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Volumn 1378, Issue 1, 1998, Pages

Signal transduction via platelet-derived growth factor receptors

Author keywords

Antagonist; Cell growth; Cell migration; Cell transformation; Kinase; Platelet derived growth factor; Receptor; Signal transduction

Indexed keywords

PLATELET DERIVED GROWTH FACTOR; PLATELET DERIVED GROWTH FACTOR RECEPTOR; PROTEIN KINASE;

EID: 0032547385     PISSN: 0304419X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-419X(98)00015-8     Document Type: Review
Times cited : (731)

References (369)
  • 3
    • 0027936261 scopus 로고
    • Mice deficient for PDGF B show renal, cardiovascular, and hematological abnormalities
    • Levéen P., Pekny M., Gebre-Medhin S., Swolin B., Larsson E., Betsholtz C. Mice deficient for PDGF B show renal, cardiovascular, and hematological abnormalities. Genes Dev. 8:1994;1875-1887.
    • (1994) Genes Dev. , vol.8 , pp. 1875-1887
    • Levéen, P.1    Pekny, M.2    Gebre-Medhin, S.3    Swolin, B.4    Larsson, E.5    Betsholtz, C.6
  • 4
    • 0028059309 scopus 로고
    • Abnormal kidney development and hematological disorders in PDGF β-receptor mutant mice
    • Soriano P. Abnormal kidney development and hematological disorders in PDGF β-receptor mutant mice. Genes Dev. 8:1994;1888-1896.
    • (1994) Genes Dev. , vol.8 , pp. 1888-1896
    • Soriano, P.1
  • 5
    • 0030756325 scopus 로고    scopus 로고
    • Pericyte loss and microaneurysm formation in PDGF-B-deficient mice
    • Lindahl P., Johansson B.R., Levéen P., Betsholtz C. Pericyte loss and microaneurysm formation in PDGF-B-deficient mice. Science. 277:1997;242-245.
    • (1997) Science , vol.277 , pp. 242-245
    • Lindahl, P.1    Johansson, B.R.2    Levéen, P.3    Betsholtz, C.4
  • 7
    • 0030808324 scopus 로고    scopus 로고
    • The PDGFα receptor is required for neural crest cell development and for normal patterning of the somites
    • Soriano P. The PDGFα receptor is required for neural crest cell development and for normal patterning of the somites. Development. 124:1997;2691-2700.
    • (1997) Development , vol.124 , pp. 2691-2700
    • Soriano, P.1
  • 8
    • 0026595966 scopus 로고
    • Platelet-derived growth factor BB for the treatment of chronic pressure ulcers
    • Robson M.C., Phillips L.G., Thomason A., Robson L.E., Pierce G.F. Platelet-derived growth factor BB for the treatment of chronic pressure ulcers. Lancet. 339:1992;23-25.
    • (1992) Lancet , vol.339 , pp. 23-25
    • Robson, M.C.1    Phillips, L.G.2    Thomason, A.3    Robson, L.E.4    Pierce, G.F.5
  • 9
    • 0029824569 scopus 로고    scopus 로고
    • A novel physiological function for platelet-derived growth factor-BB in rat dermis
    • Rodt S.Å., Åhlén K., Berg A., Rubin K., Reed R.K. A novel physiological function for platelet-derived growth factor-BB in rat dermis. J. Physiol. (Lond.). 495:1996;193-200.
    • (1996) J. Physiol. (Lond.) , vol.495 , pp. 193-200
    • Rodt, S.Å.1    Åhlén, K.2    Berg, A.3    Rubin, K.4    Reed, R.K.5
  • 11
    • 0025167577 scopus 로고
    • The platelet-derived growth factor isomers, PDGF-AA, PDGF-AB and PDGF-BB, induce contraction of vascular smooth muscle cells by different intracellular mechanisms
    • Sachinidis A., Locher R., Hoppe J., Vetter W. 90)T. The platelet-derived growth factor isomers, PDGF-AA, PDGF-AB and PDGF-BB, induce contraction of vascular smooth muscle cells by different intracellular mechanisms. FEBS Lett. 272:1990;95-98.
    • (1990) FEBS Lett. , vol.272 , pp. 95-98
    • Sachinidis, A.1    Locher, R.2    Hoppe, J.3    Vetter W.T. XC4
  • 12
    • 0026505966 scopus 로고
    • Platelet-derived growth factor receptors on macrovascular endothelial cells mediate relaxation via nitric oxide in rat aorta
    • Cunningham L.D., Brecher P., Cohen R.A. Platelet-derived growth factor receptors on macrovascular endothelial cells mediate relaxation via nitric oxide in rat aorta. J. Clin. Invest. 89:1992;878-882.
    • (1992) J. Clin. Invest. , vol.89 , pp. 878-882
    • Cunningham, L.D.1    Brecher, P.2    Cohen, R.A.3
  • 13
    • 0024542429 scopus 로고
    • Collagen-induced binding to human platelets of platelet-derived growth factor leading to inhibition of P43 and P20 phosphorylation
    • Bryckaert M.C., Rendu F., Tobelem G., Wasteson Å. Collagen-induced binding to human platelets of platelet-derived growth factor leading to inhibition of P43 and P20 phosphorylation. J. Biol. Chem. 264:1989;4336-4341.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4336-4341
    • Bryckaert, M.C.1    Rendu, F.2    Tobelem, G.3    Wasteson, Å.4
  • 14
    • 0028221289 scopus 로고
    • Negative feedback regulation of human platelets via autocrine activation of the platelet-derived growth factor α-receptor
    • Vassbotn F.S., Havnen O.K., Heldin C.-H., Holmsen H. Negative feedback regulation of human platelets via autocrine activation of the platelet-derived growth factor α-receptor. J. Biol. Chem. 269:1994;13874-13879.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13874-13879
    • Vassbotn, F.S.1    Havnen, O.K.2    Heldin, C.-H.3    Holmsen, H.4
  • 15
    • 0026583942 scopus 로고
    • PDGF α- and β-receptors activate unique and common signal transduction pathways
    • Eriksson A., Siegbahn A., Westermark B., Heldin C.-H., Claesson-Welsh L. PDGF α- and β-receptors activate unique and common signal transduction pathways. EMBO J. 11:1992;543-550.
    • (1992) EMBO J. , vol.11 , pp. 543-550
    • Eriksson, A.1    Siegbahn, A.2    Westermark, B.3    Heldin, C.-H.4    Claesson-Welsh, L.5
  • 16
    • 0025216650 scopus 로고
    • Differential effects of the various isoforms of platelet-derived growth factor on chemotaxis of fibroblasts, monocytes, and granulocytes
    • Siegbahn A., Hammacher A., Westermark B., Heldin C.-H. Differential effects of the various isoforms of platelet-derived growth factor on chemotaxis of fibroblasts, monocytes, and granulocytes. J. Clin. Invest. 85:1990;916-920.
    • (1990) J. Clin. Invest. , vol.85 , pp. 916-920
    • Siegbahn, A.1    HamMacHer, A.2    Westermark, B.3    Heldin, C.-H.4
  • 17
    • 0029793998 scopus 로고    scopus 로고
    • The fumagillin analogue TNP-470 inhibits DNA synthesis of vascular smooth muscle cells stimulated by platelet-derived growth factor and insulin-like growth factor-I - Possible involvement of cyclin-dependent kinase 2
    • Koyama H., Nishizawa Y., Hosoi M., Fukumoto S., Kogawa K., Shioi A., Morii H. The fumagillin analogue TNP-470 inhibits DNA synthesis of vascular smooth muscle cells stimulated by platelet-derived growth factor and insulin-like growth factor-I - Possible involvement of cyclin-dependent kinase 2. Circ. Res. 79:1996;757-764.
    • (1996) Circ. Res. , vol.79 , pp. 757-764
    • Koyama, H.1    Nishizawa, Y.2    Hosoi, M.3    Fukumoto, S.4    Kogawa, K.5    Shioi, A.6    Morii, H.7
  • 20
    • 0026970194 scopus 로고
    • PDGF AA homodimers are potent chemoattractants for fibroblasts and neutrophils, and for monocytes activated by lymphocytes or cytokines
    • Shure D., Senior R.M., Griffin G.L., Deuel T.F. PDGF AA homodimers are potent chemoattractants for fibroblasts and neutrophils, and for monocytes activated by lymphocytes or cytokines. Biochem. Biophys. Res. Commun. 186:1992;1510-1514.
    • (1992) Biochem. Biophys. Res. Commun. , vol.186 , pp. 1510-1514
    • Shure, D.1    Senior, R.M.2    Griffin, G.L.3    Deuel, T.F.4
  • 21
    • 0024426331 scopus 로고
    • Both homodimeric isoforms of PDGF (AA and BB) have mitogenic and chemotactic activity and stimulate phosphoinositol turnover
    • Hosang M., Rouge M., Wipf B., Eggimann B., Kaufmann F., Hunziker W. Both homodimeric isoforms of PDGF (AA and BB) have mitogenic and chemotactic activity and stimulate phosphoinositol turnover. J. Cell. Physiol. 140:1989;558-564.
    • (1989) J. Cell. Physiol. , vol.140 , pp. 558-564
    • Hosang, M.1    Rouge, M.2    Wipf, B.3    Eggimann, B.4    Kaufmann, F.5    Hunziker, W.6
  • 22
    • 0025735518 scopus 로고
    • Tyrosine mutations within the α platelet-derived growth factor receptor kinase insert domain abrogate receptor-associated phosphatidylinositol-3 kinase activity without affecting mitogenic or chemotactic signal transduction
    • Yu J.-C., Heidaran M.A., Pierce J.H., Gutkind J.S., Lombardi D., Ruggiero M., Aaronson S.A. Tyrosine mutations within the α platelet-derived growth factor receptor kinase insert domain abrogate receptor-associated phosphatidylinositol-3 kinase activity without affecting mitogenic or chemotactic signal transduction. Mol. Cell. Biol. 11:1991;3780-3785.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3780-3785
    • Yu, J.-C.1    Heidaran, M.A.2    Pierce, J.H.3    Gutkind, J.S.4    Lombardi, D.5    Ruggiero, M.6    Aaronson, S.A.7
  • 23
    • 0029153817 scopus 로고
    • Differential chemotactic responses mediated by platelet-derived growth factor α- and β-receptors
    • Hayashi N., Takehara K., Soma Y. Differential chemotactic responses mediated by platelet-derived growth factor α- and β-receptors. Arch. Biochem. Biophys. 322:1995;423-428.
    • (1995) Arch. Biochem. Biophys. , vol.322 , pp. 423-428
    • Hayashi, N.1    Takehara, K.2    Soma, Y.3
  • 24
    • 0026635544 scopus 로고
    • Platelet-derived growth factor (PDGF) α receptor activation modulates the calcium mobilizing activity of the PDGF β receptor in Balb/c3T3 fibroblasts
    • Diliberto P.A., Gordon G.W., Yu C.-L., Earp H.S., Herman B. Platelet-derived growth factor (PDGF) α receptor activation modulates the calcium mobilizing activity of the PDGF β receptor in Balb/c3T3 fibroblasts. J. Biol. Chem. 267:1992;11888-11897.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11888-11897
    • Diliberto, P.A.1    Gordon, G.W.2    Yu, C.-L.3    Earp, H.S.4    Herman, B.5
  • 25
    • 0031041073 scopus 로고    scopus 로고
    • 2+ signaling in the CG4 oligodendroglial cell line and in transformed oligodendrocytes expressing the β-PDGF receptor
    • 2+ signaling in the CG4 oligodendroglial cell line and in transformed oligodendrocytes expressing the β-PDGF receptor. J. Biol. Chem. 272:1997;4351-4358.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4351-4358
    • Fatatis, A.1    Miller, R.J.2
  • 26
    • 0031962458 scopus 로고    scopus 로고
    • Rapid disruption of gap junctional communication and phosphorylation of connexin43 by platelet-derived growth factor in T51B rat liver epithelial cells expressing platelet-derived growth factor receptor
    • Hossain M.Z., Ao P., Boynton A.L. Rapid disruption of gap junctional communication and phosphorylation of connexin43 by platelet-derived growth factor in T51B rat liver epithelial cells expressing platelet-derived growth factor receptor. J. Cell. Physiol. 174:1998;66-77.
    • (1998) J. Cell. Physiol. , vol.174 , pp. 66-77
    • Hossain, M.Z.1    Ao, P.2    Boynton, A.L.3
  • 27
    • 0028229095 scopus 로고
    • Signal transduction proteins that associate with the platelet-derived growth factor (PDGF) receptor mediate the PDGF-induced release of glucose-6-phosphate dehydrogenase from permeabilized cells
    • Tian W.-N., Pignatare J.N., Stanton R.C. Signal transduction proteins that associate with the platelet-derived growth factor (PDGF) receptor mediate the PDGF-induced release of glucose-6-phosphate dehydrogenase from permeabilized cells. J. Biol. Chem. 269:1994;14798-14805.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14798-14805
    • Tian, W.-N.1    Pignatare, J.N.2    Stanton, R.C.3
  • 28
    • 0027082893 scopus 로고
    • Platelet-derived growth factor promotes survival of rat and human mesencephalic dopaminergic neurons in culture
    • Nikkhah G., Odin P., Smits A., Tingström A., Othberg A., Brundin P., Funa K., Lindvall O. Platelet-derived growth factor promotes survival of rat and human mesencephalic dopaminergic neurons in culture. Exp. Brain Res. 92:1993;516-523.
    • (1993) Exp. Brain Res. , vol.92 , pp. 516-523
    • Nikkhah, G.1    Odin, P.2    Smits, A.3    Tingström, A.4    Othberg, A.5    Brundin, P.6    Funa, K.7    Lindvall, O.8
  • 29
    • 0030878974 scopus 로고    scopus 로고
    • Characterization of platelet-derived growth factor (PDGF) action on a mouse neuroblastoma cell line, NB41, by introduction of an antisense PDGF β-receptor RNA
    • Funa K., Åhgren A. Characterization of platelet-derived growth factor (PDGF) action on a mouse neuroblastoma cell line, NB41, by introduction of an antisense PDGF β-receptor RNA. Cell Growth Diff. 8:1997;861-869.
    • (1997) Cell Growth Diff. , vol.8 , pp. 861-869
    • Funa, K.1    Åhgren, A.2
  • 30
    • 0028903234 scopus 로고
    • Apoptosis of human vascular smooth muscle cells derived from normal vessels and coronary atherosclerotic plaques
    • Bennett M.R., Evan G.I., Schwartz S.M. Apoptosis of human vascular smooth muscle cells derived from normal vessels and coronary atherosclerotic plaques. J. Clin. Invest. 95:1995;2266-2274.
    • (1995) J. Clin. Invest. , vol.95 , pp. 2266-2274
    • Bennett, M.R.1    Evan, G.I.2    Schwartz, S.M.3
  • 31
    • 0028963084 scopus 로고
    • Requirement for phosphatidylinositol-3 kinase in the prevention of apoptosis by nerve growth factor
    • Yao R., Cooper G.M. Requirement for phosphatidylinositol-3 kinase in the prevention of apoptosis by nerve growth factor. Science. 267:1995;2003-2006.
    • (1995) Science , vol.267 , pp. 2003-2006
    • Yao, R.1    Cooper, G.M.2
  • 32
    • 0028001468 scopus 로고
    • Platelet-derived growth factor isoforms prevent cell death during starvation of AKR-2B fibroblasts
    • Simm A., Hoppe V., Gazit A., Hoppe J. Platelet-derived growth factor isoforms prevent cell death during starvation of AKR-2B fibroblasts. J. Cell. Physiol. 160:1994;295-302.
    • (1994) J. Cell. Physiol. , vol.160 , pp. 295-302
    • Simm, A.1    Hoppe, V.2    Gazit, A.3    Hoppe, J.4
  • 33
    • 0027400729 scopus 로고
    • Disulfide bonds in recombinant human platelet-derived growth factor BB dimer: Characterization of intermolecular and intramolecular disulfide linkages
    • Haniu M., Rohde M.F., Kenney W.C. Disulfide bonds in recombinant human platelet-derived growth factor BB dimer: characterization of intermolecular and intramolecular disulfide linkages. Biochemistry. 32:1993;2431-2437.
    • (1993) Biochemistry , vol.32 , pp. 2431-2437
    • Haniu, M.1    Rohde, M.F.2    Kenney, W.C.3
  • 34
    • 0025910867 scopus 로고
    • On the structure of platelet-derived growth factor AA: C-terminal processing, epitopes, and characterization of cysteine residues
    • Jaumann M., Hoppe V., Tatje D., Eichner W., Hoppe J. On the structure of platelet-derived growth factor AA: C-terminal processing, epitopes, and characterization of cysteine residues. Biochemistry. 30:1991;3303-3309.
    • (1991) Biochemistry , vol.30 , pp. 3303-3309
    • Jaumann, M.1    Hoppe, V.2    Tatje, D.3    Eichner, W.4    Hoppe, J.5
  • 35
    • 0026754383 scopus 로고
    • Assignment of interchain disulfide bonds in platelet-derived growth factor (PDGF) and evidence for agonist activity of monomeric PDGF
    • Andersson M., Östman A., Bäckström G., Hellman U., George-Nascimento C., Westermark B., Heldin C.-H. Assignment of interchain disulfide bonds in platelet-derived growth factor (PDGF) and evidence for agonist activity of monomeric PDGF. J. Biol. Chem. 267:1992;11260-11266.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11260-11266
    • Andersson, M.1    Östman, A.2    Bäckström, G.3    Hellman, U.4    George-Nascimento, C.5    Westermark, B.6    Heldin, C.-H.7
  • 36
    • 0026744790 scopus 로고
    • Crystal structure of human platelet-derived growth factor BB
    • Oefner C., D'Arcy A., Winkler F.K., Eggimann B., Hosang M. Crystal structure of human platelet-derived growth factor BB. EMBO J. 11:1992;3921-3926.
    • (1992) EMBO J. , vol.11 , pp. 3921-3926
    • Oefner, C.1    D'Arcy, A.2    Winkler, F.K.3    Eggimann, B.4    Hosang, M.5
  • 37
    • 0027497326 scopus 로고
    • Assignment of intrachain disulfide bonds in platelet-derived growth factor B-chain
    • Östman A., Andersson M., Bäckström G., Heldin C.-H. Assignment of intrachain disulfide bonds in platelet-derived growth factor B-chain. J. Biol. Chem. 268:1993;13372-13377.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13372-13377
    • Östman, A.1    Andersson, M.2    Bäckström, G.3    Heldin, C.-H.4
  • 38
    • 0030795733 scopus 로고    scopus 로고
    • Vascular endothelial growth factor: Crystal structure and functional mapping of the kinase domain receptor binding site
    • Muller Y.A., Li B., Christinger H.W., Wells J.A., Cunningham B.C., de Vos A.M. Vascular endothelial growth factor: crystal structure and functional mapping of the kinase domain receptor binding site. Proc. Natl. Acad. Sci. USA. 94:1997;7192-7197.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7192-7197
    • Muller, Y.A.1    Li, B.2    Christinger, H.W.3    Wells, J.A.4    Cunningham, B.C.5    De Vos, A.M.6
  • 42
    • 0025836223 scopus 로고
    • Identification of three amino acids in the platelet-derived growth factor (PDGF) B-chain that are important for binding to the PDGF β-receptor
    • Östman A., Andersson M., Hellman U., Heldin C.-H. Identification of three amino acids in the platelet-derived growth factor (PDGF) B-chain that are important for binding to the PDGF β-receptor. J. Biol. Chem. 266:1991;10073-10077.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10073-10077
    • Östman, A.1    Andersson, M.2    Hellman, U.3    Heldin, C.-H.4
  • 43
    • 0026806540 scopus 로고
    • Five PDGF B amino acid substitutions convert PDGF A to a PDGF B-like transforming molecule
    • LaRochelle W.J., Pierce J.H., May-Siroff M., Giese N., Aaronson S.A. Five PDGF B amino acid substitutions convert PDGF A to a PDGF B-like transforming molecule. J. Biol. Chem. 267:1992;17074-17077.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17074-17077
    • Larochelle, W.J.1    Pierce, J.H.2    May-Siroff, M.3    Giese, N.4    Aaronson, S.A.5
  • 45
    • 0026586672 scopus 로고
    • Identification of individual amino acids in platelet-derived growth factor that contribute to the specificity towards the β-type receptor
    • Jaumann M., Tatje D., Hoppe J. Identification of individual amino acids in platelet-derived growth factor that contribute to the specificity towards the β-type receptor. FEBS Lett. 302:1992;265-268.
