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THE NF-κB AND IκB PROTEINS: New Discoveries and Insights

Baldwin, Albert S.·1996·Annual Review of Immunology

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Abstract

▪ Abstract The transcription factor NF-κB has attracted widespread attention among researchers in many fields based on the following: its unusual and rapid regulation, the wide range of genes that it controls, its central role in immunological processes, the complexity of its subunits, and its apparent involvement in several diseases. A primary level of control for NF-κB is through interactions with an inhibitor protein called IκB. Recent evidence confirms the existence of multiple forms of IκB that appear to regulate NF-κB by distinct mechanisms. NF-κB can be activated by exposure of cells to LPS or inflammatory cytokines such as TNF or IL-1, viral infection or expression of certain viral gene products, UV irradiation, B or T cell activation, and by other physiological and nonphysiological stimuli. Activation of NF-κB to move into the nucleus is controlled by the targeted phosphorylation and subsequent degradation of IκB. Exciting new research has elaborated several important and unexpected findings that explain mechanisms involved in the activation of NF-κB. In the nucleus, NF-κB dimers bind to target DNA elements and activate transcription of genes encoding proteins involved with immune or inflammation responses and with cell growth control. Recent data provide evidence that NF-κB is constitutively active in several cell types, potentially playing unexpected roles in regulation of gene expression. In addition to advances in describing the mechanisms of NF-κB activation, excitement in NF-κB research has been generated by the first report of a crystal structure for one form of NF-κB, the first gene knockout studies for different forms of NF-κB and of IκB, and the implications for therapies of diseases thought to involve the inappropriate activation of NF-κB.

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A Single Ataxia Telangiectasia Gene with a Product Similar to PI-3 Kinase
Savitsky, K., Bar-Shira, A., Gilad, S., Rotman, G., Ziv, Y., Vanagaite, L., Tagle, D. A., Smith, S., Uziel, T., Sfez, S., et al. (1995) · Science · doi:10.1126/science.7792600 · Cited by 2,785
Role of transcription factor NF-kappa B/Rel in induction of nitric oxide synthase.
Xie, Q. W., Kashiwabara, Y., & Nathan, C. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37600-7 · Cited by 2,212
Characterization of Mechanisms Involved in Transrepression of NF-κB by Activated Glucocorticoid Receptors
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Self-citation

Show all 4 references

Research works printed but not linked: 176

10.1016/0092-8674(86)90346-6 · DOI
10.1016/0092-8674(86)90807-X · DOI
10.1126/science.3140380 · DOI
10.1146/annurev.cb.10.110194.002201 · DOI
10.1016/0955-0674(93)90014-H · DOI
10.1016/S0074-7696(08)61873-2 · DOI
10.1016/S0168-9525(00)89045-9 · DOI
10.1101/gad.7.11.2064 · DOI
10.1016/0168-9525(93)90106-R · DOI
