메뉴 건너뛰기




Volumn 186, Issue , 2002, Pages 189-207

Integrin-dependent regulation of gene expression in leukocytes

Author keywords

[No Author keywords available]

Indexed keywords

INTEGRIN; INTERCELLULAR ADHESION MOLECULE 1; JANUS KINASE; LYMPHOCYTE FUNCTION ASSOCIATED ANTIGEN 1; PROTEIN; PROTEIN JAB 1; STAT PROTEIN; TRANSCRIPTION FACTOR AP 1; UNCLASSIFIED DRUG;

EID: 0036696165     PISSN: 01052896     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1600-065X.2002.18616.x     Document Type: Review
Times cited : (29)

References (131)
  • 2
    • 0028935791 scopus 로고
    • Traffic signals on endothelium for lymphocyte recirculation and leukocyte emigration
    • Springer TA. Traffic signals on endothelium for lymphocyte recirculation and leukocyte emigration. Annu Rev Physiol 1995;57:827-872.
    • (1995) Annu Rev Physiol , vol.57 , pp. 827-872
    • Springer, T.A.1
  • 3
    • 0033374678 scopus 로고    scopus 로고
    • Cell adhesion. Old and new questions
    • Hynes RO. Cell adhesion. Old and new questions. Trends Cell Biol 1999;9:M33-M37.
    • (1999) Trends Cell Biol , vol.9
    • Hynes, R.O.1
  • 4
    • 0032842777 scopus 로고    scopus 로고
    • Extracellular matrix remodelling and cellular differentiation
    • Streuli C. Extracellular matrix remodelling and cellular differentiation. Curr Opin Cell Biol 1999;11:634-640.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 634-640
    • Streuli, C.1
  • 5
    • 0034977350 scopus 로고    scopus 로고
    • Shape and shift changes related to the function of leukocyte integrins LFA-1 and Mac-1
    • Hogg N, Leitinger B. Shape and shift changes related to the function of leukocyte integrins LFA-1 and Mac-1. J Leukoc Biol 2001;69:893-898.
    • (2001) J Leukoc Biol , vol.69 , pp. 893-898
    • Hogg, N.1    Leitinger, B.2
  • 6
    • 0028446566 scopus 로고
    • The dynamic regulation of integrin adhesiveness
    • Diamond MS, Springer TA. The dynamic regulation of integrin adhesiveness. Curr Biol 1994;4:506-517.
    • (1994) Curr Biol , vol.4 , pp. 506-517
    • Diamond, M.S.1    Springer, T.A.2
  • 7
    • 0033824065 scopus 로고    scopus 로고
    • Avidity regulation of integrins: The driving force in leukocyte adhesion
    • van Kooyk Y, Figdor CG. Avidity regulation of integrins: the driving force in leukocyte adhesion. Curr Opin Cell Biol 2000;12:542-547.
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 542-547
    • Van Kooyk, Y.1    Figdor, C.G.2
  • 8
    • 0030854195 scopus 로고    scopus 로고
    • Leukocyte adhesion. CD11/CD18 integrins and intercellular adhesion molecules
    • Gahmberg CG. Leukocyte adhesion. CD11/CD18 integrins and intercellular adhesion molecules. Curr Opin Cell Biol 1997;9:643-650.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 643-650
    • Gahmberg, C.G.1
  • 9
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark EA, Brugge JS. Integrins and signal transduction pathways: the road taken. Science 1995;268:233-239.
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 10
    • 0031561481 scopus 로고    scopus 로고
    • Keystone symposium on signal transduction by cell adhesion receptors
    • Clark EA, Hynes RO. Keystone symposium on signal transduction by cell adhesion receptors. Biochim Biophys Acta 1997;1333:R9-R16.
    • (1997) Biochim Biophys Acta , vol.1333
    • Clark, E.A.1    Hynes, R.O.2
  • 12
    • 0028335948 scopus 로고
    • Anchorage dependence, integrins, and apoptosis
    • Ruoslahti E, Reed JC. Anchorage dependence, integrins, and apoptosis. Cell 1994;77:477-478.
    • (1994) Cell , vol.77 , pp. 477-478
    • Ruoslahti, E.1    Reed, J.C.2
  • 13
    • 0030661566 scopus 로고    scopus 로고
    • Integrins, oncogenes, and anchorage independence
    • Schwartz MA. Integrins, oncogenes, and anchorage independence. J Cell Biol 1997;139:575-578.
    • (1997) J Cell Biol , vol.139 , pp. 575-578
    • Schwartz, M.A.1
  • 15
    • 0032734174 scopus 로고    scopus 로고
    • Cell adhesion molecules, signal transduction and cell growth
    • Aplin AE, Howe AK, Juliano RL. Cell adhesion molecules, signal transduction and cell growth. Curr Opin Cell Biol 1999;11:737-744.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 737-744
    • Aplin, A.E.1    Howe, A.K.2    Juliano, R.L.3
  • 16
    • 0035479818 scopus 로고    scopus 로고
    • Syndecan-4 and focal adhesion function
    • Woods A, Couchman JR. Syndecan-4 and focal adhesion function. Curr Opin Cell Biol 2001;13:578-583.
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 578-583
    • Woods, A.1    Couchman, J.R.2
  • 17
    • 0035911954 scopus 로고    scopus 로고
    • A role for syndecan-1 in coupling fascin spike formation by thrombospondin-1
    • Adams JC, Kureishy N, Taylor AL. A role for syndecan-1 in coupling fascin spike formation by thrombospondin-1. J Cell Biol 2001;152:1169-1182.
    • (2001) J Cell Biol , vol.152 , pp. 1169-1182
    • Adams, J.C.1    Kureishy, N.2    Taylor, A.L.3
  • 18
    • 0031908543 scopus 로고    scopus 로고
    • Long-range and selective autoregulation of cell-cell or cell-matrix adhesions by cadherin or integrin ligands
    • Levenberg S, Katz BZ, Yamada KM, Geiger B. Long-range and selective autoregulation of cell-cell or cell-matrix adhesions by cadherin or integrin ligands. J Cell Sci 1998;111:347-357.
    • (1998) J Cell Sci , vol.111 , pp. 347-357
    • Levenberg, S.1    Katz, B.Z.2    Yamada, K.M.3    Geiger, B.4
  • 19
    • 0034715923 scopus 로고    scopus 로고
    • Focal adhesions: A nexus for intracellular signaling and cytoskeletal dynamics
    • Sastry SK, Burridge K. Focal adhesions: a nexus for intracellular signaling and cytoskeletal dynamics. Exp Cell Res 2000;261:25-36.
    • (2000) Exp Cell Res , vol.261 , pp. 25-36
    • Sastry, S.K.1    Burridge, K.2
  • 20
    • 0033790713 scopus 로고    scopus 로고
    • Dynamics and segregation of cell-matrix adhesions in cultured fibroblasts
    • Zamir E, et al. Dynamics and segregation of cell-matrix adhesions in cultured fibroblasts. Nat Cell Biol 2000;2:191-196.
