The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
Shared Principles in NF-κB Signaling
Abstract
The transcription factor NF-kappaB has served as a standard for inducible transcription factors for more than 20 years. The numerous stimuli that activate NF-kappaB, and the large number of genes regulated by NF-kappaB, ensure that this transcription factor is still the subject of intense research. Here, we attempt to synthesize some of the basic principles that have emerged from studies of NF-kappaB, and we aim to generate a more unified view of NF-kappaB regulation.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Predominately under IL1β stimulation, negative regulators of AP-1 (Dusp1/2/5/6) and NF-κB signaling (Nfkbia) are upregulated49,50.”
From Clonal hematopoiesis related TET2 loss-of-function impedes IL1β-mediated epigenetic reprogramming in hematopoietic stem and progenitor cells (2023) · cites this paper as [50]
Citations
Cites
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
Self-citationNuclear factor-κB in cancer development and progression
Karin, M. (2006) · Nature · doi:10.1038/nature04870 · Cited by 3,519
IAP 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
Hayden, M. S., West, A. P., & Ghosh, S. (2006) · Oncogene · doi:10.1038/sj.onc.1209943 · Cited by 1,178
Self-citationPerkins, N. D. (2006) · Oncogene · doi:10.1038/sj.onc.1209937 · Cited by 674
SOCS1/JAB Is a Negative Regulator of LPS-Induced Macrophage Activation
Kinjyo, I., Hanada, T., Inagaki-Ohara, K., Mori, H., Aki, D., Ohishi, M., Yoshida, H., Kubo, M., & Yoshimura, A. (2002) · Immunity · doi:10.1016/s1074-7613(02)00446-6 · Cited by 630
Transcriptional Cross Talk between NF-κB and p53
Webster, G. A., & Perkins, N. D. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.5.3485 · Cited by 598
NF-κB RelA Phosphorylation Regulates RelA Acetylation
Chen, L.-F., Williams, S. A., Mu, Y., Nakano, H., Duerr, J. M., Buckbinder, L., & Greene, W. C. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.18.7966-7975.2005 · Cited by 438
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
Ubiquitination of RIP Is Required for Tumor Necrosis Factor α-induced NF-κB Activation
Li, H., Kobayashi, M., Blonska, M., You, Y., & Lin, X. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600620200 · Cited by 277
Research works printed but not linked: 161
- Abbott, 2007, Coordinated regulation of Toll-like receptor and NOD2 signaling by K63-linked polyubiquitin chains, Mol. Cell. Biol., 27, 6012, 10.1128/MCB.00270-07 · DOI
- Acharyya, 2007, Interplay of IKK/NF-kappaB signaling in macrophages and myofibers promotes muscle degeneration in Duchenne muscular dystrophy, J. Clin. Invest., 117, 889, 10.1172/JCI30556 · DOI
- Adler, 2007, Motif module map reveals enforcement of aging by continual NF-{kappa}B activity, Genes Dev., 21, 3244, 10.1101/gad.1588507 · DOI · Paper page
- Agou, 2004, The trimerization domain of NEMO is comprised of the interacting C-terminal CC2 and LZ coiled-coil subdomains, J. Biol. Chem., 279, 27861, 10.1074/jbc.M314278200 · DOI
- Amir, 2004, Mechanism of processing of the NF-kappa B2 p100 precursor: identification of the specific polyubiquitin chain-anchoring lysine residue and analysis of the role of NEDD8-modification on the SCF(beta-TrCP) ubiquitin ligase, Oncogene, 23, 2540, 10.1038/sj.onc.1207366 · DOI
- Anest, 2003, A nucleosomal function for IkappaB kinase-alpha in NF-kappaB-dependent gene expression, Nature, 423, 659, 10.1038/nature01648 · DOI
- Basak, 2007, A fourth IkappaB protein within the NF-kappaB signaling module, Cell, 128, 369, 10.1016/j.cell.2006.12.033 · DOI
- Bird, 1997, Activation of nuclear transcription factor NF-kappaB by interleukin-1 is accompanied by casein kinase II-mediated phosphorylation of the p65 subunit, J. Biol. Chem., 272, 32606, 10.1074/jbc.272.51.32606 · DOI
- Blonska, 2005, TAK1 is recruited to the tumor necrosis factor-alpha (TNF-alpha) receptor 1 complex in a receptor-interacting protein (RIP)-dependent manner and cooperates with MEKK3 leading to NF-kappaB activation, J. Biol. Chem., 280, 43056, 10.1074/jbc.M507807200 · DOI
- Bonizzi, 2004, Activation of IKKalpha target genes depends on recognition of specific kappaB binding sites by RelB:p52 dimers, EMBO J., 23, 4202, 10.1038/sj.emboj.7600391 · DOI
- Bonnard, 2000, Deficiency of T2K leads to apoptotic liver degeneration and impaired NF-kappaB-dependent gene transcription, EMBO J., 19, 4976, 10.1093/emboj/19.18.4976 · DOI
- Bours, 1993, The oncoprotein Bcl-3 directly transactivates through kappa B motifs via association with DNA-binding p50B homodimers, Cell, 72, 729, 10.1016/0092-8674(93)90401-B · DOI
- Britanova, 2008, In vitro selection of optimal RelB/p52 DNA-binding motifs, Biochem. Biophys. Res. Commun., 365, 583, 10.1016/j.bbrc.2007.10.200 · DOI
- Carmody, 2007, Negative regulation of toll-like receptor signaling by NF-kappaB p50 ubiquitination blockade, Science, 317, 675, 10.1126/science.1142953 · DOI
- Chen, 2002, TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90, Mol. Cell, 9, 401, 10.1016/S1097-2765(02)00450-1 · DOI
- Chen, 2004, Shaping the nuclear action of NF-kappaB, Nat. Rev. Mol. Cell Biol., 5, 392, 10.1038/nrm1368 · DOI
- Chen, 2002, Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-kappaB, EMBO J., 21, 6539, 10.1093/emboj/cdf660 · DOI · Paper page
- Chen, 1996, Site-specific phosphorylation of IkappaBalpha by a novel ubiquitination-dependent protein kinase activity, Cell, 84, 853, 10.1016/S0092-8674(00)81064-8 · DOI
- Cheng, 1998, Functional redundancy of the nuclear factor kappa B inhibitors I kappa B alpha and I kappa B beta, J. Exp. Med., 188, 1055, 10.1084/jem.188.6.1055 · DOI
- Cohen, 2001, Processing of p105 is inhibited by docking of p50 active subunits to the ankyrin repeat domain, and inhibition is alleviated by signaling via the carboxyl-terminal phosphorylation/ ubiquitin-ligase binding domain, J. Biol. Chem., 276, 26769, 10.1074/jbc.M102448200 · DOI
