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Volumn 1773, Issue 8, 2007, Pages 1161-1176

Regulation of MAPKs by growth factors and receptor tyrosine kinases

Author keywords

Cancer; Growth factor; Signal transduction; Transcription; Tyrosine kinase

Indexed keywords

GROWTH FACTOR; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN TYROSINE KINASE;

EID: 34547226194     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2007.01.002     Document Type: Review
Times cited : (362)

References (194)
  • 1
    • 0023942517 scopus 로고
    • Growth factor receptor tyrosine kinases
    • Yarden Y., and Ullrich A. Growth factor receptor tyrosine kinases. Annu. Rev. Biochem. 57 (1988) 443-478
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 443-478
    • Yarden, Y.1    Ullrich, A.2
  • 2
    • 0035902180 scopus 로고    scopus 로고
    • Oncogenic kinase signaling
    • Blume-Jensen P., and Hunter T. Oncogenic kinase signaling. Nature 411 (2001) 355-365
    • (2001) Nature , vol.411 , pp. 355-365
    • Blume-Jensen, P.1    Hunter, T.2
  • 3
    • 0030183048 scopus 로고    scopus 로고
    • Ligand-induced dimerization of growth factor receptors: variations on the theme
    • Heldin C.-H., and Ostman A. Ligand-induced dimerization of growth factor receptors: variations on the theme. Cytok. Growth Factor Rev. 7 (1996) 33-40
    • (1996) Cytok. Growth Factor Rev. , vol.7 , pp. 33-40
    • Heldin, C.-H.1    Ostman, A.2
  • 4
    • 0842346438 scopus 로고    scopus 로고
    • Specificity in signal transduction: from phosphotyrosine-SH2 domain interactions to complex cellular systems
    • Pawson T. Specificity in signal transduction: from phosphotyrosine-SH2 domain interactions to complex cellular systems. Cell 116 (2004) 191-203
    • (2004) Cell , vol.116 , pp. 191-203
    • Pawson, T.1
  • 7
    • 33745002702 scopus 로고    scopus 로고
    • An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
    • Zhang X., Gureasko J., Shen K., Cole P.A., and Kuriyan J. An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor. Cell 125 (2006) 1137-1149
    • (2006) Cell , vol.125 , pp. 1137-1149
    • Zhang, X.1    Gureasko, J.2    Shen, K.3    Cole, P.A.4    Kuriyan, J.5
  • 8
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse M., and Kuriyan J. The conformational plasticity of protein kinases. Cell 109 (2002) 275-282
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 9
    • 2942594298 scopus 로고    scopus 로고
    • Juxtamembrane autoinhibition in receptor tyrosine kinases
    • Hubbard S.R. Juxtamembrane autoinhibition in receptor tyrosine kinases. Nat. Rev., Mol. Cell Biol. 5 (2004) 464-471
    • (2004) Nat. Rev., Mol. Cell Biol. , vol.5 , pp. 464-471
    • Hubbard, S.R.1
  • 10
    • 0034927336 scopus 로고    scopus 로고
    • Regulation of phosphoinositide-specific phospholipase C
    • Rhee S.G. Regulation of phosphoinositide-specific phospholipase C. Annu. Rev. Biochem. 70 (2001) 281-312
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 281-312
    • Rhee, S.G.1
  • 11
    • 0028971813 scopus 로고
    • Phosphoinositide-specific phospholipase C and mitogenic signaling
    • Noh D.Y., Shin S.H., and Rhee S.G. Phosphoinositide-specific phospholipase C and mitogenic signaling. Biochim. Biophys. Acta. 1242 (1995) 99-113
    • (1995) Biochim. Biophys. Acta. , vol.1242 , pp. 99-113
    • Noh, D.Y.1    Shin, S.H.2    Rhee, S.G.3
  • 14
    • 0036731485 scopus 로고    scopus 로고
    • Stats: transcriptional control and biological impact
    • Levy D.E., and Darnell Jr. J.E. Stats: transcriptional control and biological impact. Nat. Rev., Mol. Cell Biol. 3 (2002) 651-662
    • (2002) Nat. Rev., Mol. Cell Biol. , vol.3 , pp. 651-662
    • Levy, D.E.1    Darnell Jr., J.E.2
  • 16
    • 30944447568 scopus 로고    scopus 로고
    • The extracellular signal-regulated kinase: multiple substrates regulate diverse cellular functions
    • Yoon S., and Seger R. The extracellular signal-regulated kinase: multiple substrates regulate diverse cellular functions. Growth Factors 24 (2006) 21-44
    • (2006) Growth Factors , vol.24 , pp. 21-44
    • Yoon, S.1    Seger, R.2
  • 17
    • 33646336602 scopus 로고    scopus 로고
    • MAPK signal specificity: the right place at the right time
    • Murphy L.O., and Blenis J. MAPK signal specificity: the right place at the right time. Trends Biochem. Sci. 31 (2006) 268-275
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 268-275
    • Murphy, L.O.1    Blenis, J.2
  • 18
    • 0032531881 scopus 로고    scopus 로고
    • Bmk1/Erk5 is required for cell proliferation induced by epidermal growth factor
    • Kato Y., Tapping R.I., Huang S., Watson M.H., Ulevitch R.J., and Lee J.D. Bmk1/Erk5 is required for cell proliferation induced by epidermal growth factor. Nature 395 (1998) 713-716
    • (1998) Nature , vol.395 , pp. 713-716
    • Kato, Y.1    Tapping, R.I.2    Huang, S.3    Watson, M.H.4    Ulevitch, R.J.5    Lee, J.D.6
  • 19
    • 0033579552 scopus 로고    scopus 로고
    • MEKK3 directly regulates MEK5 activity as part of the big mitogen-activated protein kinase 1 (BMK1) signaling pathway
    • Chao T.H., Hayashi M., Tapping R.I., Kato Y., and Lee J.D. MEKK3 directly regulates MEK5 activity as part of the big mitogen-activated protein kinase 1 (BMK1) signaling pathway. J. Biol. Chem. 274 (1999) 36035-36038
    • (1999) J. Biol. Chem. , vol.274 , pp. 36035-36038
    • Chao, T.H.1    Hayashi, M.2    Tapping, R.I.3    Kato, Y.4    Lee, J.D.5
  • 20
    • 0029896250 scopus 로고    scopus 로고
    • Big mitogen-activated protein kinase 1 (BMK1) is a redox-sensitive kinase
    • Abe J., Kusuhara M., Ulevitch R.J., Berk B.C., and Lee J.D. Big mitogen-activated protein kinase 1 (BMK1) is a redox-sensitive kinase. J. Biol. Chem. 271 (1996) 16586-16590
    • (1996) J. Biol. Chem. , vol.271 , pp. 16586-16590
    • Abe, J.1    Kusuhara, M.2    Ulevitch, R.J.3    Berk, B.C.4    Lee, J.D.5
  • 21
    • 0033543549 scopus 로고    scopus 로고
    • Activation of the protein kinase ERK5/BMK1 by receptor tyrosine kinases. Identification and characterization of a signaling pathway to the nucleus
    • Kamakura S., Moriguchi T., and Nishida E. Activation of the protein kinase ERK5/BMK1 by receptor tyrosine kinases. Identification and characterization of a signaling pathway to the nucleus. J. Biol. Chem. 274 (1999) 26563-26571
    • (1999) J. Biol. Chem. , vol.274 , pp. 26563-26571
    • Kamakura, S.1    Moriguchi, T.2    Nishida, E.3
  • 22
    • 0028827450 scopus 로고
    • Isolation of MEK5 and differential expression of alternatively spliced forms
    • English J.M., Vanderbilt C.A., Xu S., Marcus S., and Cobb M.H. Isolation of MEK5 and differential expression of alternatively spliced forms. J. Biol. Chem. 270 (1995) 28897-28902
    • (1995) J. Biol. Chem. , vol.270 , pp. 28897-28902
    • English, J.M.1    Vanderbilt, C.A.2    Xu, S.3    Marcus, S.4    Cobb, M.H.5
  • 23
    • 0037378478 scopus 로고    scopus 로고
    • MEK kinase 2 and the adaptor protein Lad regulate extracellular signal-regulated kinase 5 activation by epidermal growth factor via Src
    • Sun W., Wei X., Kesavan K., Garrington T.P., Fan R., Mei J., Anderson S.M., Gelf E.W., and Johnson G.L. MEK kinase 2 and the adaptor protein Lad regulate extracellular signal-regulated kinase 5 activation by epidermal growth factor via Src. Mol. Cell. Biol. 23 (2003) 2298-2308
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 2298-2308
    • Sun, W.1    Wei, X.2    Kesavan, K.3    Garrington, T.P.4    Fan, R.5    Mei, J.6    Anderson, S.M.7    Gelf, E.W.8    Johnson, G.L.9
  • 25
    • 33645800380 scopus 로고    scopus 로고
    • Cyclic AMP selectively uncouples mitogen-activated protein kinase cascades from activating signals
    • Pearson G.W., Earnest S., and Cobb M.H. Cyclic AMP selectively uncouples mitogen-activated protein kinase cascades from activating signals. Mol. Cell. Biol. 26 (2006) 3039-3047
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 3039-3047
    • Pearson, G.W.1    Earnest, S.2    Cobb, M.H.3
  • 26
    • 0033838721 scopus 로고    scopus 로고
    • Role of BMK1 in regulation of growth factor-induced cellular responses
    • Kato Y., Chao T.H., Hayashi M., Tapping R.I., and Lee J.D. Role of BMK1 in regulation of growth factor-induced cellular responses. Immunol. Res. 21 (2000) 233-237
