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Volumn 7, Issue 1, 1997, Pages 80-86

Novel mechanisms of RTK signal generation

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; GUANINE NUCLEOTIDE BINDING PROTEIN; PROTEIN TYROSINE KINASE;

EID: 0031059530     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-437X(97)80113-X     Document Type: Article
Times cited : (106)

References (50)
  • 2
    • 0028023922 scopus 로고
    • Receptor tyrosine kinases as targets for drug intervention
    • Plowman GD, Ullrich A, Shawver LK. Receptor tyrosine kinases as targets for drug intervention. Drug News Perspect. 7:1994;334-339.
    • (1994) Drug News Perspect , vol.7 , pp. 334-339
    • Plowman, G.D.1    Ullrich, A.2    Shawver, L.K.3
  • 3
    • 0028104202 scopus 로고
    • Regulation of signal transduction and signal diversity by receptor oligomerization
    • Lemmon MA, Schlessinger J. Regulation of signal transduction and signal diversity by receptor oligomerization. Trends Biochem Sci. 19:1994;459-464.
    • (1994) Trends Biochem Sci , vol.19 , pp. 459-464
    • Lemmon, M.A.1    Schlessinger, J.2
  • 4
    • 0027903152 scopus 로고
    • Cellular signaling by receptor tyrosine kinases
    • Schlessinger J. Cellular signaling by receptor tyrosine kinases. Harvey Lect. 89:1995;105-123.
    • (1995) Harvey Lect , vol.89 , pp. 105-123
    • Schlessinger, J.1
  • 5
    • 0028170817 scopus 로고
    • Receptor protein tyrosine kinases and their signal transduction pathways
    • Van der Geer P, Hunter T. Receptor protein tyrosine kinases and their signal transduction pathways. Annu Rev Cell Biol. 10:1994;251-337.
    • (1994) Annu Rev Cell Biol , vol.10 , pp. 251-337
    • Van Der Geer, P.1    Hunter, T.2
  • 6
    • 0028895654 scopus 로고
    • Modular binding domains in signal transduction proteins
    • Cohen GB, Ren R, Baltimore D. Modular binding domains in signal transduction proteins. Cell. 80:1995;237-248.
    • (1995) Cell , vol.80 , pp. 237-248
    • Cohen, G.B.1    Ren, R.2    Baltimore, D.3
  • 7
    • 0029935418 scopus 로고    scopus 로고
    • Regulation of transcription by MAP kinase cascades
    • Treisman R. Regulation of transcription by MAP kinase cascades. Curr Opin Cell Biol. 8:1996;205-215.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 205-215
    • Treisman, R.1
  • 8
    • 0029010607 scopus 로고
    • Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved flourescence imaging microscopy. A stereo-chemical model for tyrosine kinase receptor activation
    • Gadella TWJ Jr, Jovin TM. Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved flourescence imaging microscopy. A stereo-chemical model for tyrosine kinase receptor activation. J Cell Biol. 129:1995;1543-1558.
    • (1995) J Cell Biol , vol.129 , pp. 1543-1558
    • Gadella T.W.J., Jr.1    Jovin, T.M.2
  • 9
    • 0028838012 scopus 로고
    • Dimerization of cell surface receptors in signal transduction
    • Heldin CH. Dimerization of cell surface receptors in signal transduction. Cell. 80:1995;213-223.
    • (1995) Cell , vol.80 , pp. 213-223
    • Heldin, C.H.1
  • 10
    • 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
  • 11
    • 0029021518 scopus 로고
    • Heterodimerizatiion and functional interaction between EGF receptor family members: A new signaling paradigm with implications for breast cancer research
    • Earp HS, Dawson TL, Li X, Yu H. Heterodimerizatiion and functional interaction between EGF receptor family members: a new signaling paradigm with implications for breast cancer research. Breast Cancer Res Treat. 35:1995;115-132.