    • (1992) FEBS Lett. , vol.302 , pp. 265-268
    • Jaumann, M.1    Tatje, D.2    Hoppe, J.3
  • 46
    • 0030183048 scopus 로고    scopus 로고
    • Ligand-induced dimerization of growth factor receptors: Variations on the theme
    • Heldin C.-H., Östman A. Ligand-induced dimerization of growth factor receptors: variations on the theme. Cytokines Growth Factor Rev. 7:1996;3-10.
    • (1996) Cytokines Growth Factor Rev. , vol.7 , pp. 3-10
    • Heldin, C.-H.1    Östman, A.2
  • 48
    • 0027218489 scopus 로고
    • Dimerization of extracellular domains of platelet-derived growth factor receptors
    • Herren B., Rooney B., Weyer K.A., Iberg N., Schmid G., Pech M. Dimerization of extracellular domains of platelet-derived growth factor receptors. J. Biol. Chem. 268:1993;15088-15095.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15088-15095
    • Herren, B.1    Rooney, B.2    Weyer, K.A.3    Iberg, N.4    Schmid, G.5    Pech, M.6
  • 49
    • 0026007815 scopus 로고
    • A functional soluble extracellular region of the platelet-derived growth factor (PDGF) β-receptor antagonizes PDGF-stimulated responses
    • Duan D.-S.R., Pazin M.J., Fretto L.J., Williams L.T. A functional soluble extracellular region of the platelet-derived growth factor (PDGF) β-receptor antagonizes PDGF-stimulated responses. J. Biol. Chem. 266:1991;413-418.
    • (1991) J. Biol. Chem. , vol.266 , pp. 413-418
    • Duan, D.-S.R.1    Pazin, M.J.2    Fretto, L.J.3    Williams, L.T.4
  • 50
    • 0024320735 scopus 로고
    • Ligand-induced dimerization of the platelet-derived growth factor receptor. Monomer-dimer interconversion occurs independent of receptor phosphorylation
    • Bishayee S., Majumdar S., Khire J., Das M. Ligand-induced dimerization of the platelet-derived growth factor receptor. Monomer-dimer interconversion occurs independent of receptor phosphorylation. J. Biol. Chem. 264:1989;11699-11705.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11699-11705
    • Bishayee, S.1    Majumdar, S.2    Khire, J.3    Das, M.4
  • 51
    • 0024335096 scopus 로고
    • Dimerization of B-type platelet-derived growth factor receptors occurs after ligand binding and is closely associated with receptor kinase activation
    • Heldin C.-H., Ernlund A., Rorsman C., Rönnstrand L. Dimerization of B-type platelet-derived growth factor receptors occurs after ligand binding and is closely associated with receptor kinase activation. J. Biol. Chem. 264:1989;8905-8912.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8905-8912
    • Heldin, C.-H.1    Ernlund, A.2    Rorsman, C.3    Rönnstrand, L.4
  • 53
    • 0025818978 scopus 로고
    • Ligand-induced interaction between α- and β-type platelet derived growth factor (PDGF) receptors: Role of receptor heterodimers in kinase activation
    • Kanakaraj P., Raj S., Khan S.A., Bishayee S. Ligand-induced interaction between α- and β-type platelet derived growth factor (PDGF) receptors: role of receptor heterodimers in kinase activation. Biochemistry. 30:1991;1761-1767.
    • (1991) Biochemistry , vol.30 , pp. 1761-1767
    • Kanakaraj, P.1    Raj, S.2    Khan, S.A.3    Bishayee, S.4
  • 54
    • 0024426043 scopus 로고
    • Isoform-specific induction of actin reorganization by platelet-derived growth factor suggests that the functionally active receptor is a dimer
    • Hammacher A., Mellström 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. 8:1989;2489-2495.
    • (1989) EMBO J. , vol.8 , pp. 2489-2495
    • HamMacHer, A.1    Mellström, K.2    Heldin, C.-H.3    Westermark, B.4
  • 55
    • 0026095530 scopus 로고
    • Cellular response to platelet-derived growth factor (PDGF)-AB after down-regulation of PDGF α-receptors
    • Drozdoff V., Pledger W.J. Cellular response to platelet-derived growth factor (PDGF)-AB after down-regulation of PDGF α-receptors. J. Biol. Chem. 266:1991;17165-17172.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17165-17172
    • Drozdoff, V.1    Pledger, W.J.2
  • 56
    • 0027197489 scopus 로고
    • Transduction of mitogenic activity of platelet-derived growth factor (PDGF) AB by PDGF-β receptor without participation of PDGF-α receptor in vascular smooth muscle cells
    • Inui H., Kitami Y., Kondo T., Inagami T. Transduction of mitogenic activity of platelet-derived growth factor (PDGF) AB by PDGF-β receptor without participation of PDGF-α receptor in vascular smooth muscle cells. J. Biol. Chem. 268:1993;17045-17050.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17045-17050
    • Inui, H.1    Kitami, Y.2    Kondo, T.3    Inagami, T.4
  • 57
    • 0027418984 scopus 로고
    • PDGF-AB requires PDGF receptor α-subunits for high-affinity, but not for low-affinity, binding and signal transduction
    • Seifert R.A., van Koppen A., Bowen-Pope D.F. PDGF-AB requires PDGF receptor α-subunits for high-affinity, but not for low-affinity, binding and signal transduction. J. Biol. Chem. 268:1993;4473-4480.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4473-4480
    • Seifert, R.A.1    Van Koppen, A.2    Bowen-Pope, D.F.3
  • 59
    • 0242385220 scopus 로고
    • CDNA cloning and expression of the human A-type platelet-derived growth factor (PDGF) receptor establishes structural similarity to the B-type PDGF receptor
    • Claesson-Welsh L., Eriksson A., Westermark B., Heldin C.-H. cDNA cloning and expression of the human A-type platelet-derived growth factor (PDGF) receptor establishes structural similarity to the B-type PDGF receptor. Proc. Natl. Acad. Sci. USA. 86:1989;4917-4921.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4917-4921
    • Claesson-Welsh, L.1    Eriksson, A.2    Westermark, B.3    Heldin, C.-H.4
  • 61
    • 0025153862 scopus 로고
    • Chimeric α- and β-platelet-derived growth factor (PDGF) receptors define three immunoglobulin-like domains of the α-PDGF receptor that determine PDGF-AA binding specificity
    • Heidaran M.A., Pierce J.H., Jensen R.A., Matsui T., Aaronson S.A. Chimeric α- and β-platelet-derived growth factor (PDGF) receptors define three immunoglobulin-like domains of the α-PDGF receptor that determine PDGF-AA binding specificity. J. Biol. Chem. 265:1990;18741-18744.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18741-18744
    • Heidaran, M.A.1    Pierce, J.H.2    Jensen, R.A.3    Matsui, T.4    Aaronson, S.A.5
  • 62
    • 0028177593 scopus 로고
    • Structural coincidence of alphaPDGFR epitopes binding to platelet-derived growth factor-AA and a potent neutralizing monoclonal antibody
    • Yu J.C., Mahadevan D., LaRochelle W.J., Pierce J.H., Heidaran M.A. Structural coincidence of alphaPDGFR epitopes binding to platelet-derived growth factor-AA and a potent neutralizing monoclonal antibody. J. Biol. Chem. 269:1994;10668-10674.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10668-10674
    • Yu, J.C.1    Mahadevan, D.2    Larochelle, W.J.3    Pierce, J.H.4    Heidaran, M.A.5
  • 63
    • 0030782410 scopus 로고    scopus 로고
    • Crystal structure at 1.7 Å resolution of VEGF in complex with domain 2 of the Flt-1 receptor
    • Wiesmann C., Fuh G., Christinger H.W., Eigenbrot C., Wells J.A., de Vos A.M. Crystal structure at 1.7 Å resolution of VEGF in complex with domain 2 of the Flt-1 receptor. Cell. 91:1997;695-704.
    • (1997) Cell , vol.91 , pp. 695-704
    • Wiesmann, C.1    Fuh, G.2    Christinger, H.W.3    Eigenbrot, C.4    Wells, J.A.5    De Vos, A.M.6
  • 64
    • 0028790775 scopus 로고
    • Structural role of extracellular domain 1 of α-platelet-derived growth factor (PDGF) receptor for PDGF-AA and PDGF-BB binding
    • Mahadevan D., Yu J.-C., Saldanha J.W., Thanki N., McPhie P., Uren A., LaRochelle W.J., Heidaran M.A. Structural role of extracellular domain 1 of α-platelet-derived growth factor (PDGF) receptor for PDGF-AA and PDGF-BB binding. J. Biol. Chem. 270:1995;27595-27600.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27595-27600
    • Mahadevan, D.1    Yu, J.-C.2    Saldanha, J.W.3    Thanki, N.4    McPhie, P.5    Uren, A.6    Larochelle, W.J.7    Heidaran, M.A.8
  • 65
    • 0031438411 scopus 로고    scopus 로고
    • Functional importance of platelet-derived growth factor (PDGF) receptor extracellular immunoglobulin-like domains. Identification of PDGF binding site and neutralizing monoclonal antibodies
    • Lokker N.A., O'Hare J.P., Barsoumian A., Tomlinson J.E., Ramakrishnan V., Fretto L.J., Giese N.A. Functional importance of platelet-derived growth factor (PDGF) receptor extracellular immunoglobulin-like domains. Identification of PDGF binding site and neutralizing monoclonal antibodies. J. Biol. Chem. 272:1997;33037-33044.
    • (1997) J. Biol. Chem. , vol.272 , pp. 33037-33044
    • Lokker, N.A.1    O'Hare, J.P.2    Barsoumian, A.3    Tomlinson, J.E.4    Ramakrishnan, V.5    Fretto, L.J.6    Giese, N.A.7
  • 66
    • 0026646708 scopus 로고
    • A deletion in the extracellular domain of the α platelet-derived growth factor (PDGF) receptor differentially impairs PDG-AA and PDGF-BB binding affinities
    • Heidaran M.A., Yu J.-C., Jensen R.A., Pierce J.H., Aaronson S.A. A deletion in the extracellular domain of the α platelet-derived growth factor (PDGF) receptor differentially impairs PDG-AA and PDGF-BB binding affinities. J. Biol. Chem. 267:1992;2884-2887.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2884-2887
    • Heidaran, M.A.1    Yu, J.-C.2    Jensen, R.A.3    Pierce, J.H.4    Aaronson, S.A.5
  • 67
    • 0026753688 scopus 로고
    • Neomycin is a platelet-derived growth factor (PDGF) antagonist that allows discrimination of PDGF α- and β-receptor signals in cells expressing both receptor types
    • Vassbotn F.S., Östman A., Siegbahn A., Holmsen H., Heldin C.-H. Neomycin is a platelet-derived growth factor (PDGF) antagonist that allows discrimination of PDGF α- and β-receptor signals in cells expressing both receptor types. J. Biol. Chem. 267:1992;15635-15641.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15635-15641
    • Vassbotn, F.S.1    Östman, A.2    Siegbahn, A.3    Holmsen, H.4    Heldin, C.-H.5
  • 68
    • 0030977132 scopus 로고    scopus 로고
    • Immunoglobulin-like domain 4-mediated receptor-receptor interactions contribute to platelet-derived growth factor-induced receptor dimerization
    • Omura T., Heldin C.-H., Östman A. Immunoglobulin-like domain 4-mediated receptor-receptor interactions contribute to platelet-derived growth factor-induced receptor dimerization. J. Biol. Chem. 272:1997;12676-12682.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12676-12682
    • Omura, T.1    Heldin, C.-H.2    Östman, A.3
  • 69
    • 0030814101 scopus 로고    scopus 로고
    • An antibody reactive with domain 4 of the platelet-derived growth factor β receptor allows BB binding while inhibiting proliferation by impairing receptor dimerization
    • Shulman T., Sauer F.G., Jackman R.M., Chang C.N., Landolfi N.F. An antibody reactive with domain 4 of the platelet-derived growth factor β receptor allows BB binding while inhibiting proliferation by impairing receptor dimerization. J. Biol. Chem. 272:1997;17400-17404.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17400-17404
    • Shulman, T.1    Sauer, F.G.2    Jackman, R.M.3    Chang, C.N.4    Landolfi, N.F.5
  • 70
    • 0028890689 scopus 로고
    • The fourth immunoglobin domain of the stem cell factor receptor couples ligand binding to signal transduction
    • Blechman J.M., Lev S., Barg J., Eisenstein M., Vaks B., Vogel Z., Givol D., Yarden Y. The fourth immunoglobin domain of the stem cell factor receptor couples ligand binding to signal transduction. Cell. 80:1995;105-115.
    • (1995) Cell , vol.80 , pp. 105-115
    • Blechman, J.M.1    Lev, S.2    Barg, J.3    Eisenstein, M.4    Vaks, B.5    Vogel, Z.6    Givol, D.7    Yarden, Y.8
  • 72
    • 0026332810 scopus 로고
    • Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule
    • Cunningham B.C., Ultsch M., De Vos A.M., Mulkerrin M.G., Clausner K.R., Wells J.A. Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule. Science. 254:1991;821-825.
    • (1991) Science , vol.254 , pp. 821-825
    • Cunningham, B.C.1    Ultsch, M.2    De Vos, A.M.3    Mulkerrin, M.G.4    Clausner, K.R.5    Wells, J.A.6
  • 73
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • De Vos A.M., Ultsch M., Kossiakoff A.A. Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science. 255:1992;306-312.
    • (1992) Science , vol.255 , pp. 306-312
    • De Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 74
    • 0026461137 scopus 로고
    • Characterization of baculovirus-expressed human α and β platelet-derived growth factor receptors
    • Jensen R.A., Beeler J.F., Heidaran M.A., LaRochelle W.J. Characterization of baculovirus-expressed human α and β platelet-derived growth factor receptors. Biochemistry. 31:1992;10887-10892.
    • (1992) Biochemistry , vol.31 , pp. 10887-10892
    • Jensen, R.A.1    Beeler, J.F.2    Heidaran, M.A.3    Larochelle, W.J.4
  • 76
    • 0024418535 scopus 로고
    • Mutations of the platelet-derived growth factor receptor that cause a loss of ligand-induced conformational change, subtle changes in kinase activity, and impaired ability to stimulate DNA synthesis
    • Fantl W.J., Escobedo J.A., Williams L.T. Mutations of the platelet-derived growth factor receptor that cause a loss of ligand-induced conformational change, subtle changes in kinase activity, and impaired ability to stimulate DNA synthesis. Mol. Cell. Biol. 9:1989;4473-4478.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 4473-4478
    • Fantl, W.J.1    Escobedo, J.A.2    Williams, L.T.3
  • 77
    • 0024434183 scopus 로고
    • Autophosphorylation of the PDGF receptor in the kinase insert region regulates interactions with cell proteins
    • Kazlauskas A., Cooper J.A. Autophosphorylation of the PDGF receptor in the kinase insert region regulates interactions with cell proteins. Cell. 58:1989;1121-1133.
    • (1989) Cell , vol.58 , pp. 1121-1133
    • Kazlauskas, A.1    Cooper, J.A.2
  • 78
    • 0023834406 scopus 로고
    • A cascade of tyrosine autophosphorylation in the β-subunit activates the phosphotransferase of the insulin receptor
    • White M.F., Shoelson S.E., Keutmann H., Kahn C.R. A cascade of tyrosine autophosphorylation in the β-subunit activates the phosphotransferase of the insulin receptor. J. Biol. Chem. 263:1988;2969-2980.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2969-2980
    • White, M.F.1    Shoelson, S.E.2    Keutmann, H.3    Kahn, C.R.4
  • 80
    • 0030027488 scopus 로고    scopus 로고
    • Identification of six novel autophosphorylation sites on fibroblast growth factor receptor 1 and elucidation of their importance in receptor activation and signal transduction
    • Mohammadi M., Dikic I., Sorokin A., Burgess W.H., Jaye M., Schlessinger J. Identification of six novel autophosphorylation sites on fibroblast growth factor receptor 1 and elucidation of their importance in receptor activation and signal transduction. Mol. Cell. Biol. 16:1996;977-989.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 977-989
    • Mohammadi, M.1    Dikic, I.2    Sorokin, A.3    Burgess, W.H.4    Jaye, M.5    Schlessinger, J.6
  • 81
    • 0030598848 scopus 로고    scopus 로고
    • Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism
    • Mohammadi M., Schlessinger J., Hubbard S.R. Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism. Cell. 86:1996;577-587.
    • (1996) Cell , vol.86 , pp. 577-587
    • Mohammadi, M.1    Schlessinger, J.2    Hubbard, S.R.3
  • 82
    • 0028171903 scopus 로고
    • Identification of in vivo brain-derived neurotrophic factor-stimulated autophosphorylation sites on the TrkB receptor tyrosine kinase by site-directed mutagenesis
    • Guiton M., Gunn-Moore F.J., Stitt T.N., Yancopoulos G.D., Tavare J.M. Identification of in vivo brain-derived neurotrophic factor-stimulated autophosphorylation sites on the TrkB receptor tyrosine kinase by site-directed mutagenesis. J. Biol. Chem. 269:1994;30370-30377.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30370-30377
    • Guiton, M.1    Gunn-Moore, F.J.2    Stitt, T.N.3    Yancopoulos, G.D.4    Tavare, J.M.5
  • 83
    • 0028589148 scopus 로고
    • Platelet-derived growth factor receptor signals
    • Claesson-Welsh L. Platelet-derived growth factor receptor signals. J. Biol. Chem. 269:1994;32023-32026.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32023-32026
    • Claesson-Welsh, L.1
  • 84
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • Pawson T., Scott J.D. Signaling through scaffold, anchoring, and adaptor proteins. Science. 278:1997;2075-2080.
    • (1997) Science , vol.278 , pp. 2075-2080
    • Pawson, T.1    Scott, J.D.2
  • 86
    • 0029057677 scopus 로고
    • Formation of signal transfer complexes between stem cell and platelet-derived growth factor receptors and SH2 domain proteins in vitro
    • Herbst R., Shearman M.S., Jallal B., Schlessinger J., Ullrich A. Formation of signal transfer complexes between stem cell and platelet-derived growth factor receptors and SH2 domain proteins in vitro. Biochemistry. 34:1995;5971-5979.
    • (1995) Biochemistry , vol.34 , pp. 5971-5979
    • Herbst, R.1    Shearman, M.S.2    Jallal, B.3    Schlessinger, J.4    Ullrich, A.5
  • 87
    • 0030872395 scopus 로고    scopus 로고
    • Phosphotyrosine binding domain-dependent upregulation of the platelet-derived growth factor receptor α signaling cascade by transforming mutants of Cbl: Implications for Cbl's function and oncogenicity
    • Bonita D.P., Miyake S., Lupher M.L. Jr., Langdon W.Y., Band H. Phosphotyrosine binding domain-dependent upregulation of the platelet-derived growth factor receptor α signaling cascade by transforming mutants of Cbl: implications for Cbl's function and oncogenicity. Mol. Cell. Biol. 17:1997;4597-4610.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4597-4610
    • Bonita, D.P.1    Miyake, S.2    Lupher M.L., Jr.3    Langdon, W.Y.4    Band, H.5
  • 88
    • 0010523430 scopus 로고    scopus 로고
    • Multiple roles for phosphoinositide 3-kinase in signal transduction
    • in: C.-H. Heldin, M. Purton (Eds.), Chapman and Hall, London, pp.
    • G. Panayotou, Multiple roles for phosphoinositide 3-kinase in signal transduction, in: C.-H. Heldin, M. Purton (Eds.), Modular Texts in Molecular and Cell Biology: Signal Transduction, Vol. 1, Chapman and Hall, London, 1996, pp. 189-204.
    • (1996) Modular Texts in Molecular and Cell Biology: Signal Transduction , vol.1 , pp. 189-204
    • Panayotou, G.1
  • 89
    • 0024601010 scopus 로고
    • PDGF-dependent tyrosine phosphorylation stimulates production of novel polyphosphoinositides in intact cells
    • Auger K.R., Serunian L.A., Soltoff S.P., Libby P., Cantley L.C. PDGF-dependent tyrosine phosphorylation stimulates production of novel polyphosphoinositides in intact cells. Cell. 57:1989;167-175.
    • (1989) Cell , vol.57 , pp. 167-175
    • Auger, K.R.1    Serunian, L.A.2    Soltoff, S.P.3    Libby, P.4    Cantley, L.C.5
  • 90
    • 0024509946 scopus 로고
    • Role of phosphatidylinositol kinase in PDGF receptor signal transduction
    • Coughlin S.R., Escobedo J.A., Williams L.T. Role of phosphatidylinositol kinase in PDGF receptor signal transduction. Science. 243:1989;1191-1194.