10.1016/S0065-230X(08)60257-2 · DOI
10.1016/1074-7613(95)90112-4 · DOI
10.1128/MCB.14.12.8460 · DOI
10.1128/MCB.15.6.3100 · DOI
Parry G, 1994, J. Biol. Chem., 269, 20,823, 10.1016/S0021-9258(17)31895-1 · DOI
10.1016/0092-8674(91)90022-Q · DOI
10.1126/science.1891714 · DOI
10.1002/j.1460-2075.1994.tb06782.x · DOI
10.1002/j.1460-2075.1994.tb06723.x · DOI
10.1128/MCB.15.2.872 · DOI
10.1002/j.1460-2075.1993.tb05939.x · DOI
10.1128/MCB.15.4.2166 · DOI
Dobrzanski P, 1995, Oncogene, 10, 1003
10.1073/pnas.91.26.12634 · DOI
10.1128/MCB.14.6.3915 · DOI
10.1016/0092-8674(95)90511-1 · DOI
10.1074/jbc.270.18.10680 · DOI
10.1093/hmg/3.5.793 · DOI
10.1038/373303a0 · DOI
10.1038/373311a0 · DOI
Schmid R, 1994, J. Biol. Chem., 269, 32,162, 10.1016/S0021-9258(18)31615-6 · DOI
10.1016/0092-8674(94)90126-0 · DOI
10.1074/jbc.270.8.4138 · DOI
10.1016/0092-8674(92)90595-4 · DOI
10.1016/0092-8674(93)90495-C · DOI
10.1016/0092-8674(92)90596-5 · DOI
10.1101/gad.9.7.783 · DOI · Paper page
10.1128/MCB.13.10.6147 · DOI
Wu RL, 1994, J. Biol. Chem., 269, 28,450, 10.1016/S0021-9258(18)46948-7 · DOI
Lawrence R, 1994, J. Biol. Chem., 269, 28,913, 10.1016/S0021-9258(19)61994-0 · DOI
10.1101/gad.8.6.678 · DOI
10.1128/MCB.14.8.5349 · DOI
10.1128/MCB.14.5.3276 · DOI
10.1084/jem.181.3.1169 · DOI
10.1074/jbc.270.21.12343 · DOI
Berberich I, 1994, J. Immunol., 153, 4357, 10.4049/jimmunol.153.10.4357 · DOI
Sen J, 1995, J. Immunol., 154, 3213, 10.4049/jimmunol.154.7.3213 · DOI
10.1016/0896-6273(89)90266-3 · DOI
10.1002/j.1460-2075.1993.tb06110.x · DOI
10.1073/pnas.91.1.390 · DOI
10.1128/MCB.14.6.3981 · DOI
10.1074/jbc.270.8.3710 · DOI
10.1128/MCB.13.3.1572 · DOI
10.1128/MCB.14.11.7226 · DOI
10.1074/jbc.270.26.15576 · DOI
10.1074/jbc.270.13.7219 · DOI
10.1038/352733a0 · DOI
10.1074/jbc.270.7.3123 · DOI
10.1074/jbc.270.19.11453 · DOI
10.1128/MCB.14.10.6635 · DOI
10.1128/MCB.14.10.6570 · DOI
10.1074/jbc.270.15.8976 · DOI
10.1128/MCB.15.5.2558 · DOI
10.1128/MCB.14.10.6464 · DOI
10.1128/MCB.14.9.5701 · DOI
10.1074/jbc.270.2.933 · DOI
10.1073/pnas.92.8.3561 · DOI
10.1128/MCB.15.3.1786 · DOI
10.1128/MCB.15.1.152 · DOI
10.1016/0092-8674(95)90506-5 · DOI
10.1084/jem.181.4.1459 · DOI
10.1128/MCB.14.5.2926 · DOI
10.1074/jbc.270.29.17064 · DOI
10.1002/j.1460-2075.1994.tb06329.x · DOI
10.1073/pnas.90.5.1696 · DOI
10.1128/MCB.13.11.7191 · DOI
Wechler A, 1994, J. Immunol., 153, 2515, 10.4049/jimmunol.153.6.2515 · DOI
10.1182/blood.V83.9.2469.2469 · DOI
10.1128/MCB.14.2.1039 · DOI
10.1128/MCB.14.12.7967 · DOI
Wu H, 1994, J. Biol. Chem., 269, 20,067, 10.1016/S0021-9258(17)32128-2 · DOI
10.1016/0092-8674(95)90415-8 · DOI
10.1084/jem.181.1.181 · DOI
10.1016/0092-8674(95)90416-6 · DOI
10.1038/373531a0 · DOI
10.1038/376167a0 · DOI
10.1101/gad.9.16.1965 · DOI
10.1101/gad.9.22.2736 · DOI
10.1128/MCB.14.11.7377 · DOI
10.1002/j.1460-2075.1994.tb06878.x · DOI
10.1073/pnas.91.25.11884 · DOI
10.1073/pnas.91.26.12740 · DOI
10.1073/pnas.92.2.552 · DOI
10.1128/MCB.15.3.1302 · DOI · Paper page
10.1128/MCB.15.3.1294 · DOI
10.1016/S0092-8674(94)90482-0 · DOI
10.1126/science.7878466 · DOI · Paper page
