Crosstalk of reactive oxygen species and NF-κB signaling

Morgan, Michael J; Liu, Zheng-gang

doi:10.1038/cr.2010.178

Cited by 3,505NF-κB Signaling PathwaysRedox biology and oxidative stressNeutrophil, Myeloperoxidase and Oxidative Mechanisms

Crosstalk of reactive oxygen species and NF-κB signaling

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Morgan, Michael J, Liu, Zheng-gang·2011·Cell Research

DOI 10.1038/cr.2010.178PMC PMC3193400

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Abstract

NF-κB proteins are a family of transcription factors that are of central importance in inflammation and immunity. NF-κB also plays important roles in other processes, including development, cell growth and survival, and proliferation, and is involved in many pathological conditions. Reactive Oxygen Species (ROS) are created by a variety of cellular processes as part of cellular signaling events. While certain NF-κB-regulated genes play a major role in regulating the amount of ROS in the cell, ROS have various inhibitory or stimulatory roles in NF-κB signaling. Here we review the regulation of ROS levels by NF-κB targets and various ways in which ROS have been proposed to impact NF-κB signaling pathways.

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Shared Principles in NF-κB Signaling
Hayden, M. S., & Ghosh, S. (2008) · Cell · doi:10.1016/j.cell.2008.01.020 · Cited by 4,814 · see citing works
Oxidative stress: oxidants and antioxidants
Sies, H. (1997) · Experimental Physiology · doi:10.1113/expphysiol.1997.sp004024 · Cited by 4,577 · see citing works
NOX enzymes and the biology of reactive oxygen
Lambeth, J. D. (2004) · Nature Reviews Immunology · doi:10.1038/nri1312 · Cited by 3,125 · see citing works
Regulation and Function of NF-κB Transcription Factors in the Immune System
Vallabhapurapu, S., & Karin, M. (2009) · Annual Review of Immunology · doi:10.1146/annurev.immunol.021908.132641 · Cited by 2,578 · see citing works
The two NF-κB activation pathways and their role in innate and adaptive immunity
Bonizzi, G., & Karin, M. (2004) · Trends in Immunology · doi:10.1016/j.it.2004.03.008 · Cited by 2,535 · see citing works
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 · see citing works
Reactive Oxygen Species Promote TNFα-Induced Death and Sustained JNK Activation by Inhibiting MAP Kinase Phosphatases
Kamata, H., Honda, S.-I., Maeda, S., Chang, L., Hirata, H., & Karin, M. (2005) · Cell · doi:10.1016/j.cell.2004.12.041 · Cited by 1,792 · see citing works
Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase
Li, Y., Huang, T.-T., Carlson, E. J., Melov, S., Ursell, P. C., Olson, J. L., Noble, L. J., Yoshimura, M. P., Berger, C., Chan, P. H., et al. (1995) · Nature Genetics · doi:10.1038/ng1295-376 · Cited by 1,789 · see citing works
Activation by IKKα of a Second, Evolutionary Conserved, NF-κB Signaling Pathway
Senftleben, U., Cao, Y., Xiao, G., Greten, F. R., Krähn, G. M., Bonizzi, G., Chen, Y., Hu, Y., Fong, A., Sun, S., et al. (2001) · Science · doi:10.1126/science.1062677 · Cited by 1,361 · see citing works
H2O2 and antioxidants have opposite effects on activation of NF‐kappa B and AP‐1 in intact cells: AP‐1 as secondary antioxidant‐responsive factor.
Meyer, M., Schreck, R., & Baeuerle, P. A. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05850.x · Cited by 1,322 · see citing works
Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IκB kinase
Rossi, A., Kapahi, P., Natoli, G., Takahashi, T., Chen, Y., Karin, M., & Santoro, M. G. (2000) · Nature · doi:10.1038/47520 · Cited by 1,310 · see citing works
Phosphorylation of NF-κB p65 by PKA Stimulates Transcriptional Activity by Promoting a Novel Bivalent Interaction with the Coactivator CBP/p300
Zhong, H., Voll, R. E., & Ghosh, S. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80066-0 · Cited by 1,210 · see citing works
Regulation of ferritin genes and protein
Torti, F. M., & Torti, S. V. (2002) · Blood · doi:10.1182/blood.v99.10.3505 · Cited by 1,173 · see citing works
4-Hydroxy-2-nonenal: a product and mediator of oxidative stress
Uchida, K. (2003) · Progress in Lipid Research · doi:10.1016/s0163-7827(03)00014-6 · Cited by 1,164 · see citing works
Reversible Inactivation of the Tumor Suppressor PTEN by H2O2
Lee, S.-R., Yang, K., Kwon, J., Lee, C., Jeong, W., & Rhee, S. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111899200 · Cited by 1,061 · see citing works
Essential function for the kinase TAK1 in innate and adaptive immune responses
Sato, S., Sanjo, H., Takeda, K., Ninomiya‐Tsuji, J., Yamamoto, M., Kawai, T., Matsumoto, K., Takeuchi, O., & Akira, S. (2005) · Nature Immunology · doi:10.1038/ni1255 · Cited by 974 · see citing works
The Phosphorylation Status of Nuclear NF-ΚB Determines Its Association with CBP/p300 or HDAC-1
Zhong, H., May, M. J., Jimi, E., & Ghosh, S. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00477-x · Cited by 930 · see citing works
The Lymphotoxin-β Receptor Induces Different Patterns of Gene Expression via Two NF-κB Pathways
Dejardin, E., Droin, N. M., Delhase, M., Haas, E., Cao, Y., Makris, C., Li, Z., Karin, M., Ware, C. F., & Green, D. R. (2002) · Immunity · doi:10.1016/s1074-7613(02)00423-5 · Cited by 923 · see citing works
AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1
Hirota, K., Matsui, M., Iwata, S., Nishiyama, A., Mori, K., & Yodoi, J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.8.3633 · Cited by 845 · see citing works
Superoxide dismutase as a target for the selective killing of cancer cells
Huang, P., Li, F., Oldham, E. A., Keating, M. J., & Plunkett, W. K. (2000) · Nature · doi:10.1038/35030140 · Cited by 842 · see citing works
Nox proteins in signal transduction
Brown, D. I., & Griendling, K. (2009) · Free Radical Biology & Medicine · doi:10.1016/j.freeradbiomed.2009.07.023 · Cited by 841 · see citing works
NF-κB-Inducing Kinase Regulates the Processing of NF-κB2 p100
Xiao, G., Harhaj, E. W., & Sun, S. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00187-3 · Cited by 836 · see citing works
Thiordoxin regulates the DNA binding activity of NF-χB by reduction of a disulphid bond involving cysteine 62
Matthews, J. R., Wakasugi, N., Virelizier, J., Yodoi, J., & Hay, R. T. (1992) · Nucleic Acids Research · doi:10.1093/nar/20.15.3821 · Cited by 831 · see citing works
Akt Stimulates the Transactivation Potential of the RelA/p65 Subunit of NF-κB through Utilization of the IκB Kinase and Activation of the Mitogen-activated Protein Kinase p38
Madrid, L. V., Mayo, M. W., Reuther, J. Y., & Baldwin, A. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101103200 · Cited by 777 · see citing works
Regulation of protein function by S‐glutathiolation in response to oxidative and nitrosative stress
Klatt, P., & Lamas, S. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01601.x · Cited by 751 · see citing works
TAK1, but not TAB1 or TAB2, plays an essential role in multiple signaling pathways in vivoPreprint
Shim, J., Xiao, C., Paschal, A. E., Bailey, S. T., Rao, P., Hayden, M. S., Lee, K., Bussey, C., Steckel, M., Tanaka, N., et al. (2005) · Genes & Development · doi:10.1101/gad.1360605 · Cited by 735 · see citing works
NAD(P)H:quinone acceptor oxidoreductase 1 (NQO1), a multifunctional antioxidant enzyme and exceptionally versatile cytoprotector
Dinkova‐Kostova, A. T., & Talalay, P. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.03.019 · Cited by 726 · see citing works
CuZnSOD deficiency leads to persistent and widespread oxidative damage and hepatocarcinogenesis later in life
Elchuri, S., Oberley, T. D., Qi, W., Eisenstein, R. S., Jackson Roberts, L., Van Remmen, H., Epstein, C. J., & Huang, T.-T. (2005) · Oncogene · doi:10.1038/sj.onc.1208207 · Cited by 667 · see citing works
Ferritin heavy chain upregulation by NF-κB inhibits TNFα-induced apoptosis by suppressing reactive oxygen species
Pham, C. G., Bubici, C., Zazzeroni, F., Papa, S., Jones, J., Alvarez, K., Jayawardena, S., De Smaele, E., Cong, R., Beaumont, C., et al. (2004) · Cell · doi:10.1016/j.cell.2004.10.017 · Cited by 663 · see citing works
Tyrosine Phosphorylation of IκB-α Activates NF-κB without Proteolytic Degradation of IκB-α
Imbert, V., Rupec, R. A., Livolsi, A., Pahl, H. L., Traenckner, E. B.-M., Mueller‐Dieckmann, C., Farahifar, D., Rossi, B., Auberger, P., Baeuerle, P. A., et al. (1996) · Cell · doi:10.1016/s0092-8674(00)80153-1 · Cited by 660 · see citing works
Modulation of transcription factor NF-kappa B binding activity by oxidation-reduction in vitro.
Toledano, M. B., & Leonard, W. J. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.10.4328 · Cited by 657 · see citing works
Akt-dependent regulation of NF-κB is controlled by mTOR and Raptor in association with IKKPreprint
