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Volumn 10, Issue 4, 1996, Pages 215-237

Signal transduction and the u-PA/ u-PAR system

Author keywords

[No Author keywords available]

Indexed keywords

UROKINASE; UROKINASE RECEPTOR;

EID: 0029830493     PISSN: 02689499     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0268-9499(96)80018-X     Document Type: Review
Times cited : (67)

References (253)
  • 3
    • 0028618937 scopus 로고    scopus 로고
    • Structure-function relationships for the EGF/TGF-alpha family of mitogens
    • Nice E C, Burgess A W.
    • Groenen L C, Nice E C, Burgess A W. Structure-function relationships for the EGF/TGF-alpha family of mitogens. Growth Factors 1994; 11: 235-57.
    • Growth Factors 1994; 11: 235-57.
    • Groenen, L.C.1
  • 5
    • 0028872649 scopus 로고    scopus 로고
    • Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation
    • Marshall C J. Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation. Cell 1995; 80: 179-85.
    • Cell 1995; 80: 179-85.
    • Marshall, C.J.1
  • 7
    • 0028170817 scopus 로고    scopus 로고
    • Receptor protein-tyrosine kinase and their signal transduction pathways
    • Hunter T, Lindberg R A.
    • van der Geer P, Hunter T, Lindberg R A. Receptor protein-tyrosine kinase and their signal transduction pathways. Annu Rev Cell Biol 1994; 10: 251-337.
    • Annu Rev Cell Biol 1994; 10: 251-337.
    • Geer, P.1
  • 8
    • 0023665111 scopus 로고    scopus 로고
    • Common elements in growth factor stimulation and oncogenic transformation: 85 kd phosphoprotein and phosphatidylinositol kinase activity
    • Whitman M, Schaffhausen B et al.
    • Kaplan D R, Whitman M, Schaffhausen B et al. Common elements in growth factor stimulation and oncogenic transformation: 85 kd phosphoprotein and phosphatidylinositol kinase activity. Cell 1987; 50: 1021-29.
    • Cell 1987; 50: 1021-29.
    • Kaplan, D.R.1
  • 9
    • 0028178928 scopus 로고    scopus 로고
    • s6k activation mediated by phosphatidylinositol-3-OH kinase
    • Grammer T C, Lemon K P, Kazlauskas A, Blenis J.
    • s6k activation mediated by phosphatidylinositol-3-OH kinase. Nature 1994; 370: 71-5.
    • Nature 1994; 370: 71-5.
    • Chung, J.1
  • 10
    • 0026662412 scopus 로고    scopus 로고
    • Inhibition or down-regulation of protein kinase C attenuates late phase p70s6k activation induced by epidermal growth factor but not by platelet-derived growth factor or insulin
    • Vulevic D, Lane H A, Thomas G.
    • Susa M, Vulevic D, Lane H A, Thomas G. Inhibition or down-regulation of protein kinase C attenuates late phase p70s6k activation induced by epidermal growth factor but not by platelet-derived growth factor or insulin. J Biol Chem 1992; 267: 6905-9.
    • J Biol Chem 1992; 267: 6905-9.
    • Susa, M.1
  • 12
    • 0024380391 scopus 로고    scopus 로고
    • Phospholipase C-γ is a substrate for the PDGF and EGF receptor protein-tyrosine kinases in vivo and in vitro
    • Suh P G, Rhee S G, Hunter T.
    • Meisenhelder J, Suh P G, Rhee S G, Hunter T. Phospholipase C-γ is a substrate for the PDGF and EGF receptor protein-tyrosine kinases in vivo and in vitro. Cell 1989; 57: 1109-22.
    • Cell 1989; 57: 1109-22.
    • Meisenhelder, J.1
  • 13
    • 0028338460 scopus 로고    scopus 로고
    • Nerve growth factor activates a Ras-dependent protein kinase that stimulates c-fos transcription via phosphorylation of CREB
    • Bonni A, Greenberg M E.
    • Ginty D D, Bonni A, Greenberg M E. Nerve growth factor activates a Ras-dependent protein kinase that stimulates c-fos transcription via phosphorylation of CREB. Cell 1994; 77: 713-25.
    • Cell 1994; 77: 713-25.
    • Ginty, D.D.1
  • 14
    • 0027372119 scopus 로고    scopus 로고
    • Transcription factor p91 interacts with the epidermal growth factor receptor and mediates the activation of the c-fos gene promoter
    • Zhang J-J.
    • Fu X-Y, Zhang J-J. Transcription factor p91 interacts with the epidermal growth factor receptor and mediates the activation of the c-fos gene promoter. Cell 1993; 74: 1135-45.
    • Cell 1993; 74: 1135-45.
    • Fu, X.-Y.1
  • 15
    • 0025122589 scopus 로고    scopus 로고
    • Diverse forms of a receptor for acidic and basic fibroblast growth factors
    • Lee P L, Williams L T.
    • Johnson D E, Lee P L, Williams L T. Diverse forms of a receptor for acidic and basic fibroblast growth factors. Mol Cell Biol 1990; 10: 4728-36.
    • Mol Cell Biol 1990; 10: 4728-36.
    • Johnson, D.E.1
  • 16
    • 0026345394 scopus 로고    scopus 로고
    • Protein kinase catalytic domain sequence database: Identification of conserved features of primary structure and classification of family members
    • Quinn A M.
    • Hanks S K, Quinn A M. Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. Methods Enzymol 1991; 200: 38-61.
    • Methods Enzymol 1991; 200: 38-61.
    • Hanks, S.K.1
  • 17
    • 0023885305 scopus 로고    scopus 로고
    • The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains
    • Quinn A M, Hunter T.
    • Hanks S K, Quinn A M, Hunter T. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 1988; 241: 42-52.
    • Science 1988; 241: 42-52.
    • Hanks, S.K.1
  • 18
    • 0025771101 scopus 로고    scopus 로고
    • Scatter factor and hepatocyte growth factor are indistinguishable ligands for the Met receptor
    • Weidner K M, Vigna E et al.
    • Naldini L, Weidner K M, Vigna E et al. Scatter factor and hepatocyte growth factor are indistinguishable ligands for the Met receptor. EMBOJ 1991; 10: 2867-78
    • EMBOJ 1991; 10: 2867-78
    • Naldini, L.1
  • 19
    • 0040269807 scopus 로고    scopus 로고
    • Hepatocyte growth factor and its receptor
    • Naldini L, Tamagnone L et al. the tyrosine kinase encoded by the c-MET proto-oncogene.
    • Vigna E, Naldini L, Tamagnone L et al. Hepatocyte growth factor and its receptor, the tyrosine kinase encoded by the c-MET proto-oncogene. Cell Mol Biol 1994; 40: 597-604
    • Cell Mol Biol 1994; 40: 597-604
    • Vigna, E.1
  • 20
    • 0027528768 scopus 로고    scopus 로고
    • Similarities and differences in the way neurotrophins interact with the Trk receptors in neuronal and nonneuronal cells
    • Stitt T N, Tapley P et al.
    • Ip N Y, Stitt T N, Tapley P et al. Similarities and differences in the way neurotrophins interact with the Trk receptors in neuronal and nonneuronal cells. Neuron 1993; 10: 137-49.
    • Neuron 1993; 10: 137-49.
    • Ip, N.Y.1
  • 21
    • 0026332810 scopus 로고    scopus 로고
    • Dimerization of the extracellular domain of the human growth hormone by a single hormone molecule
    • Ultsch M, De Vos A M, Mulkerrin M G, Clauser K R, Wells J A.
    • Cunningham B C, Ultsch M, De Vos A M, Mulkerrin M G, Clauser K R, Wells J A. Dimerization of the extracellular domain of the human growth hormone by a single hormone molecule. Science 1991; 254: 821-5.
    • Science 1991; 254: 821-5.
    • Cunningham, B.C.1
  • 22
    • 0024426043 scopus 로고    scopus 로고
    • Isoform-specific induction of actin reorganization by platelet-derived growth factor suggests that the functionally active receptor is a dimer
    • Mellstrom K, Heldin C H, Westermark B.
    • Hammacher A, Mellstrom K, Heldin C H, Westermark B. Isoform-specific induction of actin reorganization by platelet-derived growth factor suggests that the functionally active receptor is a dimer. EMBO J 1989; 8: 2489-95.
    • EMBO J 1989; 8: 2489-95.
    • Hammacher, A.1
  • 23
    • 0026644455 scopus 로고    scopus 로고
    • Autophosphorylation promotes complex formation of recombinant hepatocyte growth factor receptor with cytoplasmic effectors containing SH2 domains
    • Maina F, Gout I et al.
    • Bardelli A, Maina F, Gout I et al. Autophosphorylation promotes complex formation of recombinant hepatocyte growth factor receptor with cytoplasmic effectors containing SH2 domains. Oncogene 1992; 7: 1973-8.
    • Oncogene 1992; 7: 1973-8.
    • Bardelli, A.1
  • 25
    • 0028958025 scopus 로고    scopus 로고
    • Src family protein tyrosine kinases and cellular signal transduction pathways
    • Courtneidge S A.
    • Erpel T, Courtneidge S A. Src family protein tyrosine kinases and cellular signal transduction pathways. Curr Opin Cell Biol 1995; 7: 176-82.
    • Curr Opin Cell Biol 1995; 7: 176-82.
    • Erpel, T.1
  • 26
    • 0026777369 scopus 로고    scopus 로고
    • A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction
    • Lanfrancone L, Grignani F et al.
    • Pelicci G, Lanfrancone L, Grignani F et al. A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction. Cell 1992; 70: 93-104.
    • Cell 1992; 70: 93-104.
    • Pelicci, G.1
  • 28
    • 0029118603 scopus 로고    scopus 로고
    • Wortmannin as a unique probe for an intracellular signalling protein
    • Okada T, Hazeki K, Hazeki O. phosphoinositide 3-kinase.
    • Ui M, Okada T, Hazeki K, Hazeki O. Wortmannin as a unique probe for an intracellular signalling protein, phosphoinositide 3-kinase. Trends Biochem Sci 1995; 20: 303-7.
    • Trends Biochem Sci 1995; 20: 303-7.
    • Ui, M.1
  • 31
    • 0028217345 scopus 로고    scopus 로고
    • Aspects of growth factor signal transduction in the cell cytoplasm
    • Panaretto B A. Aspects of growth factor signal transduction in the cell cytoplasm. J Cell Sci 1994; 107: 747-52.
    • J Cell Sci 1994; 107: 747-52.
    • Panaretto, B.A.1
  • 33
    • 0027403027 scopus 로고    scopus 로고
    • SH2 domains recognize specific phosphopeptide sequences
    • Shoelson S E, Chaudhuri M et al.
    • Songyang Z, Shoelson S E, Chaudhuri M et al. SH2 domains recognize specific phosphopeptide sequences. Cell 1993; 72: 1-20.
    • Cell 1993; 72: 1-20.
    • Songyang, Z.1
  • 34
    • 0028888604 scopus 로고    scopus 로고
    • The PTB domain: A new protein module implicated in signal transduction
    • Pawson T.
    • van der Geer P, Pawson T. The PTB domain: a new protein module implicated in signal transduction. Trends Biochem Sci 1995; 20: 277-80.
    • Trends Biochem Sci 1995; 20: 277-80.
    • Geer, P.1
  • 35
    • 0027944978 scopus 로고    scopus 로고
    • The insulin-like growth factor-I receptor
    • Wallach B, Christoffersen C T et al. ligand-binding mechanism and signal transduction. Horm Res 1994; 42: 152-69.
    • De Meyts P, Wallach B, Christoffersen C T et al. The insulin-like growth factor-I receptor. Structure, ligand-binding mechanism and signal transduction. Horm Res 1994; 42: 152-69.
    • Structure
    • De Meyts, P.1
  • 36
    • 0023814924 scopus 로고    scopus 로고
    • Mutation of the insulin receptor at tyrosine 960 inhibits signal transmission but does not affect its tyrosine kinase activity
    • Livingston J N, Backer J M et al.
    • White M F, Livingston J N, Backer J M et al. Mutation of the insulin receptor at tyrosine 960 inhibits signal transmission but does not affect its tyrosine kinase activity. Cell 1988; 54: 641-9.
    • Cell 1988; 54: 641-9.
    • White, M.F.1
  • 37
    • 0028219966 scopus 로고    scopus 로고
    • An IL-4 receptor region containing an insulin receptor motif is important for IL-4 mediated IRS-1 phosphorylation and cell growth
    • Nelms K, White M F, Wang L-M, Pierce J H, Paul W E.
    • Keegan A D, Nelms K, White M F, Wang L-M, Pierce J H, Paul W E. An IL-4 receptor region containing an insulin receptor motif is important for IL-4 mediated IRS-1 phosphorylation and cell growth. Cell 1994; 76: 811-20.
    • Cell 1994; 76: 811-20.
    • Keegan, A.D.1
  • 40
    • 0027940213 scopus 로고    scopus 로고
    • Heparan sulfate fibroblast growth factor receptor complex: Structure- Function relationships
    • Kan M.
    • McKeehan W L, Kan M. Heparan sulfate fibroblast growth factor receptor complex: structure- function relationships. Mol Reprod Dev 1994; 39: 69-82.
    • Mol Reprod Dev 1994; 39: 69-82.
    • McKeehan, W.L.1
  • 41
    • 0027323554 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycan and FGF receptor target basic FGF to different intracellular destinations
    • Rapraeger A C.