10.1128/MCB.15.5.2809 · DOI
10.1002/j.1460-2075.1995.tb07287.x · DOI
10.1101/gad.9.13.1586 · DOI
10.1073/pnas.92.24.11259 · DOI
10.1073/pnas.92.17.7637 · DOI
10.1128/MCB.15.5.2413 · DOI
10.1128/MCB.15.10.5339 · DOI
10.1002/j.1460-2075.1994.tb06781.x · DOI
10.1016/0378-1119(95)00507-3 · DOI
10.1074/jbc.270.6.2703 · DOI
10.1128/MCB.15.3.1737 · DOI
10.1128/MCB.15.5.2689 · DOI
10.1016/0092-8674(95)90435-2 · DOI
10.1073/pnas.91.14.6288 · DOI
10.1126/science.7914032 · DOI
10.1073/pnas.90.20.9247 · DOI
Finco T, 1993, J. Biol. Chem., 268, 17, 10.1016/S0021-9258(17)46756-1 · DOI
10.1002/j.1460-2075.1994.tb06578.x · DOI
Hayashi T, 1993, J. Biol. Chem., 268, 26,790, 10.1016/S0021-9258(19)74382-8 · DOI
10.1084/jem.181.3.1091 · DOI
10.1074/jbc.270.31.18347 · DOI
10.1016/0092-8674(94)90275-5 · DOI
Machleidt T, 1994, J. Biol. Chem., 269, 13,760, 10.1016/S0021-9258(17)36712-1 · DOI
10.1093/intimm/6.8.1269 · DOI
Johns L, 1994, J. Immunol., 152, 5877, 10.4049/jimmunol.152.12.5877 · DOI
10.1074/jbc.270.39.22689 · DOI · Paper page
10.1016/1074-5521(95)90076-4 · DOI
Brennan P, 1995, Biochem. Biophys. Acta, 1260, 1670
10.1006/bbrc.1995.1693 · DOI
10.1016/S0969-2126(01)00159-9 · DOI
10.1016/0165-2478(95)00213-O · DOI
Koong A, 1994, Cancer Res., 54, 1425
Koong A, 1994, Cancer Res., 54, 5273
10.1073/pnas.92.5.1480 · DOI
10.1006/viro.1995.1029 · DOI
Sukuki T, 1995, Oncogene, 10, 1199
10.1074/jbc.270.20.11745 · DOI
10.1128/MCB.14.10.6443 · DOI
Suzuki T, 1994, Oncogene, 9, 3099
10.1182/blood.V84.9.2904.2904 · DOI
10.1084/jem.179.3.961 · DOI
10.1002/j.1460-2075.1995.tb07030.x · DOI
10.1002/j.1460-2075.1995.tb07141.x · DOI
10.1016/1074-7613(94)90068-X · DOI
Niederman T, 1992, J. Virol., 66, 6213, 10.1128/jvi.66.10.6213-6219.1992 · DOI
Herrero J, 1995, J. Virol., 69, 2168, 10.1128/jvi.69.4.2168-2174.1995 · DOI
Mitchell T, 1995, J. Virol., 69, 2968, 10.1128/jvi.69.5.2968-2976.1995 · DOI
Paine E, 1995, J. Virol., 69, 4572, 10.1128/jvi.69.7.4572-4576.1995 · DOI
Huen D, 1995, Oncogene, 10, 549
10.1016/0092-8674(95)90489-1 · DOI
10.1016/0092-8674(95)90070-5 · DOI
10.1002/jcb.240570214 · DOI
10.1074/jbc.270.16.9558 · DOI
10.1016/0092-8674(93)80068-P · DOI
10.1073/pnas.91.2.752 · DOI
Mukaida N, 1994, J. Biol. Chem., 269, 13,289, 10.1016/S0021-9258(17)36831-X · DOI
10.1210/me.9.4.401 · DOI
10.1126/science.270.5234.283 · DOI
10.1126/science.270.5234.286 · DOI · Paper page
10.1126/science.8052854 · DOI
Lai JH, 1994, J. Biol. Chem., 269, 30
10.1161/01.RES.76.6.980 · DOI
10.1074/jbc.270.23.14214 · DOI
Lander H, 1993, J. Immunol., 150, 1509, 10.4049/jimmunol.150.4.1509 · DOI
10.1084/jem.179.3.931 · DOI
10.1002/j.1460-2075.1995.tb07191.x · DOI
10.1016/0014-5793(95)00157-5 · DOI
10.1016/0092-8674(95)90085-3 · DOI
10.1016/0092-8674(93)90134-C · DOI · Paper page
10.1016/0092-8674(94)90131-7 · DOI · Paper page
Pahl H, 1995, J. Virol., 69, 1480, 10.1128/jvi.69.3.1480-1484.1995 · DOI
10.1161/01.CIR.91.9.2488 · DOI
10.1172/JCI117409 · DOI
10.1006/bbrc.1994.2552 · DOI
Beauparlant P, 1994, Oncogene, 9, 3189
10.1126/science.1299224 · DOI
Zhang J, Oncogene, 9, 1931
Thakur S, 1994, Oncogene, 9, 2335
