Beyond IκBs: alternative regulation of NF‐KB activity

Phosphorylation meets ubiquitination: the control of NF-κB activity

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NF-κB-dependent induction of microRNA miR-146, an inhibitor targeted to signaling proteins of innate immune responses

Taganov, K. D., Boldin, M. P., Chang, K.-J., & Baltimore, D. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605298103 · Cited by 4,317 · see citing works

Signaling to NF-κB

Hayden, M. S., & Ghosh, S. (2004) · Genes & Development · doi:10.1101/gad.1228704 · Cited by 3,842 · see citing works

Van Damme A.

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Modulation of NF‐κB‐dependent transcription and cell survival by the SIRT1 deacetylase

Yeung, F., Hoberg, J. E., Ramsey, C. S., Keller, M. D., Jones, D. R., Frye, R. A., & Mayo, M. W. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600244 · Cited by 2,750 · see citing works

Introduction to NF-κB: players, pathways, perspectives

Gilmore, T. D. (2006) · Oncogene · doi:10.1038/sj.onc.1209954 · Cited by 2,227 · see citing works

De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-κB signalling

Wertz, I. E., O’Rourke, K. M., Zhou, H., Eby, M. T., Aravind, L., Seshagiri, S., Wu, P., Wiesmann, C., Baker, R. T., Boone, D. L., et al. (2004) · Nature · doi:10.1038/nature02794 · Cited by 1,852 · see citing works

Phosphorylation of NF-κB and IκB proteins: implications in cancer and inflammation

Viatour, P., Merville, M., Bours, V., & Chariot, A. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2004.11.009 · Cited by 1,497 · 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

Oscillations in NF-κB Signaling Control the Dynamics of Gene Expression

Nelson, D. E., Ihekwaba, A. E. C., Elliott, M., Johnson, J. R., Gibney, C. A., Foreman, B. E., Nelson, G., See, V., Horton, C. A., Spiller, D. G., et al. (2004) · Science · doi:10.1126/science.1099962 · Cited by 1,186 · see citing works

Activation of IKK by TNFα Requires Site-Specific Ubiquitination of RIP1 and Polyubiquitin Binding by NEMO

Ea, C.-K., Deng, L., Xia, Z.-P., Pineda, G., & Chen, Z. J. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.03.026 · Cited by 998 · see citing works

The Phosphorylation Status of Nuclear NF-ΚB Determines Its Association with CBP/p300 or HDAC-1

Zhong, H., May, M. J., Jimi, E., & Ghosh, S. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00477-x · Cited by 930 · see citing works

The Interplay between the Glucocorticoid Receptor and Nuclear Factor-κB or Activator Protein-1: Molecular Mechanisms for Gene Repression

De Bosscher, K., Vanden Berghe, W., & Haegeman, G. (2003) · Endocrine Reviews · doi:10.1210/er.2002-0006 · Cited by 898 · see citing works

Signalling pathways and molecular interactions of NOD1 and NOD2

Strober, W., Murray, P. J., Kitani, A., & Watanabe, T. (2005) · Nature reviews. Immunology · doi:10.1038/nri1747 · Cited by 856 · see citing works

The Transcriptional Activity of NF-κB Is Regulated by the IκB-Associated PKAc Subunit through a Cyclic AMP–Independent Mechanism

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

Acetylation 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

IκB Kinases Phosphorylate NF-κB p65 Subunit on Serine 536 in the Transactivation Domain

Sakurai, H., Chiba, H., Miyoshi, H., Sugita, T., & Toriumi, W. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.43.30353 · Cited by 827 · see citing works

Transcriptional activation of the NF‐κB p65 subunit by mitogen‐ and stress‐activated protein kinase‐1 (MSK1)

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

Glucocorticoid Receptor Recruitment of Histone Deacetylase 2 Inhibits Interleukin-1β-Induced Histone H4 Acetylation on Lysines 8 and 12

Ito, K., Barnes, P. J., & Adcock, I. M. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.18.6891-6903.2000 · Cited by 723 · see citing works

Post-translational modifications regulating the activity and function of the nuclear factor kappa B pathway

Perkins, N. D. (2006) · Oncogene · doi:10.1038/sj.onc.1209937 · Cited by 674 · see citing works

