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Volumn 41, Issue 2, 2011, Pages 149-159

Mitogen-activated protein kinase signalling and ERK1/2 bistability in asthma

Author keywords

[No Author keywords available]

Indexed keywords

CHEMOKINE; CYTOKINE; HOUSE DUST ALLERGEN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE KINASE 2; STRESS ACTIVATED PROTEIN KINASE; SYNAPTOPHYSIN;

EID: 78651442474     PISSN: 09547894     EISSN: 13652222     Source Type: Journal    
DOI: 10.1111/j.1365-2222.2010.03658.x     Document Type: Review
Times cited : (91)

References (130)
  • 2
    • 61849123548 scopus 로고    scopus 로고
    • Regulation of the immune response by stress-activated protein kinases
    • Rincón M, Davis RJ. Regulation of the immune response by stress-activated protein kinases. Immunol Rev 2009; 228:212-24.
    • (2009) Immunol Rev , vol.228 , pp. 212-224
    • Rincón, M.1    Davis, R.J.2
  • 3
    • 59749095198 scopus 로고    scopus 로고
    • Protein scaffolds in MAP kinase signalling
    • Brown MD, Sacks DB. Protein scaffolds in MAP kinase signalling. Cell Signal 2009; 21:462-9.
    • (2009) Cell Signal , vol.21 , pp. 462-469
    • Brown, M.D.1    Sacks, D.B.2
  • 4
    • 0242300107 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase 2 is necessary for mesoderm differentiation
    • Yao Y, Li W, Wu J et al. Extracellular signal-regulated kinase 2 is necessary for mesoderm differentiation. Proc Natl Acad Sci USA 2003; 100:12759-64.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 12759-12764
    • Yao, Y.1    Li, W.2    Wu, J.3
  • 5
    • 41549119065 scopus 로고    scopus 로고
    • Cell-specific activation profile of extracellular signal-regulated kinase 1/2, Jun N-terminal kinase, and p38 mitogen-activated protein kinases in asthmatic airways
    • Liu W, Liang Q, Balzar S, Wenzel S, Gorska M, Alam R. Cell-specific activation profile of extracellular signal-regulated kinase 1/2, Jun N-terminal kinase, and p38 mitogen-activated protein kinases in asthmatic airways. J Allergy Clin Immunol 2008; 121:893-902.
    • (2008) J Allergy Clin Immunol , vol.121 , pp. 893-902
    • Liu, W.1    Liang, Q.2    Balzar, S.3    Wenzel, S.4    Gorska, M.5    Alam, R.6
  • 6
    • 0344196985 scopus 로고    scopus 로고
    • Regulation of IL-4 expression by the transcription factor JunB during T helper cell differentiation
    • Li B, Tournier C, Davis RJ, Flavell RA. Regulation of IL-4 expression by the transcription factor JunB during T helper cell differentiation. EMBO J 1999; 18:420-32.
    • (1999) EMBO J , vol.18 , pp. 420-432
    • Li, B.1    Tournier, C.2    Davis, R.J.3    Flavell, R.A.4
  • 7
    • 77952902183 scopus 로고    scopus 로고
    • Ligand-specific c-Fos expression emerges from the spatiotemporal control of ErbB network dynamics
    • Nakakuki T, Birtwistle MR, Saeki Y et al. Ligand-specific c-Fos expression emerges from the spatiotemporal control of ErbB network dynamics. Cell 2010; 141:884-96.
    • (2010) Cell , vol.141 , pp. 884-896
    • Nakakuki, T.1    Birtwistle, M.R.2    Saeki, Y.3
  • 9
    • 0033602147 scopus 로고    scopus 로고
    • Conserved function of mSpry-2, a murine homolog of Drosophila sprouty, which negatively modulates respiratory organogenesis
    • Tefft JD, Lee M, Smith S et al. Conserved function of mSpry-2, a murine homolog of Drosophila sprouty, which negatively modulates respiratory organogenesis. Curr Biol 1999; 9:219-22.
    • (1999) Curr Biol , vol.9 , pp. 219-222
    • Tefft, J.D.1    Lee, M.2    Smith, S.3
  • 10
    • 77951196142 scopus 로고    scopus 로고
    • Effect of p38 MAPK inhibition on corticosteroid suppression of cytokine release in severe asthma
    • Bhavsar P, Khorasani N, Hew M, Johnson M, Chung KF. Effect of p38 MAPK inhibition on corticosteroid suppression of cytokine release in severe asthma. Eur Respir J 2010; 35:750-6.
    • (2010) Eur Respir J , vol.35 , pp. 750-756
    • Bhavsar, P.1    Khorasani, N.2    Hew, M.3    Johnson, M.4    Chung, K.F.5
  • 11
    • 33746616816 scopus 로고    scopus 로고
    • Importance of p38 mitogen-activated protein kinase pathway in allergic airway remodelling and bronchial hyperresponsiveness
    • Nath P, Leung SY, Williams A et al. Importance of p38 mitogen-activated protein kinase pathway in allergic airway remodelling and bronchial hyperresponsiveness. Eur J Pharmacol 2006; 544:160-7.
    • (2006) Eur J Pharmacol , vol.544 , pp. 160-167
    • Nath, P.1    Leung, S.Y.2    Williams, A.3
  • 12
    • 0043011579 scopus 로고    scopus 로고
    • IL-13-induced changes in the goblet cell density of human bronchial epithelial cell cultures
    • Am J Physiol Lung Cell Mol Physiol
    • Atherton HC, Jones G, Danahay H. IL-13-induced changes in the goblet cell density of human bronchial epithelial cell cultures: MAP kinase and phosphatidylinositol 3-kinase regulation. Am J Physiol Lung Cell Mol Physiol 2003; 285:L730-9.
    • (2003) MAP kinase and phosphatidylinositol 3-kinase regulation , vol.285
    • Atherton, H.C.1    Jones, G.2    Danahay, H.3
  • 13
    • 0033560126 scopus 로고    scopus 로고
    • Pulmonary expression of interleukin-13 causes inflammation, mucus hypersecretion, subepithelial fibrosis, physiologic abnormalities, and eotaxin production
    • Zhu Z, Homer RJ, Wang Z et al. Pulmonary expression of interleukin-13 causes inflammation, mucus hypersecretion, subepithelial fibrosis, physiologic abnormalities, and eotaxin production. J Clin Invest 1999; 103:779-88.
    • (1999) J Clin Invest , vol.103 , pp. 779-788
    • Zhu, Z.1    Homer, R.J.2    Wang, Z.3
  • 14
    • 31044435286 scopus 로고    scopus 로고
    • ERK1/2 mitogen-activated protein kinase selectively mediates IL-13-induced lung inflammation and remodeling in vivo
    • Lee PJ, Zhang X, Shan P et al. ERK1/2 mitogen-activated protein kinase selectively mediates IL-13-induced lung inflammation and remodeling in vivo. J Clin Invest 2006; 116:163-73.
    • (2006) J Clin Invest , vol.116 , pp. 163-173
    • Lee, P.J.1    Zhang, X.2    Shan, P.3
  • 15
    • 70350447528 scopus 로고    scopus 로고
    • Pathogenicity of a disease-associated human IL-4 receptor allele in experimental asthma
    • Tachdjian R, Mathias C, Al Khatib S et al. Pathogenicity of a disease-associated human IL-4 receptor allele in experimental asthma. J Exp Med 2009; 206:2191-204.
    • (2009) J Exp Med , vol.206 , pp. 2191-2204
    • Tachdjian, R.1    Mathias, C.2    Al Khatib, S.3
  • 16
    • 0030734010 scopus 로고    scopus 로고
    • p38 MAP kinase activation by vascular endothelial growth factor mediates actin reorganization and cell migration in human endothelial cells
    • Rousseau S, Houle F, Landry J, Huot J. p38 MAP kinase activation by vascular endothelial growth factor mediates actin reorganization and cell migration in human endothelial cells. Oncogene 1997; 15:2169-77.