    • (1989) Science , vol.243 , pp. 1191-1194
    • Coughlin, S.R.1    Escobedo, J.A.2    Williams, L.T.3
  • 91
    • 0026652899 scopus 로고
    • Distinct phosphotyrosines on a growth factor receptor bind to specific molecules that mediate different signaling pathways
    • Fantl W.J., Escobedo J.A., Martin G.A., Turck C.W., del Rosario M., McCormick F., Williams L.T. Distinct phosphotyrosines on a growth factor receptor bind to specific molecules that mediate different signaling pathways. Cell. 69:1992;413-423.
    • (1992) Cell , vol.69 , pp. 413-423
    • Fantl, W.J.1    Escobedo, J.A.2    Martin, G.A.3    Turck, C.W.4    Del Rosario, M.5    McCormick, F.6    Williams, L.T.7
  • 92
    • 0026664293 scopus 로고
    • GTPase-activating protein and phosphatidylinositol 3-kinase bind to distinct regions of the platelet-derived growth factor receptor β subunit
    • Kazlauskas A., Kashishian A., Cooper J.A., Valius M. GTPase-activating protein and phosphatidylinositol 3-kinase bind to distinct regions of the platelet-derived growth factor receptor β subunit. Mol. Cell. Biol. 12:1992;2534-2544.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2534-2544
    • Kazlauskas, A.1    Kashishian, A.2    Cooper, J.A.3    Valius, M.4
  • 93
    • 0026557517 scopus 로고
    • Phosphorylation sites in the PDGF receptor with different specificities for binding GAP and PI3 kinase in vivo
    • Kashishian A., Kazlauskas A., Cooper J.A. Phosphorylation sites in the PDGF receptor with different specificities for binding GAP and PI3 kinase in vivo. EMBO J. 11:1992;1373-1382.
    • (1992) EMBO J. , vol.11 , pp. 1373-1382
    • Kashishian, A.1    Kazlauskas, A.2    Cooper, J.A.3
  • 94
    • 0028122890 scopus 로고
    • Tyrosine 508 of the 85-kilodalton subunit of phosphatidylinositol 3-kinase is phosphorylated by the platelet-derived growth factor receptor
    • Kavanaugh W.M., Turck C.W., Klippel A., Williams L.T. Tyrosine 508 of the 85-kilodalton subunit of phosphatidylinositol 3-kinase is phosphorylated by the platelet-derived growth factor receptor. Biochemistry. 33:1994;11046-11050.
    • (1994) Biochemistry , vol.33 , pp. 11046-11050
    • Kavanaugh, W.M.1    Turck, C.W.2    Klippel, A.3    Williams, L.T.4
  • 95
    • 0026487847 scopus 로고
    • Interaction of the p85 subunit of PI 3-kinase and its N-terminal SH2 domain with a PDGF receptor phosphorylation site: Structural features and analysis of conformational changes
    • Panayotou G., Bax B., Gout I., Federwisch M., Wroblowski B., Dhand R., Fry M.J., Blundell T.L., Wollmer A., Waterfield M.D. Interaction of the p85 subunit of PI 3-kinase and its N-terminal SH2 domain with a PDGF receptor phosphorylation site: structural features and analysis of conformational changes. EMBO J. 11:1992;4261-4272.
    • (1992) EMBO J. , vol.11 , pp. 4261-4272
    • Panayotou, G.1    Bax, B.2    Gout, I.3    Federwisch, M.4    Wroblowski, B.5    Dhand, R.6    Fry, M.J.7    Blundell, T.L.8    Wollmer, A.9    Waterfield, M.D.10
  • 97
    • 0029855012 scopus 로고    scopus 로고
    • D-3 phosphoinositide metabolism in cells treated with platelet-derived growth factor
    • Whiteford C.C., Best C., Kazlauskas A., Ulug E.T. D-3 phosphoinositide metabolism in cells treated with platelet-derived growth factor. Biochem. J. 319:1996;851-860.
    • (1996) Biochem. J. , vol.319 , pp. 851-860
    • Whiteford, C.C.1    Best, C.2    Kazlauskas, A.3    Ulug, E.T.4
  • 98
    • 0029160069 scopus 로고
    • Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction
    • Burgering B.M.T., Coffer P.J. Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction. Nature. 376:1995;599-602.
    • (1995) Nature , vol.376 , pp. 599-602
    • Burgering, B.M.T.1    Coffer, P.J.2
  • 99
    • 0029079275 scopus 로고
    • The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase
    • Franke T.F., Yang S.-I., Chan T.O., Datta K., Kazlauskas A., Morrison D.K., Kaplan D.R., Tsichlis P.N. The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase. Cell. 81:1995;727-736.
    • (1995) Cell , vol.81 , pp. 727-736
    • Franke, T.F.1    Yang, S.-I.2    Chan, T.O.3    Datta, K.4    Kazlauskas, A.5    Morrison, D.K.6    Kaplan, D.R.7    Tsichlis, P.N.8
  • 100
    • 0031015986 scopus 로고    scopus 로고
    • A specific product of phosphatidylinositol 3-kinase directly activates the protein kinase Akt through its pleckstrin homology domain
    • Klippel A., Kavanaugh W.M., Pot D., Williams L.T. A specific product of phosphatidylinositol 3-kinase directly activates the protein kinase Akt through its pleckstrin homology domain. Mol. Cell. Biol. 17:1997;338-344.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 338-344
    • Klippel, A.1    Kavanaugh, W.M.2    Pot, D.3    Williams, L.T.4
  • 101
    • 9044253707 scopus 로고    scopus 로고
    • Platelet-derived growth factor activates protein kinase Cε through redundant and independent signaling pathways involving phospholipase Cγ or phosphatidylinositol 3-kinase
    • Moriya S., Kazlauskas A., Akimoto K., Hirai S.-i., Mizuno K., Takenawa T., Fukui Y., Watanabe Y., Ozaki S., Ohno S. Platelet-derived growth factor activates protein kinase Cε through redundant and independent signaling pathways involving phospholipase Cγ or phosphatidylinositol 3-kinase. Proc. Natl. Acad. Sci. USA. 93:1996;151-155.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 151-155
    • Moriya, S.1    Kazlauskas, A.2    Akimoto, K.3    Hirai, S.-i.4    Mizuno, K.5    Takenawa, T.6    Fukui, Y.7    Watanabe, Y.8    Ozaki, S.9    Ohno, S.10
  • 102
    • 0027535742 scopus 로고
    • Activation of the ζ isozyme of protein kinase C by phosphatidylinositol 3,4,5-trisphosphate
    • Nakanishi H., Brewer K.A., Exton J.H. Activation of the ζ isozyme of protein kinase C by phosphatidylinositol 3,4,5-trisphosphate. J. Biol. Chem. 268:1993;13-16.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13-16
    • Nakanishi, H.1    Brewer, K.A.2    Exton, J.H.3
  • 105
    • 0028308412 scopus 로고
    • Phosphatidylinositol 3-kinase activation is required for insulin stimulation of pp70 S6 kinase, DNA synthesis, and glucose transporter translocation
    • Cheatham B., Vlahos C.J., Cheatham L., Wang L., Blenis J., Kahn C.R. Phosphatidylinositol 3-kinase activation is required for insulin stimulation of pp70 S6 kinase, DNA synthesis, and glucose transporter translocation. Mol. Cell. Biol. 14:1994;4902-4911.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 4902-4911
    • Cheatham, B.1    Vlahos, C.J.2    Cheatham, L.3    Wang, L.4    Blenis, J.5    Kahn, C.R.6
  • 110
    • 0031039024 scopus 로고    scopus 로고
    • Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate
    • Franke T.F., Kaplan D.R., Cantley L.C., Toker A. Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate. Science. 275:1997;665-668.
    • (1997) Science , vol.275 , pp. 665-668
    • Franke, T.F.1    Kaplan, D.R.2    Cantley, L.C.3    Toker, A.4
  • 111
    • 0028819535 scopus 로고
    • Platelet-derived growth factor triggers translocation of the insulin-regulatable glucose transporter (type 4) predominantly through phosphatidylinositol 3-kinase binding sites on the receptor
    • Kamohara S., Hayashi H., Todaka M., Kanai F., Ishii K., Imanaka T., Escobedo J.A., Williams L.T., Ebina Y. Platelet-derived growth factor triggers translocation of the insulin-regulatable glucose transporter (type 4) predominantly through phosphatidylinositol 3-kinase binding sites on the receptor. Proc. Natl. Acad. Sci. USA. 92:1995;1077-1081.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1077-1081
    • Kamohara, S.1    Hayashi, H.2    Todaka, M.3    Kanai, F.4    Ishii, K.5    Imanaka, T.6    Escobedo, J.A.7    Williams, L.T.8    Ebina, Y.9
  • 112
    • 0027397544 scopus 로고
    • Inositol trisphosphate and calcium signalling
    • Berridge M.J. Inositol trisphosphate and calcium signalling. Nature. 361:1993;315-325.
    • (1993) Nature , vol.361 , pp. 315-325
    • Berridge, M.J.1
  • 113
    • 0030612481 scopus 로고    scopus 로고
    • Phospholipase C-γ1: Regulation of enzyme function and role in growth factor-dependent signal transduction
    • Kamat A., Carpenter G. Phospholipase C-γ1: Regulation of enzyme function and role in growth factor-dependent signal transduction. Cytokine Growth Factor Rev. 8:1997;109-117.
    • (1997) Cytokine Growth Factor Rev. , vol.8 , pp. 109-117
    • Kamat, A.1    Carpenter, G.2
  • 116
    • 0026674977 scopus 로고
    • Identification of two C-terminal autophosphorylation sites in the PDGF β-receptor: Involvement in the interaction with phospholipase C-γ
    • Rönnstrand L., Mori S., Arvidsson A.-K., Eriksson A., Wernstedt C., Hellman U., Claesson-Welsh L., Heldin C.-H. Identification of two C-terminal autophosphorylation sites in the PDGF β-receptor: involvement in the interaction with phospholipase C-γ EMBO J. 11:1992;3911-3919.
    • (1992) EMBO J. , vol.11 , pp. 3911-3919
    • Rönnstrand, L.1    Mori, S.2    Arvidsson, A.-K.3    Eriksson, A.4    Wernstedt, C.5    Hellman, U.6    Claesson-Welsh, L.7    Heldin, C.-H.8
  • 117
    • 0027523306 scopus 로고
    • Phosphorylation sites at the C-terminus of the platelet-derived growth factor receptor bind phospholipase Cγ1
    • Kashishian A., Cooper J.A. Phosphorylation sites at the C-terminus of the platelet-derived growth factor receptor bind phospholipase Cγ1. Mol. Biol. Cell. 4:1993;49-57.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 49-57
    • Kashishian, A.1    Cooper, J.A.2
  • 118
    • 0027506762 scopus 로고
    • Tyrosines 1021 and 1009 are phosphorylation sites in the carboxy terminus of the platelet-derived growth factor receptor β subunit and are required for binding of phospholipase Cγ and a 64-kilodalton protein, respectively
    • Valius M., Bazenet C., Kazlauskas A. Tyrosines 1021 and 1009 are phosphorylation sites in the carboxy terminus of the platelet-derived growth factor receptor β subunit and are required for binding of phospholipase Cγ and a 64-kilodalton protein, respectively. Mol. Cell. Biol. 13:1993;133-143.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 133-143
    • Valius, M.1    Bazenet, C.2    Kazlauskas, A.3
  • 120
    • 0025844951 scopus 로고
    • Phospholipase Cg complexes with ligand-activated platelet-derived growth factor (PDGF) receptors
    • Kumjian D.A., Barnstein A., Rhee S.G., Daniel T.O. Phospholipase Cg complexes with ligand-activated platelet-derived growth factor (PDGF) receptors. J. Biol. Chem. 266:1991;3973-3980.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3973-3980
    • Kumjian, D.A.1    Barnstein, A.2    Rhee, S.G.3    Daniel, T.O.4
  • 121
    • 0025341875 scopus 로고
    • Platelet-derived growth factor (PDGF)-dependent association of phospholipase C-γ with the PDGF receptor signaling complex
    • Morrison D.K., Kaplan D.R., Rhee S.G., Williams L.T. Platelet-derived growth factor (PDGF)-dependent association of phospholipase C-γ with the PDGF receptor signaling complex. Mol. Cell. Biol. 10:1990;2359-2366.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 2359-2366
    • Morrison, D.K.1    Kaplan, D.R.2    Rhee, S.G.3    Williams, L.T.4
  • 122
    • 0024380391 scopus 로고
    • Phospholipase C-γ is a substrate for the PDGF and EGF receptor protein tyrosine kinases in vivo and in vitro
    • 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. 57:1989;1109-1122.
    • (1989) Cell , vol.57 , pp. 1109-1122
    • Meisenhelder, J.1    Suh, P.-G.2    Rhee, S.G.3    Hunter, T.4
  • 123
    • 0024400973 scopus 로고
    • Platelet-derived growth factor induces rapid and sustained tyrosine phosphorylation of phospholipase C-γ in quiescent BALB/c 3T3 cells
    • Wahl M.I., Olashaw N.E., Nishibe S., Rhee S.G., Pledger W.J., Carpenter G. Platelet-derived growth factor induces rapid and sustained tyrosine phosphorylation of phospholipase C-γ in quiescent BALB/c 3T3 cells. Mol. Cell. Biol. 9:1989;2934-2943.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 2934-2943
    • Wahl, M.I.1    Olashaw, N.E.2    Nishibe, S.3    Rhee, S.G.4    Pledger, W.J.5    Carpenter, G.6
  • 126
    • 0025247881 scopus 로고
    • Tyrosine residues in bovine phospholipase C-γ phosphorylated by the epidermal growth factor receptor in vitro
    • Kim J.W., Sim S.S., Kim U.-H., Nishibe S., Wahl M.I., Carpenter G., Rhee S.G. Tyrosine residues in bovine phospholipase C-γ phosphorylated by the epidermal growth factor receptor in vitro. J. Biol. Chem. 265:1990;3940-3943.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3940-3943
    • Kim, J.W.1    Sim, S.S.2    Kim, U.-H.3    Nishibe, S.4    Wahl, M.I.5    Carpenter, G.6    Rhee, S.G.7
  • 127
    • 0031011362 scopus 로고    scopus 로고
    • Dissociation of tyrosine phosphorylation and activation of phosphoinositide phospholipase C induced by the protein kinase C inhibitor Ro-31-8220 in Swiss 3T3 cells treated with platelet-derived growth factor
    • Yeo E.-J., Provost J.J., Exton J.H. Dissociation of tyrosine phosphorylation and activation of phosphoinositide phospholipase C induced by the protein kinase C inhibitor Ro-31-8220 in Swiss 3T3 cells treated with platelet-derived growth factor. Biochim. Biophys. Acta. 1356:1997;308-320.
    • (1997) Biochim. Biophys. Acta , vol.1356 , pp. 308-320
    • Yeo, E.-J.1    Provost, J.J.2    Exton, J.H.3
  • 128
    • 0032518666 scopus 로고    scopus 로고
    • Activation of phospholipase Cγ by PI3-kinase-induced PH domain-mediated membrane targeting
    • Falasca M., Logan S.K., Lehto V.P., Baccante G., Lemmon M.A., Schlessinger J. Activation of phospholipase Cγ by PI3-kinase-induced PH domain-mediated membrane targeting. EMBO J. 17:1998;414-422.
    • (1998) EMBO J. , vol.17 , pp. 414-422
    • Falasca, M.1    Logan, S.K.2    Lehto, V.P.3    Baccante, G.4    Lemmon, M.A.5    Schlessinger, J.6
  • 129
    • 0028034025 scopus 로고
    • Activation of phospholipase D induced by platelet-derived growth factor is dependent upon the level of phospholipase C-gamma1
    • Lee Y.H., Kim H.S., Pai J.K., Ryu S.H., Suh P.G. Activation of phospholipase D induced by platelet-derived growth factor is dependent upon the level of phospholipase C-gamma1. J. Biol. Chem. 269:1994;26842-26847.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26842-26847
    • Lee, Y.H.1    Kim, H.S.2    Pai, J.K.3    Ryu, S.H.4    Suh, P.G.5
  • 130
    • 0028171403 scopus 로고
    • Activation of phospholipase C-γ is necessary for stimulation of phospholipase D by platelet-derived growth factor
    • Yeo E.J., Kazlauskas A., Exton J.H. Activation of phospholipase C-γ is necessary for stimulation of phospholipase D by platelet-derived growth factor. J. Biol. Chem. 269:1994;27823-27826.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27823-27826
    • Yeo, E.J.1    Kazlauskas, A.2    Exton, J.H.3
  • 131
    • 0027495890 scopus 로고
    • The regulation of phospholipase C-γ 1 by phosphatidic acid
    • Jones G.A., Carpenter G. The regulation of phospholipase C-γ 1 by phosphatidic acid. J. Biol. Chem. 268:1993;20845-20850.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20845-20850
    • Jones, G.A.1    Carpenter, G.2
  • 132
    • 0026725673 scopus 로고
    • Phosphatidic acid that accumulates in platelet-derived growth factor-stimulated Balb/c 3T3 cells is a potential mitogenic signal
    • Fukami K., Takenawa T. Phosphatidic acid that accumulates in platelet-derived growth factor-stimulated Balb/c 3T3 cells is a potential mitogenic signal. J. Biol. Chem. 267:1992;10988-10993.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10988-10993
    • Fukami, K.1    Takenawa, T.2
  • 133
    • 0026015161 scopus 로고
    • Multiple sources of sn-1,2-diacylglycerol in platelet-derived-growth-factor-stimulated Swiss 3T3 fibroblasts. Evidence for activation of phosphoinositidase C and phosphatidyl-choline-specific phospholipase D
    • Plevin R., Cook S.J., Palmer S., Wakelam M.J. Multiple sources of sn-1,2-diacylglycerol in platelet-derived-growth-factor-stimulated Swiss 3T3 fibroblasts. Evidence for activation of phosphoinositidase C and phosphatidyl-choline-specific phospholipase D. Biochem. J. 279:1991;559-565.
    • (1991) Biochem. J. , vol.279 , pp. 559-565
    • Plevin, R.1    Cook, S.J.2    Palmer, S.3    Wakelam, M.J.4
  • 134
    • 0024841874 scopus 로고
    • Phospholipase D activation by the mitogens platelet-derived growth factor and 12-O-tetradecanoylphorbol 13-acetate in NIH-3T3 cells
    • Ben-Av P., Liscovitch M. Phospholipase D activation by the mitogens platelet-derived growth factor and 12-O-tetradecanoylphorbol 13-acetate in NIH-3T3 cells. FEBS Lett. 259:1989;64-66.
    • (1989) FEBS Lett. , vol.259 , pp. 64-66
    • Ben-Av, P.1    Liscovitch, M.2
  • 135
    • 0027368546 scopus 로고
    • V-Src activates a unique phospholipase D activity that can be distinguished from the phospholipase D activity activated by phorbol esters
    • Song J., Foster D.A. v-Src activates a unique phospholipase D activity that can be distinguished from the phospholipase D activity activated by phorbol esters. Biochem. J. 294:1993;711-717.
    • (1993) Biochem. J. , vol.294 , pp. 711-717
    • Song, J.1    Foster, D.A.2
  • 137
    • 0027279176 scopus 로고
    • How receptor tyrosine kinases activate Ras
    • Schlessinger J. How receptor tyrosine kinases activate Ras. Trends Biol. Sci. 18:1993;273-275.
    • (1993) Trends Biol. Sci. , vol.18 , pp. 273-275
    • Schlessinger, J.1
  • 138
    • 0027263326 scopus 로고
    • Platelet-derived growth factor receptor mediates activation of Ras through different signaling pathways in different cell types
    • Satoh T., Fantl W.J., Escobedo J.A., Williams L.T., Kaziro Y. Platelet-derived growth factor receptor mediates activation of Ras through different signaling pathways in different cell types. Mol. Cell. Biol. 13:1993;3706-3713.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 3706-3713
    • Satoh, T.1    Fantl, W.J.2    Escobedo, J.A.3    Williams, L.T.4    Kaziro, Y.5
  • 139
    • 0027219341 scopus 로고
    • Platelet-derived growth factor increases the turnover of GTP/GDP on Ras in permeabilized fibroblasts
    • Nånberg E., Westermark B. Platelet-derived growth factor increases the turnover of GTP/GDP on Ras in permeabilized fibroblasts. J. Biol. Chem. 268:1993;18187-18194.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18187-18194
    • Nånberg, E.1    Westermark, B.2
  • 141
    • 0031975810 scopus 로고    scopus 로고
    • Platelet-derived growth factor (PDGF)-induced actin rearrangement is deregulated in cells expressing a mutant Y778F PDGF β-receptor
    • Ruusala A., Sundberg C., Arvidsson A.-K., Rupp-Thuresson E., Heldin C.-H., Claesson-Welsh L. Platelet-derived growth factor (PDGF)-induced actin rearrangement is deregulated in cells expressing a mutant Y778F PDGF β-receptor. J. Cell Sci. 111:1998;111-120.
