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Volumn 20, Issue 3, 2002, Pages 91-106

Transcriptional and post-transcriptional control of gene expression in inflammation

Author keywords

Gene expression; IL 1; Inflammation; MAP kinase; mRNA stability; TNF; Transcription

Indexed keywords

BINDING PROTEIN; CYCLOOXYGENASE 2; CYTOKINE; DOCKING PROTEIN; GLUCOCORTICOID; HISTONE DEACETYLASE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERCELLULAR ADHESION MOLECULE 1; INTERLEUKIN 1; INTERLEUKIN 1 RECEPTOR; INTERLEUKIN 10; INTERLEUKIN 13; INTERLEUKIN 17; INTERLEUKIN 18; INTERLEUKIN 4; INTERLEUKIN 6; INTERLEUKIN 8; INTERLEUKIN 8 RECEPTOR; LIPOPOLYSACCHARIDE; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; SERUM RESPONSE FACTOR; SYNAPTOPHYSIN; TOLL LIKE RECEPTOR; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR RECEPTOR; VASCULAR CELL ADHESION MOLECULE 1; PROTEIN KINASE;

EID: 0036435213     PISSN: 10434666     EISSN: None     Source Type: Journal    
DOI: 10.1006/cyto.2002.0895     Document Type: Review
Times cited : (214)

References (220)
  • 1
    • 0034075754 scopus 로고    scopus 로고
    • The IL-1 receptor/toll-like receptor superfamily: Crucial receptors for inflammation and host defence
    • O'Neill LA, Dinarello CA (2000) The IL-1 receptor/toll-like receptor superfamily: Crucial receptors for inflammation and host defence. Immunol Today 21(5):206-209.
    • (2000) Immunol Today , vol.21 , Issue.5 , pp. 206-209
    • O'Neill, L.A.1    Dinarello, C.A.2
  • 2
    • 0035936797 scopus 로고    scopus 로고
    • The TNF and TNF receptor superfamilies: Integrating mammalian biology
    • Locksley RM, Killeen N, Lenardo MJ (2001) The TNF and TNF receptor superfamilies: Integrating mammalian biology. Cell 104(4):487-501.
    • (2001) Cell , vol.104 , Issue.4 , pp. 487-501
    • Locksley, R.M.1    Killeen, N.2    Lenardo, M.J.3
  • 4
    • 0031801957 scopus 로고    scopus 로고
    • Signal transduction pathways activated by the IL-1 receptor family: Ancient signaling machinery in mammals, insects, and plants
    • O'Neill LA, Greene C (1998) Signal transduction pathways activated by the IL-1 receptor family: Ancient signaling machinery in mammals, insects, and plants. J Leukoc Biol 63(6):650-657.
    • (1998) J Leukoc Biol , vol.63 , Issue.6 , pp. 650-657
    • O'Neill, L.A.1    Greene, C.2
  • 5
    • 0034680145 scopus 로고    scopus 로고
    • Toll-like receptors in the induction of the innate immune response
    • Aderem A, Ulevitch RJ (2000) Toll-like receptors in the induction of the innate immune response. Nature 406(6797):782-787.
    • (2000) Nature , vol.406 , Issue.6797 , pp. 782-787
    • Aderem, A.1    Ulevitch, R.J.2
  • 6
    • 0035444539 scopus 로고    scopus 로고
    • Signal transduction by tumor necrosis factor and its relatives
    • Baud V, Karin M (2001) Signal transduction by tumor necrosis factor and its relatives. Trends Cell Biol 11(9):372-377.
    • (2001) Trends Cell Biol , vol.11 , Issue.9 , pp. 372-377
    • Baud, V.1    Karin, M.2
  • 7
    • 0031423761 scopus 로고    scopus 로고
    • MyD88: An adapter that recruits IRAK to the IL-1 receptor complex
    • Wesche H, Henzel WJ, Shillinglaw W, Li S, Cao Z (1997) MyD88: An adapter that recruits IRAK to the IL-1 receptor complex. Immunity 7(6):837-847.
    • (1997) Immunity , vol.7 , Issue.6 , pp. 837-847
    • Wesche, H.1    Henzel, W.J.2    Shillinglaw, W.3    Li, S.4    Cao, Z.5
  • 8
    • 0029761275 scopus 로고    scopus 로고
    • TRAF6 is a signal transducer for interleukin-1
    • Cao Z, Xiong J, Takeuchi M, Kurama T, Goeddel DV (1996) TRAF6 is a signal transducer for interleukin-1. Nature 383(6599):443-446.
    • (1996) Nature , vol.383 , Issue.6599 , pp. 443-446
    • Cao, Z.1    Xiong, J.2    Takeuchi, M.3    Kurama, T.4    Goeddel, D.V.5
  • 9
    • 0034599961 scopus 로고    scopus 로고
    • Requirement of tumor necrosis factor receptor-associated factor (TRAF)6 in interleukin 17 signal transduction
    • Schwandner R, Yamaguchi K, Cao Z (2000) Requirement of tumor necrosis factor receptor-associated factor (TRAF)6 in interleukin 17 signal transduction. J Exp Med 191(7):1233-1240.
    • (2000) J Exp Med , vol.191 , Issue.7 , pp. 1233-1240
    • Schwandner, R.1    Yamaguchi, K.2    Cao, Z.3
  • 10
    • 10544243364 scopus 로고    scopus 로고
    • Identification of TRAF6, a novel tumor necrosis factor receptor-associated factor protein that mediates signaling from an amino-terminal domain of the CD40 cytoplasmic region
    • Ishida T, Mizushima Si, Azuma S, Kobayashi N, Tojo T, Suzuki K, Aizawa S, Watanabe T, Mosialos G, Kieff E, Yamamoto T, Inoue J ((1996) Identification of TRAF6, a novel tumor necrosis factor receptor-associated factor protein that mediates signaling from an amino-terminal domain of the CD40 cytoplasmic region. J Biol Chem 271(46):28745-28748.
    • (1996) J Biol Chem , vol.271 , Issue.46 , pp. 28745-28748
    • Ishida, T.1    Mizushima, S.2    Azuma, S.3    Kobayashi, N.4    Tojo, T.5    Suzuki, K.6    Aizawa, S.7    Watanabe, T.8    Mosialos, G.9    Kieff, E.10    Yamamoto, T.11    Inoue, J.12
  • 12
    • 0033166472 scopus 로고    scopus 로고
    • Unresponsiveness of MyD88-deficient mice to endotoxin
    • Kawai T, Adachi O, Ogawa T, Takeda K, Akira S (1999) Unresponsiveness of MyD88-deficient mice to endotoxin. Immunity 11(1):115-122.
    • (1999) Immunity , vol.11 , Issue.1 , pp. 115-122
    • Kawai, T.1    Adachi, O.2    Ogawa, T.3    Takeda, K.4    Akira, S.5
  • 15
    • 0033563101 scopus 로고    scopus 로고
    • Signaling by proinflammatory cytokines: Oligomerization of TRAF2 and TRAF6 is sufficient for JNK and IKK activation and target gene induction via an amino-terminal effector domain
    • Baud V, Liu ZG, Bennett B, Suzuki N, Xia Y, Karin M (1999) Signaling by proinflammatory cytokines: Oligomerization of TRAF2 and TRAF6 is sufficient for JNK and IKK activation and target gene induction via an amino-terminal effector domain. Genes Dev 13(10):1297-1308.
    • (1999) Genes Dev , vol.13 , Issue.10 , pp. 1297-1308
    • Baud, V.1    Liu, Z.G.2    Bennett, B.3    Suzuki, N.4    Xia, Y.5    Karin, M.6
  • 16
    • 0035555301 scopus 로고    scopus 로고
    • TIRAP: An adapter molecule in the Toll signaling pathway
    • Horng T, Barton GM, Medzhitov R (2001) TIRAP: An adapter molecule in the Toll signaling pathway. Nat Immunol 2(9):835-844.
    • (2001) Nat Immunol , vol.2 , Issue.9 , pp. 835-844
    • Horng, T.1    Barton, G.M.2    Medzhitov, R.3
  • 17
    • 0035868884 scopus 로고    scopus 로고
    • Segregation of TRAF6-mediated signaling pathways clarifies its role in osteoclastogenesis
    • Kobayashi N, Kadono Y, Naito A, Matsumoto K, Yamamoto T, Tanaka S, Inoue J (2001) Segregation of TRAF6-mediated signaling pathways clarifies its role in osteoclastogenesis. EMBO J 20(6):1271-1280.
    • (2001) EMBO J , vol.20 , Issue.6 , pp. 1271-1280
    • Kobayashi, N.1    Kadono, Y.2    Naito, A.3    Matsumoto, K.4    Yamamoto, T.5    Tanaka, S.6    Inoue, J.7
  • 18
    • 0008206988 scopus 로고    scopus 로고
    • TRAF2 is essential for JNK but not NF-kappaB activation and regulates lymphocyte proliferation and survival
    • Lee SY, Reichlin A, Santana A, Sokol KA, Nussenzweig MC, Choi Y (1997) TRAF2 is essential for JNK but not NF-kappaB activation and regulates lymphocyte proliferation and survival. Immunity 7(5):703-713.
    • (1997) Immunity , vol.7 , Issue.5 , pp. 703-713
    • Lee, S.Y.1    Reichlin, A.2    Santana, A.3    Sokol, K.A.4    Nussenzweig, M.C.5    Choi, Y.6
  • 19
    • 0033725155 scopus 로고    scopus 로고
    • The distinct roles of TRAF2 and RIP in IKK activation by TNF-R1: TRAF2 recruits IKK to TNF-R1 while RIP mediates IKK activation
    • Devin A, Cook A, Lin Y, Rodriguez Y, Kelliher M, Liu Z (2000) The distinct roles of TRAF2 and RIP in IKK activation by TNF-R1: TRAF2 recruits IKK to TNF-R1 while RIP mediates IKK activation. Immunity 12(4):419-429.
    • (2000) Immunity , vol.12 , Issue.4 , pp. 419-429
    • Devin, A.1    Cook, A.2    Lin, Y.3    Rodriguez, Y.4    Kelliher, M.5    Liu, Z.6
  • 20
    • 0033516561 scopus 로고    scopus 로고
    • IRAK-M is a novel member of the Pelle/interleukin-1 receptor-associated kinase (IRAK) family
    • Wesche H, Gao X, Li X, Kirschning CJ, Stark GR, Cao Z (1999) IRAK-M is a novel member of the Pelle/interleukin-1 receptor-associated kinase (IRAK) family. J Biol Chem 274(27):19403-19410.
    • (1999) J Biol Chem , vol.274 , Issue.27 , pp. 19403-19410
    • Wesche, H.1    Gao, X.2    Li, X.3    Kirschning, C.J.4    Stark, G.R.5    Cao, Z.6
  • 22
    • 0034662854 scopus 로고    scopus 로고
    • T6BP, a TRAF6-interacting protein involved in IL-1 signaling
    • Ling L, Goeddel DV (2000) T6BP, a TRAF6-interacting protein involved in IL-1 signaling. Proc Natl Acad Sci USA 97(17):9567-9572.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.17 , pp. 9567-9572
    • Ling, L.1    Goeddel, D.V.2
  • 23
    • 0033634977 scopus 로고    scopus 로고
    • TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway
    • Takaesu G, Kishida S, Hiyama A, Yamaguchi K, Shibuya H, Irie K, Ninomiya-Tsuji J, Matsumoto K (2000) TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway. Mol Cell 5(4):649-658.
    • (2000) Mol Cell , vol.5 , Issue.4 , pp. 649-658
    • Takaesu, G.1    Kishida, S.2    Hiyama, A.3    Yamaguchi, K.4    Shibuya, H.5    Irie, K.6    Ninomiya-Tsuji, J.7    Matsumoto, K.8
  • 24
    • 0033567388 scopus 로고    scopus 로고
    • ECSIT is an evolutionarily conserved intermediate in the Toll/IL-1 signal transduction pathway
    • Kopp E, Medzhitov R, Carothers J, Xiao C, Douglas I, Janeway CA, Ghosh S (1999) ECSIT is an evolutionarily conserved intermediate in the Toll/IL-1 signal transduction pathway. Genes Dev 13(16):2059-2071.
    • (1999) Genes Dev , vol.13 , Issue.16 , pp. 2059-2071
    • Kopp, E.1    Medzhitov, R.2    Carothers, J.3    Xiao, C.4    Douglas, I.5    Janeway, C.A.6    Ghosh, S.7
  • 26
    • 0032573165 scopus 로고    scopus 로고
    • Ionizing radiation and short wave-length UV activate NF-kappaB through two distinct mechanisms
    • Li N, Karin M (1998) Ionizing radiation and short wave-length UV activate NF-kappaB through two distinct mechanisms. Proc Natl Acad Sci USA 95(22):13012-13017.
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.22 , pp. 13012-13017
    • Li, N.1    Karin, M.2
  • 27
    • 0029860936 scopus 로고    scopus 로고
    • Ultraviolet light and osmotic stress: Activation of the JNK cascade through multiple growth factor and cytokine receptors
    • Rosette C, Karin M (1996) Ultraviolet light and osmotic stress: Activation of the JNK cascade through multiple growth factor and cytokine receptors. Science 274(5290):1194-1197.
    • (1996) Science , vol.274 , Issue.5290 , pp. 1194-1197
    • Rosette, C.1    Karin, M.2
  • 28
    • 0039598450 scopus 로고    scopus 로고
    • Ultraviolet radiation-induced interleukin 6 release in HeLa cells is mediated via membrane events in a DNA damage-independent way
    • Kulms D, Poppelmann B, Schwarz T (2000) Ultraviolet radiation-induced interleukin 6 release in HeLa cells is mediated via membrane events in a DNA damage-independent way. J Biol Chem 275(20):15060-15066.