Dan, H. C., Cooper, M. J., Cogswell, P. C., Duncan, J. A., Ting, J. P.-Y., & Baldwin, A. S. (2008) · Genes & Development · doi:10.1101/gad.1662308 · Cited by 638 · see citing works
Functions of NF-κB1 and NF-κB2 in immune cell biology
Beinke, S., & Ley, S. C. (2004) · Biochemical Journal · doi:10.1042/bj20040544 · Cited by 611 · see citing works
Distinct Roles of Thioredoxin in the Cytoplasm and in the Nucleus
Hirota, K., Murata, M., Sachi, Y., Nakamura, H., Takeuchi, J. S., Mori, K., & Yodoi, J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.39.27891 · Cited by 610 · see citing works
Noncanonical NF-κB activation requires coordinated assembly of a regulatory complex of the adaptors cIAP1, cIAP2, TRAF2 and TRAF3 and the kinase NIK
Zarnegar, B. J., Wang, Y., Mahoney, D. J., Dempsey, P. W., Cheung, H. H., He, J., Shiba, T. L., Yang, X., Yeh, W., Mak, T. W., et al. (2008) · Nature Immunology · doi:10.1038/ni.1676 · Cited by 607 · see citing works
Nonredundant and complementary functions of TRAF2 and TRAF3 in a ubiquitination cascade that activates NIK-dependent alternative NF-κB signaling
Vallabhapurapu, S., Matsuzawa, A., Zhang, W., Tseng, P., Keats, J. J., Wang, H., Vignali, D. A. A., Bergsagel, P. L., & Karin, M. (2008) · Nature Immunology · doi:10.1038/ni.1678 · Cited by 605 · see citing works
Hepatic Microsomal Ethanol Oxidation
Thurman, R. G., Ley, H. G., & Scholz, R. W. (1972) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1972.tb01711.x · Cited by 601 · see citing works
Redox Regulation of NF-κB Activation: Distinct Redox Regulation Between the Cytoplasm and the Nucleus
Kabe, Y., Ando, K., Hirao, S., Yoshida, M., & Handa, H. (2005) · Antioxidants & Redox Signaling · doi:10.1089/ars.2005.7.395 · Cited by 585 · see citing works
Glutathione S-Transferases - A Review
Salinas, A. E., & Wong, M. G. (1999) · Current Medicinal Chemistry · doi:10.2174/0929867306666220208213032 · Cited by 557 · see citing works
Early Embryonic Lethality Caused by Targeted Disruption of the Mouse Thioredoxin Gene
Matsui, M., Oshima, M., Oshima, H., Takaku, K., Maruyama, T., Yodoi, J., & Taketo, M. M. (1996) · Developmental Biology · doi:10.1006/dbio.1996.0208 · Cited by 546 · see citing works
Activation of Apoptosis Signal-Regulating Kinase 1 (ASK1) by Tumor Necrosis Factor Receptor-Associated Factor 2 Requires Prior Dissociation of the ASK1 Inhibitor Thioredoxin
Liu, H., Nishitoh, H., Ichijo, H., & Kyriakis, J. M. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.6.2198-2208.2000 · Cited by 545 · see citing works
Arachidonic Acid Oxygenation by COX-1 and COX-2
Marnett, L. J., Rowlinson, S. W., Goodwin, D. C., Kalgutkar, A. S. S., & Lanzo, C. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.33.22903 · Cited by 524 · see citing works
Oxidative Stress, Toxicology, and Pharmacology of CYP2E1
Caro, A. A., & Cederbaum, A. I. (2004) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.44.101802.121704 · Cited by 513 · see citing works
Antioxidant Function of Thioredoxin and Glutaredoxin Systems
Holmgren, A. (2000) · Antioxidants and Redox Signaling · doi:10.1089/ars.2000.2.4-811 · Cited by 504 · see citing works
Hydrogen Peroxide Activates NF-κB through Tyrosine Phosphorylation of IκBα and Serine Phosphorylation of p65
Takada, Y., Mukhopadhyay, A., Kundu, G. C., Mahabeleshwar, G. H., Singh, S., & Aggarwal, B. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212389200 · Cited by 495 · see citing works
Good cop, bad cop: the different faces of NF-κB
Perkins, N. D., & Gilmore, T. D. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401838 · Cited by 489 · see citing works
Inhibition of NF- B DNA Binding by Nitric Oxide
Matthews, J. R., Botting, C. H., Panico, M., Morris, H. R., & Hay, R. T. (1996) · Nucleic Acids Research · doi:10.1093/nar/24.12.2236 · Cited by 489 · see citing works
Glutathione Peroxidase Protects against Peroxynitrite-mediated Oxidations
Sies, H., Sharov, V. S., Klotz, L., & Briviba, K. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.44.27812 · Cited by 488 · see citing works
Orchestrating Redox Signaling Networks through Regulatory Cysteine Switches
Paulsen, C. E., & Carroll, K. S. (2009) · ACS Chemical Biology · doi:10.1021/cb900258z · Cited by 478 · see citing works
Regulation of the NF-κB-inducing Kinase by Tumor Necrosis Factor Receptor-associated Factor 3-induced Degradation
Liao, G., Zhang, M., Harhaj, E. W., & Sun, S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403286200 · Cited by 467 · see citing works
Xanthine oxidase and xanthine dehydrogenase
Hille, R., & Nishino, T. (1995) · The FASEB Journal · doi:10.1096/fasebj.9.11.7649415 · Cited by 445 · see citing works
Hypoxia causes the activation of nuclear factor kappa B through the phosphorylation of I kappa B alpha on tyrosine residues.
Koong, A. C., Chen, E. Y., & Giaccia, A. J. (1994) · PubMed · Cited by 444 · see citing works
Dynamic redox control of NF-κB through glutaredoxin-regulated S-glutathionylation of inhibitory κB kinase β
Reynaert, N. L., van der Vliet, A., Guala, A. S., McGovern, T., Hristova, M., Pantano, C., Heintz, N. H., Heim, J., Ho, Y.-S., Matthews, D. E., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603290103 · Cited by 442 · see citing works
The Absence of Mitochondrial Thioredoxin 2 Causes Massive Apoptosis, Exencephaly, and Early Embryonic Lethality in Homozygous Mice
Nonn, L., Williams, R. R., Erickson, R. P., & Powis, G. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.3.916-922.2003 · Cited by 438 · see citing works
THE OXIDATION OF DRUGS BY LIVER MICROSOMES: ON THE ROLE OF TPNH AND OXYGEN
Gillette, J. H., Brodie, B. B., & Du, B. N. L. (1957) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(25)11915-0 · Cited by 409 · see citing works
TAK1 is Critical for IκB Kinase-mediated Activation of the NF-κB Pathway
Takaesu, G., Surabhi, R. M., Park, K.-J., Ninomiya‐Tsuji, J., Matsumoto, K., & Gaynor, R. B. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)01404-3 · Cited by 404 · see citing works
Identification of binding sites for transcription factors NF-kappa B and AP-2 in the promoter region of the human heme oxygenase 1 gene.
Lavrovsky, Y., Schwartzman, M. L., Levere, R. D., Kappas, A., & Abraham, N. G. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.13.5987 · Cited by 403 · see citing works
The essential role of MEKK3 in TNF-induced NF-κB activation
Yang, J., Lin, Y., Guo, Z., Cheng, J., Huang, J. H., Deng, L., Liao, W. S. ‐., Chen, Z. J., Liu, Z. G., & Su, B. (2001) · Nature Immunology · doi:10.1038/89769 · Cited by 396 · see citing works
Self-citation
Glutathionylation of the p50 Subunit of NF-κB: a Mechanism for Redox-Induced Inhibition of DNA Binding
Pineda‐Molina, E., Klatt, P., Vázquez, J., Marina, A., de Lacoba, M. G., Pérez‐Sala, D., & Lamas, S. (2001) · Biochemistry · doi:10.1021/bi011459o · Cited by 389 · see citing works
Thioredoxin Promotes ASK1 Ubiquitination and Degradation to Inhibit ASK1-Mediated Apoptosis in a Redox Activity-Independent Manner
Liu, Y., & Wang, M. (2002) · Circulation Research · doi:10.1161/01.res.0000022160.64355.62 · Cited by 388 · see citing works
Nitric oxide represses inhibitory κB kinase through S-nitrosylation
Reynaert, N. L., Ckless, K., Korn, S. H., Vos, N., Guala, A. S., Wouters, E. F. �., van der Vliet, A., & Janssen-Heininger, Y. M. W. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400588101 · Cited by 388 · see citing works
NF-κB Regulates Phagocytic NADPH Oxidase by Inducing the Expression of gp91
Anrather, J., Racchumi, G., & Iadecola, C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m506172200 · Cited by 387 · see citing works
Controlled Elimination of Intracellular H 2 O2: Regulation of Peroxiredoxin, Catalase, and Glutathione Peroxidase via Post-translational Modification
Rhee, S. G., Yang, K.-S., Kang, S. W., Woo, H. A., & Chang, T.-S. (2005) · Antioxidants & Redox Signaling · doi:10.1089/ars.2005.7.619 · Cited by 376 · see citing works
Manganese superoxide dismutase in disease
MacMillan-Crow, L. A., & Cruthirds, D. L. (2001) · Free Radical Research · doi:10.1080/10715760100300281 · Cited by 371 · see citing works
Reactive oxygen species mediate crosstalk between NF-κB and JNK
Nakano, H., Nakajima, A., Sakon-Komazawa, S., Piao, J.-H., Xue, X., & Okumura, K. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401830 · Cited by 367 · see citing works
Compartmentalization of Redox Signaling Through NADPH Oxidase–Derived ROS
Ushio‐Fukai, M. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2333 · Cited by 365 · see citing works
Inhibition of NF-κB Activation by Arsenite through Reaction with a Critical Cysteine in the Activation Loop of IκB Kinase
Kapahi, P., Takahashi, T., Natoli, G., Adams, S., Chen, Y., Tsien, R. Y., & Karin, M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m007204200 · Cited by 359 · see citing works