    • (1997) Oncogene , vol.15 , pp. 2169-2177
    • Rousseau, S.1    Houle, F.2    Landry, J.3    Huot, J.4
  • 18
    • 3342885962 scopus 로고    scopus 로고
    • p38 Mitogen-activated protein kinase mediates synergistic induction of inducible nitric-oxide synthase by lipopolysaccharide and interferon-gamma through signal transducer and activator of transcription 1 Ser727 phosphorylation in murine aortic endothelial cells
    • Huang H, Rose JL, Hoyt DG. p38 Mitogen-activated protein kinase mediates synergistic induction of inducible nitric-oxide synthase by lipopolysaccharide and interferon-gamma through signal transducer and activator of transcription 1 Ser727 phosphorylation in murine aortic endothelial cells. Mol Pharmacol 2004; 66:302-11.
    • (2004) Mol Pharmacol , vol.66 , pp. 302-311
    • Huang, H.1    Rose, J.L.2    Hoyt, D.G.3
  • 19
  • 20
    • 77952758245 scopus 로고    scopus 로고
    • IL-17 promotes p38 MAPK-dependent endothelial activation enhancing neutrophil recruitment to sites of inflammation
    • Roussel L, Houle F, Chan C et al. IL-17 promotes p38 MAPK-dependent endothelial activation enhancing neutrophil recruitment to sites of inflammation. J Immunol 2010; 184:4531-7.
    • (2010) J Immunol , vol.184 , pp. 4531-4537
    • Roussel, L.1    Houle, F.2    Chan, C.3
  • 21
    • 0034641614 scopus 로고    scopus 로고
    • Essential role for p38alpha mitogen-activated protein kinase in placental angiogenesis
    • Mudgett JS, Ding J, Guh-Siesel L et al. Essential role for p38alpha mitogen-activated protein kinase in placental angiogenesis. Proc Natl Acad Sci USA 2000; 97:10454-9.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10454-10459
    • Mudgett, J.S.1    Ding, J.2    Guh-Siesel, L.3
  • 22
    • 0034050739 scopus 로고    scopus 로고
    • Mekk3 is essential for early embryonic cardiovascular development
    • Yang J, Boerm M, McCarty M et al. Mekk3 is essential for early embryonic cardiovascular development. Nat Genet 2000; 24:309-13.
    • (2000) Nat Genet , vol.24 , pp. 309-313
    • Yang, J.1    Boerm, M.2    McCarty, M.3
  • 23
    • 34447258367 scopus 로고    scopus 로고
    • MK2 controls the level of negative feedback in the NF-kappaB pathway and is essential for vascular permeability and airway inflammation
    • Gorska MM, Liang Q, Stafford SJ et al. MK2 controls the level of negative feedback in the NF-kappaB pathway and is essential for vascular permeability and airway inflammation. J Exp Med 2007; 204:1637-52.
    • (2007) J Exp Med , vol.204 , pp. 1637-1652
    • Gorska, M.M.1    Liang, Q.2    Stafford, S.J.3
  • 24
    • 46849108130 scopus 로고    scopus 로고
    • The p38 mitogen-activated protein kinase (MAPK) pathway in rheumatoid arthritis
    • Schett G, Zwerina J, Firestein G. The p38 mitogen-activated protein kinase (MAPK) pathway in rheumatoid arthritis. Ann Rheum Dis 2008; 67:909-16.
    • (2008) Ann Rheum Dis , vol.67 , pp. 909-916
    • Schett, G.1    Zwerina, J.2    Firestein, G.3
  • 25
    • 0037044735 scopus 로고    scopus 로고
    • Cytoskeletal changes in hypoxic pulmonary endothelial cells are dependent on MAPK-activated protein kinase MK2
    • Kayyali US, Pennella CM, Trujillo C, Villa O, Gaestel M, Hassoun PM. Cytoskeletal changes in hypoxic pulmonary endothelial cells are dependent on MAPK-activated protein kinase MK2. J Biol Chem 2002; 277:42596-602.
    • (2002) J Biol Chem , vol.277 , pp. 42596-42602
    • Kayyali, U.S.1    Pennella, C.M.2    Trujillo, C.3    Villa, O.4    Gaestel, M.5    Hassoun, P.M.6
  • 26
    • 0028806565 scopus 로고
    • Identification of novel phosphorylation sites required for activation of MAPKAP kinase-2
    • Ben-Levy R, Leighton IA, Doza YN et al. Identification of novel phosphorylation sites required for activation of MAPKAP kinase-2. EMBO J 1995; 14:5920-30.
    • (1995) EMBO J , vol.14 , pp. 5920-5930
    • Ben-Levy, R.1    Leighton, I.A.2    Doza, Y.N.3
  • 27
    • 0033145354 scopus 로고    scopus 로고
    • MAPKAP kinase 2 is essential for LPS-induced TNF-alpha biosynthesis
    • Kotlyarov A, Neininger A, Schubert C et al. MAPKAP kinase 2 is essential for LPS-induced TNF-alpha biosynthesis. Nat Cell Biol 1999; 1:94-7.
    • (1999) Nat Cell Biol , vol.1 , pp. 94-97
    • Kotlyarov, A.1    Neininger, A.2    Schubert, C.3
  • 29
    • 26444435364 scopus 로고    scopus 로고
    • A TNF-induced gene expression program under oscillatory NF-kappaB control
    • Tian B, Nowak DE, Brasier AR. A TNF-induced gene expression program under oscillatory NF-kappaB control. BMC Genomics 2005; 6:137-54.
    • (2005) BMC Genomics , vol.6 , pp. 137-154
    • Tian, B.1    Nowak, D.E.2    Brasier, A.R.3
  • 30
    • 0037451357 scopus 로고    scopus 로고
    • Transcriptional activation of the NF-kappaB p65 subunit by mitogen- and stress-activated protein kinase-1 (MSK1)
    • Vermeulen L, De Wilde G, Van Damme P, Vanden Berghe W, Haegeman G. Transcriptional activation of the NF-kappaB p65 subunit by mitogen- and stress-activated protein kinase-1 (MSK1). EMBO J 2003; 22:1313-24.
    • (2003) EMBO J , vol.22 , pp. 1313-1324
    • Vermeulen, L.1    De Wilde, G.2    Van Damme, P.3    Vanden Berghe, W.4    Haegeman, G.5
  • 32
    • 0032479983 scopus 로고    scopus 로고
    • Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB
    • Deak M, Clifton AD, Lucocq LM, Alessi DR. Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB. EMBO J 1998; 17:4426-41.
    • (1998) EMBO J , vol.17 , pp. 4426-4441
    • Deak, M.1    Clifton, A.D.2    Lucocq, L.M.3    Alessi, D.R.4
  • 33
    • 0032563807 scopus 로고    scopus 로고
    • Nuclear export of the stress-activated protein kinase p38 mediated by its substrate MAPKAP kinase-2
    • Ben-Levy R, Hooper S, Wilson R, Paterson HF, Marshall CJ. Nuclear export of the stress-activated protein kinase p38 mediated by its substrate MAPKAP kinase-2. Curr Biol 1998; 8:1049-57.
    • (1998) Curr Biol , vol.8 , pp. 1049-1057
    • Ben-Levy, R.1    Hooper, S.2    Wilson, R.3    Paterson, H.F.4    Marshall, C.J.5
  • 34
    • 36348954401 scopus 로고    scopus 로고
    • Systemic deficiency of the MAP kinase-activated protein kinase 2 reduces atherosclerosis in hypercholesterolemic mice
    • Jagavelu K, Tietge UJ, Gaestel M, Drexler H, Schieffer B, Bavendiek U. Systemic deficiency of the MAP kinase-activated protein kinase 2 reduces atherosclerosis in hypercholesterolemic mice. Circ Res 2007; 101:1104-12.
