Signaling to NF-κB
Open accessAbstract
The transcription factor NF-κB has been the focus of intense investigation for nearly two decades. Over this period, considerable progress has been made in determining the function and regulation of NF-κB, although there are nuances in this important signaling pathway that still remain to be understood. The challenge now is to reconcile the regulatory complexity in this pathway with the complexity of responses in which NF-κB family members play important roles. In this review, we provide an overview of established NF-κB signaling pathways with focus on the current state of research into the mechanisms that regulate IKK activation and NF-κB transcriptional activity.
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A number of genes that regulate apoptosis, cell proliferation, invasion or angiogenesis are known to be NF-κB target genes in one or more models or cancer sites.
“A number of genes that regulate apoptosis, cell proliferation, invasion or angiogenesis are known to be NF-κB target genes in one or more models or cancer sites (32).”
From Tumor suppressor PDCD4 inhibits NF-κB-dependent transcription in human glioblastoma cells by direct interaction with p65 (2014) · cites this paper as [32]
The “TNFα: a model NF-κB stimulus” section identifies antiapoptotic genes, including cIAP1/2 and Bcl-XL, whose expression is regulated through NF-κB. The paper also links NF-κB signaling to lymphocyte proliferation, but the passages found do not identify NF-κB target genes regulating invasion or angiogenesis, or establish the full claim across cancer models or sites (searched: angiogenesis, invasion, proliferation). (LLM, conf=0.86)
Experimental — accuracy not yet measuredNFκB regulates various genes involved in inflammatory responses and its activation is important for host defense and repair after insult.
“In addition, the transcription factor, NFκB, regulates various genes involved in inflammatory responses and its activation is important for host defense and repair after insult (Hayden and Ghosh, 2004).”
From Thymosin beta 4 suppression of corneal NFκB: A potential anti-inflammatory pathway (2007) · cites this paper as Hayden and Ghosh, 2004
The opening section says NF-κB regulates cytokines, growth factors, and effector enzymes involved in immunity, and the Toll/IL-1 receptor section describes its essential role in early innate immune responses. The copy does not establish that NF-κB activation is important for repair after insult; the Cell stress section describes a possible role in allowing DNA repair as an unproven hypothesis. (LLM, conf=0.87)
Experimental — accuracy not yet measuredIn the NF-κB system, NF-κB is normally held inactive in the cytoplasm by binding to an inhibitor IκB; pro-inflammatory cytokines such as TNF-α, LPS and IL-1 act by binding to receptors at the cell surface and initiating signalling pathways that lead to activation of IKK; IKK phosphorylates IκB causing its release and degradation, allowing NF-κB to translocate to the nucleus where it can activate a
“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 [2021]
In resting cells, NF-κB resides in the cytoplasm bound to IκBα, which blocks the nuclear localization signal of p65.
“In an unstimulated state, NF-κB is present in the cytoplasm bound with inhibitor of κB α (IκBα), which masks the nuclear localization sequence of p65 [12]”
From Edible blue-green algae reduce the production of pro-inflammatory cytokines by inhibiting NF-κB pathway in macrophages and splenocytes (2013) · cites this paper as [12]
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Cites
Janeway, C. A., & Medzhitov, R. (2002) · Annual Review of Immunology · doi:10.1146/annurev.immunol.20.083001.084359 · Cited by 8,394 · see citing works
Takeda, K., Kaisho, T., & Akira, S. (2003) · Annual Review of Immunology · doi:10.1146/annurev.immunol.21.120601.141126 · Cited by 6,143 · see citing works
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 · see citing works
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 · see citing works
NF-κB regulation in the immune system
Li, Q., & Verma, I. M. (2002) · Nature Reviews Immunology · doi:10.1038/nri910 · Cited by 4,007 · see citing works
Missing Pieces in the NF-κB Puzzle
Ghosh, S., & Karin, M. (2002) · Cell · doi:10.1016/s0092-8674(02)00703-1 · Cited by 3,638 · see citing works
Self-citationHaine, M. M.-L., & Meeùs, N. (1986) · Cited by 3,463 · see citing works
Role of Adaptor TRIF in the MyD88-Independent Toll-Like Receptor Signaling Pathway
Yamamoto, M., Sato, S., Hemmi, H., Hoshino, K., Kaisho, T., Sanjo, H., Takeuchi, O., Sugiyama, M., Okabe, M., Takeda, K., et al. (2003) · Science · doi:10.1126/science.1087262 · Cited by 3,244 · see citing works
Wang, C.-Y., Mayo, M., Korneluk, R., Goeddel, D., & Baldwin, A. (1998) · Science · doi:10.1126/science.281.5383.1680 · Cited by 2,950 · see citing works
Signalling pathways of the TNF superfamily: a double-edged sword
Aggarwal, B. B. (2003) · Nature Reviews Immunology · doi:10.1038/nri1184 · Cited by 2,793 · see citing works
Activation of p53 Sequence-Specific DNA Binding by Acetylation of the p53 C-Terminal Domain
Gu, W., & Roeder, R. G. (1997) · Cell · doi:10.1016/s0092-8674(00)80521-8 · Cited by 2,559 · 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
Unresponsiveness of MyD88-deficient mice to endotoxin.
Kawai, T., Adachi, O., Ogawa, T., Takeda, K., & Akira, S. (1999) · Immunity · doi:10.1016/s1074-7613(00)80086-2 · Cited by 2,367 · see citing works
Targeted disruption of the MyD88 gene results in loss of IL-1- and IL-18-mediated function.
Adachi, O., Kawai, T., Takeda, K., Matsumoto, M., Tsutsui, H., Sakagami, M., Nakanishi, K., & Akira, S. (1998) · Immunity · doi:10.1016/s1074-7613(00)80596-8 · Cited by 2,358 · see citing works
Tumor necrosis factor signaling
Wajant, H., Pfizenmaier, K., & Scheurich, P. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401189 · Cited by 2,353 · see citing works
TAK1 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 · see citing works
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 · see citing works
Palombella, V. J., Rando, O. J., Goldberg, A. L., & Maniatis, T. (1994) · Cell · doi:10.1016/s0092-8674(94)90482-0 · Cited by 2,097 · see citing works
IKK-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 · see citing works
Hsu, H., Shu, H., Pan, M., & Goeddel, D. V. (1996) · Cell · doi:10.1016/s0092-8674(00)80984-8 · Cited by 1,998 · see citing works
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 · see citing works
The IκB-NF-κB Signaling Module: Temporal Control and Selective Gene Activation
Hoffmann, A., Levchenko, A., Scott, M. L., & Baltimore, D. (2002) · Science · doi:10.1126/science.1071914 · Cited by 1,866 · see citing works
Embryonic lethality and liver degeneration in mice lacking the RelA component of NF-κB
Beg, A. A., Sha, W. C., Bronson, R. T., Ghosh, S., & Baltimore, D. (1995) · Nature · doi:10.1038/376167a0 · Cited by 1,828 · see citing works
Self-citationZandi, E., Rothwarf, D. M., Delhase, M., Hayakawa, M., & Karin, M. (1997) · Cell · doi:10.1016/s0092-8674(00)80406-7 · Cited by 1,814 · see citing works
Triggering the Interferon Antiviral Response Through an IKK-Related Pathway
Sharma, S., tenOever, B. R., Grandvaux, N., Zhou, G., Lin, R., & Hiscott, J. B. (2003) · Science · doi:10.1126/science.1081315 · Cited by 1,664 · see citing works
Akira, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.r300028200 · Cited by 1,486 · see citing works
Failure to Regulate TNF-Induced NF-κB and Cell Death Responses in A20-Deficient Mice
Lee, E. G., Boone, D. L., Chai, S., Libby, S. L., Chien, M., Lodolce, J. P., & Ma, A. (2000) · Science · doi:10.1126/science.289.5488.2350 · Cited by 1,409 · see citing works
Requirement for glycogen synthase kinase-3β in cell survival and NF-κB activation
Hoeflich, K. P., Luo, J., Rubie, E. A., Tsao, M., Jin, O., & Woodgett, J. R. (2000) · Nature · doi:10.1038/35017574 · Cited by 1,394 · see citing works
The IKK NF-κB system: a treasure trove for drug development
Karin, M., Yamamoto, Y., & Wang, Q. M. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1279 · Cited by 1,364 · 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
TRAF6 is a signal transducer for interleukin-1
Cao, Z., Xiong, J., Takeuchi, M., Kurama, T., & Goeddel, D. V. (1996) · Nature · doi:10.1038/383443a0 · Cited by 1,305 · see citing works
IRAK-M Is a Negative Regulator of Toll-like Receptor Signaling
Kobayashi, K. S., Hernandez, L. D., Galán, J. E., Janeway, C. A., Medzhitov, R. M., & Flavell, R. A. (2002) · Cell · doi:10.1016/s0092-8674(02)00827-9 · Cited by 1,289 · see citing works
Toll-Like Receptor Signaling Pathways
Barton, G. M., & Medzhitov, R. M. (2003) · Science · doi:10.1126/science.1085536 · Cited by 1,270 · see citing works
TRAF6 deficiency results in osteopetrosis and defective interleukin-1, CD40, and LPS signalingPreprint
Lomaga, M. A., Yeh, W., Sarosi, I., Duncan, G. S., Furlonger, C. L., Ho, A. P., Morony, S., Capparelli, C., Van, G. Y., Kaufman, S., et al. (1999) · Genes & Development · doi:10.1101/gad.13.8.1015 · Cited by 1,253 · see citing works
MyD88: an adapter that recruits IRAK to the IL-1 receptor complex.