    • (2000) Nat Cell Biol , vol.2 , pp. 191-196
    • Zamir, E.1
  • 21
    • 0035516140 scopus 로고    scopus 로고
    • Transmembrane crosstalk between the extracellular matrix - Cytoskeleton crosstalk
    • Geiger B, Bershadsky A, Pankov R, Yamada KM. Transmembrane crosstalk between the extracellular matrix - cytoskeleton crosstalk. Nat Rev Mol Cell Biol 2001;2:793-805.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 793-805
    • Geiger, B.1    Bershadsky, A.2    Pankov, R.3    Yamada, K.M.4
  • 22
    • 0031050449 scopus 로고    scopus 로고
    • Molecular interactions in cell adhesion complexes
    • Yamada KM, Geiger B. Molecular interactions in cell adhesion complexes. Curr Opin Cell Biol 1997;9:76-85.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 76-85
    • Yamada, K.M.1    Geiger, B.2
  • 23
    • 0017812339 scopus 로고
    • The control of mRNA production, translation and turnover in suspended and reattached anchorage-dependent fibroblasts
    • Benecke BJ, Ben-Ze'ev A, Penman S. The control of mRNA production, translation and turnover in suspended and reattached anchorage-dependent fibroblasts. Cell 1978;14:931-939.
    • (1978) Cell , vol.14 , pp. 931-939
    • Benecke, B.J.1    Ben-Ze'ev A2    Penman, S.3
  • 24
    • 0034902905 scopus 로고    scopus 로고
    • Integrins and cell proliferation: Regulation of cyclin-dependent kinases via cytoplasmic signaling pathways
    • Schwartz MA, Assoian RK. Integrins and cell proliferation: regulation of cyclin-dependent kinases via cytoplasmic signaling pathways. J Cell Sci 2001;114:2553-2560.
    • (2001) J Cell Sci , vol.114 , pp. 2553-2560
    • Schwartz, M.A.1    Assoian, R.K.2
  • 25
    • 0029965695 scopus 로고    scopus 로고
    • Integrin-mediated signaling: Regulation by protein tyrosine kinases and small GTP-binding proteins
    • Parsons JT. Integrin-mediated signaling: regulation by protein tyrosine kinases and small GTP-binding proteins. Curr Opin Cell Biol 1996;8:146-152.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 146-152
    • Parsons, J.T.1
  • 26
    • 0031915021 scopus 로고    scopus 로고
    • Integrin signaling and tyrosine phosphorylation: Just the FAKs?
    • Schlaepfer DD, Hunter T. Integrin signaling and tyrosine phosphorylation: just the FAKs? Trends Cell Biol 1998;8:151-157.
    • (1998) Trends Cell Biol , vol.8 , pp. 151-157
    • Schlaepfer, D.D.1    Hunter, T.2
  • 27
    • 0030453194 scopus 로고    scopus 로고
    • Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation: Roles of integrin aggregation and occupancy of receptors
    • Miyamoto S, Teramoto H, Gutkind JS, Yamada KM. Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation: roles of integrin aggregation and occupancy of receptors. J Cell Biol 1996;135:1633-1642.
    • (1996) J Cell Biol , vol.135 , pp. 1633-1642
    • Miyamoto, S.1    Teramoto, H.2    Gutkind, J.S.3    Yamada, K.M.4
  • 28
    • 0030814976 scopus 로고    scopus 로고
    • Alphavbeta3 integrin associates with activated insulin and PDGFbeta receptors and potentiates the biological activity of PDGF
    • Schneller M, Vuori K, Ruoslahti E. Alphavbeta3 integrin associates with activated insulin and PDGFbeta receptors and potentiates the biological activity of PDGF. EMBO J 1997;16:5600-5607.
    • (1997) EMBO J , vol.16 , pp. 5600-5607
    • Schneller, M.1    Vuori, K.2    Ruoslahti, E.3
  • 29
    • 0032538798 scopus 로고    scopus 로고
    • Integrins induce activation of EGF receptor: Role in MAP kinase induction and adhesion-dependent cell survival
    • Moro L, et al. Integrins induce activation of EGF receptor: role in MAP kinase induction and adhesion-dependent cell survival. EMBO J 1998;17:6622-6632.
    • (1998) EMBO J , vol.17 , pp. 6622-6632
    • Moro, L.1
  • 30
    • 0033558087 scopus 로고    scopus 로고
    • Role of alphavbeta3 integrin in the activation of vascular endothelial growth factor receptor-2
    • Soldi R, Mitola S, Strasly M, Defilippi P, Tarone G, Bussolino F. Role of alphavbeta3 integrin in the activation of vascular endothelial growth factor receptor-2. EMBO J 1999;18:882-892.
    • (1999) EMBO J , vol.18 , pp. 882-892
    • Soldi, R.1    Mitola, S.2    Strasly, M.3    Defilippi, P.4    Tarone, G.5    Bussolino, F.6
  • 31
    • 0037088647 scopus 로고    scopus 로고
    • Integrin-induced epidermal growth factor (EGF) receptor activation requires c-Src and p130Cas and leads to phosphorylation of specific EGF receptor tyrosines
    • Moro L, et al. Integrin-induced epidermal growth factor (EGF) receptor activation requires c-Src and p130Cas and leads to phosphorylation of specific EGF receptor tyrosines. J Biol Chem 2002;277:9405-9414.
    • (2002) J Biol Chem , vol.277 , pp. 9405-9414
    • Moro, L.1
  • 32
  • 33
    • 0030926774 scopus 로고    scopus 로고
    • Focal adhesion kinase overexpression enhances ras-dependent integrin signaling to ERK2/mitogen-activated protein kinase through interactions with and activation of c-Src
    • Schlaepfer DD, Hunter T. Focal adhesion kinase overexpression enhances ras-dependent integrin signaling to ERK2/mitogen-activated protein kinase through interactions with and activation of c-Src. J Biol Chem 1997;272:13189-13195.
    • (1997) J Biol Chem , vol.272 , pp. 13189-13195
    • Schlaepfer, D.D.1    Hunter, T.2
  • 34
    • 0028986116 scopus 로고
    • pp125FAK-dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk
    • Schaller MD, Parsons JT. pp125FAK-dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk. Mol Cell Biol 1995;15:2635-2645.
    • (1995) Mol Cell Biol , vol.15 , pp. 2635-2645
    • Schaller, M.D.1    Parsons, J.T.2
  • 35
    • 0029257377 scopus 로고
    • Signal transduction through integrins: A central role for focal adhesion kinase?
    • Richardson A, Parsons JT. Signal transduction through integrins: a central role for focal adhesion kinase? Bioessays 1995;17:229-236.
    • (1995) Bioessays , vol.17 , pp. 229-236
    • Richardson, A.1    Parsons, J.T.2
  • 36
    • 0029664531 scopus 로고    scopus 로고
    • Introduction of p130cas signaling complex formation upon integrin-mediated cell adhesion: A role for Src family kinases
    • Vuori K, Hirai H, Aizawa S, Ruoslahti E. Introduction of p130cas signaling complex formation upon integrin-mediated cell adhesion: a role for Src family kinases. Mol Cell Biol 1996;16:2606-2613.