Hwang S, 1995, Cancer Biochem. Biophys., 14, 265
10.1126/science.7777860 · DOI

Oxidative stress, inflammation, and cancer: How are they linked?
Reuter, S., Gupta, S. C., Chaturvedi, M. M., & Aggarwal, B. B. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.09.006 · Cited by 5,441
NF-κB: a key role in inflammatory diseases
Tak, P. P., & Firestein, G. S. (2001) · Journal of Clinical Investigation · doi:10.1172/jci11830 · Cited by 3,918
CELLULAR RESPONSES TO INTERFERON-γ
Boehm, U., Klamp, T., Groot, M., & Howard, J. C. (1997) · Annual Review of Immunology · doi:10.1146/annurev.immunol.15.1.749 · Cited by 2,890
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
CBP/p300 in cell growth, transformation, and development
Goodman, R. H., & Smolik, S. (2000) · Genes & Development · doi:10.1101/gad.14.13.1553 · Cited by 1,778
Inflammatory and immune pathways in the pathogenesis of periodontal disease
Cekici, A., Kantarci, A., Hasturk, H., & Van Dyke, T. E. (2014) · Periodontology 2000 · doi:10.1111/prd.12002 · Cited by 1,415
Dissecting molecular cross-talk between Nrf2 and NF-κB response pathways
Wardyn, J. D., Ponsford, A. H., & Sanderson, C. M. (2015) · Biochemical Society Transactions · doi:10.1042/bst20150014 · Cited by 1,200
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
The role of the gut microbiota in NAFLD
Leung, C., Rivera, L., Furness, J. B., & Angus, P. W. (2016) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2016.85 · Cited by 1,020
The Molecular Basis of Skeletal Muscle Atrophy
Jackman, R. W., & Kandarian, S. C. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00579.2003 · Cited by 1,008
Requirement for NF-κB in osteoclast and B-cell development
Franzoso, G., Carlson, L., Xing, L., Poljak, L., Shores, E. W., Brown, K. D., Leonardi, A., Tran, T., Boyce, B. F., & Siebenlist, U. (1997) · Genes & Development · doi:10.1101/gad.11.24.3482 · Cited by 996
Virus-Dependent Phosphorylation of the IRF-3 Transcription Factor Regulates Nuclear Translocation, Transactivation Potential, and Proteasome-Mediated Degradation
Lin, R., Heylbroeck, C., Pitha, P. M., & Hiscott, J. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.5.2986 · Cited by 915
Molecular basis of the effects of shear stress on vascular endothelial cells
Li, Y.-S. J., Haga, J. H., & Chien, S. (2005) · Journal of Biomechanics · doi:10.1016/j.jbiomech.2004.09.030 · Cited by 904
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
SIRT1 Protects against Microglia-dependent Amyloid-β Toxicity through Inhibiting NF-κB Signaling
Chen, J., Zhou, Y., Mueller-Steiner, S., Chen, L.-F., Kwon, H., Yi, S., Mucke, L., & Gan, L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509329200 · Cited by 740
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
Activation of innate immunity system during aging: NF-kB signaling is the molecular culprit of inflamm-aging
Salminen, A., Huuskonen, J., Ojala, J., Kauppinen, A., Kaarniranta, K., & Suuronen, T. (2008) · Ageing Research Reviews · doi:10.1016/j.arr.2007.09.002 · Cited by 581
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