    • Reiland J, Rapraeger A C. Heparan sulfate proteoglycan and FGF receptor target basic FGF to different intracellular destinations. J Cell Sci 1993; 105: 1085-93.
    • J Cell Sci 1993; 105: 1085-93.
    • Reiland, J.1
  • 46
    • 0028358806 scopus 로고    scopus 로고
    • Diversity in function and regulation of MAP kinase pathways
    • Johnson G L.
    • Blumer K J, Johnson G L. Diversity in function and regulation of MAP kinase pathways. Trends Biochem Sci 1994; 19: 236-40.
    • Trends Biochem Sci 1994; 19: 236-40.
    • Blumer, K.J.1
  • 47
    • 0026678172 scopus 로고    scopus 로고
    • Association of the She and Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinases
    • McGlade J, Mbamalu G et al.
    • Rozakis Adcock M, McGlade J, Mbamalu G et al. Association of the She and Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinases. Nature 1992; 360: 689-92.
    • Nature 1992; 360: 689-92.
    • Rozakis Adcock, M.1
  • 48
    • 0028216328 scopus 로고    scopus 로고
    • Guanine-nucleotide exchange factors: A family of positive regulators of Ras and related GTPases
    • Feig L A. Guanine-nucleotide exchange factors: a family of positive regulators of Ras and related GTPases. Curr Opin Cell Biol 1994; 6: 204-11.
    • Curr Opin Cell Biol 1994; 6: 204-11.
    • Feig, L.A.1
  • 49
    • 0028917954 scopus 로고    scopus 로고
    • Regulation of Ras-mediated signalling: More than one way to skin a cat
    • Bos J L.
    • Burgering B M T, Bos J L. Regulation of Ras-mediated signalling: more than one way to skin a cat. Trends Biochem Sci 1995; 20: 18-22.
    • Trends Biochem Sci 1995; 20: 18-22.
    • Burgering, B.M.T.1
  • 50
    • 0027207287 scopus 로고    scopus 로고
    • Tyrosine kinase-stimulated guanine nucleotide exchange activity of Vav in T cell activation
    • Coggeshall M, Baier G, Katzav F, Burn P, Altaian A.
    • Gulbins E, Coggeshall M, Baier G, Katzav F, Burn P, Altaian A. Tyrosine kinase-stimulated guanine nucleotide exchange activity of Vav in T cell activation. Science 1993; 260: 822-5.
    • Science 1993; 260: 822-5.
    • Gulbins, E.1
  • 51
    • 0026535589 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of vav proto-oncogene product containing SH2 domain and transcription factor motifs
    • Hu P, Katzav S et al.
    • Margolis B, Hu P, Katzav S et al. Tyrosine phosphorylation of vav proto-oncogene product containing SH2 domain and transcription factor motifs. Nature 1992; 356: 71-4.
    • Nature 1992; 356: 71-4.
    • Margolis, B.1
  • 52
    • 0027586171 scopus 로고    scopus 로고
    • A conserved kinase cascade for MAP kinase activation in yeast
    • Levin D E.
    • Errede B, Levin D E. A conserved kinase cascade for MAP kinase activation in yeast. Curr Opin Cell Biol 1993; 5: 254-60.
    • Curr Opin Cell Biol 1993; 5: 254-60.
    • Errede, B.1
  • 53
    • 0026772506 scopus 로고    scopus 로고
    • Coordinate
    • Seuwen K, Meloche S, Pouysségur J. biphasic activation of p44 mitogen-activated protein kinase and S6 kinase by growth factors in hamster fibroblasts.
    • Kahan C, Seuwen K, Meloche S, Pouysségur J. Coordinate, biphasic activation of p44 mitogen-activated protein kinase and S6 kinase by growth factors in hamster fibroblasts. J Biol Chem 1992; 267: 13369-13375.
    • J Biol Chem 1992; 267: 13369-13375.
    • Kahan, C.1
  • 57
    • 0027326410 scopus 로고    scopus 로고
    • Protein kinase C alpha activates RAF-1 by direct phosphorylation
    • Heidecker G, Kochs G et al.
    • Kolch W, Heidecker G, Kochs G et al. Protein kinase C alpha activates RAF-1 by direct phosphorylation. Nature 1993; 364: 249-52.
    • Nature 1993; 364: 249-52.
    • Kolch, W.1
  • 58
    • 0029154733 scopus 로고    scopus 로고
    • 2+-induced regulation of ion channel and MAP kinase functions
    • Moreno H, Martinez R et al.
    • 2+-induced regulation of ion channel and MAP kinase functions. Nature 1995; 376: 737-45.
    • Nature 1995; 376: 737-45.
    • Lev, S.1
  • 59
    • 0028977847 scopus 로고    scopus 로고
    • Receptor-tyrosinekinase- And Gβγ-mediated MAP kinase activation by a common signalling pathway
    • Hawes B E, Luttrell D K et al.
    • van Biesen T, Hawes B E, Luttrell D K et al. Receptor-tyrosinekinase- and Gβγ-mediated MAP kinase activation by a common signalling pathway. Nature 1995; 376: 781-4.
    • Nature 1995; 376: 781-4.
    • Biesen, T.1
  • 60
    • 0029028786 scopus 로고    scopus 로고
    • G protein βγ subunits stimulate phosphorylation of She adaptor protein
    • Hawes B E, van Biesen T, Lefkowitz R J.
    • Touhara K, Hawes B E, van Biesen T, Lefkowitz R J. G protein βγ subunits stimulate phosphorylation of She adaptor protein. Proc Natl Acad Sci USA 1995; 92: 9284-7.
    • Proc Natl Acad Sci USA 1995; 92: 9284-7.
    • Touhara, K.1
  • 62
    • 0027219132 scopus 로고    scopus 로고
    • Elk-1 proteins are phosphoproteins and activators of mitogen-activated protein kinase
    • Reddy E S.
    • Rao V N, Reddy E S. Elk-1 proteins are phosphoproteins and activators of mitogen-activated protein kinase. Cancer Res 1993; 53: 3449-54.
    • Cancer Res 1993; 53: 3449-54.
    • Rao, V.N.1
  • 63
    • 85177154486 scopus 로고    scopus 로고
    • MAP kinases
    • Reddy E S. elk-1 proteins interact with
    • Rao V N, Reddy E S. elk-1 proteins interact with MAP kinases. Oncogene 1994; 9: 1855-60.
    • Oncogene 1994; 9: 1855-60.
    • Rao, V.N.1
  • 64
    • 0026695645 scopus 로고    scopus 로고
    • TCF by MAP kinase stimulates ternary complex formation at c-fos promoter
    • Sharrocks A D, Shaw P E.
    • TCF by MAP kinase stimulates ternary complex formation at c-fos promoter. Nature 1992; 358: 414-7.
    • Nature 1992; 358: 414-7.
    • Gille, H.1
  • 65
    • 0029328342 scopus 로고    scopus 로고
    • Transcriptional control by protein phosphorylation: Signal transmission from the cell surface to the nucleus
    • Hunter T.
    • Karin M, Hunter T. Transcriptional control by protein phosphorylation: signal transmission from the cell surface to the nucleus. Curr Biol 1995; 5: 747-57.
    • Curr Biol 1995; 5: 747-57.
    • Karin, M.1
  • 66
    • 0028322193 scopus 로고    scopus 로고
    • Signal transduction from the cell surface to the nucleus through the phosphorylation of transcription factors
    • Karin M. Signal transduction from the cell surface to the nucleus through the phosphorylation of transcription factors. Curr Opin Cell Biol 1994; 6: 415-24.
    • Curr Opin Cell Biol 1994; 6: 415-24.
    • Karin, M.1
  • 67
    • 0026608787 scopus 로고    scopus 로고
    • Nuclear localization and regulation of erk- And rsk-encoded protein kinases
    • Sarnecki C, Blenis J.
    • Chen R H, Sarnecki C, Blenis J. Nuclear localization and regulation of erk- and rsk-encoded protein kinases. Mol Cell Biol 1992; 12: 915-27.
    • Mol Cell Biol 1992; 12: 915-27.
    • Chen, R.H.1
  • 68
    • 0028216315 scopus 로고    scopus 로고
    • MAP kinases ERK1 and ERK2: Pleiotropic enzymes in a ubiquitous signaling network
    • Zhen E, Cheng M, Xu S, Eben D, Cobb M H.
    • Robbins D J, Zhen E, Cheng M, Xu S, Eben D, Cobb M H. MAP kinases ERK1 and ERK2: pleiotropic enzymes in a ubiquitous signaling network. Adv Cancer Res 1993; 60: 93-116.
    • Adv Cancer Res 1993; 60: 93-116.
    • Robbins, D.J.1
  • 69
    • 0026004501 scopus 로고    scopus 로고
    • Phosphorylation of c-jun mediated by MAP kinases
    • Kyriakis J M, Avruch J, Nikolakaki E, Woodgett J R.
    • Pulverer B J, Kyriakis J M, Avruch J, Nikolakaki E, Woodgett J R. Phosphorylation of c-jun mediated by MAP kinases. Nature 1991; 353: 670-4.
    • Nature 1991; 353: 670-4.
    • Pulverer, B.J.1
  • 70
    • 0027423418 scopus 로고    scopus 로고
    • Identification of an oncoprotein- And UV-responsive protein kinase that binds and potentiates the c-Jun activation domain
    • Lin A, Smeal T, Minden A, Karin M.
    • Hibi M, Lin A, Smeal T, Minden A, Karin M. Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain. Genes Dev 1993; 7: 2135-48.
    • Genes Dev 1993; 7: 2135-48.
    • Hibi, M.1
  • 71
    • 0028176732 scopus 로고    scopus 로고
    • Feedback regulation of mitogen-activated protein kinase kinase kinase activity of c-Raf-1 by insulin and phorbol ester stimulation
    • Matsuda S, Tobe K et al.
    • Ueki K, Matsuda S, Tobe K et al. Feedback regulation of mitogen-activated protein kinase kinase kinase activity of c-Raf-1 by insulin and phorbol ester stimulation. J Biol Chem 1994; 269: 15756-61.
    • J Biol Chem 1994; 269: 15756-61.
    • Ueki, K.1
  • 72
    • 0026733636 scopus 로고    scopus 로고
    • MAPKAP kinase-2: A novel protein kinase activated by mitogen-activated protein kinase
    • Campbell D G, Nakielny S et al.
    • Stokoe D, Campbell D G, Nakielny S et al. MAPKAP kinase-2: a novel protein kinase activated by mitogen-activated protein kinase. EMBOJ 1992; 11: 3985-94.
    • EMBOJ 1992; 11: 3985-94.
    • Stokoe, D.1
  • 73
    • 0026649469 scopus 로고    scopus 로고
    • Purification and properties of a protamine kinase from bovine kidney microsomes
    • Reddy S A, Damuni Z.
    • Amick G D, Reddy S A, Damuni Z. Purification and properties of a protamine kinase from bovine kidney microsomes. Arch Biochem Biophys 1992; 297: 80-5.
    • Arch Biochem Biophys 1992; 297: 80-5.
    • Amick, G.D.1
  • 74
    • 0028134981 scopus 로고    scopus 로고
    • A MAP kinase-dependent spindle assembly checkpoint in Xenopus egg extracts
    • Sun H, Tonks N K, Murray A W.
    • Minshull J, Sun H, Tonks N K, Murray A W. A MAP kinase-dependent spindle assembly checkpoint in Xenopus egg extracts. Cell 1994; 79: 475-86.
    • Cell 1994; 79: 475-86.
    • Minshull, J.1
  • 75
    • 0029317904 scopus 로고    scopus 로고
    • Cyclin-dependent protein kinases: Key regulators of the eukaryotic cell cycle
    • Nigg E A. Cyclin-dependent protein kinases: key regulators of the eukaryotic cell cycle. BioEssays 1995; 17: 471-80.
    • BioEssays 1995; 17: 471-80.
    • Nigg, E.A.1
  • 76
    • 0025290163 scopus 로고    scopus 로고
    • An insulin-stimulated protein kinase similar to yeast kinases involved in cell cycle control
    • Yancopoulos G D, Gregory JS et al.
    • Boulton T G, Yancopoulos G D, Gregory JS et al. An insulin-stimulated protein kinase similar to yeast kinases involved in cell cycle control. Science 1990; 249: 64-7.
    • Science 1990; 249: 64-7.
    • Boulton, T.G.1
  • 77
    • 0028568217 scopus 로고    scopus 로고
    • Differential activation of ERK and JNK mitogen activated protein kinases by Raf-1 and MEKK
    • Lin A, McMahon M et al.
    • Minden A, Lin A, McMahon M et al. Differential activation of ERK and JNK mitogen activated protein kinases by Raf-1 and MEKK. Science 1994; 266: 1719-23.
    • Science 1994; 266: 1719-23.
    • Minden, A.1
  • 78
    • 0028943245 scopus 로고    scopus 로고
    • Identification of a dual specificity kinase that activates the Jun kinases and p38-Mpk2
    • Minden A, Martinetto H et al.
    • Lin A, Minden A, Martinetto H et al. Identification of a dual specificity kinase that activates the Jun kinases and p38-Mpk2. Science 1995; 268: 286-90.
    • Science 1995; 268: 286-90.
    • Lin, A.1
  • 79
    • 0028144846 scopus 로고    scopus 로고
    • Fos transcriptional activity stimulated by H-Ras-activated protein kinase distinct from JNK and ERK
    • Karin M. c-
    • Deng T, Karin M. c-Fos transcriptional activity stimulated by H-Ras-activated protein kinase distinct from JNK and ERK. Nature 1994; 371: 171-5.