    • (2000) J Biol Chem , vol.275 , Issue.20 , pp. 15060-15066
    • Kulms, D.1    Poppelmann, B.2    Schwarz, T.3
  • 29
    • 0029858594 scopus 로고    scopus 로고
    • The tumor promoter arsenite stimulates AP-1 activity by inhibiting a JNK phosphatase
    • Cavigelli M, Li WW, Lin A, Su B, Yoshioka K, Karin M (2000) The tumor promoter arsenite stimulates AP-1 activity by inhibiting a JNK phosphatase. EMBO J 15(22):6269-6279.
    • (2000) EMBO J , vol.15 , Issue.22 , pp. 6269-6279
    • Cavigelli, M.1    Li, W.W.2    Lin, A.3    Su, B.4    Yoshioka, K.5    Karin, M.6
  • 30
    • 0034680928 scopus 로고    scopus 로고
    • Inhibition of NF-kappa B activation by arsenite through reaction with a critical cysteine in the activation loop of Ikappa B kinase
    • Kapahi P, Takahashi T, Natoli G, Adams SR, Chen Y, Tsien RY, Karin M (2000) Inhibition of NF-kappa B activation by arsenite through reaction with a critical cysteine in the activation loop of Ikappa B kinase. J Biol Chem 275(46):36062-36066.
    • (2000) J Biol Chem , vol.275 , Issue.46 , pp. 36062-36066
    • Kapahi, P.1    Takahashi, T.2    Natoli, G.3    Adams, S.R.4    Chen, Y.5    Tsien, R.Y.6    Karin, M.7
  • 32
    • 0033996762 scopus 로고    scopus 로고
    • The I kappa B kinase (IKK) and NF-kappa B: Key elements of proinflammatory signalling
    • Karin M, Delhase M (2000) The I kappa B kinase (IKK) and NF-kappa B: Key elements of proinflammatory signalling. Semin Immunol 12(1):85-98.
    • (2000) Semin Immunol , vol.12 , Issue.1 , pp. 85-98
    • Karin, M.1    Delhase, M.2
  • 33
    • 0033537739 scopus 로고    scopus 로고
    • Severe liver degeneration in mice lacking the IkappaB kinase 2 gene
    • Li Q, Van Antwerp D, Mercurio F, Lee KF, Verma IM (1999) Severe liver degeneration in mice lacking the IkappaB kinase 2 gene. Science 284(5412):321-325.
    • (1999) Science , vol.284 , Issue.5412 , pp. 321-325
    • Li, Q.1    Van Antwerp, D.2    Mercurio, F.3    Lee, K.F.4    Verma, I.M.5
  • 34
    • 0035066383 scopus 로고    scopus 로고
    • Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation
    • Kyriakis JM, Avruch J (2001) Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation. Physiol Rev 81(2):807-869.
    • (2001) Physiol Rev , vol.81 , Issue.2 , pp. 807-869
    • Kyriakis, J.M.1    Avruch, J.2
  • 35
    • 0033537719 scopus 로고    scopus 로고
    • Positive and negative regulation of IkappaB kinase activity through IKKbeta phosphorylation
    • Delhase M, Hayakawa M, Chen Y, Karin M (1999) Positive and negative regulation of IkappaB kinase activity through IKKbeta phosphorylation. Science 284(5412):309-313.
    • (1999) Science , vol.284 , Issue.5412 , pp. 309-313
    • Delhase, M.1    Hayakawa, M.2    Chen, Y.3    Karin, M.4
  • 36
    • 0033605575 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase/ERK kinase kinases 2 and 3 activate nuclear factor-kappaB through IkappaB kinase-alpha and IkappaB kinase-beta
    • Zhao Q, Lee FS (1999) Mitogen-activated protein kinase/ERK kinase kinases 2 and 3 activate nuclear factor-kappaB through IkappaB kinase-alpha and IkappaB kinase-beta. J Biol Chem 274(13):8355-8358.
    • (1999) J Biol Chem , vol.274 , Issue.13 , pp. 8355-8358
    • Zhao, Q.1    Lee, F.S.2
  • 37
    • 0033082990 scopus 로고    scopus 로고
    • The proto-oncogene Cot kinase participates in CD3/CD28 induction of NF-kappaB acting through the NF-kappaB-inducing kinase and IkappaB kinases
    • Lin X, Cunningham ET Jr, Mu Y, Geleziunas R, Greene WC (1999) The proto-oncogene Cot kinase participates in CD3/CD28 induction of NF-kappaB acting through the NF-kappaB-inducing kinase and IkappaB kinases. Immunity 10(2):271-280.
    • (1999) Immunity , vol.10 , Issue.2 , pp. 271-280
    • Lin, X.1    Cunningham E.T., Jr.2    Mu, Y.3    Geleziunas, R.4    Greene, W.C.5
  • 39
    • 0034644474 scopus 로고    scopus 로고
    • Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain
    • Deng L, Wang C, Spencer E, Yang L, Braun A, You J, Slaughter C, Pickart C, Chen ZJ (2000) Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Cell 103(2):351-356.
    • (2000) Cell , vol.103 , Issue.2 , pp. 351-356
    • Deng, L.1    Wang, C.2    Spencer, E.3    Yang, L.4    Braun, A.5    You, J.6    Slaughter, C.7    Pickart, C.8    Chen, Z.J.9
  • 40
    • 0035913278 scopus 로고    scopus 로고
    • TAK1 is a ubiquitin-dependent kinase of MKK and IKK
    • Wang C, Deng L, Hong M, Akkaraju GR, Inoue J, Chen ZJ (2001) TAK1 is a ubiquitin-dependent kinase of MKK and IKK. Nature 412(6844):346-351.
    • (2001) Nature , vol.412 , Issue.6844 , pp. 346-351
    • Wang, C.1    Deng, L.2    Hong, M.3    Akkaraju, G.R.4    Inoue, J.5    Chen, Z.J.6
  • 41
    • 0035896422 scopus 로고    scopus 로고
    • Defective lymphotoxin-beta receptor-induced NF-kappaB transcriptional activity in NIK-deficient mice
    • Yin L, Wu L, Wesche H, Arthur CD, White JM, Goeddel DV, Schreiber RD (2001) Defective lymphotoxin-beta receptor-induced NF-kappaB transcriptional activity in NIK-deficient mice. Science 291(5511):2162-2165.
    • (2001) Science , vol.291 , Issue.5511 , pp. 2162-2165
    • Yin, L.1    Wu, L.2    Wesche, H.3    Arthur, C.D.4    White, J.M.5    Goeddel, D.V.6    Schreiber, R.D.7
  • 44
    • 0034284131 scopus 로고    scopus 로고
    • Docking domains and substrate-specificity determination for MAP kinases
    • Sharrocks AD, Yang SH, Galanis A (2000) Docking domains and substrate-specificity determination for MAP kinases. Trends Biochem Sci 25(9):448-453.
    • (2000) Trends Biochem Sci , vol.25 , Issue.9 , pp. 448-453
    • Sharrocks, A.D.1    Yang, S.H.2    Galanis, A.3
  • 45
    • 0033788484 scopus 로고    scopus 로고
    • A conserved docking motif in MAP kinases common to substrates, activators and regulators
    • Tanoue T, Adachi M, Moriguchi T, Nishida E (2000) A conserved docking motif in MAP kinases common to substrates, activators and regulators. Nat Cell Biol 2(2):110-116.
    • (2000) Nat Cell Biol , vol.2 , Issue.2 , pp. 110-116
    • Tanoue, T.1    Adachi, M.2    Moriguchi, T.3    Nishida, E.4
  • 46
    • 0032825497 scopus 로고    scopus 로고
    • The JIP group of mitogen-activated protein kinase scaffold proteins
    • Yasuda J, Whitmarsh AJ, Cavanagh J, Sharma M, Davis RJ (1999) The JIP group of mitogen-activated protein kinase scaffold proteins. Mol Cell Biol 19(10):7245-7254.
    • (1999) Mol Cell Biol , vol.19 , Issue.10 , pp. 7245-7254
    • Yasuda, J.1    Whitmarsh, A.J.2    Cavanagh, J.3    Sharma, M.4    Davis, R.J.5
  • 47
    • 0032526988 scopus 로고    scopus 로고
    • Leptomycin B-sensitive nuclear export of MAPKAP kinase 2 is regulated by phosphorylation
    • Engel K, Kotlyarov A, Gaestel M (1998) Leptomycin B-sensitive nuclear export of MAPKAP kinase 2 is regulated by phosphorylation. EMBO J 17(12):3363-3371.
    • (1998) EMBO J , vol.17 , Issue.12 , pp. 3363-3371
    • Engel, K.1    Kotlyarov, A.2    Gaestel, M.3
  • 48
    • 0030706186 scopus 로고    scopus 로고
    • Nuclear accumulation of NFAT4 opposed by the JNK signal transduction pathway
    • Chow CW, Rincon M, Cavanagh J, Dickens M, Davis RJ (1997) Nuclear accumulation of NFAT4 opposed by the JNK signal transduction pathway. Science 278(5343):1638-1641.
    • (1997) Science , vol.278 , Issue.5343 , pp. 1638-1641
    • Chow, C.W.1    Rincon, M.2    Cavanagh, J.3    Dickens, M.4    Davis, R.J.5
  • 49
    • 0034625170 scopus 로고    scopus 로고
    • MEK kinase 1 is critically required for c-Jun N-terminal kinase activation by proinflammatory stimuli and growth factor-induced cell migration
    • Xia Y, Makris C, Su B, Li E, Yang J, Nemerow GR, Karin M (2000) MEK kinase 1 is critically required for c-Jun N-terminal kinase activation by proinflammatory stimuli and growth factor-induced cell migration. Proc Natl Acad Sci USA 97(10):5243-5248.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.10 , pp. 5243-5248
    • Xia, Y.1    Makris, C.2    Su, B.3    Li, E.4    Yang, J.5    Nemerow, G.R.6    Karin, M.7
  • 54
    • 0034992168 scopus 로고    scopus 로고
    • MKK7 is an essential component of the JNK signal transduction pathway activated by proinflammatory cytokines
    • Tournier C, Dong C, Turner TK, Jones SN, Flavell RA, Davis RJ (2001) MKK7 is an essential component of the JNK signal transduction pathway activated by proinflammatory cytokines. Genes Dev 15(11):1419-1426.
    • (2001) Genes Dev , vol.15 , Issue.11 , pp. 1419-1426
    • Tournier, C.1    Dong, C.2    Turner, T.K.3    Jones, S.N.4    Flavell, R.A.5    Davis, R.J.6
  • 55
    • 0032499687 scopus 로고    scopus 로고
    • SEK1 deficiency reveals mitogen-activated protein kinase cascade crossregulation and leads to abnormal hepatogenesis
    • Ganiatsas S, Kwee L, Fujiwara Y, Perkins A, Ikeda T, Labow MA, Zon LI (1998) SEK1 deficiency reveals mitogen-activated protein kinase cascade crossregulation and leads to abnormal hepatogenesis. Proc Natl Acad Sci USA 95(12):6881-6886.
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.12 , pp. 6881-6886
    • Ganiatsas, S.1    Kwee, L.2    Fujiwara, Y.3    Perkins, A.4    Ikeda, T.5    Labow, M.A.6    Zon, L.I.7
  • 56
    • 0033118982 scopus 로고    scopus 로고
    • Defective IL-12 production in mitogen-activated protein (MAP) kinase kinase (Mkk3)-deficient mice
    • Lu HT, Yang DD, Wysk M, Gatti E, Mellman I, Davis RJ, Flavell RA (1999) Defective IL-12 production in mitogen-activated protein (MAP) kinase kinase (Mkk3)-deficient mice. EMBO J 18(7):1845-1857.
    • (1999) EMBO J , vol.18 , Issue.7 , pp. 1845-1857
    • Lu, H.T.1    Yang, D.D.2    Wysk, M.3    Gatti, E.4    Mellman, I.5    Davis, R.J.6    Flavell, R.A.7
  • 57
    • 0033616588 scopus 로고    scopus 로고
    • Requirement of mitogen-activated protein kinase kinase 3 (MKK3) for tumor necrosis factor-induced cytokine
    • Wysk M, Yang DD, Lu HT, Flavell RA, Davis RJ (1999) Requirement of mitogen-activated protein kinase kinase 3 (MKK3) for tumor necrosis factor-induced cytokine. Proc Natl Acad Sci USA 96(7):3763-3768.
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.7 , pp. 3763-3768
    • Wysk, M.1    Yang, D.D.2    Lu, H.T.3    Flavell, R.A.4    Davis, R.J.5
  • 61
    • 0034610981 scopus 로고    scopus 로고
    • Deficiency of the stress kinase p38alpha results in embryonic lethality: Characterization of the kinase dependence of stress responses of enzyme-deficient embryonic stem cells
    • Allen M, Svensson L, Roach M, Hambor J, McNeish J, Gabel CA (2000) Deficiency of the stress kinase p38alpha results in embryonic lethality: Characterization of the kinase dependence of stress responses of enzyme-deficient embryonic stem cells. J Exp Med 191(5):859-870.
    • (2000) J Exp Med , vol.191 , Issue.5 , pp. 859-870
    • Allen, M.1    Svensson, L.2    Roach, M.3    Hambor, J.4    McNeish, J.5    Gabel, C.A.6
  • 62
    • 0034697904 scopus 로고    scopus 로고
    • Requirement for p38alpha in erythropoietin expression: A role for stress kinases in erythropoiesis
    • Tamura K, Sudo T, Senftleben U, Dadak AM, Johnson R, Karin M (2000) Requirement for p38alpha in erythropoietin expression: A role for stress kinases in erythropoiesis. Cell 102(2):221-231.