    • (1996) Mol Cell Biol , vol.16 , pp. 2606-2613
    • Vuori, K.1    Hirai, H.2    Aizawa, S.3    Ruoslahti, E.4
  • 37
    • 0028609382 scopus 로고
    • Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase
    • Schlaepfer DD, Hanks SK, Hunter T, van der Geer P. Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase. Nature 1994;372:786-791.
    • (1994) Nature , vol.372 , pp. 786-791
    • Schlaepfer, D.D.1    Hanks, S.K.2    Hunter, T.3    Van der Geer, P.4
  • 38
    • 0029994358 scopus 로고    scopus 로고
    • Integrin-mediated activation of MEK and mitogen-activated protein kinase is independent of Ras [corrected]
    • Chen Q, Der Lin THCJ, Juliano RL. Integrin-mediated activation of MEK and mitogen-activated protein kinase is independent of Ras [corrected]. J Biol Chem 1996;271:18122-18127.
    • (1996) J Biol Chem , vol.271 , pp. 18122-18127
    • Chen, Q.1    Der Lin, T.H.C.J.2    Juliano, R.L.3
  • 39
    • 0030839766 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase is required for integrin-stimulated AKT and Raf-1/mitogen-activated protein kinase pathway activation
    • King WG, Mattaliano MD, Chan TO, Tsichlis PN, Brugge JS. Phosphatidylinositol 3-kinase is required for integrin-stimulated AKT and Raf-1/mitogen-activated protein kinase pathway activation. Mol Cell Biol 1997;17:4406-4418.
    • (1997) Mol Cell Biol , vol.17 , pp. 4406-4418
    • King, W.G.1    Mattaliano, M.D.2    Chan, T.O.3    Tsichlis, P.N.4    Brugge, J.S.5
  • 40
    • 0030874021 scopus 로고    scopus 로고
    • Integrin-mediated activation of MAP kinase is independent of FAK: Evidence for dual integrin signaling pathways in fibroblasts
    • Lin TH, et al. Integrin-mediated activation of MAP kinase is independent of FAK: evidence for dual integrin signaling pathways in fibroblasts. J Cell Biol 1997;136:1385-1395.
    • (1997) J Cell Biol , vol.136 , pp. 1385-1395
    • Lin, T.H.1
  • 41
    • 0030909050 scopus 로고    scopus 로고
    • Suppression of integrin activation: A novel function of a Ras/Raf-initiated MAP kinase pathway
    • Hughes P, et al. Suppression of integrin activation: a novel function of a Ras/Raf-initiated MAP kinase pathway. Cell 1997;88:521-530.
    • (1997) Cell , vol.88 , pp. 521-530
    • Hughes, P.1
  • 42
    • 0034104592 scopus 로고    scopus 로고
    • Cell-substrate interactions and signaling through ILK
    • Dedhar S. Cell-substrate interactions and signaling through ILK. Curr Opin Cell Biol 2000;12:250-256.
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 250-256
    • Dedhar, S.1
  • 43
    • 0035969233 scopus 로고    scopus 로고
    • Integrin-linked kinase (ILK) and its interactors: A new paradigm for the coupling of extracellular matrix to actin cytoskeleton and signaling complexes
    • Wu C, Dedhar S. Integrin-linked kinase (ILK) and its interactors: a new paradigm for the coupling of extracellular matrix to actin cytoskeleton and signaling complexes. J Cell Biol 2001;155:505-510.
    • (2001) J Cell Biol , vol.155 , pp. 505-510
    • Wu, C.1    Dedhar, S.2
  • 44
    • 0000463651 scopus 로고    scopus 로고
    • The structural and mechanical complexity of cell-growth control
    • Huang S, Ingber DE. The structural and mechanical complexity of cell-growth control. Nat Cell Biol 1999;1:E131-E138.
    • (1999) Nat Cell Biol , vol.1
    • Huang, S.1    Ingber, D.E.2
  • 45
    • 0034886701 scopus 로고    scopus 로고
    • Integrin-specific activation of Rac controls progression through the G(1) phase of the cell cycle
    • Mettouchi A, et al. Integrin-specific activation of Rac controls progression through the G(1) phase of the cell cycle. Mol Cell 2001;8:115-127.
    • (2001) Mol Cell , vol.8 , pp. 115-127
    • Mettouchi, A.1
  • 46
    • 0033597825 scopus 로고    scopus 로고
    • Signal-regulated activation of serum response factor is mediated by changes in actin dynamics
    • Sotiropoulos A, Gineitis D, Copeland J, Treisman R. Signal-regulated activation of serum response factor is mediated by changes in actin dynamics. Cell 1999;98:159-169.
    • (1999) Cell , vol.98 , pp. 159-169
    • Sotiropoulos, A.1    Gineitis, D.2    Copeland, J.3    Treisman, R.4
  • 47
    • 0035253672 scopus 로고    scopus 로고
    • Coordinate signaling by integrins and receptor tyrosine kinases in the regulation of G1 phase cell-cycle progression
    • Assoian RK, Schwartz MA. Coordinate signaling by integrins and receptor tyrosine kinases in the regulation of G1 phase cell-cycle progression. Curr Opin Genet Dev 2001;11:48-53.
    • (2001) Curr Opin Genet Dev , vol.11 , pp. 48-53
    • Assoian, R.K.1    Schwartz, M.A.2
  • 48
    • 0030028947 scopus 로고    scopus 로고
    • Cytoskeletal integrity is required throughout the mitogen stimulation phase of the cell cycle and mediates the anchorage-dependent expression of cyclin D1
    • Bohmer PM, Scharf E, Assoian RK. Cytoskeletal integrity is required throughout the mitogen stimulation phase of the cell cycle and mediates the anchorage-dependent expression of cycfin D1. Mol Biol Cell 1996;7:101-111.
    • (1996) Mol Biol Cell , vol.7 , pp. 101-111
    • Bohmer, P.M.1    Scharf, E.2    Assoian, R.K.3
  • 49
    • 0034629319 scopus 로고    scopus 로고
    • Induction of anchorage-independent growth by transforming growth factor-beta linked to anchorage-independent expression of cyclin D1
    • Zhu X, Scharf E, Assoian RK. Induction of anchorage-independent growth by transforming growth factor-beta linked to anchorage-independent expression of cyclin D1. J Biol Chem 2000;275:6703-6706.
    • (2000) J Biol Chem , vol.275 , pp. 6703-6706
    • Zhu, X.1    Scharf, E.2    Assoian, R.K.3
  • 50
    • 0035954432 scopus 로고    scopus 로고
    • Role of the F-box protein Skp2 in adhesion-dependent cell cycle progression
    • Carrano AC, Pagano M. Role of the F-box protein Skp2 in adhesion-dependent cell cycle progression. J Cell Biol 2001;153:1381-1390.