    • Nature 1994; 371: 171-5.
    • Deng, T.1
  • 81
    • 0027358722 scopus 로고    scopus 로고
    • MKP-1 (3CH134)
    • Charles C H, Lau L F, Tonks N K. an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo.
    • Sun H, Charles C H, Lau L F, Tonks N K. MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo. Cell 1993; 75: 487-93.
    • Cell 1993; 75: 487-93.
    • Sun, H.1
  • 83
    • 0025720735 scopus 로고    scopus 로고
    • The role of Jun
    • Karin M. Fos and the AP-1 complex in cell-proliferation and transformation.
    • Angel P, Karin M. The role of Jun, Fos and the AP-1 complex in cell-proliferation and transformation. Biochim Biophys Acta 1991; 1072: 129-57.
    • Biochim Biophys Acta 1991; 1072: 129-57.
    • Angel, P.1
  • 84
    • 0023625090 scopus 로고    scopus 로고
    • Phorbol ester-inducible genes contain a common cis-element recognized by a TPA-modulated trans-acting factor
    • Imagawa M, Chiu R et al.
    • Angel P, Imagawa M, Chiu R et al. Phorbol ester-inducible genes contain a common cis-element recognized by a TPA-modulated trans-acting factor. Cell 1987; 49: 729-39.
    • Cell 1987; 49: 729-39.
    • Angel, P.1
  • 85
    • 0023611441 scopus 로고    scopus 로고
    • Purified transcription factor AP-1 interacts with TPA-inducible enhancer elements
    • Mitchell P J, Tjian R.
    • Lee W, Mitchell P J, Tjian R. Purified transcription factor AP-1 interacts with TPA-inducible enhancer elements. Cell 1987; 49: 741-52.
    • Cell 1987; 49: 741-52.
    • Lee, W.1
  • 86
    • 0024201551 scopus 로고    scopus 로고
    • Fos and Jun bind cooperatively to the AP-1 site: Reconstitution in vitro
    • Voulalas P J, Franza R, Curran T.
    • Rauscher F J, Voulalas P J, Franza R, Curran T. Fos and Jun bind cooperatively to the AP-1 site: reconstitution in vitro. Genes Dev 1988; 2: 1687-99.
    • Genes Dev 1988; 2: 1687-99.
    • Rauscher, F.J.1
  • 87
    • 0025276217 scopus 로고    scopus 로고
    • Heterodimer formation between CREB and JUN proteins
    • Jones N C.
    • Benbrook D M, Jones N C. Heterodimer formation between CREB and JUN proteins. Oncogene 1990; 5: 295-302.
    • Oncogene 1990; 5: 295-302.
    • Benbrook, D.M.1
  • 88
    • 0025878233 scopus 로고    scopus 로고
    • Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity
    • Curran T.
    • Hai T W, Curran T. Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity. Proc Natl Acad Sci USA 1991; 88: 3720-3724.
    • Proc Natl Acad Sci USA 1991; 88: 3720-3724.
    • Hai, T.W.1
  • 89
    • 0027472176 scopus 로고    scopus 로고
    • Heterodimer formation of c-Jun and ATF-2 is responsible for induction of c-jun by the 243 amino acid adenovirus El A protein
    • Duyndam M, Rottier R et al.
    • van Dam H, Duyndam M, Rottier R et al. Heterodimer formation of c-Jun and ATF-2 is responsible for induction of c-jun by the 243 amino acid adenovirus El A protein. EMBO J 1993; 12: 479-487.
    • EMBO J 1993; 12: 479-487.
    • Dam, H.1
  • 90
    • 0027209916 scopus 로고    scopus 로고
    • Adenovirus El A negatively and positively modulates transcription of AP- 1 dependent genes by dimer-specific regulation of the DNA binding and transactivation activities of Jun
    • Konig H, Herr I et al.
    • Hagmeyer B M, Konig H, Herr I et al. Adenovirus El A negatively and positively modulates transcription of AP- 1 dependent genes by dimer-specific regulation of the DNA binding and transactivation activities of Jun. EMBOJ 1993; 12: 3559-72.
    • EMBOJ 1993; 12: 3559-72.
    • Hagmeyer, B.M.1
  • 91
    • 0027392874 scopus 로고    scopus 로고
    • Co-purification of mitogen activated protein kinase with phorbol ester induced cJun kinase activity in U937 leukaemia cells
    • Hughes K, Franklin C C, Kraft A S, Leevers S J, Woodgett J R.
    • Pulverer B J, Hughes K, Franklin C C, Kraft A S, Leevers S J, Woodgett J R. Co-purification of mitogen activated protein kinase with phorbol ester induced cJun kinase activity in U937 leukaemia cells. Oncogene 1993; 8: 407-15.
    • Oncogene 1993; 8: 407-15.
    • Pulverer, B.J.1
  • 92
    • 0028329953 scopus 로고    scopus 로고
    • JNK1 : A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain
    • Hibi M, Wu I-H et al.
    • Dérijard B, Hibi M, Wu I-H et al. JNK1 : a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain. Cell 1994; 76: 1025-37.
    • Cell 1994; 76: 1025-37.
    • Dérijard, B.1
  • 93
    • 0029006550 scopus 로고    scopus 로고
    • Intramolecular signal transduction in c-Jun
    • Treier M, Bohmann D.
    • Papavassiliou A G, Treier M, Bohmann D. Intramolecular signal transduction in c-Jun. EMBO J 1995; 14: 2014-19.
    • EMBO J 1995; 14: 2014-19.
    • Papavassiliou, A.G.1
  • 94
    • 0029379778 scopus 로고    scopus 로고
    • Activation of the ternary complex factor Elk-1 by stress-activated protein kinases
    • Strahl T, Shaw P E.
    • Gille H, Strahl T, Shaw P E. Activation of the ternary complex factor Elk-1 by stress-activated protein kinases. Curr Biol 1995; 5: 1191-200.
    • Curr Biol 1995; 5: 1191-200.
    • Gille, H.1
  • 95
    • 0024869297 scopus 로고    scopus 로고
    • Stimulation of protein kinase C or protein kinase A mediated signal transduction pathways shows three modes of response among serum inducible genes
    • Piette J, Hirai S I, Yaniv M.
    • Mechta F, Piette J, Hirai S I, Yaniv M. Stimulation of protein kinase C or protein kinase A mediated signal transduction pathways shows three modes of response among serum inducible genes. New Biol 1989; 1: 297-304.
    • New Biol 1989; 1: 297-304.
    • Mechta, F.1
  • 96
    • 0026686624 scopus 로고    scopus 로고
    • Existence of different Fos/Jun complexes during the G0-to-G1 transition and during exponential growth in mouse fibroblasts: Differential role of Fos proteins
    • Bravo R.
    • Kovary K, Bravo R. Existence of different Fos/Jun complexes during the G0-to-G1 transition and during exponential growth in mouse fibroblasts: differential role of Fos proteins. Mol Cell Biol 1992; 12: 5015-23.
    • Mol Cell Biol 1992; 12: 5015-23.
    • Kovary, K.1
  • 97
    • 0028803402 scopus 로고    scopus 로고
    • Journey to the surface of the cell: Fos regulation and the SRE
    • Treisman R. Journey to the surface of the cell: Fos regulation and the SRE. EMBO J 1995; 14: 4905-13.
    • EMBO J 1995; 14: 4905-13.
    • Treisman, R.1
  • 98
    • 0027282295 scopus 로고    scopus 로고
    • In vivo protein-DNA interactions at the c-jun promoter: Preformed complexes mediate the UV response
    • Pfeifer G P.
    • Rozek D, Pfeifer G P. In vivo protein-DNA interactions at the c-jun promoter: preformed complexes mediate the UV response. Mol Cell Biol 1993; 13: 5490-99.
    • Mol Cell Biol 1993; 13: 5490-99.
    • Rozek, D.1
  • 99
    • 0026579203 scopus 로고    scopus 로고
    • Interference between pathway-specific transcription factors: Glucocorticoids antagonize phorbol ester-induced AP-1 activity without altering AP-1 site occupation in vivo
    • Ponta H, Rahmsdorf H J, Herrlich P.
    • Konig H, Ponta H, Rahmsdorf H J, Herrlich P. Interference between pathway-specific transcription factors: glucocorticoids antagonize phorbol ester-induced AP-1 activity without altering AP-1 site occupation in vivo. EMBO J 1992; 11: 2241-46.
    • EMBO J 1992; 11: 2241-46.
    • Konig, H.1
  • 100
    • 0029145416 scopus 로고    scopus 로고
    • Structural and functional relationships of heterotrimeric G-proteins
    • Hamm H E.
    • Rens-Domiano S, Hamm H E. Structural and functional relationships of heterotrimeric G-proteins. FASEB J 1995; 9: 1059-66.
    • FASEB J 1995; 9: 1059-66.
    • Rens-Domiano, S.1
  • 101
    • 0023888280 scopus 로고    scopus 로고
    • Cyclic AMP and the induction of eukaryotic gene expression
    • Vanderbark G R, Hanson R W.
    • Roesler W J, Vanderbark G R, Hanson R W. Cyclic AMP and the induction of eukaryotic gene expression. J Biol Chem 1988; 263: 9063-6.
    • J Biol Chem 1988; 263: 9063-6.
    • Roesler, W.J.1
  • 102
    • 0024499494 scopus 로고    scopus 로고
    • A cluster of phosphorylation sites on the cAMP-regulated nuclear factor CREB predicted by its sequence
    • Yamamoto K K, Fischer W H et al.
    • Gonzalez G A, Yamamoto K K, Fischer W H et al. A cluster of phosphorylation sites on the cAMP-regulated nuclear factor CREB predicted by its sequence. Nature 1989; 337: 749-52.
    • Nature 1989; 337: 749-52.
    • Gonzalez, G.A.1
  • 103
    • 0028787753 scopus 로고    scopus 로고
    • Multiple protein kinase A-regulated events are required for transcriptional induction by cAMP
    • Nakajima T, Montminy M R.
    • Brindle P, Nakajima T, Montminy M R. Multiple protein kinase A-regulated events are required for transcriptional induction by cAMP. Proc Natl Acad Sci USA 1995; 92: 10521-5.
    • Proc Natl Acad Sci USA 1995; 92: 10521-5.
    • Brindle, P.1
  • 104
    • 0025666845 scopus 로고    scopus 로고
    • Cyclic-AMP-responsive transcriptional activation involves interdependent phosphorylation subdomains
    • Yun Y, Hoeffler J P, Habener J F.
    • Lee C Q, Yun Y, Hoeffler J P, Habener J F. Cyclic-AMP-responsive transcriptional activation involves interdependent phosphorylation subdomains. EMBO J 1990; 9: 4455-65.
    • EMBO J 1990; 9: 4455-65.
    • Lee, C.Q.1
  • 105
    • 0028035823 scopus 로고    scopus 로고
    • Complexity and versatility of the transcriptional response to cAMP
    • Molina C A, Lalli E et al.
    • Delmas V, Molina C A, Lalli E et al. Complexity and versatility of the transcriptional response to cAMP. Rev Physiol Biochem Pharmacol 1994; 124: 1-28.
    • Rev Physiol Biochem Pharmacol 1994; 124: 1-28.
    • Delmas, V.1
  • 106
    • 0028567253 scopus 로고    scopus 로고
    • The CREB/ATF family of transcription factors: Modulation by reversible phosphorylation
    • Papavassiliou A G. The CREB/ATF family of transcription factors: modulation by reversible phosphorylation. Anticancer Res 1994; 14: 1801-05.
    • Anticancer Res 1994; 14: 1801-05.
    • Papavassiliou, A.G.1
  • 107
    • 0024445798 scopus 로고    scopus 로고
    • Cyclic AMP stimulates somatostatin gene transcription by phosphorylation of CREB at serine 133
    • Montminy M R.
    • Gonzalez G A, Montminy M R. Cyclic AMP stimulates somatostatin gene transcription by phosphorylation of CREB at serine 133. Cell 1989; 59: 675-80.
    • Cell 1989; 59: 675-80.
    • Gonzalez, G.A.1
  • 108
    • 0025967751 scopus 로고    scopus 로고
    • Characterization of motifs which are critical for activity of the cyclic AMP-responsive transcription factor CREB
    • Menzel P, Leonard J, Fischer W H, Montminy M R.
    • Gonzalez G A, Menzel P, Leonard J, Fischer W H, Montminy M R. Characterization of motifs which are critical for activity of the cyclic AMP-responsive transcription factor CREB. Mol Cell Biol 1991; 11: 1306-1312.
    • Mol Cell Biol 1991; 11: 1306-1312.
    • Gonzalez, G.A.1
  • 109
    • 0027433708 scopus 로고    scopus 로고
    • Phosphorylated CREB binds specifically to the nuclear protein CBP
    • Kwok R P, Lamb N, Hagiwara M, Montminy M R, Goodman R H.
    • Chrivia J C, Kwok R P, Lamb N, Hagiwara M, Montminy M R, Goodman R H. Phosphorylated CREB binds specifically to the nuclear protein CBP. Nature 1993; 365: 855-9.
    • Nature 1993; 365: 855-9.
    • Chrivia, J.C.1
  • 110
    • 0028060029 scopus 로고    scopus 로고
    • Nuclear protein CBP is a coactivator for the transcription factor CREB (see comments)
    • Lundblad J R, Chrivia J C et al.
