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Volumn 39, Issue 4-5, 2002, Pages 285-330

Ras-MAP kinase signaling pathways and control of cell proliferation: Relevance to cancer therapy

Author keywords

Cancer; Cell cycle checkpoints; Cell proliferation; Drug discovery; Phosphorylation; Signal transduction

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; RAS PROTEIN;

EID: 0036400204     PISSN: 10408363     EISSN: None     Source Type: Journal    
DOI: 10.1080/10408360290795538     Document Type: Review
Times cited : (88)

References (353)
  • 2
    • 0015493877 scopus 로고
    • Studies on the mechanism of hormone action
    • Sutherland EW. Studies on the mechanism of hormone action. Science 1972; 177: 401-408.
    • (1972) Science , vol.177 , pp. 401-408
    • Sutherland, E.W.1
  • 3
    • 0034600389 scopus 로고    scopus 로고
    • The Nobel chronicles. 1992: Edmond H Fischer (b 1920) and Edwin G Krebs (b 1918)
    • Raju, TN. The Nobel chronicles. 1992: Edmond H Fischer (b 1920) and Edwin G Krebs (b 1918). Lancet 2000; 355: 2004.
    • (2000) Lancet , vol.355 , pp. 2004
    • Raju, T.N.1
  • 4
    • 0031000626 scopus 로고    scopus 로고
    • Megakaryocytic differentiation induced by constitutive activation of mitogen-activated protein kinase kinase
    • Whalen AM, Galasinski SC, Shapiro PS, et al. Megakaryocytic differentiation induced by constitutive activation of mitogen-activated protein kinase kinase. Mol Cell Biol 1997; 17: 1947-1958.
    • (1997) Mol Cell Biol , vol.17 , pp. 1947-1958
    • Whalen, A.M.1    Galasinski, S.C.2    Shapiro, P.S.3
  • 6
    • 0024376173 scopus 로고
    • Ras oncogenes in human cancer: A review
    • Bos JL. Ras oncogenes in human cancer: a review. Cancer Res 1989; 49: 4682-4689.
    • (1989) Cancer Res , vol.49 , pp. 4682-4689
    • Bos, J.L.1
  • 7
    • 0020316263 scopus 로고
    • Tumorigenic transformation of mammalian cells induced by a normal human gene homologous to the oncogene of Harvey murine sarcoma virus
    • Chang EH, Furth ME, Scolnick EM, et al. Tumorigenic transformation of mammalian cells induced by a normal human gene homologous to the oncogene of Harvey murine sarcoma virus. Nature 1982; 297: 479-483.
    • (1982) Nature , vol.297 , pp. 479-483
    • Chang, E.H.1    Furth, M.E.2    Scolnick, E.M.3
  • 8
    • 0020328955 scopus 로고
    • Human EJ bladder carcinoma oncogene is homologue of Harvey sarcoma virus ras gene
    • Parada LF, Tabin CJ, Shih C, et al. Human EJ bladder carcinoma oncogene is homologue of Harvey sarcoma virus ras gene. Nature 1982; 297: 474-478.
    • (1982) Nature , vol.297 , pp. 474-478
    • Parada, L.F.1    Tabin, C.J.2    Shih, C.3
  • 9
    • 0033025807 scopus 로고    scopus 로고
    • SH2 domains: From structure to energetics, a dual approach to the study of structure-function relationships
    • Grucza RA, Bradshaw JM, Futterer K, et al. SH2 domains: from structure to energetics, a dual approach to the study of structure-function relationships. Med Res Rev 1999; 19: 273-293.
    • (1999) Med Res Rev , vol.19 , pp. 273-293
    • Grucza, R.A.1    Bradshaw, J.M.2    Futterer, K.3
  • 10
    • 0027409064 scopus 로고
    • Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: Crystal structures of the complexed and peptide-free forms
    • Waksman G, Shoelson SE, Pant N, et al. Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms. Cell 1993; 72: 779-790.
    • (1993) Cell , vol.72 , pp. 779-790
    • Waksman, G.1    Shoelson, S.E.2    Pant, N.3
  • 11
    • 0033212986 scopus 로고    scopus 로고
    • Crystal structures of the XLP protein SAP reveal a class of SH2 domains with extended, phosphotyrosine-independent sequence recognition
    • Poy F, Yaffe MB, Sayos J, et al. Crystal structures of the XLP protein SAP reveal a class of SH2 domains with extended, phosphotyrosine-independent sequence recognition. Mol Cell 1999; 4: 555-561.
    • (1999) Mol Cell , vol.4 , pp. 555-561
    • Poy, F.1    Yaffe, M.B.2    Sayos, J.3
  • 12
    • 0028944585 scopus 로고
    • Growth hormone-promoted tyrosyl phosphorylation of SHC proteins and SHC association with Grb2
    • VanderKuur J, Allevato G, Billestrup N, et al. Growth hormone-promoted tyrosyl phosphorylation of SHC proteins and SHC association with Grb2. J Biol Chem 1995; 270: 7587-7593.
    • (1995) J Biol Chem , vol.270 , pp. 7587-7593
    • VanderKuur, J.1    Allevato, G.2    Billestrup, N.3
  • 13
    • 0030014704 scopus 로고    scopus 로고
    • Sos1 rapidly associates with Grb2 and is hypophosphorylated when complexed with the EGF receptor after EGF stimulation
    • Hu Y, Bowtell DD. Sos1 rapidly associates with Grb2 and is hypophosphorylated when complexed with the EGF receptor after EGF stimulation. Oncogene 1996; 12: 1865-1872.
    • (1996) Oncogene , vol.12 , pp. 1865-1872
    • Hu, Y.1    Bowtell, D.D.2
  • 14
    • 0028148629 scopus 로고
    • Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains
    • Lim WA, Richards FM, Fox RO. Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains. Nature 1994; 372: 375-379.
    • (1994) Nature , vol.372 , pp. 375-379
    • Lim, W.A.1    Richards, F.M.2    Fox, R.O.3
  • 15
    • 0033603324 scopus 로고    scopus 로고
    • Insulin-induced desensitization of extracellular signal-regulated kinase activation results from an inhibition of Raf activity independent of Ras activation and dissociation of the Grb2-SOS complex
    • Fucini RV, Okada S, Pessin JE. Insulin-induced desensitization of extracellular signal-regulated kinase activation results from an inhibition of Raf activity independent of Ras activation and dissociation of the Grb2-SOS complex. J Biol Chem 1999; 274: 18651-18658.
    • (1999) J Biol Chem , vol.274 , pp. 18651-18658
    • Fucini, R.V.1    Okada, S.2    Pessin, J.E.3
  • 16
    • 0031929680 scopus 로고    scopus 로고
    • N terminus of Sos1 Ras exchange factor: Critical roles for the Db1 and pleckstrin homology domains
    • Qian X, Vass WC, Papageorge AG, et al. N terminus of Sos1 Ras exchange factor: critical roles for the Db1 and pleckstrin homology domains. Mol Cell Biol 1998; 18: 771-778.
    • (1998) Mol Cell Biol , vol.18 , pp. 771-778
    • Qian, X.1    Vass, W.C.2    Papageorge, A.G.3
  • 17
    • 0033553526 scopus 로고    scopus 로고
    • Pleiotropic coupling of G protein-coupled receptors to the mitogen-activated protein kinase cascade. Role of focal adhesions and receptor tyrosine kinases
    • Della Rocca GJ, Maudsley S, Daaka Y, et al. Pleiotropic coupling of G protein-coupled receptors to the mitogen-activated protein kinase cascade. Role of focal adhesions and receptor tyrosine kinases. J Biol Chem 1999; 274: 13978-13984.
    • (1999) J Biol Chem , vol.274 , pp. 13978-13984
    • Della Rocca, G.J.1    Maudsley, S.2    Daaka, Y.3
  • 18
    • 0031257749 scopus 로고    scopus 로고
    • Focal adhesion kinase in integrin signaling
    • Guan JL. Focal adhesion kinase in integrin signaling. Matrix Biol 1997; 16: 195-200.
    • (1997) Matrix Biol , vol.16 , pp. 195-200
    • Guan, J.L.1
  • 19
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark EA, Brugge JS. Integrins and signal transduction pathways: the road taken. Science 1995; 268: 233-239.
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 20
    • 0031438076 scopus 로고    scopus 로고
    • G protein-coupled receptors mediate two functionally distinct pathways of tyrosine phosphorylation in rat 1a fibroblasts. Shc phosphorylation and receptor endocytosis correlate with activation of Erk kinases
    • Luttrell LM, Daaka Y, Della Rocca GJ, et al. G protein-coupled receptors mediate two functionally distinct pathways of tyrosine phosphorylation in rat 1a fibroblasts. Shc phosphorylation and receptor endocytosis correlate with activation of Erk kinases. J Biol Chem 1997; 272: 31648-31656.
    • (1997) J Biol Chem , vol.272 , pp. 31648-31656
    • Luttrell, L.M.1    Daaka, Y.2    Della Rocca, G.J.3
  • 21
    • 0030683639 scopus 로고    scopus 로고
    • Signal characteristics of G protein-transactivated EGF receptor
    • Daub H, Wallasch C, Lankenau A, et al. Signal characteristics of G protein-transactivated EGF receptor. EMBO J 1997; 16: 7032-7044.
    • (1997) EMBO J , vol.16 , pp. 7032-7044
    • Daub, H.1    Wallasch, C.2    Lankenau, A.3
  • 22
    • 0030044360 scopus 로고    scopus 로고
    • Role of transactivation of the EGF receptor in signalling by G-protein- coupled receptors
    • Daub H, Weiss FU, Wallasch C, et al. Role of transactivation of the EGF receptor in signalling by G-protein- coupled receptors. Nature 1996; 379: 557-560.
    • (1996) Nature , vol.379 , pp. 557-560
    • Daub, H.1    Weiss, F.U.2    Wallasch, C.3
  • 23
    • 0030880741 scopus 로고    scopus 로고
    • Increasing complexity of Ras signal transduction: Involvement of Rho family proteins
    • Khosravi-Far R, Campbell S, Rossman KL, et al. Increasing complexity of Ras signal transduction: involvement of Rho family proteins. Adv Cancer Res 1998; 72: 57-107
    • (1998) Adv Cancer Res , vol.72 , pp. 57-107
    • Khosravi-Far, R.1    Campbell, S.2    Rossman, K.L.3
  • 24
    • 0035902180 scopus 로고    scopus 로고
    • Oncogenic kinase signalling
    • Blume-Jensen P, Hunter T. Oncogenic kinase signalling. Nature 2001; 411: 355-365.
    • (2001) Nature , vol.411 , pp. 355-365
    • Blume-Jensen, P.1    Hunter, T.2
  • 25
    • 0032752063 scopus 로고    scopus 로고
    • Cellular survival: A play in three Akts
    • Datta SR, Brunet A, Greenberg ME. Cellular survival: a play in three Akts. Genes Dev 1999; 13: 2905-2927.
    • (1999) Genes Dev , vol.13 , pp. 2905-2927
    • Datta, S.R.1    Brunet, A.2    Greenberg, M.E.3
  • 26
    • 0028918408 scopus 로고
    • Ras-dependent induction of cellular responses by constitutively active phosphatidylinositol-3 kinase
    • Hu Q, Klippel A, Muslin AJ, et al. Ras-dependent induction of cellular responses by constitutively active phosphatidylinositol-3 kinase. Science 1995; 268: 100-102
    • (1995) Science , vol.268 , pp. 100-102
    • Hu, Q.1    Klippel, A.2    Muslin, A.J.3
  • 27
    • 0035050958 scopus 로고    scopus 로고
    • The cell survival signal Akt is differentially activated by PDGFBB, EGF, and FGF-2 in osteoblastic cells
    • Chaudhary LR, Hruska KA. The cell survival signal Akt is differentially activated by PDGFBB, EGF, and FGF-2 in osteoblastic cells. J Cell Biochem 2001; 81: 304-311.
    • (2001) J Cell Biochem , vol.81 , pp. 304-311
    • Chaudhary, L.R.1    Hruska, K.A.2
  • 28
    • 0035869175 scopus 로고    scopus 로고
    • PTEN inhibits insulin-stimulated MEK/MAPK activation and cell growth by blocking IRS-1 phosphorylation and IRS-1/Grb-2/Sos complex formation in a breast cancer model
    • Weng LP, Smith WM, Brown JL, et al. PTEN inhibits insulin-stimulated MEK/MAPK activation and cell growth by blocking IRS-1 phosphorylation and IRS-1/Grb-2/Sos complex formation in a breast cancer model. Hum Mol Genet 2001; 10: 605-616.
    • (2001) Hum Mol Genet , vol.10 , pp. 605-616
    • Weng, L.P.1    Smith, W.M.2    Brown, J.L.3
  • 29
    • 0029883564 scopus 로고    scopus 로고
    • N-terminal sequences contained in the Src homology 2 and 3 domains of p120 GTPase-activating protein are required for full catalytic activity toward Ras
    • Bryant SS, Mitchell AL, Collins F, et al. N-terminal sequences contained in the Src homology 2 and 3 domains of p120 GTPase-activating protein are required for full catalytic activity toward Ras. J Biol Chem 1996; 271: 5195-5199.
    • (1996) J Biol Chem , vol.271 , pp. 5195-5199
    • Bryant, S.S.1    Mitchell, A.L.2    Collins, F.3
  • 30
    • 0026436279 scopus 로고
    • The prenylation of proteins
    • Sinensky M, Lutz RJ. The prenylation of proteins. Bioessays 1992; 14: 25-31.
    • (1992) Bioessays , vol.14 , pp. 25-31
    • Sinensky, M.1    Lutz, R.J.2
  • 31
    • 0026895892 scopus 로고
    • Protein prenylation: Key to ras function and cancer intervention?
    • Khosravi-Far R, Cox AD, Kato K, et al. Protein prenylation: key to ras function and cancer intervention? Cell Growth Differ 1992; 3: 461-469.
    • (1992) Cell Growth Differ , vol.3 , pp. 461-469
    • Khosravi-Far, R.1    Cox, A.D.2    Kato, K.3
  • 32
    • 0032564385 scopus 로고    scopus 로고
    • Crystal structure of farnesyl protein transferase complexed with a CaaX peptide and farnesyl diphosphate analogue
    • Strickland CL, Windsor WT, Syto R, et al. Crystal structure of farnesyl protein transferase complexed with a CaaX peptide and farnesyl diphosphate analogue. Biochemistry 1998; 37: 16601-16611.
    • (1998) Biochemistry , vol.37 , pp. 16601-16611
    • Strickland, C.L.1    Windsor, W.T.2    Syto, R.3
  • 33
    • 0034284027 scopus 로고    scopus 로고
    • Targeting the Ras signaling pathway: A rational, mechanism-based treatment for hematologic malignancies?
    • Reuter CW, Morgan MA, Bergmann L. Targeting the Ras signaling pathway: a rational, mechanism-based treatment for hematologic malignancies? Blood 2000; 96: 1655-1669.
    • (2000) Blood , vol.96 , pp. 1655-1669
    • Reuter, C.W.1    Morgan, M.A.2    Bergmann, L.3
  • 34
    • 0035064177 scopus 로고    scopus 로고
    • Ras biochemistry and farnesyl transferase inhibitors: A literature survey
    • Crul M, de Klerk GJ, Beijnen JH, et al. Ras biochemistry and farnesyl transferase inhibitors: a literature survey. Anticancer Drugs 2001; 12: 163-184.
