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Volumn 73, Issue 6, 2007, Pages 843-853

Inhibition of PI3K and calcineurin suppresses chemoattractant receptor-homologous molecule expressed on Th2 cells (CRTH2)-dependent responses of Th2 lymphocytes to prostaglandin D2

Author keywords

Calcineurin; Chemotaxis; CRTH2; Cytokines; PI3K; Th2 lymphocytes

Indexed keywords

1,4 DIAMINO 1,4 BIS(2 AMINOPHENYLTHIO) 2,3 DICYANOBUTADIENE; 2 (2,4 DICHLOROPHENYL) 3 (1 METHYL 3 INDOLYL)MALEIMIDE; 2 MORPHOLINO 8 PHENYLCHROMONE; 5 (6 CARBOXYHEXYL) 1 (3 CYCLOHEXYL 3 HYDROXYPROPYL)HYDANTOIN; ACTIN; CALCINEURIN; CALCINEURIN INHIBITOR; CALCIUM ION; CHEMOATTRACTANT; CYCLOSPORIN A; GLYCOGEN SYNTHASE KINASE 3BETA; INTERLEUKIN 13; INTERLEUKIN 4; INTERLEUKIN 5; IONOMYCIN; PHOSPHATIDYLINOSITOL 3 KINASE; PROSTAGLANDIN D2; PROTEIN; PROTEIN CRTH2; RAMATROBAN; TACROLIMUS; TRANSCRIPTION FACTOR NFAT; UNCLASSIFIED DRUG;

EID: 33846865609     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2006.11.021     Document Type: Article
Times cited : (34)

References (54)
  • 1
    • 0020001399 scopus 로고
    • Prostaglandin D2 generation after activation of rat and human mast cells with anti-IgE
    • Lewis R.A., Soter N.A., Diamond P.T., Austen K.F., Oates J.A., and Roberts II L.J. Prostaglandin D2 generation after activation of rat and human mast cells with anti-IgE. J Immunol 129 (1982) 1627-1631
    • (1982) J Immunol , vol.129 , pp. 1627-1631
    • Lewis, R.A.1    Soter, N.A.2    Diamond, P.T.3    Austen, K.F.4    Oates, J.A.5    Roberts II, L.J.6
  • 2
    • 0024432264 scopus 로고
    • The major source of endogenous prostaglandin D2 production is likely antigen-presenting cells. Localization of glutathione-requiring prostaglandin D synthetase in histiocytes, dendritic, and Kupffer cells in various rat tissues
    • Urade Y., Ujihara M., Horiguchi Y., Ikai K., and Hayaishi O. The major source of endogenous prostaglandin D2 production is likely antigen-presenting cells. Localization of glutathione-requiring prostaglandin D synthetase in histiocytes, dendritic, and Kupffer cells in various rat tissues. J Immunol 143 (1989) 2982-2989
    • (1989) J Immunol , vol.143 , pp. 2982-2989
    • Urade, Y.1    Ujihara, M.2    Horiguchi, Y.3    Ikai, K.4    Hayaishi, O.5
  • 3
    • 0034161713 scopus 로고    scopus 로고
    • Cutting edge: differential production of prostaglandin D2 by human helper T cell subsets
    • Tanaka K., Ogawa K., Sugamura K., Nakamura M., Takano S., and Nagata K. Cutting edge: differential production of prostaglandin D2 by human helper T cell subsets. J Immunol 164 (2000) 2277-2280
    • (2000) J Immunol , vol.164 , pp. 2277-2280
    • Tanaka, K.1    Ogawa, K.2    Sugamura, K.3    Nakamura, M.4    Takano, S.5    Nagata, K.6
  • 4
    • 0036135587 scopus 로고    scopus 로고
    • Pronounced eosinophilic lung inflammation and Th2 cytokine release in human lipocalin-type prostaglandin D synthase transgenic mice
    • Fujitani Y., Kanaoka Y., Aritake K., Uodome N., Okazaki-Hatake K., and Urade Y. Pronounced eosinophilic lung inflammation and Th2 cytokine release in human lipocalin-type prostaglandin D synthase transgenic mice. J Immunol 168 (2000) 443-449
    • (2000) J Immunol , vol.168 , pp. 443-449
    • Fujitani, Y.1    Kanaoka, Y.2    Aritake, K.3    Uodome, N.4    Okazaki-Hatake, K.5    Urade, Y.6
  • 5
    • 0034534447 scopus 로고    scopus 로고
    • The human prostanoid DP receptor stimulates mucin secretion in LS174T cells
    • Wright D.H., Ford-Hutchinson A.W., Chadee K., and Metters K.M. The human prostanoid DP receptor stimulates mucin secretion in LS174T cells. Br J Pharmacol 131 (2000) 1537-1545