    • (2000) Immunol. Res. , vol.21 , pp. 233-237
    • Kato, Y.1    Chao, T.H.2    Hayashi, M.3    Tapping, R.I.4    Lee, J.D.5
  • 27
    • 0035937718 scopus 로고    scopus 로고
    • BMK1 mediates growth factor-induced cell proliferation through direct cellular activation of serum and glucocorticoid-inducible kinase
    • Hayashi M., Tapping R.I., Chao T.H., Lo J.F., King C.C., Yang Y., and Lee J.D. BMK1 mediates growth factor-induced cell proliferation through direct cellular activation of serum and glucocorticoid-inducible kinase. J. Biol. Chem. 276 (2001) 8631-8634
    • (2001) J. Biol. Chem. , vol.276 , pp. 8631-8634
    • Hayashi, M.1    Tapping, R.I.2    Chao, T.H.3    Lo, J.F.4    King, C.C.5    Yang, Y.6    Lee, J.D.7
  • 29
    • 0035066383 scopus 로고    scopus 로고
    • Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation
    • Kyriakis J.M., and Avruch J. Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation. Physiol. Rev. 81 (2001) 807-869
    • (2001) Physiol. Rev. , vol.81 , pp. 807-869
    • Kyriakis, J.M.1    Avruch, J.2
  • 30
    • 0034644522 scopus 로고    scopus 로고
    • Signal transduction by the JNK group of MAP kinases
    • Davis R.J. Signal transduction by the JNK group of MAP kinases. Cell 103 (2000) 239-252
    • (2000) Cell , vol.103 , pp. 239-252
    • Davis, R.J.1
  • 31
    • 0029913510 scopus 로고    scopus 로고
    • Signaling from the small GTP-binding proteins Rac1 and Cdc42 to the c-Jun N-terminal kinase/stress-activated protein kinase pathway. A role for mixed lineage kinase 3/protein-tyrosine kinase 1, a novel member of the mixed lineage kinase family
    • Teramoto H., Coso O.A., Miyata H., Igishi T., Miki T., and Gutkind J.S. Signaling from the small GTP-binding proteins Rac1 and Cdc42 to the c-Jun N-terminal kinase/stress-activated protein kinase pathway. A role for mixed lineage kinase 3/protein-tyrosine kinase 1, a novel member of the mixed lineage kinase family. J. Biol. Chem. 271 (1996) 27225-27228
    • (1996) J. Biol. Chem. , vol.271 , pp. 27225-27228
    • Teramoto, H.1    Coso, O.A.2    Miyata, H.3    Igishi, T.4    Miki, T.5    Gutkind, J.S.6
  • 32
    • 0029070887 scopus 로고
    • Selective activation of the JNK signaling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs
    • Minden A., Lin A., Claret F.X., Abo A., and Karin M. Selective activation of the JNK signaling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs. Cell 81 (1995) 1147-1157
    • (1995) Cell , vol.81 , pp. 1147-1157
    • Minden, A.1    Lin, A.2    Claret, F.X.3    Abo, A.4    Karin, M.5
  • 33
    • 0030875602 scopus 로고    scopus 로고
    • MEK kinases are regulated by EGF and selectively interact with Rac/Cdc42
    • Fanger G.R., Johnson N.L., and Johnson G.L. MEK kinases are regulated by EGF and selectively interact with Rac/Cdc42. EMBO J. 16 (1997) 4961-4972
    • (1997) EMBO J. , vol.16 , pp. 4961-4972
    • Fanger, G.R.1    Johnson, N.L.2    Johnson, G.L.3
  • 35
  • 36
    • 0030840413 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase mediates epidermal growth factor-induced activation of the c-Jun N-terminal kinase signaling pathway
    • Logan S.K., Falasca M., Hu P., and Schlessinger J. Phosphatidylinositol 3-kinase mediates epidermal growth factor-induced activation of the c-Jun N-terminal kinase signaling pathway. Mol. Cell. Biol. 17 (1997) 5784-5790
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5784-5790
    • Logan, S.K.1    Falasca, M.2    Hu, P.3    Schlessinger, J.4
  • 37
    • 0033575235 scopus 로고    scopus 로고
    • Shc regulates epidermal growth factor-induced activation of the JNK signaling pathway
    • Hashimoto A., Kurosaki M., Gotoh N., Shibuya M., and Kurosaki T. Shc regulates epidermal growth factor-induced activation of the JNK signaling pathway. J. Biol. Chem. 274 (1999) 20139-20143
    • (1999) J. Biol. Chem. , vol.274 , pp. 20139-20143
    • Hashimoto, A.1    Kurosaki, M.2    Gotoh, N.3    Shibuya, M.4    Kurosaki, T.5
  • 38
    • 0033966557 scopus 로고    scopus 로고
    • Nck-interacting Ste20 kinase couples Eph receptors to c-Jun N-terminal kinase and integrin activation
    • Becker E., Huynh-Do U., Holland S., Pawson T., Daniel T.O., and Skolnik E.Y. Nck-interacting Ste20 kinase couples Eph receptors to c-Jun N-terminal kinase and integrin activation. Mol. Cell. Biol. 20 (2000) 1537-1545
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1537-1545
    • Becker, E.1    Huynh-Do, U.2    Holland, S.3    Pawson, T.4    Daniel, T.O.5    Skolnik, E.Y.6
  • 39
    • 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., and 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
  • 40
    • 0028880006 scopus 로고
    • Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis
    • Xia Z., Dickens M., Raingeaud J., Davis R.J., and Greenberg M.E. Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis. Science 270 (1995) 1326-1331
    • (1995) Science , vol.270 , pp. 1326-1331
    • Xia, Z.1    Dickens, M.2    Raingeaud, J.3    Davis, R.J.4    Greenberg, M.E.5
  • 41
    • 33748928434 scopus 로고    scopus 로고
    • p38 MAP kinase mediates stress_induced internalization of EGFR: implications for cancer chemotherapy
    • Zwang Y., and Yarden Y. p38 MAP kinase mediates stress_induced internalization of EGFR: implications for cancer chemotherapy. EMBO J 25 (2006) 4195-4206
    • (2006) EMBO J , vol.25 , pp. 4195-4206
    • Zwang, Y.1    Yarden, Y.2
  • 42
    • 33646416224 scopus 로고    scopus 로고
    • Activation of p38 mitogen-activated protein kinase promotes epidermal growth factor receptor internalization
    • Vergarajauregui S., San Miguel A., and Puertollano R. Activation of p38 mitogen-activated protein kinase promotes epidermal growth factor receptor internalization. Traffic 7 (2006) 686-698
    • (2006) Traffic , vol.7 , pp. 686-698
    • Vergarajauregui, S.1    San Miguel, A.2    Puertollano, R.3
  • 43
    • 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
  • 44
    • 0028483678 scopus 로고
    • EGF triggers neuronal differentiation of PC12 cells that overexpress the EGF receptor
    • Traverse S., Seedorf K., Paterson H., Marshall C.J., Cohen P., and Ullrich A. EGF triggers neuronal differentiation of PC12 cells that overexpress the EGF receptor. Curr. Biol. 4 (1994) 694-701
    • (1994) Curr. Biol. , vol.4 , pp. 694-701
    • Traverse, S.1    Seedorf, K.2    Paterson, H.3    Marshall, C.J.4    Cohen, P.5    Ullrich, A.6
  • 45
    • 0028485768 scopus 로고
    • PC12 cells overexpressing the insulin receptor undergo insulin-dependent neuronal differentiation
    • Dikic I., Schlessinger J., and Lax I. PC12 cells overexpressing the insulin receptor undergo insulin-dependent neuronal differentiation. Curr. Biol. 4 (1994) 702-708
    • (1994) Curr. Biol. , vol.4 , pp. 702-708
    • Dikic, I.1    Schlessinger, J.2    Lax, I.3
  • 46
    • 0030835430 scopus 로고    scopus 로고
    • Raf-induced proliferation or cell cycle arrest is determined by the level of Raf activity with arrest mediated by p21Cip1
    • Woods D., Parry D., Cherwinski H., Bosch E., Lees E., and McMahon M. Raf-induced proliferation or cell cycle arrest is determined by the level of Raf activity with arrest mediated by p21Cip1. Mol. Cell. Biol. 17 (1997) 5598-5611
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5598-5611
    • Woods, D.1    Parry, D.2    Cherwinski, H.3    Bosch, E.4    Lees, E.5    McMahon, M.6
  • 49
    • 29144462587 scopus 로고    scopus 로고
    • Wild-type and mutant B-RAF activate C-RAF through distinct mechanisms involving heterodimerization
    • Garnett M.J., Rana S., Paterson H., Barford D., and Marais R. Wild-type and mutant B-RAF activate C-RAF through distinct mechanisms involving heterodimerization. Mol. Cell 20 (2005) 963-969
    • (2005) Mol. Cell , vol.20 , pp. 963-969
    • Garnett, M.J.1    Rana, S.2    Paterson, H.3    Barford, D.4    Marais, R.5
  • 51
    • 4143098266 scopus 로고    scopus 로고
    • MLK3 is required for mitogen activation of B-Raf, ERK and cell proliferation
    • Chadee D.N., and Kyriakis J.M. MLK3 is required for mitogen activation of B-Raf, ERK and cell proliferation. Nat. Cell Biol. 6 (2004) 770-776
    • (2004) Nat. Cell Biol. , vol.6 , pp. 770-776
    • Chadee, D.N.1    Kyriakis, J.M.2
  • 53
    • 0032478610 scopus 로고    scopus 로고
