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Volumn 60, Issue 8, 2000, Pages 1185-1195

Signal transduction by tumor necrosis factor and gene regulation of the inflammatory cytokine interleukin-6

Author keywords

Acetyltransferase; Coactivator; Corepressor; Deacetylase; Glucocorticoid; Interleukin 6; NF B; Tumor necrosis factor

Indexed keywords

CYTOKINE; GLUCOCORTICOID RECEPTOR; HISTONE; HISTONE ACETYLTRANSFERASE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 6; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN P55; PROTEIN SUBUNIT; TRANSCRIPTION FACTOR; TUMOR NECROSIS FACTOR; TUMOR NECROSIS FACTOR RECEPTOR;

EID: 0034668173     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(00)00412-3     Document Type: Article
Times cited : (269)

References (201)
  • 1
    • 0030589152 scopus 로고    scopus 로고
    • Initiation of acute phase response and synthesis of cytokines
    • Koj A. Initiation of acute phase response and synthesis of cytokines. Biochim Biophys Acta. 1317:1996;84-94.
    • (1996) Biochim Biophys Acta , vol.1317 , pp. 84-94
    • Koj, A.1
  • 2
    • 0001929693 scopus 로고    scopus 로고
    • Cytokines in acute and chronic inflammation
    • Feghali C., Wright T. Cytokines in acute and chronic inflammation. Front Biosci. 2:1997;d12-d26.
    • (1997) Front Biosci , vol.2 , pp. 12-d26
    • Feghali, C.1    Wright, T.2
  • 3
    • 0033106338 scopus 로고    scopus 로고
    • N-acetyl-L-cysteine inhibits primary human T cell responses at the dendritic cell level: Association with NF-κB inhibition
    • Verhasselt V., Vanden Berghe W., Vanderheyde N., Willems F., Haegeman G., Goldman M. N-acetyl-L-cysteine inhibits primary human T cell responses at the dendritic cell level Association with NF-κB inhibition. J Immunol. 162:1999;2569-2574.
    • (1999) J Immunol , vol.162 , pp. 2569-2574
    • Verhasselt, V.1    Vanden Berghe, W.2    Vanderheyde, N.3    Willems, F.4    Haegeman, G.5    Goldman, M.6
  • 4
    • 0027421831 scopus 로고
    • Interleukin-6 in biology and medicine
    • Akira S., Taga T., Kishimoto T. Interleukin-6 in biology and medicine. Adv Immunol. 54:1993;1-78.
    • (1993) Adv Immunol , vol.54 , pp. 1-78
    • Akira, S.1    Taga, T.2    Kishimoto, T.3
  • 5
    • 0030964023 scopus 로고    scopus 로고
    • Interleukin-6 (IL-6) - A molecule with both beneficial and destructive potentials
    • Gadient R.A., Otten U.H. Interleukin-6 (IL-6) - A molecule with both beneficial and destructive potentials. Prog Neurobiol. 52:1997;379-390.
    • (1997) Prog Neurobiol , vol.52 , pp. 379-390
    • Gadient, R.A.1    Otten, U.H.2
  • 7
    • 0034051068 scopus 로고    scopus 로고
    • Age-associated increased interleukin-6 gene expression, late-life diseases, and frailty
    • Erschler W.B., Keller E.T. Age-associated increased interleukin-6 gene expression, late-life diseases, and frailty. Annu Rev Med. 51:2000;245-270.
    • (2000) Annu Rev Med , vol.51 , pp. 245-270
    • Erschler, W.B.1    Keller, E.T.2
  • 8
    • 0032990516 scopus 로고    scopus 로고
    • Expression and up-regulation of interleukin-6 in oesophageal carcinoma cells by n-sodium butyrate
    • Wang L.S., Chow K.C., Wu C.W. Expression and up-regulation of interleukin-6 in oesophageal carcinoma cells by n-sodium butyrate. Br J Cancer. 80:1999;1617-1622.
    • (1999) Br J Cancer , vol.80 , pp. 1617-1622
    • Wang, L.S.1    Chow, K.C.2    Wu, C.W.3
  • 9
    • 0033036097 scopus 로고    scopus 로고
    • Serum interleukin-6 levels correlate to tumor progression and prognosis in metastatic breast carcinoma
    • Zhang G.J., Adachi I. Serum interleukin-6 levels correlate to tumor progression and prognosis in metastatic breast carcinoma. Anticancer Res. 19:1999;1427-1432.
    • (1999) Anticancer Res , vol.19 , pp. 1427-1432
    • Zhang, G.J.1    Adachi, I.2
  • 10
    • 0345251973 scopus 로고    scopus 로고
    • Pharmacological modulation of cytokine action and production through signaling pathways
    • Young P.R. Pharmacological modulation of cytokine action and production through signaling pathways. Cytokine Growth Factor Rev. 9:1998;239-257.
    • (1998) Cytokine Growth Factor Rev , vol.9 , pp. 239-257
    • Young, P.R.1
  • 11
    • 0032857815 scopus 로고    scopus 로고
    • Gene-regulating protein kinases as important anti-inflammatory targets
    • Bhagwat S.S., Manning A.M., Hoekstra M.F., Lewis A. Gene-regulating protein kinases as important anti-inflammatory targets. Drug Discov Today. 4:1999;472-479.
    • (1999) Drug Discov Today , vol.4 , pp. 472-479
    • Bhagwat, S.S.1    Manning, A.M.2    Hoekstra, M.F.3    Lewis, A.4
  • 12
    • 0033178359 scopus 로고    scopus 로고
    • The development and therapeutic potential of protein kinase inhibitors
    • Cohen P. The development and therapeutic potential of protein kinase inhibitors. Curr Opin Chem Biol. 3:1999;459-465.
    • (1999) Curr Opin Chem Biol , vol.3 , pp. 459-465
    • Cohen, P.1
  • 13
    • 0033147469 scopus 로고    scopus 로고
    • Emerging targets for anti-inflammatory therapy
    • Han J., Ulevitch R.J. Emerging targets for anti-inflammatory therapy. Nat Cell Biol. 1:1999;E39-E40.
    • (1999) Nat Cell Biol , vol.1 , pp. 39-E40
    • Han, J.1    Ulevitch, R.J.2
  • 14
    • 0032850020 scopus 로고    scopus 로고
    • P38 MAPK signalling cascades in inflammatory disease
    • Herlaar E., Brown Z. p38 MAPK signalling cascades in inflammatory disease. Mol Med Today. 5:1999;439-447.
    • (1999) Mol Med Today , vol.5 , pp. 439-447
    • Herlaar, E.1    Brown, Z.2
  • 15
    • 0033178332 scopus 로고    scopus 로고
    • New targets for anti-inflammatory drugs
    • Lewis A.J., Manning A.M. New targets for anti-inflammatory drugs. Curr Opin Chem Biol. 3:1999;489-494.
    • (1999) Curr Opin Chem Biol , vol.3 , pp. 489-494
    • Lewis, A.J.1    Manning, A.M.2
  • 16
    • 0027746269 scopus 로고
    • Activation of the nuclear factor κb is not sufficient for regulation of tumor necrosis factor-induced interleukin-6 gene expression
    • Patestos N.P., Haegeman G., Vandevoorde V., Fiers W. Activation of the nuclear factor κB is not sufficient for regulation of tumor necrosis factor-induced interleukin-6 gene expression. Biochimie. 75:1993;1007-1018.
    • (1993) Biochimie , vol.75 , pp. 1007-1018
    • Patestos, N.P.1    Haegeman, G.2    Vandevoorde, V.3    Fiers, W.4
  • 17
    • 0028362019 scopus 로고
    • Multiple regulatory elements in the interleukin-6 gene mediate induction by prostaglandins, cyclic AMP, and lipopolysaccharide
    • Dendorfer U., Oettgen P., Libermann T.A. Multiple regulatory elements in the interleukin-6 gene mediate induction by prostaglandins, cyclic AMP, and lipopolysaccharide. Mol Cell Biol. 14:1994;4443-4454.
    • (1994) Mol Cell Biol , vol.14 , pp. 4443-4454
    • Dendorfer, U.1    Oettgen, P.2    Libermann, T.A.3
  • 18
    • 0028214317 scopus 로고
    • Studies on the induction of the interleukin-6 promoter in cell lines of human and simian origin
    • Vanhoenacker P., Fiers W., Haegeman G. Studies on the induction of the interleukin-6 promoter in cell lines of human and simian origin. Eur Cytokine Netw. 5:1994;283-291.
    • (1994) Eur Cytokine Netw , vol.5 , pp. 283-291
    • Vanhoenacker, P.1    Fiers, W.2    Haegeman, G.3
  • 19
    • 0028865771 scopus 로고
    • Triggering of the human interleukin-6 gene by interferon-γ And tumor necrosis factor-α In monocytic cells involves cooperation between interferon regulatory factor-1, NF-κB, and Sp1 transcription factors
    • Sanceau J., Kaisho T., Hirano T., Wietzerbin J. Triggering of the human interleukin-6 gene by interferon-γ and tumor necrosis factor-α in monocytic cells involves cooperation between interferon regulatory factor-1, NF-κB, and Sp1 transcription factors. J Biol Chem. 270:1995;27920-27931.
    • (1995) J Biol Chem , vol.270 , pp. 27920-27931
    • Sanceau, J.1    Kaisho, T.2    Hirano, T.3    Wietzerbin, J.4
  • 20
    • 0343778752 scopus 로고
    • TNF-induced mechanisms for IL6 gene induction
    • NATO ASI Series (Eds. Packer L and Wirtz K), Springer, Berlin/Heidelberg/New York
    • Haegeman G and Fiers W, TNF-induced mechanisms for IL6 gene induction. In: Signalling Mechanisms - From Transcription Factors to Oxidative Stress, NATO ASI Series (Eds. Packer L and Wirtz K), Vol. H 92, pp. 375-382. Springer, Berlin/Heidelberg/New York, 1995.
    • (1995) In: Signalling Mechanisms - From Transcription Factors to Oxidative Stress , vol.92H , pp. 375-382
    • Haegeman, G.1    Fiers, W.2
  • 21
    • 0030914237 scopus 로고    scopus 로고
    • HIV-1 Tat induces the expression of the interleukin-6 (IL6) gene by binding to the IL6 leader RNA and by interacting with CAAT enhancer-binding protein β (NF-IL6) transcription factors
    • Ambrosino C., Ruocco M.R., Chen X., Mallardo M., Baudi F., Trematerra S., Quinto I., Venuta S., Scala G. HIV-1 Tat induces the expression of the interleukin-6 (IL6) gene by binding to the IL6 leader RNA and by interacting with CAAT enhancer-binding protein β (NF-IL6) transcription factors. J Biol Chem. 272:1997;14883-14892.