    • Kwok R P, Lundblad J R, Chrivia J C et al. Nuclear protein CBP is a coactivator for the transcription factor CREB (see comments). Nature 1994; 370: 223-6.
    • Nature 1994; 370: 223-6.
    • Kwok, R.P.1
  • 111
    • 0026653422 scopus 로고    scopus 로고
    • Transcriptional attenuation following cAMP induction requires PP-1- Mediated dephosphorylation of CREB
    • Alberts A, Brindle P et al.
    • Hagiwara M, Alberts A, Brindle P et al. Transcriptional attenuation following cAMP induction requires PP-1- mediated dephosphorylation of CREB. Cell 1992; 70: 105-13.
    • Cell 1992; 70: 105-13.
    • Hagiwara, M.1
  • 112
    • 0026714673 scopus 로고    scopus 로고
    • Phosphorylation of CREB affects its binding to high and low affinity sites: Implications for cAMP induced gene transcription
    • Weih F, Schmid W et al.
    • Nichols M, Weih F, Schmid W et al. Phosphorylation of CREB affects its binding to high and low affinity sites: implications for cAMP induced gene transcription. EMBO J 1992: 11: 3337-46.
    • EMBO J 1992: 11: 3337-46.
    • Nichols, M.1
  • 113
    • 0027476994 scopus 로고    scopus 로고
    • The functional versatility of CREM is determined by its modular structure
    • Foulkes N S, Schlotter F, Sassone-Corsi P.
    • Laoide B M, Foulkes N S, Schlotter F, Sassone-Corsi P. The functional versatility of CREM is determined by its modular structure. EMBO J 1993; 12: 1179-91.
    • EMBO J 1993; 12: 1179-91.
    • Laoide, B.M.1
  • 114
    • 0027258139 scopus 로고    scopus 로고
    • Multiple and cooperative phosphorylation events regulate the CREM activator function
    • den Hertog J, Vandenheede J R, Goris J, Sassone-Corsi P.
    • de Groot R P, den Hertog J, Vandenheede J R, Goris J, Sassone-Corsi P. Multiple and cooperative phosphorylation events regulate the CREM activator function. EMBO J 1993; 12: 3903-11.
    • EMBO J 1993; 12: 3903-11.
    • Groot, R.P.1
  • 115
    • 0024817131 scopus 로고    scopus 로고
    • Transcription factor ATF cDNA clones: An extensive family of leucine zipper proteins able to selectively form da binding heterodimers
    • Liu F, Coukos W J, Green M R.
    • Hai T W, Liu F, Coukos W J, Green M R. Transcription factor ATF cDNA clones: an extensive family of leucine zipper proteins able to selectively form DA binding heterodimers. Genes Dev 1989; 3: 2083-90.
    • Genes Dev 1989; 3: 2083-90.
    • Hai, T.W.1
  • 116
    • 0026095013 scopus 로고    scopus 로고
    • The cAMP-regulated enhancer-binding protein ATF-1 activates transcription in response to cAMP-dependent protein kinase
    • Walton K M, Loriaux M M, Goodman R H.
    • Rehfuss R P, Walton K M, Loriaux M M, Goodman R H. The cAMP-regulated enhancer-binding protein ATF-1 activates transcription in response to cAMP-dependent protein kinase. J Biol Chem 1991; 266: 18431-4.
    • J Biol Chem 1991; 266: 18431-4.
    • Rehfuss, R.P.1
  • 117
    • 0029030855 scopus 로고    scopus 로고
    • ATF-2 is preferentially activated by stress-activated protein kinases to mediate c-jun induction in response to genotoxic agents
    • Wilhelm D, Herr I, Steffen A, Herrlich P, Angel P.
    • van Dam H, Wilhelm D, Herr I, Steffen A, Herrlich P, Angel P. ATF-2 is preferentially activated by stress-activated protein kinases to mediate c-jun induction in response to genotoxic agents. EMBO J 1995; 14: 1798-811.
    • EMBO J 1995; 14: 1798-811.
    • Dam, H.1
  • 118
    • 0025284903 scopus 로고    scopus 로고
    • A specific member of the ATF transcription factor family can mediate transcription activation by the adenovirus E1 a protein
    • Green M R.
    • Liu F, Green M R. A specific member of the ATF transcription factor family can mediate transcription activation by the adenovirus E1 a protein. Cell 1990; 61: 1217-24.
    • Cell 1990; 61: 1217-24.
    • Liu, F.1
  • 119
    • 0028246161 scopus 로고    scopus 로고
    • El A-associated p300 and CREB-associated CBP belong to a conserved family of coactivators
    • Sellers W R, Livingston D M, Eckner R.
    • Arany Z, Sellers W R, Livingston D M, Eckner R. El A-associated p300 and CREB-associated CBP belong to a conserved family of coactivators. Cell 1994; 77: 799-800.
    • Cell 1994; 77: 799-800.
    • Arany, Z.1
  • 120
    • 0026459649 scopus 로고    scopus 로고
    • Transcriptional repression of interleukin-6 gene by adenoviral El A proteins
    • Kalvakolanu D V, Zhang Y, Sen G C.
    • Janaswami P M, Kalvakolanu D V, Zhang Y, Sen G C. Transcriptional repression of interleukin-6 gene by adenoviral El A proteins. J Biol Chem 1992; 267: 24886-91.
    • J Biol Chem 1992; 267: 24886-91.
    • Janaswami, P.M.1
  • 121
    • 0026719682 scopus 로고    scopus 로고
    • Retinoblastoma gene product activates expression of the human TGF-β2 gene through transcription factor ATF-2
    • Wagner S, Liu F, O'Reilly M A, Robbins P D, Green M R.
    • Kim S-J, Wagner S, Liu F, O'Reilly M A, Robbins P D, Green M R. Retinoblastoma gene product activates expression of the human TGF-β2 gene through transcription factor ATF-2. Nature 1992; 358: 331-4.
    • Nature 1992; 358: 331-4.
    • Kim, S.-J.1
  • 123
  • 124
    • 0025304440 scopus 로고    scopus 로고
    • Cross-talk in signal transduction: TPA-inducible factor Jun/AP1 activates cAMP responsive enhancer elements
    • Ransone LJ, Verma IM.
    • Sassone-Corsi P, Ransone LJ, Verma IM. Cross-talk in signal transduction: TPA-inducible factor Jun/AP1 activates cAMP responsive enhancer elements. Oncogene 1990; 5: 427-31.
    • Oncogene 1990; 5: 427-31.
    • Sassone-Corsi, P.1
  • 125
    • 0028986124 scopus 로고    scopus 로고
    • Identification of p90RSK as the probable CREB-Ser133 kinase in human melanocytes
    • Moellman G, Cheng E et al.
    • Bohm M, Moellman G, Cheng E et al. Identification of p90RSK as the probable CREB-Ser133 kinase in human melanocytes. Cell Growth Differ 1995; 6: 291-302.
    • Cell Growth Differ 1995; 6: 291-302.
    • Bohm, M.1
  • 127
    • 0027458366 scopus 로고    scopus 로고
    • The Ets family of transcription factors (published erratum appears in Eur J Biochem 1993 Aug 1; 215(3):907)
    • Hahn S L, Giovane A.
    • Wasylyk B, Hahn S L, Giovane A. The Ets family of transcription factors (published erratum appears in Eur J Biochem 1993 Aug 1; 215(3):907). Eur J Biochem 1993; 211: 7-18.
    • Eur J Biochem 1993; 211: 7-18.
    • Wasylyk, B.1
  • 128
    • 0021029085 scopus 로고    scopus 로고
    • A putative second cell-derived oncogene of the avian leukaemia retrovirus E26
    • Gégonne A, Coll J et al.
    • Leprince D, Gégonne A, Coll J et al. A putative second cell-derived oncogene of the avian leukaemia retrovirus E26. Nature 1983; 306: 395-7.
    • Nature 1983; 306: 395-7.
    • Leprince, D.1
  • 129
    • 0008884352 scopus 로고    scopus 로고
    • Watson D K, Blair D G, Papas T S. c-ets-2 protooncogene has mitogenic and oncogenic activity.
    • Seth A, Watson D K, Blair D G, Papas T S. c-ets-2 protooncogene has mitogenic and oncogenic activity. Proc Natl Acad Sci USA 1989; 86: 7833-7.
    • Proc Natl Acad Sci USA 1989; 86: 7833-7.
    • Seth, A.1
  • 131
    • 0028047598 scopus 로고    scopus 로고
    • B promoter regulation: Ras mediated transactivation by c-Ets-1 and c-Ets-2
    • de Jonge M, Mettouchi A, Binétruy B, Ghysdael J, Kruijer W. jun
    • Coffer P, de Jonge M, Mettouchi A, Binétruy B, Ghysdael J, Kruijer W. junB promoter regulation: Ras mediated transactivation by c-Ets-1 and c-Ets-2. Oncogene 1994; 9: 911-21.
    • Oncogene 1994; 9: 911-21.
    • Coffer, P.1
  • 133
    • 0028335121 scopus 로고    scopus 로고
    • Participation of Ets transcription factors in the glucocorticoid response of the rat tyrosine aminotransferase gene
    • Roux J, Ghysdael J, Fielet R, Grange T.
    • Espinas M L, Roux J, Ghysdael J, Fielet R, Grange T. Participation of Ets transcription factors in the glucocorticoid response of the rat tyrosine aminotransferase gene. Mol Cell Biol 1994; 14: 4116-25.
    • Mol Cell Biol 1994; 14: 4116-25.
    • Espinas, M.L.1
  • 134
    • 0028009754 scopus 로고    scopus 로고
    • Dual control of myc expression through a single DNA binding site targeted by ets family proteins and E2F-1
    • Davis J N, Cleveland J L, Ghysdael J, Hiebert S W.
    • Roussel M F, Davis J N, Cleveland J L, Ghysdael J, Hiebert S W. Dual control of myc expression through a single DNA binding site targeted by ets family proteins and E2F-1. Oncogene 1994; 9: 405-15.
    • Oncogene 1994; 9: 405-15.
    • Roussel, M.F.1
  • 135
    • 0026533890 scopus 로고    scopus 로고
    • DNA binding by c-Ets-1
    • Kraut N, Frampton J, Graf T. but not v-Ets, is repressed by an intramolecular mechanism.
    • Lim F, Kraut N, Frampton J, Graf T. DNA binding by c-Ets-1, but not v-Ets, is repressed by an intramolecular mechanism. EMBOJ 1992; 11: 643-52.
    • EMBOJ 1992; 11: 643-52.
    • Lim, F.1
  • 136
    • 0024965788 scopus 로고    scopus 로고
    • DNA-binding domain ancestry (letter)
    • Leutz A, Gibson T J, Graf T.
    • Frampton J, Leutz A, Gibson T J, Graf T. DNA-binding domain ancestry (letter). Nature 1989; 342: 134.
    • Nature 1989; 342: 134.
    • Frampton, J.1
  • 137
    • 0026634171 scopus 로고    scopus 로고
    • A novel modulator domain of Ets transcription factors
    • Kerckaert J-P, Wasylyk B.
    • Wasylyk C, Kerckaert J-P, Wasylyk B. A novel modulator domain of Ets transcription factors. Genes Dev 1992; 6: 965-74.
    • Genes Dev 1992; 6: 965-74.
    • Wasylyk, C.1
  • 138
    • 0026730324 scopus 로고    scopus 로고
    • An inhibitory carboxyl-terminal domain in Ets-1 and Ets-2 mediates differential binding of ETS family factors to promoter sequences of the mb-1 gene
    • Grosschedl R.
    • Hagman J, Grosschedl R. An inhibitory carboxyl-terminal domain in Ets-1 and Ets-2 mediates differential binding of ETS family factors to promoter sequences of the mb-1 gene. Proc Natl Acad Sci USA 1992; 89: 8889-93.
    • Proc Natl Acad Sci USA 1992; 89: 8889-93.
    • Hagman, J.1
  • 139
    • 0027083526 scopus 로고    scopus 로고
    • Specificities of protein-protein and protein-DNA interaction of GABP alpha and two newly defined ets-related proteins
    • McKnight S L.
    • Brown T A, McKnight S L. Specificities of protein-protein and protein-DNA interaction of GABP alpha and two newly defined ets-related proteins. Genes Dev 1992; 6: 2502-12.
    • Genes Dev 1992; 6: 2502-12.
    • Brown, T.A.1
  • 141
    • 0026556859 scopus 로고    scopus 로고
    • Characterization of SAP-1
    • Treisman R. a protein recruited by serum response factor to the c-fos serum response element.
    • Dalton S, Treisman R. Characterization of SAP-1, a protein recruited by serum response factor to the c-fos serum response element. Cell 1992; 68: 597-612.
    • Cell 1992; 68: 597-612.
    • Dalton, S.1
  • 142
    • 0025812701 scopus 로고    scopus 로고
    • Convergence of Ets-and notch-related structural motifs in a heteromeric DNA binding complex (see comments)
    • Brown T A, McKnight S L.
    • Thompson C C, Brown T A, McKnight S L. Convergence of Ets-and notch-related structural motifs in a heteromeric DNA binding complex (see comments). Science 1991; 253: 762-8.
    • Science 1991; 253: 762-8.
    • Thompson, C.C.1
  • 143
    • 0025334775 scopus 로고    scopus 로고
    • The c-ets proto-oncogenes encode transcription factors that cooperate with c-Fos and c-Jun for transcriptional activation
    • Wasylyk C, Flores P, Begue A, Leprince D, Stehelin D.