    • (2007) Circ Res , vol.101 , pp. 1104-1112
    • Jagavelu, K.1    Tietge, U.J.2    Gaestel, M.3    Drexler, H.4    Schieffer, B.5    Bavendiek, U.6
  • 35
    • 0032191837 scopus 로고    scopus 로고
    • Differential roles of ERK and p38 MAP kinase pathways in positive and negative selection of T lymphocytes
    • Sugawara T, Moriguchi T, Nishida E, Takahama Y. Differential roles of ERK and p38 MAP kinase pathways in positive and negative selection of T lymphocytes. Immunity 1998; 9:565-74.
    • (1998) Immunity , vol.9 , pp. 565-574
    • Sugawara, T.1    Moriguchi, T.2    Nishida, E.3    Takahama, Y.4
  • 36
    • 0034720881 scopus 로고    scopus 로고
    • A motif in the alphabeta T-cell receptor controls positive selection by modulating ERK activity
    • Werlen G, Hausmann B, Palmer E. A motif in the alphabeta T-cell receptor controls positive selection by modulating ERK activity. Nature 2000; 406:422-6.
    • (2000) Nature , vol.406 , pp. 422-426
    • Werlen, G.1    Hausmann, B.2    Palmer, E.3
  • 39
    • 17144458301 scopus 로고    scopus 로고
    • Defective thymocyte maturation in p44 MAP kinase (Erk 1) knockout mice
    • Pagès G, Guérin S, Grall D et al. Defective thymocyte maturation in p44 MAP kinase (Erk 1) knockout mice. Science 1999; 286:1374-7.
    • (1999) Science , vol.286 , pp. 1374-1377
    • Pagès, G.1    Guérin, S.2    Grall, D.3
  • 40
    • 23444444748 scopus 로고    scopus 로고
    • ERK1-deficient mice show normal T cell effector function and are highly susceptible to experimental autoimmune encephalomyelitis
    • Nekrasova T, Shive C, Gao Y et al. ERK1-deficient mice show normal T cell effector function and are highly susceptible to experimental autoimmune encephalomyelitis. J Immunol 2005; 175:2374-80.
    • (2005) J Immunol , vol.175 , pp. 2374-2380
    • Nekrasova, T.1    Shive, C.2    Gao, Y.3
  • 41
    • 33646470960 scopus 로고    scopus 로고
    • ERK1-/- mice exhibit Th1 cell polarization and increased susceptibility to experimental autoimmune encephalomyelitis
    • Agrawal A, Dillon S, Denning TL, Pulendran B. ERK1-/- mice exhibit Th1 cell polarization and increased susceptibility to experimental autoimmune encephalomyelitis. J Immunol 2006; 176:5788-96.
    • (2006) J Immunol , vol.176 , pp. 5788-5796
    • Agrawal, A.1    Dillon, S.2    Denning, T.L.3    Pulendran, B.4
  • 42
    • 77955980932 scopus 로고    scopus 로고
    • The TCR-mediated signaling pathways that control the direction of helper T cell differentiation
    • Nakayama T, Yamashita M. The TCR-mediated signaling pathways that control the direction of helper T cell differentiation. Semin Immunol 2010; 22:303-9.
    • (2010) Semin Immunol , vol.22 , pp. 303-309
    • Nakayama, T.1    Yamashita, M.2
  • 43
    • 0033514317 scopus 로고    scopus 로고
    • T cell antigen receptor-mediated activation of the Ras/mitogen-activated protein kinase pathway controls interleukin 4 receptor function and type-2 helper T cell differentiation
    • Yamashita M, Kimura M, Kubo M et al. T cell antigen receptor-mediated activation of the Ras/mitogen-activated protein kinase pathway controls interleukin 4 receptor function and type-2 helper T cell differentiation. Proc Natl Acad Sci USA 1999; 96:1024-9.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 1024-1029
    • Yamashita, M.1    Kimura, M.2    Kubo, M.3
  • 44
    • 2442712697 scopus 로고    scopus 로고
    • Anti-inflammatory effects of mitogen-activated protein kinase kinase inhibitor U0126 in an asthma mouse model
    • Duan W, Chan JH, Wong CH, Leung BP, Wong WS. Anti-inflammatory effects of mitogen-activated protein kinase kinase inhibitor U0126 in an asthma mouse model. J Immunol 2004; 172:7053-9.
    • (2004) J Immunol , vol.172 , pp. 7053-7059
    • Duan, W.1    Chan, J.H.2    Wong, C.H.3    Leung, B.P.4    Wong, W.S.5
  • 46
    • 0032191173 scopus 로고    scopus 로고
    • Differentiation of CD4+ T cells to Th1 cells requires MAP kinase JNK2
    • Yang DD, Conze D, Whitmarsh AJ et al. Differentiation of CD4+ T cells to Th1 cells requires MAP kinase JNK2. Immunity 1998; 9:575-85.
    • (1998) Immunity , vol.9 , pp. 575-585
    • Yang, D.D.1    Conze, D.2    Whitmarsh, A.J.3
  • 47
    • 0034604093 scopus 로고    scopus 로고
    • JNK is required for effector T-cell function but not for T-cell activation
    • Dong C, Yang DD, Tournier C et al. JNK is required for effector T-cell function but not for T-cell activation. Nature 2000; 405:91-4.
    • (2000) Nature , vol.405 , pp. 91-94
    • Dong, C.1    Yang, D.D.2    Tournier, C.3
  • 48
    • 0037044718 scopus 로고    scopus 로고
    • ERK5 MAPK regulates embryonic angiogenesis and acts as a hypoxia-sensitive repressor of vascular endothelial growth factor expression
    • Sohn SJ, Sarvis BK, Cado D, Winoto A. ERK5 MAPK regulates embryonic angiogenesis and acts as a hypoxia-sensitive repressor of vascular endothelial growth factor expression. J Biol Chem 2002; 277:43344-51.
    • (2002) J Biol Chem , vol.277 , pp. 43344-43351
    • Sohn, S.J.1    Sarvis, B.K.2    Cado, D.3    Winoto, A.4
  • 49
    • 55249112351 scopus 로고    scopus 로고
    • ERK5 regulation in naïve T-cell activation and survival
    • Ananieva O, Macdonald A, Wang X et al. ERK5 regulation in naïve T-cell activation and survival. Eur J Immunol 2008; 38:2534-47.
    • (2008) Eur J Immunol , vol.38 , pp. 2534-2547
    • Ananieva, O.1    Macdonald, A.2    Wang, X.3
  • 50
    • 1642326111 scopus 로고    scopus 로고
    • Enhancement of MEK/ERK signaling promotes glucocorticoid resistance in CD4+ T cells
    • Tsitoura DC, Rothman PB. Enhancement of MEK/ERK signaling promotes glucocorticoid resistance in CD4+ T cells. J Clin Invest 2004; 113:619-27.
    • (2004) J Clin Invest , vol.113 , pp. 619-627
    • Tsitoura, D.C.1    Rothman, P.B.2
  • 51
    • 7944220552 scopus 로고    scopus 로고
    • Superantigen-induced corticosteroid resistance of human T cells occurs through activation of the mitogen-activated protein kinase kinase/extracellular signal-regulated kinase(MEK-ERK) pathway
    • Li LB, Goleva E, Hall CF, Ou LS, Leung DY. Superantigen-induced corticosteroid resistance of human T cells occurs through activation of the mitogen-activated protein kinase kinase/extracellular signal-regulated kinase(MEK-ERK) pathway. J Allergy Clin Immunol 2004; 114:1059-69.