    • (2000) Cell , vol.102 , Issue.2 , pp. 221-231
    • Tamura, K.1    Sudo, T.2    Senftleben, U.3    Dadak, A.M.4    Johnson, R.5    Karin, M.6
  • 64
    • 0034644522 scopus 로고    scopus 로고
    • Signal transduction by the JNK group of MAP kinases
    • Davis RJ (2000) Signal transduction by the JNK group of MAP kinases. Cell 103(2):239-252.
    • (2000) Cell , vol.103 , Issue.2 , pp. 239-252
    • Davis, R.J.1
  • 65
    • 0035282334 scopus 로고    scopus 로고
    • Mammalian MAP kinase signalling cascades
    • Chang L, Karin M (2001) Mammalian MAP kinase signalling cascades. Nature 410(6824):37-40.
    • (2001) Nature , vol.410 , Issue.6824 , pp. 37-40
    • Chang, L.1    Karin, M.2
  • 66
  • 67
    • 0029101772 scopus 로고
    • Transcriptional regulation of endothelial cell adhesion molecules: NF-kappa B and cytokine-inducible enhancers
    • Collins T, Read MA, Neish AS, Whitley MZ, Thanos D, Maniatis T (1995) Transcriptional regulation of endothelial cell adhesion molecules: NF-kappa B and cytokine-inducible enhancers. FASEB J 9(10):899-909.
    • (1995) FASEB J , vol.9 , Issue.10 , pp. 899-909
    • Collins, T.1    Read, M.A.2    Neish, A.S.3    Whitley, M.Z.4    Thanos, D.5    Maniatis, T.6
  • 68
    • 0035798579 scopus 로고    scopus 로고
    • The transcription factor C/EBPbeta is essential for inducible expression of the cox-2 gene in macrophages but not in fibroblasts
    • Gorgoni B, Caivano M, Arizmendi C, Poli V (2001) The transcription factor C/EBPbeta is essential for inducible expression of the cox-2 gene in macrophages but not in fibroblasts. J Biol Chem 276(44):40769-40777.
    • (2001) J Biol Chem , vol.276 , Issue.44 , pp. 40769-40777
    • Gorgoni, B.1    Caivano, M.2    Arizmendi, C.3    Poli, V.4
  • 69
    • 0035896597 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases mediate activator protein-1-dependent human inducible nitric-oxide synthase promoter
    • Kristof AS, Marks-Konczalik J, Moss J (2001) Mitogen-activated protein kinases mediate activator protein-1-dependent human inducible nitric-oxide synthase promoter. J Biol Chem 276(11):8445-52.
    • (2001) J Biol Chem , vol.276 , Issue.11 , pp. 8445-8452
    • Kristof, A.S.1    Marks-Konczalik, J.2    Moss, J.3
  • 70
    • 0031596140 scopus 로고    scopus 로고
    • Nuclear factor kappaB/p50 activates an element in the distal matrix metalloproteinase 1 promoter in interleukin-1beta-stimulated synovial fibroblasts
    • Vincenti MP, Coon CI, Brinckerhoff CE (1998) Nuclear factor kappaB/p50 activates an element in the distal matrix metalloproteinase 1 promoter in interleukin-1beta-stimulated synovial fibroblasts. Arthritis Rheum 41(11):1987-1994.
    • (1998) Arthritis Rheum , vol.41 , Issue.11 , pp. 1987-1994
    • Vincenti, M.P.1    Coon, C.I.2    Brinckerhoff, C.E.3
  • 74
    • 0029827366 scopus 로고    scopus 로고
    • The p38 and ERK MAP kinase pathways cooperate to activate Ternary Complex Factors and c-fos transcription in response to UV light
    • Price MA, Cruzalegui FH, Treisman R (1996) The p38 and ERK MAP kinase pathways cooperate to activate Ternary Complex Factors and c-fos transcription in response to UV light. EMBO J 15(23):6552-6563.
    • (1996) EMBO J , vol.15 , Issue.23 , pp. 6552-6563
    • Price, M.A.1    Cruzalegui, F.H.2    Treisman, R.3
  • 75
    • 0030906520 scopus 로고    scopus 로고
    • Role of p38 and JNK mitogen-activated protein kinases in the activation of ternary complex factors
    • Whitmarsh AJ, Yang SH, Su MS, Sharrocks AD, Davis RJ (1997) Role of p38 and JNK mitogen-activated protein kinases in the activation of ternary complex factors. Mol Cell Biol 17(5):2360-2371.
    • (1997) Mol Cell Biol , vol.17 , Issue.5 , pp. 2360-2371
    • Whitmarsh, A.J.1    Yang, S.H.2    Su, M.S.3    Sharrocks, A.D.4    Davis, R.J.5
  • 76
    • 0030660391 scopus 로고    scopus 로고
    • Effects of the inhibition of p38/RK MAP kinase on induction of five fos and jun genes by diverse stimuli
    • Hazzalin CA, Cuenda A, Cano E, Cohen P, Mahadevan LC (1997) Effects of the inhibition of p38/RK MAP kinase on induction of five fos and jun genes by diverse stimuli. Oncogene 15(19):2321-2331.
    • (1997) Oncogene , vol.15 , Issue.19 , pp. 2321-2331
    • Hazzalin, C.A.1    Cuenda, A.2    Cano, E.3    Cohen, P.4    Mahadevan, L.C.5
  • 77
    • 0032931259 scopus 로고    scopus 로고
    • The repertoire of fos and jun proteins expressed during the G1 phase of the cell cycle is determined by the duration of mitogen-activated protein kinase activation
    • Cook SJ, Aziz N, McMahon M (1999) The repertoire of fos and jun proteins expressed during the G1 phase of the cell cycle is determined by the duration of mitogen-activated protein kinase activation. Mol Cell Biol 19(1):330-341.
    • (1999) Mol Cell Biol , vol.19 , Issue.1 , pp. 330-341
    • Cook, S.J.1    Aziz, N.2    McMahon, M.3
  • 79
    • 0031018424 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha-induced E-selectin expression is activated by the nuclear factor-kappaB and c-JUN N-terminal kinase/p38 mitogen-activated protein kinase pathways
    • Read MA, Whitley MZ, Gupta S, Pierce JW, Best J, Davis RJ, Collins T (1997) Tumor necrosis factor alpha-induced E-selectin expression is activated by the nuclear factor-kappaB and c-JUN N-terminal kinase/p38 mitogen-activated protein kinase pathways. J Biol Chem 272(5):2753-2761.
    • (1997) J Biol Chem , vol.272 , Issue.5 , pp. 2753-2761
    • Read, M.A.1    Whitley, M.Z.2    Gupta, S.3    Pierce, J.W.4    Best, J.5    Davis, R.J.6    Collins, T.7
  • 80
    • 0029808748 scopus 로고    scopus 로고
    • Transcription factor AP-1 regulation by mitogen-activated protein kinase signal transduction pathways
    • Whitmarsh AJ, Davis RJ (1996) Transcription factor AP-1 regulation by mitogen-activated protein kinase signal transduction pathways. J Mol Med 74(10):589-607.
    • (1996) J Mol Med , vol.74 , Issue.10 , pp. 589-607
    • Whitmarsh, A.J.1    Davis, R.J.2
  • 81
    • 0031023756 scopus 로고    scopus 로고
    • Reduced ubiquitin-dependent degradation of c-Jun after phosphorylation by MAP kinases
    • Musti AM, Treier M, Bohmann D (1997) Reduced ubiquitin-dependent degradation of c-Jun after phosphorylation by MAP kinases. Science 275(5298):400-402.
    • (1997) Science , vol.275 , Issue.5298 , pp. 400-402
    • Musti, A.M.1    Treier, M.2    Bohmann, D.3
  • 82
    • 0034725037 scopus 로고    scopus 로고
    • Stability of the ATF2 transcription factor is regulated by phosphorylation and dephosphorylation
    • Fuchs SY, Tappin I, Ronai Z (2000) Stability of the ATF2 transcription factor is regulated by phosphorylation and dephosphorylation. J Biol Chem 275(17):12560-12564.
    • (2000) J Biol Chem , vol.275 , Issue.17 , pp. 12560-12564
    • Fuchs, S.Y.1    Tappin, I.2    Ronai, Z.3
  • 83
    • 0028144846 scopus 로고
    • c-Fos transcriptional activity stimulated by H-Ras-activated protein kinase distinct from JNK and ERK
    • Deng T, Karin M (1994) c-Fos transcriptional activity stimulated by H-Ras-activated protein kinase distinct from JNK and ERK. Nature 371(6493):171-175.
    • (1994) Nature , vol.371 , Issue.6493 , pp. 171-175
    • Deng, T.1    Karin, M.2
  • 84
    • 0028108504 scopus 로고
    • Regulation of Fra-1 and Fra-2 phosphorylation differs during the cell cycle of fibroblasts and phosphorylation in vitro by MAP kinase affects DNA binding activity
    • Gruda MC, Kovary K, Metz R, Bravo R (1994) Regulation of Fra-1 and Fra-2 phosphorylation differs during the cell cycle of fibroblasts and phosphorylation in vitro by MAP kinase affects DNA binding activity. Oncogene 9(9):2537-2547.
    • (1994) Oncogene , vol.9 , Issue.9 , pp. 2537-2547
    • Gruda, M.C.1    Kovary, K.2    Metz, R.3    Bravo, R.4
  • 85
    • 0033288055 scopus 로고    scopus 로고
    • Mapping DNA target sites of chromatin proteins in vivo by formaldehyde crosslinking
    • Strutt H, Paro R (1999) Mapping DNA target sites of chromatin proteins in vivo by formaldehyde crosslinking. Methods Mol Biol 119:455-467.
    • (1999) Methods Mol Biol , vol.119 , pp. 455-467
    • Strutt, H.1    Paro, R.2
  • 86
    • 0035971432 scopus 로고    scopus 로고
    • AP-1 in mouse development and tumorigenesis
    • Jochum W, Passegue E, Wagner EF (2001) AP-1 in mouse development and tumorigenesis. Oncogene 20(19):2401-2412.
    • (2001) Oncogene , vol.20 , Issue.19 , pp. 2401-2412
    • Jochum, W.1    Passegue, E.2    Wagner, E.F.3
  • 87
    • 0030271387 scopus 로고    scopus 로고
    • NF-kappa B: Ten years after
    • Baeuerle PA, Baltimore D (1996) NF-kappa B: Ten years after. Cell 87(1):13-20.
    • (1996) Cell , vol.87 , Issue.1 , pp. 13-20
    • Baeuerle, P.A.1    Baltimore, D.2
  • 88
    • 0027384590 scopus 로고
    • NF-kappa B subunit-specific regulation of the interleukin-8 promoter
    • Kunsch C, Rosen CA (1993) NF-kappa B subunit-specific regulation of the interleukin-8 promoter. Mol Cell Biol 13(10):6137-6146.
    • (1993) Mol Cell Biol , vol.13 , Issue.10 , pp. 6137-6146
    • Kunsch, C.1    Rosen, C.A.2
  • 89
    • 0031964687 scopus 로고    scopus 로고
    • A novel DNA recognition mode by the NF-kappa B p65 homodimer
    • Chen YQ, Ghosh S, Ghosh G (1998) A novel DNA recognition mode by the NF-kappa B p65 homodimer. Nat Struct Biol 5(1):67-73.
    • (1998) Nat Struct Biol , vol.5 , Issue.1 , pp. 67-73
    • Chen, Y.Q.1    Ghosh, S.2    Ghosh, G.3
  • 90
    • 0034665748 scopus 로고    scopus 로고
    • The glucocorticoid receptor inhibits NFkappaB by interfering with serine-2 phosphorylation of the RNA polymerase II carboxy-terminal domain
    • Nissen RM, Yamamoto KR (2000) The glucocorticoid receptor inhibits NFkappaB by interfering with serine-2 phosphorylation of the RNA polymerase II carboxy-terminal domain. Genes Dev 14(18):2314-2329.
    • (2000) Genes Dev , vol.14 , Issue.18 , pp. 2314-2329
    • Nissen, R.M.1    Yamamoto, K.R.2
  • 91
    • 0035908126 scopus 로고    scopus 로고
    • Two waves of nuclear factor kappaB recruitment to target promoters
    • Saccani S, Pantano S, Natoli G (2001) Two waves of nuclear factor kappaB recruitment to target promoters. J Exp Med 193(12):1351-1359.
    • (2001) J Exp Med , vol.193 , Issue.12 , pp. 1351-1359
    • Saccani, S.1    Pantano, S.2    Natoli, G.3
  • 92
    • 0030615201 scopus 로고    scopus 로고
    • Nuclear factor-kappaB: A pivotal transcription factor in chronic inflammatory diseases
    • Barnes PJ, Karin M (1997) Nuclear factor-kappaB: A pivotal transcription factor in chronic inflammatory diseases. N Engl J Med 336(15):1066-1071.
    • (1997) N Engl J Med , vol.336 , Issue.15 , pp. 1066-1071
    • Barnes, P.J.1    Karin, M.2
  • 93
    • 0035282213 scopus 로고    scopus 로고
    • I kappa B-independent control of NF-kappa B activity by modulatory phosphorylations
    • Schmitz ML, Bacher S, Kracht M (2001) I kappa B-independent control of NF-kappa B activity by modulatory phosphorylations. Trends Biochem Sci 26(3):186-190.
    • (2001) Trends Biochem Sci , vol.26 , Issue.3 , pp. 186-190
    • Schmitz, M.L.1    Bacher, S.2    Kracht, M.3
  • 94
    • 0035979737 scopus 로고    scopus 로고
    • Duration of nuclear NF-kappaB action regulated by reversible acetylation
    • Chen Lf, Fischle W, Verdin E, Greene WC (2001) Duration of nuclear NF-kappaB action regulated by reversible acetylation. Science 293(5535):1653-1657.