    • (2000) Br J Pharmacol , vol.131 , pp. 1537-1545
    • Wright, D.H.1    Ford-Hutchinson, A.W.2    Chadee, K.3    Metters, K.M.4
  • 7
    • 0242690217 scopus 로고    scopus 로고
    • New targets for allergic rhinitis-a disease of civilization
    • Holgate S.T., and Broide D. New targets for allergic rhinitis-a disease of civilization. Nat Rev Drug Discov. 2 (2003) 1-12
    • (2003) Nat Rev Drug Discov. , vol.2 , pp. 1-12
    • Holgate, S.T.1    Broide, D.2
  • 8
    • 0036467346 scopus 로고    scopus 로고
    • Agonistic effect of indomethacin on a prostaglandin D2 receptor, CRTH2
    • Hirai H., Tanaka K., Takano S., Ichimasa M., Nakamura M., and Nagata K. Agonistic effect of indomethacin on a prostaglandin D2 receptor, CRTH2. J Immunol 168 (2002) 981-985
    • (2002) J Immunol , vol.168 , pp. 981-985
    • Hirai, H.1    Tanaka, K.2    Takano, S.3    Ichimasa, M.4    Nakamura, M.5    Nagata, K.6
  • 9
    • 0038138607 scopus 로고    scopus 로고
    • 2 receptor CRTH2: structure, properties, and functions in leukocytes
    • 2 receptor CRTH2: structure, properties, and functions in leukocytes. Prostaglandins Leukot Essent Fatty Acids 69 (2003) 169-177
    • (2003) Prostaglandins Leukot Essent Fatty Acids , vol.69 , pp. 169-177
    • Nagata, K.1    Hirai, H.2
  • 11
    • 27744514582 scopus 로고    scopus 로고
    • Prostaglandin D2 causes preferential induction of proinflammatory Th2 cytokine production through an action on chemoattractant receptor-like molecule expressed on Th2 cells
    • Xue L., Gyles S.L., Wettey F.R., Gazi L., Townsend E., Hunter M.G., et al. Prostaglandin D2 causes preferential induction of proinflammatory Th2 cytokine production through an action on chemoattractant receptor-like molecule expressed on Th2 cells. J Immunol 175 (2005) 6531-6536
    • (2005) J Immunol , vol.175 , pp. 6531-6536
    • Xue, L.1    Gyles, S.L.2    Wettey, F.R.3    Gazi, L.4    Townsend, E.5    Hunter, M.G.6
  • 12
    • 0035883174 scopus 로고    scopus 로고
    • Prostaglandin D2 is a potent chemoattractant for human eosinophils that acts via a novel DP receptor
    • Monneret G., Gravel S., Diamond M., Rokach J., and Powell W.S. Prostaglandin D2 is a potent chemoattractant for human eosinophils that acts via a novel DP receptor. Blood 98 (2001) 1942-1948
    • (2001) Blood , vol.98 , pp. 1942-1948
    • Monneret, G.1    Gravel, S.2    Diamond, M.3    Rokach, J.4    Powell, W.S.5
  • 16
    • 0035862329 scopus 로고    scopus 로고
    • Prostaglandin D2 selectively induces chemotaxis in T helper type 2 cells, eosinophils, and basophils via seven-transmembrane receptor CRTH2
    • Hirai H., Tanaka K., Yoshie O., Ogawa K., Kenmotsu K., Takamori Y., et al. Prostaglandin D2 selectively induces chemotaxis in T helper type 2 cells, eosinophils, and basophils via seven-transmembrane receptor CRTH2. J Exp Med 193 (2001) 255-261
    • (2001) J Exp Med , vol.193 , pp. 255-261
    • Hirai, H.1    Tanaka, K.2    Yoshie, O.3    Ogawa, K.4    Kenmotsu, K.5    Takamori, Y.6
  • 17
    • 0034653460 scopus 로고    scopus 로고
    • Eotaxin induces degranulation and chemotaxis of eosinophils through the activation of ERK2 and p38 mitogen-activated protein kinases
    • Kampen G.T., Stafford S., Adachi T., Jinquan T., Quan S., Grant J.A., et al. Eotaxin induces degranulation and chemotaxis of eosinophils through the activation of ERK2 and p38 mitogen-activated protein kinases. Blood 95 (2000) 1911-1917
    • (2000) Blood , vol.95 , pp. 1911-1917