    • (1997) J Biol Chem , vol.272 , pp. 14883-14892
    • Ambrosino, C.1    Ruocco, M.R.2    Chen, X.3    Mallardo, M.4    Baudi, F.5    Trematerra, S.6    Quinto, I.7    Venuta, S.8    Scala, G.9
  • 22
    • 0032488837 scopus 로고    scopus 로고
    • P38 and extracellular signal-regulated kinase mitogen-activated protein kinase pathways are required for nuclear factor-κB p65 transactivation mediated by tumor necrosis factor
    • Vanden Berghe W., Plaisance S., Boone E., De Bosscher K., Schmitz M.L., Fiers W., Haegeman G. p38 and extracellular signal-regulated kinase mitogen-activated protein kinase pathways are required for nuclear factor-κB p65 transactivation mediated by tumor necrosis factor. J Biol Chem. 273:1998;3285-3290.
    • (1998) J Biol Chem , vol.273 , pp. 3285-3290
    • Vanden Berghe, W.1    Plaisance, S.2    Boone, E.3    De Bosscher, K.4    Schmitz, M.L.5    Fiers, W.6    Haegeman, G.7
  • 23
    • 0033527448 scopus 로고    scopus 로고
    • The nuclear factor-κB engages CBP/p300 and histone acetyltransferase activity for transcriptional activation of the interleukin-6 gene promoter
    • Vanden Berghe W., De Bosscher K., Boone E., Plaisance S., Haegeman G. The nuclear factor-κB engages CBP/p300 and histone acetyltransferase activity for transcriptional activation of the interleukin-6 gene promoter. J Biol Chem. 274:1999;32091-32098.
    • (1999) J Biol Chem , vol.274 , pp. 32091-32098
    • Vanden Berghe, W.1    De Bosscher, K.2    Boone, E.3    Plaisance, S.4    Haegeman, G.5
  • 27
    • 0033612571 scopus 로고    scopus 로고
    • The zinc finger protein A20 inhibits TNF-induced NF-κB-dependent gene expression by interfering with an RIP- Or TRAF2-mediated transactivation signal and directly binds to a novel NF-κB-inhibiting protein ABIN
    • Heyninck K., De Valck D., Vanden Berghe W., Van Criekinge W., Contreras R., Fiers W., Haegeman G., Beyaert R. The zinc finger protein A20 inhibits TNF-induced NF-κB-dependent gene expression by interfering with an RIP- or TRAF2-mediated transactivation signal and directly binds to a novel NF-κB-inhibiting protein ABIN. J Cell Biol. 145:1999;1471-1482.
    • (1999) J Cell Biol , vol.145 , pp. 1471-1482
    • Heyninck, K.1    De Valck, D.2    Vanden Berghe, W.3    Van Criekinge, W.4    Contreras, R.5    Fiers, W.6    Haegeman, G.7    Beyaert, R.8
  • 28
    • 0033712615 scopus 로고    scopus 로고
    • Recruitment of the IKK signalosome to the p55 TNF receptor: RIP and A20 bind to NEMO (IKKγ) upon receptor stimulation
    • Zhang S.Q., Kovalenko A., Cantarella G., Wallach D. Recruitment of the IKK signalosome to the p55 TNF receptor RIP and A20 bind to NEMO (IKKγ) upon receptor stimulation. Immunity. 12:2000;301-311.
    • (2000) Immunity , vol.12 , pp. 301-311
    • Zhang, S.Q.1    Kovalenko, A.2    Cantarella, G.3    Wallach, D.4
  • 29
    • 0030990123 scopus 로고    scopus 로고
    • Induced expression of trimerized intracellular domains of the human tumor necrosis factor (TNF) p55 receptor elicits TNF effects
    • Vandevoorde V., Haegeman G., Fiers W. Induced expression of trimerized intracellular domains of the human tumor necrosis factor (TNF) p55 receptor elicits TNF effects. J Cell Biol. 137:1997;1627-1638.
    • (1997) J Cell Biol , vol.137 , pp. 1627-1638
    • Vandevoorde, V.1    Haegeman, G.2    Fiers, W.3
  • 30
    • 0032414051 scopus 로고    scopus 로고
    • Activation of p42/p44 mitogen-activated protein kinases (MAPK) and p38 MAPK by tumor necrosis factor (TNF) is mediated through the death domain of the 55-kDa TNF receptor
    • Boone E., Vandevoorde V., De Wilde G., Haegeman G. Activation of p42/p44 mitogen-activated protein kinases (MAPK) and p38 MAPK by tumor necrosis factor (TNF) is mediated through the death domain of the 55-kDa TNF receptor. FEBS Lett. 441:1998;275-280.
    • (1998) FEBS Lett , vol.441 , pp. 275-280
    • Boone, E.1    Vandevoorde, V.2    De Wilde, G.3    Haegeman, G.4
  • 31
    • 0023724778 scopus 로고
    • IκB: A specific inhibitor of the NF-κB transcription factor
    • Baeuerle P.A., Baltimore D. IκB a specific inhibitor of the NF-κB transcription factor. Science. 242:1988;540-546.
    • (1988) Science , vol.242 , pp. 540-546
    • Baeuerle, P.A.1    Baltimore, D.2
  • 32
    • 0033596121 scopus 로고    scopus 로고
    • Activators and target genes of Rel/NF-κB transcription factors
    • Pahl H.L. Activators and target genes of Rel/NF-κB transcription factors. Oncogene. 18:1999;6853-6866.
    • (1999) Oncogene , vol.18 , pp. 6853-6866
    • Pahl, H.L.1
  • 33
    • 0033596126 scopus 로고    scopus 로고
    • Diverse agents act at multiple levels to inhibit the Rel/NF-κB signal transduction pathway
    • Epinat J.C., Gilmore T.D. Diverse agents act at multiple levels to inhibit the Rel/NF-κB signal transduction pathway. Oncogene. 18:1999;6896-6909.
    • (1999) Oncogene , vol.18 , pp. 6896-6909
    • Epinat, J.C.1    Gilmore, T.D.2
  • 34
    • 0032590061 scopus 로고    scopus 로고
    • Nuclear factor-κB/Rel proteins: A point of convergence of signalling pathways relevant in neuronal function and dysfunction
    • Grilli M., Memo M. Nuclear factor-κB/Rel proteins A point of convergence of signalling pathways relevant in neuronal function and dysfunction. Biochem Pharmacol. 57:1999;1-7.
    • (1999) Biochem Pharmacol , vol.57 , pp. 1-7
    • Grilli, M.1    Memo, M.2
  • 35
    • 0033595893 scopus 로고    scopus 로고
    • How NF-κB is activated: The role of the IκB kinase (IKK) complex
    • Karin M. How NF-κB is activated The role of the IκB kinase (IKK) complex. Oncogene. 18:1999;6867-6874.
    • (1999) Oncogene , vol.18 , pp. 6867-6874
    • Karin, M.1
  • 36
    • 0032939903 scopus 로고    scopus 로고
    • Multiple signals converging on NF-κB
    • Mercurio F., Manning A.M. Multiple signals converging on NF-κB. Curr Opin Cell Biol. 11:1999;226-232.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 226-232
    • Mercurio, F.1    Manning, A.M.2
  • 37
    • 0033607313 scopus 로고    scopus 로고
    • The NF-κB activation pathway: A paradigm in information transfer from membrane to nucleus
    • Rothwarf DM and Karin M, The NF-κB activation pathway: A paradigm in information transfer from membrane to nucleus. Science’s STKE, www.stke.org/cgi/content/full/OC_sigtrans 5: 1-16, 1999.
    • (1999) Science’s STKE , vol.5 , pp. 1-16
    • Rothwarf, D.M.1    Karin, M.2
  • 39
    • 0034175930 scopus 로고    scopus 로고
    • The IKK complex: An integrator of all signals that activate NF-κB
    • Israël A. The IKK complex An integrator of all signals that activate NF-κB. Trends Cell Biol. 10:2000;129-133.
    • (2000) Trends Cell Biol , vol.10 , pp. 129-133
    • Israël, A.1
  • 41
    • 0344222192 scopus 로고    scopus 로고
    • Sequential DNA damage-independent and -dependent activation of NF-κB by UV
    • Bender K., Gottlicher M., Whiteside S., Rahmsdorf H.J., Herrlich P. Sequential DNA damage-independent and -dependent activation of NF-κB by UV. EMBO J. 17:1998;5170-5181.
    • (1998) EMBO J , vol.17 , pp. 5170-5181
    • Bender, K.1    Gottlicher, M.2    Whiteside, S.3    Rahmsdorf, H.J.4    Herrlich, P.5
  • 42
    • 0032573165 scopus 로고    scopus 로고
    • Ionizing radiation and short wavelength UV activate NF-κB through two distinct mechanisms
    • Li N., Karin M. Ionizing radiation and short wavelength UV activate NF-κB through two distinct mechanisms. Proc Natl Acad Sci USA. 95:1998;13012-13017.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 13012-13017
    • Li, N.1    Karin, M.2
  • 43
    • 0033611544 scopus 로고    scopus 로고
    • TPL-2 kinase regulates the proteolysis of the NF-κB-inhibitory protein NF-κB1 p105
    • Belich M.P., Salmeron A., Johnston L.H., Ley S.C. TPL-2 kinase regulates the proteolysis of the NF-κB-inhibitory protein NF-κB1 p105. Nature. 397:1999;363-368.
    • (1999) Nature , vol.397 , pp. 363-368
    • Belich, M.P.1    Salmeron, A.2    Johnston, L.H.3    Ley, S.C.4
  • 44
    • 0033053617 scopus 로고    scopus 로고
    • Reactive oxygen intermediate-dependent NF-κB activation by interleukin-1-β requires 5-lipoxygenase or NADPH oxidase activity
    • Bonizzi G., Piette J., Schoonbroodt S., Greimers R., Havard L., Merville M.P., Bours V. Reactive oxygen intermediate-dependent NF-κB activation by interleukin-1-β requires 5-lipoxygenase or NADPH oxidase activity. Mol Cell Biol. 19:1999;1950-1960.
    • (1999) Mol Cell Biol , vol.19 , pp. 1950-1960
    • Bonizzi, G.1    Piette, J.2    Schoonbroodt, S.3    Greimers, R.4    Havard, L.5    Merville, M.P.6    Bours, V.7
  • 45
    • 0033485542 scopus 로고    scopus 로고
    • NF-κB activation by a signaling complex containing TRAF2, TANK and TBK1, a novel IKK-related kinase
    • Pomerantz J.L., Baltimore D. NF-κB activation by a signaling complex containing TRAF2, TANK and TBK1, a novel IKK-related kinase. EMBO J. 18:1999;6694-6704.
    • (1999) EMBO J , vol.18 , pp. 6694-6704
    • Pomerantz, J.L.1    Baltimore, D.2
  • 46
    • 0033623848 scopus 로고    scopus 로고
    • IKKε is part of a novel PMA-inducible IκB kinase complex
    • Peters R.T., Liao S.M., Maniatis T. IKKε is part of a novel PMA-inducible IκB kinase complex. Mol Cell. 5:2000;513.