    • (1998) J. Cell Sci. , vol.111 , pp. 111-120
    • Ruusala, A.1    Sundberg, C.2    Arvidsson, A.-K.3    Rupp-Thuresson, E.4    Heldin, C.-H.5    Claesson-Welsh, L.6
  • 142
    • 0028080912 scopus 로고
    • Platelet-derived growth factor stimulates growth factor receptor binding protein-2 association with Shc in vascular smooth muscle cells
    • Benjamin C.W., Jones D.A. Platelet-derived growth factor stimulates growth factor receptor binding protein-2 association with Shc in vascular smooth muscle cells. J. Biol. Chem. 269:1994;30911-30916.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30911-30916
    • Benjamin, C.W.1    Jones, D.A.2
  • 145
    • 0028958025 scopus 로고
    • Src family protein tyrosine kinases and cellular signal transduction pathways
    • Erpel T., Courtneidge S.A. Src family protein tyrosine kinases and cellular signal transduction pathways. Curr. Opin. Cell Biol. 7:1995;176-182.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 176-182
    • Erpel, T.1    Courtneidge, S.A.2
  • 146
    • 0025172811 scopus 로고
    • Association between the PDGF receptor and members of the src family of tyrosine kinases
    • Kypta R.M., Goldberg Y., Ulug E.T., Courtneidge S.A. Association between the PDGF receptor and members of the src family of tyrosine kinases. Cell. 62:1990;481-492.
    • (1990) Cell , vol.62 , pp. 481-492
    • Kypta, R.M.1    Goldberg, Y.2    Ulug, E.T.3    Courtneidge, S.A.4
  • 147
    • 0027251468 scopus 로고
    • Identification of two juxtamembrane autophosphorylation sites in the PDGF β-receptor; Involvement in the interaction with Src family tyrosine kinases
    • Mori S., Rönnstrand L., Yokote K., Engström Å., Courtneidge S.A., Claesson-Welsh L., Heldin C.-H. Identification of two juxtamembrane autophosphorylation sites in the PDGF β-receptor; involvement in the interaction with Src family tyrosine kinases. EMBO J. 12:1993;2257-2264.
    • (1993) EMBO J. , vol.12 , pp. 2257-2264
    • Mori, S.1    Rönnstrand, L.2    Yokote, K.3    Engström, Å.4    Courtneidge, S.A.5    Claesson-Welsh, L.6    Heldin, C.-H.7
  • 148
    • 0032489518 scopus 로고    scopus 로고
    • A role for Src in signal relay by the platelet-derived growth factor α receptor
    • Gelderloos J.A., Rosenkranz S., Bazenet C., Kazlauskas A. A role for Src in signal relay by the platelet-derived growth factor α receptor. J. Biol. Chem. 273:1998;5908-5915.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5908-5915
    • Gelderloos, J.A.1    Rosenkranz, S.2    Bazenet, C.3    Kazlauskas, A.4
  • 149
    • 0031890724 scopus 로고    scopus 로고
    • PDGF α-receptor mediated cellular responses are not dependent on Src family kinases in endothelial cells
    • Hooshmand-Rad R., Yokote K., Heldin C.-H., Claesson-Welsh L. PDGF α-receptor mediated cellular responses are not dependent on Src family kinases in endothelial cells. J. Cell Sci. 111:1998;607-614.
    • (1998) J. Cell Sci. , vol.111 , pp. 607-614
    • Hooshmand-Rad, R.1    Yokote, K.2    Heldin, C.-H.3    Claesson-Welsh, L.4
  • 150
    • 0028898383 scopus 로고
    • Sequence requirements for binding of Src family tyrosine kinases to activated growth factor receptors
    • Alonso G., Koegl M., Mazurenko N., Courtneidge S.A. Sequence requirements for binding of Src family tyrosine kinases to activated growth factor receptors. J. Biol. Chem. 270:1995;9840-9848.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9840-9848
    • Alonso, G.1    Koegl, M.2    Mazurenko, N.3    Courtneidge, S.A.4
  • 151
    • 15844365555 scopus 로고    scopus 로고
    • Modulation of the SH2 binding specificity and kinase activity of Src by tyrosine phosphorylation within its SH2 domain
    • Stover D.R., Furet P., Lydon N.B. Modulation of the SH2 binding specificity and kinase activity of Src by tyrosine phosphorylation within its SH2 domain. J. Biol. Chem. 271:1996;12481-12487.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12481-12487
    • Stover, D.R.1    Furet, P.2    Lydon, N.B.3
  • 152
    • 0031025999 scopus 로고    scopus 로고
    • The PDGF receptor phosphorylates Tyr 138 in the c-Src SH3 domain in vivo reducing peptide ligand binding
    • Broome M.A., Hunter T. The PDGF receptor phosphorylates Tyr 138 in the c-Src SH3 domain in vivo reducing peptide ligand binding. Oncogene. 14:1997;17-34.
    • (1997) Oncogene , vol.14 , pp. 17-34
    • Broome, M.A.1    Hunter, T.2
  • 154
    • 0028879873 scopus 로고
    • Myc but not Fos rescue of PDGF signalling block caused by kinase-inactive Src
    • Barone M.V., Courtneidge S.A. Myc but not Fos rescue of PDGF signalling block caused by kinase-inactive Src. Nature. 378:1995;509-512.
    • (1995) Nature , vol.378 , pp. 509-512
    • Barone, M.V.1    Courtneidge, S.A.2
  • 155
    • 0027172209 scopus 로고
    • The Src family tyrosine kinases are required for platelet-derived growth factor-mediated signal transduction in NIH 3T3 cells
    • Twamley-Stein G.M., Pepperkok R., Ansorge W., Courtneidge S.A. The Src family tyrosine kinases are required for platelet-derived growth factor-mediated signal transduction in NIH 3T3 cells. Proc. Natl. Acad. Sci. USA. 90:1993;7696-7700.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7696-7700
    • Twamley-Stein, G.M.1    Pepperkok, R.2    Ansorge, W.3    Courtneidge, S.A.4
  • 156
    • 0029003669 scopus 로고
    • The cytoplasmic tyrosine kinase FER is associated with the catenin-like substrate pp120 and is activated by growth factors
    • Kim L., Wong T.W. The cytoplasmic tyrosine kinase FER is associated with the catenin-like substrate pp120 and is activated by growth factors. Mol. Cell. Biol. 15:1995;4553-4561.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4553-4561
    • Kim, L.1    Wong, T.W.2
  • 157
    • 0030840464 scopus 로고    scopus 로고
    • STATs and gene regulation
    • Darnell J.E. Jr. STATs and gene regulation. Science. 277:1997;1630-1635.
    • (1997) Science , vol.277 , pp. 1630-1635
    • Darnell J.E., Jr.1
  • 158
    • 0030042198 scopus 로고    scopus 로고
    • PDGF receptor-to-nucleus signaling of p91 (STAT1α) transcription factor in rat smooth muscle cells
    • Yamamoto H., Crow M., Cheng L., Lakatta E., Kinsella J. PDGF receptor-to-nucleus signaling of p91 (STAT1α) transcription factor in rat smooth muscle cells. Exp. Cell Res. 222:1996;125-130.
    • (1996) Exp. Cell Res. , vol.222 , pp. 125-130
    • Yamamoto, H.1    Crow, M.2    Cheng, L.3    Lakatta, E.4    Kinsella, J.5
  • 159
    • 0030053935 scopus 로고    scopus 로고
    • PDGF stimulates tyrosine phosphorylation of JAK 1 protein tyrosine kinase in human mesangial cells
    • Choudhury G.G., Marra F., Kiyomoto H., Abboud H.E. PDGF stimulates tyrosine phosphorylation of JAK 1 protein tyrosine kinase in human mesangial cells. Kidney Int. 49:1996;19-25.
    • (1996) Kidney Int. , vol.49 , pp. 19-25
    • Choudhury, G.G.1    Marra, F.2    Kiyomoto, H.3    Abboud, H.E.4
  • 160
    • 0029966664 scopus 로고    scopus 로고
    • Platelet-derived growth factor induces phosphorylation of multiple JAK family kinases and STAT proteins
    • Vignais M.-L., Sadowski H.B., Watling D., Rogers N.C., Gilman M. Platelet-derived growth factor induces phosphorylation of multiple JAK family kinases and STAT proteins. Mol. Cell. Biol. 16:1996;1759-1769.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1759-1769
    • Vignais, M.-L.1    Sadowski, H.B.2    Watling, D.3    Rogers, N.C.4    Gilman, M.5
  • 161
    • 0032576873 scopus 로고    scopus 로고
    • Activation of Stat5 by platelet-derived growth factor (PDGF) is dependent on phosphorylation sites in PDGF β-receptor juxtamembrane and kinase insert domains
    • Valgeirsdóttir S., Paukku K., Silvennoinen O., Heldin C.-H., Claesson-Welsh L. Activation of Stat5 by platelet-derived growth factor (PDGF) is dependent on phosphorylation sites in PDGF β-receptor juxtamembrane and kinase insert domains. Oncogene. 16:1998;505-515.
    • (1998) Oncogene , vol.16 , pp. 505-515
    • Valgeirsdóttir, S.1    Paukku, K.2    Silvennoinen, O.3    Heldin, C.-H.4    Claesson-Welsh, L.5
  • 162
    • 0029763756 scopus 로고    scopus 로고
    • Formation of STAT5-containing DNA binding complexes in response to colony-stimulating factor-1 and platelet-derived growth factor
    • Novak U., Mui A., Miyajima A., Paradiso L. Formation of STAT5-containing DNA binding complexes in response to colony-stimulating factor-1 and platelet-derived growth factor. J. Biol. Chem. 271:1996;18350-18354.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18350-18354
    • Novak, U.1    Mui, A.2    Miyajima, A.3    Paradiso, L.4
  • 164
    • 0027432407 scopus 로고
    • Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor β
    • Lechleider R.J., Sugimoto S., Bennett A.M., Kashishian A.S., Cooper J.A., Shoelson S.E., Walsh C.T., Neel B.G. Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor β J. Biol. Chem. 268:1993;21478-21481.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21478-21481
    • Lechleider, R.J.1    Sugimoto, S.2    Bennett, A.M.3    Kashishian, A.S.4    Cooper, J.A.5    Shoelson, S.E.6    Walsh, C.T.7    Neel, B.G.8
  • 165
    • 0027179869 scopus 로고
    • The 64-kDa protein that associates with the platelet-derived growth factor receptor β subunit via Tyr-1009 is the SH2-containing phosphotyrosine phosphatase Syp
    • Kazlauskas A., Feng G.-S., Pawson T., Valius M. The 64-kDa protein that associates with the platelet-derived growth factor receptor β subunit via Tyr-1009 is the SH2-containing phosphotyrosine phosphatase Syp. Proc. Natl. Acad. Sci. USA. 90:1993;6939-6943.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6939-6943
    • Kazlauskas, A.1    Feng, G.-S.2    Pawson, T.3    Valius, M.4
  • 166
    • 0029860951 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine 720 in the platelet-derived growth factor α receptor is required for binding of Grb2 and SHP-2 but not for activation of Ras or cell proliferation
    • Bazenet C.E., Gelderloos J.A., Kazlauskas A. Phosphorylation of tyrosine 720 in the platelet-derived growth factor α receptor is required for binding of Grb2 and SHP-2 but not for activation of Ras or cell proliferation. Mol. Cell. Biol. 16:1996;6926-6936.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6926-6936
    • Bazenet, C.E.1    Gelderloos, J.A.2    Kazlauskas, A.3
  • 167
    • 0028854920 scopus 로고
    • Potent stimulation of SH-PTP2 phosphatase activity by simultaneous occupancy of both SH2 domains
    • Pluskey S., Wandless T.J., Walsh C.T., Shoelson S.E. Potent stimulation of SH-PTP2 phosphatase activity by simultaneous occupancy of both SH2 domains. J. Biol. Chem. 270:1995;2897-2900.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2897-2900
    • Pluskey, S.1    Wandless, T.J.2    Walsh, C.T.3    Shoelson, S.E.4
  • 168
    • 0028179013 scopus 로고
    • Protein-tyrosine-phosphatase SHPTP2 couples platelet-derived growth factor receptor β to Ras
    • Bennett A.M., Tang T.L., Sugimoto S., Walsh C.T., Neel B.G. Protein-tyrosine-phosphatase SHPTP2 couples platelet-derived growth factor receptor β to Ras. Proc. Natl. Acad. Sci. USA. 91:1994;7335-7339.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7335-7339
    • Bennett, A.M.1    Tang, T.L.2    Sugimoto, S.3    Walsh, C.T.4    Neel, B.G.5
  • 169
    • 0029844431 scopus 로고    scopus 로고
    • Multiple in vivo phosphorylated tyrosine phosphatase SHP-2 engages binding to Grb2 via tyrosine 584
    • Vogel W., Ullrich A. Multiple in vivo phosphorylated tyrosine phosphatase SHP-2 engages binding to Grb2 via tyrosine 584. Cell Growth Differ. 7:1996;1589-1597.
    • (1996) Cell Growth Differ. , vol.7 , pp. 1589-1597
    • Vogel, W.1    Ullrich, A.2
  • 170
    • 0029085194 scopus 로고
    • Identification of a putative Syp substrate, the PDGFβ receptor
    • Klinghoffer R.A., Kazlauskas A. Identification of a putative Syp substrate, the PDGFβ receptor. J. Biol. Chem. 270:1995;22208-22217.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22208-22217
    • Klinghoffer, R.A.1    Kazlauskas, A.2
  • 171
    • 0029923179 scopus 로고    scopus 로고
    • Localization and down-regulating role of the protein tyrosine phosphatase PTP2C in membrane ruffles of PDGF-stimulated cells
    • Cossette L.J., Hoglinger O., Mou L., Shen S.-H. Localization and down-regulating role of the protein tyrosine phosphatase PTP2C in membrane ruffles of PDGF-stimulated cells. Exp. Cell Res. 223:1996;459-466.
    • (1996) Exp. Cell Res. , vol.223 , pp. 459-466
    • Cossette, L.J.1    Hoglinger, O.2    Mou, L.3    Shen, S.-H.4
  • 172
    • 0032570586 scopus 로고    scopus 로고
    • 2-terminal mitogen-activated protein kinases
    • 2-terminal mitogen-activated protein kinases. J. Biol. Chem. 273:1998;4904-4908.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4904-4908
    • Shi, Z.-Q.1    Lu, W.2    Feng, G.-S.3
  • 173
    • 0028933979 scopus 로고
    • The phosphotyrosine phosphatase PTP1D, but not PTP1C, is an essential mediator of fibroblast proliferation induced by tyrosine kinase and G protein-coupled receptors
    • Rivard N., McKenzie F.R., Brondello J.-M., Pouysségur J. The phosphotyrosine phosphatase PTP1D, but not PTP1C, is an essential mediator of fibroblast proliferation induced by tyrosine kinase and G protein-coupled receptors. J. Biol. Chem. 270:1995;11017-11024.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11017-11024
    • Rivard, N.1    McKenzie, F.R.2    Brondello, J.-M.3    Pouysségur, J.4
  • 174
    • 0028837693 scopus 로고
    • Regulation of the Src tyrosine kinase and Syp tyrosine phosphatase by their cellular association
    • Peng Z.-Y., Cartwright C.A. Regulation of the Src tyrosine kinase and Syp tyrosine phosphatase by their cellular association. Oncogene. 11:1995;1955-1962.
    • (1995) Oncogene , vol.11 , pp. 1955-1962
    • Peng, Z.-Y.1    Cartwright, C.A.2
  • 176
    • 0030919893 scopus 로고    scopus 로고
    • Activation of c-Raf-1 by Ras and Src through different mechanisms: Activation in vivo and in vitro
    • Stokoe D., McCormick F. Activation of c-Raf-1 by Ras and Src through different mechanisms: activation in vivo and in vitro. EMBO J. 16:1997;2384-2396.
    • (1997) EMBO J. , vol.16 , pp. 2384-2396
    • Stokoe, D.1    McCormick, F.2
  • 177
    • 0029006126 scopus 로고
    • Ras recruits Raf-1 to the plasma membrane for activation by tyrosine phosphorylation
    • Marais R., Light Y., Paterson H.F., Marshall C.J. Ras recruits Raf-1 to the plasma membrane for activation by tyrosine phosphorylation. EMBO J. 14:1995;3136-3145.
    • (1995) EMBO J. , vol.14 , pp. 3136-3145
    • Marais, R.1    Light, Y.2    Paterson, H.F.3    Marshall, C.J.4
  • 178
    • 0031041171 scopus 로고    scopus 로고
    • Differential regulation of Raf-1, A-Raf, and B-Raf by oncogenic Ras and tyrosine kinases
    • Marais R., Light Y., Paterson H.F., Mason C.S., Marshall C.J. Differential regulation of Raf-1, A-Raf, and B-Raf by oncogenic Ras and tyrosine kinases. J. Biol. Chem. 272:1997;4378-4383.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4378-4383
    • Marais, R.1    Light, Y.2    Paterson, H.F.3    Mason, C.S.4    Marshall, C.J.5
  • 179
    • 0028079681 scopus 로고
    • The PDGF receptor alpha subunit activates p21ras and triggers DNA synthesis without interacting with rasGAP
    • Bazenet C.E., Kazlauskas A. The PDGF receptor alpha subunit activates p21ras and triggers DNA synthesis without interacting with rasGAP. Oncogene. 9:1994;517-525.
    • (1994) Oncogene , vol.9 , pp. 517-525
    • Bazenet, C.E.1    Kazlauskas, A.2
  • 181
    • 0030899808 scopus 로고    scopus 로고
    • Aberrant Ras regulation and reduced p190 tyrosine phosphorylation in cells lacking p120-Gap
    • van der Geer P., Henkemeyer M., Jacks T., Pawson T. Aberrant Ras regulation and reduced p190 tyrosine phosphorylation in cells lacking p120-Gap. Mol. Cell. Biol. 17:1997;1840-1847.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1840-1847
    • Van Der Geer, P.1    Henkemeyer, M.2    Jacks, T.3    Pawson, T.4
  • 182
    • 0028989013 scopus 로고
    • The GTPase-activating protein of Ras suppresses platelet-derived growth factor β receptor signaling by silencing phospholipase C-γ1
    • Valius M., Secrist J.P., Kazlauskas A. The GTPase-activating protein of Ras suppresses platelet-derived growth factor β receptor signaling by silencing phospholipase C-γ1. Mol. Cell. Biol. 15:1995;3058-3071.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3058-3071
    • Valius, M.1    Secrist, J.P.2    Kazlauskas, A.3
  • 184
    • 0030899807 scopus 로고    scopus 로고
    • Tyrosine phosphorylation sites at amino acids 239 and 240 of Shc are involved in epidermal growth factor-induced mitogenic signaling that is distinct from Ras/mitogen-activated protein kinase activation
    • Gotoh N., Toyoda M., Shibuya M. Tyrosine phosphorylation sites at amino acids 239 and 240 of Shc are involved in epidermal growth factor-induced mitogenic signaling that is distinct from Ras/mitogen-activated protein kinase activation. Mol. Cell. Biol. 17:1997;1824-1831.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1824-1831
    • Gotoh, N.1    Toyoda, M.2    Shibuya, M.3
  • 185
    • 0027521783 scopus 로고
    • Two signaling molecules share a phosphotyrosine-containing binding site in the platelet-derived growth factor receptor
    • Nishimura R., Li W., Kashishian A., Mondino A., Zhou M., Cooper J., Schlessinger J. Two signaling molecules share a phosphotyrosine-containing binding site in the platelet-derived growth factor receptor. Mol. Cell. Biol. 13:1993;6889-6896.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6889-6896
    • Nishimura, R.1    Li, W.2    Kashishian, A.3    Mondino, A.4    Zhou, M.5    Cooper, J.6    Schlessinger, J.7
  • 187
    • 0030907935 scopus 로고    scopus 로고
    • NIK is a new Ste20-related kinase that binds NCK and MEKK1 and activates the SAPK/JNK cascade via a conserved regulatory domain
    • Su Y.C., Han J., Xu S., Cobb M., Skolnik E.Y. NIK is a new Ste20-related kinase that binds NCK and MEKK1 and activates the SAPK/JNK cascade via a conserved regulatory domain. EMBO J. 16:1997;1279-1290.
