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Volumn 34, Issue 3, 2014, Pages 325-334

Role of Ca2+/calmodulin-dependent kinase II-IRAK1 interaction in LMP1-induced NF-ΚB activation

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 1 RECEPTOR ASSOCIATED KINASE 1; LATENT MEMBRANE PROTEIN 1; TRANSCRIPTION FACTOR RELA; EBV ASSOCIATED MEMBRANE ANTIGEN, EPSTEIN BARR VIRUS; EBV-ASSOCIATED MEMBRANE ANTIGEN, EPSTEIN-BARR VIRUS; INTERLEUKIN 1 RECEPTOR ASSOCIATED KINASE; IRAK1 PROTEIN, MOUSE; MATRIX PROTEIN; SERINE;

EID: 84892453744     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.00912-13     Document Type: Article
Times cited : (26)

References (58)
  • 2
    • 34250010253 scopus 로고    scopus 로고
    • Epstein-Barr virus and its replication
    • Knipe DM, Howley PM, Griffin DE, Lamb RA, Martin MA, Roizman B, Straus SE (ed), 5th ed, vol 2. Lippincott, Williams, and Wilkins, Philadelphia, PA
    • Kieff ED, Rickinson AB. 2007. Epstein-Barr virus and its replication, p 2603-2655. In Knipe DM, Howley PM, Griffin DE, Lamb RA, Martin MA, Roizman B, Straus SE (ed), Fields virology, 5th ed, vol 2. Lippincott, Williams, and Wilkins, Philadelphia, PA.
    • (2007) Fields virology , pp. 2603-2655
    • Kieff, E.D.1    Rickinson, A.B.2
  • 3
    • 0028987479 scopus 로고
    • Stimulation of NF-kappa B-mediated transcription by mutant derivatives of the latent membrane protein of Epstein-Barr virus
    • Mitchell T, Sugden B. 1995. Stimulation of NF-kappa B-mediated transcription by mutant derivatives of the latent membrane protein of Epstein-Barr virus. J. Virol. 69:2968-2976.
    • (1995) J. Virol. , vol.69 , pp. 2968-2976
    • Mitchell, T.1    Sugden, B.2
  • 4
    • 0028853402 scopus 로고
    • The Epstein-Barr virus latent membrane protein-1 (LMP1) mediates activation of NFkappa B and cell surface phenotype via two effector regions in its carboxyterminal cytoplasmic domain
    • Huen DS, Henderson SA, Croom-Carter D, Rowe M. 1995. The Epstein-Barr virus latent membrane protein-1 (LMP1) mediates activation of NFkappa B and cell surface phenotype via two effector regions in its carboxyterminal cytoplasmic domain. Oncogene 10:549-560.
    • (1995) Oncogene , vol.10 , pp. 549-560
    • Huen, D.S.1    Henderson, S.A.2    Croom-Carter, D.3    Rowe, M.4
  • 5
    • 0031718910 scopus 로고    scopus 로고
    • Role of the TRAF binding site and NF-kappaB activation in Epstein-Barr virus latent membrane protein 1-induced cell gene expression
    • Devergne O, Cahir McFarland ED, Mosialos G, Izumi KM, Ware CF, Kieff E. 1998. Role of the TRAF binding site and NF-kappaB activation in Epstein-Barr virus latent membrane protein 1-induced cell gene expression. J. Virol. 72:7900-7908.
    • (1998) J. Virol. , vol.72 , pp. 7900-7908
    • Devergne, O.1    Cahir McFarland, E.D.2    Mosialos, G.3    Izumi, K.M.4    Ware, C.F.5    Kieff, E.6
  • 6
    • 0029956392 scopus 로고    scopus 로고
    • Association of TRAF1, TRAF2, and TRAF3 with an Epstein-Barr virus LMP1 domain important for B-lymphocyte transformation, role in NF-kappaB activation
    • Devergne O, Hatzivassiliou E, Izumi KM, Kaye KM, Kleijnen MF, Kieff E, Mosialos G. 1996. Association of TRAF1, TRAF2, and TRAF3 with an Epstein-Barr virus LMP1 domain important for B-lymphocyte transformation: role in NF-kappaB activation. Mol. Cell. Biol. 16:7098-7108.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 7098-7108
    • Devergne, O.1    Hatzivassiliou, E.2    Izumi, K.M.3    Kaye, K.M.4    Kleijnen, M.F.5    Kieff, E.6    Mosialos, G.7
  • 7
    • 0028878977 scopus 로고
    • The Epstein-Barr virus transforming protein LMP1 engages signaling proteins for the tumor necrosis factor receptor family
    • Mosialos G, Birkenbach M, Yalamanchili R, VanArsdale T, Ware C, Kieff E. 1995. The Epstein-Barr virus transforming protein LMP1 engages signaling proteins for the tumor necrosis factor receptor family. Cell 80: 389-399. http://dx.doi.org/10.1016/0092-8674(95)90489-1.