- Cohen, 2004, Dual effects of IkappaB kinase beta-mediated phosphorylation on p105 fate: SCF(beta-TrCP)-dependent degradation and SCF(beta-TrCP)-independent processing, Mol. Cell. Biol., 24, 475, 10.1128/MCB.24.1.475-486.2004 · DOI
- Courtois, 2006, Mutations in the NF-kappaB signaling pathway: implications for human disease, Oncogene, 25, 6831, 10.1038/sj.onc.1209939 · DOI
- Cusson-Hermance, 2005, Rip1 mediates the Trif-dependent toll-like receptor 3- and 4-induced NF-{kappa}B activation but does not contribute to interferon regulatory factor 3 activation, J. Biol. Chem., 280, 36560, 10.1074/jbc.M506831200 · DOI
- De Bosscher, 2006, Cross-talk between nuclear receptors and nuclear factor kappaB, Oncogene, 25, 6868, 10.1038/sj.onc.1209935 · DOI
- Delhase, 1999, Positive and negative regulation of IkappaB kinase activity through IKKbeta subunit phosphorylation, Science, 284, 309, 10.1126/science.284.5412.309 · DOI
- Deng, 2000, Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain, Cell, 103, 351, 10.1016/S0092-8674(00)00126-4 · DOI · Paper page
- Devin, 2000, The distinct roles of TRAF2 and RIP in IKK activation by TNF-R1: TRAF2 recruits IKK to TNF-R1 while RIP mediates IKK activation, Immunity, 12, 419, 10.1016/S1074-7613(00)80194-6 · DOI
- Devin, 2001, The alpha and beta subunits of IkappaB kinase (IKK) mediate TRAF2-dependent IKK recruitment to tumor necrosis factor (TNF) receptor 1 in response to TNF, Mol. Cell. Biol., 21, 3986, 10.1128/MCB.21.12.3986-3994.2001 · DOI
- DiDonato, 1997, A cytokine-responsive IkappaB kinase that activates the transcription factor NF-kappaB, Nature, 388, 548, 10.1038/41493 · DOI · Paper page
- Drew, 2007, Inhibitor kappaB kinase beta binding by inhibitor kappaB kinase gamma, Biochemistry, 46, 12482, 10.1021/bi701137a · DOI
- Ducut Sigala, 2004, Activation of transcription factor NF-kappaB requires ELKS, an IkappaB kinase regulatory subunit, Science, 304, 1963, 10.1126/science.1098387 · DOI
- Duran, 2003, Essential role of RelA Ser311 phosphorylation by zetaPKC in NF-kappaB transcriptional activation, EMBO J., 22, 3910, 10.1093/emboj/cdg370 · DOI
- Ea, 2006, Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO, Mol. Cell, 22, 245, 10.1016/j.molcel.2006.03.026 · DOI
- Fong, 2002, S9, a 19 S proteasome subunit interacting with ubiquitinated NF-kappaB2/p100, J. Biol. Chem., 277, 40697, 10.1074/jbc.M205330200 · DOI
- Fukushima, 2007, Ubiquitin-conjugating enzyme Ubc13 is a critical component of TNF receptor-associated factor (TRAF)-mediated inflammatory responses, Proc. Natl. Acad. Sci. USA, 104, 6371, 10.1073/pnas.0700548104 · DOI
- Gerondakis, 2006, Unravelling the complexities of the NF-kappaB signalling pathway using mouse knockout and transgenic models, Oncogene, 25, 6781, 10.1038/sj.onc.1209944 · DOI
- Goudeau, 2003, IkappaBalpha/IkappaBepsilon deficiency reveals that a critical NF-kappaB dosage is required for lymphocyte survival, Proc. Natl. Acad. Sci. USA, 100, 15800, 10.1073/pnas.2535880100 · DOI
- Habelhah, 2004, Ubiquitination and translocation of TRAF2 is required for activation of JNK but not of p38 or NF-kappaB, EMBO J., 23, 322, 10.1038/sj.emboj.7600044 · DOI
- Hacker, 2006, Regulation and function of IKK and IKK-related kinases, Sci. STKE, 2006, re13, 10.1126/stke.3572006re13 · DOI
- Hacker, 2006, Specificity in Toll-like receptor signalling through distinct effector functions of TRAF3 and TRAF6, Nature, 439, 204, 10.1038/nature04369 · DOI
- Harhaj, 1996, Inhibition of p105 processing by NF-kappaB proteins in transiently transfected cells, Oncogene, 12, 2385
- Hasegawa, 2007, A critical role of RICK/RIP2 polyubiquitination in Nod-induced NF-kappaB activation, EMBO J.
- Hauer, 2005, TNF receptor (TNFR)-associated factor (TRAF) 3 serves as an inhibitor of TRAF2/5-mediated activation of the noncanonical NF-kappaB pathway by TRAF-binding TNFRs, Proc. Natl. Acad. Sci. USA, 102, 2874, 10.1073/pnas.0500187102 · DOI
- Hayden, 2004, Signaling to NF-kappaB, Genes Dev., 18, 2195, 10.1101/gad.1228704 · DOI · Paper page
- He, 2006, Rescue of TRAF3-null mice by p100 NF-kappa B deficiency, J. Exp. Med., 203, 2413, 10.1084/jem.20061166 · DOI
- Hinz, 2007, Signal responsiveness of IkappaB kinases is determined by Cdc37-assisted transient interaction with Hsp90, J. Biol. Chem., 282, 32311, 10.1074/jbc.M705785200 · DOI
- Hoberg, 2006, IkappaB kinase alpha-mediated derepression of SMRT potentiates acetylation of RelA/p65 by p300, Mol. Cell. Biol., 26, 457, 10.1128/MCB.26.2.457-471.2006 · DOI
- Hoeflich, 2000, Requirement for glycogen synthase kinase-3beta in cell survival and NF- kappaB activation, Nature, 406, 86, 10.1038/35017574 · DOI
- Hoffmann, 2002, The IkappaB-NF-kappaB signaling module: temporal control and selective gene activation, Science, 298, 1241, 10.1126/science.1071914 · DOI
- Hoffmann, 2003, Genetic analysis of NF-kappaB/Rel transcription factors defines functional specificities, EMBO J., 22, 5530, 10.1093/emboj/cdg534 · DOI
- Hoffmann, 2006, Transcriptional regulation via the NF-kappaB signaling module, Oncogene, 25, 6706, 10.1038/sj.onc.1209933 · DOI
- Hsu, 1996, TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways, Cell, 84, 299, 10.1016/S0092-8674(00)80984-8 · DOI
- Huang, 2007, Phosphorylation of CBP by IKKalpha promotes cell growth by switching the binding preference of CBP from p53 to NF-kappaB, Mol. Cell, 26, 75, 10.1016/j.molcel.2007.02.019 · DOI
- Hur, 2003, The death domain kinase RIP has an essential role in DNA damage-induced NF-kappa B activation, Genes Dev., 17, 873, 10.1101/gad.1062403 · DOI
- Huynh, 2000, Characterization of the recombinant IKK1/IKK2 heterodimer. Mechanisms regulating kinase activity, J. Biol. Chem., 275, 25883, 10.1074/jbc.M000296200 · DOI
- Inohara, 2003, NODs: intracellular proteins involved in inflammation and apoptosis, Nat. Rev. Immunol., 3, 371, 10.1038/nri1086 · DOI