    • (2001) J Cell Biol , vol.153 , pp. 1381-1390
    • Carrano, A.C.1    Pagano, M.2
  • 51
    • 0036364538 scopus 로고    scopus 로고
    • Integrin control of cell cycle: A new role for ubiquitin ligase
    • Pu QQ, Streuli CH. Integrin control of cell cycle: a new role for ubiquitin ligase. Bioessays 2002;24:17-21.
    • (2002) Bioessays , vol.24 , pp. 17-21
    • Pu, Q.Q.1    Streuli, C.H.2
  • 52
    • 0031739360 scopus 로고    scopus 로고
    • Control of cyclin D1, 27 (Kip1), and cell cycle progression in human capillary endothelial cells by cell shape and cytoskeletal tension
    • Huang S, Chen CS, Ingber DE. Control of cyclin D1, 27 (Kip1), and cell cycle progression in human capillary endothelial cells by cell shape and cytoskeletal tension. Mol Biol Cell 1998;9:3179-3193.
    • (1998) Mol Biol Cell , vol.9 , pp. 3179-3193
    • Huang, S.1    Chen, C.S.2    Ingber, D.E.3
  • 53
    • 0033136697 scopus 로고    scopus 로고
    • Anchorage dependence of mitogen-induced G1 to S transition in primary T lymphocytes
    • Geginat J, Bossi G, Bender JR, Pardi R. Anchorage dependence of mitogen-induced G1 to S transition in primary T lymphocytes. J Immunol 1999;162:5085-5093.
    • (1999) J Immunol , vol.162 , pp. 5085-5093
    • Geginat, J.1    Bossi, G.2    Bender, J.R.3    Pardi, R.4
  • 54
    • 0030589228 scopus 로고    scopus 로고
    • Impaired immune responses toward alloantigens and tumor cells but normal thymic selection in mice deficient in the beta2 integrin leukocyte function-associated antigen-1
    • Shier P, et al. Impaired immune responses toward alloantigens and tumor cells but normal thymic selection in mice deficient in the beta2 integrin leukocyte function-associated antigen-1. J Immunol 1996;157:5375-5386.
    • (1996) J Immunol , vol.157 , pp. 5375-5386
    • Shier, P.1
  • 55
    • 15844379199 scopus 로고    scopus 로고
    • LFA-1-deficient mice show normal CTL responses to virus but fail to reject immunogenic tumor
    • Schmits R, et al. LFA-1-deficient mice show normal CTL responses to virus but fail to reject immunogenic tumor. J Exp Med 1996;183:1415-1426.
    • (1996) J Exp Med , vol.183 , pp. 1415-1426
    • Schmits, R.1
  • 56
    • 0030701952 scopus 로고    scopus 로고
    • Distinct roles for LFA-1 and CD28 during activation of naive T cells: Adhesion versus co-stimulation
    • Bachmann MF, et al. Distinct roles for LFA-1 and CD28 during activation of naive T cells: adhesion versus co-stimulation. Immunity 1997;7:549-557.
    • (1997) Immunity , vol.7 , pp. 549-557
    • Bachmann, M.F.1
  • 59
    • 0032480279 scopus 로고    scopus 로고
    • Three-dimensional segregation of supramolecular activation clusters in T cells
    • Monks CR, Freiberg BA, Kupfer H, Sciaky N, Kupfer A. Three-dimensional segregation of supramolecular activation clusters in T cells. Nature 1998;395:82-86.
    • (1998) Nature , vol.395 , pp. 82-86
    • Monks, C.R.1    Freiberg, B.A.2    Kupfer, H.3    Sciaky, N.4    Kupfer, A.5
  • 60
    • 0033614036 scopus 로고    scopus 로고
    • Costimulation: Building an immunological synapse
    • Dustin ML, Shaw AS. Costimulation: building an immunological synapse. Science 1999;283:649-650.
    • (1999) Science , vol.283 , pp. 649-650
    • Dustin, M.L.1    Shaw, A.S.2
  • 61
    • 0033538574 scopus 로고    scopus 로고
    • The immunological synapse: A molecular machine controlling T cell activation
    • Grakoui A, et al. The immunological synapse: a molecular machine controlling T cell activation. Science 1999;285:221-227.
    • (1999) Science , vol.285 , pp. 221-227
    • Grakoui, A.1
  • 63
    • 0033136777 scopus 로고    scopus 로고
    • Signaling pathways activated by leukocyte function-associated Ag-1-dependent co-stimulation
    • Ni HT, Deeths MJ, Li W, Mueller DL, Mescher MF. Signaling pathways activated by leukocyte function-associated Ag-1-dependent co-stimulation. J Immunol 1999;162:5183-5189.
    • (1999) J Immunol , vol.162 , pp. 5183-5189
    • Ni, H.T.1    Deeths, M.J.2    Li, W.3    Mueller, D.L.4    Mescher, M.F.5
  • 64
    • 0033997963 scopus 로고    scopus 로고
    • CD28 and LFA-1 contribute to cyclosporin A-resistant T cell growth by stabilizing the IL-2 mRNA through distinct signaling pathways
    • Geginat J, Clissi B, Moro M, Dellabona P, Bender JR, Pardi R. CD28 and LFA-1 contribute to cyclosporin A-resistant T cell growth by stabilizing the IL-2 mRNA through distinct signaling pathways. Eur J Immunol 2000;30:1136-1144.
    • (2000) Eur J Immunol , vol.30 , pp. 1136-1144
    • Geginat, J.1    Clissi, B.2    Moro, M.3    Dellabona, P.4    Bender, J.R.5    Pardi, R.6
  • 65
    • 0035897407 scopus 로고    scopus 로고
    • Integrin-mediated adhesion regulates ERK nuclear translocation and phosphorylation of Elk-1
    • Aplin AE, Stewart SA, Assoian RK, Juliano RL. Integrin-mediated adhesion regulates ERK nuclear translocation and phosphorylation of Elk-1. J Cell Biol 2001;153:273-282.
    • (2001) J Cell Biol , vol.153 , pp. 273-282
    • Aplin, A.E.1    Stewart, S.A.2    Assoian, R.K.3    Juliano, R.L.4
  • 66
    • 0028172867 scopus 로고
    • Interleukin-2-mediated elimination of the p27Kip1 cyclin-dependent kinase inhibitor prevented by rapamycin
    • Nourse J, et al. Interleukin-2-mediated elimination of the p27Kip1 cyclin-dependent kinase inhibitor prevented by rapamycin. Nature 1994;372:570-573.
    • (1994) Nature , vol.372 , pp. 570-573
    • Nourse, J.1
  • 67
    • 0027441885 scopus 로고
    • IL-2-dependent induction of G1 cyclins in primary T cells is not blocked by rapamycin or cyclosporin A
    • Turner JM. IL-2-dependent induction of G1 cyclins in primary T cells is not blocked by rapamycin or cyclosporin A. Int Immunol 1993;5:1199-1209.