    • (1995) Cell , vol.80 , pp. 389-399
    • Mosialos, G.1    Birkenbach, M.2    Yalamanchili, R.3    VanArsdale, T.4    Ware, C.5    Kieff, E.6
  • 8
    • 0029785204 scopus 로고    scopus 로고
    • Tumor necrosis factor receptor associated factor 2 is a mediator of NF-kappa B activation by latent infection membrane protein 1, the Epstein-Barr virus transforming protein
    • Kaye KM, Devergne O, Harada JN, Izumi KM, Yalamanchili R, Kieff E, Mosialos G. 1996. Tumor necrosis factor receptor associated factor 2 is a mediator of NF-kappa B activation by latent infection membrane protein 1, the Epstein-Barr virus transforming protein. Proc. Natl. Acad. Sci. U. S. A. 93:11085-11090. http://dx.doi.org/10.1073/pnas.93.20.11085.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 11085-11090
    • Kaye, K.M.1    Devergne, O.2    Harada, J.N.3    Izumi, K.M.4    Yalamanchili, R.5    Kieff, E.6    Mosialos, G.7
  • 9
    • 0028895948 scopus 로고
    • The Epstein-Barr virus LMP1 cytoplasmic carboxy terminus is essential for B-lymphocyte transformation; fibroblast cocultivation complements a critical function within the terminal 155 residues
    • Kaye KM, Izumi KM, Mosialos G, Kieff E. 1995. The Epstein-Barr virus LMP1 cytoplasmic carboxy terminus is essential for B-lymphocyte transformation; fibroblast cocultivation complements a critical function within the terminal 155 residues. J. Virol. 69:675-683.
    • (1995) J. Virol. , vol.69 , pp. 675-683
    • Kaye, K.M.1    Izumi, K.M.2    Mosialos, G.3    Kieff, E.4
  • 10
    • 0032750932 scopus 로고    scopus 로고
    • The residues between the two transformation effector sites of Ep-stein-Barr virus latent membrane protein 1 are not critical for B-lymphocyte growth transformation
    • Izumi KM, Cahir McFarland ED, Riley EA, Rizzo D, Chen Y, Kieff E. 1999. The residues between the two transformation effector sites of Ep-stein-Barr virus latent membrane protein 1 are not critical for B-lymphocyte growth transformation. J. Virol. 73:9908-9916.
    • (1999) J. Virol. , vol.73 , pp. 9908-9916
    • Izumi, K.M.1    Cahir McFarland, E.D.2    Riley, E.A.3    Rizzo, D.4    Chen, Y.5    Kieff, E.6
  • 11
    • 1842484160 scopus 로고    scopus 로고
    • Role of NF-kappa B in cell survival and transcription of latent membrane protein 1-expressing or Epstein-Barr virus latency III-infected cells
    • Cahir-McFarland ED, Carter K, Rosenwald A, Giltnane JM, Henrickson SE, Staudt LM, Kieff E. 2004. Role of NF-kappa B in cell survival and transcription of latent membrane protein 1-expressing or Epstein-Barr virus latency III-infected cells. J. Virol. 78:4108-4119. http://dx.doi.org/10.1128/JVI.78.8.4108-4119.2004.