    • (2001) Science , vol.293 , Issue.5535 , pp. 1653-1657
    • Chen, Lf.1    Fischle, W.2    Verdin, E.3    Greene, W.C.4
  • 96
    • 0034612636 scopus 로고    scopus 로고
    • Requirement for glycogen synthase kinase-3beta in cell survival and NF-kappaB activation
    • Hoeflich KP, Luo J, Rubie EA, Tsao MS, Jin O, Woodgett JR (2000) Requirement for glycogen synthase kinase-3beta in cell survival and NF-kappaB activation. Nature 406(6791):86-90.
    • (2000) Nature , vol.406 , Issue.6791 , pp. 86-90
    • Hoeflich, K.P.1    Luo, J.2    Rubie, E.A.3    Tsao, M.S.4    Jin, O.5    Woodgett, J.R.6
  • 97
    • 0032491401 scopus 로고    scopus 로고
    • The role of C/EBP isoforms in the control of inflammatory and native immunity functions
    • Poli V (1998) The role of C/EBP isoforms in the control of inflammatory and native immunity functions. J Biol Chem 273(45):29279-29282.
    • (1998) J Biol Chem , vol.273 , Issue.45 , pp. 29279-29282
    • Poli, V.1
  • 98
    • 0029671351 scopus 로고    scopus 로고
    • C/EBP is required for the late phases of acute phase gene induction in the liver and for tumour necrosis factor-, but not interleukin-6, regulation
    • Cappelletti M, Alonzi T, Fattori E, Libert C, Poli V (1996) C/EBP is required for the late phases of acute phase gene induction in the liver and for tumour necrosis factor-, but not interleukin-6, regulation. Cell Death Differ 3:29-35.
    • (1996) Cell Death Differ , vol.3 , pp. 29-35
    • Cappelletti, M.1    Alonzi, T.2    Fattori, E.3    Libert, C.4    Poli, V.5
  • 99
    • 0035131190 scopus 로고    scopus 로고
    • Essential role of STAT3 in the control of the acute-phase response as revealed by inducible gene inactivation [correction of activation] in the liver
    • Alonzi T, Maritano D, Gorgoni B, Rizzuto G, Libert C, Poli V (2001) Essential role of STAT3 in the control of the acute-phase response as revealed by inducible gene inactivation [correction of activation] in the liver. Mol Cell Biol 21(5):1621-1632.
    • (2001) Mol Cell Biol , vol.21 , Issue.5 , pp. 1621-1632
    • Alonzi, T.1    Maritano, D.2    Gorgoni, B.3    Rizzuto, G.4    Libert, C.5    Poli, V.6
  • 100
    • 0027379055 scopus 로고
    • Distinct mechanisms for regulation of the interleukin-8 gene involve synergism and cooperativity between C/EBP and NF-kappa B
    • Stein B, Baldwin AS Jr (1993) Distinct mechanisms for regulation of the interleukin-8 gene involve synergism and cooperativity between C/EBP and NF-kappa B. Mol Cell Biol 13(11):7191-7198.
    • (1993) Mol Cell Biol , vol.13 , Issue.11 , pp. 7191-7198
    • Stein, B.1    Baldwin A.S., Jr.2
  • 101
    • 0035966082 scopus 로고    scopus 로고
    • The induction of cyclooxygenase-2 mRNA in macrophages is biphasic and requires both C/EBP (beta) and C/EBP(delta) transcription factors
    • Caivano M, Gorgoni B, Cohen P, Poli V (2001) The induction of cyclooxygenase-2 mRNA in macrophages is biphasic and requires both C/EBP (beta) and C/EBP(delta) transcription factors. J Biol Chem 276(52):48693-48701.
    • (2001) J Biol Chem , vol.276 , Issue.52 , pp. 48693-48701
    • Caivano, M.1    Gorgoni, B.2    Cohen, P.3    Poli, V.4
  • 102
    • 0034725716 scopus 로고    scopus 로고
    • Induction of secreted type IIA phospholipase A2 gene transcription by interleukin-1beta. Role of C/EBP factors
    • Massaad C, Paradon M, Jacques C, Salvat C, Bereziat G, Berenbaum F, Olivier JL (2000) Induction of secreted type IIA phospholipase A2 gene transcription by interleukin-1beta. Role of C/EBP factors. J Biol Chem 275(30):22686-22694.
    • (2000) J Biol Chem , vol.275 , Issue.30 , pp. 22686-22694
    • Massaad, C.1    Paradon, M.2    Jacques, C.3    Salvat, C.4    Bereziat, G.5    Berenbaum, F.6    Olivier, J.L.7
  • 103
    • 0027186357 scopus 로고
    • Transactivation by NF-IL6/LAP is enhanced by phosphorylation of its activation domain
    • Trautwein C, Caelles C, van der Geer P, Hunter T, Karin M, Chojkier M (1993) Transactivation by NF-IL6/LAP is enhanced by phosphorylation of its activation domain. Nature 364(6437):544-547.
    • (1993) Nature , vol.364 , Issue.6437 , pp. 544-547
    • Trautwein, C.1    Caelles, C.2    Van der Geer, P.3    Hunter, T.4    Karin, M.5    Chojkier, M.6
  • 104
    • 0034740214 scopus 로고    scopus 로고
    • C/EBPbeta phosphorylation by RSK creates a functional XEXD caspase inhibitory box critical for cell survival
    • Buck M, Poli V, Hunter T, Chojkier M (2001) C/EBPbeta phosphorylation by RSK creates a functional XEXD caspase inhibitory box critical for cell survival. Mol Cell 8(4):807-816.
    • (2001) Mol Cell , vol.8 , Issue.4 , pp. 807-816
    • Buck, M.1    Poli, V.2    Hunter, T.3    Chojkier, M.4
  • 105
    • 0033136947 scopus 로고    scopus 로고
    • The role of p38 mitogen-activated protein kinase in IL-1 beta transcription
    • Baldassare JJ, Bi Y, Bellone CJ (1999) The role of p38 mitogen-activated protein kinase in IL-1 beta transcription. J Immunol 162(9):5367-5373.
    • (1999) J Immunol , vol.162 , Issue.9 , pp. 5367-5373
    • Baldassare, J.J.1    Bi, Y.2    Bellone, C.J.3
  • 106
    • 0029938805 scopus 로고    scopus 로고
    • Stress-induced phosphorylation and activation of the transcription factor CHOP (GADD153) by p38 MAP Kinase
    • Wang XZ, Ron D (1996) Stress-induced phosphorylation and activation of the transcription factor CHOP (GADD153) by p38 MAP Kinase. Science 272(5266):1347-1349.
    • (1996) Science , vol.272 , Issue.5266 , pp. 1347-1349
    • Wang, X.Z.1    Ron, D.2
  • 107
    • 0035515347 scopus 로고    scopus 로고
    • The ETS-domain transcription factor family
    • Sharrocks AD (2001) The ETS-domain transcription factor family. Nat Rev Mol Cell Biol 2(11):827-837.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , Issue.11 , pp. 827-837
    • Sharrocks, A.D.1
  • 108
    • 0033867980 scopus 로고    scopus 로고
    • A lipopolysaccharide-specific enhancer complex involving Ets, Elk-1, Sp1, and CREB binding protein and p300 is recruited to the tumor necrosis factor alpha promoter in vivo
    • Tsai EY, Falvo JV, Tsytsykova AV, Barczak AK, Reimold AM, Glimcher LH, Fenton MJ, Gordon DC, Dunn IF, Goldfeld AE (2000) A lipopolysaccharide-specific enhancer complex involving Ets, Elk-1, Sp1, and CREB binding protein and p300 is recruited to the tumor necrosis factor alpha promoter in vivo. Mol Cell Biol 20(16):6084-6094.
    • (2000) Mol Cell Biol , vol.20 , Issue.16 , pp. 6084-6094
    • Tsai, E.Y.1    Falvo, J.V.2    Tsytsykova, A.V.3    Barczak, A.K.4    Reimold, A.M.5    Glimcher, L.H.6    Fenton, M.J.7    Gordon, D.C.8    Dunn, I.F.9    Goldfeld, A.E.10
  • 109
    • 0029125757 scopus 로고
    • Integration of MAP kinase signal transduction pathways at the serum response element
    • Whitmarsh AJ, Shore P, Sharrocks AD, Davis RJ (1995) Integration of MAP kinase signal transduction pathways at the serum response element. Science 269(5222):403-407.
    • (1995) Science , vol.269 , Issue.5222 , pp. 403-407
    • Whitmarsh, A.J.1    Shore, P.2    Sharrocks, A.D.3    Davis, R.J.4
  • 111
    • 0035469890 scopus 로고    scopus 로고
    • Lipopolysaccharide activation of the MEK-ERK1/2 pathway in human monocytic cells mediates tissue factor and tumor necrosis factor alpha expression by inducing Elk-1 phosphorylation and Egr-1 expression
    • Guha M, O'Connell MA, Pawlinski R, Hollis A, McGovern P, Yan SF, Stern D, Mackman N (2001) Lipopolysaccharide activation of the MEK-ERK1/2 pathway in human monocytic cells mediates tissue factor and tumor necrosis factor alpha expression by inducing Elk-1 phosphorylation and Egr-1 expression. Blood 98(5):1429-1439.
    • (2001) Blood , vol.98 , Issue.5 , pp. 1429-1439
    • Guha, M.1    O'Connell, M.A.2    Pawlinski, R.3    Hollis, A.4    McGovern, P.5    Yan, S.F.6    Stern, D.7    Mackman, N.8
  • 112
    • 0024355425 scopus 로고
    • A multiple cytokine- and second messenger-responsive element in the enhancer of the human interleukin-6 gene: Similarities with c-fos gene regulation
    • Ray A, Sassone-Corsi P, Sehgal PB (1989) A multiple cytokine- and second messenger-responsive element in the enhancer of the human interleukin-6 gene: Similarities with c-fos gene regulation. Mol Cell Biol 9(12):5537-5547.
    • (1989) Mol Cell Biol , vol.9 , Issue.12 , pp. 5537-5547
    • Ray, A.1    Sassone-Corsi, P.2    Sehgal, P.B.3
  • 113
    • 0030906520 scopus 로고    scopus 로고
    • Role of p38 and JNK mitogen-activated protein kinases in the activation of ternary complex factors
    • Whitmarsh AJ, Yang SH, Su MS, Sharrocks AD, Davis RJ (1997) Role of p38 and JNK mitogen-activated protein kinases in the activation of ternary complex factors. Mol Cell Biol 17(5):2360-2371.
    • (1997) Mol Cell Biol , vol.17 , Issue.5 , pp. 2360-2371
    • Whitmarsh, A.J.1    Yang, S.H.2    Su, M.S.3    Sharrocks, A.D.4    Davis, R.J.5
  • 114
    • 0032536816 scopus 로고    scopus 로고
    • Differential targeting of MAP kinases to the ETS-domain transcription factor Elk-1
    • Yang SH, Whitmarsh AJ, Davis RJ, Sharrocks AD (1998) Differential targeting of MAP kinases to the ETS-domain transcription factor Elk-1. EMBO J 17(6):1740-1749.
    • (1998) EMBO J , vol.17 , Issue.6 , pp. 1740-1749
    • Yang, S.H.1    Whitmarsh, A.J.2    Davis, R.J.3    Sharrocks, A.D.4
  • 116
    • 0035914307 scopus 로고    scopus 로고
    • ERK2- and p90Rsk2-dependent pathways regulate the CCAAT/enhancer-binding protein-beta interaction with serum response factor
    • Hanlon M, Sturgill TW, Sealy L (2001) ERK2- and p90Rsk2-dependent pathways regulate the CCAAT/enhancer-binding protein-beta interaction with serum response factor. J Biol Chem 276(42):38449-38456.
    • (2001) J Biol Chem , vol.276 , Issue.42 , pp. 38449-38456
    • Hanlon, M.1    Sturgill, T.W.2    Sealy, L.3
  • 117
    • 0035865090 scopus 로고    scopus 로고
    • NF-kappa B regulation by I kappa B kinase-2 in rheumatoid arthritis synoviocytes
    • Aupperle K, Bennett B, Han Z, Boyle D, Manning A, Firestein G (2001) NF-kappa B regulation by I kappa B kinase-2 in rheumatoid arthritis synoviocytes. J Immunol 166(4):2705-2711.
    • (2001) J Immunol , vol.166 , Issue.4 , pp. 2705-2711
    • Aupperle, K.1    Bennett, B.2    Han, Z.3    Boyle, D.4    Manning, A.5    Firestein, G.6
  • 118
    • 0034672092 scopus 로고    scopus 로고
    • Regulation of IL-6 and IL-8 expression in rheumatoid arthritis synovial fibroblasts: The dominant role for NF-kappa B but not C/EBP beta or c-Jun
    • Georganas C, Liu H, Perlman H, Hoffmann A, Thim-mapaya B, Pope RM (2000) Regulation of IL-6 and IL-8 expression in rheumatoid arthritis synovial fibroblasts: The dominant role for NF-kappa B but not C/EBP beta or c-Jun. J Immunol 165(12):7199-7206.
    • (2000) J Immunol , vol.165 , Issue.12 , pp. 7199-7206
    • Georganas, C.1    Liu, H.2    Perlman, H.3    Hoffmann, A.4    Thimmapaya, B.5    Pope, R.M.6
  • 119
    • 0034119907 scopus 로고    scopus 로고
    • NF-kappa B regulates VCAM-1 expression on fibroblast-like synoviocytes
    • Li P, Sanz I, O'Keefe RJ, Schwarz EM (2000) NF-kappa B regulates VCAM-1 expression on fibroblast-like synoviocytes. J Immunol 164(11):5990-5997.