NFκB and AP-1 mediate transcriptional responses to oxidative stress in skeletal muscle cells
Zhou, L. Z.-H., Johnson, A. P., & Rando, T. A. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00719-5 · Cited by 323 · see citing works
Thioredoxin‐2 (TRX‐2) is an essential gene regulating mitochondria‐dependent apoptosis
Tanaka, T., Hosoi, F., Yamaguchi‐Iwai, Y., Nakamura, H., Masutani, H., Ueda, S., Nishiyama, A., Takeda, S., Wada, H., Spyrou, G., et al. (2002) · The EMBO Journal · doi:10.1093/emboj/21.7.1695 · Cited by 322 · see citing works
Glutaredoxin Exerts an Antiapoptotic Effect by Regulating the Redox State of Akt*
Murata, H., Ihara, Y., Nakamura, H., Yodoi, J., Sumikawa, K., & Kondo, T. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m310171200 · Cited by 304 · see citing works
Induction of p100 Processing by NF-κB-inducing Kinase Involves Docking IκB Kinase α (IKKα) to p100 and IKKα-mediated Phosphorylation
Xiao, G., Fong, A., & Sun, S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401428200 · Cited by 296 · see citing works
Involvement of regulatory and catalytic subunits of phosphoinositide 3-kinase in NF-κB activation
Béraud, C., Henzel, W. J., & Baeuerle, P. A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.2.429 · Cited by 277 · see citing works
MEK kinase 1 is critically required for c-Jun N-terminal kinase activation by proinflammatory stimuli and growth factor-induced cell migration
Xia, Y., Makris, C., Su, B., Li, E., Yang, J., Nemerow, G. R., & Karin, M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.10.5243 · Cited by 276 · see citing works
Metabolic Regulation and Function of Glutathione Peroxidase-1
Lei, X. G., Cheng, W., & McClung, J. P. (2007) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.27.061406.093716 · Cited by 275 · see citing works
Reactive oxygen intermediates activate NF-kappa B in a tyrosine kinase- dependent mechanism and in combination with vanadate activate the p56lck and p59fyn tyrosine kinases in human lymphocytes
Schieven, G. L., Kirihara, J. M., Myers, D. E., Ledbetter, J. A., & Uckun, F. M. (1993) · Blood · doi:10.1182/blood.v82.4.1212.1212 · Cited by 264 · see citing works
Crucial role of the amino-terminal tyrosine residue 42 and the carboxyl-terminal PEST domain of IκBα in NF-κB activation by an oxidative stress
Schoonbroodt, S., Ferreira, V., Best-Belpomme, M., Boelaert, J. R., Legrand-Poels, S., Korner, M., & Piette, J. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.164.8.4292 · Cited by 263 · see citing works
Sphingosine-1-Phosphate Induces an Antiinflammatory Phenotype in Macrophages
Hughes, J., Srinivasan, S., Lynch, K., Proia, R., Ferdek, P., & Hedrick, C. (2008) · Circulation Research · doi:10.1161/circresaha.107.170779 · Cited by 253 · see citing works
Tumor Necrosis Factor Alpha and Interleukin-1β Regulate the Murine Manganese Superoxide Dismutase Gene Through a Complex Intronic Enhancer Involving C/EBP-β and NF-κB
Jones, P. L., Ping, D., & Boss, J. M. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.12.6970 · Cited by 244 · see citing works
Free radical scavenging actions of metallothionein isoforms I and II
Kumari, M. V. R., Hiramatsu, M., & Ebadi, M. (1998) · Free Radical Research · doi:10.1080/10715769800300111 · Cited by 243 · see citing works
The NF-κB-mediated control of the JNK cascade in the antagonism of programmed cell death in health and disease
Papa, S., Bubici, C., Zazzeroni, F., Pham, C. G., Kuntzen, C., Knabb, J. R., Dean, K., & Franzoso, G. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401865 · Cited by 236 · see citing works
NOS2 Regulation of NF-κB by S-Nitrosylation of p65
Kelleher, Z. T., Matsumoto, A., Stamler, J. S., & Marshall, H. E. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705929200 · Cited by 234 · see citing works
The ankyrin repeat domains of the NF-kappa B precursor p105 and the protooncogene bcl-3 act as specific inhibitors of NF-kappa B DNA binding.
Hatada, E. N., Nieters, A., Wulczyn, F. G., Naumann, M., Meyer, R., Nucifora, G., McKeithan, T. W., & Scheidereit, C. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.6.2489 · Cited by 234 · see citing works
Generation of Reactive Oxygen Species during the Enzymatic Oxidation of Polycyclic Aromatic Hydrocarbon trans-Dihydrodiols Catalyzed by Dihydrodiol Dehydrogenase
Penning, T. M., Ohnishi, S. T., Ohnishi, T., & Harvey, R. G. (1996) · Chemical Research in Toxicology · doi:10.1021/tx950055s · Cited by 234 · see citing works
Spatial Redox Regulation of a Critical Cysteine Residue of NF-κB in Vivo
Nishi, T., Shimizu, N., Hiramoto, M., Sato, I., Yamaguchi, Y., Hasegawa, M., Aizawa, S., Tanaka, H., Kataoka, K., Watanabe, H., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202970200 · Cited by 227 · see citing works
Redox Regulation of Nuclear Post-Translational Modifications During NF-κB Activation
Gloire, G., & Piette, J. G. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2463 · Cited by 220 · see citing works
Dual Role of Mitochondrial Reactive Oxygen Species in Hypoxia Signaling: Activation of Nuclear Factor-κB via c-SRC– and Oxidant-Dependent Cell Death
Lluis, J. M., Buricchi, F., Chiarugi, P., Morales, A., & Fernández-Checa, J. C. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-0515 · Cited by 220 · see citing works
Interleukin-1β Induction of NFκB Is Partially Regulated by H2O2-mediated Activation of NFκB-inducing Kinase
Li, Q., & Engelhardt, J. F. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511153200 · Cited by 219 · see citing works
Recruitment of Tumor Necrosis Factor Receptor-associated Factor Family Proteins to Apoptosis Signal-regulating Kinase 1 Signalosome Is Essential for Oxidative Stress-induced Cell Death
Noguchi, T., Takeda, K., Matsuzawa, A., Saegusa, K., Nakano, H., Gohda, J., Inoue, J., & Ichijo, H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506771200 · Cited by 218 · see citing works
Regulation of Cu/Zn-Superoxide Dismutase Expression via the Phosphatidylinositol 3 Kinase/Akt Pathway and Nuclear Factor-κB
Rojo, A. I., Salinas, M., Martı́n, D., Perona, R., & Cuadrado, A. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.2111-04.2004 · Cited by 216 · see citing works
Role of peroxynitrite in the redox regulation of cell signal transduction pathways
Liaudet, L. (2009) · Frontiers in bioscience · doi:10.2741/3569 · Cited by 214 · see citing works
CYP2E1-dependent toxicity and oxidative stress in HepG2 cells,
Cederbaum, A. I. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00743-2 · Cited by 210 · see citing works
Cytochrome P450 2E1-derived Reactive Oxygen Species Mediate Paracrine Stimulation of Collagen I Protein Synthesis by Hepatic Stellate Cells
Nieto, N., Friedman, S. L., & Cederbaum, A. I. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110506200 · Cited by 208 · see citing works
TNFα and reactive oxygen species in necrotic cell death
Morgan, M. J., Kim, Y., & Liu, Z.-G. (2008) · Cell Research · doi:10.1038/cr.2008.31 · Cited by 202 · see citing works
Self-citation
Cytokine-induced Activation of Nuclear Factor-κB Is Inhibited by Hydrogen Peroxide through Oxidative Inactivation of IκB Kinase
Korn, S. H., Wouters, E. F. �., Vos, N., & Janssen-Heininger, Y. M. W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104321200 · Cited by 200 · see citing works
Mechanisms of crosstalk between TNF-induced NF-κB and JNK activation in hepatocytes
Wullaert, A., Heyninck, K., & Beyaert, R. (2006) · Biochemical Pharmacology · doi:10.1016/j.bcp.2006.07.003 · Cited by 200 · see citing works
Reactive Oxygen Species in TNFα-Induced Signaling and Cell Death
Morgan, M. J., & Liu, Z.-G. (2010) · Molecules and Cells · doi:10.1007/s10059-010-0105-0 · Cited by 198 · see citing works
Self-citation
Molecular Basis of Heme Oxygenase-1 Induction: Implications for Chemoprevention and Chemoprotection
Prawan, A., Kundu, J. K., & Surh, Y. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.1688 · Cited by 195 · see citing works
TNF-α-induced NF-κB/RelA Ser276 phosphorylation and enhanceosome formation is mediated by an ROS-dependent PKAc pathway
Jamaluddin, M., Wang, S., Boldogh, I. R., Tian, B., & Brasier, A. R. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2007.01.020 · Cited by 185 · see citing works
Hydrogen peroxide formation and stoichiometry of hydroxylation reactions catalyzed by highly purified liver microsomal cytochrome P-450
Nordblom, G. D., & Coon, M. J. (1977) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(77)90047-9 · Cited by 185 · see citing works
Transcriptional Role of the Nuclear Factor κB Site in the Induction by Lipopolysaccharide and Suppression by Dexamethasone of Cyclooxygenase-2 in U937 Cells
Inoue, H., & Tanabe, T. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8222 · Cited by 185 · see citing works