Wesche, H., Henzel, W., Shillinglaw, W., Li, S., & Cao, Z.-D. (1997) · Immunity · doi:10.1016/s1074-7613(00)80402-1 · Cited by 1,247 · see citing works
Duration of Nuclear NF-κB Action Regulated by Reversible Acetylation
Chen, L., Fischle, W., Verdin, E. M., & Greene, W. C. (2001) · Science · doi:10.1126/science.1062374 · Cited by 1,231 · see citing works
Shaping the nuclear action of NF-κB
Chen, L., & Greene, W. C. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1368 · Cited by 1,219 · see citing works
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
Self-citationOshiumi, H., Matsumoto, M., Funami, K., Akazawa, T., & Seya, T. (2003) · Nature Immunology · doi:10.1038/ni886 · Cited by 1,208 · see citing works
LPS-TLR4 Signaling to IRF-3/7 and NF-κB Involves the Toll Adapters TRAM and TRIF
Fitzgerald, K. A., Rowe, D. C., Barnes, B. J., Caffrey, D. R., Visintin, A., Latz, E., Monks, B. G., Pitha, P. M., & Golenbock, D. T. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20031023 · Cited by 1,193 · see citing works
Ubiquitin signalling in the NF-κB pathway
Chen, Z. J. (2005) · Nature Cell Biology · doi:10.1038/ncb0805-758 · Cited by 1,184 · see citing works
IκB Kinase-β: NF-κB Activation and Complex Formation with IκB Kinase-α and NIK
Woronicz, J. D., Gao, X., Cao, Z., Rothe, M., & Goeddel, D. V. (1997) · Science · doi:10.1126/science.278.5339.866 · Cited by 1,183 · see citing works
Identification and Characterization of an IκB Kinase
Régnier, C. H., Song, H. Y., Gao, X., Goeddel, D. V., Cao, Z., & Rothe, M. (1997) · Cell · doi:10.1016/s0092-8674(00)80344-x · Cited by 1,176 · see citing works
Targeted disruption of the p50 subunit of NF-κB leads to multifocal defects in immune responses
Sha, W. C., Liou, H.-C., TUOMANEN, E. I., & Baltimore, D. (1995) · Cell · doi:10.1016/0092-8674(95)90415-8 · Cited by 1,158 · see citing works
The Death Domain Kinase RIP Mediates the TNF-Induced NF-κB Signal
Kelliher, M. A., Grimm, S., Ishida, Y., Kuo, F., Stanger, B. Z., & Leder, P. (1998) · Immunity · doi:10.1016/s1074-7613(00)80535-x · Cited by 1,102 · see citing works
Yamaoka, S., Courtois, G., Chable-Bessia, C., Whiteside, S. T., Weil, R., Agou, F., Kirk, H., Kay, R. J., & Israël, A. (1998) · Cell · doi:10.1016/s0092-8674(00)81466-x · Cited by 1,077 · see citing works
Yamamoto, M., Sato, S., Hemmi, H., Uematsu, S., Hoshino, K., Kaisho, T., Takeuchi, O., Takeda, K., & Akira, S. (2003) · Nature Immunology · doi:10.1038/ni986 · Cited by 1,052 · see citing works
SUMO-1 Modification of IκBα Inhibits NF-κB Activation
Desterro, J. M. P., Rodríguez, M. S., & Hay, R. T. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80133-1 · Cited by 1,048 · see citing works
A physical and functional map of the human TNF-α/NF-κB signal transduction pathway
Bouwmeester, T., Bauch, A., Ruffner, H., Angrand, P., Bergamini, G., Croughton, K., Cruciat, C., Eberhard, D., Gagneur, J., Ghidelli, S., et al. (2004) · Nature Cell Biology · doi:10.1038/ncb1086 · Cited by 1,030 · see citing works
The tumour suppressor CYLD negatively regulates NF-κB signalling by deubiquitination
Kovalenko, A., Chable-Bessia, C., Cantarella, G., Israël, A., Wallach, D., & Courtois, G. (2003) · Nature · doi:10.1038/nature01802 · Cited by 1,018 · see citing works
Kelly, D., Campbell, J. I., King, T. P., Grant, G., Jansson, E. Å., Coutts, A., Pettersson, S., & Conway, S. (2003) · Nature Immunology · doi:10.1038/ni1018 · Cited by 997 · see citing works
Essential role for TIRAP in activation of the signalling cascade shared by TLR2 and TLR4
Yamamoto, M., Sato, S., Hemmi, H., Sanjo, H., Uematsu, S., Kaisho, T., Hoshino, K., Takeuchi, O., Kobayashi, M., Fujita, T., et al. (2002) · Nature · doi:10.1038/nature01182 · Cited by 995 · see citing works
Modulation of Akt kinase activity by binding to Hsp90
Sato, S., Fujita, N., & Tsuruo, T. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.170276797 · Cited by 967 · see citing works
CYLD is a deubiquitinating enzyme that negatively regulates NF-κB activation by TNFR family members
Trompouki, E., Hatzivassiliou, E., Tsichritzis, T., Farmer, H., Ashworth, A., & Mosialos, G. (2003) · Nature · doi:10.1038/nature01803 · Cited by 964 · see citing works
Severe Liver Degeneration in Mice Lacking the IκB Kinase 2 Gene
Li, Q., Antwerp, D. V., Mercurio, F., Lee, K., & Verma, I. M. (1999) · Science · doi:10.1126/science.284.5412.321 · Cited by 963 · see citing works
Site-Specific Phosphorylation of IκBα by a Novel Ubiquitination-Dependent Protein Kinase Activity
Chen, Z. J., Parent, L. A., & Maniatis, T. (1996) · Cell · doi:10.1016/s0092-8674(00)81064-8 · Cited by 958 · see citing works
IKK-γ is an essential regulatory subunit of the IκB kinase complex
Rothwarf, D. M., Zandi, E., Natoli, G., & Karin, M. (1998) · Nature · doi:10.1038/26261 · Cited by 958 · see citing works
Winston, J. T., Strack, P. R., Beer‐Romero, P., Chu, C. Y., Elledge, S. J., & Harper, J. W. (1999) · Genes & Development · doi:10.1101/gad.13.3.270 · Cited by 949 · see citing works
Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-κB
Brummelkamp, T. R., Nijman, S. M. B., Dirac, A. M. G., & Bernards, R. (2003) · Nature · doi:10.1038/nature01811 · Cited by 947 · 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
Self-citationLi, Z., Chu, W., Hu, Y., Delhase, M., Deerinck, T. J., Ellisman, M. H., Johnson, R. S., & Karin, M. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.189.11.1839 · Cited by 927 · 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
NF-κB signaling pathways in mammalian and insect innate immunityPreprint
Silverman, N. S., & Maniatis, T. (2001) · Genes & Development · doi:10.1101/gad.909001 · Cited by 904 · see citing works
PKC-θ is required for TCR-induced NF-κB activation in mature but not immature T lymphocytes
Sun, Z., Arendt, C., Ellmeier, W., Schaeffer, E. M., Sunshine, M. J., Gandhi, L., Annes, J. P., Petrzilka, D., Kupfer, A., Schwartzberg, P. L., et al. (2000) · Nature · doi:10.1038/35006090 · Cited by 894 · see citing works
Severe impairment of interleukin-1 and Toll-like receptor signalling in mice lacking IRAK-4
Suzuki, N., Suzuki, S., Duncan, G. S., Millar, D. G., Wada, T., Mirtsos, C., Takada, H., Wakeham, A. C., Itié, A., Li, S., et al. (2002) · Nature · doi:10.1038/nature736 · Cited by 858 · see citing works
Positive and Negative Regulation of IκB Kinase Activity Through IKKβ Subunit Phosphorylation
Delhase, M., Hayakawa, M., Chen, Y., & Karin, M. (1999) · Science · doi:10.1126/science.284.5412.309 · Cited by 852 · see citing works
RIP1 is an essential mediator of Toll-like receptor 3–induced NF-κB activation
Meylan, E., Burns, K., Hofmann, K., Blancheteau, V., Martinon, F., Kelliher, M. A., & Tschopp, J. (2004) · Nature Immunology · doi:10.1038/ni1061 · Cited by 848 · 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
Zhong, H., Suyang, H., Erdjument‐Bromage, H., Tempst, P., & Ghosh, S. (1997) · Cell · doi:10.1016/s0092-8674(00)80222-6 · Cited by 828 · see citing works
Self-citationAcetylation of RelA at discrete sites regulates distinct nuclear functions of NF‐κB
Chen, L., Mu, Y., & Greene, W. C. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf660 · Cited by 827 · see citing works
Abnormal Morphogenesis But Intact IKK Activation in Mice Lacking the IKKα Subunit of IκB Kinase
Hu, Y., Baud, V., Delhase, M., Zhang, P., Deerinck, T. J., Ellisman, M. H., Johnson, R. S., & Karin, M. (1999) · Science · doi:10.1126/science.284.5412.316 · Cited by 822 · see citing works
Structure of an IκBα/NF-κB Complex
Jacobs, M. D., & Harrison, S. C. (1998) · Cell · doi:10.1016/s0092-8674(00)81698-0 · Cited by 822 · see citing works
The adaptor molecule TIRAP provides signalling specificity for Toll-like receptors
Horng, T., Barton, G. M., Flavell, R. A., & Medzhitov, R. M. (2002) · Nature · doi:10.1038/nature01180 · Cited by 809 · see citing works
