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Missing Pieces in the NF-κB Puzzle
Open accessAbstract
The regulation of the transcription factor NF-kappaB activity occurs at several levels including controlled cytoplasmic-nuclear shuttling and modulation of its transcriptional activity. A critical component in NF-kappaB regulation is the IkappaB kinase (IKK) complex. This review is focused on recent progress as well as unanswered questions regarding the regulation and function of NF-kappaB and IKK.
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“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 [2020]
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1 retracted
RETRACTED: DNA-PKcs Is Required for Activation of Innate Immunity by Immunostimulatory DNA
Chu, W., Gong, X., Li, Z.-W., Takabayashi, K., Ouyang, H., Chen, Y., Lois, A. F., Chen, D. J., Li, G. C., Karin, M., et al. (2000) · Cell · doi:10.1016/s0092-8674(00)00194-x · Cited by 178
Self-citationRetractedA Toll-like receptor recognizes bacterial DNA
Hemmi, H., Takeuchi, O., Kawai, T., Kaisho, T., Sato, S., Sanjo, H., Matsumoto, M., Hoshino, K., Wagner, H., Takeda, K., et al. (2000) · Nature · doi:10.1038/35047123 · Cited by 6,491
Recognition of double-stranded RNA and activation of NF-κB by Toll-like receptor 3
Alexopoulou, L., Holt, A. C., Medzhitov, R., & Flavell, R. A. (2001) · Nature · doi:10.1038/35099560 · Cited by 6,129
NF-κB AND REL PROTEINS: Evolutionarily Conserved Mediators of Immune Responses
Ghosh, S., May, M. J., & Kopp, E. B. (1998) · Annual Review of Immunology · doi:10.1146/annurev.immunol.16.1.225 · Cited by 5,182
Self-citationPhosphorylation meets ubiquitination: the control of NF-κB activity
Karin, M., & Ben-Neriah, Y. (2000) · Annual Review of Immunology · doi:10.1146/annurev.immunol.18.1.621 · Cited by 4,766
Self-citationNF-κB at the crossroads of life and death
Karin, M., & Lin, A. (2002) · Nature Immunology · doi:10.1038/ni0302-221 · Cited by 2,709
Self-citationTAK1 is a ubiquitin-dependent kinase of MKK and IKK
Wang, C., Deng, L., Hong, M., Akkaraju, G. R., Inoue, J.-I., & Chen, Z. J. (2001) · Nature · doi:10.1038/35085597 · Cited by 2,125
A cytokine-responsive IκB kinase that activates the transcription factor NF-κB
DiDonato, J. A., Hayakawa, M., Rothwarf, D. M., Zandi, E., & Karin, M. (1997) · Nature · doi:10.1038/41493 · Cited by 2,125
Self-citationIKK-1 and IKK-2: Cytokine-Activated IκB Kinases Essential for NF-κB Activation
Mercurio, F., Zhu, H., Murray, B. W., Shevchenko, A., Bennett, B. L., Li, J. W., Young, D. B., Barbosa, M. S., Mann, M., Manning, A. M., et al. (1997) · Science · doi:10.1126/science.278.5339.860 · Cited by 2,042
Deng, L., Wang, C., Spencer, E., Yang, L., Braun, A., You, J., Slaughter, C., Pickart, C., & Chen, Z. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00126-4 · Cited by 1,872
Cited by
Sorted by citations
Items 301–400 of 1,025
Ladner, K. J., Caligiuri, M. A., & D, D. C. G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m207129200 · Cited by 233
Schmidt‐Supprian, M., Tian, J. Y., Grant, E. P., Pasparakis, M., Maehr, R., Ovaa, H., Ploegh, H. L., Coyle, A. J., & Rajewsky, K. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400885101 · Cited by 232
Ramakrishnan, P., Wang, W., & Wallach, D. (2004) · Immunity · doi:10.1016/j.immuni.2004.08.009 · Cited by 232
Gan, B., Xu, P., Nagy, T., Alcaraz, A., Gu, H., & Guan, J. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200604129 · Cited by 239
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Maeda, S., & Omata, M. (2008) · Cancer Science · doi:10.1111/j.1349-7006.2008.00763.x · Cited by 236
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Mattioli, I., Sebald, A., Bucher, C., Charles, R., Nakano, H., Doi, T., Kracht, M., & Schmitz, M. L. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.10.6336 · Cited by 230
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Yu, B., Chang, J., Liu, Y., Li, J., Kevork, K., Al‐Hezaimi, K., Graves, D. T., Park, N.-H., & Wang, C. (2014) · Nature Medicine · doi:10.1038/nm.3586 · Cited by 235
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
Kaltschmidt, B., Ndiaye‐Lobry, D., Körte, M., Pothion, S., Arbibe, L., Prüllage, M., Pfeiffer, J., Lindecke, A., Staiger, V., Israël, A., et al. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.8.2936-2946.2006 · Cited by 230
NF-κB-mediated adaptive resistance to ionizing radiation
Ahmed, K. M., & Li, J.-J. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.09.022 · Cited by 222
“The newly synthesized IκB-α is able to enter the nucleus and remove NFκB from its DNA-binding sites and transport it back to the cytoplasm, thereby terminating the NF-κB-dependent gene transcription [48,49].”