Tyrosine Phosphorylation of IκBα Activates NFκB through a Redox-regulated and c-Src-dependent Mechanism Following Hypoxia/Reoxygenation
Fan, C., Li, Q., Ross, D., & Engelhardt, J. F. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m206718200 · Cited by 183 · see citing works
Hydrogen peroxide activates IκB kinases through phosphorylation of serine residues in the activation loops
Kamata, H., Manabe, T., Oka, S., Kamata, K., & Hirata, H. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02712-6 · Cited by 179 · see citing works
Turning point in apoptosis/necrosis induced by hydrogen peroxide
Saito, Y., Nishio, K., Ogawa, Y., Kimata, J., Kinumi, T., Yoshida, Y., Noguchi, N., & Niki, E. (2006) · Free Radical Research · doi:10.1080/10715760600632552 · Cited by 178 · see citing works
RelA Ser 276 Phosphorylation Is Required for Activation of a Subset of NF-κB-Dependent Genes by Recruiting Cyclin-Dependent Kinase 9/Cyclin T1 Complexes
Nowak, D. E., Tian, B., Jamaluddin, M., Boldogh, I. R., Vergara, L. A., Choudhary, S., & Brasier, A. R. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01152-07 · Cited by 176 · see citing works
Coordinated binding of NF-κB family members in the response of human cells to lipopolysaccharide
Schreiber, J., Jenner, R. G., Murray, H. L., Gerber, G. K., Gifford, D. K., & Young, R. A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510996103 · Cited by 175 · see citing works
The expanding role of NADPH oxidases in health and disease: no longer just agents of death and destruction
Quinn, M. T., Ammons, M. C. B., & DeLeo, F. R. (2006) · Clinical Science · doi:10.1042/cs20060059 · Cited by 175 · see citing works
Redox regulation of protein-tyrosine phosphatases
den Hertog, J., Groen, A. J., & WIJK, T. V. D. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2004.05.024 · Cited by 172 · see citing works
Activation of NF-kappa B and elevation of MnSOD gene expression by thiol reducing agents in lung adenocarcinoma (A549) cells
Das, K. C., Lewis-Molock, Y., & White, C. W. (1995) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1995.269.5.l588 · Cited by 168 · see citing works
Oxidative Stress Induces NF- B Nuclear Translocation Without Degradation of I B
Canty, T. G., Boyle, E. M., Farr, A. G., Morgan, E. N., Verrier, E. D., & Pohlman, T. H. (1999) · Circulation · doi:10.1161/01.cir.100.suppl_2.ii-361 · Cited by 167 · see citing works
A new APE1/Ref-1-dependent pathway leading to reduction of NF- B and AP-1, and activation of their DNA-binding activity
Ando, K., Hirao, S., Kabe, Y., Ogura, Y., Sato, I., Yamaguchi, Y., Wada, T., & Handa, H. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn416 · Cited by 155 · see citing works
Essential role of TAK1 in thymocyte development and activation
Liu, H.-H., Xie, M., Schneider, M. D., & Chen, Z. J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603089103 · Cited by 155 · see citing works
Role of cysteine62in DNA recognition by the P50 subunit of NF-xB
Matthews, J. R., Kaszubska, W., Turcatti, G., Wells, T. N. C., & Hay, R. T. (1993) · Nucleic Acids Research · doi:10.1093/nar/21.8.1727 · Cited by 147 · see citing works
Up-regulation of p300 Binding and p50 Acetylation in Tumor Necrosis Factor-α-induced Cyclooxygenase-2 Promoter Activation
Deng, W., Zhu, Y., & Wu, K. K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209286200 · Cited by 146 · see citing works
The Absence of NF-κB-Mediated Inhibition of c-Jun N-Terminal Kinase Activation Contributes to Tumor Necrosis Factor Alpha-Induced Apoptosis
Tang, F., Tang, G., Xiang, J., Dai, Q., Rosner, M. R., & Lin, A. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.24.8571-8579.2002 · Cited by 145 · see citing works
Differential Oxidation of Protein-tyrosine Phosphatases
Groen, A. J., Lemeer, S., van der Wijk, T., Overvoorde, J., Heck, A. J. R., Östman, A., Barford, D., Slijper, M., & den Hertog, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m412424200 · Cited by 142 · see citing works
TAK1 Is Recruited to the Tumor Necrosis Factor-α (TNF-α) Receptor 1 Complex in a Receptor-interacting Protein (RIP)-dependent Manner and Cooperates with MEKK3 Leading to NF-κB Activation
Blonska, M., Shambharkar, P. B., Kobayashi, M., Zhang, D., Sakurai, H., Su, B., & Lin, X. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507807200 · Cited by 142 · see citing works
NF‐κB activation prevents apoptotic oxidative stress via an increase of both thioredoxin and MnSOD levels in TNFα‐treated Ewing sarcoma cells
Djavaheri‐Mergny, M., Javelaud, D., Wietzerbin, J., & Besançon, F. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.10.082 · Cited by 134 · see citing works
Genetic Deletion of NAD(P)H:Quinone Oxidoreductase 1 Abrogates Activation of Nuclear Factor-κB, IκBα Kinase, c-Jun N-terminal Kinase, Akt, p38, and p44/42 Mitogen-activated Protein Kinases and Potentiates Apoptosis
Ahn, K. S., Sethi, G., Jain, A. K., Jaiswal, A. K., & Aggarwal, B. B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601162200 · Cited by 134 · see citing works
Hydrogen Peroxide-Induced Apoptosis and Necrosis in Human Lung Fibroblasts: Protective Roles of Glutathione
Teramoto, S., Tetsuji, T., Matsui, H., Ohga, E., Takeshi, M., & Yasuyoshi, O. (1999) · The Japanese Journal of Pharmacology · doi:10.1254/jjp.79.33 · Cited by 132 · see citing works
Divergent gene regulation and growth effects by NF-κB in epithelial and mesenchymal cells of human skin
Hinata, K., Gervin, A. M., Zhang, J. Y., & Khavari, P. A. (2003) · Oncogene · doi:10.1038/sj.onc.1206198 · Cited by 130 · see citing works
Mechanisms of cytochrome P450 regulation by inflammatory mediators
Morgan, E. T., Li-Masters, T., & Cheng, P. (2002) · Toxicology · doi:10.1016/s0300-483x(02)00283-4 · Cited by 126 · see citing works
Redox-Linked Signal Transduction Pathways for Protein Tyrosine Kinase Activation
Nakashima, I., Kato, M., Akhand, A. A., Suzuki, H., Takeda, K., Hossain, K., & Kawamoto, Y. (2002) · Antioxidants and Redox Signaling · doi:10.1089/15230860260196326 · Cited by 124 · see citing works
N-terminal DNA-binding domains contribute to differential DNA-binding specificities of NF-kappa B p50 and p65.
Tolédano, M. B., Ghosh, D., Trinh, F., & Leonard, W. J. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.2.852 · Cited by 124 · see citing works
Biochemical and cellular toxicology of peroxynitrite: implications in cell death and autoimmune phenomenon
Ahmad, R., Rasheed, Z., & Ahsan, H. (2009) · Immunopharmacology and Immunotoxicology · doi:10.1080/08923970802709197 · Cited by 118 · see citing works
The organization of the human GSTP1-1 gene promoter and its response to retinoic acid and cellular redox status
Xia, C., Hu, J., KETTERER, B., & Taylor, J. B. (1996) · Biochemical Journal · doi:10.1042/bj3130155 · Cited by 112 · see citing works
Lipid Rafts and Oxidative Stress–Induced Cell Death
Morgan, M. J., Kim, Y., & Liu, Z.-G. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1658 · Cited by 99 · see citing works
Self-citation
Molecular Cloning and Characterization of the Human Xanthine Dehydrogenase Gene (XDH)
Xu, P., Huecksteadt, T. P., & Hoidal, J. R. (1996) · Genomics · doi:10.1006/geno.1996.0262 · Cited by 99 · see citing works
Role of the NF-κB Signaling Pathway and κBcis-Regulatory Elements on theIRF-1andiNOSPromoter Regions in Mycobacterial Lipoarabinomannan Induction of Nitric Oxide
Morris, K. R., Lutz, R. D., Choi, H.-S., Kamitani, T., Chmura, K., & Chan, E. D. (2003) · Infection and Immunity · doi:10.1128/iai.71.3.1442-1452.2003 · Cited by 98 · see citing works
Reactive Oxygen Species Mediate Liver Injury Through Parenchymal Nuclear Factor-κB Inactivation in Prolonged Ischemia/Reperfusion
Llacuna, L., Marı́, M., Lluis, J. M., García‐Ruiz, C., Fernández-Checa, J. C., & Morales, A. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2009.080857 · Cited by 97 · see citing works
Sustained oxidative stress inhibits NF-κB activation partially via inactivating the proteasome
Wu, M., Bian, Q., Liu, Y., Fernandes, A. F., Taylor, A., Pereira, P., & Shang, F. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.09.021 · Cited by 97 · see citing works
Hydrogen Peroxide Has Opposing Effects on IKK Activity and I κ B α Breakdown in Airway Epithelial Cells
Jaspers, I., Zhang, W., Fraser, A., Samet, J. M., & Reed, W. (2001) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.24.6.4344 · Cited by 91 · see citing works
Cytosolic phospholipase A2, lipoxygenase metabolites, and reactive oxygen species
Kim, C.-M., Kim, J., & Kim, J. (2008) · BMB Reports · doi:10.5483/bmbrep.2008.41.8.555 · Cited by 90 · see citing works
Intermolecular disulfide bond formation in the nemo dimer requires cys54 and cys347
Herscovitch, M., Comb, W., Ennis, T., Coleman, K., Yong, S., Armstead, B., Kalaitzidis, D., Chandani, S., & Gilmore, T. D. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.12.123 · Cited by 89 · see citing works