Regulation of NF-κB Signaling by Pin1-Dependent Prolyl Isomerization and Ubiquitin-Mediated Proteolysis of p65/RelA

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

IKKα limits macrophage NF-κB activation and contributes to the resolution of inflammation

Lawrence, T., Bébien, M., Liu, G. Y., Nizet, V., & Karin, M. (2005) · Nature · doi:10.1038/nature03491 · Cited by 625 · see citing works

Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-κB activation

Wu, C.-J., Conze, D. B., Li, T., Srinivasula, S. M., & Ashwell, J. D. (2006) · Nature Cell Biology · doi:10.1038/ncb1384 · Cited by 607 · see citing works

Sequential Modification of NEMO/IKKγ by SUMO-1 and Ubiquitin Mediates NF-κB Activation by Genotoxic Stress

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

The glucocorticoid receptor inhibits NFκB by interfering with serine-2 phosphorylation of the RNA polymerase II carboxy-terminal domain

Nissen, R. M., & Yamamoto, K. R. (2000) · Genes & Development · doi:10.1101/gad.827900 · Cited by 559 · 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

Molecular Linkage Between the Kinase ATM and NF-κB Signaling in Response to Genotoxic Stimuli

Wu, Z., Shi, Y., Tibbetts, R. S., & Miyamoto, S. (2006) · Science · doi:10.1126/science.1121513 · Cited by 515 · see citing works

Tumor Necrosis Factor α-induced Phosphorylation of RelA/p65 on Ser529 Is Controlled by Casein Kinase II

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

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 · see citing works

Constitutive and Interleukin-1-inducible Phosphorylation of p65 NF-κB at Serine 536 Is Mediated by Multiple Protein Kinases Including IκB Kinase (IKK)-α, IKKβ, IKKϵ, TRAF Family Member-associated (TANK)-binding Kinase 1 (TBK1), and an Unknown Kinase and Couples p65 to TATA-binding Protein-associated Factor II31-mediated Interleukin-8 Transcription

Buss, H., Dörrie, A., Schmitz, M. L., Hoffmann, E., Resch, K., & Kracht, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409825200 · Cited by 362 · 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

Phosphorylation of RelA/p65 on Serine 536 Defines an IκBα-independent NF-κB Pathway

Sasaki, C. Y., Barberi, T. J., Ghosh, P., & Longo, D. L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504943200 · Cited by 330 · see citing works

Signals from within: the DNA-damage-induced NF-κB response

Janssens, S., & Tschopp, J. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401843 · Cited by 321 · see citing works

PIDD Mediates NF-κB Activation in Response to DNA Damage

Janssens, S., Tinel, A., Lippens, S., & Tschopp, J. (2005) · Cell · doi:10.1016/j.cell.2005.09.036 · Cited by 319 · 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

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

Modulation of NF-κB Activity by Exchange of Dimers

Saccani, S., Pantano, S., & Natoli, G. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00227-2 · Cited by 301 · see citing works

COMMD1 promotes the ubiquitination of NF‐κB subunits through a cullin‐containing ubiquitin ligase

Maine, G. N., Mao, X., Komarck, C. M., & Burstein, E. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601489 · Cited by 278 · see citing works

Cooperative Signals Governing ARF-Mdm2 Interaction and Nucleolar Localization of the Complex

Weber, J. D., Kuo, M.-L., Bothner, B. B., DiGiammarino, E. L., Kriwacki, R. W., Roussel, M. F., & Sherr, C. J. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.7.2517-2528.2000 · Cited by 273 · see citing works

p53 Induces NF-κB Activation by an IκB Kinase-independent Mechanism Involving Phosphorylation of p65 by Ribosomal S6 Kinase 1

Bohuslav, J., Chen, L., Kwon, H., Mu, Y., & Greene, W. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313509200 · Cited by 256 · see citing works

Phosphorylation of Serine 468 by GSK-3β Negatively Regulates Basal p65 NF-κB Activity

Buss, H., Dörrie, A., Schmitz, M. L., Frank, R., Livingstone, M., Resch, K., & Kracht, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c400442200 · Cited by 253 · see citing works

Degradation of Promoter-bound p65/RelA Is Essential for the Prompt Termination of the Nuclear Factor κB Response

Saccani, S., Marazzi, I., Beg, A. A., & Natoli, G. (2004) · The Journal of Experimental Medicine · doi:10.1084/jem.20040196 · Cited by 253 · see citing works