    • Requirement of Ras-GTP-Raf complexes for activation of Raf-1 by protein kinase C
    • Marais R., Light Y., Mason C., Paterson H., Olson M.F., and Marshall C.J. Requirement of Ras-GTP-Raf complexes for activation of Raf-1 by protein kinase C. Science 280 (1998) 109-112
    • (1998) Science , vol.280 , pp. 109-112
    • Marais, R.1    Light, Y.2    Mason, C.3    Paterson, H.4    Olson, M.F.5    Marshall, C.J.6
  • 54
    • 0032511882 scopus 로고    scopus 로고
    • The protein kinase Pak3 positively regulates Raf-1 activity through phosphorylation of serine 338
    • King A.J., Sun H., Diaz B., Barnard D., Miao W., Bagrodia S., and Marshall M.S. The protein kinase Pak3 positively regulates Raf-1 activity through phosphorylation of serine 338. Nature 396 (1998) 180-183
    • (1998) Nature , vol.396 , pp. 180-183
    • King, A.J.1    Sun, H.2    Diaz, B.3    Barnard, D.4    Miao, W.5    Bagrodia, S.6    Marshall, M.S.7
  • 56
    • 0032588943 scopus 로고    scopus 로고
    • Protein kinase Cdelta mediates neurogenic but not mitogenic activation of mitogen-activated protein kinase in neuronal cells
    • Corbit K.C., Foster D.A., and Rosner M.R. Protein kinase Cdelta mediates neurogenic but not mitogenic activation of mitogen-activated protein kinase in neuronal cells. Mol. Cell. Biol. 19 (1999) 4209-4818
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4209-4818
    • Corbit, K.C.1    Foster, D.A.2    Rosner, M.R.3
  • 57
    • 0033927901 scopus 로고    scopus 로고
    • Different protein kinase C isoforms determine growth factor specificity in neuronal cells
    • Corbit K.C., Soh J.W., Yoshida K., Eves E.M., Weinstein I.B., and Rosner M.R. Different protein kinase C isoforms determine growth factor specificity in neuronal cells. Mol. Cell. Biol. 20 (2000) 5392-5403
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5392-5403
    • Corbit, K.C.1    Soh, J.W.2    Yoshida, K.3    Eves, E.M.4    Weinstein, I.B.5    Rosner, M.R.6
  • 58
    • 30044445850 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 is a negative regulator of extracellular signal-regulated kinase
    • Wang Q., Zhou Y., Wang X., and Evers B.M. Glycogen synthase kinase-3 is a negative regulator of extracellular signal-regulated kinase. Oncogene 25 (2006) 43-50
    • (2006) Oncogene , vol.25 , pp. 43-50
    • Wang, Q.1    Zhou, Y.2    Wang, X.3    Evers, B.M.4
  • 61
    • 0031000626 scopus 로고    scopus 로고
    • Megakaryocytic differentiation induced by constitutive activation of mitogen-activated protein kinase kinase
    • Whalen A.M., Galasinski S.C., Shapiro P.S., Nahreini T.S., and Ahn N.G. Megakaryocytic differentiation induced by constitutive activation of mitogen-activated protein kinase kinase. Mol. Cell. Biol. 17 (1997) 1947-1958
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1947-1958
    • Whalen, A.M.1    Galasinski, S.C.2    Shapiro, P.S.3    Nahreini, T.S.4    Ahn, N.G.5
  • 62
    • 0028199799 scopus 로고
    • Trk receptors use redundant signal transduction pathways involving SHC and PLC-gamma 1 to mediate NGF responses
    • Stephens R.M., Loeb D.M., Copeland T.D., Pawson T., Greene L.A., and Kaplan D.R. Trk receptors use redundant signal transduction pathways involving SHC and PLC-gamma 1 to mediate NGF responses. Neuron 12 (1994) 691-705
    • (1994) Neuron , vol.12 , pp. 691-705
    • Stephens, R.M.1    Loeb, D.M.2    Copeland, T.D.3    Pawson, T.4    Greene, L.A.5    Kaplan, D.R.6
  • 63
    • 0028293929 scopus 로고
    • Neuronal differentiation signals are controlled by nerve growth factor receptor/Trk binding sites for SHC and PLC gamma
    • Obermeier A., Bradshaw R.A., Seedorf K., Choidas A., Schlessinger J., and Ullrich A. Neuronal differentiation signals are controlled by nerve growth factor receptor/Trk binding sites for SHC and PLC gamma. EMBO J. 13 (1994) 1585-1590
    • (1994) EMBO J. , vol.13 , pp. 1585-1590
    • Obermeier, A.1    Bradshaw, R.A.2    Seedorf, K.3    Choidas, A.4    Schlessinger, J.5    Ullrich, A.6
  • 64
    • 0027153103 scopus 로고
    • Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adapter protein, and Sos nucleotide exchange factor
    • Buday L., and Downward J. Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adapter protein, and Sos nucleotide exchange factor. Cell 73 (1993) 611-620
    • (1993) Cell , vol.73 , pp. 611-620
    • Buday, L.1    Downward, J.2
  • 66
    • 8644266706 scopus 로고    scopus 로고
    • Stimulus-coupled spatial restriction of extracellular signal-regulated kinase 1/2 activity contributes to the specificity of signal-response pathways
    • Whitehurst A., Cobb M.H., and White M.A. Stimulus-coupled spatial restriction of extracellular signal-regulated kinase 1/2 activity contributes to the specificity of signal-response pathways. Mol. Cell. Biol. 24 (2004) 10145-10150
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 10145-10150
    • Whitehurst, A.1    Cobb, M.H.2    White, M.A.3
  • 68
    • 24344491858 scopus 로고    scopus 로고
    • IQGAP1 is a scaffold for mitogen-activated protein kinase signaling
    • Roy M., Li Z., and Sacks D.B. IQGAP1 is a scaffold for mitogen-activated protein kinase signaling. Mol. Cell. Biol. 25 (2005) 7940-7952
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 7940-7952
    • Roy, M.1    Li, Z.2    Sacks, D.B.3
  • 69
    • 6344255031 scopus 로고    scopus 로고
    • Paxillin serves as an ERK-regulated scaffold for coordinating FAK and Rac activation in epithelial morphogenesis
    • Ishibe S., Joly D., Liu Z.X., and Cantley L.G. Paxillin serves as an ERK-regulated scaffold for coordinating FAK and Rac activation in epithelial morphogenesis. Mol. Cell 16 (2004) 257-267
    • (2004) Mol. Cell , vol.16 , pp. 257-267
    • Ishibe, S.1    Joly, D.2    Liu, Z.X.3    Cantley, L.G.4
  • 70
    • 0037429692 scopus 로고    scopus 로고
    • Trafficking of the ErbB receptors and its influence on signaling
    • Wiley H.S. Trafficking of the ErbB receptors and its influence on signaling. Exp. Cell Res. 284 (2003) 78-88
    • (2003) Exp. Cell Res. , vol.284 , pp. 78-88
    • Wiley, H.S.1
  • 71
    • 0035316576 scopus 로고    scopus 로고
    • Cbl: many adaptations to regulate protein tyrosine kinases
    • Thien C.B., and Langdon W.Y. Cbl: many adaptations to regulate protein tyrosine kinases. Nat. Rev., Mol. Cell Biol. 2 (2001) 294-307
    • (2001) Nat. Rev., Mol. Cell Biol. , vol.2 , pp. 294-307
    • Thien, C.B.1    Langdon, W.Y.2
  • 72
    • 1842591231 scopus 로고    scopus 로고
    • Role of protein ubiquitylation in regulating endocytosis of receptor tyrosine kinases
    • Marmor M.D., and Yarden Y. Role of protein ubiquitylation in regulating endocytosis of receptor tyrosine kinases. Oncogene 23 (2004) 2057-2070
    • (2004) Oncogene , vol.23 , pp. 2057-2070
    • Marmor, M.D.1    Yarden, Y.2
  • 73
    • 0027965262 scopus 로고
    • Compartmentalization of SHC, GRB2 and mSOS, and hyperphosphorylation of Raf-1 by EGF but not insulin in liver parenchyma
    • Di Guglielmo G.M., Baass P.C., Ou W.J., Posner B.I., and Bergeron J.J. Compartmentalization of SHC, GRB2 and mSOS, and hyperphosphorylation of Raf-1 by EGF but not insulin in liver parenchyma. EMBO J. 13 (1994) 4269-4277
    • (1994) EMBO J. , vol.13 , pp. 4269-4277
    • Di Guglielmo, G.M.1    Baass, P.C.2    Ou, W.J.3    Posner, B.I.4    Bergeron, J.J.5
  • 74
    • 34547215097 scopus 로고    scopus 로고
    • Coordinated traffic of Grb2 and Ras during epidermal growth factor receptor endocytosis visualized in living cells
    • Jiang X., and Sorkin A. Coordinated traffic of Grb2 and Ras during epidermal growth factor receptor endocytosis visualized in living cells. Mol. Biol. Cell 3 (2002) 522-535
    • (2002) Mol. Biol. Cell , vol.3 , pp. 522-535
    • Jiang, X.1    Sorkin, A.2
  • 75
    • 0033544953 scopus 로고    scopus 로고
    • Dynamin is required for the activation of mitogen-activated protein (MAP) kinase by MAP kinase kinase
    • Kranenburg O., Verlaan I., and Moolenaar W.H. Dynamin is required for the activation of mitogen-activated protein (MAP) kinase by MAP kinase kinase. J. Biol. Chem. 274 (1999) 35301-35304
    • (1999) J. Biol. Chem. , vol.274 , pp. 35301-35304
    • Kranenburg, O.1    Verlaan, I.2    Moolenaar, W.H.3
  • 76
    • 0042130366 scopus 로고    scopus 로고