    • (1997) EMBO J. , vol.16 , pp. 1279-1290
    • Su, Y.C.1    Han, J.2    Xu, S.3    Cobb, M.4    Skolnik, E.Y.5
  • 188
    • 0029943447 scopus 로고    scopus 로고
    • Drosophila photoreceptor axon guidance and targeting requires the dreadlocks SH2/SH3 adapter protein
    • Garrity P.A., Rao Y., Salecker I., McGlade J., Pawson T., Zipursky S.L. Drosophila photoreceptor axon guidance and targeting requires the dreadlocks SH2/SH3 adapter protein. Cell. 85:1996;639-650.
    • (1996) Cell , vol.85 , pp. 639-650
    • Garrity, P.A.1    Rao, Y.2    Salecker, I.3    McGlade, J.4    Pawson, T.5    Zipursky, S.L.6
  • 190
    • 0029828866 scopus 로고    scopus 로고
    • Grb7 is a downstream signaling component of platelet-derived growth factor α- and β-receptors
    • Yokote K., Margolis B., Heldin C.-H., Claesson-Welsh L. Grb7 is a downstream signaling component of platelet-derived growth factor α- and β-receptors. J. Biol. Chem. 271:1996;30942-30949.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30942-30949
    • Yokote, K.1    Margolis, B.2    Heldin, C.-H.3    Claesson-Welsh, L.4
  • 191
    • 0030614746 scopus 로고    scopus 로고
    • Human GRB-IRβ/GRB10. Splice variants of an insulin and growth factor receptor-binding protein with PH and SH2 domains
    • Frantz J.D., Giorgetti-Peraldi S., Ottinger E.A., Shoelson S.E. Human GRB-IRβ/GRB10. Splice variants of an insulin and growth factor receptor-binding protein with PH and SH2 domains. J. Biol. Chem. 272:1997;2659-2667.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2659-2667
    • Frantz, J.D.1    Giorgetti-Peraldi, S.2    Ottinger, E.A.3    Shoelson, S.E.4
  • 192
    • 17544378927 scopus 로고    scopus 로고
    • Cloning and characterization of GRB14, a novel member of the GRB7 gene family
    • Daly R.J., Sanderson G.M., Janes P.W., Sutherland R.L. Cloning and characterization of GRB14, a novel member of the GRB7 gene family. J. Biol. Chem. 271:1996;12502-12510.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12502-12510
    • Daly, R.J.1    Sanderson, G.M.2    Janes, P.W.3    Sutherland, R.L.4
  • 193
    • 0030180321 scopus 로고    scopus 로고
    • SH2 and SH3-containing adaptor proteins: Redundant or independent mediators of intracellular signal transduction
    • Birge R.B., Knudsen B.S., Besser D., Hanafusa H. SH2 and SH3-containing adaptor proteins: redundant or independent mediators of intracellular signal transduction. Genes Cells. 1:1996;595-613.
    • (1996) Genes Cells , vol.1 , pp. 595-613
    • Birge, R.B.1    Knudsen, B.S.2    Besser, D.3    Hanafusa, H.4
  • 194
    • 85046174812 scopus 로고    scopus 로고
    • Identification of Tyr-762 in the platelet-derived growth factor α-receptor as the binding site for Crk proteins
    • in press.
    • K. Yokote, U. Hellman, Y. Saito, S. Ekman, L. Rönnstrand, Y. Saito, C.-H. Heldin, S. Mori, Identification of Tyr-762 in the platelet-derived growth factor α-receptor as the binding site for Crk proteins, Oncogene, in press.
    • Oncogene
    • Yokote, K.1    Hellman, U.2    Saito, Y.3    Ekman, S.4    Rönnstrand, L.5    Saito, Y.6    Heldin, C.-H.7    Mori, S.8
  • 195
    • 0030949507 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of p130cas by bombesin, lysophosphatidic acid, phorbol esters, and platelet-derived growth factor - signaling pathways and formation of A p130cas-Crk complex
    • Casamassima A., Rozengurt E. Tyrosine phosphorylation of p130cas by bombesin, lysophosphatidic acid, phorbol esters, and platelet-derived growth factor - signaling pathways and formation of A p130cas-Crk complex. J. Biol. Chem. 272:1997;9363-9370.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9363-9370
    • Casamassima, A.1    Rozengurt, E.2
  • 196
    • 0031004266 scopus 로고    scopus 로고
    • Downstream of Crk adaptor signaling pathway: Activation of Jun kinase by v-Crk through the guanine nucleotide exchange protein C3G
    • Tanaka S., Ouchi T., Hanafusa H. Downstream of Crk adaptor signaling pathway: activation of Jun kinase by v-Crk through the guanine nucleotide exchange protein C3G. Proc. Natl. Acad. Sci. USA. 94:1997;2356-2361.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2356-2361
    • Tanaka, S.1    Ouchi, T.2    Hanafusa, H.3
  • 197
    • 0342618377 scopus 로고    scopus 로고
    • Phosphorylation of a 72-kDa protein in PDGF-stimulated cells which forms complex with c-Crk, c-Fyn and Eps15
    • Hansen K., Rönnstrand L., Claesson-Welsh L., Heldin C.-H. Phosphorylation of a 72-kDa protein in PDGF-stimulated cells which forms complex with c-Crk, c-Fyn and Eps15. FEBS Lett. 409:1997;195-200.
    • (1997) FEBS Lett. , vol.409 , pp. 195-200
    • Hansen, K.1    Rönnstrand, L.2    Claesson-Welsh, L.3    Heldin, C.-H.4
  • 198
    • 17044444647 scopus 로고    scopus 로고
    • STAM, signal transducing adaptor molecule, is associated with Janus kinases and involved in signaling for cell growth and c-myc induction
    • Takeshita T., Arita T., Higuchi M., Asao H., Endo K., Kuroda H., Tanaka N., Murata K., Ishii N., Sugamura K. STAM, signal transducing adaptor molecule, is associated with Janus kinases and involved in signaling for cell growth and c-myc induction. Immunity. 6:1997;449-457.
    • (1997) Immunity , vol.6 , pp. 449-457
    • Takeshita, T.1    Arita, T.2    Higuchi, M.3    Asao, H.4    Endo, K.5    Kuroda, H.6    Tanaka, N.7    Murata, K.8    Ishii, N.9    Sugamura, K.10
  • 199
    • 0027941342 scopus 로고
    • Stimulation of the platelet-derived growth factor β receptor signaling pathway activates protein kinase C-δ
    • Li W., Yu J.-C., Michieli P., Beeler J.F., Ellmore N., Heidaran M.A., Pierce J.H. Stimulation of the platelet-derived growth factor β receptor signaling pathway activates protein kinase C-δ Mol. Cell. Biol. 14:1994;6727-6735.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6727-6735
    • Li, W.1    Yu, J.-C.2    Michieli, P.3    Beeler, J.F.4    Ellmore, N.5    Heidaran, M.A.6    Pierce, J.H.7
  • 202
    • 0029831486 scopus 로고    scopus 로고
    • Platelet-derived growth factor-dependent activation of phosphatidylinositol 3-kinase is regulated by receptor binding of SH2-domain-containing proteins which influence Ras activity
    • Klinghoffer R.A., Duckworth B., Valius M., Cantley L., Kazlauskas A. Platelet-derived growth factor-dependent activation of phosphatidylinositol 3-kinase is regulated by receptor binding of SH2-domain-containing proteins which influence Ras activity. Mol. Cell. Biol. 16:1996;5905-5914.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5905-5914
    • Klinghoffer, R.A.1    Duckworth, B.2    Valius, M.3    Cantley, L.4    Kazlauskas, A.5
  • 203
    • 0028918408 scopus 로고
    • Ras-dependent induction of cellular responses by constitutively active phosphatidylinositol-3 kinase
    • Hu Q., Klippel A., Muslin A.J., Fantl W.J., Williams L.T. Ras-dependent induction of cellular responses by constitutively active phosphatidylinositol-3 kinase. Science. 268:1995;100-102.
    • (1995) Science , vol.268 , pp. 100-102
    • Hu, Q.1    Klippel, A.2    Muslin, A.J.3    Fantl, W.J.4    Williams, L.T.5
  • 204
    • 0029101360 scopus 로고
    • An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1
    • Olson M.F., Ashworth A., Hall A. An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1. Science. 269:1995;1270-1272.
    • (1995) Science , vol.269 , pp. 1270-1272
    • Olson, M.F.1    Ashworth, A.2    Hall, A.3
  • 205
    • 0028903247 scopus 로고
    • An essential role for Rac in Ras transformation
    • Qiu R.-G., Chen J., Kirn D., McCormick F., Symons M. An essential role for Rac in Ras transformation. Nature. 374:1995;457-459.
    • (1995) Nature , vol.374 , pp. 457-459
    • Qiu, R.-G.1    Chen, J.2    Kirn, D.3    McCormick, F.4    Symons, M.5
  • 206
    • 0028800305 scopus 로고
    • Activation of Rac1, RhoA, and mitogen-activated protein kinases is required for Ras transformation
    • Khosravi-Far R., Solski P.A., Clark G.J., Kinch M.S., Der C.J. Activation of Rac1, RhoA, and mitogen-activated protein kinases is required for Ras transformation. Mol. Cell. Biol. 15:1995;6443-6453.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6443-6453
    • Khosravi-Far, R.1    Solski, P.A.2    Clark, G.J.3    Kinch, M.S.4    Der, C.J.5
  • 207
    • 0030992814 scopus 로고    scopus 로고
    • Cdc42 regulates anchorage-independent growth and is necessary for Ras transformation
    • Qiu R.G., Abo A., McCormick F., Symons M. Cdc42 regulates anchorage-independent growth and is necessary for Ras transformation. Mol. Cell. Biol. 17:1997;3449-3458.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3449-3458
    • Qiu, R.G.1    Abo, A.2    McCormick, F.3    Symons, M.4
  • 208
    • 0028872649 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. 80:1995;179-185.
    • (1995) Cell , vol.80 , pp. 179-185
    • Marshall, C.J.1
  • 209
    • 0027299745 scopus 로고
    • On the crawling of animal cells
    • Stossel T.P. On the crawling of animal cells. Science. 260:1993;1086-1094.
    • (1993) Science , vol.260 , pp. 1086-1094
    • Stossel, T.P.1
  • 210
    • 0028281170 scopus 로고
    • Excess early signaling activity inhibits cellular chemotaxis toward PDGF-BB
    • Kundra V., Soker S., Zetter B.R. Excess early signaling activity inhibits cellular chemotaxis toward PDGF-BB. Oncogene. 9:1994;1429-1435.
    • (1994) Oncogene , vol.9 , pp. 1429-1435
    • Kundra, V.1    Soker, S.2    Zetter, B.R.3
  • 211
    • 0029991362 scopus 로고    scopus 로고
    • Impaired migration but not differentiation of hematopoietic stem cells in the absence of β1 integrins
    • Hirsch E., Iglesias A., Potocnik A.J., Hartmann U., Fassler R. Impaired migration but not differentiation of hematopoietic stem cells in the absence of β1 integrins. Nature. 380:1996;171-175.
    • (1996) Nature , vol.380 , pp. 171-175
    • Hirsch, E.1    Iglesias, A.2    Potocnik, A.J.3    Hartmann, U.4    Fassler, R.5
  • 214
    • 0028049088 scopus 로고
    • FAK) and paxillin tyrosine phosphorylation in Swiss 3T3 cells. Bell-shaped dose response and cross-talk with bombesin
    • FAK) and paxillin tyrosine phosphorylation in Swiss 3T3 cells. Bell-shaped dose response and cross-talk with bombesin. J. Biol. Chem. 269:1994;704-710.
    • (1994) J. Biol. Chem. , vol.269 , pp. 704-710
    • Rankin, S.1    Rozengurt, E.2
  • 216
    • 0028089005 scopus 로고
    • Membrane ruffling and chemotaxis transduced by the PDGF β-receptor require the binding site for phosphatidyl-inositol 3′ kinase
    • Wennström S., Siegbahn A., Yokote K., Arvidsson A.-K., Heldin C.-H., Mori S., Claesson-Welsh L. Membrane ruffling and chemotaxis transduced by the PDGF β-receptor require the binding site for phosphatidyl-inositol 3′ kinase. Oncogene. 9:1994;651-660.
    • (1994) Oncogene , vol.9 , pp. 651-660
    • Wennström, S.1    Siegbahn, A.2    Yokote, K.3    Arvidsson, A.-K.4    Heldin, C.-H.5    Mori, S.6    Claesson-Welsh, L.7
  • 217
    • 0028837170 scopus 로고
    • Activation of the small GTP-binding proteins rho and rac by growth factor receptors
    • Nobes C.D., Hawkins P., Stephens L., Hall A. Activation of the small GTP-binding proteins rho and rac by growth factor receptors. J. Cell Sci. 108:1995;225-233.
    • (1995) J. Cell Sci. , vol.108 , pp. 225-233
    • Nobes, C.D.1    Hawkins, P.2    Stephens, L.3    Hall, A.4
  • 218
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley A.J., Hall A. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell. 70:1992;389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 219
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley A.J., Paterson H.F., Johnston C.L., Diekmann D., Hall A. The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell. 70:1992;401-410.
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 220
    • 0028961293 scopus 로고
    • Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes C.D., Hall A. Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell. 81:1995;53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 221
    • 0030940218 scopus 로고    scopus 로고
    • Rho, Rac and Cdc42 regulate actin organization and cell adhesion in macrophages
    • Allen W.E., Jones G.E., Pollard J.W., Ridley A.J. Rho, Rac and Cdc42 regulate actin organization and cell adhesion in macrophages. J. Cell Sci. 110:1997;707-720.
    • (1997) J. Cell Sci. , vol.110 , pp. 707-720
    • Allen, W.E.1    Jones, G.E.2    Pollard, J.W.3    Ridley, A.J.4
  • 222
    • 0031214960 scopus 로고    scopus 로고
    • Involvement of phosphatidylinositide 3′-kinase and Rac in platelet-derived growth factor-induced actin reorganization and chemotaxis
    • Hooshmand-Rad R., Claesson-Welsh L., Wennström S., Yokote K., Siegbahn A., Heldin C.-H. Involvement of phosphatidylinositide 3′-kinase and Rac in platelet-derived growth factor-induced actin reorganization and chemotaxis. Exp. Cell Res. 234:1997;434-441.
    • (1997) Exp. Cell Res. , vol.234 , pp. 434-441
    • Hooshmand-Rad, R.1    Claesson-Welsh, L.2    Wennström, S.3    Yokote, K.4    Siegbahn, A.5    Heldin, C.-H.6
  • 224
    • 0029830747 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase-independent signal transduction pathway for platelet-derived growth factor-induced chemotaxis
    • Higaki M., Sakaue H., Ogawa W., Kasuga M., Shimokado K. Phosphatidylinositol 3-kinase-independent signal transduction pathway for platelet-derived growth factor-induced chemotaxis. J. Biol. Chem. 271:1996;29342-29346.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29342-29346
    • Higaki, M.1    Sakaue, H.2    Ogawa, W.3    Kasuga, M.4    Shimokado, K.5
  • 225
    • 0028330152 scopus 로고
    • Insulin-like growth factor-I and platelet-derived growth factor-BB induce directed migration of human arterial smooth muscle cells via signaling pathways that are distinct from those of proliferation
    • Bornfeldt K.E., Raines E.W., Nakano T., Graves L.M., Krebs E.G., Ross R. Insulin-like growth factor-I and platelet-derived growth factor-BB induce directed migration of human arterial smooth muscle cells via signaling pathways that are distinct from those of proliferation. J. Clin. Invest. 93:1994;1266-1274.
    • (1994) J. Clin. Invest. , vol.93 , pp. 1266-1274
    • Bornfeldt, K.E.1    Raines, E.W.2    Nakano, T.3    Graves, L.M.4    Krebs, E.G.5    Ross, R.6
  • 227
    • 0029791504 scopus 로고    scopus 로고
    • Mutation of a Src phosphorylation site in the PDGF β-receptor leads to increased PDGF-stimulated chemotaxis but decreased mitogenesis
    • Hansen K., Johnell M., Siegbahn A., Rorsman C., Engström U., Wernstedt C., Heldin C.-H., Rönnstrand L. Mutation of a Src phosphorylation site in the PDGF β-receptor leads to increased PDGF-stimulated chemotaxis but decreased mitogenesis. EMBO J. 15:1996;5299-5313.
    • (1996) EMBO J. , vol.15 , pp. 5299-5313
    • Hansen, K.1    Johnell, M.2    Siegbahn, A.3    Rorsman, C.4    Engström, U.5    Wernstedt, C.6    Heldin, C.-H.7    Rönnstrand, L.8
  • 228
    • 0022470480 scopus 로고
    • Induction of membrane ruffling and fluid-phase pinocytosis in quiescent fibroblasts by ras proteins
    • Bar-Sagi D., Feramisco J.R. Induction of membrane ruffling and fluid-phase pinocytosis in quiescent fibroblasts by ras proteins. Science. 233:1986;1061-1068.
    • (1986) Science , vol.233 , pp. 1061-1068
    • Bar-Sagi, D.1    Feramisco, J.R.2
  • 230
    • 0029093670 scopus 로고
    • The chemotactic response to PDGF-BB: Evidence of a role for Ras
    • Kundra V., Anand-Apte B., Feig L.A., Zetter B.R. The chemotactic response to PDGF-BB: evidence of a role for Ras. J. Cell Biol. 130:1995;725-731.
    • (1995) J. Cell Biol. , vol.130 , pp. 725-731
    • Kundra, V.1    Anand-Apte, B.2    Feig, L.A.3    Zetter, B.R.4
  • 231
    • 0030723163 scopus 로고    scopus 로고
    • Platelet-derived growth factor and fibronectin-stimulated migration are differentially regulated by the Rac and extracellular signal-regulated kinase pathways
    • Anand-Apte B., Zetter B.R., Viswanathan A., Qiu R.-G., Chen J., Ruggieri R., Symons M. Platelet-derived growth factor and fibronectin-stimulated migration are differentially regulated by the Rac and extracellular signal-regulated kinase pathways. J. Biol. Chem. 272:1997;30688-30692.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30688-30692
    • Anand-Apte, B.1    Zetter, B.R.2    Viswanathan, A.3    Qiu, R.-G.4    Chen, J.5    Ruggieri, R.6    Symons, M.7
  • 232
    • 0031033617 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase activation is involved in platelet-derived growth factor-directed migration by vascular smooth muscle cells
    • Graf K., Xi X.-P., Yang D., Fleck E., Hsueh W.A., Law R.E. Mitogen-activated protein kinase activation is involved in platelet-derived growth factor-directed migration by vascular smooth muscle cells. Hypertension. 29:(2):1997;334-339.
    • (1997) Hypertension , vol.29 , Issue.2 , pp. 334-339
    • Graf, K.1    Xi, X.-P.2    Yang, D.3    Fleck, E.4    Hsueh, W.A.5    Law, R.E.6
  • 233
    • 0026440702 scopus 로고
    • Regulatory effects of platelet-derived growth factor-AA homodimer on migration of vascular smooth muscle cells
    • Koyama N., Morisaki N., Saito Y., Yoshida S. Regulatory effects of platelet-derived growth factor-AA homodimer on migration of vascular smooth muscle cells. J. Biol. Chem. 267:1992;22806-22812.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22806-22812
    • Koyama, N.1    Morisaki, N.2    Saito, Y.3    Yoshida, S.4
  • 234
    • 0029011218 scopus 로고
    • The MAPK signaling cascade
    • Seger R., Krebs E.G. The MAPK signaling cascade. FASEB J. 9:1995;726-735.
    • (1995) FASEB J. , vol.9 , pp. 726-735
    • Seger, R.1    Krebs, E.G.2
  • 235
    • 0027371722 scopus 로고
    • Sphingosine-1-phosphate as second messenger in cell proliferation induced by PDGF and FCS mitogens
    • Olivera A., Spiegel S. Sphingosine-1-phosphate as second messenger in cell proliferation induced by PDGF and FCS mitogens. Nature. 365:1993;557-560.
    • (1993) Nature , vol.365 , pp. 557-560
    • Olivera, A.1    Spiegel, S.2
  • 237
    • 0029889045 scopus 로고    scopus 로고
    • Sphingomyelin-derived lipids differentially regulate the extracellular signal-regulated kinase 2 (ERK-2) and c-Jun N-terminal kinase (JNK) signal cascades in airway smooth muscle
    • Pyne S., Chapman J., Steele L., Pyne N.J. Sphingomyelin-derived lipids differentially regulate the extracellular signal-regulated kinase 2 (ERK-2) and c-Jun N-terminal kinase (JNK) signal cascades in airway smooth muscle. Eur. J. Biochem. 237:1996;819-826.