    • (1993) Int Immunol , vol.5 , pp. 1199-1209
    • Turner, J.M.1
  • 69
    • 0034698066 scopus 로고    scopus 로고
    • Glucocorticoid-mediated destabilization of cyclin D3 mRNA involves RNA-protein interactions in the 3′-untranslated region of the mRNA
    • Garcia-Gras EA, Chi P, Thompson EA. Glucocorticoid-mediated destabilization of cyclin D3 mRNA involves RNA-protein interactions in the 3′-untranslated region of the mRNA. J Biol Chem 2000;275:22001-22008.
    • (2000) J Biol Chem , vol.275 , pp. 22001-22008
    • Garcia-Gras, E.A.1    Chi, P.2    Thompson, E.A.3
  • 71
    • 0010586014 scopus 로고    scopus 로고
    • The transcription factor GATA-3 is necessary and sufficient for Th2 cytokine gene expression in CD4 T cells
    • Zheng W, Flavell PA. The transcription factor GATA-3 is necessary and sufficient for Th2 cytokine gene expression in CD4 T cells. Cell 1997;100:655-669.
    • (1997) Cell , vol.100 , pp. 655-669
    • Zheng, W.1    Flavell, P.A.2
  • 72
    • 0032534057 scopus 로고    scopus 로고
    • LFA-1 interaction with ICAM-1 and ICAM-2 regulates Th2 cytokine production
    • Salomon B, Bluestone JA. LFA-1 interaction with ICAM-1 and ICAM-2 regulates Th2 cytokine production. J Immunol 1998;161:5138-5142.
    • (1998) J Immunol , vol.161 , pp. 5138-5142
    • Salomon, B.1    Bluestone, J.A.2
  • 73
    • 0033013463 scopus 로고    scopus 로고
    • Intercellular adhesion molecule-1 inhibits interleukin 4 production by naive T cells
    • Luksch CR, et al. Intercellular adhesion molecule-1 inhibits interleukin 4 production by naive T cells. Proc Natl Acad Sci USA 1999;96:3023-3028.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3023-3028
    • Luksch, C.R.1
  • 74
    • 0033961475 scopus 로고    scopus 로고
    • Inhibition of IL-4 responses after T cell priming in the context of LFA-1 co-stimulation is not reversed by restimulation in the presence of CD28 co-stimulation
    • Jenks SA, Miller J. Inhibition of IL-4 responses after T cell priming in the context of LFA-1 co-stimulation is not reversed by restimulation in the presence of CD28 co-stimulation. J Immunol 2000;164:72-78.
    • (2000) J Immunol , vol.164 , pp. 72-78
    • Jenks, S.A.1    Miller, J.2
  • 75
    • 0037083338 scopus 로고    scopus 로고
    • Intercellular adhesion molecule-1/LFA-1 ligation favors human Th1 development
    • Smits HH, et al. Intercellular adhesion molecule-1/LFA-1 ligation favors human Th1 development. J Immunol 2002;168:1710-1716.
    • (2002) J Immunol , vol.168 , pp. 1710-1716
    • Smits, H.H.1
  • 76
    • 0029003507 scopus 로고
    • Regulation of interleukin 2 gene expression by CD28 co-stimulation in mouse T-cell clones: Both nuclear and cytoplasmic RNAs are regulated with complex kinetics
    • Umlauf SW, Beverly B, Lantz O, Schwartz RH. Regulation of interleukin 2 gene expression by CD28 co-stimulation in mouse T-cell clones: both nuclear and cytoplasmic RNAs are regulated with complex kinetics. Mol Cell Biol 1995;15:3197-3205.
    • (1995) Mol Cell Biol , vol.15 , pp. 3197-3205
    • Umlauf, S.W.1    Beverly, B.2    Lantz, O.3    Schwartz, R.H.4
  • 77
    • 0026756730 scopus 로고
    • Integrins as a primary signal transduction molecule regulating monocyte immediate - Early gene induction
    • Yurochko AD, Liu DY, Eierman D, Haskill D. Integrins as a primary signal transduction molecule regulating monocyte immediate - early gene induction. Proc Natl Acad Sci USA 1992;89:9034-9038.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 9034-9038
    • Yurochko, A.D.1    Liu, D.Y.2    Eierman, D.3    Haskill, D.4
  • 78
    • 0023884392 scopus 로고
    • Adherence induces selective mRNA expression of monocyte mediators and proto-oncogenes
    • Haskill S, Johnson C, Eierman D, Becker S, Warren K. Adherence induces selective mRNA expression of monocyte mediators and proto-oncogenes. J Immunol 1988;140:1690-1694.
    • (1988) J Immunol , vol.140 , pp. 1690-1694
    • Haskill, S.1    Johnson, C.2    Eierman, D.3    Becker, S.4    Warren, K.5
  • 79
    • 0025277465 scopus 로고
    • Monocyte adherence results in selective induction of novel genes sharing homology with mediators of inflammation and tissue repair
    • Sporn SA, et al. Monocyte adherence results in selective induction of novel genes sharing homology with mediators of inflammation and tissue repair. J Immunol 1990;144:4434-4441.
    • (1990) J Immunol , vol.144 , pp. 4434-4441
    • Sporn, S.A.1
  • 80
    • 0028985203 scopus 로고
    • Transcription-independent turnover of I kappa B alpha during monocyte adherence: Implications for a translational component regulating I kappa B alpha/MAD-3 mRNA levels
    • Lofquist AK, Monda K, Morris JS, Haskill S. Transcription-independent turnover of I kappa B alpha during monocyte adherence: implications for a translational component regulating I kappa B alpha/MAD-3 mRNA levels. Mol Cell Biol 1995;15:1737-1746.
    • (1995) Mol Cell Biol , vol.15 , pp. 1737-1746
    • Lofquist, A.K.1    Monda, K.2    Morris, J.S.3    Haskill, S.4
  • 81
    • 0033799989 scopus 로고    scopus 로고
    • Differential role of tyrosine phosphorylation in adhesion-induced transcription, mRNA stability, and cytoskeletal organization in human monocytes
    • Mondal K, Sirenko OI, Lofquist AK, Morris JS, Haskill JS, Watson JM. Differential role of tyrosine phosphorylation in adhesion-induced transcription, mRNA stability, and cytoskeletal organization in human monocytes. J Leukoc Biol 2000;67:216-225.
    • (2000) J Leukoc Biol , vol.67 , pp. 216-225
    • Mondal, K.1    Sirenko, O.I.2    Lofquist, A.K.3    Morris, J.S.4    Haskill, J.S.5    Watson, J.M.6
  • 83
    • 0035500637 scopus 로고    scopus 로고
    • Molecular mechanisms of IL-2 gene regulation following co-stimulation through LFA-1
    • Abraham C, Miller J. Molecular mechanisms of IL-2 gene regulation following co-stimulation through LFA-1. J Immunol 2001;167:5193-5201.
    • (2001) J Immunol , vol.167 , pp. 5193-5201
    • Abraham, C.1    Miller, J.2
  • 84
    • 0034657357 scopus 로고    scopus 로고
    • Nucleolin and YB-1 are required for JNK-mediated interleukin-2 mRNA stabilization during T-cell activation
    • Chen CY, et al. Nucleolin and YB-1 are required for JNK-mediated interleukin-2 mRNA stabilization during T-cell activation. Genes Dev 2000;14:1236-1248.