    • (2004) J Allergy Clin Immunol , vol.114 , pp. 1059-1069
    • Li, L.B.1    Goleva, E.2    Hall, C.F.3    Ou, L.S.4    Leung, D.Y.5
  • 52
    • 59149087048 scopus 로고    scopus 로고
    • IFN-gamma reverses IL-2- and IL-4-mediated T-cell steroid resistance
    • Goleva E, Li LB, Leung DY. IFN-gamma reverses IL-2- and IL-4-mediated T-cell steroid resistance. Am J Respir Cell Mol Biol 2009; 40:223-30.
    • (2009) Am J Respir Cell Mol Biol , vol.40 , pp. 223-230
    • Goleva, E.1    Li, L.B.2    Leung, D.Y.3
  • 53
    • 0031671711 scopus 로고    scopus 로고
    • The mechanism of IL-5 signal transduction
    • Adachi T, Alam R. The mechanism of IL-5 signal transduction. Am J Physiol 1998; 275 (Part 1):C623-33.
    • (1998) Am J Physiol , vol.275 , Issue.PART 1
    • Adachi, T.1    Alam, R.2
  • 54
    • 0034663903 scopus 로고    scopus 로고
    • The differential role of extracellular signal-regulated kinases and p38 mitogen-activated protein kinase in eosinophil functions
    • Adachi T, Choudhury BK, Stafford S, Sur S, Alam R. The differential role of extracellular signal-regulated kinases and p38 mitogen-activated protein kinase in eosinophil functions. J Immunol 2000; 165:2198-204.
    • (2000) J Immunol , vol.165 , pp. 2198-2204
    • Adachi, T.1    Choudhury, B.K.2    Stafford, S.3    Sur, S.4    Alam, R.5
  • 56
    • 0034653460 scopus 로고    scopus 로고
    • Eotaxin induces degranulation and chemotaxis of eosinophils through the activation of ERK2 and p38 mitogen-activated protein kinases
    • Kampen GT, Stafford S, Adachi T et al. Eotaxin induces degranulation and chemotaxis of eosinophils through the activation of ERK2 and p38 mitogen-activated protein kinases. Blood 2000; 95:1911-7.
    • (2000) Blood , vol.95 , pp. 1911-1917
    • Kampen, G.T.1    Stafford, S.2    Adachi, T.3
  • 57
    • 44849088196 scopus 로고    scopus 로고
    • A phosphosite screen identifies autocrine TGF-beta-driven activation of protein kinase R as a survival-limiting factor for eosinophils
    • Goplen N, Gorska MM, Stafford SJ et al. A phosphosite screen identifies autocrine TGF-beta-driven activation of protein kinase R as a survival-limiting factor for eosinophils. J Immunol 2008; 180:4256-64.
    • (2008) J Immunol , vol.180 , pp. 4256-4264
    • Goplen, N.1    Gorska, M.M.2    Stafford, S.J.3
  • 58
    • 0032479926 scopus 로고    scopus 로고
    • Lyn, Jak2, and Raf-1 kinases are critical for the antiapoptotic effect of interleukin 5, whereas only Raf-1 kinase is essential for eosinophil activation and degranulation
    • Pazdrak K, Olszewska-Pazdrak B, Stafford S, Garofalo RP, Alam R. Lyn, Jak2, and Raf-1 kinases are critical for the antiapoptotic effect of interleukin 5, whereas only Raf-1 kinase is essential for eosinophil activation and degranulation. J Exp Med 1998; 188:421-9.
    • (1998) J Exp Med , vol.188 , pp. 421-429
    • Pazdrak, K.1    Olszewska-Pazdrak, B.2    Stafford, S.3    Garofalo, R.P.4    Alam, R.5
  • 59
    • 0034646654 scopus 로고    scopus 로고
    • ERK1 and ERK2 activation by chemotactic factors in human eosinophils is interleukin 5-dependent and contributes to leukotriene C(4) biosynthesis
    • Bates ME, Green VL, Bertics PJ. ERK1 and ERK2 activation by chemotactic factors in human eosinophils is interleukin 5-dependent and contributes to leukotriene C(4) biosynthesis. J Biol Chem 2000; 275:10968-75.
    • (2000) J Biol Chem , vol.275 , pp. 10968-10975
    • Bates, M.E.1    Green, V.L.2    Bertics, P.J.3
  • 60
    • 77953641765 scopus 로고    scopus 로고
    • Human airway eosinophils respond to chemoattractants with greater eosinophil-derived neurotoxin release, adherence to fibronectin, and activation of the Ras-ERK pathway when compared with blood eosinophils
    • Bates ME, Sedgwick JB, Zhu Y et al. Human airway eosinophils respond to chemoattractants with greater eosinophil-derived neurotoxin release, adherence to fibronectin, and activation of the Ras-ERK pathway when compared with blood eosinophils. J Immunol 2010; 184:7125-33.
    • (2010) J Immunol , vol.184 , pp. 7125-7133
    • Bates, M.E.1    Sedgwick, J.B.2    Zhu, Y.3
  • 62
    • 0029014963 scopus 로고
    • Activation of the mitogen-activated protein kinase/cytosolic phospholipase A2 pathway in a rat mast cell line. Indications of different pathways for release of arachidonic acid and secretory granules
    • Hirasawa N, Santini F, Beaven MA. Activation of the mitogen-activated protein kinase/cytosolic phospholipase A2 pathway in a rat mast cell line. Indications of different pathways for release of arachidonic acid and secretory granules. J Immunol 1995; 154:5391-402.
    • (1995) J Immunol , vol.154 , pp. 5391-5402
    • Hirasawa, N.1    Santini, F.2    Beaven, M.A.3
  • 63
    • 58149401317 scopus 로고    scopus 로고
    • Pak1 regulates multiple c-Kit mediated Ras-MAPK gain-in-function phenotypes in Nf1+/- mast cells
    • McDaniel AS, Allen JD, Park SJ et al. Pak1 regulates multiple c-Kit mediated Ras-MAPK gain-in-function phenotypes in Nf1+/- mast cells. Blood 2008; 112:4646-54.
    • (2008) Blood , vol.112 , pp. 4646-4654
    • McDaniel, A.S.1    Allen, J.D.2    Park, S.J.3
  • 64
    • 23744515285 scopus 로고    scopus 로고
    • Stem cell factor promotes mast cell survival via inactivation of FOXO3a-mediated transcriptional induction and MEK-regulated phosphorylation of the proapoptotic protein Bim
    • Möller C, Alfredsson J, Engström M et al. Stem cell factor promotes mast cell survival via inactivation of FOXO3a-mediated transcriptional induction and MEK-regulated phosphorylation of the proapoptotic protein Bim. Blood 2005; 106:1330-6.
    • (2005) Blood , vol.106 , pp. 1330-1336
    • Möller, C.1    Alfredsson, J.2    Engström, M.3
  • 65
    • 0034675925 scopus 로고    scopus 로고
    • MEKK2 gene disruption causes loss of cytokine production in response to IgE and c-Kit ligand stimulation of ES cell-derived mast cells
    • Garrington TP, Ishizuka T, Papst PJ et al. MEKK2 gene disruption causes loss of cytokine production in response to IgE and c-Kit ligand stimulation of ES cell-derived mast cells. EMBO J 2000; 19:5387-95.
    • (2000) EMBO J , vol.19 , pp. 5387-5395
    • Garrington, T.P.1    Ishizuka, T.2    Papst, P.J.3
  • 66
    • 0034664177 scopus 로고    scopus 로고
    • Roles of mitogen-activated protein kinase pathways for mediator release from human cultured mast cells
    • Kimata M, Inagaki N, Kato T, Miura T, Serizawa I, Nagai H. Roles of mitogen-activated protein kinase pathways for mediator release from human cultured mast cells. Biochem Pharmacol 2000; 60:589-94.