Statin Treatment Upregulates Vascular Neuronal Nitric Oxide Synthase Through Akt/NF-κB Pathway
Nakata, S., Tsutsui, M., Shimokawa, H., Yamashita, T., Tanimoto, A., Tasaki, H., Ozumi, K., Sabanai, K., Morishita, T., Suda, O., et al. (2006) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000251615.61858.33 · Cited by 85 · see citing works
Mammalian Cytosolic Glutathione Transferases
Dourado, D. F. A. R., Fernandes, P. A., & Ramos, M. J. (2008) · Current Protein and Peptide Science · doi:10.2174/138920308785132677 · Cited by 83 · see citing works
The p65/RelA Subunit of NF-κB Suppresses the Sustained, Antiapoptotic Activity of Jun Kinase Induced by Tumor Necrosis Factor
Reuther-Madrid, J. Y., Kashatus, D. F., Chen, S., Li, X., Westwick, J. K., Davis, R. J., Earp, H. S., Wang, C.-Y., & Baldwin, A. S. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.23.8175-8183.2002 · Cited by 81 · see citing works
GlutathioneS-Transferase π1 Promotes Tumorigenicity in HCT116 Human Colon Cancer Cells
Dang, D. T., Chen, F., Kohli, M., Rago, C., Cummins, J. M., & Dang, L. H. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-1930 · Cited by 80 · see citing works
SENP1 mediates TNF-induced desumoylation and cytoplasmic translocation of HIPK1 to enhance ASK1-dependent apoptosis
Li, X., Luo, Y., Yu, L., Lin, Y., Luo, D., Zhang, H., He, Y., Kim, Y. K., Kim, Y., Tang, S., et al. (2008) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402303 · Cited by 79 · see citing works
Dual effect of oxidative stress on NF-κB activation in HeLa cells
Byun, M.-S., Jeon, K., Choi, J.-W., Shim, J.-Y., & Jue, D. (2002) · Experimental & Molecular Medicine · doi:10.1038/emm.2002.47 · Cited by 79 · see citing works
Dihydrodiol dehydrogenases regulate the generation of reactive oxygen species and the development of cisplatin resistance in human ovarian carcinoma cells
Chen, J., Adikari, M., Pallai, R., Parekh, H. K., & Simpkins, H. (2007) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-007-0554-0 · Cited by 74 · see citing works
IκBα and IκBβ possess injury context-specific functions that uniquely influence hepatic NF-κB induction and inflammation
Fan, C., Li, Q., Zhang, Y., Liu, X., Luo, M., Abbott, D., Zhou, W., & Engelhardt, J. F. (2004) · Journal of Clinical Investigation · doi:10.1172/jci17337 · Cited by 73 · see citing works
Redox control of catalytic activities of membrane-associated protein tyrosine kinases
Nakashima, I., Takeda, K., Kawamoto, Y., Okuno, Y., Kato, M., & Suzuki, H. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2004.06.016 · Cited by 72 · see citing works
Role of phenobarbital-inducible cytochrome P450s as a source of active oxygen species in DNA-oxidation
Imaoka, S., Osada, M., Minamiyama, Y., Yukimura, T., Toyokuni, S., Takemura, S., Hiroi, T., & Funae, Y. (2003) · Cancer Letters · doi:10.1016/j.canlet.2003.09.009 · Cited by 71 · see citing works
X-linked inhibitor of apoptosis protein increases mitochondrial antioxidants through NF-κB activation
Kairisalo, M., Korhonen, L., Blomgren, K., & Lindholm, D. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.09.115 · Cited by 69 · see citing works
Transcriptional Regulation of the Human iNOS Gene in Vascular-Smooth-Muscle Cells and Macrophages: Evidence for Tissue Specificity
Kolyada, A. Y., Savikovsky, N., & Madias, N. E. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.0449 · Cited by 69 · see citing works
Identification of a classic cytokine‐induced enhancer upstream in the human iNOS promoter
Guo, Z., Shao, L., Du, Q., Park, K. S., & Geller, D. A. (2006) · The FASEB Journal · doi:10.1096/fj.06-6739com · Cited by 68 · see citing works
Glutathionylation regulates IκB
Kil, I. S., Kim, S. Y., & Park, J. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.06.007 · Cited by 67 · see citing works
Hydrogen Peroxide Induces Necrosis, Apoptosis, Oncosis and Apoptotic Oncosis of Mouse Terminal Proximal Straight Tubule Cells
Takeda, M., Shirato, I., Kobayashi, M., & Endou, H. (1999) · The Nephron journals/Nephron journals · doi:10.1159/000045282 · Cited by 66 · see citing works
Transforming growth factor-β1 stimulates heme oxygenase-1 expression via the PI3K/Akt and NF-κB pathways in human lung epithelial cells
Lin, C.-C., Chiang, L.-L., Lin, C., Shih, C.-H., Liao, Y., Hsu, M., & Chen, B.-C. (2007) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2007.01.025 · Cited by 62 · see citing works
Inducible expression of 15-lipoxygenase-2 and 8-lipoxygenase inhibits cell growth via common signaling pathways
Schweiger, D., Fürstenberger, G., & Krieg, P. (2006) · Journal of Lipid Research · doi:10.1194/jlr.m600311-jlr200 · Cited by 54 · see citing works
Thiol oxidation of cell signaling proteins: Controlling an apoptotic equilibrium
Cross, J. V., & Templeton, D. J. (2004) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20202 · Cited by 54 · see citing works
The transcriptional regulation of human arachidonate 12‐lipoxygenase gene by NFκB/Rel
Arakawa, T., Nakamura, M., Yoshimoto, T., & Yamamoto, S. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00293-i · Cited by 46 · see citing works
Neuronal growth‐inhibitory factor (metallothionein‐3): evaluation of the biological function of growth‐inhibitory factor in the injured and neurodegenerative brain
Howells, C., West, A. K., & Chung, R. S. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07718.x · Cited by 43 · see citing works
DNA-binding activity of NF-κB and phosphorylation of p65 are induced by N-acetylcysteine through phosphatidylinositol (PI) 3-kinase
Liu, J., Yoshida, Y., & Yamashita, U. (2008) · Molecular Immunology · doi:10.1016/j.molimm.2008.06.012 · Cited by 41 · see citing works
Regulation of neuronal nitric oxide synthase exon 1f gene expression by nuclear factor‐κB acetylation in human neuroblastoma cells
Li, Y., Zhao, Y., Li, G., Wang, J., Li, T., Li, W., & Lu, J. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04407.x · Cited by 41 · see citing works
Iron-mediated H2O2 Production as a Mechanism for Cell Type-specific Inhibition of Tumor Necrosis Factor α-Induced but Not Interleukin-1β-induced IκB Kinase Complex/Nuclear Factor-κB Activation
Panopoulos, A., Harraz, M. M., Engelhardt, J. F., & Zandi, E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409524200 · Cited by 39 · see citing works
D-MEKK1, the Drosophila orthologue of mammalian MEKK4/MTK1, and Hemipterous/D-MKK7 mediate the activation of D-JNK by cadmium and arsenite in Schneider cells
Ryabinina, O. P., Subbian, E., & Iordanov, M. S. (2006) · BMC Cell Biology · doi:10.1186/1471-2121-7-7 · Cited by 36 · see citing works
Determination of interleukin-4-responsive region in the human cytochrome P450 2E1 gene promoter
Abdel‐Razzak, Z., Garlatti, M., Aggerbeck, Μ., & Barouki, R. (2004) · Biochemical Pharmacology · doi:10.1016/j.bcp.2004.06.003 · Cited by 29 · see citing works
NADH oxidase activity of rat liver xanthine dehydrogenase and xanthine oxidase—contribution for damage mechanisms
Maia, L. B., Vala, A., & Mira, L. (2005) · Free Radical Research · doi:10.1080/10715760500210962 · Cited by 29 · see citing works
Cloning of the guinea pig 5-lipoxygenase gene and nucleotide sequence of its promoter
Chopra, A., Ferreira-Alves, D. L., Sirois, P., & Thirion, J. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)91651-6 · Cited by 28 · see citing works
Involvement of activator protein-1 and nuclear factor-kappaB transcription factors in the control of the DT-diaphorase expression induced by mitomycin C treatment.
Yao, K.-S., Hageboutros, A., Ford, P., & O'Dwyer, P. J. (1997) · PubMed · Cited by 28 · see citing works
Phosphorylation and hypoxia-induced heme oxygenase-1 gene expression in cardiomyocytes
Wu, G., Marı́n-Garcı́a, J., Rogers, T. B., Lakatta, E. G., & Long, X. (2004) · Journal of Cardiac Failure · doi:10.1016/j.cardfail.2004.02.002 · Cited by 21 · see citing works
Tumour necrosis factor-α stimulates dehydroepiandrosterone metabolism in human fibroblast-like synoviocytes: a role for nuclear factor-κB and activator protein-1 in the regulation of expression of cytochrome p450 enzyme 7b
Dulos, J., Kaptein, A., Kavelaars, A., Heijnen, C. J., & Boots, A. M. H. (2005) · Arthritis Research & Therapy · doi:10.1186/ar1819 · Cited by 19 · see citing works
Promoter Analysis of a Human Dihydrodiol Dehydrogenase
Ciaccio, P. J., Walsh, E. S., & Tew, K. D. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.1693 · Cited by 18 · see citing works
Involvement of Activator Protein-1 and Nuclear Factor-κB Transcription Factors in the Control of the DT-Diaphorase Expression Induced by Mitomycin C Treatment
Yao, K.-S., Hageboutros, A., Ford, P., & O'Dwyer, P. J. (1997) · Molecular Pharmacology · doi:10.1016/s0026-895x(24)13483-9 · Cited by 11 · see citing works