Iron behaving badly: inappropriate iron chelation as a major contributor to the aetiology of vascular and other progressive inflammatory and degenerative diseases
Kell, D. B. (2009) · BMC Medical Genomics · doi:10.1186/1755-8794-2-2 · Cited by 554
Inflammation–Nature's Way to Efficiently Respond to All Types of Challenges: Implications for Understanding and Managing “the Epidemic” of Chronic Diseases
Bennett, J. M., Reeves, G., Billman, G. E., & Sturmberg, J. P. (2018) · Frontiers in Medicine · doi:10.3389/fmed.2018.00316 · Cited by 531
Transcriptional regulation of bcl-2 by nuclear factor κB and its significance in prostate cancer
Catz, S. D., & Johnson, J. L. (2001) · Oncogene · doi:10.1038/sj.onc.1204926 · Cited by 538
A critical role for NF-κB in Gata3 expression and TH2 differentiation in allergic airway inflammation
Das, J., Chen, C.-H., Yang, L., Cohn, L., Ray, P., & Ray, A. (2001) · Nature Immunology · doi:10.1038/83158 · Cited by 518
BCG Vaccination in Humans Elicits Trained Immunity via the Hematopoietic Progenitor Compartment
Cirovic, B., de Bree, L. C. J., Groh, L., Blok, B. A., Chan, J., van der Velden, W. J. F. M., Bremmers, M. E. J., van Crevel, R., Händler, K., Picelli, S., et al. (2020) · Cell Host & Microbe · doi:10.1016/j.chom.2020.05.014 · Cited by 510
Proinflammatory cytokines regulate human glucocorticoid receptor gene expression and lead to the accumulation of the dominant negative β isoform: A mechanism for the generation of glucocorticoid resistance
Webster, J. C., Oakley, R. H., Jewell, C. M., & Cidlowski, J. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.121455098 · Cited by 482
Modulation of the fecal microflora profile and immune function by a novel trans-galactooligosaccharide mixture (B-GOS) in healthy elderly volunteers
Vulevic, J., Drakoularakou, A., Yaqoob, P., Tzortzis, G., & Gibson, G. R. (2008) · The American Journal of Clinical Nutrition · doi:10.3945/ajcn.2008.26242 · Cited by 451
The role of the gut microbiota in nonalcoholic fatty liver disease
Abu-Shanab, A., & Quigley, E. M. M. (2010) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2010.172 · Cited by 457
The molecular inflammatory process in aging
Chung, H. Y., Sung, B., Jung, K. J., Zou, Y., & Yu, B. P. (2006) · Antioxidants & Redox Signaling · doi:10.1089/ars.2006.8.572 · Cited by 437
Anthocyanin‐ and hydrolyzable tannin‐rich pomegranate fruit extract modulates MAPK and NF‐κB pathways and inhibits skin tumorigenesis in CD‐1 mice
Afaq, F., Saleem, M., Krueger, C. G., Reed, J. D., & Mukhtar, H. (2005) · International Journal of Cancer · doi:10.1002/ijc.20587 · Cited by 439
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
Increased NF-Κb Signalling Up-Regulates BACE1 Expression and its Therapeutic Potential in Alzheimer's Disease
Chen, C.-H., Zhou, W., Liu, S., Deng, Y., Cai, F., Tone, M., Tone, Y., Tong, Y., & Song, W. (2012) · The International Journal of Neuropsychopharmacology · doi:10.1017/s1461145711000149 · Cited by 433
Irinotecan: mechanisms of tumor resistance and novel strategies for modulating its activity.