    • (2000) Biochem Pharmacol , vol.60 , pp. 589-594
    • Kimata, M.1    Inagaki, N.2    Kato, T.3    Miura, T.4    Serizawa, I.5    Nagai, H.6
  • 67
    • 33846897658 scopus 로고    scopus 로고
    • Selective activation of Fyn/PI3K and p38 MAPK regulates IL-4 production in BMMC under nontoxic stress condition
    • Frossi B, Rivera J, Hirsch E, Pucillo C. Selective activation of Fyn/PI3K and p38 MAPK regulates IL-4 production in BMMC under nontoxic stress condition. J Immunol 2007; 178:2549-55.
    • (2007) J Immunol , vol.178 , pp. 2549-2555
    • Frossi, B.1    Rivera, J.2    Hirsch, E.3    Pucillo, C.4
  • 68
    • 28244493479 scopus 로고    scopus 로고
    • Impaired FcepsilonRI-dependent gene expression and defective eicosanoid and cytokine production as a consequence of Fyn deficiency in mast cells
    • Gomez G, Gonzalez-Espinosa C, Odom S et al. Impaired FcepsilonRI-dependent gene expression and defective eicosanoid and cytokine production as a consequence of Fyn deficiency in mast cells. J Immunol 2005; 175:7602-10.
    • (2005) J Immunol , vol.175 , pp. 7602-7610
    • Gomez, G.1    Gonzalez-Espinosa, C.2    Odom, S.3
  • 69
    • 0035869634 scopus 로고    scopus 로고
    • A critical role for p38 mitogen-activated protein kinase in the maturation of human blood-derived dendritic cells induced by lipopolysaccharide, TNF-alpha, and contact sensitizers
    • Arrighi JF, Rebsamen M, Rousset F, Kindler V, Hauser C. A critical role for p38 mitogen-activated protein kinase in the maturation of human blood-derived dendritic cells induced by lipopolysaccharide, TNF-alpha, and contact sensitizers. J Immunol 2001; 166:3837-45.
    • (2001) J Immunol , vol.166 , pp. 3837-3845
    • Arrighi, J.F.1    Rebsamen, M.2    Rousset, F.3    Kindler, V.4    Hauser, C.5
  • 70
    • 0035496927 scopus 로고    scopus 로고
    • Extracellular signal-regulated protein kinase signaling pathway negatively regulates the phenotypic and functional maturation of monocyte-derived human dendritic cells
    • Puig-Kröger A, Relloso M, Fernández-Capetillo O et al. Extracellular signal-regulated protein kinase signaling pathway negatively regulates the phenotypic and functional maturation of monocyte-derived human dendritic cells. Blood 2001; 98:2175-82.
    • (2001) Blood , vol.98 , pp. 2175-2182
    • Puig-Kröger, A.1    Relloso, M.2    Fernández-Capetillo, O.3
  • 72
    • 63449096467 scopus 로고    scopus 로고
    • Combined sensitization of mice to extracts of dust mite, ragweed, and Aspergillus species breaks through tolerance and establishes chronic features of asthma
    • Goplen N, Karim MZ, Liang Q et al. Combined sensitization of mice to extracts of dust mite, ragweed, and Aspergillus species breaks through tolerance and establishes chronic features of asthma. J Allergy Clin Immunol 2009; 123:925-32.
    • (2009) J Allergy Clin Immunol , vol.123 , pp. 925-932
    • Goplen, N.1    Karim, M.Z.2    Liang, Q.3
  • 73
    • 22644445634 scopus 로고    scopus 로고
    • Dexamethasone induces IL-10-producing monocyte-derived dendritic cells with durable immaturity
    • Xia CQ, Peng R, Beato F, Clare-Salzler MJ. Dexamethasone induces IL-10-producing monocyte-derived dendritic cells with durable immaturity. Scand J Immunol 2005; 62:45-54.
    • (2005) Scand J Immunol , vol.62 , pp. 45-54
    • Xia, C.Q.1    Peng, R.2    Beato, F.3    Clare-Salzler, M.J.4
  • 74
    • 33749355639 scopus 로고    scopus 로고
    • TLR agonists promote ERK-mediated preferential IL-10 production of regulatory dendritic cells (diffDCs), leading to NK-cell activation
    • Qian C, Jiang X, An H et al. TLR agonists promote ERK-mediated preferential IL-10 production of regulatory dendritic cells (diffDCs), leading to NK-cell activation. Blood 2006; 108:2307-15.
    • (2006) Blood , vol.108 , pp. 2307-2315
    • Qian, C.1    Jiang, X.2    An, H.3
  • 75
    • 1842477227 scopus 로고    scopus 로고
    • A Toll-like receptor 2 ligand stimulates Th2 responses in vivo, via induction of extracellular signal-regulated kinase mitogen-activated protein kinase and c-Fos in dendritic cells
    • Dillon S, Agrawal A, Van Dyke T et al. A Toll-like receptor 2 ligand stimulates Th2 responses in vivo, via induction of extracellular signal-regulated kinase mitogen-activated protein kinase and c-Fos in dendritic cells. J Immunol 2004; 172:4733-43.
    • (2004) J Immunol , vol.172 , pp. 4733-4743
    • Dillon, S.1    Agrawal, A.2    Van Dyke, T.3
  • 76
    • 32944463876 scopus 로고    scopus 로고
    • Yeast zymosan, a stimulus for TLR2 and dectin-1, induces regulatory antigen-presenting cells and immunological tolerance
    • Dillon S, Agrawal S, Banerjee K et al. Yeast zymosan, a stimulus for TLR2 and dectin-1, induces regulatory antigen-presenting cells and immunological tolerance. J Clin Invest 2006; 116:916-28.
    • (2006) J Clin Invest , vol.116 , pp. 916-928
    • Dillon, S.1    Agrawal, S.2    Banerjee, K.3
  • 77
    • 0033120590 scopus 로고    scopus 로고
    • Differential expression and activation of p38 mitogen-activated protein kinase alpha, beta, gamma, and delta in inflammatory cell lineages
    • Hale KK, Trollinger D, Rihanek M, Manthey CL. Differential expression and activation of p38 mitogen-activated protein kinase alpha, beta, gamma, and delta in inflammatory cell lineages. J Immunol 1999; 162:4246-52.
    • (1999) J Immunol , vol.162 , pp. 4246-4252
    • Hale, K.K.1    Trollinger, D.2    Rihanek, M.3    Manthey, C.L.4
  • 78
    • 0033136947 scopus 로고    scopus 로고
    • The role of p38 mitogen-activated protein kinase in IL-1 beta transcription
    • Baldassare JJ, Bi Y, Bellone CJ. The role of p38 mitogen-activated protein kinase in IL-1 beta transcription. J Immunol 1999; 162:5367-73.
    • (1999) J Immunol , vol.162 , pp. 5367-5373
    • Baldassare, J.J.1    Bi, Y.2    Bellone, C.J.3
  • 79
    • 0032925361 scopus 로고    scopus 로고
    • Specific inhibitors of p38 and extracellular signal-regulated kinase mitogen-activated protein kinase pathways block inducible nitric oxide synthase and tumor necrosis factor accumulation in murine macrophages stimulated with lipopolysaccharide and interferon-gamma
    • Ajizian SJ, English BK, Meals EA. Specific inhibitors of p38 and extracellular signal-regulated kinase mitogen-activated protein kinase pathways block inducible nitric oxide synthase and tumor necrosis factor accumulation in murine macrophages stimulated with lipopolysaccharide and interferon-gamma. J Infect Dis 1999; 179:939-44.
    • (1999) J Infect Dis , vol.179 , pp. 939-944
    • Ajizian, S.J.1    English, B.K.2    Meals, E.A.3
  • 80
    • 0032963127 scopus 로고    scopus 로고
    • Involvement of p38 mitogen-activated protein kinase in lipopolysaccharide-induced iNOS and COX-2 expression in J774 macrophages
    • Chen C, Chen YH, Lin WW. Involvement of p38 mitogen-activated protein kinase in lipopolysaccharide-induced iNOS and COX-2 expression in J774 macrophages. Immunology 1999; 97:124-9.