    • (1996) Eur. J. Biochem. , vol.237 , pp. 819-826
    • Pyne, S.1    Chapman, J.2    Steele, L.3    Pyne, N.J.4
  • 238
    • 0030891014 scopus 로고    scopus 로고
    • Divergence in signal transduction pathways of platelet-derived growth factor (PDGF) and epidermal growth factor (EGF) receptors. Involvement of sphingosine 1-phosphate in PDGF but not EGF signaling
    • Rani C.S.S., Wang F., Fuior E., Berger A., Wu J., Sturgill T.W., Beitner-Johnson D., LeRoith D., Varticovski L., Spiegel S. Divergence in signal transduction pathways of platelet-derived growth factor (PDGF) and epidermal growth factor (EGF) receptors. Involvement of sphingosine 1-phosphate in PDGF but not EGF signaling. J. Biol. Chem. 272:1997;10777-10783.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10777-10783
    • Rani, C.S.S.1    Wang, F.2    Fuior, E.3    Berger, A.4    Wu, J.5    Sturgill, T.W.6    Beitner-Johnson, D.7    Leroith, D.8    Varticovski, L.9    Spiegel, S.10
  • 239
    • 0030808066 scopus 로고    scopus 로고
    • Platelet-derived growth factor activation of mitogen-activated protein kinase depends on the sequential activation of phosphatidylcholine-specific phospholipase C, protein kinase C-ζ and Raf-1
    • van Dijk M.C.M., Hilkmann H., van Blitterswijk W.J. Platelet-derived growth factor activation of mitogen-activated protein kinase depends on the sequential activation of phosphatidylcholine-specific phospholipase C, protein kinase C-ζ and Raf-1. Biochem. J. 325:1997;303-307.
    • (1997) Biochem. J. , vol.325 , pp. 303-307
    • Van Dijk, M.C.M.1    Hilkmann, H.2    Van Blitterswijk, W.J.3
  • 240
    • 0028239047 scopus 로고
    • Independent effects of platelet-derived growth factor isoforms on mitogen-activated protein kinase activation and mitogenesis in human dermal fibroblasts
    • Lubinus M., Meier K.E., Smith E.A., Gause K.C., LeRoy E.C., Trojanowska M. Independent effects of platelet-derived growth factor isoforms on mitogen-activated protein kinase activation and mitogenesis in human dermal fibroblasts. J. Biol. Chem. 269:1994;9822-9825.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9822-9825
    • Lubinus, M.1    Meier, K.E.2    Smith, E.A.3    Gause, K.C.4    Leroy, E.C.5    Trojanowska, M.6
  • 241
    • 0028278081 scopus 로고
    • The differential activation of phosphatidylinositol-3 kinase and mitogen-activated protein kinases by PDGF-AA and IGF-I might explain the synergistic effect of the two growth factors on the proliferation of AKR-2B fibroblasts
    • Karenberg T.-A., Fenn A., Sachinidis A., Hoppe J. The differential activation of phosphatidylinositol-3 kinase and mitogen-activated protein kinases by PDGF-AA and IGF-I might explain the synergistic effect of the two growth factors on the proliferation of AKR-2B fibroblasts. Exp. Cell Res. 213:1994;266-274.
    • (1994) Exp. Cell Res. , vol.213 , pp. 266-274
    • Karenberg, T.-A.1    Fenn, A.2    Sachinidis, A.3    Hoppe, J.4
  • 242
    • 0030578451 scopus 로고    scopus 로고
    • The synergistic effect of PDGF-AA and IGF-1 on VSMC proliferation might be explained by the differential activation of their intracellular signaling pathways
    • Thömmes K.B., Hoppe J., Vetter H., Sachinidis A. The synergistic effect of PDGF-AA and IGF-1 on VSMC proliferation might be explained by the differential activation of their intracellular signaling pathways. Exp. Cell Res. 226:1996;59-66.
    • (1996) Exp. Cell Res. , vol.226 , pp. 59-66
    • Thömmes, K.B.1    Hoppe, J.2    Vetter, H.3    Sachinidis, A.4
  • 243
    • 0029814709 scopus 로고    scopus 로고
    • Requirement of phospholipase Cγ, the tyrosine phosphatase Syp and the adaptor proteins Shc and Nck for PDGF-induced DNA synthesis: Evidence for the existence of Ras-dependent and Ras-independent pathways
    • Roche S., McGlade J., Jones M., Gish G.D., Pawson T., Courtneidge S.A. Requirement of phospholipase Cγ, the tyrosine phosphatase Syp and the adaptor proteins Shc and Nck for PDGF-induced DNA synthesis: evidence for the existence of Ras-dependent and Ras-independent pathways. EMBO J. 15:1996;4940-4948.
    • (1996) EMBO J. , vol.15 , pp. 4940-4948
    • Roche, S.1    McGlade, J.2    Jones, M.3    Gish, G.D.4    Pawson, T.5    Courtneidge, S.A.6
  • 244
    • 0029943605 scopus 로고    scopus 로고
    • Membrane localization of phosphatidylinositol 3-kinase is sufficient to activate multiple signal-transducing kinase pathways
    • Klippel A., Escobedo J.A., Hirano M., Williams L.T. Membrane localization of phosphatidylinositol 3-kinase is sufficient to activate multiple signal-transducing kinase pathways. Mol. Cell. Biol. 16:1996;4117-4127.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4117-4127
    • Klippel, A.1    Escobedo, J.A.2    Hirano, M.3    Williams, L.T.4
  • 245
    • 0031035636 scopus 로고    scopus 로고
    • Specific activation of p85-p110 phosphatidylinositol 3′-kinase stimulates DNA synthesis by ras- and p70 S6 kinase-dependent pathways
    • McIlroy J., Chen D., Wjasow C., Michaeli T., Backer J.M. Specific activation of p85-p110 phosphatidylinositol 3′-kinase stimulates DNA synthesis by ras- and p70 S6 kinase-dependent pathways. Mol. Cell. Biol. 17:1997;248-255.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 248-255
    • McIlroy, J.1    Chen, D.2    Wjasow, C.3    Michaeli, T.4    Backer, J.M.5
  • 246
    • 0027211693 scopus 로고
    • Phospholipase C-γ1 and phosphatidyl-inositol 3 kinase are the downstream mediators of the PDGF receptor's mitogenic signal
    • Valius M., Kazlauskas A. Phospholipase C-γ1 and phosphatidyl-inositol 3 kinase are the downstream mediators of the PDGF receptor's mitogenic signal. Cell. 73:1993;321-334.
    • (1993) Cell , vol.73 , pp. 321-334
    • Valius, M.1    Kazlauskas, A.2
  • 247
    • 2642593022 scopus 로고    scopus 로고
    • Requirement for phospholipase C-γ1 enzymatic activity in growth factor-induced mitogenesis
    • Wang Z., Glück S., Zhang L., Moran M.F. Requirement for phospholipase C-γ1 enzymatic activity in growth factor-induced mitogenesis. Mol. Cell. Biol. 18:1998;590-597.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 590-597
    • Wang, Z.1    Glück, S.2    Zhang, L.3    Moran, M.F.4
  • 249
    • 0025152003 scopus 로고
    • Overexpression of phospholipase C-gamma in NIH 3T3 fibroblasts results in increased phosphatidylinositol hydrolysis in response to platelet-derived growth factor and basic fibroblast growth factor
    • Cuadrado A., Molloy C.J. Overexpression of phospholipase C-gamma in NIH 3T3 fibroblasts results in increased phosphatidylinositol hydrolysis in response to platelet-derived growth factor and basic fibroblast growth factor. Mol. Cell. Biol. 10:1990;6069-6072.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 6069-6072
    • Cuadrado, A.1    Molloy, C.J.2
  • 250
    • 0027082766 scopus 로고
    • The β-PDGF receptor induces neuronal differentiation of PC12 cells
    • Heasley L.E., Johnson G.L. The β-PDGF receptor induces neuronal differentiation of PC12 cells. Mol. Biol. Cell. 3:1992;545-553.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 545-553
    • Heasley, L.E.1    Johnson, G.L.2
  • 251
    • 0029240518 scopus 로고
    • β PDGF receptor mutants defective for mitogenesis promote neurite outgrowth in PC12 cells
    • Vetter M.L., Bishop J.M. β PDGF receptor mutants defective for mitogenesis promote neurite outgrowth in PC12 cells. Curr. Biol. 5:1995;168-178.
    • (1995) Curr. Biol. , vol.5 , pp. 168-178
    • Vetter, M.L.1    Bishop, J.M.2
  • 252
  • 253
    • 0031034397 scopus 로고    scopus 로고
    • Analysis of mutant platelet-derived growth factor receptors expressed in PC12 cells identifies signals governing sodium channel induction during neuronal differentiation
    • Fanger G.R., Vaillancourt R.R., Heasley L.E., Montmayeur J.-P.R., Johnson G.L., Maue R.A. Analysis of mutant platelet-derived growth factor receptors expressed in PC12 cells identifies signals governing sodium channel induction during neuronal differentiation. Mol. Cell. Biol. 17:1997;89-99.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 89-99
    • Fanger, G.R.1    Vaillancourt, R.R.2    Heasley, L.E.3    Montmayeur, J.-P.R.4    Johnson, G.L.5    Maue, R.A.6
  • 257
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
    • Datta S.R., Dudek H., Tao X., Masters S., Fu H., Gotoh Y., Greenberg M.E. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell. 91:1997;231-241.
    • (1997) Cell , vol.91 , pp. 231-241
    • Datta, S.R.1    Dudek, H.2    Tao, X.3    Masters, S.4    Fu, H.5    Gotoh, Y.6    Greenberg, M.E.7
  • 259
    • 0031936353 scopus 로고    scopus 로고
    • Ras signalling and apoptosis
    • Downward J. Ras signalling and apoptosis. Curr. Opin. Genet. Dev. 8:1998;49-54.
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 49-54
    • Downward, J.1
  • 263
    • 0028224348 scopus 로고
    • Fusion of PDGF receptor β to a novel ets-like gene, tel, in chronic myelomonocytic leukemia with t(5;12) chromosomal translocation
    • Golub T.R., Barker G.F., Lovett M., Gilliland D.G. Fusion of PDGF receptor β to a novel ets-like gene, tel, in chronic myelomonocytic leukemia with t(5;12) chromosomal translocation. Cell. 77:1994;307-316.
    • (1994) Cell , vol.77 , pp. 307-316
    • Golub, T.R.1    Barker, G.F.2    Lovett, M.3    Gilliland, D.G.4
  • 264
    • 0029966854 scopus 로고    scopus 로고
    • The TEL/platelet-derived growth factor β receptor (PDGFβR) fusion in chronic myelomonocytic leukemia is a transforming protein that self-associates and activates PDGFβR kinase-dependent signaling pathways
    • Carroll M., Tomasson M.H., Barker G.F., Golub T.R., Gilliland D.G. The TEL/platelet-derived growth factor β receptor (PDGFβR) fusion in chronic myelomonocytic leukemia is a transforming protein that self-associates and activates PDGFβR kinase-dependent signaling pathways. Proc. Natl. Acad. Sci. USA. 93:1996;14845-14850.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14845-14850
    • Carroll, M.1    Tomasson, M.H.2    Barker, G.F.3    Golub, T.R.4    Gilliland, D.G.5
  • 265
    • 17144463437 scopus 로고    scopus 로고
    • A domain of TEL conserved in a subset of ETS proteins defines a specific oligomerization interface essential to the mitogenic properties of the TEL-PDGFRβ oncoprotein
    • Jousset C., Carron C., Boureux A., Quang C.T., Oury C., Dusanter-Fourt I., Charon M., Levin J., Bernard O., Ghysdael J. A domain of TEL conserved in a subset of ETS proteins defines a specific oligomerization interface essential to the mitogenic properties of the TEL-PDGFRβ oncoprotein. EMBO J. 16:1997;69-82.
    • (1997) EMBO J. , vol.16 , pp. 69-82
    • Jousset, C.1    Carron, C.2    Boureux, A.3    Quang, C.T.4    Oury, C.5    Dusanter-Fourt, I.6    Charon, M.7    Levin, J.8    Bernard, O.9    Ghysdael, J.10
  • 266
    • 0031454003 scopus 로고    scopus 로고
    • CGP 57148, a tyrosine kinase inhibitor, inhibits the growth of cells expressing BCR-ABL, TEL-ABL, and TEL-PDGFR fusion proteins
    • Carroll M., Ohno-Jones S., Tamura S., Buchdunger E., Zimmermann J., Lydon N.B., Gilliland D.G., Druker B.J. CGP 57148, a tyrosine kinase inhibitor, inhibits the growth of cells expressing BCR-ABL, TEL-ABL, and TEL-PDGFR fusion proteins. Blood. 90:1997;4947-4952.
    • (1997) Blood , vol.90 , pp. 4947-4952
    • Carroll, M.1    Ohno-Jones, S.2    Tamura, S.3    Buchdunger, E.4    Zimmermann, J.5    Lydon, N.B.6    Gilliland, D.G.7    Druker, B.J.8
  • 267
    • 0030669455 scopus 로고    scopus 로고
    • Fusion of the platelet-derived growth factor receptor β to a novel gene CEV14 in acute myelogenous leukemia after clonal evolution
    • Abe A., Emi N., Tanimoto M., Terasaki H., Marunouchi T., Saito H. Fusion of the platelet-derived growth factor receptor β to a novel gene CEV14 in acute myelogenous leukemia after clonal evolution. Blood. 90:1997;4271-4277.
    • (1997) Blood , vol.90 , pp. 4271-4277
    • Abe, A.1    Emi, N.2    Tanimoto, M.3    Terasaki, H.4    Marunouchi, T.5    Saito, H.6
  • 268
    • 0030823819 scopus 로고    scopus 로고
    • Integration of proviral DNA into the PDGF β-receptor gene in HTLV-I-infected T-cells results in a novel tyrosine kinase product with transforming activity
    • Chi K.D., McPhee R.A., Wagner A.S., Dietz J.J., Pantazis P., Goustin A.S. Integration of proviral DNA into the PDGF β-receptor gene in HTLV-I-infected T-cells results in a novel tyrosine kinase product with transforming activity. Oncogene. 15:1997;1051-1057.
    • (1997) Oncogene , vol.15 , pp. 1051-1057
    • Chi, K.D.1    McPhee, R.A.2    Wagner, A.S.3    Dietz, J.J.4    Pantazis, P.5    Goustin, A.S.6
  • 269
    • 0028812442 scopus 로고
    • β PDGFR-IgG chimera demonstrates that human beta PDGFR Ig-like domains 1 to 3 are sufficient for high affinity PDGF BB binding
    • Heidaran M.A., Mahadevan D., Larochelle W.J. β PDGFR-IgG chimera demonstrates that human beta PDGFR Ig-like domains 1 to 3 are sufficient for high affinity PDGF BB binding. FASEB J. 9:1995;140-145.
    • (1995) FASEB J. , vol.9 , pp. 140-145
    • Heidaran, M.A.1    Mahadevan, D.2    Larochelle, W.J.3
  • 270
    • 0029931374 scopus 로고    scopus 로고
    • Identification of a domain within the carboxyl-terminal region of the β platelet-derived growth factor (PDGF) receptor that mediates the high transforming activity of PDGF
    • Uren A., Yu J.-C., Li W., Chung I.-Y., Mahadevan D., Pierce J.H., Heidaran M.A. Identification of a domain within the carboxyl-terminal region of the β platelet-derived growth factor (PDGF) receptor that mediates the high transforming activity of PDGF. J. Biol. Chem. 271:1996;11051-11054.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11051-11054
    • Uren, A.1    Yu, J.-C.2    Li, W.3    Chung, I.-Y.4    Mahadevan, D.5    Pierce, J.H.6    Heidaran, M.A.7
  • 271
    • 0028930121 scopus 로고
    • Differential requirement of a motif within the carboxyl-terminal domain of α-platelet-derived growth factor (αPDGF) receptor for PDGF focus forming activity chemotaxis, or growth
    • Yu J.-C., Li W., Wang L.-M., Uren A., Pierce J.H., Heidaran M.A. Differential requirement of a motif within the carboxyl-terminal domain of α-platelet-derived growth factor (αPDGF) receptor for PDGF focus forming activity chemotaxis, or growth. J. Biol. Chem. 270:1995;7033-7036.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7033-7036
    • Yu, J.-C.1    Li, W.2    Wang, L.-M.3    Uren, A.4    Pierce, J.H.5    Heidaran, M.A.6
  • 272
    • 0030938093 scopus 로고    scopus 로고
    • Platelet-derived growth factor-dependent cellular transformation requires either phospholipase Cγ or phosphatidylinositol 3 kinase
    • DeMali K.A., Whiteford C.C., Ulug E.T., Kazlauskas A. Platelet-derived growth factor-dependent cellular transformation requires either phospholipase Cγ or phosphatidylinositol 3 kinase. J. Biol. Chem. 272:1997;9011-9018.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9011-9018
    • Demali, K.A.1    Whiteford, C.C.2    Ulug, E.T.3    Kazlauskas, A.4
  • 273
    • 0030768754 scopus 로고    scopus 로고
    • Identification of amino acids in the transmembrane and juxtamembrane domains of the platelet-derived growth factor receptor required for productive interaction with the bovine papillomavirus E5 protein
    • Petti L.M., Reddy V., Smith S.O., DiMaio D. Identification of amino acids in the transmembrane and juxtamembrane domains of the platelet-derived growth factor receptor required for productive interaction with the bovine papillomavirus E5 protein. J. Virol. 71:1997;7318-7327.
    • (1997) J. Virol. , vol.71 , pp. 7318-7327
    • Petti, L.M.1    Reddy, V.2    Smith, S.O.3    Dimaio, D.4
  • 274
    • 0028338904 scopus 로고
    • Cellular transformation by a transmembrane peptide: Structural requirements for the bovine papillomavirus E5 oncoprotein
    • Meyer A.N., Xu Y.-F., Webster M.K., Smith A.E., Donoghue D.J. Cellular transformation by a transmembrane peptide: Structural requirements for the bovine papillomavirus E5 oncoprotein. Proc. Natl. Acad. Sci. USA. 91:1994;4634-4638.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4634-4638
    • Meyer, A.N.1    Xu, Y.-F.2    Webster, M.K.3    Smith, A.E.4    Donoghue, D.J.5
  • 275
    • 0027397240 scopus 로고
    • Platelet-derived growth factor (PDGF) in oncogenesis: Development of a vascular connective tissue stroma in xenotransplanted human melanoma producing PDGF-BB
    • Forsberg K., Valyi-Nagy I., Heldin C.-H., Herlyn M., Westermark B. Platelet-derived growth factor (PDGF) in oncogenesis: Development of a vascular connective tissue stroma in xenotransplanted human melanoma producing PDGF-BB. Proc. Natl. Acad. Sci. USA. 90:1993;393-397.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 393-397
    • Forsberg, K.1    Valyi-Nagy, I.2    Heldin, C.-H.3    Herlyn, M.4    Westermark, B.5
  • 276
    • 0029935183 scopus 로고    scopus 로고
    • Regulation of epidermal growth factor receptor signaling by phosphorylation of the Ras exchange factor hSOS1
    • Porfiri E., McCormick F. Regulation of epidermal growth factor receptor signaling by phosphorylation of the Ras exchange factor hSOS1. J. Biol. Chem. 271:1996;5871-5877.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5871-5877
    • Porfiri, E.1    McCormick, F.2
  • 278
    • 0020804478 scopus 로고
    • Platelet-derived growth factor elicits cyclic AMP accumulation in Swiss 3T3 cells: Role of prostaglandin production
    • Rozengurt E., Stroobant P., Waterfield M.D., Deuel T.F., Keehan M. Platelet-derived growth factor elicits cyclic AMP accumulation in Swiss 3T3 cells: role of prostaglandin production. Cell. 34:1983;265-272.
    • (1983) Cell , vol.34 , pp. 265-272
    • Rozengurt, E.1    Stroobant, P.2    Waterfield, M.D.3    Deuel, T.F.4    Keehan, M.5
  • 279
    • 0030047448 scopus 로고    scopus 로고
    • Platelet-derived growth factor stimulates protein kinase A through a mitogen-activated protein kinase-dependent pathway in human arterial smooth muscle cells
    • Graves L.M., Bornfeldt K.E., Sidhu J.S., Argast G.M., Raines E.W., Ross R., Leslie C.C., Krebs E.G. Platelet-derived growth factor stimulates protein kinase A through a mitogen-activated protein kinase-dependent pathway in human arterial smooth muscle cells. J. Biol. Chem. 271:1996;505-511.