    • Stimulation of cell proliferation by endosomal epidermal growth factor receptor as revealed through two distinct phases of signaling
    • Pennock S., and Wang Z. Stimulation of cell proliferation by endosomal epidermal growth factor receptor as revealed through two distinct phases of signaling. Mol. Cell. Biol. 23 (2003) 5803-5815
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5803-5815
    • Pennock, S.1    Wang, Z.2
  • 77
    • 0030461226 scopus 로고    scopus 로고
    • Control of EGF receptor signaling by clathrin-mediated endocytosis
    • Vieira A.V., Lamaze C., and Schmid S.L. Control of EGF receptor signaling by clathrin-mediated endocytosis. Science 274 (1996) 2086-2088
    • (1996) Science , vol.274 , pp. 2086-2088
    • Vieira, A.V.1    Lamaze, C.2    Schmid, S.L.3
  • 78
    • 0035162703 scopus 로고    scopus 로고
    • Regulation of epidermal growth factor receptor signaling by endocytosis and intracellular trafficking
    • Burke P., Schooler K., and Wiley H.S. Regulation of epidermal growth factor receptor signaling by endocytosis and intracellular trafficking. Mol. Biol. Cell 12 (2001) 1897-1910
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1897-1910
    • Burke, P.1    Schooler, K.2    Wiley, H.S.3
  • 80
    • 0036899420 scopus 로고    scopus 로고
    • Localization of the MP1-MAPK scaffold complex to endosomes is mediated by p14 and required for signal transduction
    • Teis D., Wunderlich W., and Huber L.A. Localization of the MP1-MAPK scaffold complex to endosomes is mediated by p14 and required for signal transduction. Dev. Cell 3 (2002) 803-814
    • (2002) Dev. Cell , vol.3 , pp. 803-814
    • Teis, D.1    Wunderlich, W.2    Huber, L.A.3
  • 81
    • 33644556129 scopus 로고    scopus 로고
    • Ras and its signals diffuse through the cell on randomly moving nanoparticles
    • Rotblat B., Yizhar O., Haklai R., Ashery U., and Kloog Y. Ras and its signals diffuse through the cell on randomly moving nanoparticles. Cancer Res. 66 (2006) 1974-1981
    • (2006) Cancer Res. , vol.66 , pp. 1974-1981
    • Rotblat, B.1    Yizhar, O.2    Haklai, R.3    Ashery, U.4    Kloog, Y.5
  • 82
    • 33745828702 scopus 로고    scopus 로고
    • EGF-ERBB signalling: towards the systems level
    • Citri A., and Yarden Y. EGF-ERBB signalling: towards the systems level. Nat. Rev., Mol. Cell Biol. 7 (2006) 505-516
    • (2006) Nat. Rev., Mol. Cell Biol. , vol.7 , pp. 505-516
    • Citri, A.1    Yarden, Y.2
  • 85
    • 0034676456 scopus 로고    scopus 로고
    • Feedback control of intercellular signalling in development
    • Freeman M. Feedback control of intercellular signalling in development. Nature 408 (2000) 313-319
    • (2000) Nature , vol.408 , pp. 313-319
    • Freeman, M.1
  • 87
    • 0037136702 scopus 로고    scopus 로고
    • Expression of RALT, a feedback inhibitor of ErbB receptors, is subjected to an integrated transcriptional and post-translational control
    • Fiorini M., Ballaro C., Sala G., Falcone G., Alema S., and Segatto O. Expression of RALT, a feedback inhibitor of ErbB receptors, is subjected to an integrated transcriptional and post-translational control. Oncogene 21 (2002) 6530-6539
    • (2002) Oncogene , vol.21 , pp. 6530-6539
    • Fiorini, M.1    Ballaro, C.2    Sala, G.3    Falcone, G.4    Alema, S.5    Segatto, O.6
  • 88
    • 0033782304 scopus 로고    scopus 로고
    • Modeling transcriptional control in gene networks-Methods, recent results, and future directions
    • Smolen P., Baxter D.A., and Byrne J.H. Modeling transcriptional control in gene networks-Methods, recent results, and future directions. Bull. Math. Biol. 62 (2000) 247-292
    • (2000) Bull. Math. Biol. , vol.62 , pp. 247-292
    • Smolen, P.1    Baxter, D.A.2    Byrne, J.H.3
  • 89
    • 7644238181 scopus 로고    scopus 로고
    • Biological robustness
    • Kitano H. Biological robustness. Nat. Rev., Genet. 5 (2004) 826-837
    • (2004) Nat. Rev., Genet. , vol.5 , pp. 826-837
    • Kitano, H.1
  • 90
    • 0010207799 scopus 로고
    • Expression of a set of growth-related immediate early genes in BALB/c 3T3 cells: coordinate regulation with c-fos or c-myc
    • Lau L.F., and Nathans D. Expression of a set of growth-related immediate early genes in BALB/c 3T3 cells: coordinate regulation with c-fos or c-myc. Proc. Natl. Acad. Sci. U. S. A. 84 (1987) 1182-1186
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 1182-1186
    • Lau, L.F.1    Nathans, D.2
  • 91
    • 0022633687 scopus 로고
    • Effect of protein synthesis inhibitors on growth factor activation of c-fos, c-myc, and actin gene transcription
    • Greenberg M.E., Hermanowski A.L., and Ziff E.B. Effect of protein synthesis inhibitors on growth factor activation of c-fos, c-myc, and actin gene transcription. Mol. Cell. Biol. 6 (1986) 1050-1057
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 1050-1057
    • Greenberg, M.E.1    Hermanowski, A.L.2    Ziff, E.B.3
  • 92
    • 2042538029 scopus 로고    scopus 로고
    • Structure and regulation of MAPK phosphatases
    • Farooq A., and Zhou M.M. Structure and regulation of MAPK phosphatases. Cell. Signal. 16 (2004) 769-779
    • (2004) Cell. Signal. , vol.16 , pp. 769-779
    • Farooq, A.1    Zhou, M.M.2
  • 93
    • 0347363834 scopus 로고    scopus 로고
    • Identification of novel ERK-mediated feedback phosphorylation sites at the C-terminus of B-Raf
    • Brummer T., Naegele H., Reth M., and Misawa Y. Identification of novel ERK-mediated feedback phosphorylation sites at the C-terminus of B-Raf. Oncogene 22 (2003) 8823-8834
    • (2003) Oncogene , vol.22 , pp. 8823-8834
    • Brummer, T.1    Naegele, H.2    Reth, M.3    Misawa, Y.4
  • 94
    • 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
  • 95
    • 0026723089 scopus 로고
    • Negative control of photoreceptor development in Drosophila by the product of the yan gene, an ETS domain protein
    • Lai Z.C., and Rubin G.M. Negative control of photoreceptor development in Drosophila by the product of the yan gene, an ETS domain protein. Cell 70 (1992) 609-620
    • (1992) Cell , vol.70 , pp. 609-620
    • Lai, Z.C.1    Rubin, G.M.2
  • 96
    • 0033558030 scopus 로고    scopus 로고
    • Id helix-loop-helix proteins inhibit nucleoprotein complex formation by the TCF ETS-domain transcription factors
    • Yates P.R., Atherton G.T., Deed R.W., Norton J.D., and Sharrocks A.D. Id helix-loop-helix proteins inhibit nucleoprotein complex formation by the TCF ETS-domain transcription factors. EMBO J. 18 (1999) 968-976
    • (1999) EMBO J. , vol.18 , pp. 968-976
    • Yates, P.R.1    Atherton, G.T.2    Deed, R.W.3    Norton, J.D.4    Sharrocks, A.D.5
  • 97
    • 0027741257 scopus 로고
    • Inducibility and negative autoregulation of CREM: an alternative promoter directs the expression of ICER, an early response repressor
    • Molina C.A., Foulkes N.S., Lalli E., and Sassone-Corsi P. Inducibility and negative autoregulation of CREM: an alternative promoter directs the expression of ICER, an early response repressor. Cell 75 (1993) 875-886
    • (1993) Cell , vol.75 , pp. 875-886
    • Molina, C.A.1    Foulkes, N.S.2    Lalli, E.3    Sassone-Corsi, P.4
  • 98
    • 0029891229 scopus 로고    scopus 로고
    • NAB2, a corepressor of NGFI-A (Egr-1) and Krox20, is induced by proliferative and differentiative stimuli
    • Svaren J., Sevetson B.R., Apel E.D., Zimonjic D.B., Popescu N.C., and Milbrandt J. NAB2, a corepressor of NGFI-A (Egr-1) and Krox20, is induced by proliferative and differentiative stimuli. Mol. Cell. Biol. 16 (1996) 3545-3553
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3545-3553
    • Svaren, J.1    Sevetson, B.R.2    Apel, E.D.3    Zimonjic, D.B.4    Popescu, N.C.5    Milbrandt, J.6
  • 99
    • 0029000906 scopus 로고
    • Antitumor promotion by phenolic antioxidants: inhibition of AP-1 activity through induction of Fra expression
    • Yoshioka K., Deng T., Cavigelli M., and Karin M. Antitumor promotion by phenolic antioxidants: inhibition of AP-1 activity through induction of Fra expression. Proc. Natl. Acad. Sci. U. S. A. 92 (1995) 4972-4976
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 4972-4976
    • Yoshioka, K.1    Deng, T.2    Cavigelli, M.3    Karin, M.4
  • 101
  • 102
    • 31144448042 scopus 로고    scopus 로고
    • AU-rich elements and associated factors: are there unifying principles?