NEMO–IKKβ Are Essential for IRF3 and NF-κB Activation in the cGAS–STING Pathway
Fang, R., Wang, C., Jiang, Q., Lv, M., Gao, P., Yu, X., Mu, P., Zhang, R., Bi, S., Feng, J., et al. (2017) · The Journal of Immunology · doi:10.4049/jimmunol.1700699 · Cited by 227
Michlewska, S., Dransfield, I., Megson, I. L., & Rossi, A. G. (2008) · The FASEB Journal · doi:10.1096/fj.08-121228 · Cited by 239
Liu, M., Sakamaki, T., Casimiro, M. C., Willmarth, N. E., Quong, A. A., Ju, X., Ojeifo, J. O., Jiao, X., Yeow, W.-S., Katiyar, S., et al. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-0732 · Cited by 226
Shakibaei, M., Buhrmann, C., & Mobasheri, A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.198713 · Cited by 230
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Wuertz‐Kozak, K., Vo, N. N., Kletsas, D., & Boos, N. (2012) · European Cells and Materials · doi:10.22203/ecm.v023a08 · Cited by 226
Ichikawa, H., Takada, Y., Shishodia, S., Bolleddula, J., Nair, M. G., & Aggarwal, B. B. (2006) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-06-0096 · Cited by 225
NF‐κB activation in human prostate cancer: Important mediator or epiphenomenon?
Suh, J., & Rabson, A. B. (2003) · Journal of Cellular Biochemistry · doi:10.1002/jcb.10729 · Cited by 226
“1A): c-Rel, RelA (p65), RelB, NF-kB1 (p50/p105), and NF-kB2 (p52/p100) (reviewed in Ghosh et al., 1998; Karin and Ben-Neriah, 2000; Ghosh and Karin, 2002).”
Mechanisms Generating Diversity in Glucocorticoid Receptor Signaling
Revollo, J. R., & Cidlowski, J. A. (2009) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2009.04986.x · Cited by 220
IKKα, IKKβ, and NEMO/IKKγ Are Each Required for the NF-κB-mediated Inflammatory Response Program
Li, X., Massa, P. E., Hanidu, A., Peet, G. W., Aro, P., Savitt, A., Mische, S. M., Li, J., & Marcu, K. B. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205165200 · Cited by 223
A Paradigm for Gene Regulation: Inflammation, NF-κB and PPAR
Vanden Berghe, W., Vermeulen, L., Delerive, P., De Bosscher, K., Staels, B., & Haegeman, G. (2003) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-9072-3_22 · Cited by 222
Khoshnan, A., Ko, J., Watkin, E. E., Paige, L. A., Reinhart, P. H., & Patterson, P. H. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.2675-04.2004 · Cited by 223
“PC12 cells, which express wild-type (WT) HDx1-enhanced green fluorescent protein (EGFP) with 25 glutamine repeats (25Qs) or mutant HDx1-EGFP with 103Qs in response to ecdysone, were kindly provided by Dr. E. Schweitzer (University of California Los Angeles).”