    • Kampen, G.T.1    Stafford, S.2    Adachi, T.3    Jinquan, T.4    Quan, S.5    Grant, J.A.6
  • 18
    • 0034635513 scopus 로고    scopus 로고
    • Polarization of chemoattractant receptor signaling during neutrophil chemotaxis
    • Servant G., Weiner O.D., Herzmark P., Balla T., Sedat J.W., and Bourne H.R. Polarization of chemoattractant receptor signaling during neutrophil chemotaxis. Science 287 (2000) 1037-1040
    • (2000) Science , vol.287 , pp. 1037-1040
    • Servant, G.1    Weiner, O.D.2    Herzmark, P.3    Balla, T.4    Sedat, J.W.5    Bourne, H.R.6
  • 19
    • 0033486065 scopus 로고    scopus 로고
    • The CXC chemokine stromal cell-derived factor activates a Gi-coupled phosphoinositide 3-kinase in T lymphocytes
    • Sotsios Y., Whittaker G.C., Westwick J., and Ward S.G. The CXC chemokine stromal cell-derived factor activates a Gi-coupled phosphoinositide 3-kinase in T lymphocytes. J Immunol 163 (1999) 5954-5963
    • (1999) J Immunol , vol.163 , pp. 5954-5963
    • Sotsios, Y.1    Whittaker, G.C.2    Westwick, J.3    Ward, S.G.4
  • 20
    • 9644257220 scopus 로고    scopus 로고
    • Characterization of the MEK5-ERK5 module in human neutrophils and its relationship to ERK1/ERK2 in the chemotactic response
    • Hii C.S., Anson D.S., Costabile M., Mukaro V., Dunning K., and Ferrante A. Characterization of the MEK5-ERK5 module in human neutrophils and its relationship to ERK1/ERK2 in the chemotactic response. J Biol Chem 279 (2004) 49825-49834
    • (2004) J Biol Chem , vol.279 , pp. 49825-49834
    • Hii, C.S.1    Anson, D.S.2    Costabile, M.3    Mukaro, V.4    Dunning, K.5    Ferrante, A.6
  • 21
    • 5644232519 scopus 로고    scopus 로고
    • CD38 cleavage in fMLP- and IL-8-induced chemotaxis is dependent on p38 MAP kinase but independent of p44/42 MAP kinase
    • Fujita T., Zawawi K.H., Kurihara H., and Van Dyke T.E. CD38 cleavage in fMLP- and IL-8-induced chemotaxis is dependent on p38 MAP kinase but independent of p44/42 MAP kinase. Cell Signal 17 (2005) 167-175
    • (2005) Cell Signal , vol.17 , pp. 167-175
    • Fujita, T.1    Zawawi, K.H.2    Kurihara, H.3    Van Dyke, T.E.4
  • 22
    • 0037382497 scopus 로고    scopus 로고
    • An orally bioavailable small molecule antagonist of CRTH2, ramatroban (BAY u3405), inhibits prostaglandin D2-induced eosinophil migration in vitro
    • Sugimoto H., Shichijo M., Iino T., Manabe Y., Watanabe A., Shimazaki M., et al. An orally bioavailable small molecule antagonist of CRTH2, ramatroban (BAY u3405), inhibits prostaglandin D2-induced eosinophil migration in vitro. J Pharmacol Exp Ther 305 (2003) 347-352
    • (2003) J Pharmacol Exp Ther , vol.305 , pp. 347-352
    • Sugimoto, H.1    Shichijo, M.2    Iino, T.3    Manabe, Y.4    Watanabe, A.5    Shimazaki, M.6
  • 23
    • 21344464454 scopus 로고    scopus 로고
    • Signaling to cytoskeletal dynamics during chemotaxis
    • Affolter M., and Weijer C.J. Signaling to cytoskeletal dynamics during chemotaxis. Dev Cell 9 (2005) 19-34
    • (2005) Dev Cell , vol.9 , pp. 19-34
    • Affolter, M.1    Weijer, C.J.2
  • 24
    • 0034190231 scopus 로고    scopus 로고
    • P38 MAP kinase signaling pathways in T cell-mediated immune responses
    • Rincón M., Flavell R.A., Davis R.A., and The J.N.K. P38 MAP kinase signaling pathways in T cell-mediated immune responses. Free Radic Biol Med 28 (2000) 1328-1337
    • (2000) Free Radic Biol Med , vol.28 , pp. 1328-1337
    • Rincón, M.1    Flavell, R.A.2    Davis, R.A.3    The, J.N.K.4
  • 25
    • 0037184088 scopus 로고    scopus 로고
    • Analysis of the life cycle of stat6. Continuous cycling of STAT6 is required for IL-4 signaling