    • (2000) Mol Cell , vol.5 , pp. 513
    • Peters, R.T.1    Liao, S.M.2    Maniatis, T.3
  • 47
    • 0029983730 scopus 로고    scopus 로고
    • The p38/RK mitogen-activated protein kinase pathway regulates interleukin-6 synthesis in response to tumour necrosis factor
    • Beyaert R., Cuenda A., Vanden Berghe W., Plaisance S., Lee J.C., Haegeman G., Cohen P., Fiers W. The p38/RK mitogen-activated protein kinase pathway regulates interleukin-6 synthesis in response to tumour necrosis factor. EMBO J. 15:1996;1914-1923.
    • (1996) EMBO J , vol.15 , pp. 1914-1923
    • Beyaert, R.1    Cuenda, A.2    Vanden Berghe, W.3    Plaisance, S.4    Lee, J.C.5    Haegeman, G.6    Cohen, P.7    Fiers, W.8
  • 48
    • 0028170265 scopus 로고
    • Activation of NF-κB in vivo is regulated by multiple phosphorylations
    • Naumann M., Scheidereit C. Activation of NF-κB in vivo is regulated by multiple phosphorylations. EMBO J. 13:1994;4597-4607.
    • (1994) EMBO J , vol.13 , pp. 4597-4607
    • Naumann, M.1    Scheidereit, C.2
  • 49
    • 0028151080 scopus 로고
    • NF-κB/Rel family members are physically associated phosphoproteins
    • Li C.C., Korner M., Ferris D.K., Chen E., Dai R.M., Longo D.L. NF-κB/Rel family members are physically associated phosphoproteins. Biochem J. 303:1994;499-506.
    • (1994) Biochem J , vol.303 , pp. 499-506
    • Li, C.C.1    Korner, M.2    Ferris, D.K.3    Chen, E.4    Dai, R.M.5    Longo, D.L.6
  • 50
    • 0028984263 scopus 로고
    • Tumor necrosis factor-α-dependent activation of a RelA homodimer in astrocytes. Increased phosphorylation of RelA and MAD-3 precede activation of RelA
    • Diehl J.A., Tong W., Sun G., Hannink M. Tumor necrosis factor-α-dependent activation of a RelA homodimer in astrocytes. Increased phosphorylation of RelA and MAD-3 precede activation of RelA. J Biol Chem. 270:1995;2703-2707.
    • (1995) J Biol Chem , vol.270 , pp. 2703-2707
    • Diehl, J.A.1    Tong, W.2    Sun, G.3    Hannink, M.4
  • 51
    • 0031437893 scopus 로고    scopus 로고
    • 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.K., Hagen H., Virca G.D. Activation of nuclear transcription factor NF-κB by interleukin-1 is accompanied by casein kinase II-mediated phosphorylation of the p65 subunit. J Biol Chem. 272:1997;32606-32612.
    • (1997) J Biol Chem , vol.272 , pp. 32606-32612
    • Bird, T.A.1    Schooley, K.2    Dower, S.K.3    Hagen, H.4    Virca, G.D.5
  • 52
    • 0032491485 scopus 로고    scopus 로고
    • Activation of nuclear factor-κB-dependent transcription by tumor necrosis factor-α is mediated through phosphorylation of RelA/p65 on serine 529
    • Wang D., Baldwin A.S. Activation of nuclear factor-κB-dependent transcription by tumor necrosis factor-α is mediated through phosphorylation of RelA/p65 on serine 529. J Biol Chem. 273:1998;29411-29416.
    • (1998) J Biol Chem , vol.273 , pp. 29411-29416
    • Wang, D.1    Baldwin, A.S.2
  • 53
    • 0032039076 scopus 로고    scopus 로고
    • Phosphorylation of NF-κB p65 by PKA stimulates transcriptional activity by promoting a novel bivalent interaction with the coactivator CBP/p300
    • Zhong H., Voll R.E., Ghosh S. Phosphorylation of NF-κB p65 by PKA stimulates transcriptional activity by promoting a novel bivalent interaction with the coactivator CBP/p300. Mol Cell. 1:1998;661-671.
    • (1998) Mol Cell , vol.1 , pp. 661-671
    • Zhong, H.1    Voll, R.E.2    Ghosh, S.3
  • 54
    • 0033531795 scopus 로고    scopus 로고
    • Regulation of NF-κB RelA phosphorylation and transcriptional activity by p21(ras) and protein kinase C-ζ In primary endothelial cells
    • Anrather J., Csizmadia V., Soares M.P., Winkler H. Regulation of NF-κB RelA phosphorylation and transcriptional activity by p21(ras) and protein kinase C-ζ in primary endothelial cells. J Biol Chem. 274:1999;13594-13603.
    • (1999) J Biol Chem , vol.274 , pp. 13594-13603
    • Anrather, J.1    Csizmadia, V.2    Soares, M.P.3    Winkler, H.4
  • 55
    • 0033543545 scopus 로고    scopus 로고
    • Inhibition of interleukin-1-stimulated NF-κB RelA/p65 phosphorylation by mesalamine is accompanied by decreased transcriptional activity
    • Egan L.J., Mays D.C., Huntoon C.J., Bell M.P., Pike M.G., Sandborn W.J., Lipsky J.J., McKean D.J. Inhibition of interleukin-1-stimulated NF-κB RelA/p65 phosphorylation by mesalamine is accompanied by decreased transcriptional activity. J Biol Chem. 274:1999;26448-26453.
    • (1999) J Biol Chem , vol.274 , pp. 26448-26453
    • Egan, L.J.1    Mays, D.C.2    Huntoon, C.J.3    Bell, M.P.4    Pike, M.G.5    Sandborn, W.J.6    Lipsky, J.J.7    McKean, D.J.8
  • 56
    • 0032589462 scopus 로고    scopus 로고
    • IκB kinases phosphorylate NF-κB p65 subunit on serine 536 in the transactivation domain
    • Sakurai H., Chiba H., Miyoshi H., Sugita T., Toriumi W. IκB kinases phosphorylate NF-κB p65 subunit on serine 536 in the transactivation domain. J Biol Chem. 274:1999;30353-30356.
    • (1999) J Biol Chem , vol.274 , pp. 30353-30356
    • Sakurai, H.1    Chiba, H.2    Miyoshi, H.3    Sugita, T.4    Toriumi, W.5
  • 57
    • 0033579490 scopus 로고    scopus 로고
    • Chromium(VI) inhibits the transcriptional activity of nuclear factor-κB by decreasing the interaction of p65 with cAMP-responsive element-binding protein-binding protein
    • Shumilla J.A., Broderick R.J., Wang Y., Barchowsky A. Chromium(VI) inhibits the transcriptional activity of nuclear factor-κB by decreasing the interaction of p65 with cAMP-responsive element-binding protein-binding protein. J Biol Chem. 274:1999;36207-36212.
    • (1999) J Biol Chem , vol.274 , pp. 36207-36212
    • Shumilla, J.A.1    Broderick, R.J.2    Wang, Y.3    Barchowsky, A.4
  • 58
    • 0033038491 scopus 로고    scopus 로고
    • Activation of phosphatidylinositol 3-kinase in response to interleukin-1 leads to phosphorylation and activation of the NF-κB p65/RelA subunit
    • Sizemore N., Leung S., Stark G.R. Activation of phosphatidylinositol 3-kinase in response to interleukin-1 leads to phosphorylation and activation of the NF-κB p65/RelA subunit. Mol Cell Biol. 19:1999;4798-4805.
    • (1999) Mol Cell Biol , vol.19 , pp. 4798-4805
    • Sizemore, N.1    Leung, S.2    Stark, G.R.3
  • 59
    • 0033961280 scopus 로고    scopus 로고
    • Akt suppresses apoptosis by stimulating the transactivation potential of the RelA/p65 subunit of NF-κB
    • Madrid L.V., Wang C.Y., Guttridge D.C., Schottelius A.J., Baldwin A.S., Mayo M.W. Akt suppresses apoptosis by stimulating the transactivation potential of the RelA/p65 subunit of NF-κB. Mol Cell Biol. 20:2000;1626-1638.
    • (2000) Mol Cell Biol , vol.20 , pp. 1626-1638
    • Madrid, L.V.1    Wang, C.Y.2    Guttridge, D.C.3    Schottelius, A.J.4    Baldwin, A.S.5    Mayo, M.W.6
  • 60
    • 0033105577 scopus 로고    scopus 로고
    • Nuclear import of the Drosophila Rel protein Dorsal is regulated by phosphorylation
    • Drier E.A., Huang L.H., Steward R. Nuclear import of the Drosophila Rel protein Dorsal is regulated by phosphorylation. Genes Dev. 13:1999;556-568.
    • (1999) Genes Dev , vol.13 , pp. 556-568
    • Drier, E.A.1    Huang, L.H.2    Steward, R.3
  • 61
    • 0032217268 scopus 로고    scopus 로고
    • The crystal structure of the IκB-α/NF-κB complex reveals mechanisms of NF-κB inactivation
    • Huxford T., Huang D.B., Malek S., Ghosh G. The crystal structure of the IκB-α/NF-κB complex reveals mechanisms of NF-κB inactivation. Cell. 95:1998;759-770.
    • (1998) Cell , vol.95 , pp. 759-770
    • Huxford, T.1    Huang, D.B.2    Malek, S.3    Ghosh, G.4
  • 62
    • 0032217264 scopus 로고    scopus 로고
    • Structure of an IκB-α/NF-κB complex
    • Jacobs M.D., Harrison S.C. Structure of an IκB-α/NF-κB complex. Cell. 95:1998;749-758.
    • (1998) Cell , vol.95 , pp. 749-758
    • Jacobs, M.D.1    Harrison, S.C.2
  • 63
    • 0032556894 scopus 로고    scopus 로고
    • Crystal structure of p50/p65 heterodimer of transcription factor NF-κB bound to DNA
    • Chen F.E., Huang D.B., Chen Y.Q., Ghosh G. Crystal structure of p50/p65 heterodimer of transcription factor NF-κB bound to DNA. Nature. 391:1998;410-413.
    • (1998) Nature , vol.391 , pp. 410-413
    • Chen, F.E.1    Huang, D.B.2    Chen, Y.Q.3    Ghosh, G.4
  • 64
    • 0033555039 scopus 로고    scopus 로고
    • A firm hand on NF-κB: Structures of the IκB-α-NF-κB complex
    • Cramer P., Muller C.W. A firm hand on NF-κB Structures of the IκB-α-NF-κB complex. Structure Fold Des. 7:1999;R1-R6.