    • (2000) Genes Dev , vol.14 , pp. 1236-1248
    • Chen, C.Y.1
  • 85
    • 0036008013 scopus 로고    scopus 로고
    • JAM-1 is a ligand of the beta (2) integrin LFA-1 involved in transendothelial migration of leukocytes
    • Ostermann G, Weber KS, Zerneke A, Schroder A, Weber C. JAM-1 is a ligand of the beta (2) integrin LFA-1 involved in transendothelial migration of leukocytes. Nat Immunol 2002;3:116-118.
    • (2002) Nat Immunol , vol.3 , pp. 116-118
    • Ostermann, G.1    Weber, K.S.2    Zerneke, A.3    Schroder, A.4    Weber, C.5
  • 86
    • 0034787296 scopus 로고    scopus 로고
    • Differential regulation of transendothelial migration of THP-1 cells by ICAM-1/LFA-1 and VCAM-1/VLA-4
    • Ronald JA, Ionescu CV, Rogers KA, Sandig M. Differential regulation of transendothelial migration of THP-1 cells by ICAM-1/LFA-1 and VCAM-1/VLA-4. J Leukoc Biol 2001;70:601-609.
    • (2001) J Leukoc Biol , vol.70 , pp. 601-609
    • Ronald, J.A.1    Ionescu, C.V.2    Rogers, K.A.3    Sandig, M.4
  • 87
    • 0030322911 scopus 로고    scopus 로고
    • The roles of adhesion molecules and proteinases in lymphocyte transendothelial migration
    • Madri JA, Graesser D, Haas T. The roles of adhesion molecules and proteinases in lymphocyte transendothelial migration. Biochem Cell Biol 1996;74:749-757.
    • (1996) Biochem Cell Biol , vol.74 , pp. 749-757
    • Madri, J.A.1    Graesser, D.2    Haas, T.3
  • 88
    • 0029150795 scopus 로고
    • Proteolytic remodeling of extracellular matrix
    • Birkedal-Hansen H. Proteolytic remodeling of extracellular matrix. Curr Opin Cell Biol 1995;7:728-735.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 728-735
    • Birkedal-Hansen, H.1
  • 89
    • 0028362088 scopus 로고
    • The induction of 72-kD gelatinase in T cells upon adhesion to endothelial cells is VCAM-1 dependent
    • Romanic AM, Madri JA. The induction of 72-kD gelatinase in T cells upon adhesion to endothelial cells is VCAM-1 dependent. J Cell Biol 1994;125:1165-1178.
    • (1994) J Cell Biol , vol.125 , pp. 1165-1178
    • Romanic, A.M.1    Madri, J.A.2
  • 90
    • 0034703180 scopus 로고    scopus 로고
    • Distinct roles for matrix metalloproteinase-2 and alpha4 integrin in autormmune T cell extravasation and residency in brain parenchyma during experimental autoimmune encephalomyelitis
    • Graesser D, Mahooti S, Madri JA. Distinct roles for matrix metalloproteinase-2 and alpha4 integrin in autormmune T cell extravasation and residency in brain parenchyma during experimental autoimmune encephalomyelitis. J Neuroimmunol 2000;109:121-131.
    • (2000) J Neuroimmunol , vol.109 , pp. 121-131
    • Graesser, D.1    Mahooti, S.2    Madri, J.A.3
  • 91
    • 0032883939 scopus 로고    scopus 로고
    • Fibronectin upregulates gelatinase B (MMP-9) and induces coordinated expression of gelatinase A (MMP-2) and its activator MT1-MMP (MMP-14) by human T lymphocyte cell lines. A process repressed through RAS/MAP kinase signaling pathways
    • Esparza J, et al. Fibronectin upregulates gelatinase B (MMP-9) and induces coordinated expression of gelatinase A (MMP-2) and its activator MT1-MMP (MMP-14) by human T lymphocyte cell lines. A process repressed through RAS/MAP kinase signaling pathways. Blood 1999;94:2754-2766.
    • (1999) Blood , vol.94 , pp. 2754-2766
    • Esparza, J.1
  • 92
    • 0029757446 scopus 로고    scopus 로고
    • Integrin-dependent induction of functional urokinase receptors in primary T lymphocytes
    • Bianchi E, et al. Integrin-dependent induction of functional urokinase receptors in primary T lymphocytes. J Clin Invest 1996;98:1133-1141.
    • (1996) J Clin Invest , vol.98 , pp. 1133-1141
    • Bianchi, E.1
  • 94
    • 0034725593 scopus 로고    scopus 로고
    • Integrins and actin filaments: Reciprocal regulation of cell adhesion and signaling
    • Calderwood DA, Shattil SJ, Ginsberg MH. Integrins and actin filaments: reciprocal regulation of cell adhesion and signaling. J Biol Chem 2000;275:22607-22610.
    • (2000) J Biol Chem , vol.275 , pp. 22607-22610
    • Calderwood, D.A.1    Shattil, S.J.2    Ginsberg, M.H.3
  • 95
    • 0035889083 scopus 로고    scopus 로고
    • Regulation of nucleocytoplasmic trafficking by cell adhesion receptors and the cytoskeleton
    • Aplin AE, Juliano RL. Regulation of nucleocytoplasmic trafficking by cell adhesion receptors and the cytoskeleton. J Cell Biol 2001;155:187-191.
    • (2001) J Cell Biol , vol.155 , pp. 187-191
    • Aplin, A.E.1    Juliano, R.L.2
  • 96
  • 97
    • 0034611731 scopus 로고    scopus 로고
    • Integrin LFA-1 interacts with the transcriptional co-activator JAB1 to modulate AP-1 activity
    • Bianchi E, et al. Integrin LFA-1 interacts with the transcriptional co-activator JAB1 to modulate AP-1 activity. Nature 2000;404:617-621.
    • (2000) Nature , vol.404 , pp. 617-621
    • Bianchi, E.1
  • 98
    • 0029761277 scopus 로고    scopus 로고
    • A new group of conserved coactivators that increase the specificity of AP-1 transcription factors
    • Claret FX, Hibi M, Dhut S, Toda T, Karin M. A new group of conserved coactivators that increase the specificity of AP-1 transcription factors. Nature 1996;383:453-457.
    • (1996) Nature , vol.383 , pp. 453-457
    • Claret, F.X.1    Hibi, M.2    Dhut, S.3    Toda, T.4    Karin, M.5
  • 99
    • 0033545636 scopus 로고    scopus 로고
    • Degradation of the cyclin-dependent-kinase inhibitor p27Kip1 is instigated by Jab1
    • Tomoda K, Kubota Y, Kato J. Degradation of the cyclin-dependent-kinase inhibitor p27Kip1 is instigated by Jab1. Nature 1999;398:160-165.