    • (2000) J Immunol , vol.164 , Issue.11 , pp. 5990-5997
    • Li, P.1    Sanz, I.2    O'Keefe, R.J.3    Schwarz, E.M.4
  • 120
    • 0031932422 scopus 로고    scopus 로고
    • Inhibition of proinflammatory molecule production by adenovirus-mediated expression of nuclear factor kappaB super-repressor in human intestinal epithelial cells
    • Jobin C, Panja A, Hellerbrand C, Iimuro Y, Didonato J, Brenner DA, Sartor RB (1998) Inhibition of proinflammatory molecule production by adenovirus-mediated expression of nuclear factor kappaB super-repressor in human intestinal epithelial cells. J Immunol 160(1):410-418.
    • (1998) J Immunol , vol.160 , Issue.1 , pp. 410-418
    • Jobin, C.1    Panja, A.2    Hellerbrand, C.3    Iimuro, Y.4    Didonato, J.5    Brenner, D.A.6    Sartor, R.B.7
  • 121
    • 0031009807 scopus 로고    scopus 로고
    • Involvement of interleukin-8, vascular endothelial growth factor, and basic fibroblast growth factor in tumor necrosis factor alpha-dependent angiogenesis
    • Yoshida S, Ono M, Shono T, Izumi H, Ishibashi T, Suzuki H, Kuwano M (1997) Involvement of interleukin-8, vascular endothelial growth factor, and basic fibroblast growth factor in tumor necrosis factor alpha-dependent angiogenesis. Mol Cell Biol 17(7):4015-4023.
    • (1997) Mol Cell Biol , vol.17 , Issue.7 , pp. 4015-4023
    • Yoshida, S.1    Ono, M.2    Shono, T.3    Izumi, H.4    Ishibashi, T.5    Suzuki, H.6    Kuwano, M.7
  • 123
    • 0034931503 scopus 로고    scopus 로고
    • c-Jun N-terminal kinase is required for metalloproteinase expression and joint destruction in inflammatory arthritis
    • Han Z, Boyle DL, Chang L, Bennett B, Karin M, Yang L, Manning AM, Firestein GS (2001) c-Jun N-terminal kinase is required for metalloproteinase expression and joint destruction in inflammatory arthritis. J Clin Invest 108(1):73-81.
    • (2001) J Clin Invest , vol.108 , Issue.1 , pp. 73-81
    • Han, Z.1    Boyle, D.L.2    Chang, L.3    Bennett, B.4    Karin, M.5    Yang, L.6    Manning, A.M.7    Firestein, G.S.8
  • 124
    • 0032508615 scopus 로고    scopus 로고
    • Stress-activated protein kinase/Jun N-terminal kinase is required for interleukin (IL)-1-induced IL-6 and IL-8 gene expression in the human epidermal carcinoma cell line KB
    • Krause A, Holtmann H, Eickemeier S, Winzen R, Szamel M, Resch K, Saklatvala J, Kracht M (1998) Stress-activated protein kinase/Jun N-terminal kinase is required for interleukin (IL)-1-induced IL-6 and IL-8 gene expression in the human epidermal carcinoma cell line KB. J Biol Chem 273(37):23681-23689.
    • (1998) J Biol Chem , vol.273 , Issue.37 , pp. 23681-23689
    • Krause, A.1    Holtmann, H.2    Eickemeier, S.3    Winzen, R.4    Szamel, M.5    Resch, K.6    Saklatvala, J.7    Kracht, M.8
  • 125
    • 0032582347 scopus 로고    scopus 로고
    • Interleukin-1beta-induced cyclooxygenase-2 expression requires activation of both c- NH2-terminal kinase and p38 MAPK signal pathways in rat renal mesangial cells
    • Guan Z, Buckman SY, Miller BW, Springer LD, Morrison AR (1998) Interleukin-1beta-induced cyclooxygenase-2 expression requires activation of both c- NH2-terminal kinase and p38 MAPK signal pathways in rat renal mesangial cells. J Biol Chem 273(44):28670-28676.
    • (1998) J Biol Chem , vol.273 , Issue.44 , pp. 28670-28676
    • Guan, Z.1    Buckman, S.Y.2    Miller, B.W.3    Springer, L.D.4    Morrison, A.R.5
  • 126
    • 0033579210 scopus 로고    scopus 로고
    • Both p38alpha(MAPK) and JNK/SAPK pathways are important for induction of nitric-oxide synthase by interleukin-1beta in rat glomerular mesangial cells
    • Guan Z, Buckman SY, Springer LD, Morrison AR (1999) Both p38alpha(MAPK) and JNK/SAPK pathways are important for induction of nitric-oxide synthase by interleukin-1beta in rat glomerular mesangial cells. J Biol Chem 274(51):36200-36206.
    • (1999) J Biol Chem , vol.274 , Issue.51 , pp. 36200-36206
    • Guan, Z.1    Buckman, S.Y.2    Springer, L.D.3    Morrison, A.R.4
  • 128
    • 0032823313 scopus 로고    scopus 로고
    • Induction of interleukin-8 synthesis integrates effects on transcription and mRNA degradation from at least three different cytokine- or stress-activated signal transduction pathways
    • Holtmann H, Winzen R, Holland P, Eickemeier S, Hoffmann E, Wallach D, Malinin NL, Cooper JA, Resch K, Kracht M (1999) Induction of interleukin-8 synthesis integrates effects on transcription and mRNA degradation from at least three different cytokine- or stress-activated signal transduction pathways. Mol Cell Biol 19(10):6742-6753.
    • (1999) Mol Cell Biol , vol.19 , Issue.10 , pp. 6742-6753
    • Holtmann, H.1    Winzen, R.2    Holland, P.3    Eickemeier, S.4    Hoffmann, E.5    Wallach, D.6    Malinin, N.L.7    Cooper, J.A.8    Resch, K.9    Kracht, M.10
  • 129
    • 0032557678 scopus 로고    scopus 로고
    • Induction of cyclooxygenase-2 by the activated MEKK1→SEK1/MKK4→ p38 mitogen-activated protein kinase pathway
    • Guan Z, Buckman SY, Pentland AP, Templeton DJ, Morrison AR (1998) Induction of cyclooxygenase-2 by the activated MEKK1→SEK1/MKK4→ p38 mitogen-activated protein kinase pathway. J Biol Chem 273(21):12901-12908.
    • (1998) J Biol Chem , vol.273 , Issue.21 , pp. 12901-12908
    • Guan, Z.1    Buckman, S.Y.2    Pentland, A.P.3    Templeton, D.J.4    Morrison, A.R.5
  • 130
    • 0031114081 scopus 로고    scopus 로고
    • Actions of IL-1 are selectively controlled by p38 mitogen-activated protein kinase: Regulation of prostaglandin H synthase-2, metalloproteinases, and IL-6 at different levels
    • Ridley SH, Sarsfield SJ, Lee JC, Bigg HF, Cawston TE, Taylor DJ, DeWitt DL, Saklatvala J (1997) Actions of IL-1 are selectively controlled by p38 mitogen-activated protein kinase: Regulation of prostaglandin H synthase-2, metalloproteinases, and IL-6 at different levels. J Immunol 158(7):3165-3173.
    • (1997) J Immunol , vol.158 , Issue.7 , pp. 3165-3173
    • Ridley, S.H.1    Sarsfield, S.J.2    Lee, J.C.3    Bigg, H.F.4    Cawston, T.E.5    Taylor, D.J.6    DeWitt, D.L.7    Saklatvala, J.8
  • 131
    • 0032936517 scopus 로고    scopus 로고
    • The MKK6/p38 stress kinase cascade is critical for tumor necrosis factor-alpha-induced expression of monocyte-chemoattractant protein-1 in endothelial cells
    • Goebeler M, Kilian K, Gillitzer R, Kunz M, Yoshimura T, Brocker EB, Rapp UR, Ludwig S (1999) The MKK6/p38 stress kinase cascade is critical for tumor necrosis factor-alpha-induced expression of monocyte-chemoattractant protein-1 in endothelial cells. Blood 93(3):857-865.
    • (1999) Blood , vol.93 , Issue.3 , pp. 857-865
    • Goebeler, M.1    Kilian, K.2    Gillitzer, R.3    Kunz, M.4    Yoshimura, T.5    Brocker, E.B.6    Rapp, U.R.7    Ludwig, S.8
  • 132
    • 0033987112 scopus 로고    scopus 로고
    • The role of p38 mitogen-activated protein kinase in IL-6 and IL-8 production from the TNF-alpha- or IL-1beta-stimulated rheumatoid synovial fibroblasts
    • Suzuki M, Tetsuka T, Yoshida S, Watanabe N, Kobayashi M, Matsui N, Okamoto T (2000) The role of p38 mitogen-activated protein kinase in IL-6 and IL-8 production from the TNF-alpha- or IL-1beta-stimulated rheumatoid synovial fibroblasts. FEBS Lett 465(1):23-27.
    • (2000) FEBS Lett , vol.465 , Issue.1 , pp. 23-27
    • Suzuki, M.1    Tetsuka, T.2    Yoshida, S.3    Watanabe, N.4    Kobayashi, M.5    Matsui, N.6    Okamoto, T.7
  • 133
    • 0032544234 scopus 로고    scopus 로고
    • Regulation of interleukin-1beta-induced interleukin-6 gene expression in human fibroblast-like synoviocytes by p38 mitogen-activated protein kinase
    • Miyazawa K, Mori A, Miyata H, Akahane M, Ajisawa Y, Okudaira H (1998) Regulation of interleukin-1beta-induced interleukin-6 gene expression in human fibroblast-like synoviocytes by p38 mitogen-activated protein kinase. J Biol Chem 273(38):24832-24838.
    • (1998) J Biol Chem , vol.273 , Issue.38 , pp. 24832-24838
    • Miyazawa, K.1    Mori, A.2    Miyata, H.3    Akahane, M.4    Ajisawa, Y.5    Okudaira, H.6
  • 134
    • 0034604623 scopus 로고    scopus 로고
    • p38 MAPK and NF-kappa B collaborate to induce interleukin-6 gene expression and release. Evidence for a cytoprotective autocrine signaling pathway in a cardiac myocyte model system
    • Craig R, Larkin A, Mingo AM, Thuerauf DJ, Andrews C, McDonough PM, Glembotski, CC (2000) p38 MAPK and NF-kappa B collaborate to induce interleukin-6 gene expression and release. Evidence for a cytoprotective autocrine signaling pathway in a cardiac myocyte model system. J Biol Chem 275(31):23814-23824.
    • (2000) J Biol Chem , vol.275 , Issue.31 , pp. 23814-23824
    • Craig, R.1    Larkin, A.2    Mingo, A.M.3    Thuerauf, D.J.4    Andrews, C.5    McDonough, P.M.6    Glembotski, C.C.7
  • 135
    • 0029983730 scopus 로고    scopus 로고
    • The p38/RK mitogen-activated protein kinase pathway regulates interleukin-6 synthesis response to tumor necrosis factor
    • Beyaert R, Cuenda A, Vanden Berghe W, Plaisance S, Lee JC, Haegeman G, Cohen P, Fiers W (1996) The p38/RK mitogen-activated protein kinase pathway regulates interleukin-6 synthesis response to tumor necrosis factor. EMBO J 15(8):1914-1923.
    • (1996) EMBO J , vol.15 , Issue.8 , 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
  • 137
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies SP, Reddy H, Caivano M, Cohen P (2000) Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem J 351(Pt 1):95-105.
    • (2000) Biochem J , vol.351 , Issue.PART 1 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 138
    • 0032488837 scopus 로고    scopus 로고
    • p38 and extracellular signal-regulated kinase mitogen-activated protein kinase pathways are required for nuclear factor-kappaB p65 transactivation mediated by tumor necrosis factor
    • Vanden Berghe W, Plaisance S, Boone E, De Bosscher K, Schmitz ML, Fiers W, Haegeman G (1998) p38 and extracellular signal-regulated kinase mitogen-activated protein kinase pathways are required for nuclear factor-kappaB p65 transactivation mediated by tumor necrosis factor. J Biol Chem 273(6):3285-3290.
    • (1998) J Biol Chem , vol.273 , Issue.6 , 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
  • 139
    • 0035379555 scopus 로고    scopus 로고
    • Akt stimulates the transactivation potential of the RelA/p65 Subunit of NF-kappa B through utilization of the Ikappa B kinase and activation of the mitogen-activated protein kinase p38
    • Madrid LV, Mayo MW, Reuther JY, Baldwin AS Jr (2001) Akt stimulates the transactivation potential of the RelA/p65 Subunit of NF-kappa B through utilization of the Ikappa B kinase and activation of the mitogen-activated protein kinase p38. J Biol Chem 276(22):18934-18940.
    • (2001) J Biol Chem , vol.276 , Issue.22 , pp. 18934-18940
    • Madrid, L.V.1    Mayo, M.W.2    Reuther, J.Y.3    Baldwin A.S., Jr.4
  • 140
    • 0036143654 scopus 로고    scopus 로고
    • p38-dependent marking of inflammatory genes for increased NF-kappaB recruitment
    • Saccani S, Pantano S, Natoli G (2002) p38-dependent marking of inflammatory genes for increased NF-kappaB recruitment. Nat Immunol 3(1):69-75.
    • (2002) Nat Immunol , vol.3 , Issue.1 , pp. 69-75
    • Saccani, S.1    Pantano, S.2    Natoli, G.3
  • 141
    • 0032698069 scopus 로고    scopus 로고
    • The p38 mitogen-activated protein kinase is required for NF-kappaB-dependent gene expression. The role of TATA-binding protein (TBP)
    • Carter AB, Knudtson KL, Monick MM, Hunninghake GW (1999) The p38 mitogen-activated protein kinase is required for NF-kappaB-dependent gene expression. The role of TATA-binding protein (TBP). J Biol Chem 274(43):30858-30863.