    • (2001) Anticancer Drugs , vol.12 , pp. 163-184
    • Crul, M.1    De Klerk, G.J.2    Beijnen, J.H.3
  • 35
    • 0028331587 scopus 로고
    • Farnesyltransferase inhibitors: Ras research yields a potential cancer therapeutic
    • Gibbs JB, Oliff A, Kohl NE. Farnesyltransferase inhibitors: Ras research yields a potential cancer therapeutic. Cell 1994; 77: 175-178.
    • (1994) Cell , vol.77 , pp. 175-178
    • Gibbs, J.B.1    Oliff, A.2    Kohl, N.E.3
  • 36
    • 0034638835 scopus 로고    scopus 로고
    • Reversal of the Ras-induced transformed phenotype by HR12, a novel ras farnesylation inhibitor, is mediated by the Mek/Erk pathway
    • Reuveni H, Geiger T, Geiger B, et al. Reversal of the Ras-induced transformed phenotype by HR12, a novel ras farnesylation inhibitor, is mediated by the Mek/Erk pathway. J Cell Biol 2000; 151: 1179-1192.
    • (2000) J Cell Biol , vol.151 , pp. 1179-1192
    • Reuveni, H.1    Geiger, T.2    Geiger, B.3
  • 37
    • 0026909770 scopus 로고
    • Ras and human tumors
    • Rodenhuis S. ras and human tumors. Semin Cancer Biol 1992; 3: 241-247.
    • (1992) Semin Cancer Biol , vol.3 , pp. 241-247
    • Rodenhuis, S.1
  • 38
    • 0034730625 scopus 로고    scopus 로고
    • Farnesyl transferase inhibitors block the farnesylation of CENP-E and CENP-F and alter the association of CENP-E with the microtubules
    • Ashar HR, James L, Gray K, et al. Farnesyl transferase inhibitors block the farnesylation of CENP-E and CENP-F and alter the association of CENP-E with the microtubules. J Biol Chem 2000; 275: 30451-30457.
    • (2000) J Biol Chem , vol.275 , pp. 30451-30457
    • Ashar, H.R.1    James, L.2    Gray, K.3
  • 39
    • 0033539952 scopus 로고    scopus 로고
    • Growth inhibition of astrocytoma cells by farnesyl transferase inhibitors is mediated by a combination of anti-proliferative, pro-apoptotic and anti-angiogenic effects
    • Feldkamp MM, Lau N, Guha A. Growth inhibition of astrocytoma cells by farnesyl transferase inhibitors is mediated by a combination of anti-proliferative, pro-apoptotic and anti-angiogenic effects. Oncogene 1999; 18: 7514-7526.
    • (1999) Oncogene , vol.18 , pp. 7514-7526
    • Feldkamp, M.M.1    Lau, N.2    Guha, A.3
  • 40
    • 0027925812 scopus 로고
    • Proteins with SH2 and SH3 domains couple receptor tyrosine kinases to intracellular signalling pathways
    • Pawson T, Olivier P, Rozakis-Adcock M, et al. Proteins with SH2 and SH3 domains couple receptor tyrosine kinases to intracellular signalling pathways. Philos Trans R Soc Lond B Biol Sci 1993; 340: 279-285.
    • (1993) Philos Trans R Soc Lond B Biol Sci , vol.340 , pp. 279-285
    • Pawson, T.1    Olivier, P.2    Rozakis-Adcock, M.3
  • 41
    • 0034115006 scopus 로고    scopus 로고
    • Progress in the development of inhibitors of SH2 domains
    • Cody WL, Lin Z, Panek RL, et al. Progress in the development of inhibitors of SH2 domains. Curr Pharm Des 2000; 6: 59-98.
    • (2000) Curr Pharm Des , vol.6 , pp. 59-98
    • Cody, W.L.1    Lin, Z.2    Panek, R.L.3
  • 42
    • 0035140098 scopus 로고    scopus 로고
    • Bone-targeted Src SH2 inhibitors block Src cellular activity and osteoclast-mediated resorption
    • Violette SM, Guan W, Bartlett C, et al. Bone-targeted Src SH2 inhibitors block Src cellular activity and osteoclast-mediated resorption. Bone 2001; 28: 54-64.
    • (2001) Bone , vol.28 , pp. 54-64
    • Violette, S.M.1    Guan, W.2    Bartlett, C.3
  • 43
    • 0035415663 scopus 로고    scopus 로고
    • SH2 domain inhibition: A problem solved?
    • Shakespeare WC. SH2 domain inhibition: a problem solved? Curr Opin Chem Biol 2001; 5: 409-415.
    • (2001) Curr Opin Chem Biol , vol.5 , pp. 409-415
    • Shakespeare, W.C.1
  • 44
    • 0033826421 scopus 로고    scopus 로고
    • Recent advances in the design and synthesis of SH2 inhibitors of Src, Grb2 and ZAP70
    • Vu CB. Recent advances in the design and synthesis of SH2 inhibitors of Src, Grb2 and ZAP70. Curr Med Chem 2000; 7: 1081-1100.
    • (2000) Curr Med Chem , vol.7 , pp. 1081-1100
    • Vu, C.B.1
  • 45
    • 0034658354 scopus 로고    scopus 로고
    • Cloning and characterization of human Lnk, an adaptor protein with pleckstrin homology and Src homology 2 domains that can inhibit T cell activation
    • Li Y, He X, Schembri-King J, et al. Cloning and characterization of human Lnk, an adaptor protein with pleckstrin homology and Src homology 2 domains that can inhibit T cell activation. J Immunol 2000; 164: 5199-5206.
    • (2000) J Immunol , vol.164 , pp. 5199-5206
    • Li, Y.1    He, X.2    Schembri-King, J.3
  • 46
    • 0345434814 scopus 로고    scopus 로고
    • Potent inhibition of Grb2 SH2 domain binding by non-phosphate- containing ligands
    • Yao ZJ, King CR, Cao T, et al. Potent inhibition of Grb2 SH2 domain binding by non-phosphate- containing ligands. J Med Chem 1999; 42: 25-35.
    • (1999) J Med Chem , vol.42 , pp. 25-35
    • Yao, Z.J.1    King, C.R.2    Cao, T.3
  • 47
    • 0034624812 scopus 로고    scopus 로고
    • Inhibition of Grb2 SH2 domain binding by non-phosphate-containing ligands. 2. 4-(2-Malonyl)phenylalanine as a potent phosphotyrosyl mimetic
    • Gao Y, Luo J, Yao ZJ, et al. Inhibition of Grb2 SH2 domain binding by non-phosphate-containing ligands. 2. 4-(2-Malonyl)phenylalanine as a potent phosphotyrosyl mimetic. J Med Chem 2000; 43: 911-920.
    • (2000) J Med Chem , vol.43 , pp. 911-920
    • Gao, Y.1    Luo, J.2    Yao, Z.J.3
  • 48
    • 0005261734 scopus 로고
    • Rapid stimulation by insulin of a serine/threonine kinase in 3T3-L1 adipocytes that phosphorylates microtubule-associated protein 2 in vitro
    • Ray LB, Sturgill TW. Rapid stimulation by insulin of a serine/threonine kinase in 3T3-L1 adipocytes that phosphorylates microtubule-associated protein 2 in vitro. Proc Natl Acad Sci USA 1987; 84: 1502-1506.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 1502-1506
    • Ray, L.B.1    Sturgill, T.W.2
  • 49
    • 0001589410 scopus 로고
    • Insulin-stimulated microtubule-associated protein kinase is phosphorylated on tyrosine and threonine in vivo
    • Ray LB, Sturgill TW. Insulin-stimulated microtubule-associated protein kinase is phosphorylated on tyrosine and threonine in vivo. Proc Natl Acad Sci USA 1988; 85: 3753-3757.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 3753-3757
    • Ray, L.B.1    Sturgill, T.W.2
  • 50
    • 0026165752 scopus 로고
    • Identification of multiple extracellular signal-regulated kinases (ERKs) with antipeptide antibodies
    • Boulton TG, Cobb MH. Identification of multiple extracellular signal-regulated kinases (ERKs) with antipeptide antibodies. Cell Regul 1991; 2: 357-371.
    • (1991) Cell Regul , vol.2 , pp. 357-371
    • Boulton, T.G.1    Cobb, M.H.2
  • 51
    • 0031900740 scopus 로고    scopus 로고
    • Signal tranduction through MAP kinase cascades
    • Lewis TS, Shapiro PS, Ahn NG. Signal tranduction through MAP Kinase Cascades. Advan Cancer Res 1998; 74: 49-139
    • (1998) Advan Cancer Res , vol.74 , pp. 49-139
    • Lewis, T.S.1    Shapiro, P.S.2    Ahn, N.G.3
  • 52
    • 0028935974 scopus 로고
    • Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms
    • published erratum appears in Science 1995 Jul 7;269[5220]:17
    • Derijard B, Raingeaud J, Barrett T, et al. Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms (published erratum appears in Science 1995 Jul 7;269[5220]:17). Science 1995; 267: 682-685.
    • (1995) Science , vol.267 , pp. 682-685
    • Derijard, B.1    Raingeaud, J.2    Barrett, T.3
  • 53
    • 0025823448 scopus 로고
    • ERKs: A family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF
    • Boulton TG, Nye SH, Robbins DJ, et al. ERKs: a family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF. Cell 1991; 65: 663-675.
    • (1991) Cell , vol.65 , pp. 663-675
    • Boulton, T.G.1    Nye, S.H.2    Robbins, D.J.3
  • 54
    • 0025832605 scopus 로고
    • Multiple components in an epidermal growth factor-stimulated protein kinase cascade. In vitro activation of a myelin basic protein/microtubule-associated protein 2 kinase
    • Ahn NG, Seger R, Bratlien RL, et al. Multiple components in an epidermal growth factor-stimulated protein kinase cascade. In vitro activation of a myelin basic protein/microtubule-associated protein 2 kinase. J Biol Chem 1991; 266: 4220-4227.
    • (1991) J Biol Chem , vol.266 , pp. 4220-4227
    • Ahn, N.G.1    Seger, R.2    Bratlien, R.L.3
  • 55
    • 0032508538 scopus 로고    scopus 로고
    • MP1: A MEK binding partner that enhances enzymatic activation of the MAP kinase cascade
    • Schaeffer HJ, Catling AD, Eblen ST, et al. MP1: a MEK binding partner that enhances enzymatic activation of the MAP kinase cascade. Science 1998; 281: 1668-1671.
    • (1998) Science , vol.281 , pp. 1668-1671
    • Schaeffer, H.J.1    Catling, A.D.2    Eblen, S.T.3
  • 56
    • 0035911147 scopus 로고    scopus 로고
    • A novel 14-kilodalton protein interacts with the mitogen-activated protein kinase scaffold mp1 on a late endosomal/lysosomal compartment
    • Wunderlich W, Fialka I, Teis D, et al. A novel 14-kilodalton protein interacts with the mitogen-activated protein kinase scaffold mp1 on a late endosomal/lysosomal compartment. J Cell Biol 2001; 152: 765-776.
    • (2001) J Cell Biol , vol.152 , pp. 765-776
    • Wunderlich, W.1    Fialka, I.2    Teis, D.3
  • 57
    • 0030972494 scopus 로고    scopus 로고
    • Interaction of MAP kinase with MAP kinase kinase: Its possible role in the control of nucleocytoplasmic transport of MAP kinase
    • Fukuda M, Gotoh Y, Nishida E. Interaction of MAP kinase with MAP kinase kinase: its possible role in the control of nucleocytoplasmic transport of MAP kinase. EMBO J 1997; 16: 1901-1908
    • (1997) EMBO J , vol.16 , pp. 1901-1908
    • Fukuda, M.1    Gotoh, Y.2    Nishida, E.3
  • 58
    • 0026612951 scopus 로고
    • Ordered phosphorylation of p42mapk by MAP kinase kinase
    • Haystead TA, Dent P, Wu J, et al. Ordered phosphorylation of p42mapk by MAP kinase kinase. FEBS Lett 1992; 306: 17-22.
    • (1992) FEBS Lett , vol.306 , pp. 17-22
    • Haystead, T.A.1    Dent, P.2    Wu, J.3
  • 59
    • 0028233930 scopus 로고
    • Characterization of recombinant Xenopus MAP kinase kinases mutated at potential phosphorylation sites
    • Gotoh Y, Matsuda S, Takenaka K, et al. Characterization of recombinant Xenopus MAP kinase kinases mutated at potential phosphorylation sites. Oncogene 1994; 9: 1891-1898.
    • (1994) Oncogene , vol.9 , pp. 1891-1898
    • Gotoh, Y.1    Matsuda, S.2    Takenaka, K.3
  • 60
    • 0028329630 scopus 로고
    • Activation of MEK family kinases requires phosphorylation of two conserved Ser/Thr residues
    • Zheng CF, Guan KL. Activation of MEK family kinases requires phosphorylation of two conserved Ser/Thr residues. EMBO J 1994; 13: 1123-1131.
    • (1994) EMBO J , vol.13 , pp. 1123-1131
    • Zheng, C.F.1    Guan, K.L.2
  • 61
    • 0028219853 scopus 로고
    • Mitogen-activated protein kinase kinase 1 (MKK1) is negatively regulated by threonine phosphorylation
    • Rossomando AJ, Dent P, Sturgill TW, et al. Mitogen-activated protein kinase kinase 1 (MKK1) is negatively regulated by threonine phosphorylation. Mol Cell Biol 1994; 14: 1594-1602.
    • (1994) Mol Cell Biol , vol.14 , pp. 1594-1602
    • Rossomando, A.J.1    Dent, P.2    Sturgill, T.W.3
  • 62
    • 0029164688 scopus 로고
    • A proline-rich sequence unique to MEK1 and MEK2 is required for raf binding and regulates MEK function
    • Catling AD, Schaeffer HJ, Reuter CW, et al. A proline-rich sequence unique to MEK1 and MEK2 is required for raf binding and regulates MEK function. Mol Cell Biol 1995; 15: 5214-5225.
    • (1995) Mol Cell Biol , vol.15 , pp. 5214-5225
    • Catling, A.D.1    Schaeffer, H.J.2    Reuter, C.W.3
  • 63
    • 0028276218 scopus 로고
    • Growth factor-stimulated MAP kinase induces rapid retrophosphorylation and inhibition of MAP kinase kinase (MEK1)
    • Brunet A, Pages G, Pouyssegur J. Growth factor-stimulated MAP kinase induces rapid retrophosphorylation and inhibition of MAP kinase kinase (MEK1). FEBS Lett 1994; 346: 299-303
    • (1994) FEBS Lett , vol.346 , pp. 299-303
    • Brunet, A.1    Pages, G.2    Pouyssegur, J.3
  • 64
    • 0032562691 scopus 로고    scopus 로고
    • Interaction of the Grb10 adapter protein with the Raf1 and MEK1 kinases
    • Nantel A, Mohammad-Ali K, Sherk J, et al. Interaction of the Grb10 adapter protein with the Raf1 and MEK1 kinases. J Biol Chem 1998; 273: 10475-10484.
    • (1998) J Biol Chem , vol.273 , pp. 10475-10484
    • Nantel, A.1    Mohammad-Ali, K.2    Sherk, J.3
  • 65
    • 0032584728 scopus 로고    scopus 로고
    • The MEK1 proline-rich insert is required for efficient activation of the mitogen-activated protein kinases ERK1 and ERK2 in mammalian cells
    • Dang A, Frost JA, Cobb MH. The MEK1 proline-rich insert is required for efficient activation of the mitogen-activated protein kinases ERK1 and ERK2 in mammalian cells. J Biol Chem 1998; 273: 19909-19913.