- Inohara, 2000, An induced proximity model for NF-kappa B activation in the Nod1/RICK and RIP signaling pathways, J. Biol. Chem., 275, 27823, 10.1074/jbc.M003415200 · DOI
- Ishimaru, 2006, Regulation of naive T cell function by the NF-kappaB2 pathway, Nat. Immunol., 7, 763, 10.1038/ni1351 · DOI
- Janssens, 2005, PIDD mediates NF-kappaB activation in response to DNA damage, Cell, 123, 1079, 10.1016/j.cell.2005.09.036 · DOI
- Kashatus, 2006, Expression of the Bcl-3 proto-oncogene suppresses p53 activation, Genes Dev., 20, 225, 10.1101/gad.1352206 · DOI
- Kearns, 2006, IkappaBepsilon provides negative feedback to control NF-kappaB oscillations, signaling dynamics, and inflammatory gene expression, J. Cell Biol., 173, 659, 10.1083/jcb.200510155 · DOI
- Kelliher, 1998, The death domain kinase RIP mediates the TNF-induced NF-kappaB signal, Immunity, 8, 297, 10.1016/S1074-7613(00)80535-X · DOI · Paper page
- Khoshnan, 1999, Primary human CD4+ T cells contain heterogeneous I kappa B kinase complexes: role in activation of the IL-2 promoter, J. Immunol., 163, 5444, 10.4049/jimmunol.163.10.5444 · DOI
- Kim, 2008, TAK1 Is a central mediator of NOD2 signaling in epidermal cells, J. Biol. Chem., 283, 137, 10.1074/jbc.M704746200 · DOI
- Kobayashi, 2001, Segregation of TRAF6-mediated signaling pathways clarifies its role in osteoclastogenesis, EMBO J., 20, 1271, 10.1093/emboj/20.6.1271 · DOI
- Krappmann, 2000, The I kappa B kinase (IKK) complex is tripartite and contains IKK gamma but not IKAP as a regular component, J. Biol. Chem., 275, 29779, 10.1074/jbc.M003902200 · DOI
- Kray, 2005, Positive regulation of IkappaB kinase signaling by protein serine/threonine phosphatase 2A, J. Biol. Chem., 280, 35974, 10.1074/jbc.M506093200 · DOI
- Kwak, 2000, Analysis of domains in the IKKalpha and IKKbeta proteins that regulate their kinase activity, J. Biol. Chem., 275, 14752, 10.1074/jbc.M001039200 · DOI
- Lamothe, 2007, Site-specific Lys-63-linked tumor necrosis factor receptor-associated factor 6 auto-ubiquitination is a critical determinant of I kappa B kinase activation, J. Biol. Chem., 282, 4102, 10.1074/jbc.M609503200 · DOI
- Lawrence, 2005, IKKalpha limits macrophage NF-kappaB activation and contributes to the resolution of inflammation, Nature, 434, 1138, 10.1038/nature03491 · DOI
- Lee, 2004, The kinase activity of Rip1 is not required for tumor necrosis factor-alpha-induced IkappaB kinase or p38 MAP kinase activation or for the ubiquitination of Rip1 by Traf2, J. Biol. Chem., 279, 33185, 10.1074/jbc.M404206200 · DOI
- Leung, 2004, One nucleotide in a kappaB site can determine cofactor specificity for NF-kappaB dimers, Cell, 118, 453, 10.1016/j.cell.2004.08.007 · DOI
- Li, 2005, Enhanced NF-kappaB activation and cellular function in macrophages lacking IkappaB kinase 1 (IKK1), Proc. Natl. Acad. Sci. USA, 102, 12425, 10.1073/pnas.0505997102 · DOI
- Li, 2006, RNAi screen in mouse astrocytes identifies phosphatases that regulate NF-kappaB signaling, Mol. Cell, 24, 497, 10.1016/j.molcel.2006.10.015 · DOI · Paper page
- Liang, 2006, beta-TrCP binding and processing of NF-kappaB2/p100 involve its phosphorylation at serines 866 and 870, Cell. Signal., 18, 1309, 10.1016/j.cellsig.2005.10.011 · DOI
- Liao, 2004, Regulation of the NF-kappaB-inducing kinase by tumor necrosis factor receptor-associated factor 3-induced degradation, J. Biol. Chem., 279, 26243, 10.1074/jbc.M403286200 · DOI
- Lin, 1998, Cotranslational biogenesis of NF-kappaB p50 by the 26S proteasome, Cell, 92, 819, 10.1016/S0092-8674(00)81409-9 · DOI
- Lin, 2000, Cotranslational dimerization of the Rel homology domain of NF-kappaB1 generates p50-p105 heterodimers and is required for effective p50 production, EMBO J., 19, 4712, 10.1093/emboj/19.17.4712 · DOI
- Liu, 2006, Essential role of TAK1 in thymocyte development and activation, Proc. Natl. Acad. Sci. USA, 103, 11677, 10.1073/pnas.0603089103 · DOI
- Luo, 2007, Nuclear cytokine-activated IKKalpha controls prostate cancer metastasis by repressing Maspin, Nature, 446, 690, 10.1038/nature05656 · DOI
- Maine, 2007, COMMD1 promotes the ubiquitination of NF-kappaB subunits through a cullin-containing ubiquitin ligase, EMBO J., 26, 436, 10.1038/sj.emboj.7601489 · DOI
- Makris, 2002, The carboxyl-terminal region of IkappaB kinase gamma (IKKgamma) is required for full IKK activation, Mol. Cell. Biol., 22, 6573, 10.1128/MCB.22.18.6573-6581.2002 · DOI
- Marienfeld, 2006, Dimerization of the I kappa B kinase-binding domain of NEMO is required for tumor necrosis factor alpha-induced NF-kappa B activity, Mol. Cell. Biol., 26, 9209, 10.1128/MCB.00478-06 · DOI
- Martin, 2005, Toll-like receptor-mediated cytokine production is differentially regulated by glycogen synthase kinase 3, Nat. Immunol., 6, 777, 10.1038/ni1221 · DOI
- Massoumi, 2006, Cyld inhibits tumor cell proliferation by blocking Bcl-3-dependent NF-kappaB signaling, Cell, 125, 665, 10.1016/j.cell.2006.03.041 · DOI
- May, 2000, Selective inhibition of NF-kappaB activation by a peptide that blocks the interaction of NEMO with the IkappaB kinase complex, Science, 289, 1550, 10.1126/science.289.5484.1550 · DOI
- May, 2002, Characterization of the Ikappa B-kinase NEMO binding domain, J. Biol. Chem., 277, 45992, 10.1074/jbc.M206494200 · DOI
- McCarthy, 1998, RIP2 is a novel NF-kappaB-activating and cell death-inducing kinase, J. Biol. Chem., 273, 16968, 10.1074/jbc.273.27.16968 · DOI
- McKenzie, 2000, Functional isoforms of IkappaB kinase alpha (IKKalpha) lacking leucine zipper and helix-loop-helix domains reveal that IKKalpha and IKKbeta have different activation requirements, Mol. Cell. Biol., 20, 2635, 10.1128/MCB.20.8.2635-2649.2000 · DOI
- Mercurio, 1997, IKK-1 and IKK-2: cytokine-activated IkappaB kinases essential for NF- kappaB activation, Science, 278, 860, 10.1126/science.278.5339.860 · DOI