    • (1999) Structure Fold des , vol.7 , pp. 1-R6
    • Cramer, P.1    Muller, C.W.2
  • 65
    • 0031835267 scopus 로고    scopus 로고
    • Co-activators and co-repressors in the integration of transcriptional responses
    • Torchia J., Glass C., Rosenfeld M.G. Co-activators and co-repressors in the integration of transcriptional responses. Curr Opin Cell Biol. 10:1998;373-383.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 373-383
    • Torchia, J.1    Glass, C.2    Rosenfeld, M.G.3
  • 66
    • 0032142918 scopus 로고    scopus 로고
    • Roles of histone acetyltransferases and deacetylases in gene regulation
    • Kuo M.H., Allis C.D. Roles of histone acetyltransferases and deacetylases in gene regulation. Bioessays. 20:1998;615-626.
    • (1998) Bioessays , vol.20 , pp. 615-626
    • Kuo, M.H.1    Allis, C.D.2
  • 67
    • 0033153358 scopus 로고    scopus 로고
    • Gene activation by histone and factor acetyltransferases
    • Berger S.L. Gene activation by histone and factor acetyltransferases. Curr Opin Cell Biol. 11:1999;336-341.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 336-341
    • Berger, S.L.1
  • 69
    • 0032518443 scopus 로고    scopus 로고
    • Chromatin and transcription - how transcription factors battle with a repressive chromatin environment
    • Gregory P.D., Horz W. Chromatin and transcription - how transcription factors battle with a repressive chromatin environment. Eur J Biochem. 251:1998;9-18.
    • (1998) Eur J Biochem , vol.251 , pp. 9-18
    • Gregory, P.D.1    Horz, W.2
  • 70
    • 0032488855 scopus 로고    scopus 로고
    • Eukaryotic transcription: An interlaced network of transcription factors and chromatin-modifying machines
    • Kadonaga J.T. Eukaryotic transcription An interlaced network of transcription factors and chromatin-modifying machines. Cell. 92:1998;307-313.
    • (1998) Cell , vol.92 , pp. 307-313
    • Kadonaga, J.T.1
  • 71
    • 0033080794 scopus 로고    scopus 로고
    • Chromatin disruption and modification
    • Wolffe A.P., Hayes J.J. Chromatin disruption and modification. Nucleic Acids Res. 27:1999;711-720.
    • (1999) Nucleic Acids Res , vol.27 , pp. 711-720
    • Wolffe, A.P.1    Hayes, J.J.2
  • 72
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl B.D., Allis C.D. The language of covalent histone modifications. Nature. 403:2000;41-45.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 73
    • 0031604766 scopus 로고    scopus 로고
    • Recruitment of CBP/p300 by the IFNβ enhanceosome is required for synergistic activation of transcription
    • Merika M., Williams A.J., Chen G., Collins T., Thanos D. Recruitment of CBP/p300 by the IFNβ enhanceosome is required for synergistic activation of transcription. Mol Cell. 1:1998;277-287.
    • (1998) Mol Cell , vol.1 , pp. 277-287
    • Merika, M.1    Williams, A.J.2    Chen, G.3    Collins, T.4    Thanos, D.5
  • 74
    • 0032525913 scopus 로고    scopus 로고
    • Cell cycle regulation of the transcriptional coactivators p300 and CREB binding protein
    • Snowden A.W., Perkins N.D. Cell cycle regulation of the transcriptional coactivators p300 and CREB binding protein. Biochem Pharmacol. 55:1998;1947-1954.
    • (1998) Biochem Pharmacol , vol.55 , pp. 1947-1954
    • Snowden, A.W.1    Perkins, N.D.2
  • 76
    • 0033588138 scopus 로고    scopus 로고
    • How chromatin changes its shape
    • Hagmann M. How chromatin changes its shape. Science. 285:1999;1200-1201.
    • (1999) Science , vol.285 , pp. 1200-1201
    • Hagmann, M.1
  • 77
    • 0033166349 scopus 로고    scopus 로고
    • JIL-1: A novel chromosomal tandem kinase implicated in transcriptional regulation in Drosophila
    • Jin Y., Wang Y., Walker D.L., Dong H., Conley C., Johansen J., Johansen K.M. JIL-1 A novel chromosomal tandem kinase implicated in transcriptional regulation in Drosophila. Mol Cell. 4:1999;129-135.
    • (1999) Mol Cell , vol.4 , pp. 129-135
    • Jin, Y.1    Wang, Y.2    Walker, D.L.3    Dong, H.4    Conley, C.5    Johansen, J.6    Johansen, K.M.7
  • 78
    • 0032971444 scopus 로고    scopus 로고
    • Virus infection leads to localized hyperacetylation of histones H3 and H4 at the IFNβ promoter
    • Parekh B.S., Maniatis T. Virus infection leads to localized hyperacetylation of histones H3 and H4 at the IFNβ promoter. Mol Cell. 3:1999;125-129.
    • (1999) Mol Cell , vol.3 , pp. 125-129
    • Parekh, B.S.1    Maniatis, T.2
  • 79
    • 0033977889 scopus 로고    scopus 로고
    • The phosphorylation status of a cyclic AMP-responsive activator is modulated via a chromatin-dependent mechanism
    • Michael L.F., Asahara H., Shulman A.I., Kraus W.L., Montminy M. The phosphorylation status of a cyclic AMP-responsive activator is modulated via a chromatin-dependent mechanism. Mol Cell Biol. 20:2000;1596-1603.
    • (2000) Mol Cell Biol , vol.20 , pp. 1596-1603
    • Michael, L.F.1    Asahara, H.2    Shulman, A.I.3    Kraus, W.L.4    Montminy, M.5
  • 80
    • 0034695456 scopus 로고    scopus 로고
    • Rad6-dependent ubiquitination of histone H2B in yeast
    • Robzyk K., Recht J., Osley M.A. Rad6-dependent ubiquitination of histone H2B in yeast. Science. 287:2000;501-504.
    • (2000) Science , vol.287 , pp. 501-504
    • Robzyk, K.1    Recht, J.2    Osley, M.A.3
  • 81
    • 0032171040 scopus 로고    scopus 로고
    • Chromatin remodeling: A marriage between two families?
    • Pollard K.J., Peterson C.L. Chromatin remodeling A marriage between two families? Bioessays. 20:1998;771-780.
    • (1998) Bioessays , vol.20 , pp. 771-780
    • Pollard, K.J.1    Peterson, C.L.2
  • 82
    • 0033118984 scopus 로고    scopus 로고
    • RNA polymerase II as a control panel for multiple coactivator complexes
    • Hampsey M., Reinberg D. RNA polymerase II as a control panel for multiple coactivator complexes. Curr Opin Genet Dev. 9:1999;132-139.
    • (1999) Curr Opin Genet Dev , vol.9 , pp. 132-139
    • Hampsey, M.1    Reinberg, D.2
  • 83
    • 0033119021 scopus 로고    scopus 로고
    • Chromatin-modifying and -remodeling complexes
    • Kornberg R.D., Lorch Y. Chromatin-modifying and -remodeling complexes. Curr Opin Genet Dev. 9:1999;148-151.
    • (1999) Curr Opin Genet Dev , vol.9 , pp. 148-151
    • Kornberg, R.D.1    Lorch, Y.2
  • 85
    • 0032076229 scopus 로고    scopus 로고
    • Conjunction dysfunction: CBP/p300 in human disease
    • Giles R.H., Peters D.J., Breuning M.H. Conjunction dysfunction CBP/p300 in human disease. Trends Genet. 14:1998;178-183.
    • (1998) Trends Genet , vol.14 , pp. 178-183
    • Giles, R.H.1    Peters, D.J.2    Breuning, M.H.3
  • 87
    • 0033118944 scopus 로고    scopus 로고
    • Modifying chromatin and concepts of cancer
    • Jacobson S., Pillus L. Modifying chromatin and concepts of cancer. Curr Opin Genet Dev. 9:1999;175-184.
    • (1999) Curr Opin Genet Dev , vol.9 , pp. 175-184
    • Jacobson, S.1    Pillus, L.2
  • 88
    • 0033000990 scopus 로고    scopus 로고
    • Histone acetylases and deacetylases in cell proliferation
    • Kouzarides T. Histone acetylases and deacetylases in cell proliferation. Curr Opin Genet Dev. 9:1999;40-48.
    • (1999) Curr Opin Genet Dev , vol.9 , pp. 40-48
    • Kouzarides, T.1
  • 89
    • 0034141972 scopus 로고    scopus 로고
    • CREB-binding protein and p300: Molecular integrators of hematopoietic transcription
    • Blobel G.A. CREB-binding protein and p300 Molecular integrators of hematopoietic transcription. Blood. 95:2000;745-755.
    • (2000) Blood , vol.95 , pp. 745-755
    • Blobel, G.A.1
  • 91
    • 0034719683 scopus 로고    scopus 로고
    • The PCAF acetylase complex as a potential tumor suppressor
    • Schiltz R.L., Nakatani Y. The PCAF acetylase complex as a potential tumor suppressor. Biochim Biophys Acta. 1470:2000;M37-M53.
    • (2000) Biochim Biophys Acta , vol.1470 , pp. 37-M53
    • Schiltz, R.L.1    Nakatani, Y.2
  • 93
    • 0032230335 scopus 로고    scopus 로고
    • Signaling by tyrosine kinases negatively regulates the interaction between transcription factors and SMRT (silencing mediator of retinoic acid and thyroid hormone receptor) corepressor
    • Hong S.H., Wong C.W., Privalsky M.L. Signaling by tyrosine kinases negatively regulates the interaction between transcription factors and SMRT (silencing mediator of retinoic acid and thyroid hormone receptor) corepressor. Mol Endocrinol. 12:1998;1161-1171.
    • (1998) Mol Endocrinol , vol.12 , pp. 1161-1171
    • Hong, S.H.1    Wong, C.W.2    Privalsky, M.L.3
  • 94
    • 0032554825 scopus 로고    scopus 로고
    • Distinct roles of the co-activators p300 and CBP in retinoic-acid-induced F9-cell differentiation
    • Kawasaki H., Eckner R., Yao T.P., Taira K., Chiu R., Livingston D.M., Yokoyama K.K. Distinct roles of the co-activators p300 and CBP in retinoic-acid-induced F9-cell differentiation. Nature. 393:1998;284-289.
    • (1998) Nature , vol.393 , pp. 284-289
    • Kawasaki, H.1    Eckner, R.2    Yao, T.P.3    Taira, K.4    Chiu, R.5    Livingston, D.M.6    Yokoyama, K.K.7
  • 97
    • 0032909655 scopus 로고    scopus 로고
    • Activation domain-specific and general transcription stimulation by native histone acetyltransferase complexes
    • Ikeda K., Steger D.J., Eberharter A., Workman J.L. Activation domain-specific and general transcription stimulation by native histone acetyltransferase complexes. Mol Cell Biol. 19:1999;855-863.
    • (1999) Mol Cell Biol , vol.19 , pp. 855-863
    • Ikeda, K.1    Steger, D.J.2    Eberharter, A.3    Workman, J.L.4
  • 99
    • 0029919356 scopus 로고    scopus 로고
    • Transcriptional activation and chromatin remodeling of the HIV-1 promoter in response to histone acetylation
    • Van Lint C., Emiliani S., Ott M., Verdin E. Transcriptional activation and chromatin remodeling of the HIV-1 promoter in response to histone acetylation. EMBO J. 15:1996;1112-1120.