    • (1998) J Biol Chem , vol.273 , pp. 19909-19913
    • Dang, A.1    Frost, J.A.2    Cobb, M.H.3
  • 66
    • 0033604576 scopus 로고    scopus 로고
    • Isotype-specific functions of Raf kinases
    • Hagemann C, Rapp UR. Isotype-specific functions of Raf kinases. Exp Cell Res 1999; 253: 34-46.
    • (1999) Exp Cell Res , vol.253 , pp. 34-46
    • Hagemann, C.1    Rapp, U.R.2
  • 68
    • 0027337248 scopus 로고
    • Normal and oncogenic p21ras proteins bind to the amino-terminal regulatory domain of c-Raf-1
    • Zhang XF, Settleman J, Kyriakis JM, et al. Normal and oncogenic p21ras proteins bind to the amino-terminal regulatory domain of c-Raf-1. Nature 1993; 364: 308-313
    • (1993) Nature , vol.364 , pp. 308-313
    • Zhang, X.F.1    Settleman, J.2    Kyriakis, J.M.3
  • 69
    • 0028272507 scopus 로고
    • Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane
    • Leevers SJ, Paterson HF, Marshall CJ. Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane. Nature 1994; 369: 411-414.
    • (1994) Nature , vol.369 , pp. 411-414
    • Leevers, S.J.1    Paterson, H.F.2    Marshall, C.J.3
  • 70
    • 0028241533 scopus 로고
    • Activation of Raf as a result of recruitment to the plasma membrane
    • Stokoe D, Macdonald SG, Cadwallader K, et al. Activation of Raf as a result of recruitment to the plasma membrane. Science 1994; 264: 1463-1467.
    • (1994) Science , vol.264 , pp. 1463-1467
    • Stokoe, D.1    Macdonald, S.G.2    Cadwallader, K.3
  • 71
    • 0029014973 scopus 로고
    • Reversal of Raf-1 activation by purified and membrane-associated protein phosphatases
    • published erratum appears in Science 1995 Sep 22;269[5231]:1657
    • Dent P, Jelinek T, Morrison DK, et al. Reversal of Raf-1 activation by purified and membrane-associated protein phosphatases (published erratum appears in Science 1995 Sep 22;269[5231]:1657). Science 1995; 268: 1902-1906
    • (1995) Science , vol.268 , pp. 1902-1906
    • Dent, P.1    Jelinek, T.2    Morrison, D.K.3
  • 72
    • 0030029343 scopus 로고    scopus 로고
    • Ras-induced activation of Raf-1 is dependent on tyrosine phosphorylation
    • Jelinek T, Dent P, Sturgill TW, et al. Ras-induced activation of Raf-1 is dependent on tyrosine phosphorylation. Mol Cell Biol 1996; 16: 1027-1034.
    • (1996) Mol Cell Biol , vol.16 , pp. 1027-1034
    • Jelinek, T.1    Dent, P.2    Sturgill, T.W.3
  • 73
    • 0028278201 scopus 로고
    • Raf-1 interacts with Fyn and Src in a non-phosphotyrosine-dependent manner
    • Cleghon V, Morrison DK. Raf-1 interacts with Fyn and Src in a non-phosphotyrosine-dependent manner. J Biol Chem 1994; 269: 17749-17755.
    • (1994) J Biol Chem , vol.269 , pp. 17749-17755
    • Cleghon, V.1    Morrison, D.K.2
  • 74
    • 0027364980 scopus 로고
    • Critical tyrosine residues regulate the enzymatic and biological activity of Raf-1 kinase
    • Fabian JR, Daar IO, Morrison DK. Critical tyrosine residues regulate the enzymatic and biological activity of Raf-1 kinase. Mol Cell Biol 1993; 13: 7170-7179.
    • (1993) Mol Cell Biol , vol.13 , pp. 7170-7179
    • Fabian, J.R.1    Daar, I.O.2    Morrison, D.K.3
  • 75
    • 0029006126 scopus 로고
    • Ras recruits Raf-1 to the plasma membrane for activation by tyrosine phosphorylation
    • Marais R, Light Y, Paterson HF, et al. Ras recruits Raf-1 to the plasma membrane for activation by tyrosine phosphorylation. EMBO J 1995; 14: 3136-3145.
    • (1995) EMBO J , vol.14 , pp. 3136-3145
    • Marais, R.1    Light, Y.2    Paterson, H.F.3
  • 76
    • 0027326410 scopus 로고
    • Protein kinase C alpha activates RAF-1 by direct phosphorylation
    • Kolch W, Heidecker G, Kochs G, et al. Protein kinase C alpha activates RAF-1 by direct phosphorylation. Nature 1993; 364: 249-252.
    • (1993) Nature , vol.364 , pp. 249-252
    • Kolch, W.1    Heidecker, G.2    Kochs, G.3
  • 77
    • 0343742670 scopus 로고    scopus 로고
    • Kinase suppressor of Ras is ceramide-activated protein kinase
    • Zhang Y, Yao B, Delikat S, et al. Kinase suppressor of Ras is ceramide-activated protein kinase. Cell 1997; 89: 63-72
    • (1997) Cell , vol.89 , pp. 63-72
    • Zhang, Y.1    Yao, B.2    Delikat, S.3
  • 78
    • 0035971073 scopus 로고    scopus 로고
    • Kinase suppressor of Ras signals through Thr269 of c-Raf-1
    • Xing HR, Kolesnick R. Kinase suppressor of Ras signals through Thr269 of c-Raf-1. J Biol Chem 2001; 276: 9733-9741.
    • (2001) J Biol Chem , vol.276 , pp. 9733-9741
    • Xing, H.R.1    Kolesnick, R.2
  • 79
    • 0035018017 scopus 로고    scopus 로고
    • KSR: A MAPK scaffold of the Ras pathway?
    • Morrison DK. KSR: a MAPK scaffold of the Ras pathway? J Cell Sci 2001; 114: 1609-1612.
    • (2001) J Cell Sci , vol.114 , pp. 1609-1612
    • Morrison, D.K.1
  • 80
    • 0034624783 scopus 로고    scopus 로고
    • Regulation of the protein kinase Raf-1 by oncogenic Ras through phosphatidylinositol 3-kinase, Cdc42/Rac and Pak
    • Sun H, King AJ, Diaz HB, et al. Regulation of the protein kinase Raf-1 by oncogenic Ras through phosphatidylinositol 3-kinase, Cdc42/Rac and Pak. Curr Biol 2000; 10: 281-284
    • (2000) Curr Biol , vol.10 , pp. 281-284
    • Sun, H.1    King, A.J.2    Diaz, H.B.3
  • 81
    • 0035099881 scopus 로고    scopus 로고
    • S338 phosphorylation of Raf-1 is independent of phosphatidylinositol 3-kinase and Pak3
    • Chiloeches A, Mason CS, Marais R. S338 phosphorylation of Raf-1 is independent of phosphatidylinositol 3-kinase and Pak3. Mol Cell Biol 2001; 21: 2423-2434.
    • (2001) Mol Cell Biol , vol.21 , pp. 2423-2434
    • Chiloeches, A.1    Mason, C.S.2    Marais, R.3
  • 82
    • 0027485031 scopus 로고
    • Increasing cAMP attenuates activation of mitogen-activated protein kinase
    • Sevetson BR, Kong X, Lawrence JC, Jr. Increasing cAMP attenuates activation of mitogen-activated protein kinase. Proc Natl Acad Sci USA 1993; 90: 10305-10309.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10305-10309
    • Sevetson, B.R.1    Kong, X.2    Lawrence J.C., Jr.3
  • 83
    • 0027716596 scopus 로고
    • Inhibition by cAMP of Ras-dependent activation of Raf
    • Cook SJ and McCormick F. Inhibition by cAMP of Ras-dependent activation of Raf. Science 1993; 262: 1069-1072.
    • (1993) Science , vol.262 , pp. 1069-1072
    • Cook, S.J.1    McCormick, F.2
  • 84
    • 0027772672 scopus 로고
    • Inhibition of the EGF-activated MAP kinase signaling pathway by adenosine 3′,5′-monophosphate
    • Wu J, Dent P, Jelinek T, et al. Inhibition of the EGF-activated MAP kinase signaling pathway by adenosine 3′,5′-monophosphate. Science 1993; 262: 1065-1069.
    • (1993) Science , vol.262 , pp. 1065-1069
    • Wu, J.1    Dent, P.2    Jelinek, T.3
  • 85
    • 0034666006 scopus 로고    scopus 로고
    • Phosphorylation of serine 43 is not required for inhibition of c-Raf kinase by the cAMP-dependent protein kinase
    • Sidovar MF, Kozlowski P, Lee JW, et al. Phosphorylation of serine 43 is not required for inhibition of c-Raf kinase by the cAMP-dependent protein kinase. J Biol Chem 2000; 275: 28688-28694.
    • (2000) J Biol Chem , vol.275 , pp. 28688-28694
    • Sidovar, M.F.1    Kozlowski, P.2    Lee, J.W.3
  • 86
    • 0034644733 scopus 로고    scopus 로고
    • Cell type-specific regulation of B-Raf kinase by cAMP and 14-3-3 proteins
    • Qiu W, Zhuang S, von Lintig FC, et al. Cell type-specific regulation of B-Raf kinase by cAMP and 14-3-3 proteins. J Biol Chem 2000; 275: 31921-31929.
    • (2000) J Biol Chem , vol.275 , pp. 31921-31929
    • Qiu, W.1    Zhuang, S.2    Von Lintig, F.C.3
  • 87
    • 0033607784 scopus 로고    scopus 로고
    • Differentiation stage-specific inhibition of the Raf-MEK-ERK pathway by Akt
    • Rommel C, Clarke BA, Zimmermann S, et al. Differentiation stage-specific inhibition of the Raf-MEK-ERK pathway by Akt. Science 1999; 286: 1738-1741
    • (1999) Science , vol.286 , pp. 1738-1741
    • Rommel, C.1    Clarke, B.A.2    Zimmermann, S.3
  • 88
    • 0033607633 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Raf by Akt (protein kinase B)
    • Zimmermann S, Moelling K. Phosphorylation and regulation of Raf by Akt (protein kinase B). Science 1999; 286: 1741-1744
    • (1999) Science , vol.286 , pp. 1741-1744
    • Zimmermann, S.1    Moelling, K.2
  • 89
    • 0029871708 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine
    • Muslin AJ, Tanner JW, Allen PM, et al. Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell 1996; 84: 889-897.
    • (1996) Cell , vol.84 , pp. 889-897
    • Muslin, A.J.1    Tanner, J.W.2    Allen, P.M.3
  • 90
    • 0027944852 scopus 로고
    • Activation of Raf-1 by 14-3-3 proteins
    • Fantl WJ, Muslin AJ, Kikuchi A, et al, Activation of Raf-1 by 14-3-3 proteins. Nature 1994; 371: 612-614.
    • (1994) Nature , vol.371 , pp. 612-614
    • Fantl, W.J.1    Muslin, A.J.2    Kikuchi, A.3
  • 91
    • 0029071689 scopus 로고
    • 14-3-3 is not essential for Raf-1 function: Identification of Raf-1 proteins that are biologically activated in a 14-3-3- and Ras-independent manner
    • Michaud NR, Fabian JR, Mathes KD, et al. 14-3-3 is not essential for Raf-1 function: identification of Raf-1 proteins that are biologically activated in a 14-3-3- and Ras- independent manner. Mol Cell Biol 1995; 15: 3390-3397
    • (1995) Mol Cell Biol , vol.15 , pp. 3390-3397
    • Michaud, N.R.1    Fabian, J.R.2    Mathes, K.D.3
  • 92
    • 0035811597 scopus 로고    scopus 로고
    • Protein phosphatases 1 and 2A promote Raf-1 activation by regulating 14- 3-3 interactions
    • Jaumot M, Hancock JF. Protein phosphatases 1 and 2A promote Raf-1 activation by regulating 14- 3-3 interactions. Oncogene 2001; 20: 3949-3958.
    • (2001) Oncogene , vol.20 , pp. 3949-3958
    • Jaumot, M.1    Hancock, J.F.2
  • 93
    • 0034635482 scopus 로고    scopus 로고
    • Disruption of the 14-3-3 binding site within the B-Raf kinase domain uncouples catalytic activity from PC12 cell differentiation
    • MacNicol MC, Muslin AJ, MacNicol AM. Disruption of the 14-3-3 binding site within the B-Raf kinase domain uncouples catalytic activity from PC12 cell differentiation. J Biol Chem 2000; 275: 3803-3809.
    • (2000) J Biol Chem , vol.275 , pp. 3803-3809
    • MacNicol, M.C.1    Muslin, A.J.2    MacNicol, A.M.3
  • 94
    • 0028786332 scopus 로고
    • Disruption of the Raf-1-Hsp90 molecular complex results in destabilization of Raf-1 and loss of Raf-1-Ras association
    • Schulte TW, Blagosklonny MV, Ingui C, et al. Disruption of the Raf-1-Hsp90 molecular complex results in destabilization of Raf-1 and loss of Raf-1-Ras association. J Biol Chem 1995; 270: 24585-24588.
    • (1995) J Biol Chem , vol.270 , pp. 24585-24588
    • Schulte, T.W.1    Blagosklonny, M.V.2    Ingui, C.3
  • 95
    • 0031590456 scopus 로고    scopus 로고
    • Geldanamycin-induced destabilization of Raf-1 involves the proteasome
    • Schulte TW, An WG, Neckers LM. Geldanamycin-induced destabilization of Raf-1 involves the proteasome. Biochem Biophys Res Commun 1997; 239: 655-659
    • (1997) Biochem Biophys Res Commun , vol.239 , pp. 655-659
    • Schulte, T.W.1    An, W.G.2    Neckers, L.M.3
  • 96
    • 0028877441 scopus 로고
    • Conditionally oncogenic forms of the A-Raf and B-Raf protein kinases display different biological and biochemical properties in NIH 3T3 cells
    • Pritchard CA, Samuels ML, Bosch E, et al. Conditionally oncogenic forms of the A-Raf and B-Raf protein kinases display different biological and biochemical properties in NIH 3T3 cells. Mol Cell Biol 1995; 15: 6430-6442.
    • (1995) Mol Cell Biol , vol.15 , pp. 6430-6442
    • Pritchard, C.A.1    Samuels, M.L.2    Bosch, E.3
  • 97
    • 0031761118 scopus 로고    scopus 로고
    • Differential abilities of activated Raf oncoproteins to abrogate cytokine dependency, prevent apoptosis and induce autocrine growth factor synthesis in human hematopoietic cells
    • McCubrey JA, Steelman LS, Hoyle PE, et al. Differential abilities of activated Raf oncoproteins to abrogate cytokine dependency, prevent apoptosis and induce autocrine growth factor synthesis in human hematopoietic cells. Leukemia 1998; 12: 1903-1929.
    • (1998) Leukemia , vol.12 , pp. 1903-1929
    • McCubrey, J.A.1    Steelman, L.S.2    Hoyle, P.E.3
  • 98
    • 0034659736 scopus 로고    scopus 로고
    • Ras mediates the cAMP-dependent activation of extracellular signal- regulated kinases (ERKs) in melanocytes
    • Busca R, Abbe P, Mantoux F, et al. Ras mediates the cAMP-dependent activation of extracellular signal- regulated kinases (ERKs) in melanocytes. EMBO J 2000; 19: 2900-2910.