- Mercurio, 1999, IkappaB kinase (IKK)-associated protein 1, a common component of the heterogeneous IKK complex, Mol. Cell. Biol., 19, 1526, 10.1128/MCB.19.2.1526 · DOI
- Meylan, 2005, The RIP kinases: crucial integrators of cellular stress, Trends Biochem. Sci., 30, 151, 10.1016/j.tibs.2005.01.003 · DOI
- Meylan, 2004, RIP1 is an essential mediator of Toll-like receptor 3-induced NF-kappa B activation, Nat. Immunol., 5, 503, 10.1038/ni1061 · DOI
- Miller, 2001, Complete reconstitution of human IkappaB kinase (IKK) complex in yeast. Assessment of its stoichiometry and the role of IKKgamma on the complex activity in the absence of stimulation, J. Biol. Chem., 276, 36320, 10.1074/jbc.M104051200 · DOI
- Moorthy, 2006, The 20S proteasome processes NF-kappaB1 p105 into p50 in a translation-independent manner, EMBO J., 25, 1945, 10.1038/sj.emboj.7601081 · DOI
- Motoyama, 2005, Positive and negative regulation of nuclear factor-kappaB-mediated transcription by IkappaB-zeta, an inducible nuclear protein, J. Biol. Chem., 280, 7444, 10.1074/jbc.M412738200 · DOI
- Nakagawa, 2002, SOCS-1 participates in negative regulation of LPS responses, Immunity, 17, 677, 10.1016/S1074-7613(02)00449-1 · DOI
- Nakano, 1999, Targeted disruption of Traf5 gene causes defects in CD40- and CD27-mediated lymphocyte activation, Proc. Natl. Acad. Sci. USA, 96, 9803, 10.1073/pnas.96.17.9803 · DOI
- Natoli, 2005, Interactions of NF-kappaB with chromatin: the art of being at the right place at the right time, Nat. Immunol., 6, 439, 10.1038/ni1196 · DOI
- Newton, 2004, Kinase RIP3 is dispensable for normal NF-kappa Bs, signaling by the B-cell and T-cell receptors, tumor necrosis factor receptor 1, and Toll-like receptors 2 and 4, Mol. Cell. Biol., 24, 1464, 10.1128/MCB.24.4.1464-1469.2004 · DOI
- Oeckinghaus, 2007, Malt1 ubiquitination triggers NF-kappaB signaling upon T-cell activation, EMBO J., 26, 4634, 10.1038/sj.emboj.7601897 · DOI
- Oganesyan, 2006, Critical role of TRAF3 in the Toll-like receptor-dependent and -independent antiviral response, Nature, 439, 208, 10.1038/nature04374 · DOI
- Palkowitsch, 2008, Phosphorylation of serine 68 in the I{kappa}B kinase (IKK)-binding domain of NEMO interferes with the structure of the IKK complex and tumor necrosis factor-{alpha}-induced NF-{kappa}B activity, J. Biol. Chem., 283, 76, 10.1074/jbc.M708856200 · DOI
- Park, 2007, RICK/RIP2 mediates innate immune responses induced through Nod1 and Nod2 but not TLRs, J. Immunol., 178, 2380, 10.4049/jimmunol.178.4.2380 · DOI
- Pasparakis, 2006, Dissection of the NF-kappaB signalling cascade in transgenic and knockout mice, Cell Death Differ., 13, 861, 10.1038/sj.cdd.4401870 · DOI
- Petersen, 2007, Autocrine TNFalpha signaling renders human cancer cells susceptible to Smac-mimetic-induced apoptosis, Cancer Cell, 12, 445, 10.1016/j.ccr.2007.08.029 · DOI
- Poyet, 2000, Activation of the Ikappa B kinases by RIP via IKKgamma /NEMO-mediated oligomerization, J. Biol. Chem., 275, 37966, 10.1074/jbc.M006643200 · DOI
- Prajapati, 2004, Protein phosphatase 2Cbeta association with the IkappaB kinase complex is involved in regulating NF-kappaB activity, J. Biol. Chem., 279, 1739, 10.1074/jbc.M306273200 · DOI
- Qing, 2005, Essential role of IkappaB kinase alpha in the constitutive processing of NF-kappaB2 p100, J. Biol. Chem., 280, 9765, 10.1074/jbc.C400502200 · DOI
- Ramirez-Carrozzi, 2006, Selective and antagonistic functions of SWI/SNF and Mi-2beta nucleosome remodeling complexes during an inflammatory response, Genes Dev., 20, 282, 10.1101/gad.1383206 · DOI
- Regnier, 1997, Identification and characterization of an IκB kinase, Cell, 90, 373, 10.1016/S0092-8674(00)80344-X · DOI
- Rocha, 2003, p53 represses cyclin D1 transcription through down regulation of Bcl-3 and inducing increased association of the p52 NF-kappaB subunit with histone deacetylase 1, Mol. Cell. Biol., 23, 4713, 10.1128/MCB.23.13.4713-4727.2003 · DOI
- Rothwarf, 1998, IKK-gamma is an essential regulatory subunit of the IkappaB kinase complex, Nature, 395, 297, 10.1038/26261 · DOI
- Ruefli-Brasse, 2004, Rip2 participates in Bcl10 signaling and T-cell receptor-mediated NF-kappaB activation, J. Biol. Chem., 279, 1570, 10.1074/jbc.C300460200 · DOI
- Saccani, 2001, Two waves of nuclear factor kappaB recruitment to target promoters, J. Exp. Med., 193, 1351, 10.1084/jem.193.12.1351 · DOI
- Saccani, 2004, Degradation of promoter-bound p65/RelA is essential for the prompt termination of the nuclear factor kappaB response, J. Exp. Med., 200, 107, 10.1084/jem.20040196 · DOI
- Samson, 2004, Combined deficiency in IkappaBalpha and IkappaBepsilon reveals a critical window of NF-kappaB activity in natural killer cell differentiation, Blood, 103, 4573, 10.1182/blood-2003-08-2975 · DOI
- Sato, 2005, Essential function for the kinase TAK1 in innate and adaptive immune responses, Nat. Immunol., 6, 1087, 10.1038/ni1255 · DOI
- Scheidereit, 2006, IkappaB kinase complexes: gateways to NF-kappaB activation and transcription, Oncogene, 25, 6685, 10.1038/sj.onc.1209934 · DOI
- Schmidt-Supprian, 2000, NEMO/IKK gamma-deficient mice model incontinentia pigmenti, Mol. Cell, 5, 981, 10.1016/S1097-2765(00)80263-4 · DOI
- Schomer-Miller, 2006, Regulation of IkappaB kinase (IKK) complex by IKKgamma-dependent phosphorylation of the T-loop and C terminus of IKKbeta, J. Biol. Chem., 281, 15268, 10.1074/jbc.M513793200 · DOI
- Schreiber, 2006, Coordinated binding of NF-kappaB family members in the response of human cells to lipopolysaccharide, Proc. Natl. Acad. Sci. USA, 103, 5899, 10.1073/pnas.0510996103 · DOI
- Schulze-Luehrmann, 2006, Antigen-receptor signaling to nuclear factor kappa B, Immunity, 25, 701, 10.1016/j.immuni.2006.10.010 · DOI
- Senftleben, 2001, Activation by IKKalpha of a second, evolutionary conserved, NF-kappa B signaling pathway, Science, 293, 1495, 10.1126/science.1062677 · DOI