    • (1995) Breast Cancer Res Treat , vol.35 , pp. 115-132
    • Earp, H.S.1    Dawson, T.L.2    Li, X.3    Yu, H.4
  • 13
    • 0029814271 scopus 로고    scopus 로고
    • A hierarchical network of interreceptor interactions determines signal transduction by Neu differentiation factor/Neuregulin and epidermal growth factor
    • of special interest. In this comprehensive study, ectopic expression of individual HER proteins on their combinations in CHO cells are utilized to analyse the hierarchy of interreceptor interactions. Ligand-binding affinities, receptor transphosphorylation and induction of DNA synthesis are determined. Although HER2 binds neither ligand, even in the heterodimeric complex, it is found to be the preferred heterodimerizatiion partner of the three HER-receptors.
    • Tzahar E, Waterman H, Chen X, Levkowitz G, Karunagaran D, Lavi S, Ratzkin B, Yarden Y. A hierarchical network of interreceptor interactions determines signal transduction by Neu differentiation factor/Neuregulin and epidermal growth factor. of special interest Mol Cell Biol. 16:1996;5276-5287 In this comprehensive study, ectopic expression of individual HER proteins on their combinations in CHO cells are utilized to analyse the hierarchy of interreceptor interactions. Ligand-binding affinities, receptor transphosphorylation and induction of DNA synthesis are determined. Although HER2 binds neither ligand, even in the heterodimeric complex, it is found to be the preferred heterodimerizatiion partner of the three HER-receptors.
    • (1996) Mol Cell Biol , vol.16 , pp. 5276-5287
    • Tzahar, E.1    Waterman, H.2    Chen, X.3    Levkowitz, G.4    Karunagaran, D.5    Lavi, S.6    Ratzkin, B.7    Yarden, Y.8
  • 16
    • 0029118223 scopus 로고
    • The cellular response to neuregulins is governed by complex interactions of the erbB receptor family
    • Riese DJ II, Van Raaij TM, Plowman GD, Andrews GC, Stern DF. The cellular response to neuregulins is governed by complex interactions of the erbB receptor family. Mol Cell Biol. 15:1995;5770-5776.
    • (1995) Mol Cell Biol , vol.15 , pp. 5770-5776
    • Riese D.J. II1    Van Raaij, T.M.2    Plowman, G.D.3    Andrews, G.C.4    Stern, D.F.5
  • 17
    • 0028205406 scopus 로고
    • Kinase-deficient neu proteins suppress epidermal growth factor receptor function and abolish cell transformation
    • Qian X, Dougall WC, Hellman ME, Greene MI. Kinase-deficient neu proteins suppress epidermal growth factor receptor function and abolish cell transformation. Oncogene. 9:1994;1507-1514.
    • (1994) Oncogene , vol.9 , pp. 1507-1514
    • Qian, X.1    Dougall, W.C.2    Hellman, M.E.3    Greene, M.I.4
  • 18
    • 0029162564 scopus 로고
    • Heregulin-dependent regulation of HER2/neu oncogenic signalling by heterodimerization with HER3
    • of special interest. Using kinase-inactive mutants of HER2 and HER3, we could show in transient or stably transfected fibroblasts that ligand-induced activation of the heterodimeric HER2/HER3 complex, as well as the induction of a mitogenic response, is critically dependent on the kinase activity of HER2. Signal transduction of transphosphorylated HER3 subsequently involves recruitment of SHC and PI-3 kinase.
    • Wallasch C, Weiss FU, Niederfellner G, Issing W, Ullrich A. Heregulin-dependent regulation of HER2/neu oncogenic signalling by heterodimerization with HER3. of special interest EMBO J. 14:1995;4267-4275 Using kinase-inactive mutants of HER2 and HER3, we could show in transient or stably transfected fibroblasts that ligand-induced activation of the heterodimeric HER2/HER3 complex, as well as the induction of a mitogenic response, is critically dependent on the kinase activity of HER2. Signal transduction of transphosphorylated HER3 subsequently involves recruitment of SHC and PI-3 kinase.