BackgroundMethodResultInfluentialTelomere-independent Rap1 is an IKK adaptor and regulates NF-κB-dependent gene expression
Teo, H., Ghosh, S., Luesch, H., Ghosh, A., Wong, E. T., Malik, N. B. A., Orth, A. P., Jesus, P. D. D., Perry, A. S., Oliver, J. D., et al. (2010) · Nature Cell Biology · doi:10.1038/ncb2080 · Cited by 229
Self-citationBroemer, M., Krappmann, D., & Scheidereit, C. (2004) · Oncogene · doi:10.1038/sj.onc.1207705 · Cited by 221
“While genetic data suggest that IKKb is the essential kinase subunit to phosphorylate IkB molecules in response to proinflammatory signals (Ghosh and Karin, 2002), selective functions ascribed to IKKa are to transmit morphogenic signals.”
BackgroundEndo, T., Nishio, M., Enzler, T., Cottam, H. B., Fukuda, T., James, D. F., Karin, M., & Kipps, T. J. (2006) · Blood · doi:10.1182/blood-2006-06-027755 · Cited by 225
Self-citationDixit, V. M., & Mak, T. W. (2002) · Cell · doi:10.1016/s0092-8674(02)01166-2 · Cited by 221
SMRT Derepression by the IκB Kinase α
Hoberg, J. E., Yeung, F., & Mayo, M. W. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.10.010 · Cited by 220
Chang, T.-H., Kubota, T., Matsuoka, M., Jones, S. J. M., Bradfute, S. B., Bray, M., & Ozato, K. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000493 · Cited by 230
Ectodysplasin signaling in development.
Mikkola, M. L., & Thesleff, I. (2003) · Cytokine & Growth Factor Reviews · doi:10.1016/s1359-6101(03)00020-0 · Cited by 217
Pro-inflammatory cytokines and their effects in the dentate gyrus
Pickering, M., & O’Connor, J. J. (2007) · Progress in Brain Research · doi:10.1016/s0079-6123(07)63020-9 · Cited by 217
Li, Q., & Engelhardt, J. F. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511153200 · Cited by 219
Kikuno, N., Shiina, H., Urakami, S., Kawamoto, K., Hirata, H., Tanaka, Y., Majid, S., Igawa, M., & Dahiya, R. (2008) · International Journal of Cancer · doi:10.1002/ijc.23590 · Cited by 223
“NF-jB is an inducible transcription factor that can regulate a diverse number of genes involved in proliferation, apoptosis, inflammation, and the immune response.(14) In most cell types, NF-jB is predominantly a heterodimer composed of the p50 and p65 subunits.”
BackgroundRetractedRegulation at multiple levels of NF-κB-mediated transactivation by protein acetylation
Quivy, V., & Lint, C. M. V. (2004) · Biochemical Pharmacology · doi:10.1016/j.bcp.2004.05.039 · Cited by 219
Negative regulation of NF‐κB action by Set9‐mediated lysine methylation of the RelA subunit
Yang, X., Huang, B., Li, M., Lamb, A., Kelleher, N. L., & Chen, L. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.55 · Cited by 218
“Activated NF-kB needs to be terminated after induction to limit the inflammation, as sustained NF-kB activity and inflammation lead to a variety of diseases including asthma, arthritis and septic shock (Ghosh and Karin, 2002).”
BackgroundMcIntyre, K. W., Shuster, D. J., Gillooly, K. M., Dambach, D. M., Pattoli, M. A., Lu, P., Zhou, X., Qiu, Y., Zusi, F. C., & Burke, J. R. (2003) · Arthritis & Rheumatism · doi:10.1002/art.11131 · Cited by 216
The c‐myc Promoter: Still MysterY and Challenge
(2008) · Advances in Cancer Research · doi:10.1016/s0065-230x(07)99004-1 · Cited by 211
Guha, M., & Avadhani, N. G. (2013) · Mitochondrion · doi:10.1016/j.mito.2013.08.007 · Cited by 222
“The NFκB activation pathway in response to this stress signaling is distinct from the previously reported canonical and non-canonical pathways (Ghosh and Karin, 2002; Madge and May, 2011;Oeckinghaus, Hayden et al. 2011).”