Weih, F., Carrasco, D. R., Durham, S. K., Barton, D. S., Rizzo, C. A., Ryseck, R.-P., Lira, S. A., & Bravo, R. (1995) · Cell · doi:10.1016/0092-8674(95)90416-6 · Cited by 807 · see citing works
TNF-α Induction by LPS Is Regulated Posttranscriptionally via a Tpl2/ERK-Dependent Pathway
Dumitru, C. D., Ceci, J. D., Tsatsanis, C., Kontoyiannis, D. L., Stamatakis, K., Lin, J., Patriotis, C., Jenkins, N. A., Copeland, N. G., Kollias, G. A., et al. (2000) · Cell · doi:10.1016/s0092-8674(00)00210-5 · Cited by 801 · see citing works
Yeh, W., Shahinian, A., Speiser, D. E., Kraunus, J., Billia, F., Wakeham, A. C., de la Pompa, J. L., Ferrick, D. A., Hum, B., Iscove, N. N., et al. (1997) · Immunity · doi:10.1016/s1074-7613(00)80391-x · Cited by 798 · see citing works
Expression of relB is required for the development of thymic medulla and dendritic cells
Burkly, L. C., Hession, C. A., Ogata, L., Reilly, C. R., Marconi, L. A., Olson, D. L., Tizard, R., Gate, R., & Lo, D. D. (1995) · Nature · doi:10.1038/373531a0 · Cited by 781 · see citing works
To be, or not to be: NF-κB is the answer – role of Rel/NF-κB in the regulation of apoptosis
Kucharczak, J., Simmons, M. J., Fan, Y., & Gélinas, C. (2003) · Oncogene · doi:10.1038/sj.onc.1207230 · Cited by 761 · see citing works
Vermeulen, L., Wilde, G. D., Damme, P. V., Berghe, W. V., & Haegeman, G. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg139 · Cited by 760 · see citing works
Organogenesis of lymphoid tissues
Mebius, R. E. (2003) · Nature reviews. Immunology · doi:10.1038/nri1054 · Cited by 747 · see citing works
Induction of gadd45β by NF-κB downregulates pro-apoptotic JNK signalling
De Smaele, E., Zazzeroni, F., Papa, S., Nguyen, D. U., Jin, R., Jones, J., Cong, R., & Franzoso, G. (2001) · Nature · doi:10.1038/35104560 · Cited by 732 · see citing works
Köntgen, F., Grumont, R. J., Strasser, A., Metcalf, D., Li, R., Tarlinton, D. M., & Gerondakis, S. (1995) · Genes & Development · doi:10.1101/gad.9.16.1965 · Cited by 727 · see citing works
Inhibition of JNK activation through NF-κB target genes
Tang, G., Minemoto, Y., Dibling, B., Purcell, N. H., Li, Z., Karin, M., & Lin, A. (2001) · Nature · doi:10.1038/35104568 · Cited by 721 · see citing works
Dunne, A., & O'Neill, L. A. J. (2003) · Science s STKE · doi:10.1126/stke.2003.171.re3 · Cited by 712 · see citing works
Activation of the IκBα Kinase Complex by MEKK1, a Kinase of the JNK Pathway
Lee, F. S., Hagler, J., Chen, Z. J., & Maniatis, T. (1997) · Cell · doi:10.1016/s0092-8674(00)81842-5 · Cited by 710 · see citing works
Mapping of the Inducible IκB Phosphorylation Sites That Signal Its Ubiquitination and Degradation†
Didonato, J., Mercurio, F., Rosette, C., Wu-Li, J., Suyang, H., Ghosh, S., & Karin, M. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.4.1295 · Cited by 707 · see citing works
Self-citationSun, L., Deng, L., Ea, C.-K., Xia, Z.-P., & Chen, Z. J. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00236-9 · Cited by 700 · see citing works
BAFF-induced NEMO-independent processing of NF-κB2 in maturing B cells
Claudio, E., Brown, K., Park, S., Wang, H., & Siebenlist, U. K. (2002) · Nature Immunology · doi:10.1038/ni842 · Cited by 694 · see citing works
May, M. J., D’Acquisto, F., Madge, L. A., Glöckner, J., Pober, J. S., & Ghosh, S. (2000) · Science · doi:10.1126/science.289.5484.1550 · Cited by 678 · see citing works
Self-citationIdentification of the receptor component of the IκBα–ubiquitin ligase
Yaron, A., Hatzubai, A., Davis, M., Lavon, I., Amit, S., Manning, A. M., Andersen, J., Mann, M., Mercurio, F., & Ben‐Neriah, Y. (1998) · Nature · doi:10.1038/25159 · Cited by 654 · see citing works
Tumor necrosis factor receptor-associated factors (TRAFs)
Bradley, J. R., & Pober, J. S. (2001) · Oncogene · doi:10.1038/sj.onc.1204788 · Cited by 652 · see citing works
NF-kappa B activation by ultraviolet light not dependent on a nuclear signal
Devary, Y., Rosette, C., DiDonato, J. A., & Karin, M. (1993) · Science · doi:10.1126/science.8367725 · Cited by 637 · see citing works
Ryo, A., Suizu, F., Yoshida, Y., Perrem, K., Liou, Y., Wulf, G. M., Rottapel, R. K., Yamaoka, S., & Lu, K. P. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00490-8 · Cited by 632 · see citing works
Chung, J. Y., Park, Y. C., Ye, H., & Wu, H. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.4.679 · Cited by 613 · see citing works
Crystal structure of p50/p65 heterodimer of transcription factor NF-κB bound to DNA
Chen, F. E., Huang, D.-B., Chen, Y., & Ghosh, G. (1998) · Nature · doi:10.1038/34956 · Cited by 612 · see citing works
Limb and Skin Abnormalities in Mice Lacking IKKα
Takeda, K., Takeuchi, O., Tsujimura, T., Itami, S., Adachi, O., Kawai, T., Sanjo, H., Yoshikawa, K., Terada, N., & Akira, S. (1999) · Science · doi:10.1126/science.284.5412.313 · Cited by 609 · see citing works
Takaesu, G., Kishida, S., Hiyama, A., Yamaguchi, T., Shibuyà, H., Irie, K., Ninomiya‐Tsuji, J., & Matsumoto, K. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80244-0 · Cited by 606 · see citing works
SIGIRR, a negative regulator of Toll-like receptor–interleukin 1 receptor signaling
Wald, D. N., Qin, J., Zhao, Z., Qian, Y., Naramura, M., Tian, L., Towne, J. E., Sims, J. E., Stark, G. R., & Li, X. (2003) · Nature Immunology · doi:10.1038/ni968 · Cited by 606 · see citing works
Negative Regulation of Toll-like Receptor-mediated Signaling by Tollip
Zhang, G., & Ghosh, S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109537200 · Cited by 598 · see citing works
Self-citationThe Crystal Structure of the IκBα/NF-κB Complex Reveals Mechanisms of NF-κB Inactivation
Huxford, T., Huang, D.-B., Malek, S., & Ghosh, G. (1998) · Cell · doi:10.1016/s0092-8674(00)81699-2 · Cited by 581 · see citing works
NF-κB Inducers Upregulate cFLIP, a Cycloheximide-Sensitive Inhibitor of Death Receptor Signaling
Kreuz, S., Siegmund, D., Scheurich, P., & Wajant, H. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.12.3964-3973.2001 · Cited by 579 · see citing works
Histone H3 phosphorylation by IKK-α is critical for cytokine-induced gene expression
Yamamoto, Y., Verma, U. N., Prajapati, S., Kwak, Y.-T., & Gaynor, R. B. (2003) · Nature · doi:10.1038/nature01576 · Cited by 577 · see citing works
Hemmi, H., Takeuchi, O., Sato, S., Yamamoto, M., Kaisho, T., Sanjo, H., Kawai, T., Hoshino, K., Takeda, K., & Akira, S. (2004) · The Journal of Experimental Medicine · doi:10.1084/jem.20040520 · Cited by 576 · see citing works
Structure of NF-κB p50 homodimer bound to a κB site
Ghosh, G., Duyne, G. D. V., Ghosh, S., & Sigler, P. B. (1995) · Nature · doi:10.1038/373303a0 · Cited by 570 · see citing works
Self-citationEmbryonic Lethality, Liver Degeneration, and Impaired NF-κB Activation in IKK-β-Deficient Mice
Tanaka, M., Fuentes, M. E., Yamaguchi, T., Durnin, M., Dalrymple, S. A., Hardy, K. L., & Goeddel, D. V. (1999) · Immunity · doi:10.1016/s1074-7613(00)80042-4 · Cited by 569 · see citing works
Kumar, A., Haque, J., Lacoste, J., Hiscott, J. B., & Williams, B. R. G. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.14.6288 · Cited by 568 · see citing works
Huang, T. T., Wuerzberger‐Davis, S. M., Wu, Z., & Miyamoto, S. (2003) · Cell · doi:10.1016/s0092-8674(03)00895-x · Cited by 560 · see citing works
Janssens, S., & Beyaert, R. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00053-4 · Cited by 559 · see citing works
Tollip, a new component of the IL-1RI pathway, links IRAK to the IL-1 receptor
Burns, K., Clatworthy, J., Martin, L., Martinon, F., Plumpton, C., Maschera, B., Lewis, A., Ray, K. P., Tschopp, J., & Volpe, F. (2000) · Nature Cell Biology · doi:10.1038/35014038 · Cited by 554 · see citing works
Signal-induced degradation of I kappa B alpha requires site-specific ubiquitination.