    • (1999) J Biol Chem , vol.274 , Issue.43 , pp. 30858-30863
    • Carter, A.B.1    Knudtson, K.L.2    Monick, M.M.3    Hunninghake, G.W.4
  • 142
    • 0030894683 scopus 로고    scopus 로고
    • Activation of the transcription factor MEF2C by the MAP kinase p38 in inflammation
    • Han J, Jiang Y, Li Z, Kravchenko VV, Ulevitch RJ (1997) Activation of the transcription factor MEF2C by the MAP kinase p38 in inflammation. Nature 386(6622):296-299.
    • (1997) Nature , vol.386 , Issue.6622 , pp. 296-299
    • Han, J.1    Jiang, Y.2    Li, Z.3    Kravchenko, V.V.4    Ulevitch, R.J.5
  • 144
    • 0034654533 scopus 로고    scopus 로고
    • Role of mitogen-activated protein kinase cascades in mediating lipopolysaccharide-stimulated induction of cyclooxygenase-2 and IL-1 beta in RAW264 macrophages
    • Caivano M, Cohen P (2000) Role of mitogen-activated protein kinase cascades in mediating lipopolysaccharide-stimulated induction of cyclooxygenase-2 and IL-1 beta in RAW264 macrophages. J Immunol 164(6):3018-3025.
    • (2000) J Immunol , vol.164 , Issue.6 , pp. 3018-3025
    • Caivano, M.1    Cohen, P.2
  • 145
    • 0034623241 scopus 로고    scopus 로고
    • A constitutive active MEK→ ERK pathway negatively regulates NF-kappa B-dependent gene expression by modulating TATA-binding protein phosphorylation
    • Carter AB, Hunninghake GW (2000) A constitutive active MEK→ ERK pathway negatively regulates NF-kappa B-dependent gene expression by modulating TATA-binding protein phosphorylation. J Biol Chem 275(36):27858-27864.
    • (2000) J Biol Chem , vol.275 , Issue.36 , pp. 27858-27864
    • Carter, A.B.1    Hunninghake, G.W.2
  • 146
    • 0034789898 scopus 로고    scopus 로고
    • A MEK inhibitor, PD98059 enhances IL-1-induced NF-kappaB activation by the enhanced and sustained degradation of IkappaBalpha
    • Funakoshi M, Tago K, Sonoda Y, Tominaga S, Kasahara T (2001) A MEK inhibitor, PD98059 enhances IL-1-induced NF-kappaB activation by the enhanced and sustained degradation of IkappaBalpha. Biochem Biophys Res Commun 283(1):248-254.
    • (2001) Biochem Biophys Res Commun , vol.283 , Issue.1 , pp. 248-254
    • Funakoshi, M.1    Tago, K.2    Sonoda, Y.3    Tominaga, S.4    Kasahara, T.5
  • 147
    • 0032498230 scopus 로고    scopus 로고
    • The enhanceosome and transcriptional synergy
    • Carey M (1998) The enhanceosome and transcriptional synergy. Cell 92(1):5-8.
    • (1998) Cell , vol.92 , Issue.1 , pp. 5-8
    • Carey, M.1
  • 148
    • 0034644473 scopus 로고    scopus 로고
    • Signaling to chromatin through histone modifications
    • Cheung P, Allis CD, Sassone-Corsi P (2000) Signaling to chromatin through histone modifications. Cell 103(2):263-271.
    • (2000) Cell , vol.103 , Issue.2 , pp. 263-271
    • Cheung, P.1    Allis, C.D.2    Sassone-Corsi, P.3
  • 149
    • 0030570961 scopus 로고    scopus 로고
    • Transcription. A growing coactivator network
    • Janknecht R, Hunter T (1996) Transcription. A growing coactivator network. Nature 383(6595):22-23.
    • (1996) Nature , vol.383 , Issue.6595 , pp. 22-23
    • Janknecht, R.1    Hunter, T.2
  • 150
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivators p300 and CBP are histone acetyltransferases
    • Ogryzko VV, Schiltz RL, Russanova V, Howard BH, Nakatani Y (1996) The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 87(5):953-959.
    • (1996) Cell , vol.87 , Issue.5 , pp. 953-959
    • Ogryzko, V.V.1    Schiltz, R.L.2    Russanova, V.3    Howard, B.H.4    Nakatani, Y.5
  • 151
    • 0033527448 scopus 로고    scopus 로고
    • The nuclear factor-kappaB 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 (1999) The nuclear factor-kappaB engages CBP/p300 and histone acetyltransferase activity for transcriptional activation of the interleukin-6 gene promoter. J Biol Chem 274(45):32091-32098.
    • (1999) J Biol Chem , vol.274 , Issue.45 , pp. 32091-32098
    • Vanden Berghe, W.1    De Bosscher, K.2    Boone, E.3    Plaisance, S.4    Haegeman, G.5
  • 152
    • 0034802887 scopus 로고    scopus 로고
    • The p65 (RelA) Subunit of NF-kappaB Interacts with the Histone Deacetylase (HDAC) Corepressors HDAC1 and HDAC2 To Negatively Regulate Gene Expression
    • Ashburner BP, Westerheide SD, Baldwin AS Jr (2001) The p65 (RelA) Subunit of NF-kappaB Interacts with the Histone Deacetylase (HDAC) Corepressors HDAC1 and HDAC2 To Negatively Regulate Gene Expression. Mol Cell Biol 21(20):7065-7077.
    • (2001) Mol Cell Biol , vol.21 , Issue.20 , pp. 7065-7077
    • Ashburner, B.P.1    Westerheide, S.D.2    Baldwin A.S., Jr.3
  • 153
    • 0034122095 scopus 로고    scopus 로고
    • Assembly of a functional beta interferon enhanceosome is dependent on ATF-2-c-jun heterodimer orientation
    • Falvo JV, Parekh BS, Lin CH, Fraenkel E, Maniatis T (2000) Assembly of a functional beta interferon enhanceosome is dependent on ATF-2-c-jun heterodimer orientation. Mol Cell Biol 20(13):4814-4825.
    • (2000) Mol Cell Biol , vol.20 , Issue.13 , pp. 4814-4825
    • Falvo, J.V.1    Parekh, B.S.2    Lin, C.H.3    Fraenkel, E.4    Maniatis, T.5
  • 155
    • 0035876902 scopus 로고    scopus 로고
    • Evidence for epigenetic mechanisms that silence both basal and immune-stimulated transcription of the IL-8 gene
    • Wen X, Wu GD (2001) Evidence for epigenetic mechanisms that silence both basal and immune-stimulated transcription of the IL-8 gene. J Immunol 166(12):7290.
    • (2001) J Immunol , vol.166 , Issue.12 , pp. 7290
    • Wen, X.1    Wu, G.D.2
  • 156
    • 0031035380 scopus 로고    scopus 로고
    • Oct-1 and CCAAT/enhancer-binding protein (C/EBP) bind to overlapping elements within the interleukin-8 promotor
    • Wu GD, Lai EJ, Huang N, Wen X (1997) Oct-1 and CCAAT/enhancer-binding protein (C/EBP) bind to overlapping elements within the interleukin-8 promotor. J Biol Chem 272(4):2396-2403.
    • (1997) J Biol Chem , vol.272 , Issue.4 , pp. 2396-2403
    • Wu, G.D.1    Lai, E.J.2    Huang, N.3    Wen, X.4
  • 157
    • 0035830875 scopus 로고    scopus 로고
    • The NF-kappa b repressing factor is involved in basal repression and interleukin (IL)-1-induced activation of IL-8 transcription by binding to a conserved NF-kappa b-flanking sequence element
    • Nourbakhsh M, Kalble S, Dorrie A, Hauser H, Resch K, Kracht M (2001) The NF-kappa b repressing factor is involved in basal repression and interleukin (IL)-1-induced activation of IL-8 transcription by binding to a conserved NF-kappa b-flanking sequence element. J Biol Chem 276(6):4501-4508.
    • (2001) J Biol Chem , vol.276 , Issue.6 , pp. 4501-4508
    • Nourbakhsh, M.1    Kalble, S.2    Dorrie, A.3    Hauser, H.4    Resch, K.5    Kracht, M.6
  • 158
    • 0030990093 scopus 로고    scopus 로고
    • Recombination signal sequence binding protein Jkappa is constitutively bound to the NF-kappaB site of the interleukin-6 promoter and acts as a negative regulatory factor
    • Plaisance S, Vanden Berghe W, Boone E, Fiers W, Haegeman G (1997) Recombination signal sequence binding protein Jkappa is constitutively bound to the NF-kappaB site of the interleukin-6 promoter and acts as a negative regulatory factor. Mol Cell Biol 17(7):3733-3743.
    • (1997) Mol Cell Biol , vol.17 , Issue.7 , pp. 3733-3743
    • Plaisance, S.1    Vanden Berghe, W.2    Boone, E.3    Fiers, W.4    Haegeman, G.5
  • 159
    • 0037126628 scopus 로고    scopus 로고
    • Glucocorticoids inhibit MAP kinase via increased expression and decreased degradation of MKP-1
    • Kassel O, Sancono A, Kratzschmar J, Kreft B, Stassen M, Cato AC (2001) Glucocorticoids inhibit MAP kinase via increased expression and decreased degradation of MKP-1. EMBO J 20(24):7108-7116.
    • (2001) EMBO J , vol.20 , Issue.24 , pp. 7108-7116
    • Kassel, O.1    Sancono, A.2    Kratzschmar, J.3    Kreft, B.4    Stassen, M.5    Cato, A.C.6
  • 160
    • 0035138742 scopus 로고    scopus 로고
    • Dexamethasone destabilizes cyclooxygenase 2 mRNA by inhibiting mitogen-activated protein kinase p38
    • Lasa M, Brook M, Saklatvala J, Clark AR (2001) Dexamethasone destabilizes cyclooxygenase 2 mRNA by inhibiting mitogen-activated protein kinase p38. Mol Cell Biol 21(3):771-778.
    • (2001) Mol Cell Biol , vol.21 , Issue.3 , pp. 771-778
    • Lasa, M.1    Brook, M.2    Saklatvala, J.3    Clark, A.R.4
  • 161
    • 0034687778 scopus 로고    scopus 로고
    • Nitric oxide negatively regulates c-Jun N-terminal kinase/stress-activated protein kinase by means of S-nitrosylation
    • Park HS, Huh SH, Kim MS, Lee SH, Choi EJ (2000) Nitric oxide negatively regulates c-Jun N-terminal kinase/stress-activated protein kinase by means of S-nitrosylation. Proc Natl Acad Sci USA 97(26):14382-14387.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.26 , pp. 14382-14387
    • Park, H.S.1    Huh, S.H.2    Kim, M.S.3    Lee, S.H.4    Choi, E.J.5
  • 162
    • 0034605125 scopus 로고    scopus 로고
    • Glucocorticoids antagonize AP-1 by inhibiting the Activation/phosphorylation of JNK without affecting its subcellular distribution
    • Gonzalez MV, Jimenez B, Berciano MT, Gonzalez-Sancho JM, Caelles C, Lafarga M, Munoz A (2000) Glucocorticoids antagonize AP-1 by inhibiting the Activation/phosphorylation of JNK without affecting its subcellular distribution. J Cell Biol 150(5):1199-1208.
    • (2000) J Cell Biol , vol.150 , Issue.5 , pp. 1199-1208
    • Gonzalez, M.V.1    Jimenez, B.2    Berciano, M.T.3    Gonzalez-Sancho, J.M.4    Caelles, C.5    Lafarga, M.6    Munoz, A.7
  • 163
    • 0032487857 scopus 로고    scopus 로고
    • The anti-inflammatory agents aspirin and salicylate inhibit the activity of I(kappa)B kinase-beta
    • Yin MJ, Yamamoto Y, Gaynor RB (1998) The anti-inflammatory agents aspirin and salicylate inhibit the activity of I(kappa)B kinase-beta. Nature 396(6706):77-80.
    • (1998) Nature , vol.396 , Issue.6706 , pp. 77-80
    • Yin, M.J.1    Yamamoto, Y.2    Gaynor, R.B.3
  • 164
    • 0034610759 scopus 로고    scopus 로고
    • Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IkappaB kinase
    • Rossi A, Kapahi P, Natoli G, Takahashi T, Chen Y, Karin M, Santoro MG (2000) Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IkappaB kinase. Nature 403(6765):103-108.
    • (2000) Nature , vol.403 , Issue.6765 , pp. 103-108
    • Rossi, A.1    Kapahi, P.2    Natoli, G.3    Takahashi, T.4    Chen, Y.5    Karin, M.6    Santoro, M.G.7
  • 165
    • 0033821409 scopus 로고    scopus 로고
    • Glucocorticoid receptor recruitment of histone deacetylase 2 inhibits interleukin-1beta-induced histone H4 acetylation on lysines 8 and 12
    • Ito K, Barnes PJ, Adcock IM (2000) Glucocorticoid receptor recruitment of histone deacetylase 2 inhibits interleukin-1beta-induced histone H4 acetylation on lysines 8 and 12. Mol Cell Biol 20(18):6891-6903.
    • (2000) Mol Cell Biol , vol.20 , Issue.18 , pp. 6891-6903
    • Ito, K.1    Barnes, P.J.2    Adcock, I.M.3
  • 166
    • 0035839497 scopus 로고    scopus 로고
    • p65-activated histone acetyltransferase activity is repressed by glucocorticoids. Mifepristone fails to recruit HDAC2 to the p65-HAT complex
    • Ito K, Jazrawi E, Cosio B, Barnes PJ, Adcock IM (2001) p65-activated histone acetyltransferase activity is repressed by glucocorticoids. Mifepristone fails to recruit HDAC2 to the p65-HAT complex. J Biol Chem 276(32):30208-30215.