Grech, A. P., Amesbury, M., Chan, T. D., Gardam, S., Basten, A., & Brink, R. A. (2004) · Immunity · doi:10.1016/j.immuni.2004.09.011 · Cited by 216
Baeza-Raja, B., & Muñoz-Cánoves, P. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-08-0585 · Cited by 247
“…activate NF- B–dependent transcription, at least in part, through mechanisms independent of NF- B nuclear translocation, presumably by stimulating the transactivation domain (TAD) of the p65 subunit (Wang and Baldwin, 1998; Zhong et al., 1998; Ghosh and Karin, 2002; Vermeulen et al., 2003).”
BackgroundInterleukin-10 and Inhibition of Innate Immunity to Yersiniae: Roles of Yops and LcrV (V Antigen)
Brubaker, R. R. (2003) · Infection and Immunity · doi:10.1128/iai.71.7.3673-3681.2003 · Cited by 216
Molecular Inflammation as an Underlying Mechanism of the Aging Process and Age-related Diseases
Chung, H. Y., Lee, E. K., Choi, Y. J., Kim, J. M., Kim, D. H., Zou, Y., Kim, C. H., Lee, J., Kim, H. S., Kim, N. D., et al. (2011) · Journal of Dental Research · doi:10.1177/0022034510387794 · Cited by 220
“Stimulation by several factors, such as cytokines, induces NF-κB activation by IKK, which subsequently targets IκB for ubiquitination and degradation through the 26S proteasome (Ghosh and Karin, 2002).”
BackgroundSinha, S., Perdomo, G., Brown, N. F., & O'Doherty, R. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406514200 · Cited by 219
Mature T Cells Depend on Signaling through the IKK Complex
Schmidt‐Supprian, M., Courtois, G., Tian, J. Y., Coyle, A. J., Israël, A., Rajewsky, K., & Pasparakis, M. (2003) · Immunity · doi:10.1016/s1074-7613(03)00237-1 · Cited by 215
Takada, Y., Ichikawa, H., Badmaev, V., & Aggarwal, B. B. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.5.3127 · Cited by 215
“The translocation of NF- B to the nucleus is preceded by the proteolytic degradation of I B (47), so we next sought to determine whether AKBA inhibitory activity was due to inhibition of I B degradation.”
BackgroundInfluentialMaines, M. D., & Gibbs, P. (2005) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/j.bbrc.2005.08.121 · Cited by 233
Takada, Y., & Aggarwal, B. B. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.171.6.3278 · Cited by 215
Sung, B., Pandey, M., & Aggarwal, B. (2007) · Molecular Pharmacology · doi:10.1124/mol.107.034512 · Cited by 207
Intermittent fasting attenuates lipopolysaccharide-induced neuroinflammation and memory impairment.
Vasconcelos, A. R., Yshii, L. M., Viel, T. A., Buck, H. S., Mattson, M. P., Scavone, C., & Kawamoto, E. M. (2014) · Journal of Neuroinflammation · doi:10.1186/1742-2094-11-85 · Cited by 210
“Inducers of NFκB act by intracellular signaling pathways that activate the IκB kinases (IKKs), which phosphorylate two specific N-terminal serines of IκBα, resulting in IκBα polyubiquitination and degradation in the 26S protease [14].”
The Domains of Apoptosis: A Genomics Perspective
Reed, J. C., Doctor, K. S., & Godzik, A. (2004) · Science s STKE · doi:10.1126/stke.2392004re9 · Cited by 213
“The DD-containing NF-κB1 and NF-κB2 proteins, however, appear to participate in an alternative activation pathway in which these proteins are phosphorylated and then digested from p105 and p100 precursors to produce p50 and p52 polypeptides that retain the RHD but lack the DD and other structures that retain them in t…”
Requirement for O‐linked N‐acetylglucosaminyltransferase in lymphocytes activation
Golks, A., Tran, T.-T. T., Goetschy, J., & Guerini, D. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601845 · Cited by 211
“The transcription factor NFkB regulates the expression of genes crucial for innate and adaptive immune responses, cell growth and apoptosis (Ghosh and Karin, 2002).”
Rodrigues, C. M. P., Solá, S., Nan, Z., Castro, R. E., Ribeiro, P. S., Low, W. C., & Steer, C. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1031632100 · Cited by 210
Bonavida, B. (2007) · Oncogene · doi:10.1038/sj.onc.1210365 · Cited by 210
“As mentioned above, Bcl-x expression is also regulated by the NF-kB pathway (Dixit and Mak, 2002; Ghosh and Karin, 2002).”