    • Barreau C., Paillard L., and Osborne H.B. AU-rich elements and associated factors: are there unifying principles?. Nucleic Acids Res. 33 (2005) 7138-7150
    • (2005) Nucleic Acids Res. , vol.33 , pp. 7138-7150
    • Barreau, C.1    Paillard, L.2    Osborne, H.B.3
  • 103
    • 0032516626 scopus 로고    scopus 로고
    • Feedback inhibition of macrophage tumor necrosis factor-alpha production by tristetraprolin
    • Carballo E., Lai W.S., and Blackshear P.J. Feedback inhibition of macrophage tumor necrosis factor-alpha production by tristetraprolin. Science 281 (1998) 1001-1005
    • (1998) Science , vol.281 , pp. 1001-1005
    • Carballo, E.1    Lai, W.S.2    Blackshear, P.J.3
  • 104
    • 0024296025 scopus 로고
    • Removal of poly(A) and consequent degradation of c-fos mRNA facilitated by 3′ AU-rich sequences
    • Wilson T., and Treisman R. Removal of poly(A) and consequent degradation of c-fos mRNA facilitated by 3′ AU-rich sequences. Nature 336 (1988) 396-399
    • (1988) Nature , vol.336 , pp. 396-399
    • Wilson, T.1    Treisman, R.2
  • 105
    • 0344148793 scopus 로고
    • Removal of a 67-base-pair sequence in the noncoding region of protooncogene fos converts it to a transforming gene
    • Meijlink F., Curran T., Miller A.D., and Verma I.M. Removal of a 67-base-pair sequence in the noncoding region of protooncogene fos converts it to a transforming gene. Proc. Natl. Acad. Sci. U. S. A. 82 (1985) 4987-4991
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 4987-4991
    • Meijlink, F.1    Curran, T.2    Miller, A.D.3    Verma, I.M.4
  • 107
    • 29244437868 scopus 로고    scopus 로고
    • A microRNA mediates EGF receptor signaling and promotes photoreceptor differentiation in the Drosophila eye
    • Li X., and Carthew R.W. A microRNA mediates EGF receptor signaling and promotes photoreceptor differentiation in the Drosophila eye. Cell 123 (2005) 1267-1277
    • (2005) Cell , vol.123 , pp. 1267-1277
    • Li, X.1    Carthew, R.W.2
  • 108
    • 0037605637 scopus 로고    scopus 로고
    • Bistability in cell signaling: how to make continuous processes discontinuous, and reversible processes irreversible
    • Ferrell J.E., and Xiong W. Bistability in cell signaling: how to make continuous processes discontinuous, and reversible processes irreversible. Chaos 11 (2001) 227-236
    • (2001) Chaos , vol.11 , pp. 227-236
    • Ferrell, J.E.1    Xiong, W.2
  • 109
    • 0035150990 scopus 로고    scopus 로고
    • Growth-factor-dependent mitogenesis requires two distinct phases of signalling
    • Jones S.M., and Kazlauskas A. Growth-factor-dependent mitogenesis requires two distinct phases of signalling. Nat. Cell Biol. 3 (2001) 165-172
    • (2001) Nat. Cell Biol. , vol.3 , pp. 165-172
    • Jones, S.M.1    Kazlauskas, A.2
  • 110
    • 0345359924 scopus 로고    scopus 로고
    • A positive-feedback-based bistable 'memory module' that governs a cell fate decision
    • Xiong W., and Ferrell Jr. J.E. A positive-feedback-based bistable 'memory module' that governs a cell fate decision. Nature 426 (2003) 460-465
    • (2003) Nature , vol.426 , pp. 460-465
    • Xiong, W.1    Ferrell Jr., J.E.2
  • 111
    • 0036051342 scopus 로고    scopus 로고
    • Molecular interpretation of ERK signal duration by immediate early gene products
    • Murphy L.O., Smith S., Chen R.H., Fingar D.C., and Blenis J. Molecular interpretation of ERK signal duration by immediate early gene products. Nat. Cell Biol. 4 (2002) 556-564
    • (2002) Nat. Cell Biol. , vol.4 , pp. 556-564
    • Murphy, L.O.1    Smith, S.2    Chen, R.H.3    Fingar, D.C.4    Blenis, J.5
  • 112
    • 0028143002 scopus 로고
    • Overexpression of mitogen-activated protein kinase kinase (MAPKK) and its mutants in NIH 3T3 cells. Evidence that MAPKK involvement in cellular proliferation is regulated by phosphorylation of serine residues in its kinase subdomains VII and VIII
    • Seger R., Seger D., Reszka A.A., Munar E.S., Eldar-Finkelman H., Dobrowolska G., Jensen A.M., Campbell J.S., Fischer E.H., and Krebs E.G. Overexpression of mitogen-activated protein kinase kinase (MAPKK) and its mutants in NIH 3T3 cells. Evidence that MAPKK involvement in cellular proliferation is regulated by phosphorylation of serine residues in its kinase subdomains VII and VIII. J. Biol. Chem. 269 (1994) 25699-25709
    • (1994) J. Biol. Chem. , vol.269 , pp. 25699-25709
    • Seger, R.1    Seger, D.2    Reszka, A.A.3    Munar, E.S.4    Eldar-Finkelman, H.5    Dobrowolska, G.6    Jensen, A.M.7    Campbell, J.S.8    Fischer, E.H.9    Krebs, E.G.10
  • 114
    • 0028228616 scopus 로고
    • Activation of MAP kinase kinase is necessary and sufficient for PC12 differentiation and for transformation of NIH 3T3 cells
    • Cowley S., Paterson H., Kemp P., and Marshall C.J. Activation of MAP kinase kinase is necessary and sufficient for PC12 differentiation and for transformation of NIH 3T3 cells. Cell 77 (1994) 841-852
    • (1994) Cell , vol.77 , pp. 841-852
    • Cowley, S.1    Paterson, H.2    Kemp, P.3    Marshall, C.J.4
  • 116
    • 0032167654 scopus 로고    scopus 로고
    • A link between MAP kinase and p34(cdc2)/cyclin B during oocyte maturation: p90(rsk) phosphorylates and inactivates the p34(cdc2) inhibitory kinase Myt1
    • Palmer A., Gavin A.C., and Nebreda A.R. A link between MAP kinase and p34(cdc2)/cyclin B during oocyte maturation: p90(rsk) phosphorylates and inactivates the p34(cdc2) inhibitory kinase Myt1. EMBO J. 17 (1998) 5037-5047
    • (1998) EMBO J. , vol.17 , pp. 5037-5047
    • Palmer, A.1    Gavin, A.C.2    Nebreda, A.R.3
  • 117
    • 0030863161 scopus 로고    scopus 로고
    • Induction of p27Kip1 degradation and anchorage independence by Ras through the MAP kinase signaling pathway
    • Kawada M., Yamagoe S., Murakami Y., Suzuki K., Mizuno S., and Uehara Y. Induction of p27Kip1 degradation and anchorage independence by Ras through the MAP kinase signaling pathway. Oncogene 15 (1997) 629-637
    • (1997) Oncogene , vol.15 , pp. 629-637
    • Kawada, M.1    Yamagoe, S.2    Murakami, Y.3    Suzuki, K.4    Mizuno, S.5    Uehara, Y.6
  • 118
    • 0029786329 scopus 로고    scopus 로고
    • Cyclin D1 expression is regulated positively by the p42/p44MAPK and negatively by the p38/HOGMAPK pathway
    • Lavoie J.N., L'Allemain G., Brunet A., Muller R., and Pouyssegur J. Cyclin D1 expression is regulated positively by the p42/p44MAPK and negatively by the p38/HOGMAPK pathway. J. Biol. Chem. 271 (1996) 20608-20616
    • (1996) J. Biol. Chem. , vol.271 , pp. 20608-20616
    • Lavoie, J.N.1    L'Allemain, G.2    Brunet, A.3    Muller, R.4    Pouyssegur, J.5
  • 119
    • 0032959647 scopus 로고    scopus 로고
    • Activated MEK stimulates expression of AP-1 components independently of phosphatidylinositol 3-kinase (PI3-kinase) but requires a PI3-kinase signal To stimulate DNA synthesis
    • Treinies I., Paterson H.F., Hooper S., Wilson R., and Marshall C.J. Activated MEK stimulates expression of AP-1 components independently of phosphatidylinositol 3-kinase (PI3-kinase) but requires a PI3-kinase signal To stimulate DNA synthesis. Mol. Cell. Biol. 19 (1999) 321-329
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 321-329
    • Treinies, I.1    Paterson, H.F.2    Hooper, S.3    Wilson, R.4    Marshall, C.J.5
  • 120
    • 0033613250 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase kinase activity is required for the G(2)/M transition of the cell cycle in mammalian fibroblasts