    • (1995) EMBO J , vol.14 , pp. 4267-4275
    • Wallasch, C.1    Weiss, F.U.2    Niederfellner, G.3    Issing, W.4    Ullrich, A.5
  • 19
    • 0028117163 scopus 로고
    • Cytokine signal transduction
    • Kishimoto T, Taga T, Akira S. Cytokine signal transduction. Cell. 76:1994;253-262.
    • (1994) Cell , vol.76 , pp. 253-262
    • Kishimoto, T.1    Taga, T.2    Akira, S.3
  • 20
    • 0029394757 scopus 로고
    • Towards unraveling the complexity of T cell signal transduction
    • Zenner G, Dirk zur Hausen J, Burn P, Mustein T. Towards unraveling the complexity of T cell signal transduction. Bioessays. 17:1995;967-975.
    • (1995) Bioessays , vol.17 , pp. 967-975
    • Zenner, G.1    Dirk Zur Hausen, J.2    Burn, P.3    Mustein, T.4
  • 21
    • 0029866079 scopus 로고    scopus 로고
    • HER4-mediated biological and biochemical properties in NIH3T3 cells
    • Cohen BD, Green JM, Foy L, Fell HP. HER4-mediated biological and biochemical properties in NIH3T3 cells. J Biol Chem. 271:1996;4813-4818.
    • (1996) J Biol Chem , vol.271 , pp. 4813-4818
    • Cohen, B.D.1    Green, J.M.2    Foy, L.3    Fell, H.P.4
  • 22
    • 0027971393 scopus 로고
    • ErbB-3 and ErbB-4 Function as the respective low and high affinity receptors of all neu differentiation factor/heregulin isoforms
    • Tzahar E, Levkowitz G, Karunagaran D, Yi L, Peles E, Lavi S, Chang D, Yayon A, Wen D, Yarden Y. ErbB-3 and ErbB-4 Function as the respective low and high affinity receptors of all neu differentiation factor/heregulin isoforms. J Biol Chem. 269:1994;25226-25233.
    • (1994) J Biol Chem , vol.269 , pp. 25226-25233
    • Tzahar, E.1    Levkowitz, G.2    Karunagaran, D.3    Yi, L.4    Peles, E.5    Lavi, S.6    Chang, D.7    Yayon, A.8    Wen, D.9    Yarden, Y.10
  • 23
    • 13344284648 scopus 로고    scopus 로고
    • An immunological approach reveals biological differences between the two NDF/heregulin receptors, ErbB-3 and ErbB-4
    • of special interest. Using two sets of monoclonal antibodies to HER3 or HER4, it is shown that HER4 homodimers are biological active whereas HER3 requires heterodimerization, probably with HER2, for transmission of neuregulin signals.
    • Chen X, Levkowitz G, Tzahar E, Karunagaran D, Lavi S, Ben-Baruch N, Leitner O, Ratzkin BJ, Bacus SS, Yarden Y. An immunological approach reveals biological differences between the two NDF/heregulin receptors, ErbB-3 and ErbB-4. of special interest J Biol Chem. 271:1996;7620-7629 Using two sets of monoclonal antibodies to HER3 or HER4, it is shown that HER4 homodimers are biological active whereas HER3 requires heterodimerization, probably with HER2, for transmission of neuregulin signals.
    • (1996) J Biol Chem , vol.271 , pp. 7620-7629
    • Chen, X.1    Levkowitz, G.2    Tzahar, E.3    Karunagaran, D.4    Lavi, S.5    Ben-Baruch, N.6    Leitner, O.7    Ratzkin, B.J.8    Bacus, S.S.9    Yarden, Y.10
  • 24
    • 0029783549 scopus 로고    scopus 로고
    • Neu differentiation factor/neuregulin isoforms active distinct receptor combinations
    • of special interest. The authors of this paper demonstrate differences in neuregulin isoform specific binding affinities to receptor heterodimers EGFR/HER3 or HER2/HER3. In myeloid cell lines expressing these receptor pairs, isoform signals induce distinct proliferative and mitogenic responses.