Claud, E. C., Lu, L., Anton, P. M., Savidge, T., Walker, W. A., & Cherayil, B. J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401710101 · Cited by 210
Bakkar, N., Wang, J., Ladner, K. J., Wang, H., Dahlman, J. M., Carathers, M., Acharyya, S., Rudnicki, M. A., Hollenbach, A. D., & D, D. C. G. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200707179 · Cited by 208
“The online version of this article contains supplemental material.”
Celastrol protects against MPTP‐ and 3‐nitropropionic acid‐induced neurotoxicity
Cléren, C., Calingasan, N. Y., Chen, J., & Beal, M. F. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03253.x · Cited by 207
“One consequence is an up-regulation of the transcription factor NFjB (Ghosh and Karin 2002).”
Kikuno, N., Shiina, H., Urakami, S., Kawamoto, K., Hirata, H., Tanaka, Y., Place, R. F., Pookot, D., Majid, S., Igawa, M., et al. (2007) · Oncogene · doi:10.1038/sj.onc.1210572 · Cited by 207
“NF-kB is an inducible transcription factor that can regulate a diverse number of genes involved in proliferation, apoptosis, inflammation and the immune response (Ghosh and Karin, 2002).”
BackgroundRetractedWu, Z.-H., Wong, E. T., Shi, Y., Niu, J., Chen, Z. J., Miyamoto, S., & Tergaonkar, V. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.010 · Cited by 209
“Several kinases are implicated as direct upstream kinases for IKK (Ghosh and Karin, 2002; Hayden and Ghosh, 2008).”
BackgroundYoung, C. N., Koepke, J. I., Terlecky, L. J., Borkin, M. S., Boyd, S. L., & Terlecky, S. R. (2008) · Journal of Investigative Dermatology · doi:10.1038/jid.2008.122 · Cited by 209
Hu, M. S., Peluffo, G., Chen, H., Gelman, R. S., Schnitt, S. J., & Polyák, K. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0813306106 · Cited by 205
Glycogen Synthase Kinase 3β Functions To Specify Gene-Specific, NF-κB-Dependent Transcription
Steinbrecher, K. A., Wilson, W., Cogswell, P. C., & Baldwin, A. S. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.19.8444-8455.2005 · Cited by 209
Surabhi, R. M., & Gaynor, R. B. (2002) · Journal of Virology · doi:10.1128/jvi.76.24.12963-12973.2002 · Cited by 205
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Kajiura, F., Sun, S., Nomura, T., Izumi, K., Ueno, T., Bando, Y., Kuroda, N., Han, H., Li, Y., Matsushima, A., et al. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.4.2067 · Cited by 204
TNF-α drives remodeling of blood vessels and lymphatics in sustained airway inflammation in mice
Bałuk, P., Yao, L., Feng, J., Romano, T., Jung, S. S., Schreiter, J., Yan, L., Shealy, D. J., & McDonald, D. M. (2009) · Journal of Clinical Investigation · doi:10.1172/jci37626 · Cited by 209
Werner, S. L., Kearns, J. D., Zadorozhnaya, V., Lynch, C., O'Dea, E. L., Boldin, M., Ma, A. I., Baltimore, D., & Hoffmann, A. (2008) · Genes & Development · doi:10.1101/gad.1680708 · Cited by 203
Shakibaei, M., Buhrmann, C., Nebrich, S., & Mobasheri, A. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2008.05.029 · Cited by 205
Immunomodulatory Activities of Fluoroquinolones
Dalhoff, A. (2005) · Infection · doi:10.1007/s15010-005-8209-8 · Cited by 203
“66 Infection 33 · 2005 · Supplement 2 © URBAN & VOGEL of TNF-α and Il-8 and also plays an important role in superoxide production and apoptosis [131].”