    • Wright J.H., Munar E., Jameson D.R., Andreassen P.R., Margolis R.L., Seger R., and Krebs E.G. Mitogen-activated protein kinase kinase activity is required for the G(2)/M transition of the cell cycle in mammalian fibroblasts. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 11335-11340
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 11335-11340
    • Wright, J.H.1    Munar, E.2    Jameson, D.R.3    Andreassen, P.R.4    Margolis, R.L.5    Seger, R.6    Krebs, E.G.7
  • 122
    • 0032555891 scopus 로고    scopus 로고
    • Activation of the MKK/ERK pathway during somatic cell mitosis: direct interactions of active ERK with kinetochores and regulation of the mitotic 3F3/2 phosphoantigen
    • Shapiro P.S., Vaisberg E., Hunt A.J., Tolwinski N.S., Whalen A.M., McIntosh J.R., and Ahn N.G. Activation of the MKK/ERK pathway during somatic cell mitosis: direct interactions of active ERK with kinetochores and regulation of the mitotic 3F3/2 phosphoantigen. J. Cell Biol. 142 (1998) 1533-1545
    • (1998) J. Cell Biol. , vol.142 , pp. 1533-1545
    • Shapiro, P.S.1    Vaisberg, E.2    Hunt, A.J.3    Tolwinski, N.S.4    Whalen, A.M.5    McIntosh, J.R.6    Ahn, N.G.7
  • 123
    • 0032190629 scopus 로고    scopus 로고
    • Premature senescence involving p53 and p16 is activated in response to constitutive MEK/MAPK mitogenic signaling
    • Lin A.W., Barradas M., Stone J.C., van Aelst L., Serrano M., and Lowe S.W. Premature senescence involving p53 and p16 is activated in response to constitutive MEK/MAPK mitogenic signaling. Genes Dev. 12 (1998) 3008-3019
    • (1998) Genes Dev. , vol.12 , pp. 3008-3019
    • Lin, A.W.1    Barradas, M.2    Stone, J.C.3    van Aelst, L.4    Serrano, M.5    Lowe, S.W.6
  • 125
    • 33746942671 scopus 로고    scopus 로고
    • Raf kinase inhibitory protein regulates aurora B kinase and the spindle checkpoint
    • Eves E.M., Shapiro P., Naik K., Klein U.R., Trakul N., and Rosner M.R. Raf kinase inhibitory protein regulates aurora B kinase and the spindle checkpoint. Mol. Cell 23 (2006) 561-574
    • (2006) Mol. Cell , vol.23 , pp. 561-574
    • Eves, E.M.1    Shapiro, P.2    Naik, K.3    Klein, U.R.4    Trakul, N.5    Rosner, M.R.6
  • 126
    • 0032192153 scopus 로고    scopus 로고
    • Senescence of human fibroblasts induced by oncogenic Raf
    • Zhu J., Woods D., McMahon M., and Bishop J.M. Senescence of human fibroblasts induced by oncogenic Raf. Genes Dev. 12 (1998) 2997-3007
    • (1998) Genes Dev. , vol.12 , pp. 2997-3007
    • Zhu, J.1    Woods, D.2    McMahon, M.3    Bishop, J.M.4
  • 128
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: a physically integrated molecular process
    • Lauffenburger D.A., and Horwitz A.F. Cell migration: a physically integrated molecular process. Cell 84 (1996) 359-369
    • (1996) Cell , vol.84 , pp. 359-369
    • Lauffenburger, D.A.1    Horwitz, A.F.2
  • 129
    • 5044238876 scopus 로고    scopus 로고
    • Integrin signalling during tumour progression
    • Guo W., and Giancotti F.G. Integrin signalling during tumour progression. Nat. Rev., Mol. Cell Biol. 5 (2004) 816-826
    • (2004) Nat. Rev., Mol. Cell Biol. , vol.5 , pp. 816-826
    • Guo, W.1    Giancotti, F.G.2
  • 132
    • 0029134104 scopus 로고
    • Essential role for the c-met receptor in the migration of myogenic precursor cells into the limb bud
    • Bladt F., Riethmacher D., Isenmann S., Aguzzi A., and Birchmeier C. Essential role for the c-met receptor in the migration of myogenic precursor cells into the limb bud. Nature 376 (1995) 768-771
    • (1995) Nature , vol.376 , pp. 768-771
    • Bladt, F.1    Riethmacher, D.2    Isenmann, S.3    Aguzzi, A.4    Birchmeier, C.5
  • 133
    • 0001517943 scopus 로고    scopus 로고
    • Hepatocyte growth factor/scatter factor is an axonal chemoattractant and a neurotrophic factor for spinal motor neurons
    • Ebens A., Brose K., Leonardo E.D., Hanson Jr. M.G., Bladt F., Birchmeier C., Barres B.A., and Tessier-Lavigne M. Hepatocyte growth factor/scatter factor is an axonal chemoattractant and a neurotrophic factor for spinal motor neurons. Neuron 17 (1996) 1157-1172
    • (1996) Neuron , vol.17 , pp. 1157-1172
    • Ebens, A.1    Brose, K.2    Leonardo, E.D.3    Hanson Jr., M.G.4    Bladt, F.5    Birchmeier, C.6    Barres, B.A.7    Tessier-Lavigne, M.8
  • 135
    • 2542459332 scopus 로고    scopus 로고
    • EGF family of growth factors: essential roles and functional redundancy in the nerve system
    • Xian C.J., and Zhou X.F. EGF family of growth factors: essential roles and functional redundancy in the nerve system. Front. Biosci. 9 (2004) 85-92
    • (2004) Front. Biosci. , vol.9 , pp. 85-92
    • Xian, C.J.1    Zhou, X.F.2
  • 137
    • 27644556565 scopus 로고    scopus 로고
    • HB-EGF promotes epithelial cell migration in eyelid development
    • Mine N., Iwamoto R., and Mekada E. HB-EGF promotes epithelial cell migration in eyelid development. Development 132 (2005) 4317-4326
    • (2005) Development , vol.132 , pp. 4317-4326
    • Mine, N.1    Iwamoto, R.2    Mekada, E.3
  • 138
    • 0032387827 scopus 로고    scopus 로고
    • Contributions of the epidermal growth factor receptor to keratinocyte motility
    • Hudson L.G., and McCawley L.J. Contributions of the epidermal growth factor receptor to keratinocyte motility. Microsc. Res. Tech. 43 (1998) 444-455
    • (1998) Microsc. Res. Tech. , vol.43 , pp. 444-455
    • Hudson, L.G.1    McCawley, L.J.2
  • 140
    • 0028089832 scopus 로고
    • Epidermal growth factor receptor-mediated cell motility: phospholipase C activity is required, but mitogen-activated protein kinase activity is not sufficient for induced cell movement
    • Chen P., Xie H., Sekar M.C., Gupta K., and Wells A. Epidermal growth factor receptor-mediated cell motility: phospholipase C activity is required, but mitogen-activated protein kinase activity is not sufficient for induced cell movement. J. Cell Biol. 127 (1994) 847-857
    • (1994) J. Cell Biol. , vol.127 , pp. 847-857
    • Chen, P.1    Xie, H.2    Sekar, M.C.3    Gupta, K.4    Wells, A.5
  • 141
    • 0029758126 scopus 로고    scopus 로고
    • A role for gelsolin in actuating epidermal growth factor receptor-mediated cell motility
    • Chen P., Murphy-Ullrich J.E., and Wells A. A role for gelsolin in actuating epidermal growth factor receptor-mediated cell motility. J. Cell Biol. 134 (1996) 689-698
    • (1996) J. Cell Biol. , vol.134 , pp. 689-698
    • Chen, P.1    Murphy-Ullrich, J.E.2    Wells, A.3
  • 142
    • 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., and 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
  • 145
    • 0032549570 scopus 로고    scopus 로고
    • Overexpression of EGFR and c-erbB2 causes enhanced cell migration in human breast cancer cells and NIH3T3 fibroblasts
    • Verbeek B.S., Adriaansen-Slot S.S., Vroom T.M., Beckers T., and Rijksen G. Overexpression of EGFR and c-erbB2 causes enhanced cell migration in human breast cancer cells and NIH3T3 fibroblasts. FEBS Lett. 425 (1998) 145-150
    • (1998) FEBS Lett. , vol.425 , pp. 145-150
    • Verbeek, B.S.1    Adriaansen-Slot, S.S.2    Vroom, T.M.3    Beckers, T.4    Rijksen, G.5
  • 147
    • 0034723310 scopus 로고    scopus 로고
    • Epidermal growth factor receptor activation of calpain is required for fibroblast motility and occurs via an ERK/MAP kinase signaling pathway