    • (2000) EMBO J , vol.19 , pp. 2900-2910
    • Busca, R.1    Abbe, P.2    Mantoux, F.3
  • 99
    • 0026446907 scopus 로고
    • The mos proto-oncogene product: Its role in oocyte maturation, metaphase arrest, and neoplastic transformation
    • Singh B and Arlinghaus RB. The mos proto-oncogene product: its role in oocyte maturation, metaphase arrest, and neoplastic transformation. Mol Carcinog 1992; 6: 182-189.
    • (1992) Mol Carcinog , vol.6 , pp. 182-189
    • Singh, B.1    Arlinghaus, R.B.2
  • 100
    • 0027462979 scopus 로고
    • Mos stimulates MAP kinase in Xenopus oocytes and activates a MAP kinase kinase in vitro
    • Posada J, Yew N, Ahn NG, et al. Mos stimulates MAP kinase in Xenopus oocytes and activates a MAP kinase kinase in vitro. Mol Cell Biol 1993; 13: 2546-2553.
    • (1993) Mol Cell Biol , vol.13 , pp. 2546-2553
    • Posada, J.1    Yew, N.2    Ahn, N.G.3
  • 101
    • 0034599722 scopus 로고    scopus 로고
    • Hsp90 is required for c-Mos activation and biphasic MAP kinase activation in Xenopus oocytes
    • Fisher DL, Mandart E, Doree M. Hsp90 is required for c-Mos activation and biphasic MAP kinase activation in Xenopus oocytes. EMBO J 2000; 19: 1516-1524.
    • (2000) EMBO J , vol.19 , pp. 1516-1524
    • Fisher, D.L.1    Mandart, E.2    Doree, M.3
  • 102
    • 0028316977 scopus 로고
    • Requirement for the MAP kinase kinase/MAP kinase cascade in Xenopus oocyte maturation
    • Kosako H, Gotoh Y, Nishida E. Requirement for the MAP kinase kinase/MAP kinase cascade in Xenopus oocyte maturation. EMBO J 1994; 13: 2131-2138.
    • (1994) EMBO J , vol.13 , pp. 2131-2138
    • Kosako, H.1    Gotoh, Y.2    Nishida, E.3
  • 103
    • 0027984535 scopus 로고
    • Mitogen-activated protein kinase kinase is required for the mos-induced metaphase arrest
    • Kosako H, Gotoh Y, Nishida E. Mitogen-activated protein kinase kinase is required for the mos-induced metaphase arrest. J Biol Chem 1994; 269: 28354-28358.
    • (1994) J Biol Chem , vol.269 , pp. 28354-28358
    • Kosako, H.1    Gotoh, Y.2    Nishida, E.3
  • 104
    • 0024280269 scopus 로고
    • Function of c-mos proto-oncogene product in meiotic maturation in Xenopus oocytes
    • Sagata N, Oskarsson M, Copeland T, et al. Function of c-mos proto-oncogene product in meiotic maturation in Xenopus oocytes. Nature 1988; 335: 519-525.
    • (1988) Nature , vol.335 , pp. 519-525
    • Sagata, N.1    Oskarsson, M.2    Copeland, T.3
  • 105
    • 0028820784 scopus 로고
    • Initiation of Xenopus oocyte maturation by activation of the mitogen-activated protein kinase cascade
    • Gotoh Y, Masuyama N, Dell K, et al. Initiation of Xenopus oocyte maturation by activation of the mitogen-activated protein kinase cascade. J Biol Chem 1995; 270: 25898-25904.
    • (1995) J Biol Chem , vol.270 , pp. 25898-25904
    • Gotoh, Y.1    Masuyama, N.2    Dell, K.3
  • 106
    • 0033214147 scopus 로고    scopus 로고
    • Xenopus oocyte maturation: New lessons from a good egg
    • Ferrell JE, Jr. Xenopus oocyte maturation: new lessons from a good egg. Bioessays 1999; 21: 833-842.
    • (1999) Bioessays , vol.21 , pp. 833-842
    • Ferrell J.E., Jr.1
  • 107
    • 0028134981 scopus 로고
    • A MAP kinase-dependent spindle assembly checkpoint in Xenopus egg extracts
    • Minshull J, Sun H, Tonks NK, et al. A MAP kinase-dependent spindle assembly checkpoint in Xenopus egg extracts. Cell 1994; 79: 475-486.
    • (1994) Cell , vol.79 , pp. 475-486
    • Minshull, J.1    Sun, H.2    Tonks, N.K.3
  • 108
    • 0027283659 scopus 로고
    • Growth factors induce nuclear translocation of MAP kinases (p42mapk and p44mapk) but not of their activator MAP kinase kinase (p45mapkk) in fibroblasts
    • Lenormand P, Sardet C, Pages G, et al. Growth factors induce nuclear translocation of MAP kinases (p42mapk and p44mapk) but not of their activator MAP kinase kinase (p45mapkk) in fibroblasts. J. Cell Biol. 1993; 122: 1079-1088.
    • (1993) J Cell Biol , vol.122 , pp. 1079-1088
    • Lenormand, P.1    Sardet, C.2    Pages, G.3
  • 109
    • 0028125887 scopus 로고
    • Control of MAP kinase activation by the mitogen-induced threonine/tyrosine phosphatase PAC1
    • Ward Y, Gupta S, Jensen P, et al. Control of MAP kinase activation by the mitogen-induced threonine/tyrosine phosphatase PAC1. Nature 1994; 367: 651-654.
    • (1994) Nature , vol.367 , pp. 651-654
    • Ward, Y.1    Gupta, S.2    Jensen, P.3
  • 110
    • 0027283659 scopus 로고
    • Growth factors induce nuclear translocation of MAP kinases (p42mapk and p44mapk) but not of their activator MAP kinase kinase (p45mapkk) in fibroblasts
    • Lenormand P, Sardet C, Pages G, et al. Growth factors induce nuclear translocation of MAP kinases (p42mapk and p44mapk) but not of their activator MAP kinase kinase (p45mapkk) in fibroblasts. J Cell Biol 1993; 122: 1079-1088.
    • (1993) J Cell Biol , vol.122 , pp. 1079-1088
    • Lenormand, P.1    Sardet, C.2    Pages, G.3
  • 111
    • 0032524356 scopus 로고    scopus 로고
    • Phosphorylation of the MAP kinase ERK2 promotes its homodimerization and nuclear translocation
    • Khokhlatchev AV, Canagarajah B, Wilsbacher J, et al. Phosphorylation of the MAP kinase ERK2 promotes its homodimerization and nuclear translocation. Cell 1998; 93: 605-615.
    • (1998) Cell , vol.93 , pp. 605-615
    • Khokhlatchev, A.V.1    Canagarajah, B.2    Wilsbacher, J.3
  • 112
    • 0032749494 scopus 로고    scopus 로고
    • Identification of a cytoplasmic-retention sequence in ERK2
    • Rubinfeld H, Hanoch T, Seger R. Identification of a cytoplasmic-retention sequence in ERK2. J Biol Chem 1999; 274: 30349-30352.
    • (1999) J Biol Chem , vol.274 , pp. 30349-30352
    • Rubinfeld, H.1    Hanoch, T.2    Seger, R.3
  • 113
    • 0032534791 scopus 로고    scopus 로고
    • PTP-SL and STEP protein tyrosine phosphatases regulate the activation of the extracellular signal-regulated kinases ERK1 and ERK2 by association through a kinase interaction motif
    • Pulido R, Zuniga A, Ullrich A. PTP-SL and STEP protein tyrosine phosphatases regulate the activation of the extracellular signal-regulated kinases ERK1 and ERK2 by association through a kinase interaction motif. EMBO J 1998; 17: 7337-7350.
    • (1998) EMBO J , vol.17 , pp. 7337-7350
    • Pulido, R.1    Zuniga, A.2    Ullrich, A.3
  • 114
    • 0038845769 scopus 로고    scopus 로고
    • Interaction of mitogen-activated protein kinases with the kinase interaction motif of the tyrosine phosphatase PTP-SL provides substrate specificity and retains ERK2 in the cytoplasm
    • Zuniga A, Torres J, Ubeda J, et al. Interaction of mitogen-activated protein kinases with the kinase interaction motif of the tyrosine phosphatase PTP-SL provides substrate specificity and retains ERK2 in the cytoplasm. J Biol Chem 1999; 274: 21900-21907.
    • (1999) J Biol Chem , vol.274 , pp. 21900-21907
    • Zuniga, A.1    Torres, J.2    Ubeda, J.3
  • 115
    • 0033552609 scopus 로고    scopus 로고
    • A novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphatase
    • Blanco-Aparicio C, Torres J, Pulido R. A novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphatase. J Cell Biol 1999; 147: 1129-1136.
    • (1999) J Cell Biol , vol.147 , pp. 1129-1136
    • Blanco-Aparicio, C.1    Torres, J.2    Pulido, R.3
  • 116
    • 0030935258 scopus 로고    scopus 로고
    • Nuclear translocation of mitogen-activated protein kinase kinase (MEK1) in response to mitogenic stimulation
    • Jaaro H, Rubinfeld H, Hanoch T, et al. Nuclear translocation of mitogen-activated protein kinase kinase (MEK1) in response to mitogenic stimulation. Proc Natl Acad Sci USA 1997; 94: 3742-3747
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3742-3747
    • Jaaro, H.1    Rubinfeld, H.2    Hanoch, T.3
  • 117
    • 0033525528 scopus 로고    scopus 로고
    • Nuclear localization of mitogen-activated protein kinase kinase 1 (MKK1) is promoted by serum stimulation and G2-M progression. Requirement for phosphorylation at the activation lip and signaling downstream of MKK
    • Tolwinski NS, Shapiro PS, Goueli S, et al. Nuclear localization of mitogen-activated protein kinase kinase 1 (MKK1) is promoted by serum stimulation and G2-M progression. Requirement for phosphorylation at the activation lip and signaling downstream of MKK. J Biol Chem 1999; 274: 6168-6174.
    • (1999) J Biol Chem , vol.274 , pp. 6168-6174
    • Tolwinski, N.S.1    Shapiro, P.S.2    Goueli, S.3
  • 118
    • 0025823448 scopus 로고
    • ERKs: A family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF
    • Boulton TG, Nye SH, Robbins DJ, et al. ERKs: a family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF. Cell 1991; 65: 663-675.
    • (1991) Cell , vol.65 , pp. 663-675
    • Boulton, T.G.1    Nye, S.H.2    Robbins, D.J.3
  • 119
    • 0029988873 scopus 로고    scopus 로고
    • ERK3 is a constitutively nuclear protein kinase
    • Cheng M, Boulton TG, Cobb MH. ERK3 is a constitutively nuclear protein kinase. J Biol Chem 1996; 271: 8951-8958.
    • (1996) J Biol Chem , vol.271 , pp. 8951-8958
    • Cheng, M.1    Boulton, T.G.2    Cobb, M.H.3
  • 120
    • 0034652303 scopus 로고    scopus 로고
    • Cloning and characterization of mouse extracellular-signal-regulated protein kinase 3 as a unique gene product of 100 kDa
    • Turgeon B, Saba-El-Leil MK, Meloche S. Cloning and characterization of mouse extracellular-signal-regulated protein kinase 3 as a unique gene product of 100 kDa. Biochem J 2000; 346 Pt 1 169-175.
    • (2000) Biochem J , vol.346 , Issue.PART 1 , pp. 169-175
    • Turgeon, B.1    Saba-El-Leil, M.K.2    Meloche, S.3
  • 121
    • 0030046667 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of extracellular signal-regulated protein kinase 4 in response to growth factors
    • Peng X, Angelastro JM, Greene LA, Tyrosine phosphorylation of extracellular signal-regulated protein kinase 4 in response to growth factors. J Neurochem 1996; 66: 1191-1197.
    • (1996) J Neurochem , vol.66 , pp. 1191-1197
    • Peng, X.1    Angelastro, J.M.2    Greene, L.A.3
  • 122
    • 0029055761 scopus 로고
    • Components of a new human protein kinase signal transduction pathway
    • Zhou G, Bao ZQ, Dixon JE. Components of a new human protein kinase signal transduction pathway. J Biol Chem 1995; 270: 12665-12669.
    • (1995) J Biol Chem , vol.270 , pp. 12665-12669
    • Zhou, G.1    Bao, Z.Q.2    Dixon, J.E.3
  • 123
    • 0029911710 scopus 로고    scopus 로고
    • ERK6, a mitogen-activated protein kinase involved in C2C12 myoblast differentiation
    • Lechner C, Zahalka MA, Giot JF, et al. ERK6, a mitogen-activated protein kinase involved in C2C12 myoblast differentiation. Proc Natl Acad Sci USA 1996; 93: 4355-4359.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4355-4359
    • Lechner, C.1    Zahalka, M.A.2    Giot, J.F.3
  • 124
    • 0033625759 scopus 로고    scopus 로고
    • Involvement of the MKK6-p38gamma cascade in gamma-radiation-induced cell cycle arrest
    • Wang X, McGowan CH, Zhao M, et al. Involvement of the MKK6-p38gamma cascade in gamma-radiation-induced cell cycle arrest. Mol Cell Biol 2000; 20: 4543-4552.
    • (2000) Mol Cell Biol , vol.20 , pp. 4543-4552
    • Wang, X.1    McGowan, C.H.2    Zhao, M.3
  • 125
    • 0032958382 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase 7 (ERK7), a novel ERK with a C-terminal domain that regulates its activity, its cellular localization, cell growth
    • Abe MK, Kuo WL, Hershenson MB, et al. Extracellular signal-regulated kinase 7 (ERK7), a novel ERK with a C-terminal domain that regulates its activity, its cellular localization, cell growth. Mol Cell Biol 1999; 19: 1301-1312.
    • (1999) Mol Cell Biol , vol.19 , pp. 1301-1312
    • Abe, M.K.1    Kuo, W.L.2    Hershenson, M.B.3
  • 126
    • 0035815688 scopus 로고    scopus 로고
    • Proteasome- and p38-dependent regulation of ERK3 expression
    • Zimmermann J, Lamerant N, Grossenbacher R, et al. Proteasome- and p38-dependent regulation of ERK3 expression. J Biol Chem 2001; 276: 10759-10766.
    • (2001) J Biol Chem , vol.276 , pp. 10759-10766
    • Zimmermann, J.1    Lamerant, N.2    Grossenbacher, R.3
  • 127
    • 0033615653 scopus 로고    scopus 로고
    • Contribution of the ERK5/MEK5 pathway to Ras/Raf signaling and growth control
    • English JM, Pearson G, Hockenberry T, et al. Contribution of the ERK5/MEK5 pathway to Ras/Raf signaling and growth control. J Biol Chem 1999; 274: 31588-31592.
    • (1999) J Biol Chem , vol.274 , pp. 31588-31592
    • English, J.M.1    Pearson, G.2    Hockenberry, T.3
  • 128
    • 0032531881 scopus 로고    scopus 로고
    • Bmk1/Erk5 is required for cell proliferation induced by epidermal growth factor
    • Kato Y, Tapping RI, Huang S, et al. Bmk1/Erk5 is required for cell proliferation induced by epidermal growth factor. Nature 1998; 395: 713-716.
    • (1998) Nature , vol.395 , pp. 713-716
    • Kato, Y.1    Tapping, R.I.2    Huang, S.3
  • 129
    • 0032512770 scopus 로고    scopus 로고
    • Identification of substrates and regulators of the mitogen-activated protein kinase ERK5 using chimeric protein kinases
    • English JM, Pearson G, Baer R, et al. Identification of substrates and regulators of the mitogen-activated protein kinase ERK5 using chimeric protein kinases. J Biol Chem 1998; 273: 3854-3860.