    • (2004) J. Virol. , vol.78 , pp. 4108-4119
    • Cahir-McFarland, E.D.1    Carter, K.2    Rosenwald, A.3    Giltnane, J.M.4    Henrickson, S.E.5    Staudt, L.M.6    Kieff, E.7
  • 12
    • 0034705110 scopus 로고    scopus 로고
    • NF- kappa B inhibition causes spontaneous apoptosis in Epstein-Barr virus-transformed lymphoblastoid cells
    • Cahir-McFarland ED, Davidson DM, Schauer SL, Duong J, Kieff E. 2000. NF-kappa B inhibition causes spontaneous apoptosis in Epstein-Barr virus-transformed lymphoblastoid cells. Proc. Natl. Acad. Sci. U. S. A. 97:6055-6060. http://dx.doi.org/10.1073/pnas.100119497.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6055-6060
    • Cahir-McFarland, E.D.1    Davidson, D.M.2    Schauer, S.L.3    Duong, J.4    Kieff, E.5
  • 13
    • 0036234459 scopus 로고    scopus 로고
    • Missing pieces in the NF-kappaB puzzle
    • Ghosh S, Karin M. 2002. Missing pieces in the NF-kappaB puzzle. Cell 109(Suppl):S81-S96. http://dx.doi.org/10.1016/S0092-8674(02)00703-1.
    • (2002) Cell , vol.109 , Issue.SUPPL.
    • Ghosh, S.1    Karin, M.2
  • 14
    • 4444376712 scopus 로고    scopus 로고
    • Signaling to NF-kappaB
    • Hayden MS, Ghosh S. 2004. Signaling to NF-kappaB. Genes Dev. 18: 2195-2224. http://dx.doi.org/10.1101/gad.1228704.
    • (2004) Genes Dev , vol.18 , pp. 2195-2224
    • Hayden, M.S.1    Ghosh, S.2
  • 15
    • 2342464085 scopus 로고    scopus 로고
    • The two NF-kappaB activation pathways and their role in innate and adaptive immunity
    • Bonizzi G, Karin M. 2004. The two NF-kappaB activation pathways and their role in innate and adaptive immunity. Trends Immunol. 25:280- 288. http://dx.doi.org/10.1016/j.it.2004.03.008.
    • (2004) Trends Immunol , vol.25 , pp. 280-288
    • Bonizzi, G.1    Karin, M.2
  • 16
    • 0032788548 scopus 로고    scopus 로고
    • The Epstein-Barr virus oncoprotein latent membrane protein 1 engages the tumor necrosis factor receptor-associated proteins TRADD and receptor-interacting protein (RIP) but does not induce apoptosis or require RIP for NF-kappaB activation
    • Izumi KM, Cahir McFarland ED, Ting AT, Riley EA, Seed B, Kieff ED. 1999. The Epstein-Barr virus oncoprotein latent membrane protein 1 engages the tumor necrosis factor receptor-associated proteins TRADD and receptor-interacting protein (RIP) but does not induce apoptosis or require RIP for NF-kappaB activation. Mol. Cell. Biol. 19:5759-5767.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5759-5767
    • Izumi, K.M.1    Cahir McFarland, E.D.2    Ting, A.T.3    Riley, E.A.4    Seed, B.5    Kieff, E.D.6
  • 17
    • 0031038403 scopus 로고    scopus 로고
    • The Epstein-Barr virus LMP1 amino acid sequence that engages tumor necrosis factor receptor associated factors is critical for primary B lymphocyte growth transformation
    • Izumi KM, Kaye KM, Kieff ED. 1997. The Epstein-Barr virus LMP1 amino acid sequence that engages tumor necrosis factor receptor associated factors is critical for primary B lymphocyte growth transformation. Proc. Natl. Acad. Sci. U. S. A. 94:1447-1452. http://dx.doi.org/10.1073/pnas.94.4.1447.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 1447-1452
    • Izumi, K.M.1    Kaye, K.M.2    Kieff, E.D.3
  • 18
    • 0030815756 scopus 로고    scopus 로고
    • The Epstein-Barr virus oncogene product latent membrane protein 1 engages the tumor necrosis factor receptorassociated death domain protein to mediate B lymphocyte growth transformation and activate NF-kappaB