    • (1999) Immunology , vol.97 , pp. 124-129
    • Chen, C.1    Chen, Y.H.2    Lin, W.W.3
  • 81
    • 0038265538 scopus 로고    scopus 로고
    • Myeloid differentiation factor 88-dependent transcriptional regulation of cyclooxygenase-2 expression by CpG DNA
    • J Biol Chem
    • Yeo SJ, Gravis D, Yoon JG, Yi AK. Myeloid differentiation factor 88-dependent transcriptional regulation of cyclooxygenase-2 expression by CpG DNA: role of NF-kappaB and p38. J Biol Chem 2003; 278:22563-73.
    • (2003) role of NF-kappaB and p38 , vol.278 , pp. 22563-22573
    • Yeo, S.J.1    Gravis, D.2    Yoon, J.G.3    Yi, A.K.4
  • 82
    • 50049122380 scopus 로고    scopus 로고
    • The kinase p38 alpha serves cell type-specific inflammatory functions in skin injury and coordinates pro- and anti-inflammatory gene expression
    • Kim C, Sano Y, Todorova K et al. The kinase p38 alpha serves cell type-specific inflammatory functions in skin injury and coordinates pro- and anti-inflammatory gene expression. Nat Immunol 2008; 9:1019-27.
    • (2008) Nat Immunol , vol.9 , pp. 1019-1027
    • Kim, C.1    Sano, Y.2    Todorova, K.3
  • 83
    • 21244502077 scopus 로고    scopus 로고
    • ERK activation following macrophage FcgammaR ligation leads to chromatin modifications at the IL-10 locus
    • Lucas M, Zhang X, Prasanna V, Mosser DM. ERK activation following macrophage FcgammaR ligation leads to chromatin modifications at the IL-10 locus. J Immunol 2005; 175:469-77.
    • (2005) J Immunol , vol.175 , pp. 469-477
    • Lucas, M.1    Zhang, X.2    Prasanna, V.3    Mosser, D.M.4
  • 84
    • 0034663958 scopus 로고    scopus 로고
    • The involvement of tyrosine kinases, cyclic AMP/protein kinase A, and p38 mitogen-activated protein kinase in IL-13-mediated arginase I induction in macrophages
    • J Immunol
    • Chang CI, Zoghi B, Liao JC, Kuo L. The involvement of tyrosine kinases, cyclic AMP/protein kinase A, and p38 mitogen-activated protein kinase in IL-13-mediated arginase I induction in macrophages: its implications in IL-13-inhibited nitric oxide production. J Immunol 2000; 165:2134-41.
    • (2000) its implications in IL-13-inhibited nitric oxide production , vol.165 , pp. 2134-2141
    • Chang, C.I.1    Zoghi, B.2    Liao, J.C.3    Kuo, L.4
  • 85
    • 0024378214 scopus 로고
    • Alveolar macrophage elimination in vivo is associated with an increase in pulmonary immune response in mice
    • Thepen T, Van Rooijen N, Kraal G. Alveolar macrophage elimination in vivo is associated with an increase in pulmonary immune response in mice. J Exp Med 1989; 170:499-509.
    • (1989) J Exp Med , vol.170 , pp. 499-509
    • Thepen, T.1    Van Rooijen, N.2    Kraal, G.3
  • 86
    • 0035253346 scopus 로고    scopus 로고
    • Th type 1-stimulating activity of lung macrophages inhibits Th2-mediated allergic airway inflammation by an IFN-gamma-dependent mechanism
    • Tang C, Inman MD, van Rooijen N et al. Th type 1-stimulating activity of lung macrophages inhibits Th2-mediated allergic airway inflammation by an IFN-gamma-dependent mechanism. J Immunol 2001; 166:1471-81.
    • (2001) J Immunol , vol.166 , pp. 1471-1481
    • Tang, C.1    Inman, M.D.2    van Rooijen, N.3
  • 88
    • 77955333700 scopus 로고    scopus 로고
    • Elevated GM-CSF and IL-1beta levels compromise the ability of p38 MAPK inhibitors to modulate TNFalpha levels in the human monocytic/macrophage U937 cell line
    • Espelin CW, Goldsipe A, Sorger PK, Lauffenburger DA, de Graaf D, Hendriks BS. Elevated GM-CSF and IL-1beta levels compromise the ability of p38 MAPK inhibitors to modulate TNFalpha levels in the human monocytic/macrophage U937 cell line. Mol Biosyst 2010; 6:1956-72.
    • (2010) Mol Biosyst , vol.6 , pp. 1956-1972
    • Espelin, C.W.1    Goldsipe, A.2    Sorger, P.K.3    Lauffenburger, D.A.4    de Graaf, D.5    Hendriks, B.S.6
  • 90
    • 41549103208 scopus 로고    scopus 로고
    • Erk kinases link pre-B cell receptor signaling to transcriptional events required for early B cell expansion
    • Yasuda T, Sanjo H, Pagès G et al. Erk kinases link pre-B cell receptor signaling to transcriptional events required for early B cell expansion. Immunity 2008; 28:499-508.
    • (2008) Immunity , vol.28 , pp. 499-508
    • Yasuda, T.1    Sanjo, H.2    Pagès, G.3
  • 92
    • 0032487507 scopus 로고    scopus 로고
    • Involvement of guanosine triphosphatases and phospholipase C-gamma2 in extracellular signal-regulated kinase, c-Jun NH2-terminal kinase, and p38 mitogen-activated protein kinase activation by the B cell antigen receptor
    • Hashimoto A, Okada H, Jiang A et al. Involvement of guanosine triphosphatases and phospholipase C-gamma2 in extracellular signal-regulated kinase, c-Jun NH2-terminal kinase, and p38 mitogen-activated protein kinase activation by the B cell antigen receptor. J Exp Med 1998; 188:1287-95.
    • (1998) J Exp Med , vol.188 , pp. 1287-1295
    • Hashimoto, A.1    Okada, H.2    Jiang, A.3
  • 93
    • 0035869267 scopus 로고    scopus 로고
    • Inhibition of the MEK/ERK signaling pathway blocks a subset of B cell responses to antigen
    • Richards JD, Davé SH, Chou CH, Mamchak AA, DeFranco AL. Inhibition of the MEK/ERK signaling pathway blocks a subset of B cell responses to antigen. J Immunol 2001; 166:3855-64.
    • (2001) J Immunol , vol.166 , pp. 3855-3864
    • Richards, J.D.1    Davé, S.H.2    Chou, C.H.3    Mamchak, A.A.4    DeFranco, A.L.5
  • 94
    • 33846907736 scopus 로고    scopus 로고
    • Extracellular signal-regulated protein kinase 2 is required for efficient generation of B cells bearing antigen-specific immunoglobulin G
    • Sanjo H, Hikida M, Aiba Y et al. Extracellular signal-regulated protein kinase 2 is required for efficient generation of B cells bearing antigen-specific immunoglobulin G. Mol Cell Biol 2007; 27:1236-46.
    • (2007) Mol Cell Biol , vol.27 , pp. 1236-1246
    • Sanjo, H.1    Hikida, M.2    Aiba, Y.3
  • 95
    • 0037501347 scopus 로고    scopus 로고
    • Resistance to CpG DNA-induced autoimmunity through tolerogenic B cell antigen receptor ERK signaling
    • Rui L, Vinuesa CG, Blasioli J, Goodnow CC. Resistance to CpG DNA-induced autoimmunity through tolerogenic B cell antigen receptor ERK signaling. Nat Immunol 2003; 4:594-600.