    • (1998) J Biol Chem , vol.273 , pp. 3854-3860
    • English, J.M.1    Pearson, G.2    Baer, R.3
  • 130
    • 0035896513 scopus 로고    scopus 로고
    • ERK5 and ERK2 cooperate to regulate NF-kappaB and cell transformation
    • Pearson G, English JM, White MA, et al. ERK5 and ERK2 cooperate to regulate NF-kappaB and cell transformation. J Biol Chem 2001; 276: 7927-7931.
    • (2001) J Biol Chem , vol.276 , pp. 7927-7931
    • Pearson, G.1    English, J.M.2    White, M.A.3
  • 131
    • 0035281564 scopus 로고    scopus 로고
    • Regulation of gene expression by the small GTPase Rho through the ERK6 (p38 gamma) MAP kinase pathway
    • Marinissen MJ, Chiariello M, Gutkind JS. Regulation of gene expression by the small GTPase Rho through the ERK6 (p38 gamma) MAP kinase pathway. Genes Dev 2001; 15: 535-553.
    • (2001) Genes Dev , vol.15 , pp. 535-553
    • Marinissen, M.J.1    Chiariello, M.2    Gutkind, J.S.3
  • 132
    • 0035877631 scopus 로고    scopus 로고
    • ERK7 is an autoactivated member of the MAPK family
    • Abe MK, Kahle KT, Saelzler MP, et al. ERK7 is an autoactivated member of the MAPK family. J Biol Chem 2001; 276: 21272-21279.
    • (2001) J Biol Chem , vol.276 , pp. 21272-21279
    • Abe, M.K.1    Kahle, K.T.2    Saelzler, M.P.3
  • 133
    • 0034717036 scopus 로고    scopus 로고
    • ERK1b, a 46-kDa ERK isoform that is differentially regulated by MEK
    • Yung Y, Yao Z, Hanoch T, et al. ERK1b, a 46-kDa ERK isoform that is differentially regulated by MEK. J Biol Chem 2000; 275: 15799-15808.
    • (2000) J Biol Chem , vol.275 , pp. 15799-15808
    • Yung, Y.1    Yao, Z.2    Hanoch, T.3
  • 134
    • 0033567291 scopus 로고    scopus 로고
    • The stress-activated protein kinase pathways
    • Tibbles LA, Woodgett JR. The stress-activated protein kinase pathways. Cell Mol Life Sci 1999; 55: 1230-1254.
    • (1999) Cell Mol Life Sci , vol.55 , pp. 1230-1254
    • Tibbles, L.A.1    Woodgett, J.R.2
  • 135
    • 0028609209 scopus 로고
    • JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation
    • Kallunki T, Su B, Tsigelny I, et al. JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation. Genes Dev 1994; 8: 2996-3007.
    • (1994) Genes Dev , vol.8 , pp. 2996-3007
    • Kallunki, T.1    Su, B.2    Tsigelny, I.3
  • 136
    • 0029885419 scopus 로고    scopus 로고
    • Selective interaction of JNK protein kinase isoforms with transcription factors
    • Gupta S, Barrett T, Whitmarsh AJ, et al. Selective interaction of JNK protein kinase isoforms with transcription factors. EMBO J 1996; 15: 2760-2770.
    • (1996) EMBO J , vol.15 , pp. 2760-2770
    • Gupta, S.1    Barrett, T.2    Whitmarsh, A.J.3
  • 137
    • 0030765077 scopus 로고    scopus 로고
    • Stress-activated protein kinases: Activation, regulation and function
    • Paul A, Wilson S, Belham CM, et al. Stress-activated protein kinases: activation, regulation and function. Cell Signal 1997; 9: 403-410.
    • (1997) Cell Signal , vol.9 , pp. 403-410
    • Paul, A.1    Wilson, S.2    Belham, C.M.3
  • 138
    • 0031916832 scopus 로고    scopus 로고
    • Selective activation of p38 mitogen-activated protein (MAP) kinase isoforms by the MAP kinase kinases MKK3 and MKK6
    • Enslen H, Raingeaud J, Davis RJ. Selective activation of p38 mitogen-activated protein (MAP) kinase isoforms by the MAP kinase kinases MKK3 and MKK6. J Biol Chem 1998; 273: 1741-1748.
    • (1998) J Biol Chem , vol.273 , pp. 1741-1748
    • Enslen, H.1    Raingeaud, J.2    Davis, R.J.3
  • 140
    • 0027215820 scopus 로고
    • A divergence in the MAP kinase regulatory network defined by MEK kinase and Raf
    • Lange-Carter CA, Pleiman CM, Gardner AM, et al. A divergence in the MAP kinase regulatory network defined by MEK kinase and Raf. Science 1993; 260: 315-319.
    • (1993) Science , vol.260 , pp. 315-319
    • Lange-Carter, C.A.1    Pleiman, C.M.2    Gardner, A.M.3
  • 141
    • 0028568217 scopus 로고
    • Differential activation of ERK and JNK mitogen-activated protein kinases by Raf-1 and MEKK
    • Minden A, Lin A, McMahon M, et al. Differential activation of ERK and JNK mitogen-activated protein kinases by Raf-1 and MEKK. Science 1994; 266: 1719-1723.
    • (1994) Science , vol.266 , pp. 1719-1723
    • Minden, A.1    Lin, A.2    McMahon, M.3
  • 142
    • 0032483967 scopus 로고    scopus 로고
    • Role of MEKK1 in cell survival and activation of JNK and ERK pathways defined by targeted gene disruption
    • Yujiri T, Sather S, Fanger GR, et al. Role of MEKK1 in cell survival and activation of JNK and ERK pathways defined by targeted gene disruption. Science 1998; 282: 1911-1914.
    • (1998) Science , vol.282 , pp. 1911-1914
    • Yujiri, T.1    Sather, S.2    Fanger, G.R.3
  • 143
    • 0034704153 scopus 로고    scopus 로고
    • MEKK1 binds raf-1 and the ERK2 cascade components
    • Karandikar M, Xu S, Cobb MH. MEKK1 binds raf-1 and the ERK2 cascade components. J Biol Chem 2000; 275: 40120-40127.
    • (2000) J Biol Chem , vol.275 , pp. 40120-40127
    • Karandikar, M.1    Xu, S.2    Cobb, M.H.3
  • 144
    • 0033553558 scopus 로고    scopus 로고
    • Platelet-derived growth factor activates p38 mitogen-activated protein kinase through a Ras-dependent pathway that is important for actin reorganization and cell migration
    • Matsumoto T, Yokote K, Tamura K, et al. Platelet-derived growth factor activates p38 mitogen-activated protein kinase through a Ras-dependent pathway that is important for actin reorganization and cell migration. J Biol Chem 1999; 274: 13954-13960.
    • (1999) J Biol Chem , vol.274 , pp. 13954-13960
    • Matsumoto, T.1    Yokote, K.2    Tamura, K.3
  • 145
    • 0029077563 scopus 로고
    • Direct interaction between Ras and the kinase domain of mitogen-activated protein kinase kinase kinase (MEKK1)
    • Russell M, Lange-Carter CA, Johnson GL. Direct interaction between Ras and the kinase domain of mitogen-activated protein kinase kinase kinase (MEKK1). J Biol Chem 1995; 270: 11757-11760.
    • (1995) J Biol Chem , vol.270 , pp. 11757-11760
    • Russell, M.1    Lange-Carter, C.A.2    Johnson, G.L.3
  • 146
    • 0031954631 scopus 로고    scopus 로고
    • MEK kinase 1, a substrate for DEVD-directed caspases, is involved in genotoxin-induced apoptosis
    • Widmann C, Gerwins P, Johnson NL, et al. MEK kinase 1, a substrate for DEVD-directed caspases, is involved in genotoxin-induced apoptosis. Mol Cell Biol 1998; 18: 2416-2429.
    • (1998) Mol Cell Biol , vol.18 , pp. 2416-2429
    • Widmann, C.1    Gerwins, P.2    Johnson, N.L.3
  • 147
    • 0033574434 scopus 로고    scopus 로고
    • Differential involvement of MEK kinase 1 (MEKK1) in the induction of apoptosis in response to microtubule-targeted drugs versus DNA damaging agents
    • Gibson S, Widmann C, Johnson GL. Differential involvement of MEK kinase 1 (MEKK1) in the induction of apoptosis in response to microtubule-targeted drugs versus DNA damaging agents. J Biol Chem 1999; 274: 10916-10922.
    • (1999) J Biol Chem , vol.274 , pp. 10916-10922
    • Gibson, S.1    Widmann, C.2    Johnson, G.L.3
  • 148
    • 0033605366 scopus 로고    scopus 로고
    • Activation of stress-activated protein kinase/c-Jun NH2-terminal kinase and p38 kinase in calphostin C-induced apoptosis requires caspase-3- like proteases but is dispensable for cell death
    • Ozaki I, Tani E, Ikemoto H, et al. Activation of stress-activated protein kinase/c-Jun NH2-terminal kinase and p38 kinase in calphostin C-induced apoptosis requires caspase-3- like proteases but is dispensable for cell death. J Biol Chem 1999; 274: 5310-5317.
    • (1999) J Biol Chem , vol.274 , pp. 5310-5317
    • Ozaki, I.1    Tani, E.2    Ikemoto, H.3
  • 149
    • 0032776120 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathway is dispensable for microtubule-active drug-induced Raf-1/Bcl-2 phosphorylation and apoptosis in leukemia cells
    • Blagosklonny MV, Chuman Y, Bergan RC, et al. Mitogen-activated protein kinase pathway is dispensable for microtubule-active drug-induced Raf-1/Bcl-2 phosphorylation and apoptosis in leukemia cells. Leukemia 1999; 13: 1028-1036.
    • (1999) Leukemia , vol.13 , pp. 1028-1036
    • Blagosklonny, M.V.1    Chuman, Y.2    Bergan, R.C.3
  • 150
    • 0028143060 scopus 로고
    • Identification, molecular cloning, and characterization of dual leucine zipper bearing kinase. A novel serine/threonine protein kinase that defines a second subfamily of mixed lineage kinases
    • Holzman LB, Merritt SE, Fan G. Identification, molecular cloning, and characterization of dual leucine zipper bearing kinase. A novel serine/threonine protein kinase that defines a second subfamily of mixed lineage kinases. J Biol Chem 1994; 269: 30808-30817.
    • (1994) J Biol Chem , vol.269 , pp. 30808-30817
    • Holzman, L.B.1    Merritt, S.E.2    Fan, G.3
  • 151
    • 23444453486 scopus 로고
    • MLK-3: Identification of a widely-expressed protein kinase bearing an SH3 domain and a leucine zipper-basic region domain
    • Ing YL, Leung IW, Heng HH, et al. MLK-3: identification of a widely-expressed protein kinase bearing an SH3 domain and a leucine zipper-basic region domain. Oncogene 1994; 9: 1745-1750.
    • (1994) Oncogene , vol.9 , pp. 1745-1750
    • Ing, Y.L.1    Leung, I.W.2    Heng, H.H.3
  • 152
    • 0030918591 scopus 로고    scopus 로고
    • MST/MLK2, a member of the mixed lineage kinase family, directly phosphorylates and activates SEK1, an activator of c-Jun N-terminal kinase/stress-activated protein kinase
    • Hirai S, Katoh M, Terada M, et al. MST/MLK2, a member of the mixed lineage kinase family, directly phosphorylates and activates SEK1, an activator of c-Jun N-terminal kinase/stress-activated protein kinase. J Biol Chem 1997; 272: 15167-15173.
    • (1997) J Biol Chem , vol.272 , pp. 15167-15173
    • Hirai, S.1    Katoh, M.2    Terada, M.3
  • 153
    • 0030462564 scopus 로고    scopus 로고
    • MLK-3 activates the SAPK/JNK and p38/RK pathways via SEK1 and MKK3/6
    • Tibbles LA, Ing YL, Kiefer F, et al. MLK-3 activates the SAPK/JNK and p38/RK pathways via SEK1 and MKK3/6. Embo J 1996; 15: 7026-7035.
    • (1996) Embo J , vol.15 , pp. 7026-7035
    • Tibbles, L.A.1    Ing, Y.L.2    Kiefer, F.3
  • 154
    • 0033538003 scopus 로고    scopus 로고
    • The mixed lineage kinase DLK utilizes MKK7 and not MKK4 as substrate
    • Merritt SE, Mata M, Nihalani D, et al. The mixed lineage kinase DLK utilizes MKK7 and not MKK4 as substrate. J Biol Chem 1999; 274: 10195-10202.
    • (1999) J Biol Chem , vol.274 , pp. 10195-10202
    • Merritt, S.E.1    Mata, M.2    Nihalani, D.3
  • 155
    • 0033135621 scopus 로고    scopus 로고
    • The JNK/SAPK activator mixed lineage kinase 3 (MLK3) transforms NIH 3T3 cells in a MEK-dependent fashion
    • Hartkamp J, Troppmair J, Rapp UR. The JNK/SAPK activator mixed lineage kinase 3 (MLK3) transforms NIH 3T3 cells in a MEK-dependent fashion. Cancer Res 1999; 59: 2195-2202.
    • (1999) Cancer Res , vol.59 , pp. 2195-2202
    • Hartkamp, J.1    Troppmair, J.2    Rapp, U.R.3
  • 156
    • 0029101360 scopus 로고
    • An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1
    • Olson MF, Ashworth A, Hall A. An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1. Science 1995; 269: 1270-1272.
    • (1995) Science , vol.269 , pp. 1270-1272
    • Olson, M.F.1    Ashworth, A.2    Hall, A.3
  • 157
    • 0028875683 scopus 로고
    • Cdc42 and PAK-mediated signaling leads to Jun kinase and p38 mitogen-activated protein kinase activation
    • Bagrodia S, Derijard B, Davis RJ, et al. Cdc42 and PAK-mediated signaling leads to Jun kinase and p38 mitogen-activated protein kinase activation. J Biol Chem 1995; 270: 27995-27998.
    • (1995) J Biol Chem , vol.270 , pp. 27995-27998
    • Bagrodia, S.1    Derijard, B.2    Davis, R.J.3
  • 158
    • 0030134625 scopus 로고    scopus 로고
    • Human Ste20 homologue hPAK1 links GTPases to the JNK MAP kinase pathway
    • Brown JL, Stowers L, Baer M, et al. Human Ste20 homologue hPAK1 links GTPases to the JNK MAP kinase pathway. Curr Biol 1996; 6: 598-605.
    • (1996) Curr Biol , vol.6 , pp. 598-605
    • Brown, J.L.1    Stowers, L.2    Baer, M.3
  • 159
    • 0030830220 scopus 로고    scopus 로고
    • Cross-cascade activation of ERKs and ternary complex factors by Rho family proteins
    • Frost JA, Steen H, Shapiro P, et al. Cross-cascade activation of ERKs and ternary complex factors by Rho family proteins. EMBO J 1997; 16: 6426-6438.
    • (1997) EMBO J , vol.16 , pp. 6426-6438
    • Frost, J.A.1    Steen, H.2    Shapiro, P.3
  • 160
    • 0028884033 scopus 로고
    • PD 098059 is a specific inhibitor of the activation of mitogen- activated protein kinase kinase in vitro and in vivo
    • Alessi DR, Cuenda A, Cohen P, et al. PD 098059 is a specific inhibitor of the activation of mitogen- activated protein kinase kinase in vitro and in vivo. J Biol Chem 1995; 270: 27489-27494.