    • Izumi KM, Kieff ED. 1997. The Epstein-Barr virus oncogene product latent membrane protein 1 engages the tumor necrosis factor receptorassociated death domain protein to mediate B lymphocyte growth transformation and activate NF-kappaB. Proc. Natl. Acad. Sci. U. S. A. 94: 12592-12597. http://dx.doi.org/10.1073/pnas.94.23.12592.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 12592-12597
    • Izumi, K.M.1    Kieff, E.D.2
  • 19
    • 57449104909 scopus 로고    scopus 로고
    • IRF7 activation by Epstein-Barr virus latent membrane protein 1 requires localization at activation sites and TRAF6, but not TRAF2 or TRAF3
    • Song YJ, Izumi KM, Shinners NP, Gewurz BE, Kieff E. 2008. IRF7 activation by Epstein-Barr virus latent membrane protein 1 requires localization at activation sites and TRAF6, but not TRAF2 or TRAF3. Proc. Natl. Acad. Sci. U. S. A. 105:18448-18453. http://dx.doi.org/10.1073/pnas.0809933105.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 18448-18453
    • Song, Y.J.1    Izumi, K.M.2    Shinners, N.P.3    Gewurz, B.E.4    Kieff, E.5
  • 20
    • 37549002500 scopus 로고    scopus 로고
    • IRAK1, a critical signaling mediator of innate immunity
    • Gottipati S, Rao NL, Fung-Leung WP. 2008. IRAK1: a critical signaling mediator of innate immunity. Cell. Signal. 20:269-276. http://dx.doi.org/10.1016/j.cellsig.2007.08.009.
    • (2008) Cell. Signal. , vol.20 , pp. 269-276
    • Gottipati, S.1    Rao, N.L.2    Fung-Leung, W.P.3
  • 21
    • 0037292275 scopus 로고    scopus 로고
    • Functional diversity and regulation of different interleukin-1 receptor-associated kinase (IRAK) family members
    • Janssens S, Beyaert R. 2003. Functional diversity and regulation of different interleukin-1 receptor-associated kinase (IRAK) family members. Mol. Cell 11:293-302. http://dx.doi.org/10.1016/S1097-2765(03)00053-4.
    • (2003) Mol. Cell , vol.11 , pp. 293-302
    • Janssens, S.1    Beyaert, R.2
  • 22
    • 0036788753 scopus 로고    scopus 로고
    • Interleukin-1 (IL-1) receptor-associated kinase-dependent IL-1-induced signaling complexes phosphorylate TAK1 and TAB2 at the plasma membrane and activate TAK1 in the cytosol
    • Jiang Z, Ninomiya-Tsuji J, Qian Y, Matsumoto K, Li X. 2002. Interleukin-1 (IL-1) receptor-associated kinase-dependent IL-1-induced signaling complexes phosphorylate TAK1 and TAB2 at the plasma membrane and activate TAK1 in the cytosol. Mol. Cell. Biol. 22:7158-7167. http://dx.doi.org/10.1128/MCB.22.20.7158-7167.2002.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7158-7167
    • Jiang, Z.1    Ninomiya-Tsuji, J.2    Qian, Y.3    Matsumoto, K.4    Li, X.5
  • 23
    • 70350690506 scopus 로고    scopus 로고
    • IRAK1-independent pathways required for the interleukin-1-stimulated activation of the Tpl2 catalytic subunit and its dissociation from ABIN2
    • Handoyo H, Stafford MJ, McManus E, Baltzis D, Peggie M, Cohen P. 2009. IRAK1-independent pathways required for the interleukin-1-stimulated activation of the Tpl2 catalytic subunit and its dissociation from ABIN2. Biochem. J. 424:109-118. http://dx.doi.org/10.1042/BJ20091271.
    • (2009) Biochem. J. , vol.424 , pp. 109-118
    • Handoyo, H.1    Stafford, M.J.2    McManus, E.3    Baltzis, D.4    Peggie, M.5    Cohen, P.6
  • 25
    • 84864083448 scopus 로고    scopus 로고
    • Pellino 2 is critical for Toll-like receptor/interleukin-1 receptor (TLR/IL-1R)-mediated post-transcriptional control
    • Kim TW, Yu M, Zhou H, Cui W, Wang J, DiCorleto P, Fox P, Xiao H, Li X. 2012. Pellino 2 is critical for Toll-like receptor/interleukin-1 receptor (TLR/IL-1R)-mediated post-transcriptional control. J. Biol. Chem. 287: 25686-25695. http://dx.doi.org/10.1074/jbc.M112.352625.