    • Andrews R.P., Ericksen M.B., Cunningham C.M., Daines M.O., and Hershey G.K. Analysis of the life cycle of stat6. Continuous cycling of STAT6 is required for IL-4 signaling. J Biol Chem 277 (2002) 36563-36569
    • (2002) J Biol Chem , vol.277 , pp. 36563-36569
    • Andrews, R.P.1    Ericksen, M.B.2    Cunningham, C.M.3    Daines, M.O.4    Hershey, G.K.5
  • 26
    • 0036781052 scopus 로고    scopus 로고
    • NF-κB regulation in the immune system
    • Li Q., and Verma I.M. NF-κB regulation in the immune system. Nat Rev Immunol 2 (2002) 725-734
    • (2002) Nat Rev Immunol , vol.2 , pp. 725-734
    • Li, Q.1    Verma, I.M.2
  • 28
    • 0347928864 scopus 로고    scopus 로고
    • Rocaglamide derivatives are potent inhibitors of NF-kappa B activation in T-cells
    • Baumann B., Bohnenstengel F., Siegmund D., Wajant H., Weber C., Herr I., et al. Rocaglamide derivatives are potent inhibitors of NF-kappa B activation in T-cells. J Biol Chem 277 (2002) 44791-44800
    • (2002) J Biol Chem , vol.277 , pp. 44791-44800
    • Baumann, B.1    Bohnenstengel, F.2    Siegmund, D.3    Wajant, H.4    Weber, C.5    Herr, I.6
  • 29
    • 0030973579 scopus 로고    scopus 로고
    • Transcription factors of the NFAT family: regulation and function
    • Rao A., Luo C., and Hogan P.G. Transcription factors of the NFAT family: regulation and function. Annu Rev Immunol 15 (1997) 707-747
    • (1997) Annu Rev Immunol , vol.15 , pp. 707-747
    • Rao, A.1    Luo, C.2    Hogan, P.G.3
  • 30
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • Cross D.A., Alessi D.R., Cohen P., Andjelkovich M., and Hemmings B.A. Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 378 (1995) 785-789
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 31
    • 0030890234 scopus 로고    scopus 로고
    • Nuclear export of NF-ATc enhanced by glycogen synthase kinase-3
    • Beals C.R., Sheridan C.M., Turck C.W., Gardner P., and Crabtree G.R. Nuclear export of NF-ATc enhanced by glycogen synthase kinase-3. Science 275 (1997) 1930-1934
    • (1997) Science , vol.275 , pp. 1930-1934
    • Beals, C.R.1    Sheridan, C.M.2    Turck, C.W.3    Gardner, P.4    Crabtree, G.R.5
  • 32
    • 0028334738 scopus 로고
    • A novel phosphoinositide 3 kinase activity in myeloid-derived cells is activated by G protein beta gamma subunits
    • Stephens L., Smrcka A., Cooke F.T., Jackson T.R., Sternweis P.C., and Hawkins P.T. A novel phosphoinositide 3 kinase activity in myeloid-derived cells is activated by G protein beta gamma subunits. Cell 77 (1994) 83-93
    • (1994) Cell , vol.77 , pp. 83-93
    • Stephens, L.1    Smrcka, A.2    Cooke, F.T.3    Jackson, T.R.4    Sternweis, P.C.5    Hawkins, P.T.6
  • 33
    • 0033605718 scopus 로고    scopus 로고
    • The role of phosphoinositide 3-kinase lipid products in cell function
    • Rameh L.E., and Cantley L.C. The role of phosphoinositide 3-kinase lipid products in cell function. J Biol Chem 274 (1999) 8347-8350
    • (1999) J Biol Chem , vol.274 , pp. 8347-8350
    • Rameh, L.E.1    Cantley, L.C.2
  • 34
    • 0034635452 scopus 로고    scopus 로고
    • Central role for G protein-coupled phosphoinositide 3-kinase gamma in inflammation
    • Hirsch E., Katanaev V.L., Garlanda C., Azzolino O., Pirola L., Silengo L., et al. Central role for G protein-coupled phosphoinositide 3-kinase gamma in inflammation. Science 287 (2000) 1049-1053
    • (2000) Science , vol.287 , pp. 1049-1053
    • Hirsch, E.1    Katanaev, V.L.2    Garlanda, C.3    Azzolino, O.4    Pirola, L.5    Silengo, L.6
  • 36