    • Pinkas-Kramarski R, Shelly M, Glathe S, Ratzkin BJ, Yarden Y. Neu differentiation factor/neuregulin isoforms active distinct receptor combinations. of special interest J Biol Chem. 271:1996;19029-19032 The authors of this paper demonstrate differences in neuregulin isoform specific binding affinities to receptor heterodimers EGFR/HER3 or HER2/HER3. In myeloid cell lines expressing these receptor pairs, isoform signals induce distinct proliferative and mitogenic responses.
    • (1996) J Biol Chem , vol.271 , pp. 19029-19032
    • Pinkas-Kramarski, R.1    Shelly, M.2    Glathe, S.3    Ratzkin, B.J.4    Yarden, Y.5
  • 25
    • 0024538540 scopus 로고
    • Ligand-independent tyrosine phosphorylation of EGF receptor and the erbB2/neu proto-oncogene product is induced by hyperosmotic shock
    • King CR, Borello I, Porter L, Comoglio P, Schlessinger J. Ligand-independent tyrosine phosphorylation of EGF receptor and the erbB2/neu proto-oncogene product is induced by hyperosmotic shock. Oncogene. 4:1989;13-18.
    • (1989) Oncogene , vol.4 , pp. 13-18
    • King, C.R.1    Borello, I.2    Porter, L.3    Comoglio, P.4    Schlessinger, J.5
  • 26
    • 0028029162 scopus 로고
    • Activation of the FGF receptor underlies neurite outgrowth stimulated by L1, N-Cam, and N-Cadherin
    • Williams EJ, Furness J, Walsh FS, Doherty P. Activation of the FGF receptor underlies neurite outgrowth stimulated by L1, N-Cam, and N-Cadherin. Neuron. 13:1994;583-594.
    • (1994) Neuron , vol.13 , pp. 583-594
    • Williams, E.J.1    Furness, J.2    Walsh, F.S.3    Doherty, P.4
  • 27
    • 0028817332 scopus 로고
    • A soluble chimeric form of the L1 glycoprotein stimulates neurite outgrowth
    • Doherty P, Williams E, Walsh FS. A soluble chimeric form of the L1 glycoprotein stimulates neurite outgrowth. Neuron. 14:1995;57-66.
    • (1995) Neuron , vol.14 , pp. 57-66
    • Doherty, P.1    Williams, E.2    Walsh, F.S.3
  • 28
    • 0030218948 scopus 로고    scopus 로고
    • Promiscuity of fibroblast growth factor receptors
    • Green PJ, Walsh FS, Doherty P. Promiscuity of fibroblast growth factor receptors. Bioessays. 18:1996;639-646.
    • (1996) Bioessays , vol.18 , pp. 639-646
    • Green, P.J.1    Walsh, F.S.2    Doherty, P.3
  • 29
    • 0029670904 scopus 로고    scopus 로고
    • Stimulation of β1 integrins on fibroblasts induces PDGF independent tyrosine phosphorylation of PDGF β-receptors
    • of special interest. A demonstration of the ligand-independent activation of PDGF β receptors during the dynamic phase of cell adhesion, suggesting a new biological role of RTKs in integrin signaling.
    • Sundberg C, Rubin K. Stimulation of β1 integrins on fibroblasts induces PDGF independent tyrosine phosphorylation of PDGF β-receptors. of special interest J Cell Biol. 132:1996;741-752 A demonstration of the ligand-independent activation of PDGF β receptors during the dynamic phase of cell adhesion, suggesting a new biological role of RTKs in integrin signaling.