- Shim, 2005, TAK1, but not TAB1 or TAB2, plays an essential role in multiple signaling pathways in vivo, Genes Dev., 19, 2668, 10.1101/gad.1360605 · DOI
- Simonson, 2007, CYLD: a DUB with many talents, Dev. Cell, 13, 601, 10.1016/j.devcel.2007.10.009 · DOI
- Solan, 2002, RelB cellular regulation and transcriptional activity are regulated by p100, J. Biol. Chem., 277, 1405, 10.1074/jbc.M109619200 · DOI
- Solt, 2007, Interleukin-1-induced NF-kappaB activation is NEMO-dependent but does not require IKKbeta, J. Biol. Chem., 282, 8724, 10.1074/jbc.M609613200 · DOI
- Sun, 2004, The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes, Mol. Cell, 14, 289, 10.1016/S1097-2765(04)00236-9 · DOI
- Suyang, 1996, Role of unphosphorylated, newly synthesized I kappa B beta in persistent activation of NF-kappa B, Mol. Cell. Biol., 16, 5444, 10.1128/MCB.16.10.5444 · DOI
- Takaesu, 2003, TAK1 is critical for IkappaB kinase-mediated activation of the NF-kappaB pathway, J. Mol. Biol., 326, 105, 10.1016/S0022-2836(02)01404-3 · DOI
- Tang, 2003, Roles for homotypic interactions and transautophosphorylation in IkappaB kinase (IKKbeta) activation, J. Biol. Chem., 278, 38566, 10.1074/jbc.M304374200 · DOI
- Tegethoff, 2003, Tetrameric oligomerization of IkappaB kinase gamma (IKKgamma) is obligatory for IKK complex activity and NF-kappaB activation, Mol. Cell. Biol., 23, 2029, 10.1128/MCB.23.6.2029-2041.2003 · DOI
- Tergaonkar, 2005, Distinct roles of IkappaB proteins in regulating constitutive NF-kappaB activity, Nat. Cell Biol., 7, 921, 10.1038/ncb1296 · DOI
- Thompson, 1995, I kappa B-beta regulates the persistent response in a biphasic activation of NF-kappa B, Cell, 80, 573, 10.1016/0092-8674(95)90511-1 · DOI
- Ting, 1996, RIP mediates tumor necrosis factor receptor 1 activation of NF-kappaB but not Fas/APO-1-initiated apoptosis, EMBO J., 15, 6189, 10.1002/j.1460-2075.1996.tb01007.x · DOI · Paper page
- Vermeulen, 2003, Transcriptional activation of the NF-kappaB p65 subunit by mitogen- and stress-activated protein kinase-1 (MSK1), EMBO J., 22, 1313, 10.1093/emboj/cdg139 · DOI
- Vince, 2007, IAP antagonists target cIAP1 to induce TNFalpha-dependent apoptosis, Cell, 131, 682, 10.1016/j.cell.2007.10.037 · DOI
- Vivarelli, 2004, RIP links TLR4 to Akt and is essential for cell survival in response to LPS stimulation, J. Exp. Med., 200, 399, 10.1084/jem.20040446 · DOI
- Wan, 2006, The kinase TAK1 integrates antigen and cytokine receptor signaling for T cell development, survival and function, Nat. Immunol., 7, 851, 10.1038/ni1355 · DOI
- Wan, 2007, Ribosomal protein S3: a KH domain subunit in NF-kappaB complexes that mediates selective gene regulation, Cell, 131, 927, 10.1016/j.cell.2007.10.009 · DOI
- Wang, 2000, Tumor necrosis factor alpha-induced phosphorylation of RelA/p65 on Ser529 is controlled by casein kinase II, J. Biol. Chem., 275, 32592, 10.1074/jbc.M001358200 · DOI
- Westerheide, 2001, The putative oncoprotein Bcl-3 induces cyclin D1 to stimulate G(1) transition, Mol. Cell. Biol., 21, 8428, 10.1128/MCB.21.24.8428-8436.2001 · DOI
- Windheim, 2008, IL-1 induces the Lys63-linked polyubiquitination of IRAK1 to facilitate NEMO binding and the activation of IKK, Mol. Cell. Biol., 10.1128/MCB.02380-06 · DOI
- Woronicz, 1997, IkappaB kinase-beta: NF-kappaB activation and complex formation with IkappaB kinase-alpha and NIK, Science, 278, 866, 10.1126/science.278.5339.866 · DOI
- Wu, 2003, Differential phosphorylation of the signal-responsive domain of I kappa B alpha and I kappa B beta by I kappa B kinases, J. Biol. Chem., 278, 31980, 10.1074/jbc.M304278200 · DOI
- Wu, 2006, Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-kappaB activation, Nat. Cell Biol., 8, 398, 10.1038/ncb1384 · DOI
- Xiao, 2004, Induction of p100 processing by NF-kappaB-inducing kinase involves docking IkappaB kinase alpha (IKKalpha) to p100 and IKKalpha-mediated phosphorylation, J. Biol. Chem., 279, 30099, 10.1074/jbc.M401428200 · DOI
- Xiao, 2001, NF-kappaB-inducing kinase regulates the processing of NF-kappaB2 p100, Mol. Cell, 7, 401, 10.1016/S1097-2765(01)00187-3 · DOI
- Yamamoto, 2004, Regulation of Toll/IL-1-receptor-mediated gene expression by the inducible nuclear protein IkappaBzeta, Nature, 430, 218, 10.1038/nature02738 · DOI · Paper page
- Yamamoto, 2006, Key function for the Ubc13 E2 ubiquitin-conjugating enzyme in immune receptor signaling, Nat. Immunol., 7, 962, 10.1038/ni1367 · DOI
- Yamamoto, 2006, Cutting edge: Pivotal function of Ubc13 in thymocyte TCR signaling, J. Immunol., 177, 7520, 10.4049/jimmunol.177.11.7520 · DOI
- Yamamoto, 2003, Histone H3 phosphorylation by IKK-alpha is critical for cytokine-induced gene expression, Nature, 423, 655, 10.1038/nature01576 · DOI
- Yamaoka, 1998, Complementation cloning of NEMO, a component of the IkappaB kinase complex essential for NF-kappaB activation, Cell, 93, 1231, 10.1016/S0092-8674(00)81466-X · DOI
- Yang, 2007, NOD2 pathway activation by MDP or mycobacterium tuberculosis infection involves the stable polyubiquitination of Rip2, J. Biol. Chem., 282, 36223, 10.1074/jbc.M703079200 · DOI
- Yeh, 1997, Early lethality, functional NF-kappaB activation, and increased sensitivity to TNF-induced cell death in TRAF2-deficient mice, Immunity, 7, 715, 10.1016/S1074-7613(00)80391-X · DOI
- Zandi, 1997, The IkappaB kinase complex (IKK) contains two kinase subunits, IKKalpha and IKKbeta, necessary for IkappaB phosphorylation and NF-kappaB activation, Cell, 91, 243, 10.1016/S0092-8674(00)80406-7 · DOI
- Zandi, 1998, Direct phosphorylation of IkappaB by IKKalpha and IKKbeta: discrimination between free and NF-kappaB-bound substrate, Science, 281, 1360, 10.1126/science.281.5381.1360 · DOI
- Zhang, 2000, Recruitment of the IKK signalosome to the p55 TNF receptor: RIP and A20 bind to NEMO (IKKgamma) upon receptor stimulation, Immunity, 12, 301, 10.1016/S1074-7613(00)80183-1 · DOI