A20 inhibits NF-κB activation by dual ubiquitin-editing functions

Heyninck, K., & Beyaert, R. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2004.11.001 · Cited by 252 · see citing works

ABIN-1 Binds to NEMO/IKKγ and Co-operates with A20 in Inhibiting NF-κB

Mauro, C., Pacifico, F., Lavorgna, A., Mellone, S., Iannetti, A., Acquaviva, R., Formisano, S., Vito, P., & Leonardi, A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601502200 · Cited by 250 · see citing works

Cross-talk between nuclear receptors and nuclear factor κB

Bosscher, K. D., Berghe, W. V., & Haegeman, G. (2006) · Oncogene · doi:10.1038/sj.onc.1209935 · Cited by 247 · see citing works

PIASy mediates NEMO sumoylation and NF-κB activation in response to genotoxic stress

Mabb, A. M., Wuerzberger‐Davis, S. M., & Miyamoto, S. (2006) · Nature Cell Biology · doi:10.1038/ncb1458 · Cited by 226 · see citing works

The glucocorticoid receptor blocks P-TEFb recruitment by NFκB to effect promoter-specific transcriptional repressionPreprint

Luecke, H. F., & Yamamoto, K. R. (2005) · Genes & Development · doi:10.1101/gad.1297105 · Cited by 217 · see citing works

Activation of Nuclear Transcription Factor NF-κB by Interleukin-1 Is Accompanied by Casein Kinase II-mediated Phosphorylation of the p65 Subunit

Bird, T. A., Schooley, K., Dower, S., Hagen, H., & Virca, G. D. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.51.32606 · Cited by 208 · see citing works

Formation of an IKKα-Dependent Transcription Complex Is Required for Estrogen Receptor-Mediated Gene Activation

Park, K.-J., Krishnan, V., O’Malley, B. W., Yamamoto, Y., & Gaynor, R. B. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.03.006 · Cited by 193 · see citing works

Proteolytic degradation of MAD3 (IϰBα) and enhanced processing of the NF-ϰB precursor p105 are obligatory steps in the activation of NF-ϰB

Mellits, K. H., Hay, R. T., & Goodbourn, S. (1993) · Nucleic Acids Research · doi:10.1093/nar/21.22.5059 · Cited by 182 · see citing works

IκB Kinase α-Mediated Derepression of SMRT Potentiates Acetylation of RelA/p65 by p300

Hoberg, J. E., Popko, A. E., Ramsey, C. S., & Mayo, M. W. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.26.2.457-471.2006 · Cited by 181 · see citing works

The NF-κB Activation in Lymphotoxin β Receptor Signaling Depends on the Phosphorylation of p65 at Serine 536

Jiang, X., Takahashi, N., Matsui, N., Tetsuka, T., & Okamoto, T. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m208696200 · Cited by 171 · see citing works

Identification of NAP1, a Regulatory Subunit of IκB Kinase-Related Kinases That Potentiates NF-κB Signaling

Fujita, F., Taniguchi, Y., Kato, T., Narita, Y., Furuya, A., Ogawa, T., Sakurai, H., Joh, T., Itoh, M., Delhase, M., et al. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.21.7780-7793.2003 · Cited by 164 · see citing works

Regulation of NF‐κB and p53 through activation of ATR and Chk1 by the ARF tumour suppressor

Rocha, S., Garrett, M. D., Campbell, K. J., Schumm, K., & Perkins, N. D. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600608 · Cited by 161 · see citing works

Glucocorticoids: Effects on Gene Transcription

Adcock, I. M., Ito, K., & Barnes, P. J. (2004) · Proceedings of the American Thoracic Society · doi:10.1513/pats.200402-001ms · Cited by 160 · see citing works

Regulating the Regulators: Control of Protein Ubiquitination and Ubiquitin-like Modifications by Extracellular Stimuli

Gao, M., & Karin, M. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.08.017 · Cited by 159 · see citing works

IKK-i/IKKϵ Controls Constitutive, Cancer Cell-associated NF-κB Activity via Regulation of Ser-536 p65/RelA Phosphorylation

Adli, M., & Baldwin, A. S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603133200 · Cited by 150 · see citing works

Neddylation of a breast cancer-associated protein recruits a class III histone deacetylase that represses NFκB-dependent transcription