    • (2001) J Biol Chem , vol.276 , Issue.32 , pp. 30208-30215
    • Ito, K.1    Jazrawi, E.2    Cosio, B.3    Barnes, P.J.4    Adcock, I.M.5
  • 167
    • 0034284349 scopus 로고    scopus 로고
    • Mechanisms of anti-inflammatory action and of immunosuppression by glucocorticoids: Negative interference of activated glucocorticoid receptor with transcription factors
    • De Bosscher K, Vanden Berghe W, Haegeman G (2000) Mechanisms of anti-inflammatory action and of immunosuppression by glucocorticoids: Negative interference of activated glucocorticoid receptor with transcription factors. J Neuroimmunol 109(1):16-22.
    • (2000) J Neuroimmunol , vol.109 , Issue.1 , pp. 16-22
    • De Bosscher, K.1    Vanden Berghe, W.2    Haegeman, G.3
  • 168
    • 0034636021 scopus 로고    scopus 로고
    • Glucocorticoids repress NF-kappaB-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 (2000) Glucocorticoids repress NF-kappaB-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(8):3919-3924.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.8 , pp. 3919-3924
    • De Bosscher, K.1    Vanden Berghe, W.2    Vermeulen, L.3    Plaisance, S.4    Boone, E.5    Haegeman, G.6
  • 170
    • 0023058975 scopus 로고
    • A conserved AU sequence from the 3′ untranslated region of GM-CSF mRNA mediates selective mRNA degradation
    • Shaw G, Kamen R (1986) A conserved AU sequence from the 3′ untranslated region of GM-CSF mRNA mediates selective mRNA degradation. Cell 46(5):659-667.
    • (1986) Cell , vol.46 , Issue.5 , pp. 659-667
    • Shaw, G.1    Kamen, R.2
  • 171
    • 0035162672 scopus 로고    scopus 로고
    • ARED: Human AU-rich element-containing mRNA database reveals an unexpectedly diverse functional repertoire of encoded proteins
    • Bakheet T, Frevel M, Williams BR, Greer W, Khabar KS (2001) ARED: Human AU-rich element-containing mRNA database reveals an unexpectedly diverse functional repertoire of encoded proteins. Nucleic Acids Res 29(1):246-254.
    • (2001) Nucleic Acids Res , vol.29 , Issue.1 , pp. 246-254
    • Bakheet, T.1    Frevel, M.2    Williams, B.R.3    Greer, W.4    Khabar, K.S.5
  • 172
    • 0030872398 scopus 로고    scopus 로고
    • Modulation of the fate of cytoplasmic mRNA by AU-rich elements: Key sequence features controlling mRNA deadenylation and decay
    • Xu N, Chen CY, Shyu AB (1997) Modulation of the fate of cytoplasmic mRNA by AU-rich elements: Key sequence features controlling mRNA deadenylation and decay. Mol Cell Biol 17(8):4611-4621.
    • (1997) Mol Cell Biol , vol.17 , Issue.8 , pp. 4611-4621
    • Xu, N.1    Chen, C.Y.2    Shyu, A.B.3
  • 173
    • 0034644837 scopus 로고    scopus 로고
    • Regulation of tumour necrosis factor alpha mRNA stability by the mitogen-activated protein kinase p38 signalling cascade
    • Brook M, Sully G, Clark AR, Saklatvala J (2000) Regulation of tumour necrosis factor alpha mRNA stability by the mitogen-activated protein kinase p38 signalling cascade. FEBS Lett 483(1):57-61.
    • (2000) FEBS Lett , vol.483 , Issue.1 , pp. 57-61
    • Brook, M.1    Sully, G.2    Clark, A.R.3    Saklatvala, J.4
  • 174
    • 0029126879 scopus 로고
    • mRNA decay mediated by two distinct AU-rich elements from c-fos and granulocyte-macrophage colony-stimulating factor transcripts: Different dead-enylation kinetics and uncoupling from translation
    • Chen CY, Xu N, Shyu AB (1995) mRNA decay mediated by two distinct AU-rich elements from c-fos and granulocyte-macrophage colony-stimulating factor transcripts: Different dead-enylation kinetics and uncoupling from translation. Mol Cell Biol 15(10):5777-5788.
    • (1995) Mol Cell Biol , vol.15 , Issue.10 , pp. 5777-5788
    • Chen, C.Y.1    Xu, N.2    Shyu, A.B.3
  • 175
    • 0029918710 scopus 로고    scopus 로고
    • Functional characterization of a non-AUUUA AU-rich element from the c-jun proto-oncogene mRNA: Evidence for a novel class of AU-rich elements
    • Peng SS, Chen CY, Shyu AB (1996) Functional characterization of a non-AUUUA AU-rich element from the c-jun proto-oncogene mRNA: Evidence for a novel class of AU-rich elements. Mol Cell Biol 16(4):1490-1499.
    • (1996) Mol Cell Biol , vol.16 , Issue.4 , pp. 1490-1499
    • Peng, S.S.1    Chen, C.Y.2    Shyu, A.B.3
  • 177
    • 0035861864 scopus 로고    scopus 로고
    • Functional link between the mammalian exosome and mRNA decapping
    • Wang Z, Kiledjian M (2001) Functional link between the mammalian exosome and mRNA decapping. Cell 107(6):751-762.
    • (2001) Cell , vol.107 , Issue.6 , pp. 751-762
    • Wang, Z.1    Kiledjian, M.2
  • 178
    • 0035282971 scopus 로고    scopus 로고
    • A novel mRNA-decapping activity in HeLa cytoplasmic extracts is regulated by AU-rich elements
    • Gao M, Wilusz CJ, Peltz SW, Wilusz J (2001) A novel mRNA-decapping activity in HeLa cytoplasmic extracts is regulated by AU-rich elements. EMBO J 20(5):1134-1143.
    • (2001) EMBO J , vol.20 , Issue.5 , pp. 1134-1143
    • Gao, M.1    Wilusz, C.J.2    Peltz, S.W.3    Wilusz, J.4
  • 179
    • 0026648923 scopus 로고
    • Evidence for instability of mRNAs containing AUUUA motifs mediated through translation-dependent assembly of a >20S degradation complex
    • Savant-Bhonsaler S, Cleveland DW (1992) Evidence for instability of mRNAs containing AUUUA motifs mediated through translation-dependent assembly of a >20S degradation complex. Genes & Development 6:1927-1939.
    • (1992) Genes & Development , vol.6 , pp. 1927-1939
    • Savant-Bhonsaler, S.1    Cleveland, D.W.2
  • 180
    • 0028801330 scopus 로고
    • Rapid degradation of AU-rich element (ARE) mRNAs is activated by ribosome transit and blocked by secondary structure at any position 5′ to the ARE
    • Curatola AM, Nadal MS, Schneider RJ (1995) Rapid degradation of AU-rich element (ARE) mRNAs is activated by ribosome transit and blocked by secondary structure at any position 5′ to the ARE. Mol Cell Biol 15(11):6331-6340.
    • (1995) Mol Cell Biol , vol.15 , Issue.11 , pp. 6331-6340
    • Curatola, A.M.1    Nadal, M.S.2    Schneider, R.J.3
  • 181
  • 182
    • 0032515186 scopus 로고    scopus 로고
    • A p38 MAP kinase inhibitor regulates stability of interleukin-1-induced cyclooxygenase-2 mRNA
    • Ridley SH, Dean JL, Sarsfield SJ, Brook M, Clark AR, Saklatvala J (1998) A p38 MAP kinase inhibitor regulates stability of interleukin-1-induced cyclooxygenase-2 mRNA. FEBS Lett 439(1-2):75-80.
    • (1998) FEBS Lett , vol.439 , Issue.1-2 , pp. 75-80
    • Ridley, S.H.1    Dean, J.L.2    Sarsfield, S.J.3    Brook, M.4    Clark, A.R.5    Saklatvala, J.6
  • 183
    • 0032951716 scopus 로고    scopus 로고
    • p38 mitogen-activated protein kinase regulates cyclooxygenase-2 mRNA stability and transcription in lipopolysaccharide-treated human monocytes
    • Dean JLE, Brook M, Clark AR, Saklatvala J (1999) p38 mitogen-activated protein kinase regulates cyclooxygenase-2 mRNA stability and transcription in lipopolysaccharide-treated human monocytes. J Biol Chem 274:264-269.
    • (1999) J Biol Chem , vol.274 , pp. 264-269
    • Dean, J.L.E.1    Brook, M.2    Clark, A.R.3    Saklatvala, J.4
  • 184
    • 0033568608 scopus 로고    scopus 로고
    • The p38 MAP kinase pathway signals for cytokine-induced mRNA stabilization via MAP kinase-activated protein kinase 2 and an AU-rich region-targeted mechanism
    • Winzen R, Kracht M, Ritter B, Wilhelm A, Chen CYA, Shyu AB, Muller M, Gaestel M, Resch K, Holtmann H (1999) The p38 MAP kinase pathway signals for cytokine-induced mRNA stabilization via MAP kinase-activated protein kinase 2 and an AU-rich region-targeted mechanism. EMBO J 18(18):4969-4980.
    • (1999) EMBO J , vol.18 , Issue.18 , pp. 4969-4980
    • Winzen, R.1    Kracht, M.2    Ritter, B.3    Wilhelm, A.4    Chen, C.Y.A.5    Shyu, A.B.6    Muller, M.7    Gaestel, M.8    Resch, K.9    Holtmann, H.10
  • 185
    • 0034077529 scopus 로고    scopus 로고
    • Regulation of cyclooxygenase 2 mRNA stability by the mitogen-activated protein kinase p38 signaling cascade
    • Lasa M, Mahtani KR, Finch A, Brewer G, Saklatvala J, Clark AR (2000) Regulation of cyclooxygenase 2 mRNA stability by the mitogen-activated protein kinase p38 signaling cascade. Mol Cell Biol 20(12):4265-4274.
    • (2000) Mol Cell Biol , vol.20 , Issue.12 , pp. 4265-4274
    • Lasa, M.1    Mahtani, K.R.2    Finch, A.3    Brewer, G.4    Saklatvala, J.5    Clark, A.R.6
  • 186
    • 0032546972 scopus 로고    scopus 로고
    • Stabilization of interleukin-2 mRNA by the c-Jun NH2-terminal kinase pathway
    • Chen CY, Del Gatto-Konczak F, Wu Z, Karin M (1998) Stabilization of interleukin-2 mRNA by the c-Jun NH2-terminal kinase pathway. Science 280(5371):1945-1949.
    • (1998) Science , vol.280 , Issue.5371 , pp. 1945-1949
    • Chen, C.Y.1    Del Gatto-Konczak, F.2    Wu, Z.3    Karin, M.4
  • 187
    • 0034714265 scopus 로고    scopus 로고
    • Stress-activated protein kinases (JNK and p38/HOG) are essential for vascular endothelial growth factor mRNA stability
    • Pages G, Berra E, Milanini J, Levy AP, Pouyssegur J (2000) Stress-activated protein kinases (JNK and p38/HOG) are essential for vascular endothelial growth factor mRNA stability. J Biol Chem 275(34):26484-264891.
    • (2000) J Biol Chem , vol.275 , Issue.34 , pp. 26484-264891
    • Pages, G.1    Berra, E.2    Milanini, J.3    Levy, A.P.4    Pouyssegur, J.5
  • 188
    • 0032033151 scopus 로고    scopus 로고
    • Structure and genomic organization of the human AUF1 gene: Alternative pre-mRNA splicing generates four protein isoforms
    • Wagner BJ, DeMaria CT, Sun Y, Wilson GM, Brewer G (1998) Structure and genomic organization of the human AUF1 gene: Alternative pre-mRNA splicing generates four protein isoforms. Genomics 48(2):195-202.
    • (1998) Genomics , vol.48 , Issue.2 , pp. 195-202
    • Wagner, B.J.1    DeMaria, C.T.2    Sun, Y.3    Wilson, G.M.4    Brewer, G.5
  • 189
    • 0033565383 scopus 로고    scopus 로고
    • Unraveling a cytoplasmic role for hnRNP D in the in vivo mRNA destabilization directed by the AU-rich element
    • Loflin P, Chen CY, Shyu AB (1999) Unraveling a cytoplasmic role for hnRNP D in the in vivo mRNA destabilization directed by the AU-rich element. Genes Dev 13(14):1884-1897.
    • (1999) Genes Dev , vol.13 , Issue.14 , pp. 1884-1897
    • Loflin, P.1    Chen, C.Y.2    Shyu, A.B.3
  • 190
    • 0034806974 scopus 로고    scopus 로고
    • Versatile role for hnRNP D isoforms in the differential regulation of cytoplasmic mRNA turnover
    • Xu N, Chen CY, Shyu AB (2001) Versatile role for hnRNP D isoforms in the differential regulation of cytoplasmic mRNA turnover. Mol Cell Biol 21(20):6960-6971.
    • (2001) Mol Cell Biol , vol.21 , Issue.20 , pp. 6960-6971
    • Xu, N.1    Chen, C.Y.2    Shyu, A.B.3
  • 191
    • 0026337150 scopus 로고
    • An A+U-rich element RNA-binding factor regulates c-myc mRNA stability in vitro
    • Brewer G (1991) An A+U-rich element RNA-binding factor regulates c-myc mRNA stability in vitro. Mol Cell Biol 11(5):2460-2466.
    • (1991) Mol Cell Biol , vol.11 , Issue.5 , pp. 2460-2466
    • Brewer, G.1
  • 192
    • 0032526427 scopus 로고    scopus 로고
    • Overexpression of HuR, a nuclear-cytoplasmic shuttling protein, increases the in vivo stability of ARE-containing mRNAs
    • Fan XC, Steitz JA (1998) Overexpression of HuR, a nuclear-cytoplasmic shuttling protein, increases the in vivo stability of ARE-containing mRNAs. EMBO J 17(12):3448-3460.