- Zhong, 1998, Phosphorylation of NF-kappa B p65 by PKA stimulates transcriptional activity by promoting a novel bivalent interaction with the coactivator CBP/p300, Mol. Cell, 1, 661, 10.1016/S1097-2765(00)80066-0 · DOI · Paper page
- Zhou, 2004, Bcl10 activates the NF-kappaB pathway through ubiquitination of NEMO, Nature, 427, 167, 10.1038/nature02273 · DOI
Cited by
NF-κB signaling in inflammation
Liu, T., Zhang, L., Joo, D., & Sun, S.-C. (2017) · Signal Transduction and Targeted Therapy · doi:10.1038/sigtrans.2017.23 · Cited by 8,791
Crosstalk of reactive oxygen species and NF-κB signaling
Morgan, M. J., & Liu, Z.-G. (2011) · Cell Research · doi:10.1038/cr.2010.178 · Cited by 3,505
NF-κB, Inflammation, and Metabolic Disease
Baker, R. G., Hayden, M. S., & Ghosh, S. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2010.12.008 · Cited by 1,952
Self-citationNF-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
Self-citationHypothalamic IKKβ/NF-κB and ER Stress Link Overnutrition to Energy Imbalance and Obesity
Zhang, X., Zhang, G., Zhang, H., Karin, M., Bai, H., & Cai, D. (2008) · Cell · doi:10.1016/j.cell.2008.07.043 · Cited by 1,350
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
Transcription Factors in Long-Term Memory and Synaptic Plasticity
Alberini, C. M. (2009) · Physiological Reviews · doi:10.1152/physrev.00017.2008 · Cited by 991
A Large Fraction of Extragenic RNA Pol II Transcription Sites Overlap Enhancers
De Santa, F., Barozzi, I., Mietton, F., Ghisletti, S., Polletti, S., Tusi, B. K., Muller, H., Ragoussis, J., Wei, C.-L., & Natoli, G. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000384 · Cited by 934
The Sterile Inflammatory Response
Rock, K. L., Latz, E., Ontiveros, F., & Kono, H. (2010) · Annual Review of Immunology · doi:10.1146/annurev-immunol-030409-101311 · Cited by 865
Signaling pathways in cancer-associated fibroblasts and targeted therapy for cancer
Wu, F., Yang, J., Liu, J., Wang, Y., Mu, J., Zeng, Q., Deng, S., & Zhou, H. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00641-0 · Cited by 773
Denison, M. S., Soshilov, A. A., He, G., DeGroot, D. E., & Zhao, B. (2011) · Toxicological Sciences · doi:10.1093/toxsci/kfr218 · Cited by 748
SHARPIN forms a linear ubiquitin ligase complex regulating NF-κB activity and apoptosis
Ikeda, F., Deribe, Y. L., Skånland, S. S., Stieglitz, B., Grabbe, C., Franz-Wachtel, M., van Wijk, S. J. L., Goswami, P., Nagy, V., Terzic, J., et al. (2011) · Nature · doi:10.1038/nature09814 · Cited by 745
Regulation of hypoxia-inducible factor-1α by NF-κB
van Uden, P., Kenneth, N. S., & Rocha, S. (2008) · Biochemical Journal · doi:10.1042/bj20080476 · Cited by 729
Ghisletti, S., Barozzi, I., Mietton, F., Polletti, S., De Santa, F., Venturini, E., Gregory, L., Lonie, L., Chew, A., Wei, C.-L., et al. (2010) · Immunity · doi:10.1016/j.immuni.2010.02.008 · Cited by 666
Microglia Induce Motor Neuron Death via the Classical NF-κB Pathway in Amyotrophic Lateral Sclerosis
Frakes, A. E., Ferraiuolo, L., Haidet-Phillips, A. M., Schmelzer, L., Braun, L., Miranda, C. J., Ladner, K. J., Bevan, A. K., Foust, K. D., Godbout, J. P., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.01.013 · Cited by 638
A Molecular Web: Endoplasmic Reticulum Stress, Inflammation, and Oxidative Stress
Chaudhari, N., Talwar, P., Parimisetty, A., Lefebvre d’Hellencourt, C., & Ravanan, P. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00213 · Cited by 600
SHARPIN is a component of the NF-κB-activating linear ubiquitin chain assembly complex
Tokunaga, F., Nakagawa, T., Nakahara, M., Saeki, Y., Taniguchi, M., Sakata, S.-I., Tanaka, K., Nakano, H., & Iwai, K. (2011) · Nature · doi:10.1038/nature09815 · Cited by 609
Pulsatile Stimulation Determines Timing and Specificity of NF-κB-Dependent Transcription
Ashall, L., Horton, C. A., Nelson, D. E., Paszek, P., Harper, C. V., Sillitoe, K., Ryan, S., Spiller, D. G., Unitt, J. F., Broomhead, D. S., et al. (2009) · Science · doi:10.1126/science.1164860 · Cited by 543
NF-κB inhibition delays DNA damage–induced senescence and aging in mice
Tilstra, J. S., Robinson, A. R., Wang, J., Gregg, S. Q., Clauson, C. L., Reay, D. P., Nasto, L. A., St Croix, C. M., Usas, A., Vo, N., et al. (2012) · Journal of Clinical Investigation · doi:10.1172/jci45785 · Cited by 462
RANK/RANKL: Regulators of Immune Responses and Bone Physiology
Leibbrandt, A., & Penninger, J. M. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1443.016 · Cited by 420
Zhou, F., Mei, J., Han, X., Li, H., Yang, S., Wang, M., Chu, L., Qiao, H., & Tang, T. (2019) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2019.01.015 · Cited by 400
Telomerase directly regulates NF-κB-dependent transcription
Ghosh, A., Saginc, G., Leow, S. C., Khattar, E., Shin, E. M., Yan, T. D., Wong, M., Zhang, Z., Li, G., Sung, W.-K., et al. (2012) · Nature Cell Biology · doi:10.1038/ncb2621 · Cited by 378
Responsive Exosome Nano-bioconjugates for Synergistic Cancer Therapy
Nie, W., Wu, G., Zhang, J., Huang, L., Ding, J., Jiang, A., Zhang, Y., Liu, Y., Li, J., Pu, K., et al. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.201912524 · Cited by 376
ZIP8 Regulates Host Defense through Zinc-Mediated Inhibition of NF-κB
Liu, M.-J., Bao, S., Gálvez-Peralta, M., Pyle, C. J., Rudawsky, A. C., Pavlovicz, R. E., Killilea, D. W., Li, C., Nebert, D. W., Wewers, M. D., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.01.009 · Cited by 367
Li, Y., Reddy, M. A., Miao, F., Shanmugam, N., Yee, J.-K., Hawkins, D., Ren, B., & Natarajan, R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802800200 · Cited by 353
Cellular Specificity of NF-κB Function in the Nervous System
Dresselhaus, E. C., & Meffert, M. K. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01043 · Cited by 345
Regulation of RIPK1 activation by TAK1-mediated phosphorylation dictates apoptosis and necroptosis
Geng, J., Ito, Y., Shi, L., Amin, P., Chu, J., Ouchida, A. T., Mookhtiar, A. K., Zhao, H., Xu, D., Shan, B., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00406-w · Cited by 325