    • Wasylyk B, Wasylyk C, Flores P, Begue A, Leprince D, Stehelin D. The c-ets proto-oncogenes encode transcription factors that cooperate with c-Fos and c-Jun for transcriptional activation. Nature 1990; 346: 191-3.
    • Nature 1990; 346: 191-3.
    • Wasylyk, B.1
  • 144
    • 0027411689 scopus 로고    scopus 로고
    • Synergistic activation of the HTLV1 LTR Ets-responsive region by transcription factors Ets1 and Sp1
    • Bosselut R, Bailly R-A, Ghysdael J.
    • Gégonne A, Bosselut R, Bailly R-A, Ghysdael J. Synergistic activation of the HTLV1 LTR Ets-responsive region by transcription factors Ets1 and Sp1. EMBO J 1993; 12: 1169-78.
    • EMBO J 1993; 12: 1169-78.
    • Gégonne, A.1
  • 145
    • 0028239101 scopus 로고    scopus 로고
    • Inhibition oiv-raf-dependent c-fos expression and transformation by a kinase defective mutant of the mitogen-activated protein kinase Erk2
    • Thomae O, Shaw P E.
    • Kortenjann M, Thomae O, Shaw P E. Inhibition oiv-raf-dependent c-fos expression and transformation by a kinase defective mutant of the mitogen-activated protein kinase Erk2. Mol Cell Biol 1994; 14: 4815-24.
    • Mol Cell Biol 1994; 14: 4815-24.
    • Kortenjann, M.1
  • 146
    • 0028931406 scopus 로고    scopus 로고
    • ERK phosphorylation potentiates Elk-1-mediated ternary complex formation and transactivation
    • Kortenjann M, Thomae O et al.
    • Gille H, Kortenjann M, Thomae O et al. ERK phosphorylation potentiates Elk-1-mediated ternary complex formation and transactivation. EMBO J 1995; 14: 951-62.
    • EMBO J 1995; 14: 951-62.
    • Gille, H.1
  • 147
    • 0027425113 scopus 로고    scopus 로고
    • Activation of ternary complex factor Elk-1 by MAP kinases
    • Ernst W H, Pingoud V, Nordheim A.
    • Janknecht R, Ernst W H, Pingoud V, Nordheim A. Activation of ternary complex factor Elk-1 by MAP kinases. EMBO J 1993; 12: 5097-104.
    • EMBO J 1993; 12: 5097-104.
    • Janknecht, R.1
  • 148
    • 0027297647 scopus 로고    scopus 로고
    • The SRF accessory protein ELK-1 contains a growth factor regulated transcription domain
    • Wynne J, Treisman R.
    • Marais R, Wynne J, Treisman R. The SRF accessory protein ELK-1 contains a growth factor regulated transcription domain. Cell 1993; 73: 381-93.
    • Cell 1993; 73: 381-93.
    • Marais, R.1
  • 149
    • 0024453716 scopus 로고    scopus 로고
    • Repression of c-fos transcription is mediated through p67SRF bound to the SRE
    • Frasch S, Nordheim A.
    • Shaw P E, Frasch S, Nordheim A. Repression of c-fos transcription is mediated through p67SRF bound to the SRE. EMBO J 1989; 8: 2567-74.
    • EMBO J 1989; 8: 2567-74.
    • Shaw, P.E.1
  • 150
    • 0027322153 scopus 로고    scopus 로고
    • Hipskind R A, Pingoud V, Nordheim A. c-fos transcriptional activation and repression correlate temporally with the phosphorylation status of
    • Zinck R, Hipskind R A, Pingoud V, Nordheim A. c-fos transcriptional activation and repression correlate temporally with the phosphorylation status of TCF. EMBO J 1993; 12: 2377-87.
    • EMBO J 1993; 12: 2377-87.
    • Zinck, R.1
  • 151
    • 0027984806 scopus 로고    scopus 로고
    • The ETS domain protein pointed-P2 is a target of MAP kinase in the sevenless signal transduction pathway
    • Dücker K, Oellers N, Hafen E, Scholz H, Klambt C.
    • Brunner D, Dücker K, Oellers N, Hafen E, Scholz H, Klambt C. The ETS domain protein pointed-P2 is a target of MAP kinase in the sevenless signal transduction pathway. Nature 1994; 370: 386-9.
    • Nature 1994; 370: 386-9.
    • Brunner, D.1
  • 152
    • 0028239896 scopus 로고    scopus 로고
    • The activities of two Ets-related transcription factors required for Drosophila eye development are modulated by the Ras/MAPK pathway
    • Rebay I, Tjian R, Rubin G M.
    • O Neill E M, Rebay I, Tjian R, Rubin G M. The activities of two Ets-related transcription factors required for Drosophila eye development are modulated by the Ras/MAPK pathway. Cell 1994; 78: 137-47.
    • Cell 1994; 78: 137-47.
    • Neill E M, O.1
  • 154
    • 0028107237 scopus 로고    scopus 로고
    • Physical association and functional antagonism between the p65 subunit of transcription factor NF-kappa B and the glucocorticoid receptor
    • Prefontaine K E.
    • Ray A, Prefontaine K E. Physical association and functional antagonism between the p65 subunit of transcription factor NF-kappa B and the glucocorticoid receptor. Proc Natl Acad Sci USA 1994; 91: 752-6.
    • Proc Natl Acad Sci USA 1994; 91: 752-6.
    • Ray, A.1
  • 155
    • 0025940872 scopus 로고    scopus 로고
    • Regulatory crosstalk at composite response elements
    • Yamamoto K R.
    • Miner J N, Yamamoto K R. Regulatory crosstalk at composite response elements. Trends Biochem Sci 1991; 16: 423-6.
    • Trends Biochem Sci 1991; 16: 423-6.
    • Miner, J.N.1
  • 156
    • 0025950381 scopus 로고    scopus 로고
    • Cross-coupling of signal transduction pathways: Zinc finger meets leucine zipper
    • Evans R M.
    • Schule R, Evans R M. Cross-coupling of signal transduction pathways: zinc finger meets leucine zipper. Trends Genet 1991; 7: 377-81.
    • Trends Genet 1991; 7: 377-81.
    • Schule, R.1
  • 157
    • 0028527272 scopus 로고    scopus 로고
    • Negative transcriptional regulation by nuclear receptors
    • Claret F X, Karin M.
    • Saatcioglu F, Claret F X, Karin M. Negative transcriptional regulation by nuclear receptors. Semin Cancer Biol 1994; 5: 347-59.
    • Semin Cancer Biol 1994; 5: 347-59.
    • Saatcioglu, F.1
  • 159
    • 0028084338 scopus 로고    scopus 로고
    • Myc-Max-Mad: A transcription factor network controlling cell cycle progression
    • Land H. differentiation and death.
    • Amati B, Land H. Myc-Max-Mad: a transcription factor network controlling cell cycle progression, differentiation and death. Curr Opin Genet Dev 1994; 4: 102-8.
    • Curr Opin Genet Dev 1994; 4: 102-8.
    • Amati, B.1
  • 160
    • 0028800220 scopus 로고    scopus 로고
    • Myc and Max: Molecular evolution of a family of proto-oncogene products and their dimerization partner
    • Fitch W M.
    • Atchley W R, Fitch W M. Myc and Max: Molecular evolution of a family of proto-oncogene products and their dimerization partner. Proc Natl Acad Sci USA 1995; 92: 10217-21.
    • Proc Natl Acad Sci USA 1995; 92: 10217-21.
    • Atchley, W.R.1
  • 161
    • 0029111411 scopus 로고    scopus 로고
    • Contrasting roles for Myc and Mad proteins in cellular growth and differentiation
    • Schreiber-Agus N, Pellicer I et al.
    • Chin L, Schreiber-Agus N, Pellicer I et al. Contrasting roles for Myc and Mad proteins in cellular growth and differentiation. Proc Natl Acad Sci USA 1995; 92: 8488-92.
    • Proc Natl Acad Sci USA 1995; 92: 8488-92.
    • Chin, L.1
  • 162
    • 0028921573 scopus 로고    scopus 로고
    • Jaks and Stats in signaling by the cytokine receptor superfamily
    • Kerr I M.
    • Ihle J N, Kerr I M. Jaks and Stats in signaling by the cytokine receptor superfamily. Trends Genet 1995; 11: 69-74.
    • Trends Genet 1995; 11: 69-74.
    • Ihle, J.N.1
  • 163
    • 0026024663 scopus 로고    scopus 로고
    • Nuclear targets for transcription regulation by oncogenes
    • Wasylyk B.
    • Gutman A, Wasylyk B. Nuclear targets for transcription regulation by oncogenes. Trends Genet 1991; 7: 49-54.
    • Trends Genet 1991; 7: 49-54.
    • Gutman, A.1
  • 164
    • 0023748088 scopus 로고    scopus 로고
    • Multiple nuclear factors interact with promoter sequences of the urokinase-type plasminogen activator gene
    • Pearson D, Nakagawa J, Rajput B, Nagamine Y.
    • von der Ahe D, Pearson D, Nakagawa J, Rajput B, Nagamine Y. Multiple nuclear factors interact with promoter sequences of the urokinase-type plasminogen activator gene. Nucleic Acids Res 1988; 16: 7527-44.
    • Nucleic Acids Res 1988; 16: 7527-44.
    • Ahe, D.1
  • 165
    • 0026338119 scopus 로고    scopus 로고
    • Constitutive expression of the urokinase plasminogen activator gene in murine Raw264 macrophages involves distal and 5′ non-coding sequences that are conserved between mouse and pig
    • Stacey K J, Nimmo K A et al.
    • Cassady A I, Stacey K J, Nimmo K A et al. Constitutive expression of the urokinase plasminogen activator gene in murine Raw264 macrophages involves distal and 5′ non-coding sequences that are conserved between mouse and pig. Nucleic Acids Res 1991; 19: 6839-47.
    • Nucleic Acids Res 1991; 19: 6839-47.
    • Cassady, A.I.1
  • 166
    • 0022432081 scopus 로고    scopus 로고
    • The human urokinase-plasminogen activator gene and its promoter
    • Grimaldi G, Verde P, Sebastio G, Boast S, Blasi F.
    • Riccio A, Grimaldi G, Verde P, Sebastio G, Boast S, Blasi F. The human urokinase-plasminogen activator gene and its promoter. Nucleic Acids Res 1985; 13: 2759-71.
    • Nucleic Acids Res 1985; 13: 2759-71.
    • Riccio, A.1
  • 167
    • 85030000843 scopus 로고    scopus 로고
    • Structure and function of the urokinase-type plasminogen activator gene
    • Lee J S, Menoud P-A, Nanbu R. ed. Fibrinolysis in disease. Boca Raton, Florida, USA: CRC Press Inc. 1995: 10-20.
    • Nagamine Y, Lee J S, Menoud P-A, Nanbu R. Structure and function of the urokinase-type plasminogen activator gene. In: Glas-Greenwalt P, ed. Fibrinolysis in disease. Boca Raton, Florida, USA: CRC Press Inc. 1995: 10-20.
    • In: Glas-Greenwalt P
    • Nagamine, Y.1
  • 168
    • 0025879527 scopus 로고    scopus 로고
    • Essential AP-1 and PEA3 binding elements in the human urokinase enhancer display cell type-specific activity
    • Rorth P, Blasi F, Johnsen M.
    • Nerlov C, Rorth P, Blasi F, Johnsen M. Essential AP-1 and PEA3 binding elements in the human urokinase enhancer display cell type-specific activity. Oncogene 1991; 6: 1583-92.
    • Oncogene 1991; 6: 1583-92.
    • Nerlov, C.1
  • 169
    • 0029589521 scopus 로고    scopus 로고
    • Urokinase-type plasminogen activator gene regulation by polyomavirus middle-T antigen
    • Urich M, Sakaue M, Messetschmitt A, Ballmer-Hofer K, Nagamine Y.
    • Besser D, Urich M, Sakaue M, Messetschmitt A, Ballmer-Hofer K, Nagamine Y. Urokinase-type plasminogen activator gene regulation by polyomavirus middle-T antigen. Oncogene 1995; 11: 2383-91.
    • Oncogene 1995; 11: 2383-91.
    • Besser, D.1
  • 170
    • 0029133267 scopus 로고    scopus 로고
    • Elucidation of a signaling pathway induced by FGF-2 leading to u-PA gene expression in NIH 3T3 fibroblasts
    • Presta M, Nagamine Y.
    • Besser D, Presta M, Nagamine Y. Elucidation of a signaling pathway induced by FGF-2 leading to u-PA gene expression in NIH 3T3 fibroblasts. Cell Growth Differ 1995; 6: 1009-17.
    • Cell Growth Differ 1995; 6: 1009-17.
    • Besser, D.1
  • 171
    • 0029148763 scopus 로고    scopus 로고
    • Involvement of a mitogen-activated protein kinase signaling pathway in the regulation of urokinase promoter activity by c-Ha-ras
    • Stepp E, Gum R, Boyd D.
    • Lengyel E, Stepp E, Gum R, Boyd D. Involvement of a mitogen-activated protein kinase signaling pathway in the regulation of urokinase promoter activity by c-Ha-ras. J Biol Chem 1995; 270: 23007-12.
    • J Biol Chem 1995; 270: 23007-12.
    • Lengyel, E.1
  • 172
    • 0029583938 scopus 로고    scopus 로고
    • Regulation of urokinase-type plasminogen activator expression by the v-mos oncogene
    • Singh B, Gum R et al.
    • Lengyel E, Singh B, Gum R et al. Regulation of urokinase-type plasminogen activator expression by the v-mos oncogene. Oncogene 1995; 11: 2639-48.