    • Glading A., Chang P., Lauffenburger D.A., and Wells A. Epidermal growth factor receptor activation of calpain is required for fibroblast motility and occurs via an ERK/MAP kinase signaling pathway. J. Biol. Chem. 275 (2000) 2390-2398
    • (2000) J. Biol. Chem. , vol.275 , pp. 2390-2398
    • Glading, A.1    Chang, P.2    Lauffenburger, D.A.3    Wells, A.4
  • 149
    • 0842288222 scopus 로고    scopus 로고
    • Distinct roles of MLCK and ROCK in the regulation of membrane protrusions and focal adhesion dynamics during cell migration of fibroblasts
    • Totsukawa G., Wu Y., Sasaki Y., Hartshorne D.J., Yamakita Y., Yamashiro S., and Matsumura F. Distinct roles of MLCK and ROCK in the regulation of membrane protrusions and focal adhesion dynamics during cell migration of fibroblasts. J. Cell Biol. 164 (2004) 427-439
    • (2004) J. Cell Biol. , vol.164 , pp. 427-439
    • Totsukawa, G.1    Wu, Y.2    Sasaki, Y.3    Hartshorne, D.J.4    Yamakita, Y.5    Yamashiro, S.6    Matsumura, F.7
  • 150
    • 0031829163 scopus 로고    scopus 로고
    • Activation of both MAP kinase and phosphatidylinositide 3-kinase by Ras is required for hepatocyte growth factor/scatter factor-induced adherens junction disassembly
    • Potempa S., and Ridley A.J. Activation of both MAP kinase and phosphatidylinositide 3-kinase by Ras is required for hepatocyte growth factor/scatter factor-induced adherens junction disassembly. Mol. Biol. Cell 9 (1998) 2185-2200
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2185-2200
    • Potempa, S.1    Ridley, A.J.2
  • 151
    • 6344248651 scopus 로고    scopus 로고
    • PKC controls HGF-dependent c-Met traffic, signalling and cell migration
    • Kermorgant S., Zicha D., and Parker P.J. PKC controls HGF-dependent c-Met traffic, signalling and cell migration. EMBO J. 23 (2004) 3721-3734
    • (2004) EMBO J. , vol.23 , pp. 3721-3734
    • Kermorgant, S.1    Zicha, D.2    Parker, P.J.3
  • 152
    • 0041924982 scopus 로고    scopus 로고
    • A novel role for FAK as a protease-targeting adaptor protein: regulation by p42 ERK and Src
    • Carragher N.O., Westhoff M.A., Fincham V.J., Schaller M.D., and Frame M.C. A novel role for FAK as a protease-targeting adaptor protein: regulation by p42 ERK and Src. Curr. Biol. 13 (2003) 1442-1450
    • (2003) Curr. Biol. , vol.13 , pp. 1442-1450
    • Carragher, N.O.1    Westhoff, M.A.2    Fincham, V.J.3    Schaller, M.D.4    Frame, M.C.5
  • 153
    • 0032539001 scopus 로고    scopus 로고
    • The transcription factor AP-1 is required for EGF-induced activation of rho-like GTPases, cytoskeletal rearrangements, motility, and in vitro invasion of A431 cells
    • Malliri A., Symons M., Hennigan R.F., Hurlstone A.F., Lamb R.F., Wheeler T., and Ozanne B.W. The transcription factor AP-1 is required for EGF-induced activation of rho-like GTPases, cytoskeletal rearrangements, motility, and in vitro invasion of A431 cells. J. Cell Biol. 143 (1998) 1087-1099
    • (1998) J. Cell Biol. , vol.143 , pp. 1087-1099
    • Malliri, A.1    Symons, M.2    Hennigan, R.F.3    Hurlstone, A.F.4    Lamb, R.F.5    Wheeler, T.6    Ozanne, B.W.7
  • 154
    • 0025066916 scopus 로고
    • Role of the cytoskeleton during injury-induced cell migration in corneal endothelium
    • Gordon S.R., and Staley C.A. Role of the cytoskeleton during injury-induced cell migration in corneal endothelium. Cell Motil. Cytoskelet. 16 (1990) 47-57
    • (1990) Cell Motil. Cytoskelet. , vol.16 , pp. 47-57
    • Gordon, S.R.1    Staley, C.A.2
  • 155
    • 0026471680 scopus 로고
    • In vitro model of angiogenesis using a human endothelium-derived permanent cell line: contributions of induced gene expression, G-proteins, and integrins
    • Bauer J., Margolis M., Schreiner C., Edgell C.J., Azizkhan J., Lazarowski E., and Juliano R.L. In vitro model of angiogenesis using a human endothelium-derived permanent cell line: contributions of induced gene expression, G-proteins, and integrins. J. Cell. Physiol. 153 (1992) 437-449
    • (1992) J. Cell. Physiol. , vol.153 , pp. 437-449
    • Bauer, J.1    Margolis, M.2    Schreiner, C.3    Edgell, C.J.4    Azizkhan, J.5    Lazarowski, E.6    Juliano, R.L.7
  • 156
  • 157
    • 0042349229 scopus 로고    scopus 로고
    • ERK-MAPK signaling coordinately regulates activity of Rac1 and RhoA for tumor cell motility
    • Vial E., Sahai E., and Marshall C.J. ERK-MAPK signaling coordinately regulates activity of Rac1 and RhoA for tumor cell motility. Cancer Cell 4 (2003) 67-79
    • (2003) Cancer Cell , vol.4 , pp. 67-79
    • Vial, E.1    Sahai, E.2    Marshall, C.J.3
  • 158
    • 20344379187 scopus 로고    scopus 로고
    • The MEK1 scaffolding protein MP1 regulates cell spreading by integrating PAK1 and Rho signals
    • Pullikuth A., McKinnon E., Schaeffer H.J., and Catling A.D. The MEK1 scaffolding protein MP1 regulates cell spreading by integrating PAK1 and Rho signals. Mol. Cell. Biol. 25 (2005) 5119-5133
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 5119-5133
    • Pullikuth, A.1    McKinnon, E.2    Schaeffer, H.J.3    Catling, A.D.4
  • 159
    • 18844438135 scopus 로고    scopus 로고
    • Activation of either ERK1/2 or ERK5 MAP kinase pathways can lead to disruption of the actin cytoskeleton
    • Barros J.C., and Marshall C.J. Activation of either ERK1/2 or ERK5 MAP kinase pathways can lead to disruption of the actin cytoskeleton. J. Cell. Sci. 118 (2005) 1663-1671
    • (2005) J. Cell. Sci. , vol.118 , pp. 1663-1671
    • Barros, J.C.1    Marshall, C.J.2
  • 160
  • 161
    • 0035476836 scopus 로고    scopus 로고
    • Inhibition of focal adhesion kinase expression or activity disrupts epidermal growth factor-stimulated signaling promoting the migration of invasive human carcinoma cells
    • Hauck C.R., Sieg D.J., Hsia D.A., Loftus J.C., Gaarde W.A., Monia B.P., and Schlaepfer D.D. Inhibition of focal adhesion kinase expression or activity disrupts epidermal growth factor-stimulated signaling promoting the migration of invasive human carcinoma cells. Cancer Res. 61 (2001) 7079-7090
    • (2001) Cancer Res. , vol.61 , pp. 7079-7090
    • Hauck, C.R.1    Sieg, D.J.2    Hsia, D.A.3    Loftus, J.C.4    Gaarde, W.A.5    Monia, B.P.6    Schlaepfer, D.D.7
  • 163
    • 0034625170 scopus 로고    scopus 로고
    • MEK kinase 1 is critically required for c-Jun N-terminal kinase activation by proinflammatory stimuli and growth factor-induced cell migration
    • Xia Y., Makris C., Su B., Li E., Yang J., Nemerow G.R., and Karin M. MEK kinase 1 is critically required for c-Jun N-terminal kinase activation by proinflammatory stimuli and growth factor-induced cell migration. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 5243-5248
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 5243-5248
    • Xia, Y.1    Makris, C.2    Su, B.3    Li, E.4    Yang, J.5    Nemerow, G.R.6    Karin, M.7
  • 165
    • 33744927684 scopus 로고    scopus 로고
    • Epidermal growth factor induces insulin receptor substrate-2 in breast cancer cells via c-Jun NH(2)-terminal kinase/activator protein-1 signaling to regulate cell migration
    • Cui X., Kim H.J., Kuiatse I., Kim H., Brown P.H., and Lee A.V. Epidermal growth factor induces insulin receptor substrate-2 in breast cancer cells via c-Jun NH(2)-terminal kinase/activator protein-1 signaling to regulate cell migration. Cancer Res. 66 (2006) 5304-5313
    • (2006) Cancer Res. , vol.66 , pp. 5304-5313