Gao, F., Cheng, J., Shi, T., & Yeh, E. T. H. (2006) · Nature Cell Biology · doi:10.1038/ncb1483 · Cited by 135 · see citing works

Glycogen Synthase Kinase 3β-Mediated Apoptosis of Primary Cortical Astrocytes Involves Inhibition of Nuclear Factor κB Signaling

Sanchez, J. F., Sniderhan, L. F., Williamson, A. L., Fan, S., Chakraborty‐Sett, S., & Maggirwar, S. B. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.13.4649-4662.2003 · Cited by 135 · see citing works

Protein-Protein Interactions and Transcriptional Antagonism between the Subfamily of NGFI-B/Nur77 Orphan Nuclear Receptors and Glucocorticoid Receptor

Martens, C., Bilodeau, S., Maira, M., Gauthier, Y., & Drouin, J. (2004) · Molecular Endocrinology · doi:10.1210/me.2004-0333 · Cited by 128 · see citing works

Inducible Phosphorylation of NF-κB p65 at Serine 468 by T Cell Costimulation Is Mediated by IKKϵ

Mattioli, I., Geng, H. Z., Sebald, A., Hodel, M., Bucher, C., Kracht, M., & Schmitz, M. L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m508045200 · Cited by 124 · see citing works

Nucleolar Sequestration of RelA (p65) Regulates NF-κB-Driven Transcription and Apoptosis

Stark, L. A., & Dunlop, M. G. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.14.5985-6004.2005 · Cited by 121 · see citing works

Suppression of MEK/ERK Signaling Pathway Enhances Cisplatin-induced NF-κB Activation by Protein Phosphatase 4-mediated NF-κB p65 Thr Dephosphorylation

Yeh, P.-Y., Yeh, K., Chuang, S., Song, Y., & Cheng, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402362200 · Cited by 119 · see citing works

RelA repression of RelB activity induces selective gene activation downstream of TNF receptors

Jacque, É., Tchénio, T., Piton, G., Roméo, P., & Baud, V. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507342102 · Cited by 117 · see citing works

Glucocorticoid Ligands Specify Different Interactions with NF-κB by Allosteric Effects on the Glucocorticoid Receptor DNA Binding Domain

Garside, H., Stevens, A., Farrow, S. N., Normand, C., Houle, B., Berry, A., Maschera, B., & Ray, D. W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407309200 · Cited by 115 · see citing works

Myc-ARF (Alternate Reading Frame) Interaction Inhibits the Functions of Myc

Datta, A., Nag, A., Pan, W., Hay, N., Gartel, A. L., Colamonici, O. R., Mori, Y., & Raychaudhuri, P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312305200 · Cited by 112 · see citing works

Identification of Nucleophosmin as an NF-κB Co-activator for the Induction of the Human SOD2 Gene

Dhar, S. K., Lynn, B. C., Daosukho, C., & Clair, D. K. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403553200 · Cited by 109 · see citing works

Human T-cell Lymphotropic Virus Type 1 Tax Induction of Biologically Active NF-κB Requires IκB Kinase-1-mediated Phosphorylation of RelA/p65

O’Mahony, A., Montaño, M., Beneden, K. V., Chen, L. F., & Greene, W. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401397200 · Cited by 109 · see citing works

DNA Binding of Repressor Nuclear Factor-κB p50/p50 Depends on Phosphorylation of Ser337 by the Protein Kinase A Catalytic Subunit

Guan, H., Hou, S., & Ricciardi, R. P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412180200 · Cited by 104 · see citing works

Nuclear Accumulation of cRel following C-Terminal phosphorylation by TBK1/IKKε

Harris, J., Olière, S., Sharma, S., Sun, Q., Lin, R., Hiscott, J. B., & Grandvaux, N. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.4.2527 · Cited by 102 · see citing works

Wnt-1 dependent activation of the survival factor NF-?B in PC12 cells

Bournat, J. C., Brown, A. M. C., & Soler, A. P. (2000) · Journal of Neuroscience Research · doi:10.1002/1097-4547(20000701)61:1 · Cited by 100 · see citing works

Regulation of Nuclear Factor κB Transactivation

Martín, Á. G., San-Antonio, B., & Fresno, M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011313200 · Cited by 96 · see citing works