    • (1996) J. Biol. Chem. , vol.271 , pp. 505-511
    • Graves, L.M.1    Bornfeldt, K.E.2    Sidhu, J.S.3    Argast, G.M.4    Raines, E.W.5    Ross, R.6    Leslie, C.C.7    Krebs, E.G.8
  • 280
    • 0030823407 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase pathway can mediate growth inhibition and proliferation in smooth muscle cells. Dependence on the availability of downstream targets
    • Bornfeldt K.E., Campbell J.S., Koyama H., Argast G.M., Leslie C.C., Raines E.W., Krebs E.G., Ross R. The mitogen-activated protein kinase pathway can mediate growth inhibition and proliferation in smooth muscle cells. Dependence on the availability of downstream targets. J. Clin. Invest. 100:1997;875-885.
    • (1997) J. Clin. Invest. , vol.100 , pp. 875-885
    • Bornfeldt, K.E.1    Campbell, J.S.2    Koyama, H.3    Argast, G.M.4    Leslie, C.C.5    Raines, E.W.6    Krebs, E.G.7    Ross, R.8
  • 281
    • 0027374550 scopus 로고
    • Protein kinase A antagonizes platelet-derived growth factor-induced signaling by mitogen-activated protein kinase in human arterial smooth muscle cells
    • Graves L.M., Bornfeldt K.E., Raines E.W., Potts B.C., Macdonald S.G., Ross R., Krebs E.G. Protein kinase A antagonizes platelet-derived growth factor-induced signaling by mitogen-activated protein kinase in human arterial smooth muscle cells. Proc. Natl. Acad. Sci. USA. A 90:1993;10300-10304.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10300-10304
    • Graves, L.M.1    Bornfeldt, K.E.2    Raines, E.W.3    Potts, B.C.4    MacDonald, S.G.5    Ross, R.6    Krebs, E.G.7
  • 282
    • 0030610064 scopus 로고    scopus 로고
    • Cyclic AMP inhibits PDGF-stimulated mitogen-activated protein kinase activity in rat aortic smooth muscle cells via inactivation of c-Raf-1 kinase and induction of MAP kinase phosphatase-1
    • Plevin R., Malarkey K., Aidulis D., McLees A., Gould G.W. Cyclic AMP inhibits PDGF-stimulated mitogen-activated protein kinase activity in rat aortic smooth muscle cells via inactivation of c-Raf-1 kinase and induction of MAP kinase phosphatase-1. Cell. Signal. 9:1997;323-328.
    • (1997) Cell. Signal. , vol.9 , pp. 323-328
    • Plevin, R.1    Malarkey, K.2    Aidulis, D.3    McLees, A.4    Gould, G.W.5
  • 283
    • 0027501802 scopus 로고
    • CAMP antagonizes p21ras-directed activation of extracellular signal- regulated kinase 2 and phosphorylation of mSos nucleotide exchange factor
    • Burgering B.M., Pronk G.J., van Weeren P.C., Chardin P., Bos J.L. cAMP antagonizes p21ras-directed activation of extracellular signal- regulated kinase 2 and phosphorylation of mSos nucleotide exchange factor. EMBO J. 12:1993;4211-4220.
    • (1993) EMBO J. , vol.12 , pp. 4211-4220
    • Burgering, B.M.1    Pronk, G.J.2    Van Weeren, P.C.3    Chardin, P.4    Bos, J.L.5
  • 284
    • 0027772672 scopus 로고
    • Inhibition of the EGF-activated MAP kinase signaling pathway by adenosine 3′,5′-monophosphate
    • Wu J., Dent P., Jelinek T., Wolfman A., Weber M.J., Sturgill T.W. Inhibition of the EGF-activated MAP kinase signaling pathway by adenosine 3′,5′-monophosphate. Science. 262:1993;1065-1069.
    • (1993) Science , vol.262 , pp. 1065-1069
    • Wu, J.1    Dent, P.2    Jelinek, T.3    Wolfman, A.4    Weber, M.J.5    Sturgill, T.W.6
  • 285
    • 0027716596 scopus 로고
    • Inhibition by cAMP of Ras-dependent activation of Raf
    • S.J. Cook, F. McCormick, Inhibition by cAMP of Ras-dependent activation of Raf, Science 262 (1993).
    • (1993) Science , vol.262
    • Cook, S.J.1    McCormick, F.2
  • 286
    • 0029120591 scopus 로고
    • CAMP- and rapamycin-sensitive regulation of the association of eukaryotic initiation factor 4E and the translational regulator PHAS-I in aortic smooth muscle cells
    • Graves L.M., Bornfeldt K.E., Argast G.M., Krebs E.G., Kong X., Lin T.A., Lawrence J.C. Jr. cAMP- and rapamycin-sensitive regulation of the association of eukaryotic initiation factor 4E and the translational regulator PHAS-I in aortic smooth muscle cells. Proc. Natl. Acad. Sci. USA. 92:1995;7222-7226.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7222-7226
    • Graves, L.M.1    Bornfeldt, K.E.2    Argast, G.M.3    Krebs, E.G.4    Kong, X.5    Lin, T.A.6    Lawrence J.C., Jr.7
  • 287
    • 0028908804 scopus 로고
    • Activation of pp70/85 S6 kinases in interleukin-2-responsive lymphoid cells is mediated by phosphatidylinositol 3-kinase and inhibited by cyclic AMP
    • Monfar M., Lemon K.P., Grammer T.C., Cheatham L., Chung J., Vlahos C.J., Blenis J. Activation of pp70/85 S6 kinases in interleukin-2-responsive lymphoid cells is mediated by phosphatidylinositol 3-kinase and inhibited by cyclic AMP. Mol. Cell. Biol. 15:1995;326-337.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 326-337
    • Monfar, M.1    Lemon, K.P.2    Grammer, T.C.3    Cheatham, L.4    Chung, J.5    Vlahos, C.J.6    Blenis, J.7
  • 288
    • 0027941753 scopus 로고
    • Inhibition of G1 cyclin expression and G1 cyclin-dependent protein kinases by cAMP in an astrocytic cell line
    • Gagelin C., Pierre M., Toru-Delbauffe D. Inhibition of G1 cyclin expression and G1 cyclin-dependent protein kinases by cAMP in an astrocytic cell line. Biochem. Biophys. Res. Commun. 205:1994;923-929.
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 923-929
    • Gagelin, C.1    Pierre, M.2    Toru-Delbauffe, D.3
  • 289
    • 0027973043 scopus 로고
    • Cyclic AMP-induced G1 phase arrest mediated by an inhibitor (p27Kip1) of cyclin-dependent kinase 4 activation
    • Kato J.Y., Matsuoka M., Polyak K., Massagué J., Sherr C.J. Cyclic AMP-induced G1 phase arrest mediated by an inhibitor (p27Kip1) of cyclin-dependent kinase 4 activation. Cell. 79:1994;487-496.
    • (1994) Cell , vol.79 , pp. 487-496
    • Kato, J.Y.1    Matsuoka, M.2    Polyak, K.3    Massagué, J.4    Sherr, C.J.5
  • 292
    • 0027076013 scopus 로고
    • Expression of a transmembrane phosphotyrosine phosphatase inhibits cellular response to platelet-derived growh factor and insulin-like growth factor-1
    • Mooney R.A., Freund G.G., Way B.A., Bordwell K.L. Expression of a transmembrane phosphotyrosine phosphatase inhibits cellular response to platelet-derived growh factor and insulin-like growth factor-1. J. Biol. Chem. 267:1992;23443-23446.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23443-23446
    • Mooney, R.A.1    Freund, G.G.2    Way, B.A.3    Bordwell, K.L.4
  • 293
    • 0027375277 scopus 로고
    • Activation of phosphatidylinositol-3-kinase by platelet-derived growth factor and insulin-like growth factor-1 is inhibited by a transmembrane phosphotyrosine phosphatase
    • Way B.A., Mooney R.A. Activation of phosphatidylinositol-3-kinase by platelet-derived growth factor and insulin-like growth factor-1 is inhibited by a transmembrane phosphotyrosine phosphatase. J. Biol. Chem. 268:1993;26409-26415.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26409-26415
    • Way, B.A.1    Mooney, R.A.2
  • 296
    • 0023737477 scopus 로고
    • Induction of platelet-derived growth factor receptor expression in smooth muscle cells and fibroblasts upon tissue culturing
    • Terracio L., Rönnstrand L., Tingström A., Rubin K., Claesson-Welsh L., Funa K., Heldin C.-H. Induction of platelet-derived growth factor receptor expression in smooth muscle cells and fibroblasts upon tissue culturing. J. Cell Biol. 107:1988;1947-1957.
    • (1988) J. Cell Biol. , vol.107 , pp. 1947-1957
    • Terracio, L.1    Rönnstrand, L.2    Tingström, A.3    Rubin, K.4    Claesson-Welsh, L.5    Funa, K.6    Heldin, C.-H.7
  • 297
    • 0029842415 scopus 로고    scopus 로고
    • Regulation of platelet-derived growth factor receptor expression by cell context overrides regulation by cytokines
    • Barrett T.B., Seifert R.A., Bowen-Pope D.F. Regulation of platelet-derived growth factor receptor expression by cell context overrides regulation by cytokines. J. Cell. Physiol. 169:1996;126-138.
    • (1996) J. Cell. Physiol. , vol.169 , pp. 126-138
    • Barrett, T.B.1    Seifert, R.A.2    Bowen-Pope, D.F.3
  • 298
    • 0024344660 scopus 로고
    • Differential regulation of expression of two platelet-derived growth factor receptor subunits by transforming growth factor-β
    • Gronwald R.G.K., Seifert R.A., Bowen-Pope D.F. Differential regulation of expression of two platelet-derived growth factor receptor subunits by transforming growth factor-β J. Biol. Chem. 264:1989;8120-8125.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8120-8125
    • Gronwald, R.G.K.1    Seifert, R.A.2    Bowen-Pope, D.F.3
  • 300
    • 0028136094 scopus 로고
    • A unique autophosphorylation site in the platelet-derived growth factor α receptor from a heterodimeric receptor complex
    • Rupp E., Siegbahn A., Rönnstrand L., Wernstedt C., Claesson-Welsh L., Heldin C.-H. A unique autophosphorylation site in the platelet-derived growth factor α receptor from a heterodimeric receptor complex. Eur. J. Biochem. 225:1994;29-41.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 29-41
    • Rupp, E.1    Siegbahn, A.2    Rönnstrand, L.3    Wernstedt, C.4    Claesson-Welsh, L.5    Heldin, C.-H.6
  • 301
    • 0029977051 scopus 로고    scopus 로고
    • The kinase-inactive PDGF β-receptor mediates activation of the MAP kinase cascade via the endogenous PDGF α-receptor in HepG2 cells
    • Vaillancourt R.R., Gardner A.M., Kazlauskas A., Johnson G.L. The kinase-inactive PDGF β-receptor mediates activation of the MAP kinase cascade via the endogenous PDGF α-receptor in HepG2 cells. Oncogene. 13:1996;151-159.
    • (1996) Oncogene , vol.13 , pp. 151-159
    • Vaillancourt, R.R.1    Gardner, A.M.2    Kazlauskas, A.3    Johnson, G.L.4
  • 302
    • 0031022256 scopus 로고    scopus 로고
    • Anchorage-dependent cell cycle progression
    • Assoian R.K. Anchorage-dependent cell cycle progression. J. Cell Biol. 136:1997;1-4.
    • (1997) J. Cell Biol. , vol.136 , pp. 1-4
    • Assoian, R.K.1
  • 303
    • 0029948080 scopus 로고    scopus 로고
    • Stimulation of cell migration by overexpression of focal adhesion kinase and its association with Src and Fyn
    • Cary L.A., Chang J.F., Guan J.-L. Stimulation of cell migration by overexpression of focal adhesion kinase and its association with Src and Fyn. J. Cell Sci. 108:1996;1787-1794.
    • (1996) J. Cell Sci. , vol.108 , pp. 1787-1794
    • Cary, L.A.1    Chang, J.F.2    Guan, J.-L.3
  • 306
    • 0027176804 scopus 로고
    • Adhesion to fibronectin stimulates inositol lipid synthesis and enhances PDGF-induced inositol lipid breakdown
    • McNamee H.P., Ingber D.E., Schwartz M.A. Adhesion to fibronectin stimulates inositol lipid synthesis and enhances PDGF-induced inositol lipid breakdown. J. Cell Biol. 121:1993;673-678.
    • (1993) J. Cell Biol. , vol.121 , pp. 673-678
    • McNamee, H.P.1    Ingber, D.E.2    Schwartz, M.A.3
  • 307
    • 0030814976 scopus 로고    scopus 로고
    • αvβ3 integrin associates with activated insulin and PDGFβ receptors and potentiates the biological activity of PDGF
    • Schneller M., Vuori K., Ruoslahti E. αvβ3 integrin associates with activated insulin and PDGFβ receptors and potentiates the biological activity of PDGF. EMBO J. 16:1997;5600-5607.
    • (1997) EMBO J. , vol.16 , pp. 5600-5607
    • Schneller, M.1    Vuori, K.2    Ruoslahti, E.3
  • 308
    • 0029670904 scopus 로고    scopus 로고
    • 1 integrins on fibroblasts induces PDGF independent tyrosine phosphorylation of PDGF β-receptors
    • 1 integrins on fibroblasts induces PDGF independent tyrosine phosphorylation of PDGF β-receptors. J. Cell Biol. 132:1996;741-752.
    • (1996) J. Cell Biol. , vol.132 , pp. 741-752
    • Sundberg, C.1    Rubin, K.2
  • 309
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark E.A., Brugge J.S. Integrins and signal transduction pathways: the road taken. Science. 268:1995;233-239.
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 310
    • 0026674919 scopus 로고
    • Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin
    • Hanks S.K., Calalb M.B., Harper M.C., Patel S.K. Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin. Proc. Natl. Acad. Sci. USA. 89:1992;8487-8491.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8487-8491
    • Hanks, S.K.1    Calalb, M.B.2    Harper, M.C.3    Patel, S.K.4
  • 312
    • 0029947181 scopus 로고    scopus 로고
    • Requirement for phosphatidylinositol 3′-kinase activity in platelet-derived growth factor-stimulated tyrosine phosphorylation of p125 focal adhesion kinase and paxillin
    • Rankin S., Hooshmand-Rad R., Claesson-Welsh L., Rozengurt E. Requirement for phosphatidylinositol 3′-kinase activity in platelet-derived growth factor-stimulated tyrosine phosphorylation of p125 focal adhesion kinase and paxillin. J. Biol. Chem. 271:1996;7829-7834.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7829-7834
    • Rankin, S.1    Hooshmand-Rad, R.2    Claesson-Welsh, L.3    Rozengurt, E.4
  • 313
    • 0029833286 scopus 로고    scopus 로고
    • Platelet-derived growth factor-induced formation of tensin and phosphoinositide 3-kinase complexes
    • Auger K.R., Songyang Z., Lo S.H., Roberts T.M., Chen L.B. Platelet-derived growth factor-induced formation of tensin and phosphoinositide 3-kinase complexes. J. Biol. Chem. 271:1996;23452-23457.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23452-23457
    • Auger, K.R.1    Songyang, Z.2    Lo, S.H.3    Roberts, T.M.4    Chen, L.B.5
  • 315
    • 0027292231 scopus 로고
    • Decreased level of PDGF-stimulated receptor autophosphorylation by fibroblasts in mechanically relaxed collagen matrices
    • Lin Y.-C., Grinnell F. Decreased level of PDGF-stimulated receptor autophosphorylation by fibroblasts in mechanically relaxed collagen matrices. J. Cell Biol. 122:1993;663-672.
    • (1993) J. Cell Biol. , vol.122 , pp. 663-672
    • Lin, Y.-C.1    Grinnell, F.2
  • 316
    • 0027997094 scopus 로고
    • 2-subunit in human diploid fibroblasts
    • 2-subunit in human diploid fibroblasts. Exp. Cell Res. 215:1994;347-353.
    • (1994) Exp. Cell Res. , vol.215 , pp. 347-353
    • Åhlén, K.1    Rubin, K.2
  • 317
    • 0028978783 scopus 로고
    • 1 integrin synthesis by recombinant platelet-derived growth factor (PDGF-AB) correlates with an enhanced migratory response of human dermal fibroblasts to various extracellular matrix proteins
    • 1 integrin synthesis by recombinant platelet-derived growth factor (PDGF-AB) correlates with an enhanced migratory response of human dermal fibroblasts to various extracellular matrix proteins. Exp. Cell Res. 220:1995;29-35.
    • (1995) Exp. Cell Res. , vol.220 , pp. 29-35
    • Kirchberg, K.1    Lange, T.S.2    Klein, E.C.3    Jungtäubl, H.4    Heinen, G.5    Meyer-Ingold, W.6    Scharffetter-Kochanek, K.7
  • 318
    • 0030023905 scopus 로고    scopus 로고
    • Extracellular matrix alters PDGF regulation of fibroblast integrins
    • Xu J., Clark R.A.F. Extracellular matrix alters PDGF regulation of fibroblast integrins. J. Cell Biol. 132:1996;239-249.
    • (1996) J. Cell Biol. , vol.132 , pp. 239-249
    • Xu, J.1    Clark, R.A.F.2
  • 319
    • 0029879507 scopus 로고    scopus 로고
    • Localization of platelet-derived growth factor-stimulated phosphorylation cascade to caveolae
    • Liu P., Ying Y., Ko Y.-G., Anderson R.G.W. Localization of platelet-derived growth factor-stimulated phosphorylation cascade to caveolae. J. Biol. Chem. 271:1996;10299-10303.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10299-10303
    • Liu, P.1    Ying, Y.2    Ko, Y.-G.3    Anderson, R.G.W.4
  • 320
    • 0343035665 scopus 로고    scopus 로고
    • Aggregation of PDGF-β receptors in human skin fibroblasts: Characterization by image correlation spectroscopy (ICS)
    • Wiseman P.W., Höddelius P., Petersen N.O., Magnusson K.-E. Aggregation of PDGF-β receptors in human skin fibroblasts: characterization by image correlation spectroscopy (ICS). FEBS Lett. 401:1997;43-48.
    • (1997) FEBS Lett. , vol.401 , pp. 43-48
    • Wiseman, P.W.1    Höddelius, P.2    Petersen, N.O.3    Magnusson, K.-E.4
  • 321
    • 0019983285 scopus 로고
    • Interaction of platelet-derived growth factor with its fibroblast receptor. Demonstration of ligand degradation and receptor modulation
    • Heldin C.-H., Wasteson Å., Westermark B. Interaction of platelet-derived growth factor with its fibroblast receptor. Demonstration of ligand degradation and receptor modulation. J. Biol. Chem. 257:1982;4216-4221.
    • (1982) J. Biol. Chem. , vol.257 , pp. 4216-4221
    • Heldin, C.-H.1    Wasteson, Å.2    Westermark, B.3
  • 322
    • 0025971082 scopus 로고
    • Effect of receptor kinase inactivation on the rate of internalization and degradation of PDGF and the PDGF β-receptor
    • Sorkin A., Westermark B., Heldin C.-H., Claesson-Welsh L. Effect of receptor kinase inactivation on the rate of internalization and degradation of PDGF and the PDGF β-receptor. J. Cell Biol. 112:1991;469-478.
    • (1991) J. Cell Biol. , vol.112 , pp. 469-478
    • Sorkin, A.1    Westermark, B.2    Heldin, C.-H.3    Claesson-Welsh, L.4
  • 323
    • 0026664626 scopus 로고
    • Ligand-induced polyubiquitination of the platelet-derived growth factor β-receptor
    • Mori S., Heldin C.-H., Claesson-Welsh L. Ligand-induced polyubiquitination of the platelet-derived growth factor β-receptor. J. Biol. Chem. 267:1992;6429-6434.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6429-6434
    • Mori, S.1    Heldin, C.-H.2    Claesson-Welsh, L.3
  • 324
    • 0028788180 scopus 로고
    • Degradation process of ligand-stimulated platelet-derived growth factor β-receptor involves ubiquitin-proteasome proteolytic pathway
    • Mori S., Tanaka K., Omura S., Saito Y. Degradation process of ligand-stimulated platelet-derived growth factor β-receptor involves ubiquitin-proteasome proteolytic pathway. J. Biol. Chem. 270:1995;29447-29452.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29447-29452
    • Mori, S.1    Tanaka, K.2    Omura, S.3    Saito, Y.4
  • 325
    • 0027235878 scopus 로고
    • Pool of ligand-bound platelet-derived growth factor β-receptors remain activated and tyrosine phosphorylated after internalization
    • Sorkin A., Eriksson A., Heldin C.-H., Westermark B., Claesson-Welsh L. Pool of ligand-bound platelet-derived growth factor β-receptors remain activated and tyrosine phosphorylated after internalization. J. Cell. Physiol. 156:1993;373-382.