    • (1999) Nature , vol.398 , pp. 160-165
    • Tomoda, K.1    Kubota, Y.2    Kato, J.3
  • 100
    • 0033621780 scopus 로고    scopus 로고
    • p27kip1 functions as an anergy factor inhibiting interleukin 2 transcription and clonal expansion of alloreactive human and mouse helper T lymphocytes
    • Boussiotis VA, et al. p27kip1 functions as an anergy factor inhibiting interleukin 2 transcription and clonal expansion of alloreactive human and mouse helper T lymphocytes. Nat Med 2000;6:290-297.
    • (2000) Nat Med , vol.6 , pp. 290-297
    • Boussiotis, V.A.1
  • 101
    • 0037127256 scopus 로고    scopus 로고
    • The cytoplasmic shuttling and subsequent degradation of p27Kip1 mediated by Jab1/CSN5 and the COP9 signalosome complex
    • Tomoda K, et al. The cytoplasmic shuttling and subsequent degradation of p27Kip1 mediated by Jab1/CSN5 and the COP9 signalosome complex. J Biol Chem 2002;277:2302-2310.
    • (2002) J Biol Chem , vol.277 , pp. 2302-2310
    • Tomoda, K.1
  • 102
    • 0035098524 scopus 로고    scopus 로고
    • JAB1/CSN5 and the COP9 signalosome. A complex situation
    • Chamovitz DA, Segal D. JAB1/CSN5 and the COP9 signalosome. A complex situation. EMBO Rep 2001;2:96-101.
    • (2001) EMBO Rep , vol.2 , pp. 96-101
    • Chamovitz, D.A.1    Segal, D.2
  • 103
    • 0034491482 scopus 로고    scopus 로고
    • The COP/DET/FUS proteins-regulators of eukaryotic growth and development
    • Schwechheimer C, Deng XW. The COP/DET/FUS proteins-regulators of eukaryotic growth and development. Semin Cell Dev Biol 2000;11:495-503.
    • (2000) Semin Cell Dev Biol , vol.11 , pp. 495-503
    • Schwechheimer, C.1    Deng, X.W.2
  • 104
    • 0032993486 scopus 로고    scopus 로고
    • Making sense of the COP9 signalosome. A regulatory protein complex conserved from Arabidopsis to human
    • Wei N, Deng XW. Making sense of the COP9 signalosome. A regulatory protein complex conserved from Arabidopsis to human. Trends Genet 1999;15:98-103.
    • (1999) Trends Genet , vol.15 , pp. 98-103
    • Wei, N.1    Deng, X.W.2
  • 105
    • 0031921216 scopus 로고    scopus 로고
    • A novel protein complex involved in signal transduction possessing similarities to 26S proteasome subunits
    • Seeger M, et al. A novel protein complex involved in signal transduction possessing similarities to 26S proteasome subunits. FASEB J 1998;12:469-478.
    • (1998) FASEB J , vol.12 , pp. 469-478
    • Seeger, M.1
  • 106
    • 0035478483 scopus 로고    scopus 로고
    • COP9 signalosome revisited: A novel mediator of protein degradation
    • Schwechheimer C, Deng XW. COP9 signalosome revisited: a novel mediator of protein degradation. Trends Cell Biol 2001;11:420-426.
    • (2001) Trends Cell Biol , vol.11 , pp. 420-426
    • Schwechheimer, C.1    Deng, X.W.2
  • 107
    • 0035907047 scopus 로고    scopus 로고
    • Interactions of the COP9 signalosome with the E3 ubiquitin ligase SCFTIRI in mediating auxin response
    • Schwechheimer C, et al. Interactions of the COP9 signalosome with the E3 ubiquitin ligase SCFTIRI in mediating auxin response. Science 2001;292:1379-1382.
    • (2001) Science , vol.292 , pp. 1379-1382
    • Schwechheimer, C.1
  • 108
    • 0033105621 scopus 로고    scopus 로고
    • The role of COP1 in repression of Arabidopsis photomorphogenic development
    • Osterlund MT, Ang LH, Deng XW. The role of COP1 in repression of Arabidopsis photomorphogenic development. Trends Cell Biol 1999;9:113-118.
    • (1999) Trends Cell Biol , vol.9 , pp. 113-118
    • Osterlund, M.T.1    Ang, L.H.2    Deng, X.W.3
  • 109
    • 0034713297 scopus 로고    scopus 로고
    • Targeted destabilization of HY5 during light-regulated development of Arabidopsis
    • Osterlund MT, Hardtke CS, Wei N, Deng XW. Targeted destabilization of HY5 during light-regulated development of Arabidopsis. Nature 2000;405:462-466.
    • (2000) Nature , vol.405 , pp. 462-466
    • Osterlund, M.T.1    Hardtke, C.S.2    Wei, N.3    Deng, X.W.4
  • 110
    • 0033534648 scopus 로고    scopus 로고
    • Characterization of two subunits of Arabidopsis 19S proteasome regulatory complex and its possible interaction with the COP9 complex
    • Kwok SF, Staub JM, Deng XW. Characterization of two subunits of Arabidopsis 19S proteasome regulatory complex and its possible interaction with the COP9 complex. J Mol Biol 1999;285:85-95.
    • (1999) J Mol Biol , vol.285 , pp. 85-95
    • Kwok, S.F.1    Staub, J.M.2    Deng, X.W.3
  • 111
    • 0032514947 scopus 로고    scopus 로고
    • The Arabidopsis homologue of an eIF3 complex subunit associates with the COP9 complex
    • Karniol B, et al. The Arabidopsis homologue of an eIF3 complex subunit associates with the COP9 complex. FEBS Lett 1998;439:173-179.
    • (1998) FEBS Lett , vol.439 , pp. 173-179
    • Karniol, B.1
  • 112
    • 0035906430 scopus 로고    scopus 로고
    • Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome
    • Lyapina S, et al. Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome. Science 2001;292:1382-1385.
    • (2001) Science , vol.292 , pp. 1382-1385
    • Lyapina, S.1
  • 113
    • 0036195134 scopus 로고    scopus 로고
    • An intact NEDD8 pathway is required for Cullin-dependent ubiquitylation in mammalian cells
    • Ohh M, et al. An intact NEDD8 pathway is required for Cullin-dependent ubiquitylation in mammalian cells. EMBO Rep 2002;3:177-182.
    • (2002) EMBO Rep , vol.3 , pp. 177-182
    • Ohh, M.1
  • 114
    • 0035895604 scopus 로고    scopus 로고
    • Regulation of the G1 to S transition by the ubiquitin pathway
    • DeSalle LM, Pagano M. Regulation of the G1 to S transition by the ubiquitin pathway. FEBS Lett 2001;490:179-189.
    • (2001) FEBS Lett , vol.490 , pp. 179-189
    • DeSalle, L.M.1    Pagano, M.2
  • 115
    • 0033612572 scopus 로고    scopus 로고
    • Integrin-mediated activation of focal adhesion kinase is required for signaling to Jun NH2-terminal kinase and progression through the G1 phase of the cell cycle
    • Oktay M, Wary KK, Dans M, Birge RB, Giancotti FG. Integrin-mediated activation of focal adhesion kinase is required for signaling to Jun NH2-terminal kinase and progression through the G1 phase of the cell cycle. J Cell Biol 1999;145:1461-1469.