    • 0037135567 scopus 로고    scopus 로고
    • Indomethacin causes prostaglandin D(2)-like and eotaxin-like selective responses in eosinophils and basophils
    • Stubbs V.E., Schratl P., Hartnell A., Williams T.J., Peskar B.A., Heinemann A., et al. Indomethacin causes prostaglandin D(2)-like and eotaxin-like selective responses in eosinophils and basophils. J Biol Chem 277 (2002) 26012-26020
    • (2002) J Biol Chem , vol.277 , pp. 26012-26020
    • Stubbs, V.E.1    Schratl, P.2    Hartnell, A.3    Williams, T.J.4    Peskar, B.A.5    Heinemann, A.6
  • 37
    • 0027178468 scopus 로고
    • Activation of phospholipase C beta 2 by the alpha and beta gamma subunits of trimeric GTP-binding protein
    • Wu D., Katz A., and Simon M.I. Activation of phospholipase C beta 2 by the alpha and beta gamma subunits of trimeric GTP-binding protein. Proc Natl Acad Sci USA 90 (1993) 5297-5301
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 5297-5301
    • Wu, D.1    Katz, A.2    Simon, M.I.3
  • 39
    • 0033779101 scopus 로고    scopus 로고
    • Structure, function, and control of phosphoinositide-specific phospholipase C
    • Rebecchi M.J., and Pentyala S.N. Structure, function, and control of phosphoinositide-specific phospholipase C. Physiol Rev 80 (2000) 1291-1335
    • (2000) Physiol Rev , vol.80 , pp. 1291-1335
    • Rebecchi, M.J.1    Pentyala, S.N.2
  • 41
    • 0027096253 scopus 로고
    • Signal transduction by T-cell receptors: mobilization of Ca and regulation of Ca-dependent effector molecules
    • Premack B.A., and Gardner P. Signal transduction by T-cell receptors: mobilization of Ca and regulation of Ca-dependent effector molecules. Am J Physiol 263 6 Pt 1 (1992) C1119-C1140
    • (1992) Am J Physiol , vol.263 , Issue.6 PART 1
    • Premack, B.A.1    Gardner, P.2
  • 42
    • 0032989834 scopus 로고    scopus 로고
    • T cell antigen-receptor signal transduction
    • van Leeuwen J.E., and Samelson L.E. T cell antigen-receptor signal transduction. Curr Opin Immunol 11 (1999) 242-248
    • (1999) Curr Opin Immunol , vol.11 , pp. 242-248
    • van Leeuwen, J.E.1    Samelson, L.E.2
  • 43
    • 0030899131 scopus 로고    scopus 로고
    • Nuclear localization of NF-ATc by a calcineurin-dependent, cyclosporin-sensitive intramolecular interaction
    • Beals C.R., Clipstone N.A., Ho S.N., and Crabtree G.R. Nuclear localization of NF-ATc by a calcineurin-dependent, cyclosporin-sensitive intramolecular interaction. Genes Dev 11 (1997) 824-834
    • (1997) Genes Dev , vol.11 , pp. 824-834
    • Beals, C.R.1    Clipstone, N.A.2    Ho, S.N.3    Crabtree, G.R.4
  • 45
    • 0031415048 scopus 로고    scopus 로고
    • Down-regulation of IL-4 gene transcription and control of Th2 cell differentiation by a mechanism involving NFAT1
    • Kiani A., Viola J.P., Lichtman A.H., and Rao A. Down-regulation of IL-4 gene transcription and control of Th2 cell differentiation by a mechanism involving NFAT1. Immunity 7 (1997) 849-860
    • (1997) Immunity , vol.7 , pp. 849-860
    • Kiani, A.1    Viola, J.P.2    Lichtman, A.H.3    Rao, A.4
  • 46
    • 0031933037 scopus 로고    scopus 로고
    • Delayed lymphoid repopulation with defects in IL-4-driven responses produced by inactivation of NF-ATc
    • Ranger A.M., Hodge M.R., Gravallese E.M., Oukka M., Davidson L., Alt F.W., et al. Delayed lymphoid repopulation with defects in IL-4-driven responses produced by inactivation of NF-ATc. Immunity 8 (1998) 125-134
    • (1998) Immunity , vol.8 , pp. 125-134
    • Ranger, A.M.1    Hodge, M.R.2    Gravallese, E.M.3    Oukka, M.4    Davidson, L.5    Alt, F.W.6
  • 47