    • (1996) EMBO J , vol.15 , pp. 1112-1120
    • Van Lint, C.1    Emiliani, S.2    Ott, M.3    Verdin, E.4
  • 100
    • 0031455415 scopus 로고    scopus 로고
    • Histone acetyltransferases regulate HIV-1 enhancer activity in vitro
    • Sheridan P.L., Mayall T.P., Verdin E., Jones K.A. Histone acetyltransferases regulate HIV-1 enhancer activity in vitro. Genes Dev. 11:1997;3327-3340.
    • (1997) Genes Dev , vol.11 , pp. 3327-3340
    • Sheridan, P.L.1    Mayall, T.P.2    Verdin, E.3    Jones, K.A.4
  • 101
    • 0031942998 scopus 로고    scopus 로고
    • Transcriptional activation of the integrated chromatin-associated human immunodeficiency virus type 1 promoter
    • El Kharroubi A., Piras G., Zensen R., Martin M.A. Transcriptional activation of the integrated chromatin-associated human immunodeficiency virus type 1 promoter. Mol Cell Biol. 18:1998;2535-2544.
    • (1998) Mol Cell Biol , vol.18 , pp. 2535-2544
    • El Kharroubi, A.1    Piras, G.2    Zensen, R.3    Martin, M.A.4
  • 103
    • 0344936739 scopus 로고    scopus 로고
    • Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB. A model for activator:coactivator interactions
    • Radhakrishnan I., Perez-Alvarado G.C., Parker D., Dyson H.J., Montminy M.R., Wright P.E. Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB. A model for activator:coactivator interactions. Cell. 91:1998;741-752.
    • (1998) Cell , vol.91 , pp. 741-752
    • Radhakrishnan, I.1    Perez-Alvarado, G.C.2    Parker, D.3    Dyson, H.J.4    Montminy, M.R.5    Wright, P.E.6
  • 104
    • 0031255138 scopus 로고    scopus 로고
    • Drosophila CBP is required for dorsal-dependent twist gene expression
    • Akimaru H., Hou-Dx, Ishii S. Drosophila CBP is required for dorsal-dependent twist gene expression. Nat Genet. 17:1997;211-214.
    • (1997) Nat Genet , vol.17 , pp. 211-214
    • Akimaru, H.1    Hou-Dx2    Ishii, S.3
  • 106
    • 0030614504 scopus 로고    scopus 로고
    • Regulation of NF-κB by cyclin-dependent kinases associated with the p300 coactivator
    • Perkins N.D., Felzien L.K., Betts J.C., Leung K., Beach D.H., Nabel G.J. Regulation of NF-κB by cyclin-dependent kinases associated with the p300 coactivator. Science. 275:1997;523-527.
    • (1997) Science , vol.275 , pp. 523-527
    • Perkins, N.D.1    Felzien, L.K.2    Betts, J.C.3    Leung, K.4    Beach, D.H.5    Nabel, G.J.6
  • 107
    • 0031604766 scopus 로고    scopus 로고
    • Recruitment of CBP/p300 by the IFNβ enhanceosome is required for synergistic activation of transcription
    • Merika M., Williams A.J., Chen G., Collins T., Thanos D. Recruitment of CBP/p300 by the IFNβ enhanceosome is required for synergistic activation of transcription. Mol Cell. 1:1998;277-287.
    • (1998) Mol Cell , vol.1 , pp. 277-287
    • Merika, M.1    Williams, A.J.2    Chen, G.3    Collins, T.4    Thanos, D.5
  • 108
  • 109
    • 0029656068 scopus 로고    scopus 로고
    • The interferon-inducible p202 protein as a modulator of transcription: Inhibition of NF-κB, c-Fos, and c-Jun activities
    • Min W., Ghosh S., Lengyel P. The interferon-inducible p202 protein as a modulator of transcription Inhibition of NF-κB, c-Fos, and c-Jun activities. Mol Cell Biol. 16:1996;359-368.
    • (1996) Mol Cell Biol , vol.16 , pp. 359-368
    • Min, W.1    Ghosh, S.2    Lengyel, P.3
  • 111
    • 0032080237 scopus 로고    scopus 로고
    • Steroid receptor coactivator-1 interacts with the p50 subunit and coactivates nuclear factor κb-mediated transactivations
    • Na S.Y., Lee S.K., Han S.J., Choi H.S., Im S.Y., Lee J.W. Steroid receptor coactivator-1 interacts with the p50 subunit and coactivates nuclear factor κB-mediated transactivations. J Biol Chem. 273:1998;10831-10834.
    • (1998) J Biol Chem , vol.273 , pp. 10831-10834
    • Na, S.Y.1    Lee, S.K.2    Han, S.J.3    Choi, H.S.4    Im, S.Y.5    Lee, J.W.6
  • 112
    • 0031795513 scopus 로고    scopus 로고
    • Dorsal-mediated repression requires the formation of a multiprotein repression complex at the ventral silencer
    • Valentine S.A., Chen G., Shandala T., Fernandez J., Mische S., Saint R., Courey A.J. Dorsal-mediated repression requires the formation of a multiprotein repression complex at the ventral silencer. Mol Cell Biol. 18:1998;6584-6594.
    • (1998) Mol Cell Biol , vol.18 , pp. 6584-6594
    • Valentine, S.A.1    Chen, G.2    Shandala, T.3    Fernandez, J.4    Mische, S.5    Saint, R.6    Courey, A.J.7
  • 114
    • 0033199348 scopus 로고    scopus 로고
    • NF-κB p105 is a target of IκB kinases and controls signal induction of Bcl-3-p50 complexes
    • Heissmeyer V., Krappmann D., Wulczyn F.G., Scheidereit C. NF-κB p105 is a target of IκB kinases and controls signal induction of Bcl-3-p50 complexes. EMBO J. 18:1999;4766-4778.
    • (1999) EMBO J , vol.18 , pp. 4766-4778
    • Heissmeyer, V.1    Krappmann, D.2    Wulczyn, F.G.3    Scheidereit, C.4
  • 115
    • 0040368298 scopus 로고    scopus 로고
    • Composite co-activator ARC mediates chromatin-directed transcriptional activation
    • Naar A.M., Beaurang P.A., Zhou S., Abraham S., Solomon W., Tjian R. Composite co-activator ARC mediates chromatin-directed transcriptional activation. Nature. 398:1999;828-832.
    • (1999) Nature , vol.398 , pp. 828-832
    • Naar, A.M.1    Beaurang, P.A.2    Zhou, S.3    Abraham, S.4    Solomon, W.5    Tjian, R.6
  • 116
    • 0034635524 scopus 로고    scopus 로고
    • Inhibition of nuclear factor-κB-mediated transcription by association with the amino-terminal enhancer of split, a groucho-related protein lacking WD40 repeats
    • Tetsuka T., Uranishi H., Imai H., Ono T., Sonta S., Takahashi N., Asamitsu K., Okamoto T. Inhibition of nuclear factor-κB-mediated transcription by association with the amino-terminal enhancer of split, a groucho-related protein lacking WD40 repeats. J Biol Chem. 275:2000;4383-4390.
    • (2000) J Biol Chem , vol.275 , pp. 4383-4390
    • Tetsuka, T.1    Uranishi, H.2    Imai, H.3    Ono, T.4    Sonta, S.5    Takahashi, N.6    Asamitsu, K.7    Okamoto, T.8
  • 117
    • 0033958683 scopus 로고    scopus 로고
    • Tumor suppression and sensitization to tumor necrosis factor α-induced apoptosis by an interferon-inducible protein, p202, in breast cancer cells
    • Wen Y., Yan D.H., Spohn B., Deng J., Lin S.Y., Hung M.C. Tumor suppression and sensitization to tumor necrosis factor α-induced apoptosis by an interferon-inducible protein, p202, in breast cancer cells. Cancer Res. 60:2000;42-46.
    • (2000) Cancer Res , vol.60 , pp. 42-46
    • Wen, Y.1    Yan, D.H.2    Spohn, B.3    Deng, J.4    Lin, S.Y.5    Hung, M.C.6
  • 118
    • 0034650893 scopus 로고    scopus 로고
    • The coregulator exchange in transcriptional functions of nuclear receptors
    • Glass C.K., Rosenfeld M.G. The coregulator exchange in transcriptional functions of nuclear receptors. Genes Dev. 14:2000;121-141.
    • (2000) Genes Dev , vol.14 , pp. 121-141
    • Glass, C.K.1    Rosenfeld, M.G.2
  • 120
    • 0034654011 scopus 로고    scopus 로고
    • Acetylation: A regulatory modification to rival phosphorylation?
    • Kouzarides T. Acetylation A regulatory modification to rival phosphorylation? EMBO J. 19:2000;1176-1179.
    • (2000) EMBO J , vol.19 , pp. 1176-1179
    • Kouzarides, T.1
  • 121
    • 0032186185 scopus 로고    scopus 로고
    • Acetylation of HMG I(Y) by CBP turns off IFNβ expression by disrupting the enhanceosome
    • Munshi N., Merika M., Yie J., Senger K., Chen G., Thanos D. Acetylation of HMG I(Y) by CBP turns off IFNβ expression by disrupting the enhanceosome. Mol Cell. 2:1998;457-468.
    • (1998) Mol Cell , vol.2 , pp. 457-468
    • Munshi, N.1    Merika, M.2    Yie, J.3    Senger, K.4    Chen, G.5    Thanos, D.6
  • 122
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • Gu W., Roeder R.G. Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell. 90:1997;595-606.
    • (1997) Cell , vol.90 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 123
    • 0030796349 scopus 로고    scopus 로고
    • Induction of caspase-3 protease activity and apoptosis by butyrate and trichostatin A (inhibitors of histone deacetylase): Dependence on protein synthesis and synergy with a mitochrondrial cytochrome c-dependent pathway
    • Medina V., Edmonds B., Young G.P., James R., Appleton S., Zalewski P.D. Induction of caspase-3 protease activity and apoptosis by butyrate and trichostatin A (inhibitors of histone deacetylase) Dependence on protein synthesis and synergy with a mitochrondrial cytochrome c-dependent pathway. Cancer Res. 57:1997;3697-3707.
    • (1997) Cancer Res , vol.57 , pp. 3697-3707
    • Medina, V.1    Edmonds, B.2    Young, G.P.3    James, R.4    Appleton, S.5    Zalewski, P.D.6
  • 124
    • 0032574859 scopus 로고    scopus 로고
    • Methylation meets acetylation
    • Bestor T.H. Methylation meets acetylation. Nature. 393:1998;311-389.