Scherer, D. C., Brockman, J. A., Chen, Z., Maniatis, T., & Ballard, D. W. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.24.11259 · Cited by 554 · see citing works
The NF-κB Activation Pathway: A Paradigm in Information Transfer from Membrane to Nucleus
Rothwarf, D., & Karin, M. (1999) · Science's STKE · doi:10.1126/stke.1999.5.re1 · Cited by 553 · see citing works
Ting, A. T., Pimentel‐Muiños, F. X., & Seed, B. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb01007.x · Cited by 550 · see citing works
Recognition of microbial infection by Toll-like receptors
Kopp, E. B., & Medzhitov, R. M. (2003) · Current Opinion in Immunology · doi:10.1016/s0952-7915(03)00080-3 · Cited by 547 · see citing works
Ruland, J., Duncan, G. S., Elia, A., Barrantes, I. D. B., Nguyen, L. T., Plyte, S., Millar, D. G., Bouchard, D., Wakeham, A. C., Ohashi, P. S., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00189-1 · Cited by 545 · see citing works
McWhirter, S. M., Fitzgerald, K. A., Rosains, J., Rowe, D. C., Golenbock, D. T., & Maniatis, T. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2237236100 · Cited by 542 · see citing works
An Induced Proximity Model for NF-κB Activation in the Nod1/RICK and RIP Signaling Pathways
Inohara, N., Koseki, T., Lin, J., del Peso, L., Lucas, P. C., Chen, F. F., Ogura, Y., & Núñez, G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003415200 · Cited by 538 · see citing works
Structure of the NF-κB p50 homodimer bound to DNA
Müller, C. W., Rey, F. A., Sodeoka, M., Verdine, G. L., & Harrison, S. C. (1995) · Nature · doi:10.1038/373311a0 · Cited by 536 · see citing works
NF-κB-inducing kinase activates IKK-α by phosphorylation of Ser-176
Lei, L., Cao, Z., & Goeddel, D. V. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.7.3792 · Cited by 536 · see citing works
Post-activation Turn-off of NF-κB-dependent Transcription Is Regulated by Acetylation of p65
Kiernan, R. E., Brès, V., Ng, R. W. M., Coudart, M.-P., Messaoudi, S. E., Sardet, C., Jin, D., Emiliani, S., & Benkirane, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209572200 · Cited by 536 · see citing works
Bcl10 activates the NF-κB pathway through ubiquitination of NEMO
Zhou, H., Wertz, I. E., O’Rourke, K. M., Ultsch, M. H., Seshagiri, S., Eby, M. T., Xiao, W., & Dixit, V. M. (2003) · Nature · doi:10.1038/nature02273 · Cited by 527 · see citing works
A nucleosomal function for IκB kinase-α in NF-κB-dependent gene expression
Anest, V., Ostrander, J. H., Cogswell, P. C., Steinbrecher, K. A., Strahl, B. D., & Baldwin, A. S. (2003) · Nature · doi:10.1038/nature01648 · Cited by 522 · see citing works
Severe liver degeneration and lack of NF-kappaB activation in NEMO/IKKgamma-deficient mice.
Rudolph, D., Yeh, W., Wakeham, A. C., Rudolph, B., Nallainathan, D., Potter, J., Elia, A., & Mak, T. W. (2000) · PubMed Central · Cited by 518 · see citing works
Burns, K., Janssens, S., Brissoni, B., Olivos, N., Beyaert, R., & Tschopp, J. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20021790 · Cited by 512 · see citing works
The signaling adaptors and pathways activated by TNF superfamily
Dempsey, P. W., Doyle, S. E., He, J. Q., & Cheng, G. (2003) · Cytokine & Growth Factor Reviews · doi:10.1016/s1359-6101(03)00021-2 · Cited by 502 · see citing works
Bours, V. (1993) · Cell · doi:10.1016/0092-8674(93)90401-b · Cited by 502 · see citing works
Cao, Y., Bonizzi, G., Seagroves, T. N., Greten, F. R., Johnson, R. S., Schmidt, E. V., & Karin, M. (2001) · Cell · doi:10.1016/s0092-8674(01)00599-2 · Cited by 479 · see citing works
Rudolph, D., Yeh, W.-C., Wakeham, A., Rudolph, B., Nallainathan, D., Potter, J., Elia, A. J., & Mak, T. W. (2000) · Genes & Development · doi:10.1101/gad.14.7.854 · Cited by 479 · see citing works
IRAK-M Is a Novel Member of the Pelle/Interleukin-1 Receptor-associated Kinase (IRAK) Family*
Wesche, H., Gao, X., Li, X.-X., Kirschning, C., Stark, G., & Cao, Z.-D. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.27.19403 · Cited by 475 · see citing works
Beg, A. A., Sha, W. C., Bronson, R. T., & Baltimore, D. (1995) · Genes & Development · doi:10.1101/gad.9.22.2736 · Cited by 473 · see citing works
IKK1-deficient mice exhibit abnormal development of skin and skeletonPreprint
Li, Q., Lu, Q., Hwang, J. Y., Büscher, D., Lee, K., Izpisúa‐Belmonte, J. C., & Verma, I. M. (1999) · Genes & Development · doi:10.1101/gad.13.10.1322 · Cited by 470 · see citing works
Recruitment of TNF Receptor 1 to Lipid Rafts Is Essential for TNFα-Mediated NF-κB Activation
Legler, D. F., Micheau, O., Doucey, M., Tschopp, J., & Bron, C. (2003) · Immunity · doi:10.1016/s1074-7613(03)00092-x · Cited by 464 · see citing works
Recruitment of the IKK Signalosome to the p55 TNF Receptor
Zhang, S. Q., Kovalenko, A., Cantarella, G., & Wallach, D. (2000) · Immunity · doi:10.1016/s1074-7613(00)80183-1 · Cited by 456 · see citing works
Wang, D., Westerheide, S. D., Ostrander, J. H., & Baldwin, A. S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001358200 · Cited by 454 · see citing works
Alymphoplasia is caused by a point mutation in the mouse gene encoding Nf-κb-inducing kinase
Shinkura, R., Kitada, K., Matsuda, F., Tashiro, K., Ikuta, K., Suzuki, M., Kogishi, K., Serikawa, T., & Honjo, T. (1999) · Nature Genetics · doi:10.1038/8780 · Cited by 451 · see citing works
Zandi, E., Chen, Y., & Karin, M. (1998) · Science · doi:10.1126/science.281.5381.1360 · Cited by 446 · see citing works
Krikos, A., Laherty, C. D., & Dixit, V. M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)37138-8 · Cited by 444 · see citing works
Alkalay, I., Yaron, A., Hatzubai, A., Orian, A., Ciechanover, A. J., & Ben‐Neriah, Y. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.23.10599 · Cited by 441 · see citing works
RIP2 Is a Novel NF-κB-activating and Cell Death-inducing Kinase
McCarthy, J. V., Ni, J., & Dixit, V. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.27.16968 · Cited by 438 · see citing works
NEMO/IKKγ-Deficient Mice Model Incontinentia Pigmenti
Schmidt‐Supprian, M., Bloch, W., Courtois, G., Addicks, K., Israël, A., Rajewsky, K., & Pasparakis, M. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80263-4 · Cited by 437 · see citing works
The atypical PKC‐interacting protein p62 channels NF‐κB activation by the IL‐1–TRAF6 pathway
Sanz, L., Diaz‐Meco, M. T., Nakano, H., & Moscat, J. (2000) · The EMBO Journal · doi:10.1093/emboj/19.7.1576 · Cited by 436 · see citing works
Signal-induced ubiquitination of Ikappa Balpha by the F-box protein Slimb/beta -TrCPPreprint
Spencer, E., Jiang, J., & Chen, Z. J. (1999) · Genes & Development · doi:10.1101/gad.13.3.284 · Cited by 434 · see citing works