Enhanced NFκB and AP-1 transcriptional activity associated with antiestrogen resistant breast cancer
Zhou, Y., Yau, C. S. F., Gray, J. W., Chew, K., Dairkee, S. H., Moore, D. H., Eppenberger, U., Eppenberger‐Castori, S., & Benz, C. C. (2007) · BMC Cancer · doi:10.1186/1471-2407-7-59 · Cited by 208
“... expression in both MCF7/HER2 and BT474 compared to MCF7 (panels B and C, respectively), despite comparable levels of NFκB p65 and p50 component proteins in all three cell lines (panel A). Since the increased NFκB activation in both MCF7/HER2 and BT474 appeared largely due to increased p50 DNA-binding (panel B), an…”
BackgroundJackson-Bernitsas, D., Ichikawa, H., Takada, Y., Myers, J. N., Lin, X., Darnay, B. G., Chaturvedi, M., & Aggarwal, B. B. (2006) · Oncogene · doi:10.1038/sj.onc.1209945 · Cited by 206
“IKK activity is essential for the activation of NF-kB through the phosphorylation and subsequent degradation of IkBa (Li et al., 2000; Ghosh and Karin, 2002; Li and Verma, 2002).”
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Weih, F., & Caamaño, J. (2003) · Immunological Reviews · doi:10.1034/j.1600-065x.2003.00064.x · Cited by 201
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“However, even in an inactive state, the p65/p50/I B complex is able to shuttle between the cytoplasm and nucleus due to an exposed NLS within p50 that is not completely covered by I B interaction (46).”
Non-canonical NF-κB signalling and ETS1/2 cooperatively drive C250T mutant TERT promoter activation
Li, Y., Zhou, Q.-L., Sun, W., Chandrasekharan, P., Cheng, H. S., Ying, Z., Lakshmanan, M., Raju, A., Tenen, D. G., Cheng, S., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3240 · Cited by 196
Regulation of gene expression by oxygen: NF-κB and HIF-1, two extremes
Michiels, C., Minet, E., Mottet, D., & Raes, M. J. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01045-6 · Cited by 202
Host cell manipulation by the human pathogen Toxoplasma gondii
Laliberté, J., & Carruthers, V. B. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-7556-x · Cited by 199
Qiao, X., He, B., Chiu, A., Knowles, D. M., Chadburn, A., & Cerutti, A. (2006) · Nature Immunology · doi:10.1038/ni1302 · Cited by 199
RetractedMechanisms for the role of tetrahydrobiopterin in endothelial function and vascular disease
Schmidt, T. S., & Alp, N. J. (2007) · Clinical Science · doi:10.1042/cs20070108 · Cited by 195
Loo, G., Lorenzi, R. D., Schmidt, H., Huth, M., Mildner, A., Schmidt‐Supprian, M., Lassmann, H., Prinz, M., & Pasparakis, M. (2006) · Nature Immunology · doi:10.1038/ni1372 · Cited by 196
Takada, Y., Murakami, A., & Aggarwal, B. B. (2005) · Oncogene · doi:10.1038/sj.onc.1208845 · Cited by 199
“…zerumbone is not cell type specific Distinct signal transduction pathways can mediate NFkB induction in different cell types (Bonizzi et al., 1997; Ghosh and Karin, 2002), so we investigated whether zerumbone could block TNF-induced NF-kB activation in human myeloid leukemia KBM-5 (Figure 4a) and…”
BackgroundInfluentialRoles of NF-κB in health and disease: mechanisms and therapeutic potential
Wong, E. T., & Tergaonkar, V. (2009) · Clinical Science · doi:10.1042/cs20080502 · Cited by 196
Pan, L., Zhu, B., Hao, W., Zeng, X., Vlahopoulos, S., Hazra, T. K., Hegde, M. L., Radak, Z. O., Bácsi, A., Brasier, A. R., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.751453 · Cited by 203
Protein kinase C theta (PKCθ): A key player in T cell life and death
HAYASHI, K., & Altman, A. (2007) · Pharmacological Research · doi:10.1016/j.phrs.2007.04.009 · Cited by 195
The Role of Vitamin D in Cancer Prevention and Treatment
Krishnan, A. V., Trump, D. L., Johnson, C. S., & Feldman, D. (2010) · Endocrinology and Metabolism Clinics of North America · doi:10.1016/j.ecl.2010.02.011 · Cited by 199
Sundar, I. K., Yao, H., & Rahman, I. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4863 · Cited by 201
Kinase signalling pathways in endometriosis: potential targets for non-hormonal therapeutics
McKinnon, B. D., Kocbek, V., Nirgianakis, K., Bersinger, N. A., & Mueller, M. D. (2016) · Human Reproduction Update · doi:10.1093/humupd/dmv060 · Cited by 195
“The canonical NFkB pathway is characterized by activity of the IKKb catalytic subunit removing IkB from p65 and targeting it for ubiquitin ligase-mediated degradation (Ghosh and Karin, 2002).”