    • (1999) J Cell Biol , vol.145 , pp. 1461-1469
    • Oktay, M.1    Wary, K.K.2    Dans, M.3    Birge, R.B.4    Giancotti, F.G.5
  • 116
    • 0035910411 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha activation of the c-Jun N-terminal kinase pathway in human neutrophils. Integrin involvement in a pathway leading from cytoplasmic tyrosine kinases apoptosis
    • Avdi NJ, et al. Tumor necrosis factor-alpha activation of the c-Jun N-terminal kinase pathway in human neutrophils. Integrin involvement in a pathway leading from cytoplasmic tyrosine kinases apoptosis. J Biol Chem 2001;276:2189-2199.
    • (2001) J Biol Chem , vol.276 , pp. 2189-2199
    • Avdi, N.J.1
  • 118
    • 0028234529 scopus 로고
    • Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins
    • Darnell JE Jr, Kerr IM, Stark GR. Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins. Science 1994;264:1415-1421.
    • (1994) Science , vol.264 , pp. 1415-1421
    • Darnell J.E., Jr.1    Kerr, I.M.2    Stark, G.R.3
  • 119
    • 0030840464 scopus 로고    scopus 로고
    • STATs and gene regulation
    • Darnell JE Jr. STATs and gene regulation. Science 1997;277:1630-1635.
    • (1997) Science , vol.277 , pp. 1630-1635
    • Darnell J.E., Jr.1
  • 120
    • 0028925284 scopus 로고
    • A direct signaling pathway through tyrosine kinase activation of SH2 domain-containing transcription factors
    • Fu XY. A direct signaling pathway through tyrosine kinase activation of SH2 domain-containing transcription factors. J Leukoc Biol 1995;57:529-535.
    • (1995) J Leukoc Biol , vol.57 , pp. 529-535
    • Fu, X.Y.1
  • 121
    • 0030765924 scopus 로고    scopus 로고
    • Jaks, STATs, cytokine signal transduction, and immunoregulation: Are we there yet?
    • O'Shea JJ. Jaks, STATs, cytokine signal transduction, and immunoregulation: are we there yet? Immunity 1997;7:1-11.
    • (1997) Immunity , vol.7 , pp. 1-11
    • O'Shea, J.J.1
  • 122
    • 0031919849 scopus 로고    scopus 로고
    • Jaks and STATs: Biological implications
    • Leonard WJ, O'Shea JJ. Jaks and STATs: biological implications. Annu Rev Immunol 1998;16:293-322.
    • (1998) Annu Rev Immunol , vol.16 , pp. 293-322
    • Leonard, W.J.1    O'Shea, J.J.2
  • 124
    • 0035378669 scopus 로고    scopus 로고
    • Focal adhesion kinase activates STAT1 in integrin-mediated cell migration and adhesion
    • Xie B, et al. Focal adhesion kinase activates STAT1 in integrin-mediated cell migration and adhesion. J Biol Chem 2001;276:19512-19523.
    • (2001) J Biol Chem , vol.276 , pp. 19512-19523
    • Xie, B.1
  • 125
    • 0032850424 scopus 로고    scopus 로고
    • Integrin-mediated adhesion of endothelial cells induces JAK2 and STAT5A activation: Role in the control of c-fos gene expression
    • Brizzi MF, et al. Integrin-mediated adhesion of endothelial cells induces JAK2 and STAT5A activation: role in the control of c-fos gene expression. Mol Biol Cell 1999;10:3463-3471.
    • (1999) Mol Biol Cell , vol.10 , pp. 3463-3471
    • Brizzi, M.F.1
  • 126
    • 0000253450 scopus 로고    scopus 로고
    • Posttranscriptional regulation of urokinase plasminogen activator receptor messenger RNA levels by leukocyte integrin engagement
    • Wang GJ, Collinge M, Blasi F, Pardi R, Bender JR. Posttranscriptional regulation of urokinase plasminogen activator receptor messenger RNA levels by leukocyte integrin engagement. Proc Natl Acad Sci USA 1998;95:6296-6301.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6296-6301
    • Wang, G.J.1    Collinge, M.2    Blasi, F.3    Pardi, R.4    Bender, J.R.5
  • 127
    • 0028788194 scopus 로고
    • AU-rich elements: Characterization and importance in mRNA degradation
    • Chen CY, Shyu A-B. AU-rich elements: characterization and importance in mRNA degradation. Trends Biochem Sci 1995;20:465-470.
    • (1995) Trends Biochem Sci , vol.20 , pp. 465-470
    • Chen, C.Y.1    Shyu, A.-B.2
  • 128
    • 0010623164 scopus 로고
    • Regulation of interleukin 3 mRNA expression in mast cells occurs at the posttranscriptional level and is mediated by calcium ions
    • Wodnar-Filipowicz A, Moroni C. Regulation of interleukin 3 mRNA expression in mast cells occurs at the posttranscriptional level and is mediated by calcium ions. Ultrasound Obstet Gynecol 1990;6:447-450.
    • (1990) Ultrasound Obstet Gynecol , vol.6 , pp. 447-450
    • Wodnar-Filipowicz, A.1    Moroni, C.2
  • 129
    • 0027335519 scopus 로고
    • + ionophore A23187-dependent stabilization of granulocyte-macrophage colony-stimulating factor messenger RNA in murine thymoma EL-4 cells is mediated through two distinct regions in the 3′-untranslated region
    • + ionophore A23187-dependent stabilization of granulocyte-macrophage colony-stimulating factor messenger RNA in murine thymoma EL-4 cells is mediated through two distinct regions in the 3′-untranslated region. J Immunol 1993;150:4386-4394.
    • (1993) J Immunol , vol.150 , pp. 4386-4394
    • Iwai, Y.1    Akahane, K.2    Pluznik, D.H.3    Cohen, R.B.4
  • 130
    • 0031027464 scopus 로고    scopus 로고
    • Posttranscriptional regulation of urokinase receptor mRNA: Identification of a novel urokinase receptor mRNA binding protein in human mesothelioma cells
    • Shetty S, Kumar A, Idell S. Posttranscriptional regulation of urokinase receptor mRNA: identification of a novel urokinase receptor mRNA binding protein in human mesothelioma cells. Mol Cell Biol 1997;17:1075-1083.
    • (1997) Mol Cell Biol , vol.17 , pp. 1075-1083
    • Shetty, S.1    Kumar, A.2    Idell, S.3
  • 131
    • 0028129989 scopus 로고
    • Conserved structures and diversity of functions of RNA-binding proteins
    • Burd CG, Greyfuss G. Conserved structures and diversity of functions of RNA-binding proteins. Science 1994;265:615-621.
    • (1994) Science , vol.265 , pp. 615-621
    • Burd, C.G.1    Greyfuss, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.