    • (1996) J Cell Biol , vol.132 , pp. 741-752
    • Sundberg, C.1    Rubin, K.2
  • 30
    • 0028095102 scopus 로고
    • Ultraviolet B injury increases prostaglandin synthesis through and tyrosine kinase-dependent pathway
    • Miller CC, Hale P, Pentland AP. Ultraviolet B injury increases prostaglandin synthesis through and tyrosine kinase-dependent pathway. J Biol Chem. 269:1994;3529-3533.
    • (1994) J Biol Chem , vol.269 , pp. 3529-3533
    • Miller, C.C.1    Hale, P.2    Pentland, A.P.3
  • 32
    • 0029790979 scopus 로고    scopus 로고
    • Dephosphorylation of receptor tyrosine kinases as a target of regulation by radiation, oxidants or alkylating agents
    • of special interest. The authors of this paper demonstrate that ligand-independent RTK activation by non-physiological agents, such as UV irradiation, results from inactivation of antogonizing membrane-associated phosphatases.
    • Knebel A, Rahmsdorf HJ, Ullrich A, Herrlich P. Dephosphorylation of receptor tyrosine kinases as a target of regulation by radiation, oxidants or alkylating agents. of special interest EMBO J. 15:1996;5314-5325 The authors of this paper demonstrate that ligand-independent RTK activation by non-physiological agents, such as UV irradiation, results from inactivation of antogonizing membrane-associated phosphatases.
    • (1996) EMBO J , vol.15 , pp. 5314-5325
    • Knebel, A.1    Rahmsdorf, H.J.2    Ullrich, A.3    Herrlich, P.4
  • 33
    • 0029993503 scopus 로고    scopus 로고
    • UV activates growth factor receptors via reactive oxygen intermediates
    • Huang RP, Wu JX, Fan Y, Adamson ED. UV activates growth factor receptors via reactive oxygen intermediates. J Cell Biol. 133:1996;211-220.
    • (1996) J Cell Biol , vol.133 , pp. 211-220
    • Huang, R.P.1    Wu, J.X.2    Fan, Y.3    Adamson, E.D.4
  • 35
    • 0029763774 scopus 로고    scopus 로고
    • Hydrogen peroxide induces complex formation of SHC-Grb2-SOS with receptor tyrosine kinase and activates Ras and extracellular signal-regulated kinases group of mitogen-activated protein kinases
    • Rao GN. Hydrogen peroxide induces complex formation of SHC-Grb2-SOS with receptor tyrosine kinase and activates Ras and extracellular signal-regulated kinases group of mitogen-activated protein kinases. Oncogene. 13:1996;713-719.
    • (1996) Oncogene , vol.13 , pp. 713-719
    • Rao, G.N.1
  • 36
    • 0029074408 scopus 로고
    • Convergence of angiotensin II and platelet-derived growth factor receptor signaling cascades in vascular smooth muscle cells
    • Linseman DA, Benjamin CW, Jones DA. Convergence of angiotensin II and platelet-derived growth factor receptor signaling cascades in vascular smooth muscle cells. J Biol Chem. 270:1995;12563-12568.
    • (1995) J Biol Chem , vol.270 , pp. 12563-12568
    • Linseman, D.A.1    Benjamin, C.W.2    Jones, D.A.3
  • 37
    • 0028805435 scopus 로고
    • Thrombin stimulates phosphorylation of insulin-like growth factor-1 receptor, insulin receptor substrate-1, and phospholipase C-γ1 in rat aortic smooth muscle cells
    • Rao GN, Delafontaine P, Runge MS. Thrombin stimulates phosphorylation of insulin-like growth factor-1 receptor, insulin receptor substrate-1, and phospholipase C-γ1 in rat aortic smooth muscle cells. J Biol Chem. 270:1995;27871-27875.