Glucocorticoid Effects on NF-κB Binding in the Transcription of the ICAM-1 Gene

Lidén, J., Rafter, I., Truss, M., Gustafsson, J.-Α., & Okret, S. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3079 · Cited by 89 · see citing works

IKKβ phosphorylates p65 at S468 in transactivaton domain 2

Schwabe, R. F., & Sakurai, H. (2005) · The FASEB Journal · doi:10.1096/fj.05-3736fje · Cited by 84 · see citing works

Suberoylanilide Hydroxamic Acid Induces Akt-mediated Phosphorylation of p300, Which Promotes Acetylation and Transcriptional Activation of RelA/p65

Liu, Y., Denlinger, C. E., Rundall, B. K., Smith, P. W., & Jones, D. R. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604478200 · Cited by 83 · see citing works

NF-κB activation by combinations of NEMO SUMOylation and ATM activation stresses in the absence of DNA damage

Wuerzberger‐Davis, S. M., Nakamura, Y., Seufzer, B. J., & Miyamoto, S. (2006) · Oncogene · doi:10.1038/sj.onc.1209815 · Cited by 82 · see citing works

Cisplatin Mimics ARF Tumor Suppressor Regulation of RelA (p65) Nuclear Factor-κB Transactivation

Campbell, K. J., Witty, J., Rocha, S., & Perkins, N. D. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-2234 · Cited by 77 · see citing works

Cytosolic, nuclear and nucleolar localization signals determine subcellular distribution and activity of the NF-κB inducing kinase NIK

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Non-activated p53 co-localizes with sites of transcription within both the nucleoplasm and the nucleolus

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Signal-specific and phosphorylation-dependent RelB degradation: a potential mechanism of NF-κB control

Marienfeld, R. B., Berberich‐Siebelt, F., Berberich, I., Denk, A., Serfling, E., & Neumann, M. (2001) · Oncogene · doi:10.1038/sj.onc.1204884 · Cited by 73 · see citing works

Tumor Necrosis Factor-α Activation of NF-κB Requires the Phosphorylation of Ser-471 in the Transactivation Domain of c-Rel

Martín, Á. G., & Fresno, M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m909396199 · Cited by 70 · see citing works

Alternative Splicing— When Two’s a Crowd

Smith, C. W. J. (2005) · Cell · doi:10.1016/j.cell.2005.09.010 · Cited by 66 · see citing works

Estrogen Up-Regulation of p53 Gene Expression in MCF-7 Breast Cancer Cells Is Mediated by Calmodulin Kinase IV-Dependent Activation of a Nuclear Factor κB/CCAAT-Binding Transcription Factor-1 Complex

Qin, C., Nguyen, T. A., Stewart, J., Samudio, I. J., Burghardt, R. C., & Safe, S. H. (2002) · Molecular Endocrinology · doi:10.1210/me.2002-0006 · Cited by 60 · see citing works

C/EBPβ Blocks p65 Phosphorylation and Thereby NF-κB-Mediated Transcription in TNF-Tolerant Cells

Zwergal, A., Quirling, M., Saugel, B., Huth, K. C., Sydlik, C., Poli, V., Neumeier, D., Ziegler‐Heitbrock, H. W. L., & Brand, K. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.1.665 · Cited by 60 · see citing works

Critical Role of RelB Serine 368 for Dimerization and p100 Stabilization

Maier, H. J., Marienfeld, R. B., Wirth, T., & Baumann, B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301521200 · Cited by 57 · see citing works

NF-κB-Inducing Kinase Is Involved in the Activation of the CD28 Responsive Element through Phosphorylation of c-Rel and Regulation of Its Transactivating Activity

Sánchez-Valdepeñas, C., Martín, Á. G., Ramakrishnan, P., Wallach, D., & Fresno, M. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.8.4666 · Cited by 56 · see citing works

NF-κB RelB Forms an Intertwined Homodimer

Huang, D.-B., Vu, D., & Ghosh, G. (2005) · Structure · doi:10.1016/j.str.2005.06.018 · Cited by 51 · see citing works

NIK Is Involved in Nucleosomal Regulation by Enhancing Histone H3 Phosphorylation by IKKα

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rel Is rapidly tyrosine-phosphorylated following granulocyte-colony stimulating factor treatment of human neutrophils.

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