    • (1995) J Biol Chem , vol.270 , pp. 27489-27494
    • Alessi, D.R.1    Cuenda, A.2    Cohen, P.3
  • 161
    • 14444279192 scopus 로고    scopus 로고
    • Identification of a novel inhibitor of mitogen-activated protein kinase kinase
    • Favata MF, Horiuchi KY, Manos EJ, et al. Identification of a novel inhibitor of mitogen-activated protein kinase kinase. J Biol Chem 1998; 273: 18623-18632.
    • (1998) J Biol Chem , vol.273 , pp. 18623-18632
    • Favata, M.F.1    Horiuchi, K.Y.2    Manos, E.J.3
  • 162
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies SP, Reddy H, Caivano M, et al. Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem J 2000; 351: 95-105.
    • (2000) Biochem J , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3
  • 164
    • 0032581040 scopus 로고    scopus 로고
    • Ro 09-2210 exhibits potent anti-proliferative effects on activated T cells by selectively blocking MKK activity
    • Williams DH, Wilkinson SE, Purton T, et al. Ro 09-2210 exhibits potent anti-proliferative effects on activated T cells by selectively blocking MKK activity. Biochemistry 1998; 37: 9579-9585.
    • (1998) Biochemistry , vol.37 , pp. 9579-9585
    • Williams, D.H.1    Wilkinson, S.E.2    Purton, T.3
  • 165
    • 0035879004 scopus 로고    scopus 로고
    • Extremely low-dose ionizing radiation causes activation of mitogen-activated protein kinase pathway and enhances proliferation of normal human diploid cells
    • Suzuki K, Kodama S, Watanabe M. Extremely low-dose ionizing radiation causes activation of mitogen-activated protein kinase pathway and enhances proliferation of normal human diploid cells. Cancer Res 2001; 61: 5396-5401.
    • (2001) Cancer Res , vol.61 , pp. 5396-5401
    • Suzuki, K.1    Kodama, S.2    Watanabe, M.3
  • 166
    • 0035034537 scopus 로고    scopus 로고
    • Modulating sensitivity to drug-induced apoptosis: The future for chemotherapy?
    • Makin G, Dive C. Modulating sensitivity to drug-induced apoptosis: the future for chemotherapy? Breast Cancer Res 2001; 3: 150-153.
    • (2001) Breast Cancer Res , vol.3 , pp. 150-153
    • Makin, G.1    Dive, C.2
  • 167
    • 0033615657 scopus 로고    scopus 로고
    • Inhibition of extracellular signal-regulated protein kinase or c-Jun N-terminal protein kinase cascade, differentially activated by cisplatin, sensitizes human ovarian cancer cell line
    • Hayakawa J, Ohmichi M, Kurachi H, et al. Inhibition of extracellular signal-regulated protein kinase or c-Jun N-terminal protein kinase cascade, differentially activated by cisplatin, sensitizes human ovarian cancer cell line. J Biol Chem 1999; 274: 31648-31654.
    • (1999) J Biol Chem , vol.274 , pp. 31648-31654
    • Hayakawa, J.1    Ohmichi, M.2    Kurachi, H.3
  • 168
    • 0034671751 scopus 로고    scopus 로고
    • Requirement for ERK activation in cisplatin-induced apoptosis
    • Wang X, Martindale JL, Holbrook NJ. Requirement for ERK activation in cisplatin-induced apoptosis. J Biol Chem 2000; 275: 39435-39443.
    • (2000) J Biol Chem , vol.275 , pp. 39435-39443
    • Wang, X.1    Martindale, J.L.2    Holbrook, N.J.3
  • 169
    • 0029737462 scopus 로고    scopus 로고
    • Activation of Raf by ionizing radiation
    • Kasid U, Suy S, Dent P, et al. Activation of Raf by ionizing radiation. Nature 1996; 382: 813-816.
    • (1996) Nature , vol.382 , pp. 813-816
    • Kasid, U.1    Suy, S.2    Dent, P.3
  • 170
    • 0032815618 scopus 로고    scopus 로고
    • Radiation-induced release of transforming growth factor alpha activates the epidermal growth factor receptor and mitogen-activated protein kinase pathway in carcinoma cells, leading to increased proliferation and protection from radiation-induced cell death
    • Dent P, Reardon DB, Park JS, et al. Radiation-induced release of transforming growth factor alpha activates the epidermal growth factor receptor and mitogen-activated protein kinase pathway in carcinoma cells, leading to increased proliferation and protection from radiation-induced cell death. Mol Biol Cell 1999; 10: 2493-2506.
    • (1999) Mol Biol Cell , vol.10 , pp. 2493-2506
    • Dent, P.1    Reardon, D.B.2    Park, J.S.3
  • 171
    • 0034029550 scopus 로고    scopus 로고
    • Ionizing radiation-induced mitogen-activated protein (MAP) kinase activation in DU145 prostate carcinoma cells: MAP kinase inhibition enhances radiation-induced cell killing and G2/M-phase arrest
    • Hagan M, Wang L, Hanley JR, et al. Ionizing radiation-induced mitogen-activated protein (MAP) kinase activation in DU145 prostate carcinoma cells: MAP kinase inhibition enhances radiation-induced cell killing and G2/M-phase arrest. Radiat Res 2000; 153: 371-383.
    • (2000) Radiat Res , vol.153 , pp. 371-383
    • Hagan, M.1    Wang, L.2    Hanley, J.R.3
  • 172
    • 0031742981 scopus 로고    scopus 로고
    • Ionizing radiation-induced MEK and Erk activation does not enhance survival of irradiated human squamous carcinoma cells
    • Bonner JA, Vroman BT, Christianson TJ, et al. Ionizing radiation-induced MEK and Erk activation does not enhance survival of irradiated human squamous carcinoma cells. Int J Radiat Oncol Biol Phys 1998; 42: 921-925.
    • (1998) Int J Radiat Oncol Biol Phys , vol.42 , pp. 921-925
    • Bonner, J.A.1    Vroman, B.T.2    Christianson, T.J.3
  • 173
    • 0032984348 scopus 로고    scopus 로고
    • Blockade of the MAP kinase pathway suppresses growth of colon tumors in vivo
    • Sebolt-Leopold JS, Dudley DT, Herrera R, et al. Blockade of the MAP kinase pathway suppresses growth of colon tumors in vivo. Nat Med 1999; 5: 810-816
    • (1999) Nat Med , vol.5 , pp. 810-816
    • Sebolt-Leopold, J.S.1    Dudley, D.T.2    Herrera, R.3
  • 174
    • 17144460676 scopus 로고    scopus 로고
    • The discovery of potent cRaf1 kinase inhibitors
    • Lackey K, Cory M, Davis R, et al. The discovery of potent cRaf1 kinase inhibitors. Bioorg Med Chem Lett 2000; 10: 223-226.
    • (2000) Bioorg Med Chem Lett , vol.10 , pp. 223-226
    • Lackey, K.1    Cory, M.2    Davis, R.3
  • 175
    • 0035872442 scopus 로고    scopus 로고
    • Inhibition of signal transduction by the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin results in cytostasis and apoptosis
    • Hostein I, Robertson D, DiStefano F, et al. Inhibition of signal transduction by the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin results in cytostasis and apoptosis. Cancer Res 2001; 61: 4003-4009.
    • (2001) Cancer Res , vol.61 , pp. 4003-4009
    • Hostein, I.1    Robertson, D.2    DiStefano, F.3
  • 176
    • 0033378009 scopus 로고    scopus 로고
    • c-raf-1 depletion and tumor responses in patients treated with the c-raf-1 antisense oligodeoxynucleotide ISIS 5132 (CGP 69846A)
    • O'Dwyer PJ, Stevenson JP, Gallagher M, et al. c-raf-1 depletion and tumor responses in patients treated with the c-raf-1 antisense oligodeoxynucleotide ISIS 5132 (CGP 69846A). Clin Cancer Res 1999; 5: 3977-3982.
    • (1999) Clin Cancer Res , vol.5 , pp. 3977-3982
    • O'Dwyer, P.J.1    Stevenson, J.P.2    Gallagher, M.3
  • 177
    • 0032984099 scopus 로고    scopus 로고
    • Phase I clinical/pharmacokinetic and pharmacodynamic trial of the c-raf-1 antisense oligonucleotide ISIS 5132 (CGP 69846A)
    • Stevenson JP, Yao KS, Gallagher M, et al. Phase I clinical/pharmacokinetic and pharmacodynamic trial of the c-raf-1 antisense oligonucleotide ISIS 5132 (CGP 69846A). J Clin Oncol 1999; 17: 2227-2236.
    • (1999) J Clin Oncol , vol.17 , pp. 2227-2236
    • Stevenson, J.P.1    Yao, K.S.2    Gallagher, M.3
  • 178
    • 0033610788 scopus 로고    scopus 로고
    • Specific inhibitors of p38 mitogen-activated protein kinase block 3T3- L1 adipogenesis
    • Engelman JA, Lisanti MP, Scherer PE. Specific inhibitors of p38 mitogen-activated protein kinase block 3T3- L1 adipogenesis. J Biol Chem 1998; 273: 32111-32120.
    • (1998) J Biol Chem , vol.273 , pp. 32111-32120
    • Engelman, J.A.1    Lisanti, M.P.2    Scherer, P.E.3
  • 179
    • 0035062232 scopus 로고    scopus 로고
    • Analysis of pharmacologic inhibitors of Jun N-terminal kinases
    • Murray BW, Bennett BL, Sasaki DT. Analysis of pharmacologic inhibitors of Jun N-terminal kinases. Methods Enzymol 2001; 332: 432-452.
    • (2001) Methods Enzymol , vol.332 , pp. 432-452
    • Murray, B.W.1    Bennett, B.L.2    Sasaki, D.T.3
  • 180
    • 0032850020 scopus 로고    scopus 로고
    • p38 MAPK signalling cascades in inflammatory disease
    • Herlaar E, Brown Z. p38 MAPK signalling cascades in inflammatory disease. Mol Med Today 1999; 5: 439-447.
    • (1999) Mol Med Today , vol.5 , pp. 439-447
    • Herlaar, E.1    Brown, Z.2
  • 181
    • 0005318501 scopus 로고    scopus 로고
    • Effect of SB 203580 on the activity of c-Raf in vitro and in vivo
    • Hall-Jackson CA, Goedert M, Hedge P, et al. Effect of SB 203580 on the activity of c-Raf in vitro and in vivo. Oncogene 1999; 18: 2047-2054.
    • (1999) Oncogene , vol.18 , pp. 2047-2054
    • Hall-Jackson, C.A.1    Goedert, M.2    Hedge, P.3
  • 182
    • 0034629345 scopus 로고    scopus 로고
    • The pyridinyl imidazole inhibitor SB203580 blocks phosphoinositide- dependent protein kinase activity, protein kinase B phosphorylation, and retinoblastoma hyperphosphorylation in interleukin-2-stimulated T cells independently of p38 mitogen-activated protein kinase
    • Lali FV, Hunt AE, Turner SJ, et al. The pyridinyl imidazole inhibitor SB203580 blocks phosphoinositide- dependent protein kinase activity, protein kinase B phosphorylation, and retinoblastoma hyperphosphorylation in interleukin-2-stimulated T cells independently of p38 mitogen-activated protein kinase. J Biol Chem 2000; 275: 7395-7402.
    • (2000) J Biol Chem , vol.275 , pp. 7395-7402
    • Lali, F.V.1    Hunt, A.E.2    Turner, S.J.3
  • 183
    • 0035019371 scopus 로고    scopus 로고
    • CEP-1347/KT-7515, an inhibitor of SAPK/JNK pathway activation, promotes survival and blocks multiple events associated with Abeta-induced cortical neuron apoptosis
    • Bozyczko-Coyne D, O'Kane TM, Wu ZL, et al. CEP-1347/KT-7515, an inhibitor of SAPK/JNK pathway activation, promotes survival and blocks multiple events associated with Abeta-induced cortical neuron apoptosis. J Neurochem 2001; 77: 849-863.
    • (2001) J Neurochem , vol.77 , pp. 849-863
    • Bozyczko-Coyne, D.1    O'Kane, T.M.2    Wu, Z.L.3
  • 184
    • 0035816685 scopus 로고    scopus 로고
    • Cep-1347 (kt7515), a semisynthetic inhibitor of the mixed lineage kinase family
    • Maroney AC, Finn JP, Connors TJ, et al. Cep-1347 (kt7515), a semisynthetic inhibitor of the mixed lineage kinase family. J Biol Chem 2001; 276: 25302-25308.
    • (2001) J Biol Chem , vol.276 , pp. 25302-25308
    • Maroney, A.C.1    Finn, J.P.2    Connors, T.J.3
  • 185
    • 0033965714 scopus 로고    scopus 로고
    • Glutathione-S-Transferase as a selective inhibitor of oncogenic ras-p21-induced mitogenic signaling through blockade of activation of jun by jun-N-terminal kinase
    • Villafania A, Anwar K, Amar S, et al. Glutathione-S-Transferase as a selective inhibitor of oncogenic ras-p21-induced mitogenic signaling through blockade of activation of jun by jun-N-terminal kinase. Ann Clin Lab Sci 2000; 30: 57-64.
    • (2000) Ann Clin Lab Sci , vol.30 , pp. 57-64
    • Villafania, A.1    Anwar, K.2    Amar, S.3
  • 186
    • 0035958732 scopus 로고    scopus 로고
    • Effects of MAP kinase cascade inhibitors on the MKK5/ERK5 pathway
    • Mody N, Leitch J, Armstrong C, et al. Effects of MAP kinase cascade inhibitors on the MKK5/ERK5 pathway. FEBS Lett 2001; 502: 21-24.
    • (2001) FEBS Lett , vol.502 , pp. 21-24
    • Mody, N.1    Leitch, J.2    Armstrong, C.3
  • 187
    • 0034655220 scopus 로고    scopus 로고
    • U0126 reverses Ki-ras-mediated transformation by blocking both mitogen-activated protein kinase and p70 S6 kinase pathways
    • Fukazawa H, Uehara Y. U0126 reverses Ki-ras-mediated transformation by blocking both mitogen-activated protein kinase and p70 S6 kinase pathways. Cancer Res 2000; 60: 2104-2107.
    • (2000) Cancer Res , vol.60 , pp. 2104-2107
    • Fukazawa, H.1    Uehara, Y.2
  • 188
    • 0035877641 scopus 로고    scopus 로고
    • Signal transduction pathways involved in phosphorylation and activation of p70S6K following exposure to UVA irradiation
    • Zhang Y, Dong Z, Nomura M, et al. Signal transduction pathways
    • (2001) J Biol Chem , vol.276 , pp. 20913-20923
    • Zhang, Y.1    Dong, Z.2    Nomura, M.3
  • 189
    • 0028880006 scopus 로고
    • Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis
    • Xia Z, Dickens M, Raingeaud J, et al. Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis. Science 1995; 270: 1326-1331.
    • (1995) Science , vol.270 , pp. 1326-1331
    • Xia, Z.1    Dickens, M.2    Raingeaud, J.3
  • 190
    • 0033970533 scopus 로고    scopus 로고
    • Dual specificity phosphatases: A gene family for control of MAP kinase function
    • Camps M, Nichols A, Arkinstall S. Dual specificity phosphatases: a gene family for control of MAP kinase function. FASEB J 2000; 14: 6-16.