    • (2012) J. Biol. Chem. , vol.287 , pp. 25686-25695
    • Kim, T.W.1    Yu, M.2    Zhou, H.3    Cui, W.4    Wang, J.5    DiCorleto, P.6    Fox, P.7    Xiao, H.8    Li, X.9
  • 26
    • 47249088365 scopus 로고    scopus 로고
    • CpG DNA prevents liver injury and shock-mediated death by modulating expression of interleukin-1 receptor-associated kinases
    • Kim YI, Park JE, Martinez-Hernandez A, Yi AK. 2008. CpG DNA prevents liver injury and shock-mediated death by modulating expression of interleukin-1 receptor-associated kinases. J. Biol. Chem. 283:15258- 15270. http://dx.doi.org/10.1074/jbc.M709549200.
    • (2008) J. Biol. Chem. , vol.283 , pp. 15258-15270
    • Kim, Y.I.1    Park, J.E.2    Martinez-Hernandez, A.3    Yi, A.K.4
  • 28
    • 40749139505 scopus 로고    scopus 로고
    • Interleukin-1 (IL-1) induces the Lys63-linked polyubiquitination of IL-1 receptorassociated kinase 1 to facilitate NEMO binding and the activation of IkappaBalpha kinase
    • Windheim M, Stafford M, Peggie M, Cohen P. 2008. Interleukin-1 (IL-1) induces the Lys63-linked polyubiquitination of IL-1 receptorassociated kinase 1 to facilitate NEMO binding and the activation of IkappaBalpha kinase. Mol. Cell. Biol. 28:1783-1791. http://dx.doi.org/10.1128/MCB.02380-06.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 1783-1791
    • Windheim, M.1    Stafford, M.2    Peggie, M.3    Cohen, P.4
  • 29
    • 43249120917 scopus 로고    scopus 로고
    • Lys63- linked polyubiquitination of IRAK-1 is required for interleukin-1 receptor- and toll-like receptor-mediated NF-kappaB activation
    • Conze DB, Wu CJ, Thomas JA, Landstrom A, Ashwell JD. 2008. Lys63-linked polyubiquitination of IRAK-1 is required for interleukin-1 receptor- and toll-like receptor-mediated NF-kappaB activation. Mol. Cell. Biol. 28:3538-3547. http://dx.doi.org/10.1128/MCB.02098-07.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 3538-3547
    • Conze, D.B.1    Wu, C.J.2    Thomas, J.A.3    Landstrom, A.4    Ashwell, J.D.5
  • 30
    • 0034655280 scopus 로고    scopus 로고
    • IL- 1 receptorassociated kinase modulates host responsiveness to endotoxin
    • Swantek JL, Tsen MF, Cobb MH, Thomas JA. 2000. IL-1 receptorassociated kinase modulates host responsiveness to endotoxin. J. Immunol. 164:4301-4306. http://www.jimmunol.org/content/164/8/4301.
    • (2000) J. Immunol. , vol.164 , pp. 4301-4306
    • Swantek, J.L.1    Tsen, M.F.2    Cobb, M.H.3    Thomas, J.A.4
  • 31
    • 46749110737 scopus 로고    scopus 로고
    • Interleukin-1 receptor-associated kinase (IRAK)-1-mediated NF-kappaB activation requires cytosolic and nuclear activity
    • Liu G, Park YJ, Abraham E. 2008. Interleukin-1 receptor-associated kinase (IRAK)-1-mediated NF-kappaB activation requires cytosolic and nuclear activity. FASEB J. 22:2285-2296. http://dx.doi.org/10.1096/fj.07 -101816.