    • Oncogene 1995; 11: 2639-48.
    • Lengyel, E.1
  • 173
    • 0029024932 scopus 로고    scopus 로고
    • Regulation of urokinase-type plasminogen activator gene transcription by macrophage colony-stimulating factor
    • Fowles L F, Coman M S, Ostrowski M C, Hume D A.
    • Stacey K J, Fowles L F, Coman M S, Ostrowski M C, Hume D A. Regulation of urokinase-type plasminogen activator gene transcription by macrophage colony-stimulating factor. Mol Cell Biol 1995; 15: 3430-41
    • Mol Cell Biol 1995; 15: 3430-41
    • Stacey, K.J.1
  • 174
    • 0025025394 scopus 로고    scopus 로고
    • Transcription factor PEA3 participates in the induction of urokinase plasminogen activator transcription in murine keratinocytes stimulated with epidermal growth factor or phorbol-ester
    • Nerlov C, Blasi F, Johnsen M.
    • Rorth P, Nerlov C, Blasi F, Johnsen M. Transcription factor PEA3 participates in the induction of urokinase plasminogen activator transcription in murine keratinocytes stimulated with epidermal growth factor or phorbol-ester. Nucleic Acids Res 1990; 18: 5009-17.
    • Nucleic Acids Res 1990; 18: 5009-17.
    • Rorth, P.1
  • 176
    • 0027934202 scopus 로고    scopus 로고
    • Okadaic acid-dependent induction of the urokinase-type plasminogen activator gene associated with stabilization and autoregulation of c-Jun
    • Favre B, Hemmings B A, Kiefer B, Nagamine Y.
    • Lee J S, Favre B, Hemmings B A, Kiefer B, Nagamine Y. Okadaic acid-dependent induction of the urokinase-type plasminogen activator gene associated with stabilization and autoregulation of c-Jun. J Biol Chem 1994; 269: 2887-94.
    • J Biol Chem 1994; 269: 2887-94.
    • Lee, J.S.1
  • 177
    • 0026469664 scopus 로고    scopus 로고
    • A regulatory element that mediates co-operation between a PEA3-AP-1 element and an AP-1 site is required for phorbol ester induction of urokinase enhancer activity in HepG2 hepatoma cells
    • De Cesare D, Pergola F et al.
    • Nerlov C, De Cesare D, Pergola F et al. A regulatory element that mediates co-operation between a PEA3-AP-1 element and an AP-1 site is required for phorbol ester induction of urokinase enhancer activity in HepG2 hepatoma cells. EMBO J 1992; 11: 4573-82.
    • EMBO J 1992; 11: 4573-82.
    • Nerlov, C.1
  • 178
    • 0030063504 scopus 로고    scopus 로고
    • Purification and characterization of UEF3
    • Vandekerchove J, Blasi F. a novel factor involved in the regulation of the urokinase and other AP-1 controlled promoters.
    • Berthelsen J, Vandekerchove J, Blasi F. Purification and characterization of UEF3, a novel factor involved in the regulation of the urokinase and other AP-1 controlled promoters. J Biol Chem 1996; 271: 3822-30.
    • J Biol Chem 1996; 271: 3822-30.
    • Berthelsen, J.1
  • 179
    • 0028981659 scopus 로고    scopus 로고
    • Heterodimerization of c-Jun with ATF-2 and c-Fos is required for positive and negative regulation of the human urokinase enhancer
    • Vallone D, Caracciolo A, Sassone-Corsi P, Nerlov C, Verde P.
    • De Cesare D, Vallone D, Caracciolo A, Sassone-Corsi P, Nerlov C, Verde P. Heterodimerization of c-Jun with ATF-2 and c-Fos is required for positive and negative regulation of the human urokinase enhancer. Oncogene 1995; 11: 365-76.
    • Oncogene 1995; 11: 365-76.
    • De Cesare, D.1
  • 180
    • 0028890340 scopus 로고    scopus 로고
    • A transcriptional repressor obtained by alternative translation of a trinucleotide repeat
    • Wieland S, Hug M, Rusconi S.
    • Lanz R B, Wieland S, Hug M, Rusconi S. A transcriptional repressor obtained by alternative translation of a trinucleotide repeat. Nucleic Acids Res 1995; 23; 138-45.
    • Nucleic Acids Res 1995; 23; 138-45.
    • Lanz, R.B.1
  • 181
    • 0020575876 scopus 로고    scopus 로고
    • Hormonal regulation of plasminogen activator mRNA production in porcine kidney cells
    • Sudol M, Reich E.
    • Nagamine Y, Sudol M, Reich E. Hormonal regulation of plasminogen activator mRNA production in porcine kidney cells. Cell 1983; 32: 1181-90.
    • Cell 1983; 32: 1181-90.
    • Nagamine, Y.1
  • 182
    • 0022395280 scopus 로고    scopus 로고
    • Induction and desensitization of plasminogen activator gene expression by tumor promoters
    • Estensen R D, Nagamine Y, Reich E.
    • Degen J L, Estensen R D, Nagamine Y, Reich E. Induction and desensitization of plasminogen activator gene expression by tumor promoters. J Biol Chem 1985; 260: 12426-33.
    • J Biol Chem 1985; 260: 12426-33.
    • Degen, J.L.1
  • 183
    • 0027030649 scopus 로고    scopus 로고
    • Regulation of plasminogen activators and type-1 plasminogen activator inhibitor by cyclic AMP and phorbol ester in rat astrocytes
    • Robbins R, Naftolin F, Andrade Gordon P.
    • Tranque P, Robbins R, Naftolin F, Andrade Gordon P. Regulation of plasminogen activators and type-1 plasminogen activator inhibitor by cyclic AMP and phorbol ester in rat astrocytes. Glia 1992; 6: 163-71.
    • Glia 1992; 6: 163-71.
    • Tranque, P.1
  • 184
    • 0028954925 scopus 로고    scopus 로고
    • Effect of cyclic AMP on urokinase-type plasminogen activator receptor and fibrinolytic factors in a human osteoblast-like cell line
    • Matsumoto H, Shimada W et al.
    • Nonaka T, Matsumoto H, Shimada W et al. Effect of cyclic AMP on urokinase-type plasminogen activator receptor and fibrinolytic factors in a human osteoblast-like cell line. Biochim Biophys Acta 1995; 1266: 50-6.
    • Biochim Biophys Acta 1995; 1266: 50-6.
    • Nonaka, T.1
  • 185
    • 0026654216 scopus 로고    scopus 로고
    • Cyclic AMP-dependent protein kinase controls basal gene activity and steroidogenesis in Y1 adrenal tumor cells
    • Abrahamsen M S, Degen J L, Morris D R, McKnight G S.
    • Clegg C H, Abrahamsen M S, Degen J L, Morris D R, McKnight G S. Cyclic AMP-dependent protein kinase controls basal gene activity and steroidogenesis in Y1 adrenal tumor cells. Biochemistry 1992; 31: 3720-26.
    • Biochemistry 1992; 31: 3720-26.
    • Clegg, C.H.1
  • 186
    • 0025009846 scopus 로고    scopus 로고
    • Follicle-stimulating hormone and cyclic AMP induce transcription from the human urokinase promoter in primary cultures of mouse Sertoli cells
    • Grimaldi P, Blasi F, Geremia R, Verde P.
    • Rossi P, Grimaldi P, Blasi F, Geremia R, Verde P. Follicle-stimulating hormone and cyclic AMP induce transcription from the human urokinase promoter in primary cultures of mouse Sertoli cells. Mol Endocrinol 1990; 4: 940-6.
    • Mol Endocrinol 1990; 4: 940-6.
    • Rossi, P.1
  • 187
    • 0029009983 scopus 로고    scopus 로고
    • The species-specific differences in the cAMP regulation of the tissue-type plasminogen activator gene between rat
    • Leonardson G, Ny T. mouse and human is caused by a one-nucleotide substitution in the cAMP-responsive element of the promoters.
    • Holmberg M, Leonardson G, Ny T. The species-specific differences in the cAMP regulation of the tissue-type plasminogen activator gene between rat, mouse and human is caused by a one-nucleotide substitution in the cAMP-responsive element of the promoters. Eur J Biochem 1995; 231: 466-74.
    • Eur J Biochem 1995; 231: 466-74.
    • Holmberg, M.1
  • 188
    • 0023663116 scopus 로고    scopus 로고
    • Transcription factor AP-2 mediates induction by two different signal-transduction pathways: Protein kinase C and cAMP
    • Chiu R, Karin M.
    • Imagawa M, Chiu R, Karin M. Transcription factor AP-2 mediates induction by two different signal-transduction pathways: protein kinase C and cAMP. Cell 1987; 51: 251-60.
    • Cell 1987; 51: 251-60.
    • Imagawa, M.1
  • 189
    • 0028292296 scopus 로고    scopus 로고
    • Activation of cAMP-dependent protein kinase alters the chromatin structure of the urokinase-type plasminogen activator gene promoter
    • Catanzariti L, Hemmings B A, Kiefer B, Nagamine Y.
    • Lee J S, Catanzariti L, Hemmings B A, Kiefer B, Nagamine Y. Activation of cAMP-dependent protein kinase alters the chromatin structure of the urokinase-type plasminogen activator gene promoter. Nucleic Acids Res 1994; 22: 569-75.
    • Nucleic Acids Res 1994; 22: 569-75.
    • Lee, J.S.1
  • 190
    • 0027298881 scopus 로고    scopus 로고
    • Purification and cDNA cloning of a transcription factor which functionally cooperates within a cAMP regulatory unit in the porcine u-PA gene
    • Matthies R, Hofsteenge J, Nagamine Y.
    • Menoud P-A, Matthies R, Hofsteenge J, Nagamine Y. Purification and cDNA cloning of a transcription factor which functionally cooperates within a cAMP regulatory unit in the porcine u-PA gene. Nucleic Acids Res 1993; 21: 1845-52.
    • Nucleic Acids Res 1993; 21: 1845-52.
    • Menoud, P.-A.1
  • 191
    • 0029144137 scopus 로고    scopus 로고
    • Role of LFB3 in cell-specific cAMP induction of the urokinase-type plasminogen activator gene
    • Stief A, Menoud P-A, Nagamine Y.
    • Marksitzer R, Stief A, Menoud P-A, Nagamine Y. Role of LFB3 in cell-specific cAMP induction of the urokinase-type plasminogen activator gene. J Biol Chem 1995; 270:
    • J Biol Chem 1995; 270
    • Marksitzer, R.1
  • 192
    • 0026299937 scopus 로고    scopus 로고
    • Transcriptional regulation of liverspecific gene expression
    • Cortese R.
    • De Simone V, Cortese R. Transcriptional regulation of liverspecific gene expression. Curr Opin Cell Biol 1992; 3: 960-5.
    • Curr Opin Cell Biol 1992; 3: 960-5.
    • De Simone, V.1
  • 193
    • 0026592340 scopus 로고    scopus 로고
    • A novel complex between the p65 subunit of NF-kappa B and c-Rel binds to a DNA element involved in the phorbol ester induction of the human urokinase gene
    • Nerlov C, Zabel U et al.
    • Hansen S K, Nerlov C, Zabel U et al. A novel complex between the p65 subunit of NF-kappa B and c-Rel binds to a DNA element involved in the phorbol ester induction of the human urokinase gene. EMBO J 1992; 11: 205-13.
    • EMBO J 1992; 11: 205-13.
    • Hansen, S.K.1
  • 194
    • 0025899613 scopus 로고    scopus 로고
    • A labile repressor acts through the NFkB-like binding sites of the human urokinase gene
    • Cocks BG, Hamilton J A.
    • Novak U, Cocks BG, Hamilton J A. A labile repressor acts through the NFkB-like binding sites of the human urokinase gene. Nucleic Acids Res 1991; 19: 3389-93.
    • Nucleic Acids Res 1991; 19: 3389-93.
    • Novak, U.1
  • 195
    • 0023691347 scopus 로고    scopus 로고
    • An upstream enhancer and a negative element in the 5′ flanking region of the human urokinase plasminogen activator gene
    • Boast S, Franze A, Robbiati F, Blasi F.
    • Verde P, Boast S, Franze A, Robbiati F, Blasi F. An upstream enhancer and a negative element in the 5′ flanking region of the human urokinase plasminogen activator gene. Nucleic Acids Res 1988; 16: 10699-716.
    • Nucleic Acids Res 1988; 16: 10699-716.
    • Verde, P.1
  • 196
    • 0025730632 scopus 로고    scopus 로고
    • A cell-type specific and enhancer-dependent silencer in the regulation of the expression of the human urokinase plasminogen activator gene
    • Rennie P S, Blasi F.
    • Cannio R, Rennie P S, Blasi F. A cell-type specific and enhancer-dependent silencer in the regulation of the expression of the human urokinase plasminogen activator gene. Nucleic Acids Res 1991; 19: 2303-8.
    • Nucleic Acids Res 1991; 19: 2303-8.
    • Cannio, R.1
  • 197
    • 0025311495 scopus 로고    scopus 로고
    • Macromolecular interaction on a cAMP responsive region in the urokinase-type plasminogen activator gene: A role of protein phosphorylation
    • Pearson D, Nagamine Y.
    • von der Ahe D, Pearson D, Nagamine Y. Macromolecular interaction on a cAMP responsive region in the urokinase-type plasminogen activator gene: a role
    • Nucleic Acids Res 1990; 18: 1991-9.