    • Cui, X.1    Kim, H.J.2    Kuiatse, I.3    Kim, H.4    Brown, P.H.5    Lee, A.V.6
  • 166
    • 33744544424 scopus 로고    scopus 로고
    • p38 and a p38-interacting protein are critical for downregulation of E-cadherin during mouse gastrulation
    • Zohn I.E., Li Y., Skolnik E.Y., Anderson K.V., Han J., and Niswander L. p38 and a p38-interacting protein are critical for downregulation of E-cadherin during mouse gastrulation. Cell 125 (2006) 957-969
    • (2006) Cell , vol.125 , pp. 957-969
    • Zohn, I.E.1    Li, Y.2    Skolnik, E.Y.3    Anderson, K.V.4    Han, J.5    Niswander, L.6
  • 169
    • 0028252924 scopus 로고
    • Steel factor and c-kit protooncogene: genetic lessons in signal transduction
    • Lev S., Blechman J.M., Givol D., and Yarden Y. Steel factor and c-kit protooncogene: genetic lessons in signal transduction. Crit. Rev. Oncog. 5 (1994) 141-168
    • (1994) Crit. Rev. Oncog. , vol.5 , pp. 141-168
    • Lev, S.1    Blechman, J.M.2    Givol, D.3    Yarden, Y.4
  • 170
    • 0032857449 scopus 로고    scopus 로고
    • The biology of stem cell factor and its receptor C-kit
    • Ashman L.K. The biology of stem cell factor and its receptor C-kit. Int. J. Biochem. Cell Biol. 31 (1999) 1037-1051
    • (1999) Int. J. Biochem. Cell Biol. , vol.31 , pp. 1037-1051
    • Ashman, L.K.1
  • 171
    • 0029891236 scopus 로고    scopus 로고
    • Regulation of colony-stimulating factor 1 receptor signaling by the SH2 domain-containing tyrosine phosphatase SHPTP1
    • Chen H.E., Chang S., Trub T., and Neel B.G. Regulation of colony-stimulating factor 1 receptor signaling by the SH2 domain-containing tyrosine phosphatase SHPTP1. Mol. Cell. Biol. 16 (1996) 3685-3697
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3685-3697
    • Chen, H.E.1    Chang, S.2    Trub, T.3    Neel, B.G.4
  • 172
    • 0034693757 scopus 로고    scopus 로고
    • The Ret proto-oncogene in human cancer
    • Jhiang S.M. The Ret proto-oncogene in human cancer. Oncogene 19 (2000) 5590-5597
    • (2000) Oncogene , vol.19 , pp. 5590-5597
    • Jhiang, S.M.1
  • 175
    • 5644293135 scopus 로고    scopus 로고
    • Gefitinib induces apoptosis in the EGFRL858R non-small-cell lung cancer cell line H3255
    • Tracy S., Mukohara T., Hansen M., Meyerson M., Johnson B.E., and Janne P.A. Gefitinib induces apoptosis in the EGFRL858R non-small-cell lung cancer cell line H3255. Cancer Res. 64 (2004) 7241-7244
    • (2004) Cancer Res. , vol.64 , pp. 7241-7244
    • Tracy, S.1    Mukohara, T.2    Hansen, M.3    Meyerson, M.4    Johnson, B.E.5    Janne, P.A.6
  • 176
    • 1842471336 scopus 로고    scopus 로고
    • Signaling through the epidermal growth factor receptor during the development of malignancy
    • Grandis J.R., and Sok J.C. Signaling through the epidermal growth factor receptor during the development of malignancy. Pharmacol. Ther. 102 (2004) 37-46
    • (2004) Pharmacol. Ther. , vol.102 , pp. 37-46
    • Grandis, J.R.1    Sok, J.C.2
  • 180
    • 0026521394 scopus 로고
    • Amplified and rearranged epidermal growth factor receptor genes in human glioblastomas reveal deletions of sequences encoding portions of the N- and/or C-terminal tails
    • Ekstrand A.J., Sugawa N., James C.D., and Collins V.P. Amplified and rearranged epidermal growth factor receptor genes in human glioblastomas reveal deletions of sequences encoding portions of the N- and/or C-terminal tails. Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 4309-4313
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 4309-4313
    • Ekstrand, A.J.1    Sugawa, N.2    James, C.D.3    Collins, V.P.4
  • 181
    • 0023912033 scopus 로고
    • Amplification of the structurally and functionally altered epidermal growth factor receptor gene (c-erbB) in human brain tumors
    • Yamazaki H., Fukui Y., Ueyama Y., Tamaoki N., Kawamoto T., Taniguchi S., and Shibuya M. Amplification of the structurally and functionally altered epidermal growth factor receptor gene (c-erbB) in human brain tumors. Mol. Cell. Biol. 8 (1988) 1816-1820
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 1816-1820
    • Yamazaki, H.1    Fukui, Y.2    Ueyama, Y.3    Tamaoki, N.4    Kawamoto, T.5    Taniguchi, S.6    Shibuya, M.7
  • 182
    • 14444288522 scopus 로고    scopus 로고
    • H.S. Huang, M. Nagane, C.K. Klingbeil, H. Lin, R. Nishikawa, X.D. Ji, C.M. Huang, G.N. Gill, H.S. Wiley and W.K. Cavenee, The enhanced tumorigenic activity of a mutant epidermal growth factor receptor common in human cancers is mediated by threshold levels of constitutive tyrosine phosphorylation and unattenuated signaling, J. Biol. Chem. 272 (1997) 2927-35 0021-9258.
  • 185
    • 0028670125 scopus 로고
    • The biology of erbB-2/neu/HER-2 and its role in cancer
    • Hynes N.E., and Stern D.F. The biology of erbB-2/neu/HER-2 and its role in cancer. Biochem. Biophys. Acta 1198 (1994) 165-184
    • (1994) Biochem. Biophys. Acta , vol.1198 , pp. 165-184
    • Hynes, N.E.1    Stern, D.F.2
  • 186
    • 0033992633 scopus 로고    scopus 로고
    • Biochemical and clinical implications of the ErbB/HER signaling network of growth factor receptors
    • Klapper L.N., Kirschbaum M.H., Sela M., and Yarden Y. Biochemical and clinical implications of the ErbB/HER signaling network of growth factor receptors. Adv. Cancer Res. 77 (2000) 25-79
    • (2000) Adv. Cancer Res. , vol.77 , pp. 25-79
    • Klapper, L.N.1    Kirschbaum, M.H.2    Sela, M.3    Yarden, Y.4
  • 187
    • 0032460777 scopus 로고    scopus 로고
    • Clinical results of transhiatal esophagectomy for carcinoma of the lower thoracic esophagus according to biological markers
    • Hirai T., Kuwahara M., Yoshida K., Kagawa Y., Hihara J., Yamashita Y., and Toge T. Clinical results of transhiatal esophagectomy for carcinoma of the lower thoracic esophagus according to biological markers. Dis. Esophagus 11 (1998) 221-225
    • (1998) Dis. Esophagus , vol.11 , pp. 221-225
    • Hirai, T.1    Kuwahara, M.2    Yoshida, K.3    Kagawa, Y.4    Hihara, J.5    Yamashita, Y.6    Toge, T.7
  • 188
    • 0010622002 scopus 로고
    • Immunohistochemical evidence of autocrine growth factors in adenocarcinoma of the human lung
    • Tateishi M., Ishida T., Mitsudomi T., Kaneko S., and Sugimachi K. Immunohistochemical evidence of autocrine growth factors in adenocarcinoma of the human lung. Cancer Res. 12 (1990) 1183-1188
    • (1990) Cancer Res. , vol.12 , pp. 1183-1188
    • Tateishi, M.1    Ishida, T.2    Mitsudomi, T.3    Kaneko, S.4    Sugimachi, K.5
  • 190
    • 0037264633 scopus 로고    scopus 로고
    • Targeting RAS signalling pathways in cancer therapy
    • Downward J. Targeting RAS signalling pathways in cancer therapy. Nat. Rev., Cancer 3 (2003) 11-22
    • (2003) Nat. Rev., Cancer , vol.3 , pp. 11-22
    • Downward, J.1
  • 191
    • 0032544525 scopus 로고    scopus 로고
    • Modulation of kinase activity and oncogenic properties by alternative splicing reveals a novel regulatory mechanism for B-Raf
    • Papin C., Denouel-Galy A., Laugier D., Calothy G., and Eychene A. Modulation of kinase activity and oncogenic properties by alternative splicing reveals a novel regulatory mechanism for B-Raf. J. Biol. Chem. 273 (1998) 24939-24947
    • (1998) J. Biol. Chem. , vol.273 , pp. 24939-24947
    • Papin, C.1    Denouel-Galy, A.2    Laugier, D.3    Calothy, G.4    Eychene, A.5


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