Xu, Y., & Villalona-Calero, M. A. (2002) · Annals of Oncology · doi:10.1093/annonc/mdf337 · Cited by 413
Eicosapentaenoic Acid Prevents LPS-Induced TNF-α Expression by Preventing NF-κB Activation
Zhao, Y., Joshi-Barve, S., Barve, S., & Chen, L. H. (2004) · Journal of the American College of Nutrition · doi:10.1080/07315724.2004.10719345 · Cited by 405
The Role of Curcumin in Aging and Senescence: Molecular Mechanisms
Zia, A., Farkhondeh, T., Pourbagher-Shahri, A. M., & Samarghandian, S. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.111119 · Cited by 378
NF-κB as a therapeutic target in chronic inflammation: recent advances
Makarov, S. S. (2000) · Molecular Medicine Today · doi:10.1016/s1357-4310(00)01814-1 · Cited by 379
Nedd8 Modification of Cul-1 Activates SCFβTrCP-Dependent Ubiquitination of IκBα
Read, M. A., Brownell, J. E., Gladysheva, T. B., Hottelet, M., Parent, L. A., Coggins, M. B., Pierce, J. W., Podust, V. N., Luo, R.-S., Chau, V., et al. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.7.2326-2333.2000 · Cited by 363
Requirement of tumor necrosis factor receptor-associated factor (TRAF)6 in interleukin 17 signal transduction
Schwandner, R., Yamaguchi, K., & Cao, Z. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.191.7.1233 · Cited by 349
Inflammation and the development of pancreatic cancer
Farrow, B., & Evers, B. M. (2002) · Surgical Oncology · doi:10.1016/s0960-7404(02)00015-4 · Cited by 338
Zinc: Mechanisms of Host Defense1,
Prasad, A. S. (2007) · The Journal of Nutrition · doi:10.1093/jn/137.5.1345 · Cited by 314
Immunosuppressive and Anti-Inflammatory Mechanisms of Triptolide, the Principal Active Diterpenoid from the Chinese Medicinal Herb Tripterygium wilfordii Hook. f.
Qiu, D., & Kao, P. N. (2003) · Drugs in R & D · doi:10.2165/00126839-200304010-00001 · Cited by 311
The Inflammation Hypothesis of Aging: Molecular Modulation by Calorie Restriction
Chung, H. Y., Kim, H. J., Kim, J. W., & Yu, B. P. (2001) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2001.tb05662.x · Cited by 305
Role of PGC-1α Signaling in Skeletal Muscle Health and Disease
Kang, C., & Li Ji, L. (2012) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2012.06738.x · Cited by 291
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
Chronic Unpredictable Stress Exacerbates Lipopolysaccharide-Induced Activation of Nuclear Factor-κB in the Frontal Cortex and Hippocampus via Glucocorticoid Secretion
Munhoz, C. D., Lepsch, L. B., Kawamoto, E. M., Malta, M. B., Lima, L. D. S., Werneck Avellar, M. C., Sapolsky, R. M., & Scavone, C. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.4398-05.2006 · Cited by 274
Tumor Necrosis Factor Alpha and Interleukin-1β Regulate the Murine Manganese Superoxide Dismutase Gene Through a Complex Intronic Enhancer Involving C/EBP-β and NF-κB
Jones, P. L., Ping, D., & Boss, J. M. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.12.6970 · Cited by 244
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Madrigal, J. (2002) · Neuropsychopharmacology · doi:10.1016/s0893-133x(01)00292-5 · Cited by 232
Tumour Necrosis Factor Alpha in Intestinal Homeostasis and Gut Related Diseases
Ruder, B., Atreya, R., & Becker, C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20081887 · Cited by 228
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Pamukcu, B., Lip, G. Y. H., & Shantsila, E. (2011) · Thrombosis Research · doi:10.1016/j.thromres.2011.03.025 · Cited by 218
SMRT Derepression by the IκB Kinase α
Hoberg, J. E., Yeung, F., & Mayo, M. W. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.10.010 · Cited by 220
Anti-inflammatory effects of fluoxetine in lipopolysaccharide(LPS)-stimulated microglial cells
Liu, D., Wang, Z., Liu, S., Wang, F., Zhao, S., & Hao, A. (2011) · Neuropharmacology · doi:10.1016/j.neuropharm.2011.04.033 · Cited by 221