Ben Haim, L., Ceyzériat, K., Carrillo-de Sauvage, M. A., Aubry, F., Auregan, G., Guillermier, M., Ruiz, M., Petit, F., Houitte, D., Faivre, E., et al. (2015) · The Journal of Neuroscience · doi:10.1523/jneurosci.3516-14.2015 · Cited by 335
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
Hinz, M., Stilmann, M., Arslan, S. Ç., Khanna, K. K., Dittmar, G., & Scheidereit, C. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.008 · Cited by 280
Regulation of TNF-Induced Osteoclast Differentiation
Yao, Z., Getting, S. J., & Locke, I. C. (2021) · Cells · doi:10.3390/cells11010132 · Cited by 280
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
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
NEMO and RIP1 Control Cell Fate in Response to Extensive DNA Damage via TNF-α Feedforward Signaling
Biton, S., & Ashkenazi, A. (2011) · Cell · doi:10.1016/j.cell.2011.02.023 · Cited by 262
Regulation of NF-κB by ubiquitination
Chen, J., & Chen, Z. J. (2013) · Current Opinion in Immunology · doi:10.1016/j.coi.2012.12.005 · Cited by 258
Nuclear initiated NF-κB signaling: nemo and ATM take center stage
Miyamoto, S. (2011) · Cell Research · doi:10.1038/cr.2010.179 · Cited by 253
Neuroinflammation and neurodegeneration in overnutrition-induced diseases
Cai, D. (2013) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2012.11.003 · Cited by 256
A20 Negatively Regulates T Cell Receptor Signaling to NF-κB by Cleaving Malt1 Ubiquitin Chains
Düwel, M., Welteke, V., Oeckinghaus, A., Baens, M., Kloo, B., Ferch, U., Darnay, B. G., Ruland, J., Marynen, P., & Krappmann, D. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0803313 · Cited by 233
Pamukcu, B., Lip, G. Y. H., & Shantsila, E. (2011) · Thrombosis Research · doi:10.1016/j.thromres.2011.03.025 · Cited by 218
Uncoupling the mechanisms of obesity and hypertension by targeting hypothalamic IKK-β and NF-κB
Purkayastha, S., Zhang, G., & Cai, D. (2011) · Nature Medicine · doi:10.1038/nm.2372 · Cited by 220
Blakely, C. M., Pazarentzos, E., Olivas, V., Asthana, S., Yan, J. J., Tan, I., Hrustanovic, G., Chan, E., Lin, L., Neel, D. S., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.03.012 · Cited by 204
Vinciguerra, M., Sgroi, A., Veyrat-Durebex, C., Rubbia-Brandt, L., Buhler, L. H., & Foti, M. (2009) · Hepatology · doi:10.1002/hep.22737 · Cited by 198
IAPs limit activation of RIP kinases by TNF receptor 1 during development
Moulin, M., Anderton, H., Voss, A. K., Thomas, T., Wong, W. W., Bankovacki, A., Feltham, R., Chau, D., Cook, W. D., Silke, J., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.18 · Cited by 193
Therapeutic Modulation of the Immune Response in Arrhythmogenic Cardiomyopathy
Chelko, S. P., Asimaki, A., Lowenthal, J., Bueno-Beti, C., Bedja, D., Scalco, A., Amat-Alarcon, N., Andersen, P., Judge, D. P., Tung, L., et al. (2019) · Circulation · doi:10.1161/circulationaha.119.040676 · Cited by 192
Inhibiting microglia expansion prevents diet-induced hypothalamic and peripheral inflammation
André, C., Guzman-Quevedo, O., Rey, C., Rémus-Borel, J., Clark, S., Castellanos-Jankiewicz, A., Ladeveze, E., Leste-Lasserre, T., Nadjar, A., Abrous, D. N., et al. (2017) · Diabetes · doi:10.2337/db16-0586 · Cited by 182
The Role of NF‐κB in Hypoxia‐Induced Gene Expression
Taylor, C. T., & Cummins, E. P. (2009) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2009.05024.x · Cited by 175
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
Kandhaya-Pillai, R., Miro-Mur, F., Alijotas-Reig, J., Tchkonia, T., Kirkland, J. L., & Schwartz, S. (2017) · Aging · doi:10.18632/aging.101328 · Cited by 165
Evolutionary Conserved Regulation of HIF-1β by NF-κB
van Uden, P., Kenneth, N. S., Webster, R., Müller, H. A., Mudie, S., & Rocha, S. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1001285 · Cited by 163
Cell Senescence, DNA Damage, and Metabolism
Shmulevich, R., & Krizhanovsky, V. (2021) · Antioxidants & Redox Signaling · doi:10.1089/ars.2020.8043 · Cited by 157
Phycocyanin: Anti-inflammatory effect and mechanism
Liu, R., Qin, S., & Li, W. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113362 · Cited by 157
Tanaka, M., Kishimoto, Y., Sasaki, M., Sato, A., Kamiya, T., Kondo, K., & Iida, K. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/9364364 · Cited by 154
Deubiquitination of NF-κB by Ubiquitin-Specific Protease-7 promotes transcription
Colleran, A., Collins, P. E., O’Carroll, C., Ahmed, A., Mao, X., McManus, B., Kiely, P. A., Burstein, E., & Carmody, R. J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1208446110 · Cited by 150
A Review on Fucoidan Structure, Extraction Techniques, and Its Role as an Immunomodulatory Agent
Jayawardena, T. U., Nagahawatta, D. P., Fernando, I. P. S., Kim, Y.-T., Kim, J.-S., Kim, W.-S., Lee, J. S., & Jeon, Y.-J. (2022) · Marine Drugs · doi:10.3390/md20120755 · Cited by 149
Crockett, J. C., Mellis, D. J., Scott, D. I., & Helfrich, M. H. (2011) · Osteoporosis International · doi:10.1007/s00198-010-1272-8 · Cited by 143
The kinase TBK1 controls IgA class switching by negatively regulating noncanonical NF-κB signaling
Jin, J., Xiao, Y., Chang, J.-H., Yu, J., Hu, H., Starr, R., Brittain, G. C., Chang, M., Cheng, X., & Sun, S.-C. (2012) · Nature Immunology · doi:10.1038/ni.2423 · Cited by 136
Janjetovic, Z., Zmijewski, M. A., Tuckey, R. C., DeLeon, D. A., Nguyen, M. N., Pfeffer, L. M., & Slominski, A. T. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005988 · Cited by 130
Jefsen, O. H., Elfving, B., Wegener, G., & Müller, H. K. (2021) · Journal of Psychopharmacology · doi:10.1177/0269881120959614 · Cited by 127
p53 regulates Toll-like receptor 3 expression and function in human epithelial cell lines
Taura, M., Eguma, A., Suico, M. A., Shuto, T., Koga, T., Komatsu, K., Komune, T., Sato, T., Saya, H., Li, J.-D., et al. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01202-08 · Cited by 129