    • (2008) FASEB J , vol.22 , pp. 2285-2296
    • Liu, G.1    Park, Y.J.2    Abraham, E.3
  • 32
    • 10944228420 scopus 로고    scopus 로고
    • IRAK1 serves as a novel regulator essential for lipopolysaccharide-induced interleukin-10 gene expression
    • Huang Y, Li T, Sane DC, Li L. 2004. IRAK1 serves as a novel regulator essential for lipopolysaccharide-induced interleukin-10 gene expression. J. Biol. Chem. 279:51697-51703. http://dx.doi.org/10.1074/jbc.M410369200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 51697-51703
    • Huang, Y.1    Li, T.2    Sane, D.C.3    Li, L.4
  • 34
    • 84859855891 scopus 로고    scopus 로고
    • The extract of Chrysanthemum indicum Linne inhibits EBV LMP1-induced NF-kappaB activation and the viability of EBV-transformed lymphoblastoid cell lines
    • Kim JE, Jun S, Song M, Kim JH, Song YJ. 2012. The extract of Chrysanthemum indicum Linne inhibits EBV LMP1-induced NF-kappaB activation and the viability of EBV-transformed lymphoblastoid cell lines. Food Chem. Toxicol. 50:1524-1528. http://dx.doi.org/10.1016/j.fct.2012.02.034.
    • (2012) Food Chem. Toxicol. , vol.50 , pp. 1524-1528
    • Kim, J.E.1    Jun, S.2    Song, M.3    Kim, J.H.4    Song, Y.J.5
  • 35
    • 79961112609 scopus 로고    scopus 로고
    • Suppressed induction of proinflammatory cytokines by a unique metabolite produced by Vibrio cholerae O1 El Tor biotype in cultured host cells
    • Bari W, Song YJ, Yoon SS. 2011. Suppressed induction of proinflammatory cytokines by a unique metabolite produced by Vibrio cholerae O1 El Tor biotype in cultured host cells. Infect. Immun. 79:3149-3158. http://dx.doi.org/10.1128/IAI.01237-10.
    • (2011) Infect. Immun. , vol.79 , pp. 3149-3158
    • Bari, W.1    Song, Y.J.2    Yoon, S.S.3
  • 37
    • 0345303850 scopus 로고    scopus 로고
    • Organization and evolution of multifunctional Ca(2)/CaM-dependent protein kinase genes
    • Tombes RM, Faison MO, Turbeville JM. 2003. Organization and evolution of multifunctional Ca(2)/CaM-dependent protein kinase genes. Gene 322:17-31. http://dx.doi.org/10.1016/j.gene.2003.08.023.
    • (2003) Gene , vol.322 , pp. 17-31
    • Tombes, R.M.1    Faison, M.O.2    Turbeville, J.M.3
  • 38
    • 0032584671 scopus 로고    scopus 로고
    • Phosphorylation at the nuclear localization signal of Ca2/calmodulin-dependent protein kinase II blocks its nuclear targeting
    • Heist EK, Srinivasan M, Schulman H. 1998. Phosphorylation at the nuclear localization signal of Ca2/calmodulin-dependent protein kinase II blocks its nuclear targeting. J. Biol. Chem. 273:19763-19771. http://dx.doi.org/10.1074/jbc.273.31.19763.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19763-19771
    • Heist, E.K.1    Srinivasan, M.2    Schulman, H.3
  • 39
    • 2342522110 scopus 로고    scopus 로고
    • Shaping the nuclear action of NF-kappaB
    • Chen LF, Greene WC. 2004. Shaping the nuclear action of NF-kappaB. Nat. Rev. Mol. Cell Biol. 5:392-401. http://dx.doi.org/10.1038/nrm1368.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 392-401
    • Chen, L.F.1    Greene, W.C.2
  • 40
    • 80051988785 scopus 로고    scopus 로고
    • Hierarchies of NF-kappaB target-gene regulation
    • Smale ST. 2011. Hierarchies of NF-kappaB target-gene regulation. Nat. Immunol. 12:689-694. http://dx.doi.org/10.1038/ni.2070.
