 · 2013: 17 · 2012: 16
- FWCI
- 9.85
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5p50hl060316-05)
- National Heart, Lung, and Blood Institute (HL 60316)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK54759, P30DK054759)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- lipopolysaccharide, Rac1, reactive oxygen species, NF-κB activation, IKKα, IKKβ, macrophages, CD14, sepsis, dominant negative Rac1
- MeSH terms
- Adenoviridae, Animals, Catalase, Cell Line, Cell Nucleus, Dose-Response Relationship, Drug, Electron Spin Resonance Spectroscopy, Enzyme Activation, Ethidium, Gene Expression Regulation, Genes, Dominant, Glutathione Transferase, Humans, Lipopolysaccharides, Luciferases, Models, Biological, Mutation, Oxidation-Reduction, Protein Binding, RNA, Messenger, Superoxides, Time Factors, Tumor Necrosis Factor-alpha, Blotting, Western, Signal Transduction, Down-Regulation, Up-Regulation, Cytokines, NF-kappa B, Protein Serine-Threonine Kinases, Reactive Oxygen Species, Lipopolysaccharide Receptors, Protein Isoforms, Reverse Transcriptase Polymerase Chain Reaction, rac1 GTP-Binding Protein, Mice, I-kappa B Kinase
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