    • (2000) FASEB J , vol.14 , pp. 6-16
    • Camps, M.1    Nichols, A.2    Arkinstall, S.3
  • 191
    • 0027306121 scopus 로고
    • The human CL100 gene encodes a Tyr/Thr-protein phosphatase which potently and specifically inactivates MAP kinase and suppresses its activation by oncogenic ras in Xenopus oocyte extracts
    • Alessi DR, Smythe C, Keyse SM. The human CL100 gene encodes a Tyr/Thr-protein phosphatase which potently and specifically inactivates MAP kinase and suppresses its activation by oncogenic ras in Xenopus oocyte extracts. Oncogene 1993; 8: 2015-2020.
    • (1993) Oncogene , vol.8 , pp. 2015-2020
    • Alessi, D.R.1    Smythe, C.2    Keyse, S.M.3
  • 192
    • 15144352589 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of a novel mitogen-activated protein kinase phosphatase, MKP-4
    • Muda M, Boschert U, Smith A, et al. Molecular cloning and functional characterization of a novel mitogen-activated protein kinase phosphatase, MKP-4. J Biol Chem 1997; 272: 5141-5151.
    • (1997) J Biol Chem , vol.272 , pp. 5141-5151
    • Muda, M.1    Boschert, U.2    Smith, A.3
  • 193
    • 0035854673 scopus 로고    scopus 로고
    • A Novel MAPK Phosphatase MKP-7 acts preferentially on JNK/SAPK and p38alpha and beta MAPKs
    • Tanoue T, Yamamoto T, Maeda R, et al. A Novel MAPK Phosphatase MKP-7 acts preferentially on JNK/SAPK and p38alpha and beta MAPKs. J Biol Chem 2001; 276: 26629-26639.
    • (2001) J Biol Chem , vol.276 , pp. 26629-26639
    • Tanoue, T.1    Yamamoto, T.2    Maeda, R.3
  • 194
    • 0029910140 scopus 로고    scopus 로고
    • The dual specificity phosphatases M3/6 and MKP-3 are highly selective for inactivation of distinct mitogen-activated protein kinases
    • Muda M, Theodosiou A, Rodrigues N, et al. The dual specificity phosphatases M3/6 and MKP-3 are highly selective for inactivation of distinct mitogen-activated protein kinases. J Biol Chem 1996; 271: 27205-27208.
    • (1996) J Biol Chem , vol.271 , pp. 27205-27208
    • Muda, M.1    Theodosiou, A.2    Rodrigues, N.3
  • 195
    • 9244244243 scopus 로고    scopus 로고
    • A member of the MAP kinase phosphatase gene family in mouse containing a complex trinucleotide repeat in the coding region
    • Theodosiou AM, Rodrigues NR, Nesbit MA, et al. A member of the MAP kinase phosphatase gene family in mouse containing a complex trinucleotide repeat in the coding region. Hum Mol Genet 1996; 5: 675-684.
    • (1996) Hum Mol Genet , vol.5 , pp. 675-684
    • Theodosiou, A.M.1    Rodrigues, N.R.2    Nesbit, M.A.3
  • 196
    • 0027476773 scopus 로고
    • PAC-1: A mitogen-induced nuclear protein tyrosine phosphatase
    • Rohan PJ, Davis P, Moskaluk CA, et al. PAC-1: a mitogen-induced nuclear protein tyrosine phosphatase. Science 1993; 259: 1763-1766.
    • (1993) Science , vol.259 , pp. 1763-1766
    • Rohan, P.J.1    Davis, P.2    Moskaluk, C.A.3
  • 197
    • 0029918680 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase phosphatases PAC1, MKP-1, and MKP- 2 have unique substrate specificities and reduced activity in vivo toward the ERK2 sevenmaker mutation
    • Chu Y, Solski PA, Khosravi-Far R, et al. The mitogen-activated protein kinase phosphatases PAC1, MKP-1, and MKP- 2 have unique substrate specificities and reduced activity in vivo toward the ERK2 sevenmaker mutation. J Biol Chem 1996; 271: 6497-6501.
    • (1996) J Biol Chem , vol.271 , pp. 6497-6501
    • Chu, Y.1    Solski, P.A.2    Khosravi-Far, R.3
  • 198
    • 0032557632 scopus 로고    scopus 로고
    • Catalytic activation of the phosphatase MKP-3 by ERK2 mitogen-activated protein kinase
    • Camps M, Nichols A, Gillieron C, et al. Catalytic activation of the phosphatase MKP-3 by ERK2 mitogen-activated protein kinase. Science 1998; 280: 1262-1265.
    • (1998) Science , vol.280 , pp. 1262-1265
    • Camps, M.1    Nichols, A.2    Gillieron, C.3
  • 199
    • 0027358722 scopus 로고
    • MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo
    • Sun H, Charles CH, Lau LF, et al. MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo. Cell 1993; 75: 487-493.
    • (1993) Cell , vol.75 , pp. 487-493
    • Sun, H.1    Charles, C.H.2    Lau, L.F.3
  • 200
    • 0032571535 scopus 로고    scopus 로고
    • Induction of the mitogen-activated protein kinase phosphatase MKP3 by nerve growth factor in differentiating PC12
    • Camps M, Chabert C, Muda M, et al. Induction of the mitogen-activated protein kinase phosphatase MKP3 by nerve growth factor in differentiating PC12. FEBS Lett 1998; 425: 271-276.
    • (1998) FEBS Lett , vol.425 , pp. 271-276
    • Camps, M.1    Chabert, C.2    Muda, M.3
  • 201
    • 0038832564 scopus 로고    scopus 로고
    • Reduced MAP kinase phosphatase-1 degradation after p42/p44MAPK-dependent phosphorylation
    • Brondello JM, Pouyssegur J, McKenzie FR. Reduced MAP kinase phosphatase-1 degradation after p42/p44MAPK-dependent phosphorylation. Science 1999; 286: 2514-2517
    • (1999) Science , vol.286 , pp. 2514-2517
    • Brondello, J.M.1    Pouyssegur, J.2    McKenzie, F.R.3
  • 202
    • 0027143725 scopus 로고
    • Protein serine/threonine phosphatases: Structure, regulation, and functions in cell growth
    • Mumby MC, Walter G. Protein serine/threonine phosphatases: structure, regulation, and functions in cell growth. Physiol Rev 1993; 73: 673-699.
    • (1993) Physiol Rev , vol.73 , pp. 673-699
    • Mumby, M.C.1    Walter, G.2
  • 203
    • 0029257329 scopus 로고
    • Inactivation of p42 MAP kinase by protein phosphatase 2A and a protein tyrosine phosphatase, but not CL100, in various cell lines
    • Alessi DR, Gomez N, Moorhead G, et al. Inactivation of p42 MAP kinase by protein phosphatase 2A and a protein tyrosine phosphatase, but not CL100, in various cell lines. Curr Biol 1995; 5: 283-295.
    • (1995) Curr Biol , vol.5 , pp. 283-295
    • Alessi, D.R.1    Gomez, N.2    Moorhead, G.3
  • 204
    • 0027772552 scopus 로고
    • The interaction of SV40 small tumor antigen with protein phosphatase 2A stimulates the map kinase pathway and induces cell proliferation
    • Sontag E, Fedorov S, Kamibayashi C, et al. The interaction of SV40 small tumor antigen with protein phosphatase 2A stimulates the map kinase pathway and induces cell proliferation. Cell 1993; 75: 887-897.
    • (1993) Cell , vol.75 , pp. 887-897
    • Sontag, E.1    Fedorov, S.2    Kamibayashi, C.3
  • 205
    • 0029257329 scopus 로고
    • Inactivation of p42 MAP kinase by protein phosphatase 2A and a protein tyrosine phosphatase, but not CL100, in various cell lines
    • Alessi DR, Gomez N, Moorhead G, et al. Inactivation of p42 MAP kinase by protein phosphatase 2A and a protein tyrosine phosphatase, but not CL100, in various cell lines. Curr Biol 1995; 5: 283-295.
    • (1995) Curr Biol , vol.5 , pp. 283-295
    • Alessi, D.R.1    Gomez, N.2    Moorhead, G.3
  • 206
    • 0000714961 scopus 로고    scopus 로고
    • Regulation of protein kinase cascades by protein phosphatase 2A
    • Millward TA, Zolnierowicz S, Hemmings BA. Regulation of protein kinase cascades by protein phosphatase 2A. Trends Biochem Sci 1999; 24: 186-191.
    • (1999) Trends Biochem Sci , vol.24 , pp. 186-191
    • Millward, T.A.1    Zolnierowicz, S.2    Hemmings, B.A.3
  • 207
    • 0033961307 scopus 로고    scopus 로고
    • Small-molecule inhibitors of the cell cycle
    • Crews CM, Mohan R. Small-molecule inhibitors of the cell cycle. Curr Opin Chem Biol 2000; 4: 47-53.
    • (2000) Curr Opin Chem Biol , vol.4 , pp. 47-53
    • Crews, C.M.1    Mohan, R.2
  • 208
    • 0002193472 scopus 로고    scopus 로고
    • Protein dephosphorylation and the intracellular control of the cell number
    • Berndt N. Protein dephosphorylation and the intracellular control of the cell number. Front Biosci 1999; 4: D22-42.
    • (1999) Front Biosci , vol.4
    • Berndt, N.1
  • 209
    • 0032744493 scopus 로고    scopus 로고
    • Cell cycle-regulated proteolysis of mitotic target proteins
    • Bastians H, Topper LM, Gorbsky GL, et al. Cell cycle-regulated proteolysis of mitotic target proteins. Mol Biol Cell 1999; 10: 3927-3941.
    • (1999) Mol Biol Cell , vol.10 , pp. 3927-3941
    • Bastians, H.1    Topper, L.M.2    Gorbsky, G.L.3
  • 210
    • 0028931265 scopus 로고
    • Principles of CDK regulation
    • Morgan DO. Principles of CDK regulation. Nature 1995; 374: 131-134.
    • (1995) Nature , vol.374 , pp. 131-134
    • Morgan, D.O.1
  • 211
    • 0024473604 scopus 로고
    • G1 events and regulation of cell proliferation
    • Pardee AB. G1 events and regulation of cell proliferation. Science 1989; 246: 603-608.
    • (1989) Science , vol.246 , pp. 603-608
    • Pardee, A.B.1
  • 212
    • 0344671608 scopus 로고    scopus 로고
    • Functions of the retinoblastoma protein
    • Kaelin WG, Jr. Functions of the retinoblastoma protein. Bioessays 1999; 21: 950-958.
    • (1999) Bioessays , vol.21 , pp. 950-958
    • Kaelin W.G., Jr.1
  • 213
    • 0029033861 scopus 로고
    • The retinoblastoma protein and cell cycle control
    • Weinberg RA. The retinoblastoma protein and cell cycle control. Cell 1995; 81: 323-330.
    • (1995) Cell , vol.81 , pp. 323-330
    • Weinberg, R.A.1
  • 214
    • 0029119740 scopus 로고
    • Cell cycle control in mammalian cells: Role of cyclins, cyclin dependent kinases (CDKs), growth suppressor genes and cyclin-dependent kinase inhibitors (CKIs)
    • Grana X, Reddy EP. Cell cycle control in mammalian cells: role of cyclins, cyclin dependent kinases (CDKs), growth suppressor genes and cyclin-dependent kinase inhibitors (CKIs). Oncogene 1995; 11: 211-219.
    • (1995) Oncogene , vol.11 , pp. 211-219
    • Grana, X.1    Reddy, E.P.2
  • 215
    • 0033629383 scopus 로고    scopus 로고
    • Cell cycle regulation by the Cdc25 phosphatase family
    • Nilsson I, Hoffmann I. Cell cycle regulation by the Cdc25 phosphatase family. Prog Cell Cycle Res 2000; 4: 107-114.
    • (2000) Prog Cell Cycle Res , vol.4 , pp. 107-114
    • Nilsson, I.1    Hoffmann, I.2
  • 216
    • 0029025606 scopus 로고
    • The cyclosome, a large complex containing cyclin-selective ubiquitin ligase activity, targets cyclins for destruction at the end of mitosis
    • Sudakin V, Ganoth D, Dahan A, et al. The cyclosome, a large complex containing cyclin-selective ubiquitin ligase activity, targets cyclins for destruction at the end of mitosis. Mol Biol Cell 1995; 6: 185-197.
    • (1995) Mol Biol Cell , vol.6 , pp. 185-197
    • Sudakin, V.1    Ganoth, D.2    Dahan, A.3
  • 217
    • 0029075883 scopus 로고
    • Reversible phosphorylation controls the activity of cyclosome- associated cyclin-ubiquitin ligase
    • Lahav-Baratz S, Sudakin V, Ruderman JV, et al. Reversible phosphorylation controls the activity of cyclosome- associated cyclin-ubiquitin ligase. Proc Natl Acad Sci USA 1995; 92: 9303-9307.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9303-9307
    • Lahav-Baratz, S.1    Sudakin, V.2    Ruderman, J.V.3
  • 218
    • 0024425887 scopus 로고
    • Checkpoints: Controls that ensure the order of cell cycle events
    • Hartwell LH and Weinert TA. Checkpoints: controls that ensure the order of cell cycle events. Science 1989; 246: 629-634.
    • (1989) Science , vol.246 , pp. 629-634
    • Hartwell, L.H.1    Weinert, T.A.2
  • 219
    • 0029808466 scopus 로고    scopus 로고
    • Cell cycle checkpoints: Preventing an identity crisis
    • Elledge, SJ. Cell cycle checkpoints: preventing an identity crisis. Science 1996; 274: 1664-1672.
    • (1996) Science , vol.274 , pp. 1664-1672
    • Elledge, S.J.1
  • 220
    • 0028868260 scopus 로고
    • The tumor suppressor protein p53: A receptor to genotoxic stress that controls cell growth and survival
    • Hainaut P. The tumor suppressor protein p53: a receptor to genotoxic stress that controls cell growth and survival. Curr Opin Oncol 1995; 7: 76-82.
    • (1995) Curr Opin Oncol , vol.7 , pp. 76-82
    • Hainaut, P.1
  • 221
    • 0034707047 scopus 로고    scopus 로고
    • The DNA damage response: Putting checkpoints in perspective
    • Zhou BB, Elledge SJ. The DNA damage response: putting checkpoints in perspective. Nature 2000; 408: 433-439.
    • (2000) Nature , vol.408 , pp. 433-439
    • Zhou, B.B.1    Elledge, S.J.2
  • 222
    • 0034641724 scopus 로고    scopus 로고
    • Ataxia telangiectasia-mutated phosphorylates Chk2 in vivo and in vitro
    • Matsuoka S, Rotman G, Ogawa A, et al. Ataxia telangiectasia-mutated phosphorylates Chk2 in vivo and in vitro. Proc Natl Acad Sci USA 2000; 97: 10389-10394.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10389-10394
    • Matsuoka, S.1    Rotman, G.2    Ogawa, A.3
  • 223
    • 0032973830 scopus 로고    scopus 로고
    • Basis for the checkpoint signal specificity that regulates Chk1 and Cds1 protein kinases
    • Brondello JM, Boddy MN, Furnari B, et al. Basis for the checkpoint signal specificity that regulates Chk1 and Cds1 protein kinases. Mol Cell Biol 1999; 19: 4262-4269.
    • (1999) Mol Cell Biol , vol.19 , pp. 4262-4269
    • Brondello, J.M.1    Boddy, M.N.2    Furnari, B.3
  • 224
    • 0032146974 scopus 로고    scopus 로고
    • The vertebrate cell kinetochore and its roles during mitosis
    • Rieder CL, Salmon ED. The vertebrate cell kinetochore and its roles during mitosis. Trends Cell Biol 1998; 8: 310-318.