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Research works printed but not linked: 12

Hayden MS, Ghosh S. Shared principles in NF-kappaB sig- naling. Cell 2008; 132:344-362.
Xiao G, Fong A, Sun SC. Induction of p100 processing by NF-kappaB-inducing kinase involves docking IkappaB kinase alpha (IKKalpha) to p100 and IKKalpha-mediated phospho- rylation. J Biol Chem 2004; 279:30099-30105.
Dourado DF, Fernandes PA, Ramos MJ. Mammalian cyto- solic glutathione transferases. Curr Protein Pept Sci 2008; 9:325-337.
Morris KR, Lutz RD, Choi HS, et al. Role of the NF-kappaB signaling pathway and kappaB cis-regulatory elements on the IRF-1 and iNOS promoter regions in mycobacterial lipoara- binomannan induction of nitric oxide. Infect Immun 2003; 71:1442-1452.
Kim C, Kim JY, Kim JH. Cytosolic phospholipase A(2), li- poxygenase metabolites, and reactive oxygen species. BMB Rep 2008; 41:555-559.
Thurman RG, Ley HG, Scholz R. Hepatic microsomal etha- nol oxidation. Hydrogen peroxide formation and the role of catalase. Eur J Biochem 1972; 25:420-430.
Matthews JR, Kaszubska W, Turcatti G, Wells TN, Hay RT. Role of cysteine62 in DNA recognition by the P50 subunit of NF-kappa B. Nucleic Acids Res 1993; 21:1727-1734. 115
Matthews JR, Botting CH, Panico M, Morris HR, Hay RT. In- hibition of NF-kappaB DNA binding by nitric oxide. Nucleic Acids Res 1996; 24:2236-2242. 121
Imbert V, Rupec RA, Livolsi A, et al. Tyrosine phosphoryla- tion of I kappa B-alpha activates NF-kappa B without prote- olytic degradation of I kappa B-alpha. Cell 1996; 86:787-798. 134
Kil IS, Kim SY, Park JW. Glutathionylation regulates Ikap- paB. Biochem Biophys Res Commun 2008; 373:169-173. 140
Wu M, Bian Q, Liu Y, et al. Sustained oxidative stress inhib- its NF-kappaB activation partially via inactivating the protea- some. Free Radic Biol Med 2009; 46:62-69. 141
Takaesu G, Surabhi RM, Park KJ, et al. TAK1 is critical for IkappaB kinase-mediated activation of the NF-kappaB path- way. J Mol Biol 2003; 326:105-115. 160