Targeting melanocortin receptors as potential novel therapeutics
Getting, S. J. (2006) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2005.06.022 · Cited by 194
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
Park, K.-J., Krishnan, V., O’Malley, B. W., Yamamoto, Y., & Gaynor, R. B. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.03.006 · Cited by 193
Kundu, J. K., Shin, Y. K., & Surh, Y. (2006) · Biochemical Pharmacology · doi:10.1016/j.bcp.2006.08.005 · Cited by 196
Loss of p53 enhances catalytic activity of IKKβ through O-linked β-N-acetyl glucosamine modification
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IKKβ Is Required for Peripheral B Cell Survival and Proliferation
Li, Z., Omori, S. A., Labuda, T., Karin, M., & Rickert, R. C. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.170.9.4630 · Cited by 189
Self-citationNF-κB signaling pathway and free radical impact.
Siomek, A. (2012) · Acta Biochimica Polonica · doi:10.18388/abp.2012_2116 · Cited by 192
“NF-κB Although NF-κB was initially identified in activated B cells, it rapidly appeared that this transcription factor exerts many biological functions in essential processes, such as both the innate and adaptive immunity, cell survival, and inflammation, also in other cells (Ghosh & Karin, 2002).”
BackgroundInfluentialWajant, H., Pfizenmaier, K., & Scheurich, P. (2002) · Cytokine & Growth Factor Reviews · doi:10.1016/s1359-6101(02)00072-2 · Cited by 196
Muraoka, R. S., Koh, Y., Roebuck, L. R., Sanders, M. E., Brantley‐Sieders, D. M., Gorska, A. E., Moses, H. L., & Arteaga, C. L. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.23.8691-8703.2003 · Cited by 192
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Nadeau, S., & Rivest, S. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-13-05536.2003 · Cited by 190
“NF- B is then translocated into the nucleus and may bind to its B consensus sequence on target genes (Ghosh and Karin, 2002).”
Qiao, X., He, B., Chiu, A., Knowles, D. M., Chadburn, A., & Cerutti, A. (2016) · Nature Immunology · doi:10.1038/ni1016-1235a · Cited by 189
Low dose cyclophosphamide: Mechanisms of T cell modulation
Madondo, M., Quinn, M. A., & Plebanski, M. (2015) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2015.11.005 · Cited by 188
The c-FLIP–NH2 terminus (p22-FLIP) induces NF-κB activation
Golks, A., Brenner, D., Krammer, P. H., & Lavrik, I. N. (2006) · The Journal of Experimental Medicine · doi:10.1084/jem.20051556 · Cited by 185
Saeed, N. M., El‐Demerdash, E., Abdel-Rahman, H. M., Algandaby, M. M., Al-Abbasi, F. A., & Abdel‐Naim, A. B. (2012) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2012.07.020 · Cited by 186
Metadata
- Authors
- Ghosh, S., & Karin, M.
- Affiliations
- Howard Hughes Medical Institute (US)
- University of California San Diego (US)
- Corresponding author
- Ghosh, Sankar
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2002-04
- Volume
- 109
- Issue
- 2
- Pages
- S81-S96
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W1976382352
- Cited by
- 3,638
- References
- 158
- Citations by year
- 2026: 29 · 2025: 65 · 2024: 66 · 2023: 49 · 2022: 66 · 2021: 94 · 2020: 100 · 2019: 84 · 2018: 103 · 2017: 111 · 2016: 122 · 2015: 141 · 2014: 134 · 2013: 144 · 2012: 189
- FWCI
- 19.54
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- 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 › Signaling Pathways in Disease
- Keywords
- NF-κB, IκB kinase complex, transcription factor regulation, transcriptional activity, IκB, signal transduction
- MeSH terms
- Animals, Cell Nucleus, Cytoplasm, Enzyme Activation, Gene Expression Regulation, Humans, Signal Transduction, NF-kappa B, Protein Serine-Threonine Kinases, Catalytic Domain, Active Transport, Cell Nucleus, I-kappa B Kinase
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