The Distinct Roles of TRAF2 and RIP in IKK Activation by TNF-R1
Devin, A., Cook, A., Lin, Y., Rodriguez, Y., Kelliher, M. A., & Liu, Z.-G. (2000) · Immunity · doi:10.1016/s1074-7613(00)80194-6 · Cited by 433 · see citing works
Melmed, G., Thomas, L. S., Lee, N., Tesfay, S. Y., Lukasek, K., Michelsen, K. S., Zhou, Y., Hu, B., Arditi, M., & Abreu, M. T. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.170.3.1406 · Cited by 431 · see citing works
Ionizing radiation and short wavelength UV activate NF-κB through two distinct mechanisms
Li, N., & Karin, M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.22.13012 · Cited by 429 · see citing works
Franzoso, G., Carlson, L. M., Poljak, L., Shores, E. W., Epstein, S. L., Leonardi, A., Grinberg, A., Tran, T., Scharton‐Kersten, T., Anver, M. R., et al. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.187.2.147 · Cited by 425 · see citing works
Shu, H., Takeuchi, M., & Goeddel, D. V. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.24.13973 · Cited by 418 · see citing works
Prevention of Constitutive TNF Receptor 1 Signaling by Silencer of Death Domains
Jiang, Y., Woronicz, J. D., Liu, W., & Goeddel, D. V. (1999) · Science · doi:10.1126/science.283.5401.543 · Cited by 415 · see citing works
Song, H. Y., Rothe, M., & Goeddel, D. V. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.13.6721 · Cited by 414 · see citing works
The interaction of p62 with RIP links the atypical PKCs to NF‐κB activation
Sanz, L., Sánchez‐Gómez, P., Lallena, M., Díaz-Meco, M. T., & Moscat, J. (1999) · The EMBO Journal · doi:10.1093/emboj/18.11.3044 · Cited by 410 · see citing works
Laherty, C. D., Hu, H., Opipari, A. W., Wang, F., & Dixit, V. M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35741-7 · Cited by 409 · see citing works
Fujita, T., Nolan, G. P., Liou, H. C., Scott, M. L., & Baltimore, D. (1993) · Genes & Development · doi:10.1101/gad.7.7b.1354 · Cited by 409 · see citing works
Ionizing radiation induces expression and binding activity of the nuclear factor kappa B.
Brach, M. A., Hass, R., Sherman, M., Gunji, H., Weichselbaum, R. R., & Kufe, D. W. (1991) · Journal of Clinical Investigation · doi:10.1172/jci115354 · Cited by 408 · 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
Regulatory functions of ubiquitination in the immune system
Ben‐Neriah, Y. (2002) · Nature Immunology · doi:10.1038/ni0102-20 · Cited by 403 · see citing works
Casper Is a FADD- and Caspase-Related Inducer of Apoptosis
Shu, H., Halpin, D. R., & Goeddel, D. V. (1997) · Immunity · doi:10.1016/s1074-7613(00)80450-1 · Cited by 399 · see citing works
TNF-Induced Recruitment and Activation of the IKK Complex Require Cdc37 and Hsp90
Chen, G., Cao, P., & Goeddel, D. V. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00450-1 · Cited by 399 · 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
I kappa B epsilon, a novel member of the IκB family, controls RelA and cRel NF‐κB activity
Whiteside, S. T., Epinat, J.-C., Rice, N. R., & Israël, A. (1997) · The EMBO Journal · doi:10.1093/emboj/16.6.1413 · Cited by 396 · see citing works
Caamaño, J., Rizzo, C. A., Durham, S. K., Barton, D. S., Raventós-Suárez, C., Snapper, C. M., & Bravo, R. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.187.2.185 · Cited by 395 · see citing works
Yang, F., Tang, E., Guan, K., & Wang, C. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.170.11.5630 · Cited by 393 · see citing works
Makris, C., Godfrey, V., Krähn‐Senftleben, G., Takahashi, T., Roberts, J. L., Schwarz, T., Feng, L., Johnson, R. S., & Karin, M. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80262-2 · Cited by 393 · see citing works
CARMA1, BCL-10 and MALT1 in lymphocyte development and activation
Thome, M. (2004) · Nature Reviews Immunology · doi:10.1038/nri1352 · Cited by 391 · see citing works
Sizemore, N., Lerner, N., Dombrowski, N., Sakurai, H., & Stark, G. R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110572200 · Cited by 391 · see citing works
JNK2 and IKKβ Are Required for Activating the Innate Response to Viral Infection
Chu, W., Ostertag, D. G., Li, Z.-W., Chang, L., Chen, Y., Hu, Y., Williams, B. R. G., Perrault, J., & Karin, M. (1999) · Immunity · doi:10.1016/s1074-7613(00)80146-6 · Cited by 389 · see citing works
Active Repression of Antiapoptotic Gene Expression by RelA(p65) NF-κB
Campbell, K. J., Rocha, S., & Perkins, N. D. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00131-5 · Cited by 386 · see citing works
Huang, T. T., Kudo, N. R., Yoshida, M., & Miyamoto, S. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.3.1014 · Cited by 381 · see citing works
Bulut, Y., Faure, E., Thomas, L. S., Equils, O., & Arditi, M. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.167.2.987 · Cited by 381 · see citing works
Regulation of NF-κB-Dependent Lymphocyte Activation and Development by Paracaspase
Ruefli-Brasse, A. A., French, D. M., & Dixit, V. M. (2003) · Science · doi:10.1126/science.1090769 · Cited by 381 · see citing works
Bonnard, M., Mirtsos, C., Suzuki, S., Graham, K., Huang, J., Ng, M., Itié, A., Wakeham, A., Shahinian, A., Henzel, W. J., et al. (2000) · The EMBO Journal · doi:10.1093/emboj/19.18.4976 · Cited by 381 · see citing works
Wang, D., & Baldwin, A. S. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.45.29411 · Cited by 375 · see citing works
Sakurai, H., Suzuki, S., Kawasaki, N., Nakano, H., Okazaki, T., CHINO, A., Doi, T., & Saiki, I. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301598200 · Cited by 374 · see citing works
Targeted Disruption of the ζPKC Gene Results in the Impairment of the NF-κB Pathway
Leitges, M., Sanz, L., Martı́n, P., Durán, Á., Braun, U., García, J. F., Camacho, F., Díaz-Meco, M. T., Rennert, P. D., & Moscat, J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00361-6 · Cited by 371 · see citing works
Activation of IκB Kinase β by Protein Kinase C Isoforms
Lallena, M.-J., Díaz-Meco, M. T., Bren, G. D., Payá, C. V., & Moscat, J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.3.2180 · Cited by 360 · see citing works
IKKα controls formation of the epidermis independently of NF-κB
Hu, Y., Baud, V., Oga, T., Kim, K. I., Yoshida, K., & Karin, M. (2001) · Nature · doi:10.1038/35070605 · Cited by 358 · see citing works
Activation of NF‐kappa B in vivo is regulated by multiple phosphorylations.
Naumann, M., & Scheidereit, C. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06781.x · Cited by 355 · see citing works
RelB, a new Rel family transcription activator that can interact with p50-NF-kappa B.