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Neufeldt, C. J., Cerikan, B., Cortese, M., Frankish, J., Lee, J., Płóciennikowska, A., Heigwer, F., Prasad, V. R., Joecks, S., Burkart, S. S., et al. (2022) · Communications Biology · doi:10.1038/s42003-021-02983-5 · Cited by 279 · see citing works
Phytochemicals as inhibitors of NF-κB for treatment of Alzheimer’s disease
Seo, E.-J., Fischer, N., & Efferth, T. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2017.11.030 · Cited by 265 · see citing works
The brain as an insulin-sensitive metabolic organ
Milstein, J. L., & Ferris, H. A. (2021) · Molecular Metabolism · doi:10.1016/j.molmet.2021.101234 · Cited by 269 · see citing works
NF‐κB signalling pathways in nucleus pulposus cell function and intervertebral disc degeneration
Zhang, G., Liu, M., Chen, H., Wu, Z., Gao, Y., Ma, Z., He, X., & Kang, X. (2021) · Cell Proliferation · doi:10.1111/cpr.13057 · Cited by 263 · see citing works
Insulin Resistance and Oxidative Stress in the Brain: What’s New?
Maciejczyk, M., Żebrowska, E., & Chabowski, A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20040874 · Cited by 262 · see citing works
Cytomegalovirus Latency and Reactivation: An Intricate Interplay With the Host Immune Response
Forte, E., Zhang, Z., Thorp, E. B., & Hummel, M. (2020) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.00130 · Cited by 259 · see citing works
Oxidative stress in sepsis: Pathophysiological implications justifying antioxidant co-therapy.
Prauchner, C. A. (2017) · Burns · doi:10.1016/j.burns.2016.09.023 · Cited by 252 · see citing works
Emerging Role of Sirtuin 2 in the Regulation of Mammalian Metabolism
Gomes, P., Outeiro, T. F., & Cavadas, C. (2015) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2015.08.001 · Cited by 253 · see citing works
Beyond Hemostasis: Platelet Innate Immune Interactions and Thromboinflammation
Mandel, J., Casari, M., Stepanyan, M. G., Martyanov, A. A., & Deppermann, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23073868 · Cited by 267 · see citing works
The Necroptosis Adaptor RIPK3 Promotes Injury-Induced Cytokine Expression and Tissue Repair
Moriwaki, K., Balaji, S., McQuade, T. J., Malhotra, N., Kang, J., & Chan, F. K.-M. (2014) · Immunity · doi:10.1016/j.immuni.2014.09.016 · Cited by 251 · see citing works
Fatigue, Sleep, and Autoimmune and Related Disorders
Zielinski, M. R., Systrom, D. M., & Rose, N. R. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01827 · Cited by 266 · see citing works
Cystathionine Beta-Synthase (CBS) Contributes to Advanced Ovarian Cancer Progression and Drug Resistance
Bhattacharyya, S., Saha, S., Giri, K., Lanza, I. R., Nair, K. S., Jennings, N. B., Rodriguez‐Aguayo, C., Lopez‐Berestein, G., Basal, E., Weaver, A. L., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0079167 · Cited by 251 · see citing works
Urinary biomarkers of oxidative status
Il’yasova, D., Scarbrough, P. M., & Spasojević, I. (2012) · Clinica Chimica Acta · doi:10.1016/j.cca.2012.06.012 · Cited by 252 · see citing works