    • (2003) Nat Immunol , vol.4 , pp. 594-600
    • Rui, L.1    Vinuesa, C.G.2    Blasioli, J.3    Goodnow, C.C.4
  • 96
    • 33847002355 scopus 로고    scopus 로고
    • Kinase MEKK1 is required for CD40-dependent activation of the kinases Jnk and p38, germinal center formation, B cell proliferation and antibody production
    • Gallagher E, Enzler T, Matsuzawa A et al. Kinase MEKK1 is required for CD40-dependent activation of the kinases Jnk and p38, germinal center formation, B cell proliferation and antibody production. Nat Immunol 2007; 8:57-63.
    • (2007) Nat Immunol , vol.8 , pp. 57-63
    • Gallagher, E.1    Enzler, T.2    Matsuzawa, A.3
  • 97
    • 0042858444 scopus 로고    scopus 로고
    • Inhibition of interleukin-4-induced class switch recombination by a human immunoglobulin Fc gamma-Fc epsilon chimeric protein
    • Yamada T, Zhu D, Zhang K, Saxon A. Inhibition of interleukin-4-induced class switch recombination by a human immunoglobulin Fc gamma-Fc epsilon chimeric protein. J Biol Chem 2003; 278:32818-24.
    • (2003) J Biol Chem , vol.278 , pp. 32818-32824
    • Yamada, T.1    Zhu, D.2    Zhang, K.3    Saxon, A.4
  • 98
    • 0036739925 scopus 로고    scopus 로고
    • CD40-mediated p38 mitogen-activated protein kinase activation is required for immunoglobulin class switch recombination to IgE
    • Zhang K, Zhang L, Zhu D, Bae D, Nel A, Saxon A. CD40-mediated p38 mitogen-activated protein kinase activation is required for immunoglobulin class switch recombination to IgE. J Allergy Clin Immunol 2002; 110:421-8.
    • (2002) J Allergy Clin Immunol , vol.110 , pp. 421-428
    • Zhang, K.1    Zhang, L.2    Zhu, D.3    Bae, D.4    Nel, A.5    Saxon, A.6
  • 99
    • 27844541328 scopus 로고    scopus 로고
    • Modeling T cell antigen discrimination based on feedback control of digital ERK responses
    • Altan-Bonnet G, Germain RN. Modeling T cell antigen discrimination based on feedback control of digital ERK responses. PLoS Biol 2005; 3:e356.
    • (2005) PLoS Biol , vol.3
    • Altan-Bonnet, G.1    Germain, R.N.2
  • 100
    • 34848887670 scopus 로고    scopus 로고
    • Competing docking interactions can bring about bistability in the MAPK cascade
    • Legewie S, Schoeberl B, Blüthgen N, Herzel H. Competing docking interactions can bring about bistability in the MAPK cascade. Biophys J 2007; 93:2279-88.
    • (2007) Biophys J , vol.93 , pp. 2279-2288
    • Legewie, S.1    Schoeberl, B.2    Blüthgen, N.3    Herzel, H.4
  • 101
    • 0842288229 scopus 로고    scopus 로고
    • Signaling switches and bistability arising from multisite phosphorylation in protein kinase cascades
    • Markevich NI, Hoek JB, Kholodenko BN. Signaling switches and bistability arising from multisite phosphorylation in protein kinase cascades. J Cell Biol 2004; 164:353-9.
    • (2004) J Cell Biol , vol.164 , pp. 353-359
    • Markevich, N.I.1    Hoek, J.B.2    Kholodenko, B.N.3
  • 102
    • 78651458019 scopus 로고    scopus 로고
    • What is hysteresis? Available at, accessed 1 June 2010).
    • Sethna J. What is hysteresis? Available at (accessed 1 June 2010).
    • Sethna, J.1
  • 103
    • 3042596483 scopus 로고    scopus 로고
    • Dynamics and bistability in a reduced model of the lac operon
    • Yildirim N, Santillan M, Horike D, Mackey MC. Dynamics and bistability in a reduced model of the lac operon. Chaos 2004; 14:279-92.
    • (2004) Chaos , vol.14 , pp. 279-292
    • Yildirim, N.1    Santillan, M.2    Horike, D.3    Mackey, M.C.4
  • 104
    • 0010424768 scopus 로고
    • A mechanism for memory storage insensitive to molecular turnover
    • Proc Natl Acad Sci USA
    • Lisman JE. A mechanism for memory storage insensitive to molecular turnover: a bistable autophosphorylating kinase. Proc Natl Acad Sci USA 1985; 82:3055-7.
    • (1985) a bistable autophosphorylating kinase , vol.82 , pp. 3055-3057
    • Lisman, J.E.1
  • 106
    • 0345359924 scopus 로고    scopus 로고
    • A positive-feedback-based bistable 'memory module' that governs a cell fate decision
    • Xiong W, Ferrell JE Jr. A positive-feedback-based bistable 'memory module' that governs a cell fate decision. Nature 2003; 426:460-5.
    • (2003) Nature , vol.426 , pp. 460-465
    • Xiong, W.1    Ferrell Jr, J.E.2
  • 107
    • 0037047611 scopus 로고    scopus 로고
    • MAP kinase phosphatase as a locus of flexibility in a mitogen-activated protein kinase signaling network
    • Bhalla US, Ram PT, Iyengar R. MAP kinase phosphatase as a locus of flexibility in a mitogen-activated protein kinase signaling network. Science 2002; 297:1018-23.
    • (2002) Science , vol.297 , pp. 1018-1023
    • Bhalla, U.S.1    Ram, P.T.2    Iyengar, R.3
  • 108
    • 64649094816 scopus 로고    scopus 로고
    • KSR1 modulates the sensitivity of mitogen-activated protein kinase pathway activation in T cells without altering fundamental system outputs
    • Lin J, Harding A, Giurisato E, Shaw AS. KSR1 modulates the sensitivity of mitogen-activated protein kinase pathway activation in T cells without altering fundamental system outputs. Mol Cell Biol 2009; 29:2082-91.
    • (2009) Mol Cell Biol , vol.29 , pp. 2082-2091
    • Lin, J.1    Harding, A.2    Giurisato, E.3    Shaw, A.S.4
  • 109
    • 0035822634 scopus 로고    scopus 로고
    • Bistability in the JNK cascade
    • Bagowski CP, Ferrell JE Jr. Bistability in the JNK cascade. Curr Biol 2001; 11:1176-82.
    • (2001) Curr Biol , vol.11 , pp. 1176-1182
    • Bagowski, C.P.1    Ferrell Jr, J.E.2
  • 110
    • 58249092059 scopus 로고    scopus 로고
    • Digital signaling and hysteresis characterize ras activation in lymphoid cells
    • Das J, Ho M, Zikherman J et al. Digital signaling and hysteresis characterize ras activation in lymphoid cells. Cell 2009; 136:337-51.
    • (2009) Cell , vol.136 , pp. 337-351
    • Das, J.1    Ho, M.2    Zikherman, J.3
  • 111
    • 58149279827 scopus 로고    scopus 로고
    • Activation of the MAPK module from different spatial locations generates distinct system outputs
    • Inder K, Harding A, Plowman SJ, Philips MR, Parton RG, Hancock JF. Activation of the MAPK module from different spatial locations generates distinct system outputs. Mol Biol Cell 2008; 19:4776-84.
    • (2008) Mol Biol Cell , vol.19 , pp. 4776-4784
    • Inder, K.1    Harding, A.2    Plowman, S.J.3    Philips, M.R.4    Parton, R.G.5    Hancock, J.F.6
  • 112
    • 5344244073 scopus 로고    scopus 로고
    • Translational regulatory mechanisms in persistent forms of synaptic plasticity
    • Kelleher RJ III, Govindarajan A, Tonegawa S. Translational regulatory mechanisms in persistent forms of synaptic plasticity. Neuron 2004; 44:59-73.