The c‐myc Promoter: Still MysterY and Challenge
(2008) · Advances in Cancer Research · doi:10.1016/s0065-230x(07)99004-1 · Cited by 211
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Tan, K. S., Nackley, A. G., Satterfield, K., Maixner, W., Diatchenko, L., & Flood, P. M. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2006.06.007 · Cited by 204
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Hong, Y., Lee, J. H., Jeong, K. W., Choi, C. S., & Jun, H. (2019) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12434 · Cited by 188
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Piret, B., Schoonbroodt, S., & Piette, J. (1999) · Oncogene · doi:10.1038/sj.onc.1202541 · Cited by 176
Central role of transcription factor NF‐IL6 for cytokine and iron‐mediated regulation of murine inducible nitric oxide synthase expression
Dlaska, M., & Weiss, G. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.162.10.6171 · Cited by 176
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Zi, M., & Xu, Y. (2018) · Immunology Letters · doi:10.1016/j.imlet.2018.01.006 · Cited by 170
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Ishida, Y., Kondo, T., Kimura, A., Matsushima, K., & Mukaida, N. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.9.5598 · Cited by 168
Distinct roles for the NF-κB1 (p50) and c-Rel transcription factors in inflammatory arthritis
Campbell, I. K., Gerondakis, S., O’Donnell, K., & Wicks, I. P. (2000) · Journal of Clinical Investigation · doi:10.1172/jci8298 · Cited by 168
NF-κB p50 and p52 Expression Is Not Required for RANK-Expressing Osteoclast Progenitor Formation but Is Essential for RANK- and Cytokine-Mediated Osteoclastogenesis
Xing, L., Bushnell, T. P., Carlson, L., Tai, Z., Tondravi, M., Siebenlist, U., Young, F., & Boyce, B. F. (2002) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.2002.17.7.1200 · Cited by 165
Hypothesis: Ataxia‐telangiectasia: Is ATM a sensor of oxidative damage and stress?
Rotman, G., & Shiloh, Y. (1997) · BioEssays · doi:10.1002/bies.950191011 · Cited by 160
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Li, X., Bu, X., Lu, B., Avraham, H., Flavell, R. A., & Lim, B. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.4.1158-1171.2002 · Cited by 153
Signaling pathways weigh in on decisions to make or break skeletal muscle
Guttridge, D. C. (2004) · Current Opinion in Clinical Nutrition and Metabolic Care · doi:10.1097/01.mco.0000134364.61406.26 · Cited by 149
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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
DNA damage drives accelerated bone aging via an NF- κ B–dependent mechanism
Chen, Q., Liu, K., Robinson, A. R., Clauson, C. L., Blair, H. C., Robbins, P. D., Niedernhofer, L. J., & Ouyang, H. (2013) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.1851 · Cited by 135
Protein phosphatase 2A interacts with and directly dephosphorylates RelA
Yang, J., Fan, G.-H., Wadzinski, B. E., Sakurai, H., & Richmond, A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106103200 · Cited by 130
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Authors: Baldwin, A. S.
Affiliations: Lineberger Comprehensive Cancer Center, Curriculum in Genetics and Molecular Biology, and Department of Biology, University of North Carolina, Chapel Hill, North Carolina 27599
Venue: Annual Review of Immunology
Publisher: Annual Reviews
Published: 1996-04
Volume: 14
Issue: 1
Pages: 649-681
ISSN: 0732-0582
1545-3278
DOI: 10.1146/annurev.immunol.14.1.649
Cited by: 4,979
References: 4
Language: en

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THE NF-κB AND IκB PROTEINS: New Discoveries and Insights

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