Reactive Oxygen Species Regulate NF-κB and JNK-Mediated Signaling Pathway
Li, Q. (2008) · Letters in Biotechnology · Cited by 1 · see citing works
Bidirectional regulation of NF-κB by reactive oxygen species: A role of unfolded protein response
Nakajima, S., & Kitamura, M. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.06.020 · Cited by 315 · see citing works
Mutual cross-talk between reactive oxygen species and nuclear factor-kappa B: molecular basis and biological significance
Bubici, C., Papa, S., Dean, K., & Franzoso, G. (2006) · Oncogene · doi:10.1038/sj.onc.1209936 · Cited by 399 · see citing works
Reactive Oxygen Species as Costimulatory Signals of Cytokine-Induced NF-κ B Activation Pathways
Baeuerle, P. A. (2000) · Elsevier eBooks · doi:10.1016/b978-012636670-9/50010-6 · Cited by 5 · see citing works
NF-κB in oxidative stress
Lingappan, K. (2018) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2017.11.002 · Cited by 1,051 · see citing works

Authors: Morgan, M. J., & Liu, Z.-G.
Affiliations: National Institutes of Health (US)
Corresponding author: Liu, Zheng-gang
ORCID: Liu, Zheng-gang
Venue: Cell Research
Publisher: Springer Science and Business Media LLC
Published: 2010-12-28
Volume: 21
Issue: 1
Pages: 103-115
ISSN: 1001-0602 (ISSN-L)
1748-7838
DOI: 10.1038/cr.2010.178
PMC: PMC3193400
OpenAlex: W2086667809
Cited by: 3,505
References: 165
Citations by year: 2026: 409 · 2025: 401 · 2024: 364 · 2023: 321 · 2022: 330 · 2021: 282 · 2020: 234 · 2019: 210 · 2018: 229 · 2017: 179 · 2016: 139 · 2015: 113 · 2014: 96 · 2013: 81 · 2012: 92
FWCI: 5.10
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springer.com/tdm (tdm)
Locations: Cell Research (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Cancer Institute
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
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
Keywords: reactive oxygen species, NF-κB signaling, redox signaling, inflammation, immunity, transcription factors, NF-κB target genes
MeSH terms: Antioxidants, Humans, Signal Transduction, NF-kappa B, Reactive Oxygen Species, Oxidative Stress

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