    • (1998) EMBO J , vol.17 , Issue.12 , pp. 3448-3460
    • Fan, X.C.1    Steitz, J.A.2
  • 193
    • 0032526417 scopus 로고    scopus 로고
    • RNA stabilization by the AU-rich element binding protein, HuR, an ELAV protein
    • Peng SS, Chen CY, Xu N, Shyu AB (1998) RNA stabilization by the AU-rich element binding protein, HuR, an ELAV protein. EMBO J 17(12):3461-3470.
    • (1998) EMBO J , vol.17 , Issue.12 , pp. 3461-3470
    • Peng, S.S.1    Chen, C.Y.2    Xu, N.3    Shyu, A.B.4
  • 194
    • 0034746363 scopus 로고    scopus 로고
    • The 3′ untranslated region of tumor necrosis factor alpha mRNA is a target of the mRNA-stabilizing factor HuR
    • Dean JL, Wait R, Mahtani KR, Sully G, Clark AR, Saklatvala J (2001) The 3′ untranslated region of tumor necrosis factor alpha mRNA is a target of the mRNA-stabilizing factor HuR. Mol Cell Biol 21(3):721-730.
    • (2001) Mol Cell Biol , vol.21 , Issue.3 , pp. 721-730
    • Dean, J.L.1    Wait, R.2    Mahtani, K.R.3    Sully, G.4    Clark, A.R.5    Saklatvala, J.6
  • 195
    • 0033555659 scopus 로고    scopus 로고
    • ELAV proteins stabilize deadenylated intermediates in a novel in vitro mRNA deadenylation/degradation system
    • Ford LP, Watson J, Keene JD, Wilusz J (1999) ELAV proteins stabilize deadenylated intermediates in a novel in vitro mRNA deadenylation/degradation system. Genes Dev 13(2):188-201.
    • (1999) Genes Dev , vol.13 , Issue.2 , pp. 188-201
    • Ford, L.P.1    Watson, J.2    Keene, J.D.3    Wilusz, J.4
  • 196
    • 0032513043 scopus 로고    scopus 로고
    • Hypoxic stabilization of vascular endothelial growth factor mRNA by the RNA-binding protein HuR
    • Levy NS, Chung S, Furneaux H, Levy AP (1998) Hypoxic stabilization of vascular endothelial growth factor mRNA by the RNA-binding protein HuR. J Biol Chem 273(11):6417-6423.
    • (1998) J Biol Chem , vol.273 , Issue.11 , pp. 6417-6423
    • Levy, N.S.1    Chung, S.2    Furneaux, H.3    Levy, A.P.4
  • 197
    • 0034657686 scopus 로고    scopus 로고
    • HuR regulates cyclin A and cyclin B1 mRNA stability during cell proliferation
    • Wang W, Caldwell MC, Lin S, Furneaux H, Gorospe M (2000) HuR regulates cyclin A and cyclin B1 mRNA stability during cell proliferation. EMBO J 19(10):2340-2350.
    • (2000) EMBO J , vol.19 , Issue.10 , pp. 2340-2350
    • Wang, W.1    Caldwell, M.C.2    Lin, S.3    Furneaux, H.4    Gorospe, M.5
  • 199
    • 0032516626 scopus 로고    scopus 로고
    • Feedback inhibition of macrophage tumor necrosis factor-alpha production by tristetraprolin
    • Carballo E, Lai WS, Blackshear PJ (1998) Feedback inhibition of macrophage tumor necrosis factor-alpha production by tristetraprolin. Science 281(5379):1001-1005.
    • (1998) Science , vol.281 , Issue.5379 , pp. 1001-1005
    • Carballo, E.1    Lai, W.S.2    Blackshear, P.J.3
  • 200
    • 0033049125 scopus 로고    scopus 로고
    • Evidence that tristetraprolin binds to AU-rich elements and promotes the deadenylation and destabilization of tumor necrosis factor alpha mRNA
    • Lai WS, Carballo E, Strum JR, Kennington EA, Phillips RS, Blackshear PJ (1999) Evidence that tristetraprolin binds to AU-rich elements and promotes the deadenylation and destabilization of tumor necrosis factor alpha mRNA. Mol Cell Biol 19(6):4311-4323.
    • (1999) Mol Cell Biol , vol.19 , Issue.6 , pp. 4311-4323
    • Lai, W.S.1    Carballo, E.2    Strum, J.R.3    Kennington, E.A.4    Phillips, R.S.5    Blackshear, P.J.6
  • 201
    • 0034653560 scopus 로고    scopus 로고
    • Evidence that tristetraprolin is a physiological regulator of granulocyte-macrophage colony-stimulating factor messenger RNA deadenylation and stability
    • Carballo E, Lai WS, Blackshear PJ (2000) Evidence that tristetraprolin is a physiological regulator of granulocyte-macrophage colony-stimulating factor messenger RNA deadenylation and stability. Blood 95(6):1891-1899.
    • (2000) Blood , vol.95 , Issue.6 , pp. 1891-1899
    • Carballo, E.1    Lai, W.S.2    Blackshear, P.J.3
  • 202
    • 0034073984 scopus 로고    scopus 로고
    • Somatic mRNA turnover mutants implicate tristetraprolin in the interleukin-3 mRNA degradation pathway
    • Stoecklin G, Ming XF, Looser R, Moroni C (2000) Somatic mRNA turnover mutants implicate tristetraprolin in the interleukin-3 mRNA degradation pathway. Mol Cell Biol 20(11):3753-3763.
    • (2000) Mol Cell Biol , vol.20 , Issue.11 , pp. 3753-3763
    • Stoecklin, G.1    Ming, X.F.2    Looser, R.3    Moroni, C.4
  • 203
    • 0035933724 scopus 로고    scopus 로고
    • Interactions of CCCH zinc finger proteins with mRNA: Tristetraprolin-mediated AU-rich element-dependent mRNA degradation can occur in the absence of a poly(A) tail
    • Lai WS, Blackshear PJ (2001) Interactions of CCCH zinc finger proteins with mRNA: Tristetraprolin-mediated AU-rich element-dependent mRNA degradation can occur in the absence of a poly(A) tail. J Biol Chem 276(25):23144-23154.
    • (2001) J Biol Chem , vol.276 , Issue.25 , pp. 23144-23154
    • Lai, W.S.1    Blackshear, P.J.2
  • 204
    • 0034816062 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase p38 controls the expression and posttranslational modification of tristetraprolin, a regulator of tumor necrosis factor alpha mRNA stability
    • Mahtani KR, Brook M, Dean JL, Sully G, Saklatvala J, Clark AR (2001) Mitogen-activated protein kinase p38 controls the expression and posttranslational modification of tristetraprolin, a regulator of tumor necrosis factor alpha mRNA stability. Mol Cell Biol 21(19):6461-6469.
    • (2001) Mol Cell Biol , vol.21 , Issue.19 , pp. 6461-6469
    • Mahtani, K.R.1    Brook, M.2    Dean, J.L.3    Sully, G.4    Saklatvala, J.5    Clark, A.R.6
  • 205
    • 0035834741 scopus 로고    scopus 로고
    • Decreased sensitivity of tristetraprolin-deficient cells to p38 inhibitors suggests the involvement of tristetraprolin in the p38 signaling pathway
    • Carballo E, Cao H, Lai WS, Kennington EA, Campbell D, Blackshear PJ (2001) Decreased sensitivity of tristetraprolin-deficient cells to p38 inhibitors suggests the involvement of tristetraprolin in the p38 signaling pathway. J Biol Chem 276(45):42580-42587.
    • (2001) J Biol Chem , vol.276 , Issue.45 , pp. 42580-42587
    • Carballo, E.1    Cao, H.2    Lai, W.S.3    Kennington, E.A.4    Campbell, D.5    Blackshear, P.J.6
  • 207
    • 0034907223 scopus 로고    scopus 로고
    • Parallel and independent regulation of interleukin-3 mRNA turn-over by phosphatidylinositol 3-kinase and p38 mitogen-activated protein kinase
    • Ming XF, Stoecklin G, Lu M, Looser R, Moroni C (2001) Parallel and independent regulation of interleukin-3 mRNA turn-over by phosphatidylinositol 3-kinase and p38 mitogen-activated protein kinase. Mol Cell Biol 21(17):5778-5789.
    • (2001) Mol Cell Biol , vol.21 , Issue.17 , pp. 5778-5789
    • Ming, X.F.1    Stoecklin, G.2    Lu, M.3    Looser, R.4    Moroni, C.5
  • 208
    • 0034284362 scopus 로고    scopus 로고
    • The stress-activated MAP kinase Sty1/Spc1 and a 3′-regulatory element mediate UV-induced expression of the uvi15(+) gene at the post-transcriptional level
    • Kim M, Lee W, Park J, Kim JB, Jang YK, Seong RH, Choe SY, Park SD (2000) The stress-activated MAP kinase Sty1/Spc1 and a 3′-regulatory element mediate UV-induced expression of the uvi15(+) gene at the post-transcriptional level. Nucleic Acids Res 28(17):3392-3402.
    • (2000) Nucleic Acids Res , vol.28 , Issue.17 , pp. 3392-3402
    • Kim, M.1    Lee, W.2    Park, J.3    Kim, J.B.4    Jang, Y.K.5    Seong, R.H.6    Choe, S.Y.7    Park, S.D.8
  • 209
    • 0034964525 scopus 로고    scopus 로고
    • Regulated ARE-mediated mRNA decay in Saccharomyces cerevisiae
    • Vasudevan S, Peltz SW (2001) Regulated ARE-mediated mRNA decay in Saccharomyces cerevisiae. Mol Cell 7(6):1191-1200.
    • (2001) Mol Cell , vol.7 , Issue.6 , pp. 1191-1200
    • Vasudevan, S.1    Peltz, S.W.2
  • 210
    • 0024432688 scopus 로고
    • Translational blockade imposed by cytokine-derived UA-rich sequences
    • Kruys V, Marinx O, Shaw G, Deschamps J, Huez G (1989) Translational blockade imposed by cytokine-derived UA-rich sequences. Science 245(4920):852-855.
    • (1989) Science , vol.245 , Issue.4920 , pp. 852-855
    • Kruys, V.1    Marinx, O.2    Shaw, G.3    Deschamps, J.4    Huez, G.5
  • 212
    • 0029090620 scopus 로고
    • Mechanism of action of bicyclic imidazoles defines a translational regulatory pathway for tumor necrosis factor alpha
    • Prichett W, Hand A, Sheilds J, Dunnington D (1995) Mechanism of action of bicyclic imidazoles defines a translational regulatory pathway for tumor necrosis factor alpha. J Inflamm 45(2):97-105.
    • (1995) J Inflamm , vol.45 , Issue.2 , pp. 97-105
    • Prichett, W.1    Hand, A.2    Sheilds, J.3    Dunnington, D.4
  • 214
    • 0033103805 scopus 로고    scopus 로고
    • Impaired on/off regulation of TNF biosynthesis in mice lacking TNF AU- rich elements: Implications for joint and gut-associated immunopathologies
    • Kontoyiannis D, Pasparakis M, Pizarro TT, Cominelli F, Kollias G (1999) Impaired on/off regulation of TNF biosynthesis in mice lacking TNF AU- rich elements: Implications for joint and gut-associated immunopathologies . Immunity 10(3):387-398.
    • (1999) Immunity , vol.10 , Issue.3 , pp. 387-398
    • Kontoyiannis, D.1    Pasparakis, M.2    Pizarro, T.T.3    Cominelli, F.4    Kollias, G.5
  • 215
    • 0034130914 scopus 로고    scopus 로고
    • Molecular mechanisms of glucocorticoid action: What is important?
    • Newton R (2000) Molecular mechanisms of glucocorticoid action: What is important? Thorax 55(7):603-613.
    • (2000) Thorax , vol.55 , Issue.7 , pp. 603-613
    • Newton, R.1
  • 216
    • 0032524357 scopus 로고    scopus 로고
    • New twists in gene regulation by glucocorticoid receptor: Is DNA binding dispensable?
    • Karin M (1998) New twists in gene regulation by glucocorticoid receptor: Is DNA binding dispensable? Cell 93(4):487-490.
    • (1998) Cell , vol.93 , Issue.4 , pp. 487-490
    • Karin, M.1
  • 217
    • 0031455626 scopus 로고    scopus 로고
    • Nuclear hormone receptor antagonism with AP-1 by inhibition of the JNK pathway
    • Caelles C, Gonzalez-Sancho JM, Munoz A (1997) Nuclear hormone receptor antagonism with AP-1 by inhibition of the JNK pathway. Genes Dev 11(24):3351-3364.
    • (1997) Genes Dev , vol.11 , Issue.24 , pp. 3351-3364
    • Caelles, C.1    Gonzalez-Sancho, J.M.2    Munoz, A.3
  • 220
    • 0037040293 scopus 로고    scopus 로고
    • Interleukin (IL)-4 indirectly suppresses IL-2 production by human T lymphocytes via peroxisome proliferator-activated receptor γ activated by macrophage-derived 12/15-lipoxygenase ligands
    • Yang XY, Wang LH, Mihalic K, Xioa W, Chen T, Li P, Wahl LM, Farrar WL (2002) Interleukin (IL)-4 indirectly suppresses IL-2 production by human T lymphocytes via peroxisome proliferator-activated receptor γ activated by macrophage-derived 12/15-lipoxygenase ligands. J Biol Chem 277(6):3973-3978.
    • (2002) J Biol Chem , vol.277 , Issue.6 , pp. 3973-3978
    • Yang, X.Y.1    Wang, L.H.2    Mihalic, K.3    Xioa, W.4    Chen, T.5    Li, P.6    Wahl, L.M.7    Farrar, W.L.8


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