The DOI matches its Crossref record; 165 of the 165 references it cites were found in a registry or an index.
Crosstalk of reactive oxygen species and NF-κB signaling
Open accessAbstract
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
The cited source says what the claim attributes to it.
In the citing paper
“NF-κB can be co-regulated by multiple pathways including MAPK and PI3K/Akt to enhance transcriptional activity, thus promoting the expression of pro-inflammatory and pro-oxidant enzyme genes.239,243,244”
From Recent advances in Alzheimer's disease: Mechanisms, clinical trials and new drug development strategies. (2024) · cites this paper as [244]
In the citing paper
“The elevated concentrations of TNF-alpha, TNF-beta, LPS, IL-1beta and CD40 in peritoneal fluid in women with endometriosis promote processes such as adhesion, invasion, proliferation and angiogenesis that stimulate the development of the disease [155].”
From Endometriosis: Epidemiology, Classification, Pathogenesis, Treatment and Genetics (Review of Literature) (2021) · cites this paper as [155]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Shared Principles in NF-κB Signaling
Hayden, M. S., & Ghosh, S. (2008) · Cell · doi:10.1016/j.cell.2008.01.020 · Cited by 4,954
Oxidative stress: oxidants and antioxidants
Sies, H. (1997) · Experimental Physiology · doi:10.1113/expphysiol.1997.sp004024 · Cited by 4,577
NOX enzymes and the biology of reactive oxygen
Lambeth, J. D. (2004) · Nature Reviews Immunology · doi:10.1038/nri1312 · Cited by 3,125
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 2,635
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
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
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
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
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
Meyer, M., Schreck, R., & Baeuerle, P. A. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05850.x · Cited by 1,306
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 1,303
Zhong, H., Voll, R. E., & Ghosh, S. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80066-0 · Cited by 1,210
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
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
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
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
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 951
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
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 847
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 846
Nox proteins in signal transduction
Brown, D., & Griendling, K. K. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.07.023 · Cited by 837
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 836
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
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
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 757
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 747
Dinkova‐Kostova, A. T., & Talalay, P. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.03.019 · Cited by 726
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
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
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
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 647
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 647
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 615
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
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
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
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
Kabe, Y., Ando, K., Hirao, S., Yoshida, M., & Handa, H. (2005) · Antioxidants & Redox Signaling · doi:10.1089/ars.2005.7.395 · Cited by 585
Glutathione S-Transferases - A Review
Salinas, A. E., & Wong, M. G. (1999) · Current Medicinal Chemistry · doi:10.2174/0929867306666220208213032 · Cited by 556
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
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
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
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
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
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
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 490
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
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
Orchestrating Redox Signaling Networks through Regulatory Cysteine Switches
Paulsen, C. E., & Carroll, K. S. (2009) · ACS Chemical Biology · doi:10.1021/cb900258z · Cited by 487
Liao, G., Zhang, M., Harhaj, E. W., & Sun, S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403286200 · Cited by 480
Xanthine oxidase and xanthine dehydrogenase
Hille, R., & Nishino, T. (1995) · The FASEB Journal · doi:10.1096/fasebj.9.11.7649415 · Cited by 445
Koong, A. C., Chen, E. Y., & Giaccia, A. J. (1994) · PubMed · Cited by 445
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
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
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 410
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
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
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 397
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
Self-citationLiu, Y., & Wang, M. (2002) · Circulation Research · doi:10.1161/01.res.0000022160.64355.62 · Cited by 391
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 390
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
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
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 375
Manganese superoxide dismutase in disease
MacMillan-Crow, L. A., & Cruthirds, D. L. (2001) · Free Radical Research · doi:10.1080/10715760100300281 · Cited by 371
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 370
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
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
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
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
Xiao, G., Fong, A., & Sun, S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401428200 · Cited by 296
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 278
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
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
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
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
Jones, P. L., Ping, D., & Boss, J. M. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.12.6970 · Cited by 244
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
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 238
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 237
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
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
Penning, T. M., Ohnishi, S. T., Ohnishi, T., & Harvey, R. G. (1996) · Chemical Research in Toxicology · doi:10.1021/tx950055s · Cited by 234
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
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 224
Role of peroxynitrite in the redox regulation of cell signal transduction pathways