    • (1995) J Biol Chem , vol.270 , pp. 27871-27875
    • Rao, G.N.1    Delafontaine, P.2    Runge, M.S.3
  • 38
    • 0030044360 scopus 로고    scopus 로고
    • Role of transactivation of the EGF receptor in signalling by G-protein-coupled receptors
    • of special interest. The first demonstration of an essential role of RTK-transactivation in GPCR-mediated signaling including activation of the MAP kinase pathway. The approach to inhibit RTK function either by dominant-negative RTK mutants or selective RTK inhibitors might be very useful to analyse the functional importance of RTK-transactivation induced by different stimuli.
    • Daub H, Weiss FU, Wallasch C, Ullrich A. Role of transactivation of the EGF receptor in signalling by G-protein-coupled receptors. of special interest Nature. 379:1996;557-560 The first demonstration of an essential role of RTK-transactivation in GPCR-mediated signaling including activation of the MAP kinase pathway. The approach to inhibit RTK function either by dominant-negative RTK mutants or selective RTK inhibitors might be very useful to analyse the functional importance of RTK-transactivation induced by different stimuli.
    • (1996) Nature , vol.379 , pp. 557-560
    • Daub, H.1    Weiss, F.U.2    Wallasch, C.3    Ullrich, A.4
  • 39
    • 0028246461 scopus 로고
    • Angiotensin II stimulates tyrosine phosphorylation of phospholipase C-γI in vascular smooth muscle cells
    • Marrero MB, Paxton WG, Duff JL, Berk BC, Bernstein KE. Angiotensin II stimulates tyrosine phosphorylation of phospholipase C-γI in vascular smooth muscle cells. J Biol Chem. 269:1994;10935-10939.
    • (1994) J Biol Chem , vol.269 , pp. 10935-10939
    • Marrero, M.B.1    Paxton, W.G.2    Duff, J.L.3    Berk, B.C.4    Bernstein, K.E.5
  • 40
    • 0030032998 scopus 로고    scopus 로고
    • Stimulation of growth factor receptor signal transduction by activation of voltage-sensitive calcium channels
    • Rosen LB, Greenberg ME. Stimulation of growth factor receptor signal transduction by activation of voltage-sensitive calcium channels. Proc Natl Acad Sci USA. 93:1996;1113-1118.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1113-1118
    • Rosen, L.B.1    Greenberg, M.E.2
  • 41
    • 0029670941 scopus 로고    scopus 로고
    • 2+-dependent routes to Ras: Mechanisms for neuronal survival, differentiation, and plasticity?
    • of special interest. A summary of the potential calcium-induced pathways leading to Ras activation in PC12 cells, including transactivation of the EGFR. Furthermore the possibility of src-mediated EGFR phosphorylation is discussed.
    • 2+-dependent routes to Ras: mechanisms for neuronal survival, differentiation, and plasticity? of special interest Neuron. 16:1996;233-236 A summary of the potential calcium-induced pathways leading to Ras activation in PC12 cells, including transactivation of the EGFR. Furthermore the possibility of src-mediated EGFR phosphorylation is discussed.
    • (1996) Neuron , vol.16 , pp. 233-236
    • Finkbeiner, S.1    Greenberg, M.E.2
  • 43
    • 0028806450 scopus 로고
    • Participation of reactive oxygen species in the lysophosphatic acid-stimulated mitogen-activated protein kinase activation pathway
    • Chen Q, Olashaw N, Wu J. Participation of reactive oxygen species in the lysophosphatic acid-stimulated mitogen-activated protein kinase activation pathway. J Biol Chem. 270:1995;28499-28502.
    • (1995) J Biol Chem , vol.270 , pp. 28499-28502
    • Chen, Q.1    Olashaw, N.2    Wu, J.3
  • 45
    • 0027500349 scopus 로고
    • The cytochrome b-558 molecules involved in the fibroblast and polymorphonuclear leucocyte superoxide-generating NADPH oxidase systems are structurally and genetically distinct
    • Meier B, Jesaitis AJ, Emmendörfer A, Roesler J, Quinn MT. The cytochrome b-558 molecules involved in the fibroblast and polymorphonuclear leucocyte superoxide-generating NADPH oxidase systems are structurally and genetically distinct. Biochem J. 289:1993;481-486.