    • (1998) Nature , vol.393 , pp. 311-389
    • Bestor, T.H.1
  • 126
    • 0032574977 scopus 로고    scopus 로고
    • Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex
    • Nan X., Ng H.H., Johnson C.A., Laherty C.D., Turner B.M., Eisenman R.N., Bird A. Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex. Nature. 393:1998;386-389.
    • (1998) Nature , vol.393 , pp. 386-389
    • Nan, X.1    Ng, H.H.2    Johnson, C.A.3    Laherty, C.D.4    Turner, B.M.5    Eisenman, R.N.6    Bird, A.7
  • 127
    • 0033988813 scopus 로고    scopus 로고
    • DNA methyltransferase Dnmt1 associates with histone deacetylase activity
    • Fuks F., Burgers W.A., Brehm A., Hughes-Davies L., Kouzarides T. DNA methyltransferase Dnmt1 associates with histone deacetylase activity. Nat Genet. 24:2000;88-91.
    • (2000) Nat Genet , vol.24 , pp. 88-91
    • Fuks, F.1    Burgers, W.A.2    Brehm, A.3    Hughes-Davies, L.4    Kouzarides, T.5
  • 128
    • 0032549013 scopus 로고    scopus 로고
    • Activation of SRF-regulated chromosomal templates by rho-family GTPases requires a signal that also induces H4 hyperacetylation
    • Alberts A.S., Geneste O., Treisman R. Activation of SRF-regulated chromosomal templates by rho-family GTPases requires a signal that also induces H4 hyperacetylation. Cell. 92:1998;475-487.
    • (1998) Cell , vol.92 , pp. 475-487
    • Alberts, A.S.1    Geneste, O.2    Treisman, R.3
  • 129
    • 0032933432 scopus 로고    scopus 로고
    • Cooperation between phosphorylation and acetylation processes in transcriptional control
    • Espinos E., Le Van Thai A., Pomies C., Weber M.J. Cooperation between phosphorylation and acetylation processes in transcriptional control. Mol Cell Biol. 19:1999;3474-3484.
    • (1999) Mol Cell Biol , vol.19 , pp. 3474-3484
    • Espinos, E.1    Le Van Thai, A.2    Pomies, C.3    Weber, M.J.4
  • 130
    • 0034176006 scopus 로고    scopus 로고
    • Butyrate-induced erythroid differentiation of human K562 leukemia cells involves inhibition of ERK and activation of p38 MAP kinase pathways
    • Witt O., Sand K., Pekrun A. Butyrate-induced erythroid differentiation of human K562 leukemia cells involves inhibition of ERK and activation of p38 MAP kinase pathways. Blood. 95:2000;2391-2396.
    • (2000) Blood , vol.95 , pp. 2391-2396
    • Witt, O.1    Sand, K.2    Pekrun, A.3
  • 131
    • 0032698069 scopus 로고    scopus 로고
    • The p38 mitogen-activated protein kinase is required for NF-κB-dependent gene expression. The role of TATA-binding protein (TBP)
    • Carter A.B., Knudtson K.L., Monick M.M., Hunninghake G.W. The p38 mitogen-activated protein kinase is required for NF-κB-dependent gene expression. The role of TATA-binding protein (TBP). J Biol Chem. 274:1999;30858-30863.
    • (1999) J Biol Chem , vol.274 , pp. 30858-30863
    • Carter, A.B.1    Knudtson, K.L.2    Monick, M.M.3    Hunninghake, G.W.4
  • 134
    • 0032483380 scopus 로고    scopus 로고
    • CBP: A signal-regulated transcriptional coactivator controlled by nuclear calcium and CaM kinase IV
    • Chawla S., Hardingham G.E., Quinn D.R., Bading H. CBP A signal-regulated transcriptional coactivator controlled by nuclear calcium and CaM kinase IV. Science. 281:1998;1505-1509.
    • (1998) Science , vol.281 , pp. 1505-1509
    • Chawla, S.1    Hardingham, G.E.2    Quinn, D.R.3    Bading, H.4
  • 135
    • 0032484204 scopus 로고    scopus 로고
    • Nerve growth factor up-regulates the transcriptional activity of CBP through activation of the p42/p44(MAPK) cascade
    • Liu Y.Z., Chrivia J.C., Latchman D.S. Nerve growth factor up-regulates the transcriptional activity of CBP through activation of the p42/p44(MAPK) cascade. J Biol Chem. 273:1998;32400-32407.
    • (1998) J Biol Chem , vol.273 , pp. 32400-32407
    • Liu, Y.Z.1    Chrivia, J.C.2    Latchman, D.S.3
  • 136
    • 0032726061 scopus 로고    scopus 로고
    • CREB-independent regulation by CBP is a novel mechanism of human growth hormone gene expression
    • Cohen L.E., Hashimoto Y., Zanger K., Wondisford F., Radovick S. CREB-independent regulation by CBP is a novel mechanism of human growth hormone gene expression. J Clin Invest. 104:1999;1123-1130.
    • (1999) J Clin Invest , vol.104 , pp. 1123-1130
    • Cohen, L.E.1    Hashimoto, Y.2    Zanger, K.3    Wondisford, F.4    Radovick, S.5
  • 137
    • 0033606042 scopus 로고    scopus 로고
    • CBP associates with the p42/p44 MAPK enzymes and is phosphorylated following NGF treatment
    • Liu Y.Z., Thomas N.S., Latchman D.S. CBP associates with the p42/p44 MAPK enzymes and is phosphorylated following NGF treatment. Neuroreport. 10:1999;1239-1243.
    • (1999) Neuroreport , vol.10 , pp. 1239-1243
    • Liu, Y.Z.1    Thomas, N.S.2    Latchman, D.S.3
  • 138
    • 0032530154 scopus 로고    scopus 로고
    • Mitotic inactivation of a human SWI/SNF chromatin remodeling complex
    • Sif S., Stukenberg P.T., Kirschner M.W., Kingston R.E. Mitotic inactivation of a human SWI/SNF chromatin remodeling complex. Genes Dev. 12:1998;2842-2851.
    • (1998) Genes Dev , vol.12 , pp. 2842-2851
    • Sif, S.1    Stukenberg, P.T.2    Kirschner, M.W.3    Kingston, R.E.4
  • 139
    • 0033019307 scopus 로고    scopus 로고
    • The histone acetylase PCAF is a phorbol-ester-inducible coactivator of the IRF family that confers enhanced interferon responsiveness
    • Masumi A., Wang I.M., Lefebvre B., Yang X.J., Nakatani Y., Ozato K. The histone acetylase PCAF is a phorbol-ester-inducible coactivator of the IRF family that confers enhanced interferon responsiveness. Mol Cell Biol. 19:1999;1810-1820.
    • (1999) Mol Cell Biol , vol.19 , pp. 1810-1820
    • Masumi, A.1    Wang, I.M.2    Lefebvre, B.3    Yang, X.J.4    Nakatani, Y.5    Ozato, K.6
  • 142
    • 0033113010 scopus 로고    scopus 로고
    • MAP kinase-mediated signalling to nucleosomes and immediate-early gene induction
    • Thomson S., Mahadevan L.C., Clayton A.L. MAP kinase-mediated signalling to nucleosomes and immediate-early gene induction. Semin Cell Dev Biol. 10:1999;205-214.
    • (1999) Semin Cell Dev Biol , vol.10 , pp. 205-214
    • Thomson, S.1    Mahadevan, L.C.2    Clayton, A.L.3
  • 143
    • 0032555283 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases enhance long-range activation by the β-globin locus control region
    • Versaw W.K., Blank V., Andrews N.M., Bresnick E.H. Mitogen-activated protein kinases enhance long-range activation by the β-globin locus control region. Proc Natl Acad Sci USA. 95:1998;8756-8760.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 8756-8760
    • Versaw, W.K.1    Blank, V.2    Andrews, N.M.3    Bresnick, E.H.4
  • 144
    • 0033588993 scopus 로고    scopus 로고
    • Regulation of p21(cip1) expression by growth factors and the extracellular matrix reveals a role for transient ERK activity in G1 phase
    • Bottazzi M.E., Zhu X., Bohmer R.M., Assoian R.K. Regulation of p21(cip1) expression by growth factors and the extracellular matrix reveals a role for transient ERK activity in G1 phase. J Cell Biol. 146:1999;1255-1264.
    • (1999) J Cell Biol , vol.146 , pp. 1255-1264
    • Bottazzi, M.E.1    Zhu, X.2    Bohmer, R.M.3    Assoian, R.K.4
  • 145
    • 0033109313 scopus 로고    scopus 로고
    • Histone acetylation in signal transduction by growth regulatory signals
    • Magnaghi-Jaulin L., Ait-Si-Ali S., Harel-Bellan A. Histone acetylation in signal transduction by growth regulatory signals. Semin Cell Dev Biol. 10:1999;197-203.
    • (1999) Semin Cell Dev Biol , vol.10 , pp. 197-203
    • Magnaghi-Jaulin, L.1    Ait-Si-Ali, S.2    Harel-Bellan, A.3
  • 146
    • 0031028381 scopus 로고    scopus 로고
    • Cell cycle arrest mediated by the MEK/mitogen-activated protein kinase pathway
    • Pumiglia K.M., Decker S.J. Cell cycle arrest mediated by the MEK/mitogen-activated protein kinase pathway. Proc Natl Acad Sci USA. 94:1997;448-452.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 448-452
    • Pumiglia, K.M.1    Decker, S.J.2
  • 147
    • 0033527752 scopus 로고    scopus 로고
    • Inactivation of p42 mitogen-activated protein kinase is required for exit from M-phase after cyclin destruction
    • Chau A.S., Shibuya E.K. Inactivation of p42 mitogen-activated protein kinase is required for exit from M-phase after cyclin destruction. J Biol Chem. 274:1999;32085-32090.
    • (1999) J Biol Chem , vol.274 , pp. 32085-32090
    • Chau, A.S.1    Shibuya, E.K.2
  • 150
    • 0033571245 scopus 로고    scopus 로고
    • Transcription-independent phosphorylation of the RNA polymerase II C-terminal domain (CTD) involves ERK kinases (MEK1/2)
    • Bonnet F., Vigneron M., Bensaude O., Dubois M.F. Transcription-independent phosphorylation of the RNA polymerase II C-terminal domain (CTD) involves ERK kinases (MEK1/2). Nucleic Acids Res. 27:1999;4399-4404.
    • (1999) Nucleic Acids Res , vol.27 , pp. 4399-4404
    • Bonnet, F.1    Vigneron, M.2    Bensaude, O.3    Dubois, M.F.4
  • 151
    • 0034688287 scopus 로고    scopus 로고
    • A central control for cell growth
    • Whitmarsh A.J., Davis R.J. A central control for cell growth. Nature. 403:2000;255-256.