    • 0031951071 scopus 로고    scopus 로고
    • The transcription factor NF-ATc1 regulates lymphocyte proliferation and Th2 cytokine production
    • Yoshida H., Nishina H., Takimoto H., Marengere L.E., Wakeham A.C., Bouchard D., et al. The transcription factor NF-ATc1 regulates lymphocyte proliferation and Th2 cytokine production. Immunity 8 (1998) 115-124
    • (1998) Immunity , vol.8 , pp. 115-124
    • Yoshida, H.1    Nishina, H.2    Takimoto, H.3    Marengere, L.E.4    Wakeham, A.C.5    Bouchard, D.6
  • 48
    • 0035477020 scopus 로고    scopus 로고
    • GSK3 takes centre stage more than 20 years after its discovery
    • Frame S., and Cohen P. GSK3 takes centre stage more than 20 years after its discovery. Biochem J 359 (2001) 1-16
    • (2001) Biochem J , vol.359 , pp. 1-16
    • Frame, S.1    Cohen, P.2
  • 49
    • 0026029808 scopus 로고
    • Activation of protein kinase C decreases phosphorylation of c-Jun at sites that negatively regulate its DNA-binding activity
    • Boyle W.J., Smeal T., Defize L.H., Angel P., Woodgett J.R., Karin M., et al. Activation of protein kinase C decreases phosphorylation of c-Jun at sites that negatively regulate its DNA-binding activity. Cell 64 (1991) 573-584
    • (1991) Cell , vol.64 , pp. 573-584
    • Boyle, W.J.1    Smeal, T.2    Defize, L.H.3    Angel, P.4    Woodgett, J.R.5    Karin, M.6
  • 50
    • 0029664368 scopus 로고    scopus 로고
    • Binding of GSK3beta to the APC-beta-catenin complex and regulation of complex assembly
    • Rubinfeld B., Albert I., Porfiri E., Fiol C., Munemitsu S., and Polakis P. Binding of GSK3beta to the APC-beta-catenin complex and regulation of complex assembly. Science 272 (1996) 1023-1026
    • (1996) Science , vol.272 , pp. 1023-1026
    • Rubinfeld, B.1    Albert, I.2    Porfiri, E.3    Fiol, C.4    Munemitsu, S.5    Polakis, P.6
  • 51
    • 0027383378 scopus 로고
    • Phosphorylation sites mapping in the N-terminal domain of c-myc modulate its transforming potential
    • Henriksson M., Bakardjiev A., Klein G., and Luscher B. Phosphorylation sites mapping in the N-terminal domain of c-myc modulate its transforming potential. Oncogene 8 (1993) 3199-3209
    • (1993) Oncogene , vol.8 , pp. 3199-3209
    • Henriksson, M.1    Bakardjiev, A.2    Klein, G.3    Luscher, B.4
  • 52
    • 0034235776 scopus 로고    scopus 로고
    • Wnt-1 dependent activation of the survival factor NF-kappaB in PC12 cells
    • Bournat J.C., Brown A.M., and Soler A.P. Wnt-1 dependent activation of the survival factor NF-kappaB in PC12 cells. J Neurosci Res 61 (2000) 21-32
    • (2000) J Neurosci Res , vol.61 , pp. 21-32
    • Bournat, J.C.1    Brown, A.M.2    Soler, A.P.3
  • 53
    • 0033773645 scopus 로고    scopus 로고
    • Opposing actions of phosphatidylinositol 3-kinase and glycogen synthase kinase-3beta in the regulation of HSF-1 activity
    • Bijur G.N., and Jope R.S. Opposing actions of phosphatidylinositol 3-kinase and glycogen synthase kinase-3beta in the regulation of HSF-1 activity. J Neurochem 75 (2000) 2401-2408
    • (2000) J Neurochem , vol.75 , pp. 2401-2408
    • Bijur, G.N.1    Jope, R.S.2
  • 54
    • 0034806590 scopus 로고    scopus 로고
    • CREB DNA binding activity is inhibited by glycogen synthase kinase-3 beta and facilitated by lithium
    • Grimes C.A., and Jope R.S. CREB DNA binding activity is inhibited by glycogen synthase kinase-3 beta and facilitated by lithium. J Neurochem 78 (2001) 1219-1232
    • (2001) J Neurochem , vol.78 , pp. 1219-1232
    • Grimes, C.A.1    Jope, R.S.2


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