Bi, L., Gojestani, S., Wu, W., Hsu, Y.-M. S., Zhu, J., Ariizumi, K., & Lin, X. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.131300 · Cited by 126
Rodríguez-Calvo, R., Tajes, M., & Vázquez-Carrera, M. (2017) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2017.1279146 · Cited by 117
Genome-wide siRNA screen for mediators of NF-κB activation
Gewurz, B. E., Towfic, F., Mar, J. C., Shinners, N. P., Takasaki, K., Zhao, B., Cahir-McFarland, E. D., Quackenbush, J., Xavier, R. J., & Kieff, E. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1120542109 · Cited by 108
Kumar, M., Allison, D. F., Baranova, N. N., Wamsley, J. J., Katz, A. J., Bekiranov, S., Jones, D. R., & Mayo, M. W. (2013) · PLoS ONE · doi:10.1371/journal.pone.0068597 · Cited by 107
Raasch, J., Zeller, N., van Loo, G., Merkler, D., Mildner, A., Erny, D., Knobeloch, K.-P., Bethea, J. R., Waisman, A., Knust, M., et al. (2011) · Brain · doi:10.1093/brain/awq359 · Cited by 106
S-nitrosylation in the regulation of gene transcription
Sha, Y., & Marshall, H. E. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.05.008 · Cited by 101
McClatchy, J., Strogantsev, R., Wolfe, E., Lin, H. Y., Mohammadhosseini, M., Davis, B. A., Eden, C., Goldman, D., Fleming, W. H., Conley, P., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-43697-y · Cited by 95
Luo, Q., Yan, X., Bobrovskaya, L., Ji, M., Yuan, H., Lou, H., & Fan, P. (2017) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-016-2923-7 · Cited by 90
Reduced mitochondrial calcium uptake in macrophages is a major driver of inflammaging
Seegren, P. V., Harper, L. R., Downs, T. K., Zhao, X.-Y., Viswanathan, S. B., Stremska, M. E., Olson, R. J., Kennedy, J., Ewald, S. E., Kumar, P., et al. (2023) · Nature Aging · doi:10.1038/s43587-023-00436-8 · Cited by 88
NFκB/p53 crosstalk—a promising new therapeutic target
Schneider, G., & Krämer, O. H. (2011) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2010.10.003 · Cited by 87
Ge, X., Huang, S., Gao, H., Han, Z., Chen, F., Zhang, S., Wang, Z., Kang, C., Jiang, R., Yue, S., et al. (2016) · Brain Research · doi:10.1016/j.brainres.2016.07.015 · Cited by 86
Current Understanding of Human Enterovirus D68
Sun, J., Hu, X.-Y., & Yu, X.-F. (2019) · Viruses · doi:10.3390/v11060490 · Cited by 81
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
Federman, N., de la Fuente, V., Zalcman, G., Corbi, N., Onori, A., Passananti, C., & Romano, A. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.4181-12.2013 · Cited by 73
Kumar, G. R., Shum, L., & Glaunsinger, B. A. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05402-11 · Cited by 71
Gold nanoparticles reduce inflammation in cerebral microvessels of mice with sepsis
Di Bella, D., Ferreira, J. P. S., Silva, R. D. N. O., Echem, C., Milan, A., Akamine, E. H., Carvalho, M. H., & Rodrigues, S. F. (2021) · Journal of Nanobiotechnology · doi:10.1186/s12951-021-00796-6 · Cited by 69
Mitochondria-Derived Peptide MOTS-c: Effects and Mechanisms Related to Stress, Metabolism and Aging
Wan, W., Zhang, L., Lin, Y., Rao, X., Wang, X., Hua, F., & Ying, J. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-03885-2 · Cited by 70
Controlling the Fate of NIK: A Central Stage in Noncanonical NF-κB Signaling
Sun, S.-C. (2010) · Science Signaling · doi:10.1126/scisignal.3123pe18 · Cited by 61
The Activation of IL-1-Induced Enhancers Depends on TAK1 Kinase Activity and NF-κB p65
Jurida, L., Soelch, J., Bartkuhn, M., Handschick, K., Müller, H., Newel, D., Weber, A., Dittrich-Breiholz, O., Schneider, H., Bhuju, S., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.01.001 · Cited by 51
NFκB signaling in T cell memory
Daniels, M. A., Luera, D., & Teixeiro, E. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1129191 · Cited by 47
Altered DNA base excision repair profile in brain tissue and blood in Alzheimer’s disease
Lillenes, M. S., Rabano, A., Støen, M., Riaz, T., Misaghian, D., Møllersen, L., Esbensen, Y., Günther, C.-C., Selnes, P., Stenset, V. T. V., et al. (2016) · Molecular Brain · doi:10.1186/s13041-016-0237-z · Cited by 46
Martincuks, A., Andryka, K., Küster, A., Schmitz-Van de Leur, H., Komorowski, M., & Müller-Newen, G. (2017) · Cellular Signalling · doi:10.1016/j.cellsig.2017.01.006 · Cited by 45
Diverse functions within the IAP family
Rumble, J. M., & Duckett, C. S. (2008) · Journal of Cell Science · doi:10.1242/jcs.040303 · Cited by 40
BET bromodomain proteins regulate transcriptional reprogramming in genetic dilated cardiomyopathy
Antolic, A., Wakimoto, H., Jiao, Z., Gorham, J. M., DePalma, S. R., Lemieux, M. E., Conner, D. A., Lee, D. Y., Qi, J., Seidman, J. G., et al. (2020) · JCI Insight · doi:10.1172/jci.insight.138687 · Cited by 41
Wang, H., Wang, H., Song, Y., Liu, C., Qian, X., Zhang, D., Jiang, X., & Zhang, S. (2022) · Molecular Medicine Reports · doi:10.3892/mmr.2022.12623 · Cited by 36
Lambert, W. S., Carlson, B. J., Formichella, C. R., Sappington, R. M., Ahlem, C., & Calkins, D. J. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00045 · Cited by 31
Ling, J., Chan, C.-L., Ho, C.-Y., Gao, X., Tsang, S.-M., Leung, P.-C., Hu, J.-M., & Wong, C.-K. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911195 · Cited by 31
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
Cho, Y.-C., Vuong, H. L., Ha, J., Lee, S., Park, J., Wibow, A. E., & Cho, S. (2020) · The American Journal of Chinese Medicine · doi:10.1142/s0192415x20500548 · Cited by 15
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
Metadata
- Authors
- Hayden, M. S., & Ghosh, S.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2008-02
- Volume
- 132
- Issue
- 3
- Pages
- 344-362
- ISSN
- 0092-8674
- Cited by
- 4,494
- References
- 11
- Language
- en
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 2024 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review