    • (2011) Nat. Immunol. , vol.12 , pp. 689-694
    • Smale, S.T.1
  • 41
    • 11844269840 scopus 로고    scopus 로고
    • Phosphorylation of NF-kappaB and IkappaB proteins, implications in cancer and inflammation
    • Viatour P, Merville MP, Bours V, Chariot A. 2005. Phosphorylation of NF-kappaB and IkappaB proteins: implications in cancer and inflammation. Trends Biochem. Sci. 30:43-52. http://dx.doi.org/10.1016/j.tibs.2004.11.009.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 43-52
    • Viatour, P.1    Merville, M.P.2    Bours, V.3    Chariot, A.4
  • 42
    • 11244285329 scopus 로고    scopus 로고
    • p65 NF-{kappa}B at serine 536 is mediated by multiple protein kinases including I{kappa}B kinase (IKK)-{alpha}, IKK{beta}, IKK{epsilon}, TRAF family member-associated (TANK)-binding kinase 1 (TBK1)
    • p65 to TATA-binding protein-associated factor II31-mediated interleukin-8 transcription
    • p65 to TATA-binding protein-associated factor II31-mediated interleukin-8 transcription. J. Biol. Chem. 279:55633-55643. http://dx.doi.org/10.1074/jbc.M409825200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 55633-55643
    • Buss, H.1    Dorrie, A.2    Schmitz, M.L.3    Hoffmann, E.4    Resch, K.5    Kracht, M.6
  • 44
    • 0035379555 scopus 로고    scopus 로고
    • p65 Subunit of NF-kappa B through utilization of the Ikappa B kinase and activation of the mitogenactivated protein kinase p38
    • p65 Subunit of NF-kappa B through utilization of the Ikappa B kinase and activation of the mitogenactivated protein kinase p38. J. Biol. Chem. 276:18934-18940. http://dx.doi.org/10.1074/jbc.M101103200.
    • (2001) J. Biol. Chem. , vol.276 , pp. 18934-18940
    • Madrid, L.V.1    Mayo, M.W.2    Reuther, J.Y.3    Baldwin Jr., A.S.4
  • 47
    • 78049438756 scopus 로고    scopus 로고
    • p65 phosphorylation and TNF-induced nuclear translocation of IKK epsilon
    • p65 phosphorylation and TNF-induced nuclear translocation of IKK epsilon. Nucleic Acids Res. 38:6029-6044. http://dx.doi.org/10.1093/nar/gkq439
    • (2010) Nucleic Acids Res , vol.38 , pp. 6029-6044
    • Moreno, R.1    Sobotzik, J.M.2    Schultz, C.3    Schmitz, M.L.4
  • 48
    • 0028917370 scopus 로고
    • The multifunctional calcium/calmodulindependent protein kinase, from form to function
    • Braun AP, Schulman H. 1995. The multifunctional calcium/calmodulindependent protein kinase: from form to function. Annu. Rev. Physiol. 57:417-445. http://dx.doi.org/10.1146/annurev.ph.57.030195.002221.
    • (1995) Annu. Rev. Physiol. , vol.57 , pp. 417-445
    • Braun, A.P.1    Schulman, H.2
  • 49
    • 34247231879 scopus 로고    scopus 로고
    • Bcl10 is phosphorylated on Ser138 by Ca2+/calmodulin-dependent protein kinase II
    • Ishiguro K, Ando T, Goto H, Xavier R. 2007. Bcl10 is phosphorylated on Ser138 by Ca2+/calmodulin-dependent protein kinase II. Mol. Immunol. 44:2095-2100. http://dx.doi.org/10.1016/j.molimm.2006.09.012
    • (2007) Mol. Immunol. , vol.44 , pp. 2095-2100
    • Ishiguro, K.1    Ando, T.2    Goto, H.3    Xavier, R.4
  • 51
    • 58149401211 scopus 로고    scopus 로고
    • CaMKII promotes TLR-triggered proinflammatory cytokine and type I interferon production by directly binding and activating TAK1 and IRF3 in macrophages
    • Liu X, Yao M, Li N, Wang C, Zheng Y, Cao X. 2008. CaMKII promotes TLR-triggered proinflammatory cytokine and type I interferon production by directly binding and activating TAK1 and IRF3 in macrophages. Blood 112:4961-4970. http://dx.doi.org/10.1182/blood-2008-03-144022
    • (2008) Blood , vol.112 , pp. 4961-4970
    • Liu, X.1    Yao, M.2    Li, N.3    Wang, C.4    Zheng, Y.5    Cao, X.6
  • 52
    • 79956327962 scopus 로고    scopus 로고