    • (1993) Biochem J , vol.289 , pp. 481-486
    • Meier, B.1    Jesaitis, A.J.2    Emmendörfer, A.3    Roesler, J.4    Quinn, M.T.5
  • 46
    • 0029985733 scopus 로고    scopus 로고
    • 60rc-src
    • of special interest. Angiotensin-II-induced stimulation of a G-protein-coupled receptor induces Ras activation and Ras - Raf1 complex formation. By using an electroporation-based approach to load cells anti-src antibodies, direct evidence for an essential role of src in GPCR-mediated Ras activation is provided.
    • rc-src. of special interest J Biol Chem. 271:1996;10329-10333 Angiotensin-II-induced stimulation of a G-protein-coupled receptor induces Ras activation and Ras - Raf1 complex formation. By using an electroporation-based approach to load cells anti-src antibodies, direct evidence for an essential role of src in GPCR-mediated Ras activation is provided.
    • (1996) J Biol Chem , vol.271 , pp. 10329-10333
    • Schieffer, B.1    Paxton, W.G.2    Chai, Q.3    Marrero, M.B.4    Bernstein, K.E.5
  • 47
    • 0029778177 scopus 로고    scopus 로고
    • Role of c-src tytrosine kinase in G protein-coupled receptor and Gβγ subunit-mediated activation of mitogen-activated protein kinases
    • Luttrell LM, Hawes BE, Van Biesen T, Luttrell DK, Lansing TJ, Lefkowitz RJ. Role of c-src tytrosine kinase in G protein-coupled receptor and Gβγ subunit-mediated activation of mitogen-activated protein kinases. J Biol Chem. 271:1996;19443-19450.
    • (1996) J Biol Chem , vol.271 , pp. 19443-19450
    • Luttrell, L.M.1    Hawes, B.E.2    Van Biesen, T.3    Luttrell, D.K.4    Lansing, T.J.5    Lefkowitz, R.J.6
  • 48
    • 0027049804 scopus 로고
    • The mammalian ulraviolet response is triggered by activtion of Src tyrosine kinases
    • Devary Y, Gottlieb RA, Smeal T, Karin M. The mammalian ulraviolet response is triggered by activtion of Src tyrosine kinases. Cell. 71:1993;1081-1091.
    • (1993) Cell , vol.71 , pp. 1081-1091
    • Devary, Y.1    Gottlieb, R.A.2    Smeal, T.3    Karin, M.4
  • 49
    • 0029616354 scopus 로고
    • Calcium influx induces neurite outgrowth through a Src - Ras signaling cassette
    • Rusanescu G, Qi H, Thomas SM, Brugge JS, Haleggoua S. Calcium influx induces neurite outgrowth through a Src - Ras signaling cassette. Neuron. 15:1995;1415-1425.
    • (1995) Neuron , vol.15 , pp. 1415-1425
    • Rusanescu, G.1    Qi, H.2    Thomas, S.M.3    Brugge, J.S.4    Haleggoua, S.5
  • 50
    • 0025966624 scopus 로고
    • Phosphorylation and activation of epidermal growth factor receptors in cells transformed by the src oncogene
    • Wasilenko WJ, Payne DM, Fitzgerald DL, Weber MJ. Phosphorylation and activation of epidermal growth factor receptors in cells transformed by the src oncogene. Mol Cell Biol. 11:1991;309-321.
    • (1991) Mol Cell Biol , vol.11 , pp. 309-321
    • Wasilenko, W.J.1    Payne, D.M.2    Fitzgerald, D.L.3    Weber, M.J.4


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