    • (2000) Nature , vol.403 , pp. 255-256
    • Whitmarsh, A.J.1    Davis, R.J.2
  • 152
    • 0030990093 scopus 로고    scopus 로고
    • Recombination signal sequence binding protein Jκ is constitutively bound to the NF-κB site of the interleukin-6 promoter and is a negative regulatory factor
    • Plaisance S., Vanden Berghe W., Boone E., Fiers W., Haegeman G. Recombination signal sequence binding protein Jκ is constitutively bound to the NF-κB site of the interleukin-6 promoter and is a negative regulatory factor. Mol Cell Biol. 17:1997;3733-3743.
    • (1997) Mol Cell Biol , vol.17 , pp. 3733-3743
    • Plaisance, S.1    Vanden Berghe, W.2    Boone, E.3    Fiers, W.4    Haegeman, G.5
  • 154
    • 0033524444 scopus 로고    scopus 로고
    • CIR, a corepressor linking the DNA binding factor CBF1 to the histone deacetylase complex
    • Hsieh J.J., Zhou S., Chen L., Young D.B., Hayward S.D. CIR, a corepressor linking the DNA binding factor CBF1 to the histone deacetylase complex. Proc Natl Acad Sci USA. 96:1999;23-28.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 23-28
    • Hsieh, J.J.1    Zhou, S.2    Chen, L.3    Young, D.B.4    Hayward, S.D.5
  • 157
    • 0029778179 scopus 로고    scopus 로고
    • Glucocorticoid-mediated repression of NF-κB activity in endothelial cells does not involve induction of IκB-α synthesis
    • Brostjan C., Anrather J., Csizmadia V., Stroka D., Soares M., Bach F.H., Winkler H. Glucocorticoid-mediated repression of NF-κB activity in endothelial cells does not involve induction of IκB-α synthesis. J Biol Chem. 271:1996;19612-19616.
    • (1996) J Biol Chem , vol.271 , pp. 19612-19616
    • Brostjan, C.1    Anrather, J.2    Csizmadia, V.3    Stroka, D.4    Soares, M.5    Bach, F.H.6    Winkler, H.7
  • 158
    • 0031459881 scopus 로고    scopus 로고
    • Glucocorticoid-mediated repression of nuclear factor-κB-dependent transcription involves direct interference with transactivation
    • De Bosscher K., Schmitz M.L., Vanden Berghe W., Plaisance S., Fiers W., Haegeman G. Glucocorticoid-mediated repression of nuclear factor-κB-dependent transcription involves direct interference with transactivation. Proc Natl Acad Sci USA. 94:1997;13504-13509.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 13504-13509
    • De Bosscher, K.1    Schmitz, M.L.2    Vanden Berghe, W.3    Plaisance, S.4    Fiers, W.5    Haegeman, G.6
  • 159
    • 0030789420 scopus 로고    scopus 로고
    • IκB-α-independent downregulation of NF-κB activity by glucocorticoid receptor
    • Heck S., Bender K., Kullmann M., Gottlicher M., Herrlich P., Cato A.C. IκB-α-independent downregulation of NF-κB activity by glucocorticoid receptor. EMBO J. 16:1997;4698-4707.
    • (1997) EMBO J , vol.16 , pp. 4698-4707
    • Heck, S.1    Bender, K.2    Kullmann, M.3    Gottlicher, M.4    Herrlich, P.5    Cato, A.C.6
  • 160
    • 0032870623 scopus 로고    scopus 로고
    • Dissociated glucocorticoids with anti-inflammatory potential repress interleukin-6 gene expression by a nuclear factor-κB-dependent mechanism
    • Vanden Berghe W., Francesconi E., De Bosscher K., Resche-Rigon M., Haegeman G. Dissociated glucocorticoids with anti-inflammatory potential repress interleukin-6 gene expression by a nuclear factor-κB-dependent mechanism. Mol Pharmacol. 56:1999;797-806.
    • (1999) Mol Pharmacol , vol.56 , pp. 797-806
    • Vanden Berghe, W.1    Francesconi, E.2    De Bosscher, K.3    Resche-Rigon, M.4    Haegeman, G.5
  • 161
    • 0032491483 scopus 로고    scopus 로고
    • Nuclear integration of glucocorticoid receptor and nuclear factor-κB signaling by CREB-binding protein and steroid receptor coactivator-1
    • Sheppard K.A., Phelps K.M., Williams A.J., Thanos D., Glass C.K., Rosenfeld M.G., Gerritsen M.E., Collins T. Nuclear integration of glucocorticoid receptor and nuclear factor-κB signaling by CREB-binding protein and steroid receptor coactivator-1. J Biol Chem. 273:1998;29291-29294.
    • (1998) J Biol Chem , vol.273 , pp. 29291-29294
    • Sheppard, K.A.1    Phelps, K.M.2    Williams, A.J.3    Thanos, D.4    Glass, C.K.5    Rosenfeld, M.G.6    Gerritsen, M.E.7    Collins, T.8
  • 162
    • 0034454583 scopus 로고    scopus 로고
    • Nuclear hormone receptor coregulators in action: Diversity for shared tasks
    • Robyr D., Wolffe A.P., Wahli W. Nuclear hormone receptor coregulators in action Diversity for shared tasks. Mol Endocrinol. 14:2000;329-347.
    • (2000) Mol Endocrinol , vol.14 , pp. 329-347
    • Robyr, D.1    Wolffe, A.P.2    Wahli, W.3
  • 163
    • 0028960452 scopus 로고
    • Interaction of the COOH-terminal transactivation domain of p65 NF-κB with TATA-binding protein, transcription factor IIB, and coactivators
    • Schmitz M.L., Stelzer G., Altmann H., Meisterernst M., Baeuerle P.A. Interaction of the COOH-terminal transactivation domain of p65 NF-κB with TATA-binding protein, transcription factor IIB, and coactivators. J Biol Chem. 270:1995;7219-7226.
    • (1995) J Biol Chem , vol.270 , pp. 7219-7226
    • Schmitz, M.L.1    Stelzer, G.2    Altmann, H.3    Meisterernst, M.4    Baeuerle, P.A.5
  • 164
    • 0030666901 scopus 로고    scopus 로고
    • A weak TATA box is a prerequisite for glucocorticoid-dependent repression of the osteocalcin gene
    • Meyer T., Carlstedt-Duke J., Starr D.B. A weak TATA box is a prerequisite for glucocorticoid-dependent repression of the osteocalcin gene. J Biol Chem. 272:1997;30709-30714.
    • (1997) J Biol Chem , vol.272 , pp. 30709-30714
    • Meyer, T.1    Carlstedt-Duke, J.2    Starr, D.B.3
  • 165
    • 0032162228 scopus 로고    scopus 로고
    • TAF(II)105 mediates activation of anti-apoptotic genes by NF-κB
    • Yamit-Hezi A., Dikstein R. TAF(II)105 mediates activation of anti-apoptotic genes by NF-κB. EMBO J. 17:1998;5161-5169.
    • (1998) EMBO J , vol.17 , pp. 5161-5169
    • Yamit-Hezi, A.1    Dikstein, R.2
  • 167
    • 0034636021 scopus 로고    scopus 로고
    • Glucocorticoids repress NF-κB-driven genes by disturbing the interaction of p65 with the basal transcription machinery, irrespective of coactivator levels in the cell
    • De Bosscher K., Vanden Berghe W., Vermeulen L., Plaisance S., Boone E., Haegeman G. Glucocorticoids repress NF-κB-driven genes by disturbing the interaction of p65 with the basal transcription machinery, irrespective of coactivator levels in the cell. Proc Natl Acad Sci USA. 97:2000;3919-3924.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3919-3924
    • De Bosscher, K.1    Vanden Berghe, W.2    Vermeulen, L.3    Plaisance, S.4    Boone, E.5    Haegeman, G.6
  • 168
    • 0034284349 scopus 로고    scopus 로고
    • Mechanisms of anti-inflammatory action and of immunosuppression by glucocorticoids: Negative interference of activated glucocorticoid receptor with transcription factors
    • in press
    • De Bosscher K, Vanden Berghe W and Haegeman G, Mechanisms of anti-inflammatory action and of immunosuppression by glucocorticoids: Negative interference of activated glucocorticoid receptor with transcription factors. J Neuroimmunol 1: in press, 2000.
    • (2000) J Neuroimmunol , vol.1
    • De Bosscher, K.1    Vanden Berghe, W.2    Haegeman, G.3
  • 169
    • 0032580207 scopus 로고    scopus 로고
    • Allosteric effects of DNA on transcriptional regulators
    • Lefstin J.A., Yamamoto K.R. Allosteric effects of DNA on transcriptional regulators. Nature. 392:1998;885-888.
    • (1998) Nature , vol.392 , pp. 885-888
    • Lefstin, J.A.1    Yamamoto, K.R.2
  • 170
    • 0031455626 scopus 로고    scopus 로고
    • Nuclear hormone receptor antagonism with AP-1 by inhibition of the JNK pathway
    • Caelles C., Gonzalez-Sancho J.M., Munoz A. Nuclear hormone receptor antagonism with AP-1 by inhibition of the JNK pathway. Genes Dev. 11:1997;3351-3364.
    • (1997) Genes Dev , vol.11 , pp. 3351-3364
    • Caelles, C.1    Gonzalez-Sancho, J.M.2    Munoz, A.3
  • 171
    • 0344423816 scopus 로고    scopus 로고
    • Hormone-activated nuclear receptors inhibit the stimulation of the JNK and ERK signalling pathways in endothelial cells
    • Gonzalez M.V., Gonzalez-Sancho J.M., Caelles C., Munoz A., Jimenez B. Hormone-activated nuclear receptors inhibit the stimulation of the JNK and ERK signalling pathways in endothelial cells. FEBS Lett. 459:1999;272-276.
    • (1999) FEBS Lett , vol.459 , pp. 272-276
    • Gonzalez, M.V.1    Gonzalez-Sancho, J.M.2    Caelles, C.3    Munoz, A.4    Jimenez, B.5
  • 172
    • 0034629290 scopus 로고    scopus 로고
    • Disruption of raf-1/heat shock protein 90 complex and raf signaling by dexamethasone in mast cells
    • Cissel D.S., Beaven M.A. Disruption of raf-1/heat shock protein 90 complex and raf signaling by dexamethasone in mast cells. J Biol Chem. 275:2000;7066-7070.
    • (2000) J Biol Chem , vol.275 , pp. 7066-7070
    • Cissel, D.S.1    Beaven, M.A.2
  • 173
    • 0033527569 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor α negatively regulates the vascular inflammatory gene response by negative cross-talk with transcription factors NF-κB and AP-1
    • Delerive P., De Bosscher K., Besnard S., Vanden Berghe W., Peters J.M., Gonzalez F.J., Fruchart J.C., Tedgui A., Haegeman G., Staels B. Peroxisome proliferator-activated receptor α negatively regulates the vascular inflammatory gene response by negative cross-talk with transcription factors NF-κB and AP-1. J Biol Chem. 274:1999;32048-32054.