    • (1993) J. Cell. Physiol. , vol.156 , pp. 373-382
    • Sorkin, A.1    Eriksson, A.2    Heldin, C.-H.3    Westermark, B.4    Claesson-Welsh, L.5
  • 326
    • 0027997221 scopus 로고
    • A tyrosine residue in the juxtamembrane segment of the platelet-derived growth factor β-receptor is critical for ligand-mediated endocytosis
    • Mori S., Rönnstrand L., Claesson-Welsh L., Heldin C.-H. A tyrosine residue in the juxtamembrane segment of the platelet-derived growth factor β-receptor is critical for ligand-mediated endocytosis. J. Biol. Chem. 269:1994;4917-4921.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4917-4921
    • Mori, S.1    Rönnstrand, L.2    Claesson-Welsh, L.3    Heldin, C.-H.4
  • 327
    • 0028351218 scopus 로고
    • Disruption of PDGF receptor trafficking by mutation of its PI-3 kinase binding sites
    • Joly M., Kazlauskas A., Fay F.S., Corvera S. Disruption of PDGF receptor trafficking by mutation of its PI-3 kinase binding sites. Science. 263:1994;684-687.
    • (1994) Science , vol.263 , pp. 684-687
    • Joly, M.1    Kazlauskas, A.2    Fay, F.S.3    Corvera, S.4
  • 328
    • 0025885433 scopus 로고
    • Identification of a hydrophobic region in the carboxyl terminus of the platelet-derived growth factor β-receptor which is important for ligand-mediated endocytosis
    • Mori S., Claesson-Welsh L., Heldin C.-H. Identification of a hydrophobic region in the carboxyl terminus of the platelet-derived growth factor β-receptor which is important for ligand-mediated endocytosis. J. Biol. Chem. 266:1991;21158-21164.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21158-21164
    • Mori, S.1    Claesson-Welsh, L.2    Heldin, C.-H.3
  • 329
    • 0021811642 scopus 로고
    • Similar action of platelet-derived growth factor and epidermal growth factor in the prereplicative phase of human fibroblasts suggests a common intracellular pathway
    • Westermark B., Heldin C.-H. Similar action of platelet-derived growth factor and epidermal growth factor in the prereplicative phase of human fibroblasts suggests a common intracellular pathway. J. Cell. Physiol. 124:1985;43-48.
    • (1985) J. Cell. Physiol. , vol.124 , pp. 43-48
    • Westermark, B.1    Heldin, C.-H.2
  • 330
    • 0027402689 scopus 로고
    • Ligand-induced ubiquitination of the platelet-derived growth factor β-receptor plays a negative regulatory role in its mitogenic signaling
    • Mori S., Heldin C.-H., Claesson-Welsh L. Ligand-induced ubiquitination of the platelet-derived growth factor β-receptor plays a negative regulatory role in its mitogenic signaling. J. Biol. Chem. 268:1993;577-583.
    • (1993) J. Biol. Chem. , vol.268 , pp. 577-583
    • Mori, S.1    Heldin, C.-H.2    Claesson-Welsh, L.3
  • 331
    • 0029766539 scopus 로고    scopus 로고
    • Detergent solubility defines an alternative itinerary for a subpopulation of PDGF β receptors
    • Coats S.R., Pledger W.J., Awazu M., Daniel T.O. Detergent solubility defines an alternative itinerary for a subpopulation of PDGF β receptors. J. Cell. Physiol. 168:1996;412-423.
    • (1996) J. Cell. Physiol. , vol.168 , pp. 412-423
    • Coats, S.R.1    Pledger, W.J.2    Awazu, M.3    Daniel, T.O.4
  • 332
    • 0026418308 scopus 로고
    • Inhibition of neointimal smooth muscle accumulation after angioplasty by an antibody to PDGF
    • Ferns G.A.A., Raines E.W., Sprugel K.H., Motani A.S., Reidy M.A., Ross R. Inhibition of neointimal smooth muscle accumulation after angioplasty by an antibody to PDGF. Science. 253:1991;1129-1132.
    • (1991) Science , vol.253 , pp. 1129-1132
    • Ferns, G.A.A.1    Raines, E.W.2    Sprugel, K.H.3    Motani, A.S.4    Reidy, M.A.5    Ross, R.6
  • 333
    • 0030990547 scopus 로고    scopus 로고
    • Substantial inhibition of neo-intimal response to balloon injury in the rat carotid artery using a combination of antibodies to platelet-derived growth factor-BB and basic fibroblast growth factor
    • Rutherford C., Martin W., Salame M., Carrier M., Änggård E., Ferns G. Substantial inhibition of neo-intimal response to balloon injury in the rat carotid artery using a combination of antibodies to platelet-derived growth factor-BB and basic fibroblast growth factor. Atherosclerosis. 130:1997;45-51.
    • (1997) Atherosclerosis , vol.130 , pp. 45-51
    • Rutherford, C.1    Martin, W.2    Salame, M.3    Carrier, M.4    Änggård, E.5    Ferns, G.6
  • 334
    • 0025107374 scopus 로고
    • Localization of platelet-derived growth factor (PDGF) in CHO cells transfected with PDGF A- or B-chain cDNA: Retention of PDGF-BB in the endoplasmic reticulum and Golgi complex
    • Thyberg J., Östman A., Bäckström G., Westermark B., Heldin C.-H. Localization of platelet-derived growth factor (PDGF) in CHO cells transfected with PDGF A- or B-chain cDNA: retention of PDGF-BB in the endoplasmic reticulum and Golgi complex. J. Cell Sci. 97:1990;219-229.
    • (1990) J. Cell Sci. , vol.97 , pp. 219-229
    • Thyberg, J.1    Östman, A.2    Bäckström, G.3    Westermark, B.4    Heldin, C.-H.5
  • 335
    • 0024992559 scopus 로고
    • A monoclonal antibody against PDGF B-chain inhibits PDGF-induced DNA synthesis in C3H fibroblasts and prevents binding of PDGF to its receptor
    • Vassbotn F.S., Langeland N., Hagen I., Holmsen H. A monoclonal antibody against PDGF B-chain inhibits PDGF-induced DNA synthesis in C3H fibroblasts and prevents binding of PDGF to its receptor. Biochim. Biophys. Acta. 1054:1990;246-249.
    • (1990) Biochim. Biophys. Acta , vol.1054 , pp. 246-249
    • Vassbotn, F.S.1    Langeland, N.2    Hagen, I.3    Holmsen, H.4
  • 336
    • 0028268686 scopus 로고
    • Production of platelet-derived growth factor receptor (PDGFR-beta) in E. coli: Mapping ligand binding domain
    • Rooney B.C., Hosang M., Hunziker W. Production of platelet-derived growth factor receptor (PDGFR-beta) in E. coli: mapping ligand binding domain. FEBS Lett. 339:1994;181-184.
    • (1994) FEBS Lett. , vol.339 , pp. 181-184
    • Rooney, B.C.1    Hosang, M.2    Hunziker, W.3
  • 338
    • 0029819129 scopus 로고    scopus 로고
    • Gangliosides GM1, GM2 and GM3 inhibit the platelet-derived growth factor-induced signalling transduction pathway in vascular smooth muscle cells by different mechanisms
    • Sachinidis A., Kraus R., Seul C., Zu Brickwedde M.K.M., Schulte K., Ko Y., Hoppe J., Vetter H. Gangliosides GM1, GM2 and GM3 inhibit the platelet-derived growth factor-induced signalling transduction pathway in vascular smooth muscle cells by different mechanisms. Eur. J. Cell Biol. 71:1996;79-88.
    • (1996) Eur. J. Cell Biol. , vol.71 , pp. 79-88
    • Sachinidis, A.1    Kraus, R.2    Seul, C.3    Zu Brickwedde, M.K.M.4    Schulte, K.5    Ko, Y.6    Hoppe, J.7    Vetter, H.8
  • 339
    • 0028214075 scopus 로고
    • Inhibition of PDGF receptor binding and PDGF-stimulated biological activity in vitro and of intimal lesion formation in vivo by 2-bromomethyl-5-chl orobenzene sulfonylphthalimide
    • Mullins D.E., Hamud F., Reim R., Davis H.R. Inhibition of PDGF receptor binding and PDGF-stimulated biological activity in vitro and of intimal lesion formation in vivo by 2-bromomethyl-5-chl orobenzene sulfonylphthalimide. Arterioscleros. Thromb. 14:1994;1047-1055.
    • (1994) Arterioscleros. Thromb. , vol.14 , pp. 1047-1055
    • Mullins, D.E.1    Hamud, F.2    Reim, R.3    Davis, H.R.4
  • 340
    • 0027185832 scopus 로고
    • A novel monoclonal antibody dependent on domain 5 of the platelet-derived growth factor beta receptor inhibits ligand binding and receptor activation
    • Ramakrishnan V., Escobedo M.-A., Fretto L.J., Seroogy J.J., Tomlinson J.E., Wolf D.L. A novel monoclonal antibody dependent on domain 5 of the platelet-derived growth factor beta receptor inhibits ligand binding and receptor activation. Growth Factors. 8:1993;253-265.
    • (1993) Growth Factors , vol.8 , pp. 253-265
    • Ramakrishnan, V.1    Escobedo, M.-A.2    Fretto, L.J.3    Seroogy, J.J.4    Tomlinson, J.E.5    Wolf, D.L.6
  • 341
    • 0027634192 scopus 로고
    • Inhibition of platelet-derived growth factor autocrine growth stimulation by a monoclonal antibody to the human α platelet-derived growth factor receptor
    • LaRochelle W.J., Jensen R.A., Heidaran M.A., May-Siroff M., Wang L.-M., Aaronson S.A., Pierce J.H. Inhibition of platelet-derived growth factor autocrine growth stimulation by a monoclonal antibody to the human α platelet-derived growth factor receptor. Cell Growth Differ. 4:1993;547-553.
    • (1993) Cell Growth Differ. , vol.4 , pp. 547-553
    • Larochelle, W.J.1    Jensen, R.A.2    Heidaran, M.A.3    May-Siroff, M.4    Wang, L.-M.5    Aaronson, S.A.6    Pierce, J.H.7
  • 343
    • 0030805072 scopus 로고    scopus 로고
    • Identification of a cyclic peptide inhibitor of platelet-derived growth factor-BB receptor-binding and mitogen-induced DNA synthesis in human fibroblasts
    • Brennand D.M., Dennehy U., Ellis V., Scully M.F., Tripathi P., Kakkar V.V., Patel G. Identification of a cyclic peptide inhibitor of platelet-derived growth factor-BB receptor-binding and mitogen-induced DNA synthesis in human fibroblasts. FEBS Lett. 413:1997;70-74.
    • (1997) FEBS Lett. , vol.413 , pp. 70-74
    • Brennand, D.M.1    Dennehy, U.2    Ellis, V.3    Scully, M.F.4    Tripathi, P.5    Kakkar, V.V.6    Patel, G.7
  • 344
    • 0021327281 scopus 로고
    • Platelet-derived growth factor receptors form a high affinity state in membrane preparations
    • Williams L.T., Tremble P.M., Lavin M.F., Sunday M.E. Platelet-derived growth factor receptors form a high affinity state in membrane preparations. J. Biol. Chem. 259:1984;5287-5294.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5287-5294
    • Williams, L.T.1    Tremble, P.M.2    Lavin, M.F.3    Sunday, M.E.4
  • 345
    • 0020464965 scopus 로고
    • A new approach to treatment of atherosclerosis and trapidil as an antagonist to platelet-derived growth factor
    • Ohnishi H., Yamaguchi K., Shimada S., Suzuki Y., Kumagai A. A new approach to treatment of atherosclerosis and trapidil as an antagonist to platelet-derived growth factor. Life Sci. 31:1982;2595-2602.
    • (1982) Life Sci. , vol.31 , pp. 2595-2602
    • Ohnishi, H.1    Yamaguchi, K.2    Shimada, S.3    Suzuki, Y.4    Kumagai, A.5
  • 347
    • 0028968949 scopus 로고
    • Tyrosine kinase inhibition: An approach to drug development
    • Levitzki A., Gazit A. Tyrosine kinase inhibition: an approach to drug development. Science. 267:1995;1782-1788.
    • (1995) Science , vol.267 , pp. 1782-1788
    • Levitzki, A.1    Gazit, A.2
  • 349
    • 0029899585 scopus 로고    scopus 로고
    • Tyrphostins. 5. Potent inhibitors of platelet-derived growth factor receptor tyrosine kinase: Structure-activity relationships in quinoxalines, quinolines, and indole tyrphostins
    • Gazit A., App H., McMahon G., Chen J., Levitzki A., Böhmer F.D. Tyrphostins. 5. Potent inhibitors of platelet-derived growth factor receptor tyrosine kinase: structure-activity relationships in quinoxalines, quinolines, and indole tyrphostins. J. Med. Chem. 39:1996;2170-2177.
    • (1996) J. Med. Chem. , vol.39 , pp. 2170-2177
    • Gazit, A.1    App, H.2    McMahon, G.3    Chen, J.4    Levitzki, A.5    Böhmer, F.D.6
  • 350
    • 0028968622 scopus 로고
    • Selective inhibition of the platelet-derived growth factor signal transduction pathway by a protein-tyrosine kinase inhibitor of the 2-phenylaminopyrimidine class
    • Buchdunger E., Zimmermann J., Mett H., Meyer T., Müller M., Regenass U., Lydon N.B. Selective inhibition of the platelet-derived growth factor signal transduction pathway by a protein-tyrosine kinase inhibitor of the 2-phenylaminopyrimidine class. Proc. Natl. Acad. Sci. USA. 92:1995;2558-2562.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2558-2562
    • Buchdunger, E.1    Zimmermann, J.2    Mett, H.3    Meyer, T.4    Müller, M.5    Regenass, U.6    Lydon, N.B.7
  • 353
    • 0028243048 scopus 로고
    • A new series of PDGF receptor tyrosine kinase inhibitors: 3-substituted quinoline derivatives
    • Maguire M.P., Sheets K.R., McVety K., Spada A.P., Zilberstein A. A new series of PDGF receptor tyrosine kinase inhibitors: 3-substituted quinoline derivatives. J. Med. Chem. 37:1994;2129-2137.
    • (1994) J. Med. Chem. , vol.37 , pp. 2129-2137
    • Maguire, M.P.1    Sheets, K.R.2    McVety, K.3    Spada, A.P.4    Zilberstein, A.5
  • 356
    • 0029926493 scopus 로고    scopus 로고
    • Platelet-derived growth factor receptor tyrosine phosphorylation requires protein geranylgeranylation but not farnesylation
    • McGuire T.F., Qian Y.M., Vogt A., Hamilton A.D., Sebti S.M. Platelet-derived growth factor receptor tyrosine phosphorylation requires protein geranylgeranylation but not farnesylation. J. Biol. Chem. 271:1996;27402-27407.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27402-27407
    • McGuire, T.F.1    Qian, Y.M.2    Vogt, A.3    Hamilton, A.D.4    Sebti, S.M.5
  • 357
    • 0028309545 scopus 로고
    • Preferential inhibition of platelet-derived growth factor-stimulated DNA synthesis and protein tyrosine phosphorylation by nordihydroguaiaretic acid
    • Domin J., Higgins T., Rozengurt E. Preferential inhibition of platelet-derived growth factor-stimulated DNA synthesis and protein tyrosine phosphorylation by nordihydroguaiaretic acid. J. Biol. Chem. 269:1994;8260-8267.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8260-8267
    • Domin, J.1    Higgins, T.2    Rozengurt, E.3
  • 359
    • 0027159221 scopus 로고
    • Reversion of autocrine transformation by a dominant negative platelet-derived growth factor mutant
    • Vassbotn F.S., Andersson M., Westermark B., Heldin C.-H., Östman A. Reversion of autocrine transformation by a dominant negative platelet-derived growth factor mutant. Mol. Cell. Biol. 13:1993;4066-4076.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4066-4076
    • Vassbotn, F.S.1    Andersson, M.2    Westermark, B.3    Heldin, C.-H.4    Östman, A.5
  • 360
    • 0025734507 scopus 로고
    • Inhibition of PDGF β receptor signal transduction by coexpression of a truncated receptor
    • Ueno H., Colbert H., Escobedo J.A., Williams L.T. Inhibition of PDGF β receptor signal transduction by coexpression of a truncated receptor. Science. 252:1991;844-848.
    • (1991) Science , vol.252 , pp. 844-848
    • Ueno, H.1    Colbert, H.2    Escobedo, J.A.3    Williams, L.T.4
  • 361
    • 0027241856 scopus 로고
    • The pathogenesis of atherosclerosis: A perspective for the 1990s
    • Ross R. The pathogenesis of atherosclerosis: a perspective for the 1990s. Nature. 362:1993;801-809.
    • (1993) Nature , vol.362 , pp. 801-809
    • Ross, R.1
  • 362
    • 0031058702 scopus 로고    scopus 로고
    • Antisense oligonucleotide inhibition of PDGFR-β receptor subunit expression directs suppression of intimal thickening
    • Sirois M.G., Simons M., Edelman E.R. Antisense oligonucleotide inhibition of PDGFR-β receptor subunit expression directs suppression of intimal thickening. Circulation. 95:1997;669-676.
    • (1997) Circulation , vol.95 , pp. 669-676
    • Sirois, M.G.1    Simons, M.2    Edelman, E.R.3
  • 364
    • 0027232199 scopus 로고
    • Growth factors in glomerulonephritis
    • Abboud H.E. Growth factors in glomerulonephritis. Kidney Int. 43:1993;252-267.
    • (1993) Kidney Int. , vol.43 , pp. 252-267
    • Abboud, H.E.1
  • 365
    • 0026562550 scopus 로고
    • Inhibition of mesangial cell proliferation and matrix expansion in glomerulonephritis in the rat by antibody to platelet-derived growth factor
    • Johnson R.J., Raines E.W., Floege J., Yoshimura A., Pritzl P., Alpers C., Ross R. Inhibition of mesangial cell proliferation and matrix expansion in glomerulonephritis in the rat by antibody to platelet-derived growth factor. J. Exp. Med. 175:1992;1413-1416.
    • (1992) J. Exp. Med. , vol.175 , pp. 1413-1416
    • Johnson, R.J.1    Raines, E.W.2    Floege, J.3    Yoshimura, A.4    Pritzl, P.5    Alpers, C.6    Ross, R.7
  • 366
    • 0027361809 scopus 로고
    • Dominant-negative mutants of platelet-derived growth factor revert the transformed phenotype of human astrocytoma cells
    • Shamah S.M., Stiles C.D., Guha A. Dominant-negative mutants of platelet-derived growth factor revert the transformed phenotype of human astrocytoma cells. Mol. Cell. Biol. 13:1993;7203-7212.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7203-7212
    • Shamah, S.M.1    Stiles, C.D.2    Guha, A.3
  • 368
    • 0027952893 scopus 로고
    • Activated platelet-derived growth factor autocrine pathway drives the transformed phenotype of a human glioblastoma cell line
    • Vassbotn F.S., Östman A., Langeland N., Holmsen H., Westermark B., Heldin C.-H., Nistér M. Activated platelet-derived growth factor autocrine pathway drives the transformed phenotype of a human glioblastoma cell line. J. Cell. Physiol. 158:1994;381-389.
    • (1994) J. Cell. Physiol. , vol.158 , pp. 381-389
    • Vassbotn, F.S.1    Östman, A.2    Langeland, N.3    Holmsen, H.4    Westermark, B.5    Heldin, C.-H.6    Nistér, M.7
  • 369
    • 0030297362 scopus 로고    scopus 로고
    • Platelet-derived growth factor is an autocrine stimulator for the growth and survival of human esophageal carcinoma cell lines
    • Liu Y.C., Chen S.C., Chang C.M., Leu C.M., Hu C.P. Platelet-derived growth factor is an autocrine stimulator for the growth and survival of human esophageal carcinoma cell lines. Exp. Cell Res. 228:1996;206-211.
    • (1996) Exp. Cell Res. , vol.228 , pp. 206-211
    • Liu, Y.C.1    Chen, S.C.2    Chang, C.M.3    Leu, C.M.4    Hu, C.P.5


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