    • Epstein-Barr virus latent membrane protein 1 increases calcium influx through store-operated channels in B lymphoid cells
    • Dellis O, Arbabian A, Papp B, Rowe M, Joab I, Chomienne C. 2011. Epstein-Barr virus latent membrane protein 1 increases calcium influx through store-operated channels in B lymphoid cells. J. Biol. Chem. 286: 18583-18592. http://dx.doi.org/10.1074/jbc.M111.222257
    • (2011) J. Biol. Chem. , vol.286 , pp. 18583-18592
    • Dellis, O.1    Arbabian, A.2    Papp, B.3    Rowe, M.4    Joab, I.5    Chomienne, C.6
  • 53
    • 0035834704 scopus 로고    scopus 로고
    • Cytosolic targeting domains ofgammaand delta calmodulin-dependent protein kinase II
    • Caran N, Johnson LD, Jenkins KJ, Tombes RM. 2001. Cytosolic targeting domains ofgammaand delta calmodulin-dependent protein kinase II. J. Biol. Chem. 276:42514-42519. http://dx.doi.org/10.1074/jbc.M103013200.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42514-42519
    • Caran, N.1    Johnson, L.D.2    Jenkins, K.J.3    Tombes, R.M.4
  • 54
    • 0034727880 scopus 로고    scopus 로고
    • Induction and alternative splicing of delta isoform of Ca(+_)/calmodulin-dependent protein kinase II during neural differentiation of P19 embryonal carcinoma cells and during brain development
    • Donai H, Murakami T, Amano T, Sogawa Y, Yamauchi T. 2000. Induction and alternative splicing of delta isoform of Ca(+_)/calmodulin-dependent protein kinase II during neural differentiation of P19 embryonal carcinoma cells and during brain development. Brain Res. Mol. Brain Res. 85:189-199. http://dx.doi.org/10.1016/S0169-328X(00)00221-7
    • (2000) Brain Res. Mol Brain Res. , vol.85 , pp. 189-199
    • Donai, H.1    Murakami, T.2    Amano, T.3    Sogawa, Y.4    Yamauchi, T.5
  • 55
    • 0034721606 scopus 로고    scopus 로고
    • Involvement of Ca2+/calmodulin-dependent protein kinase II in neurite outgrowth induced by cAMP treatment and serum deprivation in a central nervous system cell line
    • Donai H, Nakamura M, Sogawa Y, Wang JK, Urushihara M, Yamauchi T. 2000. Involvement of Ca2+/calmodulin-dependent protein kinase II in neurite outgrowth induced by cAMP treatment and serum deprivation in a central nervous system cell line, CAD derived from rat brain. Neurosci. Lett. 293:111-114. http://dx.doi.org/10.1016/S0304-3940(00)01500-7
    • (2000) CAD derived from rat brain. Neurosci. Lett. , vol.293 , pp. 111-114
    • Donai, H.1    Nakamura, M.2    Sogawa, Y.3    Wang, J.K.4    Urushihara, M.5    Yamauchi, T.6
  • 56
    • 0033769156 scopus 로고    scopus 로고
    • delta Ca(2+)/calmodulin-dependent protein kinase II isozyme-specific induction of neurite outgrowth in P19 embryonal carcinoma cells
    • Johnson LD, Willoughby CA, Burke SH, Paik DS, Jenkins KJ, Tombes RM. 2000. delta Ca(2+)/calmodulin-dependent protein kinase II isozyme-specific induction of neurite outgrowth in P19 embryonal carcinoma cells. J. Neurochem. 75:2380-2391. http://dx.doi.org/10.1046/j.1471-4159.2000.0752380.x.
    • (2000) J. Neurochem , vol.75 , pp. 2380-2391
    • Johnson, L.D.1    Willoughby, C.A.2    Burke, S.H.3    Paik, D.S.4    Jenkins, K.J.5    Tombes, R.M.6
  • 57
    • 0038363445 scopus 로고    scopus 로고
    • Nuclear CaMKII inhibits neuronal differentiation of PC12 cells without affecting MAPK or CREB activation
    • Kutcher LW, Beauman SR, Gruenstein EI, Kaetzel MA, Dedman JR. 2003. Nuclear CaMKII inhibits neuronal differentiation of PC12 cells without affecting MAPK or CREB activation. Am. J. Physiol. Cell Physiol. 284:C1334-C1345. http://dx.doi.org/10.1152/ajpcell.00510.2002
    • (2003) Am. J. Physiol. Cell Physiol , vol.284
    • Kutcher, L.W.1    Beauman, S.R.2    Gruenstein, E.I.3    Kaetzel, M.A.4    Dedman, J.R.5


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