Ryseck, R.-P., Bull, P., Takamiya, M., Bours, V., Siebenlist, U. K., Dobrzański, P., & Bravo, R. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.2.674 · Cited by 355 · see citing works
CARMA1 is a critical lipid raft–associated regulator of TCR-induced NF-κB activation
Gaide, O., Favier, B., Legler, D. F., Bonnet, D., Brissoni, B., Valitutti, S., Bron, C., Tschopp, J., & Thome, M. (2002) · Nature Immunology · doi:10.1038/ni830 · Cited by 343 · see citing works
Bertin, J., Wang, L., Guo, Y., Jacobson, M. D., Poyet, J., Srinivasula, S. M., Merriam, S., DiStefano, P. S., & Alnemri, E. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010512200 · Cited by 343 · see citing works
IκBα Deficiency Results in a Sustained NF-κB Response and Severe Widespread Dermatitis in Mice
Klement, J. F., Rice, N. R., Car, B. D., Abbondanzo, S. J., Powers, G. D., Bhatt, H., Chen, C.-H., Rosen, C. A., & Stewart, C. L. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.5.2341 · Cited by 340 · see citing works
The MAGUK Family Protein CARD11 Is Essential for Lymphocyte Activation
Hara, H., Wada, T., Bakal, C., Kozieradzki, I., Suzuki, S., Suzuki, N., Nghiem, M. P., Griffiths, E. K., Krawczyk, C. M., Bauer, B., et al. (2003) · Immunity · doi:10.1016/s1074-7613(03)00148-1 · Cited by 336 · see citing works
Self-citationECSIT is an evolutionarily conserved intermediate in the Toll/IL-1 signal transduction pathway
Kopp, E., Medzhitov, R., Carothers, J., Xiao, C., Douglas, I., Janeway, C. A., & Ghosh, S. (1999) · Genes & Development · doi:10.1101/gad.13.16.2059 · Cited by 334 · see citing works
Self-citationGenetic analysis of NF‐κB/Rel transcription factors defines functional specificities
Hoffmann, A., Leung, T., & Baltimore, D. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg534 · Cited by 329 · see citing works
IκB Kinase (IKK)-Associated Protein 1, a Common Component of the Heterogeneous IKK Complex
Mercurio, F., Murray, B. W., Shevchenko, A., Bennett, B. L., Young, D. B., Li, J. W., Pascual, G., Motiwala, A., Zhu, H., Mann, M., et al. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.2.1526 · Cited by 325 · see citing works
Gadd45β mediates the NF-κB suppression of JNK signalling by targeting MKK7/JNKK2
Papa, S., Zazzeroni, F., Bubici, C., Jayawardena, S., Alvarez, K., Matsuda, S., Nguyen, D. U., Pham, C. G., Nelsbach, A. H., Melis, T., et al. (2004) · Nature Cell Biology · doi:10.1038/ncb1093 · Cited by 321 · see citing works
Essential role of RelA Ser311 phosphorylation by ζPKC in NF‐κB transcriptional activation
Duran, A., Díaz-Meco, M. T., & Moscat, J. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg370 · Cited by 319 · see citing works
Durán, A., Serrano, M., Leitges, M., Flores, J. M., Picard, S., Brown, J. P., Moscat, J., & Diaz-Meco, M. T. (2004) · Developmental Cell · doi:10.1016/s1534-5807(03)00403-9 · Cited by 316 · see citing works
CK2 Is a C-Terminal IκB Kinase Responsible for NF-κB Activation during the UV Response
Kato, T., Delhase, M., Hoffmann, A., & Karin, M. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00358-7 · Cited by 313 · see citing works
Cotranslational Biogenesis of NF-κB p50 by the 26S Proteasome
Li, L., Demartino, G., & Greene, W. C. (1998) · Cell · doi:10.1016/s0092-8674(00)81409-9 · Cited by 312 · see citing works
Generation of p50 subunit of NF-kB by processing of p105 through an ATP-dependent pathway
Fan, C., & Maniatis, T. (1991) · Nature · doi:10.1038/354395a0 · Cited by 308 · see citing works
Tada, K., Okazaki, T., Sakon, S., Kobarai, T., Kurosawa, K., Yamaoka, S., Hashimoto, H., Mak, T. W., Yagita, H., Okumura, K., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104837200 · Cited by 306 · see citing works
Absence of tumor necrosis factor rescues RelA-deficient mice from embryonic lethality
Doi, T. S., Marino, M. W., Takahashi, T., Yoshida, T., Sakakura, T., Old, L. J., & Obata, Y. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.2994 · Cited by 299 · see citing works
TRAF6, a molecular bridge spanning adaptive immunity, innate immunity and osteoimmunology
Wu, H., & Arron, J. R. (2003) · BioEssays · doi:10.1002/bies.10352 · Cited by 299 · see citing works
Xiao, G., Fong, A., & Sun, S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401428200 · Cited by 296 · see citing works
Doi, T. S., Takahashi, T., Taguchi, O., Azuma, T., & Obata, Y. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.185.5.953 · Cited by 292 · see citing works
IKAP is a scaffold protein of the IκB kinase complex
Cohen, L., Henzel, W. J., & Baeuerle, P. A. (1998) · Nature · doi:10.1038/26254 · Cited by 288 · see citing works
Janssens, S., Burns, K., Tschopp, J., & Beyaert, R. (2002) · Current Biology · doi:10.1016/s0960-9822(02)00712-1 · Cited by 287 · see citing works
Induction of COX‐2 by LPS in macrophages is regulated by Tpl2‐dependent CREB activation signals
Eliopoulos, A. G., Dumitru, C. D., Wang, C., Cho, J., & Tsichlis, P. N. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf478 · Cited by 284 · see citing works
Yamazaki, S., Muta, T., & Takeshige, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103426200 · Cited by 277 · see citing works
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
IκBγ, a 70 kd protein identical to the C-terminal half of p110 NF-κB: A new member of the IκB family
Inoue, J., Kerr, L. D., Kakizuka, A., et al. (1992) · Cell · doi:10.1016/0092-8674(92)90082-n · Cited by 270 · see citing works
Flagged first, then by citations
Research works printed but not linked: 6
- Barroga, C.F., Stevenson, J.K., Schwarz, E.M., and Verma, I.M. 1995. Constitutive phosphorylation of I B ␣ by casein ki- nase II. Proc. Natl. Acad. Sci. 92: 7637-7641.
- Ghosh, G. 2004. NF-B biology at the interface of structure and biochemistry. In Keystone Symposium on NF-B: Biology and pathology (eds. A.R. Ulrich et al.). Keystone Symposia, Snowbird Resort, Snowbird, UT.
- Israel, A. 2004. Biochemical and genetic analysis of the NF-B signaling pathway. In Keystone Symposium on NF-B: Biol- ogy and pathology (eds. A.R. Ulrich et al.). Keystone Sym- posia, Snowbird Resort, Snowbird, UT.
- Li, X. 2004. Act1, a negative regulator in B cell survival. In Keystone Symposium on NF-kB: Biology and pathology (eds.
- Mercurio, F. 2004. IKK-related kinases as a target for drug therapy. In Keystone Symposium on NF-B: Biology and pa- thology (eds. A.R. Ulrich et al.). Keystone Symposia, Snow- bird Resort, Snowbird, UT.
- Scherer, D.C., Brockman, J.A., Chen, Z., Maniatis, T., and Bal- lard, D.W. 1995. Signal-induced degradation of IB␣ requires site-specific ubiquitination. Proc. Natl. Acad. Sci. 92: 11259- 11263.
Cited by
Sorted by citations
Molecular mechanisms of necroptosis: an ordered cellular explosion
Vandenabeele, P., Galluzzi, L., Vanden Berghe, T., & Kroemer, G. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2970 · Cited by 2,382 · see citing works
Integrating cell-signalling pathways with NF-κB and IKK function
Perkins, N. D. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2083 · Cited by 2,350 · see citing works
Crosstalk in NF-κB Signaling Pathways
Oeckinghaus, A., Hayden, M. S., & Ghosh, S. (2011) · Nature Immunology · doi:10.1038/ni.2065 · Cited by 1,942 · see citing works
Self-citationRedox regulation of cell survival
Trachootham, D., Lu, W., Ogasawara, M. A., Valle, N. R.-D., & Huang, P. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1957 · Cited by 1,781 · see citing works
The Immunomodulatory and Anti-Inflammatory Role of Polyphenols
Yahfoufi, N., Alsadi, N., Jambi, M., & Matar, C. (2018) · Nutrients · doi:10.3390/nu10111618 · Cited by 1,737 · see citing works
NF-κB, the first quarter-century: remarkable progress and outstanding questions
Hayden, M. S., & Ghosh, S. (2012) · Genes & Development · doi:10.1101/gad.183434.111 · Cited by 1,693 · see citing works
Self-citationIAP Antagonists Induce Autoubiquitination of c-IAPs, NF-κB Activation, and TNFα-Dependent Apoptosis
Varfolomeev, E., Blankenship, J. W., Wayson, S. M., Fedorova, A. V., Kayagaki, N., Garg, P., Zobel, K., Dynek, J. N., Elliott, L. O., Wallweber, H. J. A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.10.030 · Cited by 1,218 · see citing works
Ubiquitin signalling in the NF-κB pathway
Chen, Z. J. (2005) · Nature Cell Biology · doi:10.1038/ncb0805-758 · Cited by 1,184 · see citing works
Kawahara, T. L. A., Michishita, E., Adler, A. S., Damian, M., Berber, E., Lin, M., McCord, R. A., Ongaigui, K. C. L., Boxer, L. D., Chang, H. Y., et al. (2009) · Cell · doi:10.1016/j.cell.2008.10.052 · Cited by 1,090 · see citing works
Pro-inflammatory cytokines: The link between obesity and osteoarthritis
Wang, T., & He, C. (2018) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2018.10.002 · Cited by 1,034 · see citing works
Lingappan, K. (2018) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2017.11.002 · Cited by 1,051 · see citing works
Inhibiting NF-κB activation by small molecules as a therapeutic strategy
Gupta, S. C., Sundaram, C., Reuter, S., & Aggarwal, B. B. (2010) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2010.05.004 · Cited by 762 · see citing works
S100A8 and S100A9 in inflammation and cancer
Gebhardt, C., Németh, J., Angel, P., & Hess, J. (2006) · Biochemical Pharmacology · doi:10.1016/j.bcp.2006.05.017 · Cited by 696 · see citing works
Perkins, N. D. (2006) · Oncogene · doi:10.1038/sj.onc.1209937 · Cited by 674 · see citing works
Liu, G.-H., Qu, J., & Shen, X. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.01.002 · Cited by 697 · see citing works
Regulation of NFATc1 in Osteoclast Differentiation
Kim, J. H., & Kim, N. (2014) · Journal of Bone Metabolism · doi:10.11005/jbm.2014.21.4.233 · Cited by 570 · see citing works
“[32,33] In the alternative pathway, NF-κB-inducing kinase (NIK) and IKKα phosphorylate and process p100 to generate p52 by proteasomes, resulting in the activation of the p52/RelB complex.”