    • (2004) Neuron , vol.44 , pp. 59-73
    • Kelleher III, R.J.1    Govindarajan, A.2    Tonegawa, S.3
  • 113
    • 33846437825 scopus 로고    scopus 로고
    • The role of the extracellular signal-regulated kinase pathway in memory encoding
    • Giovannini MG. The role of the extracellular signal-regulated kinase pathway in memory encoding. Rev Neurosci 2006; 17:619-34.
    • (2006) Rev Neurosci , vol.17 , pp. 619-634
    • Giovannini, M.G.1
  • 114
    • 1342322145 scopus 로고    scopus 로고
    • Translational control by MAPK signaling in long-term synaptic plasticity and memory
    • Kelleher RJ III, Govindarajan A, Jung HY, Kang H, Tonegawa S. Translational control by MAPK signaling in long-term synaptic plasticity and memory. Cell 2004; 116:467-79.
    • (2004) Cell , vol.116 , pp. 467-479
    • Kelleher III, R.J.1    Govindarajan, A.2    Jung, H.Y.3    Kang, H.4    Tonegawa, S.5
  • 115
    • 0034660615 scopus 로고    scopus 로고
    • The MAPK/ERK cascade targets both Elk-1 and cAMP response element-binding protein to control long-term potentiation-dependent gene expression in the dentate gyrus in vivo
    • Davis S, Vanhoutte P, Pages C, Caboche J, Laroche S. The MAPK/ERK cascade targets both Elk-1 and cAMP response element-binding protein to control long-term potentiation-dependent gene expression in the dentate gyrus in vivo. J Neurosci 2000; 20:4563-72.
    • (2000) J Neurosci , vol.20 , pp. 4563-4572
    • Davis, S.1    Vanhoutte, P.2    Pages, C.3    Caboche, J.4    Laroche, S.5
  • 116
    • 35148894535 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase 2 (ERK2) knockdown mice show deficits in long-term memory; ERK2 has a specific function in learning and memory
    • Satoh Y, Endo S, Ikeda T et al. Extracellular signal-regulated kinase 2 (ERK2) knockdown mice show deficits in long-term memory; ERK2 has a specific function in learning and memory. J Neurosci 2007; 27:10765-76.
    • (2007) J Neurosci , vol.27 , pp. 10765-10776
    • Satoh, Y.1    Endo, S.2    Ikeda, T.3
  • 119
    • 0033983004 scopus 로고    scopus 로고
    • Viral and bacterial infections in the development and progression of asthma
    • Gern JE. Viral and bacterial infections in the development and progression of asthma. J Allergy Clin Immunol 2000; 105:S497-502.
    • (2000) J Allergy Clin Immunol , vol.105
    • Gern, J.E.1
  • 120
    • 0033830764 scopus 로고    scopus 로고
    • Viruses and atopic sensitization in the first years of life
    • Martinez FD. Viruses and atopic sensitization in the first years of life. Am J Respir Crit Care Med 2000; 162:S95-9.
    • (2000) Am J Respir Crit Care Med , vol.162
    • Martinez, F.D.1
  • 121
    • 77949390343 scopus 로고    scopus 로고
    • Establishment of extracellular signal-regulated kinase 1/2 bistability and sustained activation through Sprouty 2 and its relevance for epithelial function
    • Liu W, Tundwal K, Liang Q et al. Establishment of extracellular signal-regulated kinase 1/2 bistability and sustained activation through Sprouty 2 and its relevance for epithelial function. Mol Cell Biol 2010; 30:1783-99.
    • (2010) Mol Cell Biol , vol.30 , pp. 1783-1799
    • Liu, W.1    Tundwal, K.2    Liang, Q.3
  • 122
    • 29544433771 scopus 로고    scopus 로고
    • Negative regulation of the E3 ubiquitin ligase itch via Fyn-mediated tyrosine phosphorylation
    • Yang C, Zhou W, Jeon MS et al. Negative regulation of the E3 ubiquitin ligase itch via Fyn-mediated tyrosine phosphorylation. Mol Cell 2006; 21:135-41.
    • (2006) Mol Cell , vol.21 , pp. 135-141
    • Yang, C.1    Zhou, W.2    Jeon, M.S.3
  • 123
    • 5044225158 scopus 로고    scopus 로고
    • Jun turnover is controlled through JNK-dependent phosphorylation of the E3 ligase Itch
    • Gao M, Labuda T, Xia Y et al. Jun turnover is controlled through JNK-dependent phosphorylation of the E3 ligase Itch. Science 2004; 306:271-5.
    • (2004) Science , vol.306 , pp. 271-275
    • Gao, M.1    Labuda, T.2    Xia, Y.3
  • 124
    • 0037197922 scopus 로고    scopus 로고
    • The bimodal regulation of epidermal growth factor signaling by human Sprouty proteins
    • Egan JE, Hall AB, Yatsula BA, Bar-Sagi D. The bimodal regulation of epidermal growth factor signaling by human Sprouty proteins. Proc Natl Acad Sci USA 2002; 99:6041-6.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 6041-6046
    • Egan, J.E.1    Hall, A.B.2    Yatsula, B.A.3    Bar-Sagi, D.4
  • 125
    • 0037119950 scopus 로고    scopus 로고
    • Sprouty2 attenuates epidermal growth factor receptor ubiquitylation and endocytosis, and consequently enhances Ras/ERK signalling
    • Wong ES, Fong CW, Lim J et al. Sprouty2 attenuates epidermal growth factor receptor ubiquitylation and endocytosis, and consequently enhances Ras/ERK signalling. EMBO J 2002; 21:4796-808.
    • (2002) EMBO J , vol.21 , pp. 4796-4808
    • Wong, E.S.1    Fong, C.W.2    Lim, J.3
  • 126
    • 0242684548 scopus 로고    scopus 로고
    • Sprouty fine-tunes EGF signaling through interlinked positive and negative feedback loops
    • Rubin C, Litvak V, Medvedovsky H, Zwang Y, Lev S., Yarden Y. Sprouty fine-tunes EGF signaling through interlinked positive and negative feedback loops. Curr Biol 2003; 13:297-307.
    • (2003) Curr Biol , vol.13 , pp. 297-307
    • Rubin, C.1    Litvak, V.2    Medvedovsky, H.3    Zwang, Y.4    Lev, S.5    Yarden, Y.6
  • 127
    • 34250823515 scopus 로고    scopus 로고
    • Gene-specific control of inflammation by TLR-induced chromatin modifications
    • Foster SL, Hargreaves DC, Medzhitov R. Gene-specific control of inflammation by TLR-induced chromatin modifications. Nature 2007; 447:972-8.
    • (2007) Nature , vol.447 , pp. 972-978
    • Foster, S.L.1    Hargreaves, D.C.2    Medzhitov, R.3
  • 128
    • 40849100220 scopus 로고    scopus 로고
    • Using engineered scaffold interactions to reshape MAP kinase pathway signaling dynamics
    • Bashor CJ, Helman NC, Yan S, Lim WA Using engineered scaffold interactions to reshape MAP kinase pathway signaling dynamics. Science 2008; 319:1539-43.
    • (2008) Science , vol.319 , pp. 1539-1543
    • Bashor, C.J.1    Helman, N.C.2    Yan, S.3    Lim, W.A.4
  • 130
    • 75949115944 scopus 로고    scopus 로고
    • Noncooperative interactions between transcription factors and clustered DNA binding sites enable graded transcriptional responses to environmental inputs
    • Giorgetti L, Siggers T, Tiana G et al. Noncooperative interactions between transcription factors and clustered DNA binding sites enable graded transcriptional responses to environmental inputs. Mol Cell 2010; 37:418-28.
    • (2010) Mol Cell , vol.37 , pp. 418-428
    • Giorgetti, L.1    Siggers, T.2    Tiana, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.