    • Ahe, D.1
  • 198
    • 0023118944 scopus 로고    scopus 로고
    • Inhibition of protein synthesis in LLC-PK1 cells increases calcitonin-induced plasminogen-activator gene transcription and mRNA stability
    • Pearson D, Horiuchi A, Nagamine Y.
    • Altus M S, Pearson D, Horiuchi A, Nagamine Y. Inhibition of protein synthesis in LLC-PK1 cells increases calcitonin-induced plasminogen-activator gene transcription and mRNA stability. Biochem J 1987; 242: 387-92.
    • Biochem J 1987; 242: 387-92.
    • Altus, M.S.1
  • 199
    • 0026068754 scopus 로고    scopus 로고
    • Okadaic acid induction of the urokinase-type plasminogen activator gene occurs independently of cAMP-dependent protein kinase and protein kinase C and is sensitive to protein synthesis inhibition
    • Ziegler A.
    • Nagamine Y, Ziegler A. Okadaic acid induction of the urokinase-type plasminogen activator gene occurs independently of cAMP-dependent protein kinase and protein kinase C and is sensitive to protein synthesis inhibition. EMBO J 1991; 10: 117-22.
    • EMBO J 1991; 10: 117-22.
    • Nagamine, Y.1
  • 200
    • 0023138146 scopus 로고    scopus 로고
    • Dexamethasone coordinately inhibits plasminogen activator gene expression and enzyme activity in porcine kidney cells
    • Altus M S, Horiuchi A, Nagamine Y.
    • Pearson D, Altus M S, Horiuchi A, Nagamine Y. Dexamethasone coordinately inhibits plasminogen activator gene expression and enzyme activity in porcine kidney cells. Biochem Biophys Res Commun 1987; 143: 329-36.
    • Biochem Biophys Res Commun 1987; 143: 329-36.
    • Pearson, D.1
  • 201
    • 0022773448 scopus 로고    scopus 로고
    • Suppression of urokinase-type plasminogen activator mRNA levels in human fibrosarcoma cells and synovial fibroblasts by anti-inflammatory glucocorticoids
    • Richards R I, Crawford R J, Hamilton J A.
    • Medcalf R L, Richards R I, Crawford R J, Hamilton J A. Suppression of urokinase-type plasminogen activator mRNA levels in human fibrosarcoma cells and synovial fibroblasts by anti-inflammatory glucocorticoids. EMBO J 1986; 5: 2217-22.
    • EMBO J 1986; 5: 2217-22.
    • Medcalf, R.L.1
  • 202
    • 0023680161 scopus 로고    scopus 로고
    • Modulation of urokinase-type plasminogen activator messenger RNA levels in human synovial fibroblasts by interleukin-1
    • Hamilton J A. retinoic acid, and a glucocorticoid.
    • Vitti G F, Hamilton J A. Modulation of urokinase-type plasminogen activator messenger RNA levels in human synovial fibroblasts by interleukin-1, retinoic acid, and a glucocorticoid. Arthritis Rheum 1988; 31: 1046-51.
    • Arthritis Rheum 1988; 31: 1046-51.
    • Vitti, G.F.1
  • 204
    • 0025900910 scopus 로고    scopus 로고
    • The ligand-binding domain of the cell surface receptor for urokinase-type plasminogen activator
    • Ploug M, Patthy L, Houen G, Blasi F, Danø K.
    • Behrendt N, Ploug M, Patthy L, Houen G, Blasi F, Danø K. The ligand-binding domain of the cell surface receptor for urokinase-type plasminogen activator. J. Biol. Chem. 1991; 266: 7842-7.
    • J. Biol. Chem. 1991; 266: 7842-7.
    • Behrendt, N.1
  • 206
    • 0030026674 scopus 로고    scopus 로고
    • In vivo expression of functional mutant urokinase receptor lacking domain D2 or domain D3
    • Limongi P, Crippa M P et al.
    • Riittinen L, Limongi P, Crippa M P et al. In vivo expression of functional mutant urokinase receptor lacking domain D2 or domain D3. FEES Lett 1996; 381: 1-6.
    • FEES Lett 1996; 381: 1-6.
    • Riittinen, L.1
  • 207
    • 0024508318 scopus 로고    scopus 로고
    • Plasminogen activation initiated by single-chain urokinase plasminogen activator: Potentiation by U937 cells
    • Scully M F, Kakkar V V.
    • Ellis V, Scully M F, Kakkar V V. Plasminogen activation initiated by single-chain urokinase plasminogen activator: potentiation by U937 cells. J Biol Chem 1989; 264: 2185-8.
    • J Biol Chem 1989; 264: 2185-8.
    • Ellis, V.1
  • 208
    • 0024544506 scopus 로고    scopus 로고
    • Activation of pro-urokinase and plasminogen on human sarcoma cells: A proteolytic system with surface-bound reactants
    • Pöllänen J, Tapiovaara H et al.
    • Stephens R W, Pöllänen J, Tapiovaara H et al. Activation of pro-urokinase and plasminogen on human sarcoma cells: a proteolytic system with surface-bound reactants. J Cell Biol 1989; 108: 1987-95.
    • J Cell Biol 1989; 108: 1987-95.
    • Stephens, R.W.1
  • 209
    • 0025310993 scopus 로고    scopus 로고
    • Characterization of the activation of latent TFG-b by co-cultures of endothelial cells and pericytes or smooth muscle cells: A self regulating system
    • Tsuboi R, Lyons R, Moses H, Rifkin D B.
    • Sato Y, Tsuboi R, Lyons R, Moses H, Rifkin D B. Characterization of the activation of latent TFG-b by co-cultures of endothelial cells and pericytes or smooth muscle cells: a self regulating system. J Cell Biol 1990; 111: 757-74.
    • J Cell Biol 1990; 111: 757-74.
    • Sato, Y.1
  • 210
    • 0028268212 scopus 로고    scopus 로고
    • A requirement for receptor-bound urokinase in plasmin-dependent cellular conversion of latent TGF-β to TGF-β
    • Blasi F, Rifkin D B.
    • Odekon L E, Blasi F, Rifkin D B. A requirement for receptor-bound urokinase in plasmin-dependent cellular conversion of latent TGF-β to TGF-β. J Cell Physiol 1994; 158: 396-407.
    • J Cell Physiol 1994; 158: 396-407.
    • Odekon, L.E.1
  • 211
    • 0027077443 scopus 로고    scopus 로고
    • Extracellular proteolytic cleavage by urokinase is required for activation of hepatocyte growth factor/scatter factor
    • Tamagnone L, Vigna et al.
    • Naldini L, Tamagnone L, Vigna et al. Extracellular proteolytic cleavage by urokinase is required for activation of hepatocyte growth factor/scatter factor. EMBO J 1992; 11: 4825-33.
    • EMBO J 1992; 11: 4825-33.
    • Naldini, L.1
  • 212
    • 0028912590 scopus 로고    scopus 로고
    • Biological activation of pro-HGF (hepatocyte growth factor) by urokinase is controlled by a stoichiometric reaction
    • Vigna E, Bardelli A, Follenzi A, Galimi F, Comoglio P M.
    • Naldini L, Vigna E, Bardelli A, Follenzi A, Galimi F, Comoglio P M. Biological activation of pro-HGF (hepatocyte growth factor) by urokinase is controlled by a stoichiometric reaction. J Biol Chem 1995; 270: 603-11.
    • J Biol Chem 1995; 270: 603-11.
    • Naldini, L.1
  • 213
    • 0029923744 scopus 로고    scopus 로고
    • Proteolytic cleavage of the urokinase receptor substitutes for the agonist-induced chemotactic effect
    • Guttinger M, Valcamonica S, Sidenius N, Blasi F, Fazioli F.
    • Resnati M, Guttinger M, Valcamonica S, Sidenius N, Blasi F, Fazioli F. Proteolytic cleavage of the urokinase receptor substitutes for the agonist-induced chemotactic effect. EMBO J 1996; 15: 1572-82.
    • EMBO J 1996; 15: 1572-82.
    • Resnati, M.1
  • 214
    • 0028925552 scopus 로고    scopus 로고
    • Urokinase plasminogen activator receptor β2-type integrins and src-kinases within a single receptor complex of human monocytes
    • Horejsi V, Hansmann C et al.
    • Bohuslav J, Horejsi V, Hansmann C et al. Urokinase plasminogen activator receptor β2-type integrins and src-kinases within a single receptor complex of human monocytes. J Exp Med 1995; 181: 1381-90.
    • J Exp Med 1995; 181: 1381-90.
    • Bohuslav, J.1
  • 215
    • 0028334672 scopus 로고    scopus 로고
    • Reversible cellular adhesion to vitronectin linked to urokinase receptor occupancy
    • Chapman H A.
    • Waltz D A, Chapman H A. Reversible cellular adhesion to vitronectin linked to urokinase receptor occupancy. J Biol Chem 1994; 269: 32380-8.
    • J Biol Chem 1994; 269: 32380-8.
    • Waltz, D.A.1
  • 216
    • 0028569183 scopus 로고    scopus 로고
    • Identification of the urokinase receptor as an adhesion receptor for vitronectin
    • Waltz D A, Rao N, Drummond R J, Rosenberg S, Chapman H A.
    • Wei Y, Waltz D A, Rao N, Drummond R J, Rosenberg S, Chapman H A. Identification of the urokinase receptor as an adhesion receptor for vitronectin. J Biol Chem 1994; 269: 32380-8.
    • J Biol Chem 1994; 269: 32380-8.
    • Wei, Y.1
  • 217
    • 0029873910 scopus 로고    scopus 로고
    • The urokinase receptor is a major vitronectin-binding protein on endothelial cells
    • Kost C, Wilhelm O G, Andreasen P A, Preissner K T.
    • Kanse S M, Kost C, Wilhelm O G, Andreasen P A, Preissner K T. The urokinase receptor is a major vitronectin-binding protein on endothelial cells. Exp Cell Res 1996; 224: (in press).
    • Exp Cell Res 1996; 224: (In Press).
    • Kanse, S.M.1
  • 218
    • 0023229547 scopus 로고    scopus 로고
    • Human urokinase-type plasminogen activator stimulates chemotaxis of human neutrophils
    • Gilboa N.
    • Gudewicz P W, Gilboa N. Human urokinase-type plasminogen activator stimulates chemotaxis of human neutrophils. Biochem. Biophys Res Commun 1987; 147: 1176-81.
    • Biochem. Biophys Res Commun 1987; 147: 1176-81.
    • Gudewicz, P.W.1
  • 219
    • 0024239460 scopus 로고    scopus 로고
    • Interaction of urokinase with specific receptors stimulates mobilization of bovine adrenal capillary endothelial cells
    • Ziehe M, Morbidelli L, Magnelli L, Del Rosso M.
    • Fibbi G, Ziehe M, Morbidelli L, Magnelli L, Del Rosso M. Interaction of urokinase with specific receptors stimulates mobilization of bovine adrenal capillary endothelial cells. Exp Cell Res 1988; 179: 385-95.
    • Exp Cell Res 1988; 179: 385-95.
    • Fibbi, G.1
  • 221
    • 0027219030 scopus 로고    scopus 로고
    • Urokinase-urokinase receptor interaction: Non-mitogenic signal transduction in human epidermal cells
    • Anichini E, Pedersen N et al.
    • Del Rosso M, Anichini E, Pedersen N et al. Urokinase-urokinase receptor interaction: non-mitogenic signal transduction in human epidermal cells. Biochem Biophys Res. Commun 1993; 190: 347-52.
    • Biochem Biophys Res. Commun 1993; 190: 347-52.
    • Del Rosso, M.1
  • 222
    • 0027506444 scopus 로고    scopus 로고
    • Interaction of the urokinase-type plasminogen activator (u-PA) with its cellular receptor (u-PAR) induces phosphorylation on tyrosine of a 38 kDa protein
    • Petri T, Schleuning W D.
    • Dumler I, Petri T, Schleuning W D. Interaction of the urokinase-type plasminogen activator (u-PA) with its cellular receptor (u-PAR) induces phosphorylation on tyrosine of a 38 kDa protein. FEBS Lett 1993; 322: 37-40.
    • FEBS Lett 1993; 322: 37-40.
    • Dumler, I.1
  • 223
    • 0028305433 scopus 로고    scopus 로고
    • Induction of cell migration by pro-urokinase binding to its receptor: Possible mechanism for signal transduction in human epithelial cells
    • Masur S K, Lazega D, Waxman S, Ossowski L.
    • Busso N, Masur S K, Lazega D, Waxman S, Ossowski L. Induction of cell migration by pro-urokinase binding to its receptor: possible mechanism for signal transduction in human epithelial cells. J Cell Biol 1994; 126: 259-70.
    • J Cell Biol 1994; 126: 259-70.
    • Busso, N.1
  • 224
    • 0028331139 scopus 로고    scopus 로고
    • The urokinase receptor is required for human monocyte chemotaxis in vivo
    • Todd R F, Wilkinson C C, Sitrian R G.
    • Gyetko M R, Todd R F, Wilkinson C C, Sitrian R G. The urokinase receptor is required for human monocyte chemotaxis in vivo. J Clin Invest 1994; 93: 1380-7.
    • J Clin Invest 1994; 93: 1380-7.
    • Gyetko, M.R.1
  • 226
    • 0024571517 scopus 로고    scopus 로고
    • Regulation of urokinase receptors in in monocyte-like U937 cells by phorbol ester phorbol-myristate-acetate
    • Kajtaniak E L, Nielsen L S et al.