BackgroundKell, D. B. (2009) · BMC Medical Genomics · doi:10.1186/1755-8794-2-2 · Cited by 554 · 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
Two-site substrate recognition model for the Keap1-Nrf2 system: A hinge and latch mechanism
Tong, K. I., Kobayashi, A., Katsuoka, F., & Yamamoto, M. (2006) · Biological Chemistry · doi:10.1515/bc.2006.164 · Cited by 473 · see citing works
Motif module map reveals enforcement of aging by continual NF-κB activity
Adler, A. S., Sinha, S., Kawahara, T. L. A., Zhang, J. Y., Segal, E., & Chang, H. Y. (2007) · Genes & Development · doi:10.1101/gad.1588507 · Cited by 466 · see citing works
Bubici, C., Papa, S., Dean, K., & Franzoso, G. (2006) · Oncogene · doi:10.1038/sj.onc.1209936 · Cited by 399 · see citing works
Chen, C.-Y., Peng, W.-H., Tsai, K.-D., & Hsu, S.-L. (2007) · Life Sciences · doi:10.1016/j.lfs.2007.09.028 · Cited by 358 · see citing works
What Is Nuclear Factor Kappa B (NF-κB) Doing in and to the Mitochondrion?
Albensi, B. C. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00154 · Cited by 341 · see citing works
Microglial phenotypes in Parkinson’s disease and animal models of the disease
Joers, V., Tansey, M. G., Mulas, G., & Carta, A. R. (2017) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.04.006 · Cited by 285 · see citing works
Beck, I. M. E., Vanden Berghe, W., Vermeulen, L., Yamamoto, K. R., Haegeman, G., & De Bosscher, K. (2009) · Endocrine Reviews · doi:10.1210/er.2009-0013 · Cited by 298 · see citing works
Development of an antioxidant system after early weaning in piglets2
Yin, J., Wu, M. M., Xiao, H., Ren, W. K., Duan, J. L., Yang, G., Li, T. J., & Yin, Y. L. (2014) · Journal of Animal Science · doi:10.2527/jas.2013-6986 · Cited by 289 · see citing works
Cockman, M. E., Lancaster, D. E., Stolze, I. P., Hewitson, K. S., McDonough, M. A., Coleman, M. L., Coles, C. H., Yu, X., Hay, R. T., Ley, S. C., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606877103 · Cited by 285 · see citing works
Osorio, F. G., Bárcena, C., Soria-Valles, C., Ramsay, A. J., de Carlos, F., Cobo, J., Fueyo, A., Freije, J. M. P., & López-Otín, C. (2012) · Genes & Development · doi:10.1101/gad.197954.112 · Cited by 276 · see citing works
Beyond IκBs: alternative regulation of NF‐KB activity
Neumann, M., & Naumann, M. (2007) · The FASEB Journal · doi:10.1096/fj.06-7615rev · Cited by 267 · see citing works
The UV response of the skin: a review of the MAPK, NFκB and TNFα signal transduction pathways
Muthusamy, V., & Piva, T. J. (2010) · Archives of Dermatological Research · doi:10.1007/s00403-009-0994-y · Cited by 265 · see citing works
A nuclear poly(ADP-Ribose)-dependent signalosome confers DNA damage-induced IκB kinase activation.
Stilmann, M., Hinz, M., Arslan, S. Ç., Zimmer, A., Schreiber, V., & Scheidereit, C. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.032 · Cited by 232 · see citing works
The c‐myc Promoter: Still MysterY and Challenge
(2008) · Advances in Cancer Research · doi:10.1016/s0065-230x(07)99004-1 · Cited by 211 · see citing works
Maier, H. J., Schmidt-Straßburger, U., Huber, M. A., Wiedemann, E. M., Beug, H., & Wirth, T. (2010) · Cancer Letters · doi:10.1016/j.canlet.2010.03.003 · Cited by 215 · see citing works
The role of free radicals in the aging brain and Parkinson’s Disease: Convergence and parallelism
Kumar, H., Lim, H.-W., More, S. V., Kim, B.-W., Koppula, S., Kim, I. S., & Choi, D.-K. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms130810478 · Cited by 212 · see citing works
Anti-inflammatory effects of bifidobacteria by inhibition of LPS-induced NF-κB activation
Riedel, C. U. (2006) · World Journal of Gastroenterology · doi:10.3748/wjg.v12.i23.3729 · Cited by 210 · see citing works
Sebe-Pedros, A., de Mendoza, A., Lang, B. F., Degnan, B. M., & Ruiz-Trillo, I. (2011) · Molecular Biology and Evolution · doi:10.1093/molbev/msq309 · Cited by 195 · see citing works
Insulin/IGF-1 paradox of aging: Regulation via AKT/IKK/NF-κB signaling
Salminen, A., & Kaarniranta, K. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2009.10.006 · Cited by 177 · see citing works
Calcitriol blunts the deleterious impact of advanced glycation end products on endothelial cells
Talmor, Y., Golan, E., Benchetrit, S., Bernheim, J., Klein, O., Green, J., & Rashid, G. (2008) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00051.2008 · Cited by 169 · see citing works
Elsharkawy, A. M., Oakley, F., Lin, F., Packham, G., Mann, D. A., & Mann, J. (2010) · Journal of Hepatology · doi:10.1016/j.jhep.2010.03.025 · Cited by 160 · see citing works
C-Reactive protein as a biomarker for major depressive disorder?
Orsolini, L., Pompili, S., Tempia Valenta, S., Salvi, V., & Volpe, U. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031616 · Cited by 171 · see citing works
López-Camarillo, C., Aréchaga Ocampo, E., López Casamichana, M., Pérez-Plasencia, C., Álvarez-Sánchez, E., & Marchat, L. A. (2011) · International Journal of Molecular Sciences · doi:10.3390/ijms13010142 · Cited by 165 · see citing works
Zhang, Q.-S., Heng, Y., Yuan, Y.-H., & Chen, N.-H. (2017) · Toxicology Letters · doi:10.1016/j.toxlet.2016.11.002 · Cited by 156 · see citing works
Thymosin beta 4 suppression of corneal NFκB: A potential anti-inflammatory pathway
Sosne, G., Qiu, P., Christopherson, P. L., & Wheater, M. K. (2007) · Experimental Eye Research · doi:10.1016/j.exer.2006.12.004 · Cited by 139 · see citing works
Structural studies of NF-κB signaling
Zheng, C., Yin, Q., & Wu, H. (2011) · Cell Research · doi:10.1038/cr.2010.171 · Cited by 134 · see citing works
RNAi Screen in Mouse Astrocytes Identifies Phosphatases that Regulate NF-κB Signaling
Li, S., Wang, L., Berman, M. A., Zhang, Y., & Dorf, M. E. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.10.015 · Cited by 132 · see citing works
A pervasive role of ubiquitin conjugation in activation and termination of IκB kinase pathways
Krappmann, D., & Scheidereit, C. (2005) · The EMBO Reports · doi:10.1038/sj.embor.7400380 · Cited by 128 · see citing works
Fluoxetine protects neurons against microglial activation-mediated neurotoxicity
Zhang, F., Zhou, H., Wilson, B. C., Shi, J.-S., Hong, J.-S., & Gao, H.-M. (2012) · Parkinsonism & Related Disorders · doi:10.1016/s1353-8020(11)70066-9 · Cited by 123 · see citing works
Nadjar, A., Bluthé, R.-M., May, M. J., Dantzer, R., & Parnet, P. (2005) · Neuropsychopharmacology · doi:10.1038/sj.npp.1300755 · Cited by 120 · see citing works
RETRACTED: The anti-inflammatory activity of 1,25-dihydroxyvitamin D3 in macrophages
Cohen-Lahav, M., Douvdevani, A., Chaimovitz, C., & Shany, S. (2007) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2006.12.093 · Cited by 118 · see citing works
RetractedRodríguez-Calvo, R., Tajes, M., & Vázquez-Carrera, M. (2017) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2017.1279146 · Cited by 117 · see citing works
Ku, C. S., Pham, T. X., Park, Y., Kim, B., Shin, M. S., Kang, I., & Lee, J. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.01.018 · Cited by 109 · see citing works
Park, Y.-K., Rasmussen, H. E., Ehlers, S. J., Blobaum, K. R., Lu, F., Schlegal, V. L., Carr, T. P., & Lee, J.-Y. (2008) · Nutrition Research · doi:10.1016/j.nutres.2007.11.008 · Cited by 103 · see citing works
Autosomal dominant anhidrotic ectodermal dysplasias at the EDARADD locus