Liaudet, L. (2009) · Frontiers in bioscience · doi:10.2741/3569 · Cited by 219
Li, Q., & Engelhardt, J. F. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511153200 · Cited by 219
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 218
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
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 215
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 213
Self-citationCYP2E1-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
Nieto, N., Friedman, S. L., & Cederbaum, A. I. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110506200 · Cited by 208
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 204
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 203
Self-citationMechanisms 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 202
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 198
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
Nordblom, G. D., & Coon, M. J. (1977) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(77)90047-9 · Cited by 185
Inoue, H., & Tanabe, T. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8222 · Cited by 185
Quinn, M. T., Ammons, M. C. B., & DeLeo, F. R. (2006) · Clinical Science · doi:10.1042/cs20060059 · Cited by 183
Fan, C., Li, Q., Ross, D., & Engelhardt, J. F. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m206718200 · Cited by 183
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 183
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 181
Kamata, H., Manabe, T., Oka, S., Kamata, K., & Hirata, H. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02712-6 · Cited by 179
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 177
Redox regulation of protein-tyrosine phosphatases
den Hertog, J., Groen, A. J., & van der Wijk, T. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2004.05.024 · Cited by 175
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
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
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
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
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 147
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
Deng, W., Zhu, Y., & Wu, K. K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209286200 · Cited by 146
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
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
Djavaheri‐Mergny, M., Javelaud, D., Wietzerbin, J., & Besançon, F. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.10.082 · Cited by 139
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
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
Hinata, K., Gervin, A. M., Zhang, J. Y., & Khavari, P. A. (2003) · Oncogene · doi:10.1038/sj.onc.1206198 · Cited by 130
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
Tolédano, M. B., Ghosh, D., Trinh, F., & Leonard, W. J. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.2.852 · Cited by 126
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 125
Ahmad, R., Rasheed, Z., & Ahsan, H. (2009) · Immunopharmacology and Immunotoxicology · doi:10.1080/08923970802709197 · Cited by 118
Xia, C., Hu, J., KETTERER, B., & Taylor, J. B. (1996) · Biochemical Journal · doi:10.1042/bj3130155 · Cited by 112
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 101
Self-citationSustained 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 99
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
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 98
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 96
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 93
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
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
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 87
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
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
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
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
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
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 75
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
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
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 71
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
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
Kolyada, A. Y., Savikovsky, N., & Madias, N. E. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.0449 · Cited by 69
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
Takeda, M., Shirato, I., Kobayashi, M., & Endou, H. (1999) · The Nephron journals/Nephron journals · doi:10.1159/000045282 · Cited by 66
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
Schweiger, D., Fürstenberger, G., & Krieg, P. (2006) · Journal of Lipid Research · doi:10.1194/jlr.m600311-jlr200 · Cited by 54
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
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
Howells, C., West, A. K., & Chung, R. S. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07718.x · Cited by 43
Liu, J., Yoshida, Y., & Yamashita, U. (2008) · Molecular Immunology · doi:10.1016/j.molimm.2008.06.012 · Cited by 41
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
Panopoulos, A., Harraz, M. M., Engelhardt, J. F., & Zandi, E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409524200 · Cited by 39
Ryabinina, O. P., Subbian, E., & Iordanov, M. S. (2006) · BMC Cell Biology · doi:10.1186/1471-2121-7-7 · Cited by 36
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
Maia, L. B., Vala, A., & Mira, L. (2005) · Free Radical Research · doi:10.1080/10715760500210962 · Cited by 29
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
Yao, K.-S., Hageboutros, A., Ford, P., & O'Dwyer, P. J. (1997) · PubMed · Cited by 28
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
Dulos, J., Kaptein, A., Kavelaars, A., Heijnen, C. J., & Boots, A. M. H. (2005) · Arthritis Research & Therapy · doi:10.1186/ar1819 · Cited by 19
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
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
Flagged first, then by citations
Cited by
Sorted by citations
Ayala, A., Muñoz, M., & Argüelles, S. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/360438 · Cited by 6,837
Activation of apoptosis signalling pathways by reactive oxygen species
Redza-Dutordoir, M., & Averill-Bates, D. A. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.09.012 · Cited by 3,731
The complexity of NF-κB signaling in inflammation and cancer
Hoesel, B., & Schmid, J. A. (2013) · Molecular Cancer · doi:10.1186/1476-4598-12-86 · Cited by 3,277
Microbiota in health and diseases
Hou, K., Wu, Z.-X., Chen, X.-Y., Wang, J.-Q., Zhang, D., Xiao, C., Zhu, D., Koya, J. B., Wei, L., Li, J., et al. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-00974-4 · Cited by 3,171
Hayes, J. D., Dinkova-Kostova, A. T., & Tew, K. D. (2020) · Cancer Cell · doi:10.1016/j.ccell.2020.06.001 · Cited by 2,654
Metadata
- 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
- Published
- 2010-12-28
- Volume
- 21
- Issue
- 1
- Pages
- 103-115
- ISSN
- 1001-0602 (ISSN-L)
- 1748-7838
- 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
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