    • Picone R, Kajtaniak E L, Nielsen L S et al. Regulation of urokinase receptors in in monocyte-like U937 cells by phorbol ester phorbol-myristate-acetate. J Cell Biol 1989; 108: 693-702.
    • J Cell Biol 1989; 108: 693-702.
    • Picone, R.1
  • 227
    • 0027174189 scopus 로고    scopus 로고
    • Cytokines induce urokinase-dependent adhesion of human myeloid cells: A regulatory role for plasminogen activator inhibitors
    • Sailor L Z, Chapman H A.
    • Waltz D S, Sailor L Z, Chapman H A. Cytokines induce urokinase-dependent adhesion of human myeloid cells: a regulatory role for plasminogen activator inhibitors. J Clin Invest 1993; 91: 1541-52.
    • J Clin Invest 1993; 91: 1541-52.
    • Waltz, D.S.1
  • 228
    • 0029113231 scopus 로고    scopus 로고
    • Urokinase receptor is a multifunctional protein: Influence of receptor occupancy on macrophage gene expression
    • Shi G-P, Chapman H A.
    • Rao N K, Shi G-P, Chapman H A. Urokinase receptor is a multifunctional protein: influence of receptor occupancy on macrophage gene expression. J Clin Invest 1995; 96: 465-74.
    • J Clin Invest 1995; 96: 465-74.
    • Rao, N.K.1
  • 229
    • 0025882214 scopus 로고    scopus 로고
    • An autocrine role for urokinase in phorbol-ester-mediated differentiation of myeloid cell lines
    • Chapman H A.
    • Nusrat A R, Chapman H A. An autocrine role for urokinase in phorbol-ester-mediated differentiation of myeloid cell lines. J Clin Invest 1991; 87: 1091-7.
    • J Clin Invest 1991; 87: 1091-7.
    • Nusrat, A.R.1
  • 230
    • 0023948675 scopus 로고    scopus 로고
    • Attachment of cultured human endothelial cells is promoted by specific association with S protein (vitronectin) as well as with the ternary S-protein-thrombin-antithrombin III complex
    • Anders E, Grulich-Henn J, Müller-Berghaus G.
    • Preissner K T, Anders E, Grulich-Henn J, Müller-Berghaus G. Attachment of cultured human endothelial cells is promoted by specific association with S protein (vitronectin) as well as with the ternary S-protein-thrombin-antithrombin III complex. Blood 1998; 71: 1581-9.
    • Blood 1998; 71: 1581-9.
    • Preissner, K.T.1
  • 231
    • 0024532550 scopus 로고    scopus 로고
    • Purification of a protein from human plasma that binds to type 1 plasminogen activator inhibitor and prevents its interaction with extracellular matrix
    • Loskutoff D J.
    • Mimuro J, Loskutoff D J. Purification of a protein from human plasma that binds to type 1 plasminogen activator inhibitor and prevents its interaction with extracellular matrix. Evidence that the protein is vitronectin. J Biol Chem 1989; 264: 936-9.
    • Evidence That the Protein Is Vitronectin. J Biol Chem 1989; 264: 936-9.
    • Mimuro, J.1
  • 232
    • 0029053053 scopus 로고    scopus 로고
    • Specific binding of urinary-type plasminogen activator (u-PA) to vitronectin and its role in mediating u-PA dependent adhesion of U-937 cells
    • Enghild J J, Pizzo S V, Stack S M.
    • Moser T L, Enghild J J, Pizzo S V, Stack S M. Specific binding of urinary-type plasminogen activator (u-PA) to vitronectin and its role in mediating u-PA dependent adhesion of U-937 cells. Biochem J 1995; 307: 867-73.
    • Biochem J 1995; 307: 867-73.
    • Moser, T.L.1
  • 233
    • 0028173624 scopus 로고    scopus 로고
    • Physical association of complement receptor type 3 and urokinase type plasminogen activator receptor in neutrophil membranes
    • Kindzelskii A L, Todd R F, Petty H R.
    • Xue W, Kindzelskii A L, Todd R F, Petty H R. Physical association of complement receptor type 3 and urokinase type plasminogen activator receptor in neutrophil membranes. J Immunol 1994; 152: 4630-40.
    • J Immunol 1994; 152: 4630-40.
    • Xue, W.1
  • 234
    • 0030068772 scopus 로고    scopus 로고
    • Urokinase-type plasminogen activator receptor reversibly dissociates from complement receptor type 3 (αMβ2 CD1 1b/CD18) during neutrophil polarization
    • Laska Z O, Todd II R F, Petty H R.
    • Kindzelskii A L, Laska Z O, Todd II R F, Petty H R. Urokinase-type plasminogen activator receptor reversibly dissociates from complement receptor type 3 (αMβ2 CD1 1b/CD18) during neutrophil polarization. J Immunol 1996; 156: 297-309.
    • J Immunol 1996; 156: 297-309.
    • Kindzelskii, A.L.1
  • 235
    • 0025856309 scopus 로고    scopus 로고
    • Role of lymphocyte adhesion receptors in transient interactions and cell locomotion
    • Springer T.
    • Dustin M L, Springer T. Role of lymphocyte adhesion receptors in transient interactions and cell locomotion. Annu Rev Immunol 1991; 9: 27-66.
    • Annu Rev Immunol 1991; 9: 27-66.
    • Dustin, M.L.1
  • 236
    • 0023192953 scopus 로고    scopus 로고
    • Distinct localization of urokinase-type plasminogen activator and its type-1 inhibitor under cultured human fibroblasts and sarcoma cells
    • Saksela O, Salonen E-M et al.
    • Pöllänen J, Saksela O, Salonen E-M et al. Distinct localization of urokinase-type plasminogen activator and its type-1 inhibitor under cultured human fibroblasts and sarcoma cells. J Cell Biol 1987; 104: 1085-96.
    • J Cell Biol 1987; 104: 1085-96.
    • Pöllänen, J.1
  • 237
    • 0027250146 scopus 로고    scopus 로고
    • Distribution and lateral mobility of the urokinase receptor complex at the cell surface
    • Stephens R W, Hedman K et al.
    • Myöhänen H T, Stephens R W, Hedman K et al. Distribution and lateral mobility of the urokinase receptor complex at the cell surface. J Histochem Cytochem 1993; 41: 1291-301.
    • J Histochem Cytochem 1993; 41: 1291-301.
    • Myöhänen, H.T.1
  • 238
    • 0024349195 scopus 로고    scopus 로고
    • Accessibility of receptor-bound urokinase to type-1 plasminogen activator inhibitor
    • Andreasen P A, Ragno P, Mayer M, Danø K, Blasi F.
    • Cubellis M V, Andreasen P A, Ragno P, Mayer M, Danø K, Blasi F. Accessibility of receptor-bound urokinase to type-1 plasminogen activator inhibitor. Proc Nad Acad Sci USA 1989; 86: 4828-32.
    • Proc Nad Acad Sci USA 1989; 86: 4828-32.
    • Cubellis, M.V.1
  • 239
    • 0025273735 scopus 로고    scopus 로고
    • Receptor-mediated internalization and degradation of urokinase-PAI-1 complex in human U937 cells
    • Wun T-C, Blasi F.
    • Cubellis M V, Wun T-C, Blasi F. Receptor-mediated internalization and degradation of urokinase-PAI-1 complex in human U937 cells. EMBO J, 1990; 9: 1079-85.
    • EMBO J, 1990; 9: 1079-85.
    • Cubellis, M.V.1
  • 240
    • 0028236893 scopus 로고    scopus 로고
    • Protease Nexin-1:urokinase complexes are internalized and degraded through a mechanism that requires both urokinase receptor and alpha-2 macroglobulin receptor
    • Olson D, Blasi F.
    • Conese M, Olson D, Blasi F. Protease Nexin-1:urokinase complexes are internalized and degraded through a mechanism that requires both urokinase receptor and alpha-2 macroglobulin receptor. J Biol Chem, 1994; 269: 17886-92.
    • J Biol Chem, 1994; 269: 17886-92.
    • Conese, M.1
  • 242
    • 0029589630 scopus 로고    scopus 로고
    • Alpha-2 macroglobulin receptor-dependent internalization of the urokinase receptor
    • Nykjær A, Christensen EI et al.
    • Conese M, Nykjær A, Christensen EI et al. Alpha-2 macroglobulin receptor-dependent internalization of the urokinase receptor. J Cell Biol 1995; 131: 1609-22.
    • J Cell Biol 1995; 131: 1609-22.
    • Conese, M.1
  • 243
    • 0025133170 scopus 로고    scopus 로고
    • Plasminogen activator type-1 stabilizes vitronectin-dependent adhesion in HT1080 cells
    • McKeown-Longo P J et al.
    • Ciambrone G L, McKeown-Longo P J et al. Plasminogen activator type-1 stabilizes vitronectin-dependent adhesion in HT1080 cells. J Cell Biol 1990; 111: 2183-2195.
    • J Cell Biol 1990; 111: 2183-2195.
    • Ciambrone, G.L.1
  • 244
    • 0025995880 scopus 로고    scopus 로고
    • Clinical relevance of the urokinase-type and tissue-type plasminogen activators and their type-1 inhibitor in breast cancer
    • Schmitt M, Graeff H.
    • Jänicke F, Schmitt M, Graeff H. Clinical relevance of the urokinase-type and tissue-type plasminogen activators and their type-1 inhibitor in breast cancer. Semin Thromb Hemost 1991; 17: 303-12.
    • Semin Thromb Hemost 1991; 17: 303-12.
    • Jänicke, F.1
  • 245
    • 0027550662 scopus 로고    scopus 로고
    • Urokinase and its receptor: A paracrine/autocrine system regulating cell migration and invasiveness
    • Blasi F. Urokinase and its receptor: a paracrine/autocrine system regulating cell migration and invasiveness. BioEssays 1993; 15: 105-11.
    • BioEssays 1993; 15: 105-11.
    • Blasi, F.1
  • 247
    • 0023603282 scopus 로고    scopus 로고
    • Proliferation of a human epidermal tumor cell line stimulated by urokinase
    • Wojta J, Christ G, Binder B R.
    • Kirchheimer J C, Wojta J, Christ G, Binder B R. Proliferation of a human epidermal tumor cell line stimulated by urokinase. FASEB J 1987; 1: 125-8.
    • FASEB J 1987; 1: 125-8.
    • Kirchheimer, J.C.1
  • 248
    • 0025800278 scopus 로고    scopus 로고
    • Growth factor-like effect of urokinase type plasminogen activator in human renal cells
    • Rebibou J M, Peraldi M N, Meulders Q, Rondeau E.
    • He C J, Rebibou J M, Peraldi M N, Meulders Q, Rondeau E. Growth factor-like effect of urokinase type plasminogen activator in human renal cells. Biochem Biophys Res Commun 1991; 176: 1408-16.
    • Biochem Biophys Res Commun 1991; 176: 1408-16.
    • He, C.J.1
  • 249
    • 0025543131 scopus 로고    scopus 로고
    • An amino-terminal fragment of urokinase isolated from a prostate cancer cell line (PC-3) is mitogenic for osteoblast-like cells
    • Desjardins J, Bell A W et al.
    • Rabbani S A, Desjardins J, Bell A W et al. An amino-terminal fragment of urokinase isolated from a prostate cancer cell line (PC-3) is mitogenic for osteoblast-like cells. Biochem Biophys Res Commun 1990; 173: 1058-64.
    • Biochem Biophys Res Commun 1990; 173: 1058-64.
    • Rabbani, S.A.1
  • 250
    • 0026643491 scopus 로고    scopus 로고
    • Structural requirements for the growth factor activity of the amino-terminal domain of urokinase
    • Mazar A P, Bernier S M et al.
    • Rabbani S A, Mazar A P, Bernier S M et al. Structural requirements for the growth factor activity of the amino-terminal domain of urokinase. J Biol Chem 1992; 267: 14151-6.
    • J Biol Chem 1992; 267: 14151-6.
    • Rabbani, S.A.1
  • 251
    • 0029034939 scopus 로고    scopus 로고
    • Src enhances the spreading of src-/- Fibroblasts on fibronectin by a kinase-independent mechanism
    • Swedlow J R, Morgan D O, Varmus H E. c-
    • Kaplan K B, Swedlow J R, Morgan D O, Varmus H E. c-Src enhances the spreading of src-/- fibroblasts on fibronectin by a kinase-independent mechanism. Genes Dev 1995; 9: 1505-17.
    • Genes Dev 1995; 9: 1505-17.
    • Kaplan, K.B.1
  • 252
    • 0026644421 scopus 로고    scopus 로고
    • Urokinase plasminogen activator cleaves its cell surface receptor releasing the ligand-binding domain
    • Rønne E, Solberg H et al.
    • Høyer-Hansen G, Rønne E, Solberg H et al. Urokinase plasminogen activator cleaves its cell surface receptor releasing the ligand-binding domain. J Biol Chem 1992; 267: 18224-9.
    • J Biol Chem 1992; 267: 18224-9.
    • Høyer-Hansen, G.1
  • 253
    • 0028101329 scopus 로고    scopus 로고
    • A cleaved form of the receptor for urokinase-type plasminogen activator in invasive transplanted human and murine tumors
    • Rømer J, Brünner N et al.
    • Solberg H, Rømer J, Brünner N et al. A cleaved form of the receptor for urokinase-type plasminogen activator in invasive transplanted human and murine tumors. Int J Cancer 1994; 58: 877-81.
    • Int J Cancer 1994; 58: 877-81.
    • Solberg, H.1


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