Bal, E., Baala, L., Cluzeau, C., El Kerch, F., Ouldim, K., Hadj-Rabia, S., Bodemer, C., Munnich, A., Courtois, G., Sefiani, A., et al. (2007) · Human Mutation · doi:10.1002/humu.20500 · Cited by 100 · see citing works
Ruiz-García, A., Monsalve, E., Novellasdemunt, L., Navarro-Sabaté, À., Manzano, A., Rivero, S., Castrillo, A., Casado, M., Laborda, J., Bartrons, R., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.190298 · Cited by 95 · see citing works
Li, S.-N., Wang, X., Zeng, Q.-T., Feng, Y.-B., Cheng, X., Mao, X.-B., Wang, T.-H., & Deng, H.-P. (2009) · Heart and Vessels · doi:10.1007/s00380-008-1137-7 · Cited by 88 · see citing works
Atkinson, G. P., Nozell, S. E., Harrison, D. K., Stonecypher, M. S., Chen, D., & Benveniste, E. N. (2009) · Oncogene · doi:10.1038/onc.2009.232 · Cited by 75 · see citing works
Kumar, G. R., Shum, L., & Glaunsinger, B. A. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05402-11 · Cited by 71 · see citing works
Bradesi, S., Svensson, C. I., Steinauer, J., Pothoulakis, C., Yaksh, T. L., & Mayer, E. A. (2009) · Gastroenterology · doi:10.1053/j.gastro.2008.12.044 · Cited by 69 · see citing works
Noncoding RNAs regulate NF-κB signaling to modulate blood vessel inflammation
Cheng, H. S., Njock, M.-S., Khyzha, N., Dang, L. T., & Fish, J. E. (2014) · Frontiers in Genetics · doi:10.3389/fgene.2014.00422 · Cited by 69 · see citing works
Identification of novel mechanisms involved in generating localized vulvodynia pain
Falsetta, M. L., Foster, D. C., Woeller, C. F., Pollock, S. J., Bonham, A. D., Haidaris, C. G., Stodgell, C. J., & Phipps, R. P. (2015) · American Journal of Obstetrics and Gynecology · doi:10.1016/j.ajog.2015.02.002 · Cited by 69 · see citing works
Hepatic Nuclear Factor κB Regulates Neutrophil Recruitment to the Injured Brain
Campbell, S. J., Anthony, D. C., Oakley, F., Carlsen, H., Elsharkawy, A. M., Blomhoff, R., & Mann, D. A. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181654957 · Cited by 67 · see citing works
Metformin activation of AMPK suppresses AGE-induced inflammatory response in hNSCs
Chung, M.-M., Nicol, C. J., Cheng, Y.-C., Lin, K.-H., Chen, Y.-L., Pei, D., Lin, C.-H., Shih, Y.-N., Yen, C.-H., Chen, S.-J., et al. (2017) · Experimental Cell Research · doi:10.1016/j.yexcr.2017.01.017 · Cited by 66 · see citing works
Wang, C.-Y., Xie, J.-W., Xu, Y., Wang, T., Cai, J.-H., Wang, X., Zhao, B.-L., An, L., & Wang, Z.-Y. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.5158 · Cited by 66 · see citing works
Wieck, A., Grassi-Oliveira, R., do Prado, C. H., Rizzo, L. B., de Oliveira, A. S., Kommers-Molina, J., Viola, T. W., Teixeira, A. L., & Bauer, M. E. (2013) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2013.07.005 · Cited by 63 · see citing works
Galectin-3 Modulates Th17 Responses by Regulating Dendritic Cell Cytokines
Fermin Lee, A., Chen, H.-Y., Wan, L., Wu, S.-Y., Yu, J.-S., Huang, A. C., Miaw, S.-C., Hsu, D. K., Wu-Hsieh, B. A., & Liu, F.-T. (2013) · The American Journal of Pathology · doi:10.1016/j.ajpath.2013.06.017 · Cited by 63 · see citing works
Lee, S. A., Kim, H. J., Chang, K. C., Baek, J. C., Park, J. K., Shin, J. K., Choi, W. J., Lee, J. H., & Paik, W. Y. (2009) · The Korean Journal of Physiology and Pharmacology · doi:10.4196/kjpp.2009.13.4.301 · Cited by 53 · see citing works
The Interaction Between NF-κB and Estrogen in Alzheimer’s Disease
Mishra, P., Davies, D. A., & Albensi, B. C. (2023) · Molecular Neurobiology · doi:10.1007/s12035-022-03152-3 · Cited by 51 · see citing works
Hwang, S.-K., Baker, A. R., Young, M. R., & Colburn, N. H. (2014) · Carcinogenesis · doi:10.1093/carcin/bgu008 · Cited by 49 · see citing works
Relevance of new drug discovery to reduce NF-κB activation in cardiovascular disease
Madonna, R., & De Caterina, R. (2012) · Vascular Pharmacology · doi:10.1016/j.vph.2012.02.005 · Cited by 46 · see citing works
Naujokat, C., Berges, C., Höh, A., Wieczorek, H., Fuchs, D., Ovens, J., Miltz, M., Sadeghi, M., Opelz, G., & Daniel, V. (2007) · Immunology · doi:10.1111/j.1365-2567.2006.02487.x · Cited by 41 · see citing works
Mechanisms of HIV transcriptional regulation by drugs of abuse
Tyagi, M., Bukrinsky, M., & L. Simon, G. (2016) · Current HIV Research · doi:10.2174/1570162x14666160324124736 · Cited by 42 · see citing works
Breuer, R., Becker, M. S., Brechmann, M., Mock, T., Arnold, R., & Krammer, P. H. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.533547 · Cited by 40 · see citing works
Encephalomyocarditis Virus 2A Protein Is Required for Viral Pathogenesis and Inhibition of Apoptosis
Carocci, M., Cordonnier, N., Huet, H., Romey, A., Relmy, A., Gorna, K., Blaise-Boisseau, S., Zientara, S., & Kassimi, L. B. (2011) · Journal of Virology · doi:10.1128/jvi.00394-11 · Cited by 34 · see citing works
Klein, B. Y., Tamir, H., Ludwig, R. J., Glickstein, S. B., & Welch, M. G. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.04.011 · Cited by 31 · see citing works
New treatment regimes for virus-induced exacerbations of asthma
Edwards, M. R., Kebadze, T., Johnson, M. W., & Johnston, S. L. (2006) · Pulmonary Pharmacology & Therapeutics · doi:10.1016/j.pupt.2005.09.005 · Cited by 30 · see citing works
AlKhoury, H., Hautmann, A., Erdmann, F., Zhou, G., Stojanović, S., Najman, S., & Groth, T. (2020) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.36885 · Cited by 30 · see citing works
Shen, C., Zhao, X.-L., Ju, W., Zou, X.-B., Huo, L.-R., Yan, W., Zou, J.-H., Yan, G.-D., Jenkins, E. C., Brown, W. T., et al. (2011) · Journal of Molecular Neuroscience · doi:10.1007/s12031-010-9463-5 · Cited by 18 · see citing works
Wäster, P., Rosdahl, I., & Öllinger, K. (2014) · British Journal of Dermatology · doi:10.1111/bjd.13278 · Cited by 15 · see citing works
Incontinentia pigmenti in adults
Scheuerle, A. E. (2019) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.61205 · Cited by 13 · see citing works
UVB-stimulated TNFα release from human melanocyte and melanoma cells is mediated by p38 MAPK
Muthusamy, V., & Piva, T. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms140817029 · Cited by 11 · see citing works
- Authors
- Hayden, M. S., & Ghosh, S.
- Affiliations
- Yale University (US)
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2004-09-15
- Volume
- 18
- Issue
- 18
- Pages
- 2195-2224
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- OpenAlex
- W2148119611
- Cited by
- 3,842
- References
- 367
- Citations by year
- 2026: 42 · 2025: 59 · 2024: 82 · 2023: 76 · 2022: 110 · 2021: 166 · 2020: 137 · 2019: 116 · 2018: 152 · 2017: 126 · 2016: 181 · 2015: 193 · 2014: 243 · 2013: 234 · 2012: 239
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (1r01ai059440-01)
- National Institute of General Medical Sciences (GM07205, T32GM007205)
- National Institute of Allergy and Infectious Diseases (R37 AI33443, R37AI033443, AI59440)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Keywords
- NF-κB, NF-κB signaling, transcriptional regulation, signal transduction
- MeSH terms
- Animals, Gene Expression Regulation, Humans, Transcription, Genetic, Signal Transduction, NF-kappa B, Protein Serine-Threonine Kinases, I-kappa B Proteins, I-kappa B Kinase
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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.
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