    • (1999) J Biol Chem , vol.274 , pp. 32048-32054
    • Delerive, P.1    De Bosscher, K.2    Besnard, S.3    Vanden Berghe, W.4    Peters, J.M.5    Gonzalez, F.J.6    Fruchart, J.C.7    Tedgui, A.8    Haegeman, G.9    Staels, B.10
  • 174
    • 0343417089 scopus 로고    scopus 로고
    • The p300/CBP family: Integrating signals with transcription factors and chromatin
    • Shikama N., Lyon J., La Thangue N.B. The p300/CBP family Integrating signals with transcription factors and chromatin. Trends Cell Biol. 7:1997;230-236.
    • (1997) Trends Cell Biol , vol.7 , pp. 230-236
    • Shikama, N.1    Lyon, J.2    La Thangue, N.B.3
  • 175
    • 0033574784 scopus 로고    scopus 로고
    • Nuclear fusion of signaling pathways
    • Janknecht R., Hunter T. Nuclear fusion of signaling pathways. Science. 284:1999;443-444.
    • (1999) Science , vol.284 , pp. 443-444
    • Janknecht, R.1    Hunter, T.2
  • 176
    • 0032498230 scopus 로고    scopus 로고
    • The enhanceosome and transcriptional synergy
    • Carey M. The enhanceosome and transcriptional synergy. Cell. 92:1998;5-8.
    • (1998) Cell , vol.92 , pp. 5-8
    • Carey, M.1
  • 177
    • 0033606999 scopus 로고    scopus 로고
    • Transcription: Common cofactors and cooperative recruitment
    • Wu W.H., Hampsey M. Transcription Common cofactors and cooperative recruitment. Curr Biol. 9:1999;R606-R609.
    • (1999) Curr Biol , vol.9 , pp. 606-R609
    • Wu, W.H.1    Hampsey, M.2
  • 178
    • 0032100763 scopus 로고    scopus 로고
    • Modulation of cytokine-induced HIV gene expression by competitive binding of transcription factors to the coactivator p300
    • Hottiger M.O., Felzien L.K., Nabel G.J. Modulation of cytokine-induced HIV gene expression by competitive binding of transcription factors to the coactivator p300. EMBO J. 17:1998;3124-3134.
    • (1998) EMBO J , vol.17 , pp. 3124-3134
    • Hottiger, M.O.1    Felzien, L.K.2    Nabel, G.J.3
  • 181
    • 0032951890 scopus 로고    scopus 로고
    • Characterization of an E1A-CBP interaction defines a novel transcriptional adapter motif (TRAM) in CBP/p300
    • O’Connor M.J., Zimmermann H., Nielsen S., Bernard H.U., Kouzarides T. Characterization of an E1A-CBP interaction defines a novel transcriptional adapter motif (TRAM) in CBP/p300. J Virol. 73:1999;3574-3581.
    • (1999) J Virol , vol.73 , pp. 3574-3581
    • O’Connor, M.J.1    Zimmermann, H.2    Nielsen, S.3    Bernard, H.U.4    Kouzarides, T.5
  • 182
    • 0032412441 scopus 로고    scopus 로고
    • Modulation of chromatin structure regulates cytokine gene expression during T cell differentiation
    • Agarwal S., Rao A. Modulation of chromatin structure regulates cytokine gene expression during T cell differentiation. Immunity. 9:1998;765-775.
    • (1998) Immunity , vol.9 , pp. 765-775
    • Agarwal, S.1    Rao, A.2
  • 183
    • 0345019804 scopus 로고    scopus 로고
    • Long-range transcriptional regulation of cytokine gene expression
    • Agarwal S., Rao A. Long-range transcriptional regulation of cytokine gene expression. Curr Opin Immunol. 10:1998;345-352.
    • (1998) Curr Opin Immunol , vol.10 , pp. 345-352
    • Agarwal, S.1    Rao, A.2
  • 185
    • 0033451474 scopus 로고    scopus 로고
    • Rapid and selective remodeling of a positioned nucleosome during the induction of IL-12 p40 transcription
    • Weinmann A.S., Plevy S.E., Smale S.T. Rapid and selective remodeling of a positioned nucleosome during the induction of IL-12 p40 transcription. Immunity. 11:1999;665-675.
    • (1999) Immunity , vol.11 , pp. 665-675
    • Weinmann, A.S.1    Plevy, S.E.2    Smale, S.T.3
  • 186
    • 0032954699 scopus 로고    scopus 로고
    • Innovative treatment programs against cancer: II. Nuclear factor-κB (NF-κB) as a molecular target
    • Waddick K.G., Uckun F.M. Innovative treatment programs against cancer II. Nuclear factor-κB (NF-κB) as a molecular target. Biochem Pharmacol. 57:1999;9-17.
    • (1999) Biochem Pharmacol , vol.57 , pp. 9-17
    • Waddick, K.G.1    Uckun, F.M.2
  • 189
    • 0030747128 scopus 로고    scopus 로고
    • NF-κB as a frequent target for immunosuppressive and anti-inflammatory molecules
    • Baeuerle P.A., Baichwal V.R. NF-κB as a frequent target for immunosuppressive and anti-inflammatory molecules. Adv Immunol. 65:1997;111-137.
    • (1997) Adv Immunol , vol.65 , pp. 111-137
    • Baeuerle, P.A.1    Baichwal, V.R.2
  • 190
    • 0032900439 scopus 로고    scopus 로고
    • New insights into the role of nuclear factor-κB, a ubiquitous transcription factor in the initiation of diseases
    • Chen F., Castranova V., Shi X., Demers L.M. New insights into the role of nuclear factor-κB, a ubiquitous transcription factor in the initiation of diseases. Clin Chem. 45:1999;7-17.
    • (1999) Clin Chem , vol.45 , pp. 7-17
    • Chen, F.1    Castranova, V.2    Shi, X.3    Demers, L.M.4
  • 191
    • 0041661592 scopus 로고    scopus 로고
    • NF-κB as an emerging target in atopy
    • Beyaert R. NF-κB as an emerging target in atopy. Emerg Ther Targets. 3:1999;1-16.
    • (1999) Emerg Ther Targets , vol.3 , pp. 1-16
    • Beyaert, R.1
  • 192
    • 0031593664 scopus 로고    scopus 로고
    • Role of NF-κB in immune and inflammatory responses in the gut
    • Neurath M.F., Becker C., Barbulescu K. Role of NF-κB in immune and inflammatory responses in the gut. Gut. 43:1998;856-860.
    • (1998) Gut , vol.43 , pp. 856-860
    • Neurath, M.F.1    Becker, C.2    Barbulescu, K.3
  • 193
    • 17544365995 scopus 로고    scopus 로고
    • The IκB/NF-κB system: A key determinant of mucosal inflammation and protection
    • Jobin C., Sartor R.B. The IκB/NF-κB system A key determinant of mucosal inflammation and protection. Am J Physiol Cell Physiol. 278:2000;C451-C462.
    • (2000) Am J Physiol Cell Physiol , vol.278 , pp. 451-C462
    • Jobin, C.1    Sartor, R.B.2
  • 194
    • 0031842804 scopus 로고    scopus 로고
    • Transcription factors and asthma
    • Barnes P.J., Adcock I.M. Transcription factors and asthma. Eur Respir J. 12:1998;221-234.
    • (1998) Eur Respir J , vol.12 , pp. 221-234
    • Barnes, P.J.1    Adcock, I.M.2
  • 195
    • 0032724630 scopus 로고    scopus 로고
    • Novel approaches and targets for treatment of chronic obstructive pulmonary disease
    • Barnes P.J. Novel approaches and targets for treatment of chronic obstructive pulmonary disease. Am J Respir Crit Care Med. 160:1999;S72-S79.
    • (1999) Am J Respir Crit Care Med , vol.160 , pp. 72-S79
    • Barnes, P.J.1
  • 196
    • 0033144367 scopus 로고    scopus 로고
    • Nuclear factor κb (NF-κB) pathway as a therapeutic target in rheumatoid arthritis
    • Jue D.M., Jeon K.I., Jeong J.Y. Nuclear factor κB (NF-κB) pathway as a therapeutic target in rheumatoid arthritis. J Korean Med Sci. 14:1999;231-238.
    • (1999) J Korean Med Sci , vol.14 , pp. 231-238
    • Jue, D.M.1    Jeon, K.I.2    Jeong, J.Y.3
  • 197
    • 0031755148 scopus 로고    scopus 로고
    • Nuclear factor κb: A pivotal role in the systemic inflammatory response syndrome and new target for therapy
    • Christman J.W., Lancaster L.H., Blackwell T.S. Nuclear factor κB A pivotal role in the systemic inflammatory response syndrome and new target for therapy. Intensive Care Med. 24:1998;1131-1138.
    • (1998) Intensive Care Med , vol.24 , pp. 1131-1138
    • Christman, J.W.1    Lancaster, L.H.2    Blackwell, T.S.3
  • 198
    • 0001112989 scopus 로고    scopus 로고
    • The anti-inflammatory sesquiterpene lactone helenalin inhibits the transcription factor NF-κB by directly targeting p65
    • Lyss G., Knorre A., Schmidt T.J., Pahl H.L., Merfort I. The anti-inflammatory sesquiterpene lactone helenalin inhibits the transcription factor NF-κB by directly targeting p65. J Biol Chem. 273:1998;33508-33516.
    • (1998) J Biol Chem , vol.273 , pp. 33508-33516
    • Lyss, G.1    Knorre, A.2    Schmidt, T.J.3    Pahl, H.L.4    Merfort, I.5
  • 199
    • 0343765810 scopus 로고    scopus 로고
    • Sesquiterpene lactone containing Mexican Indian medicinal plants and pure sesquiterpene lactones as potent inhibitors of transcription factor NF-κB
    • Bork P.M., Schmitz M.L., Kuhnt M., Escher C., Heinrich M. Sesquiterpene lactone containing Mexican Indian medicinal plants and pure sesquiterpene lactones as potent inhibitors of transcription factor NF-κB. FEBS Lett. 402:1997;85-90.
    • (1997) FEBS Lett , vol.402 , pp. 85-90
    • Bork, P.M.1    Schmitz, M.L.2    Kuhnt, M.3    Escher, C.4    Heinrich, M.5
  • 200
    • 0032487857 scopus 로고    scopus 로고
    • The anti-inflammatory agents aspirin and salicylate inhibit the activity of IκB kinase-β
    • Yin M.J., Yamamoto Y., Gaynor R.B. The anti-inflammatory agents aspirin and salicylate inhibit the activity of IκB kinase-β Nature. 396:1998;77-80.
    • (1998) Nature , vol.396 , pp. 77-80
    • Yin, M.J.1    Yamamoto, Y.2    Gaynor, R.B.3
  • 201
    • 0032487869 scopus 로고    scopus 로고
    • A new target for aspirin
    • O’Neill E. A new target for aspirin. Nature. 396:1998;15-17.
    • (1998) Nature , vol.396 , pp. 15-17
    • O’Neill, E.1


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