    • (1998) Trends Cell Biol , vol.8 , pp. 310-318
    • Rieder, C.L.1    Salmon, E.D.2
  • 225
    • 14444267778 scopus 로고    scopus 로고
    • How cells get the right chromosomes
    • Nicklas RB. How cells get the right chromosomes. Science 1997; 275: 632-637.
    • (1997) Science , vol.275 , pp. 632-637
    • Nicklas, R.B.1
  • 226
    • 0033621361 scopus 로고    scopus 로고
    • MAPK mediates RAS-induced chromosome instability
    • Saavedra HI, Fukasawa K, Conn CW, et al. MAPK mediates RAS-induced chromosome instability. J Biol Chem 1999; 274: 38083-38090.
    • (1999) J Biol Chem , vol.274 , pp. 38083-38090
    • Saavedra, H.I.1    Fukasawa, K.2    Conn, C.W.3
  • 227
    • 0033618410 scopus 로고    scopus 로고
    • Multiple ras effector pathways contribute to G(1) cell cycle progression
    • Gille H, Downward J. Multiple ras effector pathways contribute to G(1) cell cycle progression. J Biol Chem 1999; 274: 22033-22040.
    • (1999) J Biol Chem , vol.274 , pp. 22033-22040
    • Gille, H.1    Downward, J.2
  • 228
    • 0027965563 scopus 로고
    • Ras/MAP kinase-dependent and -independent signaling pathways target distinct ternary complex factors
    • Hipskind RA, Buscher D, Nordheim A, et al. Ras/MAP kinase-dependent and -independent signaling pathways target distinct ternary complex factors. Genes Dev 1994; 8: 1803-1816.
    • (1994) Genes Dev , vol.8 , pp. 1803-1816
    • Hipskind, R.A.1    Buscher, D.2    Nordheim, A.3
  • 229
    • 0030310201 scopus 로고    scopus 로고
    • A temporal and biochemical link between growth factor-activated MAP kinases, cyclin D1 induction and cell cycle entry
    • Lavoie JN, Rivard N, L'Allemain G, et al. A temporal and biochemical link between growth factor-activated MAP kinases, cyclin D1 induction and cell cycle entry. Prog Cell Cycle Res 1996; 2: 49-58.
    • (1996) Prog Cell Cycle Res , vol.2 , pp. 49-58
    • Lavoie, J.N.1    Rivard, N.2    L'Allemain, G.3
  • 230
    • 0029786329 scopus 로고    scopus 로고
    • Cyclin D1 expression is regulated positively by the p42/p44MAPK and negatively by the p38/HOGMAPK pathway
    • Lavoie JN, L'Allemain G, Brunet A, et al. Cyclin D1 expression is regulated positively by the p42/p44MAPK and negatively by the p38/HOGMAPK pathway. J Biol Chem 1996; 271: 20608-20616.
    • (1996) J Biol Chem , vol.271 , pp. 20608-20616
    • Lavoie, J.N.1    L'Allemain, G.2    Brunet, A.3
  • 231
    • 0033006919 scopus 로고    scopus 로고
    • eIF4E activity is regulated at multiple levels
    • Raught B and Gingras AC. eIF4E activity is regulated at multiple levels. Int J Biochem Cell Biol 1999; 31: 43-57.
    • (1999) Int J Biochem Cell Biol , vol.31 , pp. 43-57
    • Raught, B.1    Gingras, A.C.2
  • 232
    • 0029166667 scopus 로고
    • A synthetic inhibitor of the mitogen-activated protein kinase cascade
    • Dudley DT, Pang L, Decker SJ, et al. A synthetic inhibitor of the mitogen-activated protein kinase cascade. Proc Natl Acad Sci USA 1995; 92: 7686-7689.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7686-7689
    • Dudley, D.T.1    Pang, L.2    Decker, S.J.3
  • 233
    • 0027170451 scopus 로고
    • Mitogen-activated protein kinases p42mapk and p44mapk are required for fibroblast proliferation
    • Pages G, Lenormand P, L'Allemain G, et al. Mitogen-activated protein kinases p42mapk and p44mapk are required for fibroblast proliferation. Proc Natl Acad Sci USA 1993; 90: 8319-8323.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8319-8323
    • Pages, G.1    Lenormand, P.2    L'Allemain, G.3
  • 234
    • 0028222136 scopus 로고
    • A requirement for extracellular signal-regulated kinase (ERK) function in the activation of AP-1 by Ha-Ras, phorbol 12-myristate 13-acetate, and serum
    • Frost JA, Geppert TD, Cobb MH, et al. A requirement for extracellular signal-regulated kinase (ERK) function in the activation of AP-1 by Ha-Ras, phorbol 12-myristate 13-acetate, and serum. Proc Natl Acad Sci USA 1994; 91: 3844-3848.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 3844-3848
    • Frost, J.A.1    Geppert, T.D.2    Cobb, M.H.3
  • 235
    • 0028079956 scopus 로고
    • Constitutively active mutants of MAP kinase kinase (MEK1) induce growth factor-relaxation and oncogenicity when expressed in fibroblasts
    • Brunet A, Pages G, Pouyssegur J. Constitutively active mutants of MAP kinase kinase (MEK1) induce growth factor-relaxation and oncogenicity when expressed in fibroblasts. Oncogene 1994; 9: 3379-3387.
    • (1994) Oncogene , vol.9 , pp. 3379-3387
    • Brunet, A.1    Pages, G.2    Pouyssegur, J.3
  • 236
    • 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 AA, et al. 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 1994; 269: 25699-25709.
    • (1994) J Biol Chem , vol.269 , pp. 25699-25709
    • Seger, R.1    Seger, D.2    Reszka, A.A.3
  • 237
    • 0033587009 scopus 로고    scopus 로고
    • Sustained MAP kinase activation is required for the expression of cyclin D1, p21Cip1 and a subset of AP-1 proteins in CCL39 cells
    • Balmanno K, Cook SJ. Sustained MAP kinase activation is required for the expression of cyclin D1, p21Cip1 and a subset of AP-1 proteins in CCL39 cells. Oncogene 1999; 18: 3085-3097.
    • (1999) Oncogene , vol.18 , pp. 3085-3097
    • Balmanno, K.1    Cook, S.J.2
  • 238
    • 0033548548 scopus 로고    scopus 로고
    • pp60(v-src) induction of cyclin D1 requires collaborative interactions between the extracellular signal-regulated kinase, p38, and Jun kinase pathways. A role for cAMP response element-binding protein and activating transcription factor-2 in pp60(v-src) signaling in breast cancer cells
    • Lee RJ, Albanese C, Stenger RJ, et al. pp60(v-src) induction of cyclin D1 requires collaborative interactions between the extracellular signal-regulated kinase, p38, and Jun kinase pathways. A role for cAMP response element-binding protein and activating transcription factor-2 in pp60(v-src) signaling in breast cancer cells. J Biol Chem 1999; 274: 7341-7350.
    • (1999) J Biol Chem , vol.274 , pp. 7341-7350
    • Lee, R.J.1    Albanese, C.2    Stenger, R.J.3
  • 239
    • 0033521651 scopus 로고    scopus 로고
    • c-Jun regulates cell cycle progression and apoptosis by distinct mechanisms
    • Wisdom R, Johnson RS, Moore C. c-Jun regulates cell cycle progression and apoptosis by distinct mechanisms. EMBO J 1999; 18: 188-197.
    • (1999) EMBO J , vol.18 , pp. 188-197
    • Wisdom, R.1    Johnson, R.S.2    Moore, C.3
  • 240
    • 0030883584 scopus 로고    scopus 로고
    • Sustained activation of extracellular-signal-regulated kinase 1 (ERK1) is required for the continued expression of cyclin D1 in G1 phase
    • Weber JD, Raben DM, Phillips PJ, et al. Sustained activation of extracellular-signal-regulated kinase 1 (ERK1) is required for the continued expression of cyclin D1 in G1 phase. Biochem J 1997; 326: 61-68.
    • (1997) Biochem J , vol.326 , pp. 61-68
    • Weber, J.D.1    Raben, D.M.2    Phillips, P.J.3
  • 241
    • 0034715917 scopus 로고    scopus 로고
    • Evidence for a direct correlation between c-Jun NH2 terminal kinase 1 activation, cyclin D2 expression, and G(1)/S phase transition in the murine hybridoma 7TD1 cells
    • Turchi L, Loubat, A Rochet N, et al. Evidence for a direct correlation between c-Jun NH2 terminal kinase 1 activation, cyclin D2 expression, and G(1)/S phase transition in the murine hybridoma 7TD1 cells. Exp Cell Res 2000; 261: 220-228.
    • (2000) Exp Cell Res , vol.261 , pp. 220-228
    • Turchi, L.1    Loubat2    Rochet, N.A.3
  • 242
    • 0031693211 scopus 로고    scopus 로고
    • p21WAF1 is dynamically associated with JNK in human T-lymphocytes during cell cycle progression
    • Patel R, Bartosch B, Blank JL. p21WAF1 is dynamically associated with JNK in human T-lymphocytes during cell cycle progression. J Cell Sci 1998; 111: 2247-2255.
    • (1998) J Cell Sci , vol.111 , pp. 2247-2255
    • Patel, R.1    Bartosch, B.2    Blank, J.L.3
  • 243
    • 0032805496 scopus 로고    scopus 로고
    • Nuclear translocation of mitogen-activated protein kinase p42MAPK during the ongoing cell cycle
    • Hulleman E, Bijvelt JJ, Verkleij AJ, et al. Nuclear translocation of mitogen-activated protein kinase p42MAPK during the ongoing cell cycle, J Cell Physiol 1999; 180: 325-333.
    • (1999) J Cell Physiol , vol.180 , pp. 325-333
    • Hulleman, E.1    Bijvelt, J.J.2    Verkleij, A.J.3
  • 244
    • 0028931406 scopus 로고
    • ERK phosphorylation potentiates Elk-1-mediated ternary complex formation and transactivation
    • Gille H, Kortenjann M, Thomae O, et al. ERK phosphorylation potentiates Elk-1-mediated ternary complex formation and transactivation. EMBO J 1995; 14: 951-962.
    • (1995) EMBO J , vol.14 , pp. 951-962
    • Gille, H.1    Kortenjann, M.2    Thomae, O.3
  • 245
    • 0028239101 scopus 로고
    • Inhibition of v-raf-dependent c-fos expression and transformation by a kinase-defective mutant of the mitogen-activated protein kinase Erk2
    • Kortenjann M, Thomae O, Shaw PE. Inhibition of v-raf-dependent c-fos expression and transformation by a kinase-defective mutant of the mitogen-activated protein kinase Erk2. Mol Cell Biol 1994; 14: 4815-4824.
    • (1994) Mol Cell Biol , vol.14 , pp. 4815-4824
    • Kortenjann, M.1    Thomae, O.2    Shaw, P.E.3
  • 246
    • 0032553412 scopus 로고    scopus 로고
    • Growth hormone stimulates phosphorylation and activation of elk-1 and expression of c-fos, egr-1, and junB through activation of extracellular signal-regulated kinases 1 and 2
    • Hodge C, Liao J, Stofega M, et al. Growth hormone stimulates phosphorylation and activation of elk-1 and expression of c-los, egr-1, and junB through activation of extracellular signal-regulated kinases 1 and 2. J Biol Chem 1998; 273: 31327-31336.
    • (1998) J Biol Chem , vol.273 , pp. 31327-31336
    • Hodge, C.1    Liao, J.2    Stofega, M.3
  • 247
    • 0031438751 scopus 로고    scopus 로고
    • Transforming growth factor-alpha enhances cyclin D1 transcription through the binding of early growth response protein to a cis-regulatory element in the cyclin D1 promoter
    • Yan YX, Nakagawa H, Lee MH, et al. Transforming growth factor-alpha enhances cyclin D1 transcription through the binding of early growth response protein to a cis-regulatory element in the cyclin D1 promoter. J Biol Chem 1997; 272: 33181-33190.
    • (1997) J Biol Chem , vol.272 , pp. 33181-33190
    • Yan, Y.X.1    Nakagawa, H.2    Lee, M.H.3
  • 248
    • 0032996623 scopus 로고    scopus 로고
    • c-Myc regulates cyclin D-Cdk4 and -Cdk6 activity but affects cell cycle progression at multiple independent points
    • Mateyak MK, Obaya AJ, Sedivy JM. c-Myc regulates cyclin D-Cdk4 and -Cdk6 activity but affects cell cycle progression at multiple independent points. Mol Cell Biol 1999; 19: 4672-4683.
    • (1999) Mol Cell Biol , vol.19 , pp. 4672-4683
    • Mateyak, M.K.1    Obaya, A.J.2    Sedivy, J.M.3
  • 249
    • 0035397653 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases control p27/Kip1 expression and growth of human melanoma cells
    • Kortylewski M, Heinrich PC, Kauffmann ME, et al. Mitogen-activated protein kinases control p27/Kip1 expression and growth of human melanoma cells. Biochem J 2001; 357: 297-303.
    • (2001) Biochem J , vol.357 , pp. 297-303
    • Kortylewski, M.1    Heinrich, P.C.2    Kauffmann, M.E.3
  • 250
    • 0035836706 scopus 로고    scopus 로고
    • Myc represses the p21(WAF1/CIP1) promoter and interacts with Sp1/Sp3
    • Gartel AL, Ye X, Goufman E, et al. Myc represses the p21(WAF1/CIP1) promoter and interacts with Sp1/Sp3. Proc Natl Acad Sci USA 2001; 98: 4510-4515.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 4510-4515
    • Gartel, A.L.1    Ye, X.2    Goufman, E.3
  • 251
    • 0034662959 scopus 로고    scopus 로고
    • A role for transcriptional repression of p21CIP1 by c-Myc in overcoming transforming growth factor beta -induced cell-cycle arrest
    • Claassen GF, Hann SR. A role for transcriptional repression of p21CIP1 by c-Myc in overcoming transforming growth factor beta -induced cell-cycle arrest. Proc Natl Acad Sci USA 2000; 97: 9498-9503.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 9498-9503
    • Claassen, G.F.1    Hann, S.R.2
  • 252
    • 0033050069 scopus 로고    scopus 로고
    • Transcriptional repressor ERF is a Ras/mitogen-activated protein kinase target that regulates cellular proliferation
    • Le Gallic L, Sgouras D, Beal G, Jr., et al. Transcriptional repressor ERF is a Ras/mitogen-activated protein kinase target that regulates cellular proliferation. Mol Cell Biol 1999; 19: 4121-4133.
    • (1999) Mol Cell Biol , vol.19 , pp. 4121-4133
    • Le Gallic, L.1    Sgouras, D.2    Beal G., Jr.3
  • 253
    • 0030977269 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2
    • Waskiewicz AJ, Flynn A, Proud CG, et al. Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2. EMBO J 1997; 16: 1909-1920.
    • (1997) EMBO J , vol.16 , pp. 1909-1920
    • Waskiewicz, A.J.1    Flynn, A.2    Proud, C.G.3
  • 254
    • 0034928792 scopus 로고    scopus 로고
    • Negative regulation of protein translation by mitogen-activated protein kinase-interacting kinases 1 and 2
    • Knauf U, Tschopp C, Gram H. Negative regulation of protein translation by mitogen-activated protein kinase-interacting kinases 1 and 2. Mol Cell Biol 2001; 21: 5500-5511.
    • (2001) Mol Cell Biol , vol.21 , pp. 5500-5511
    • Knauf, U.1    Tschopp, C.2    Gram, H.3
  • 255
    • 0032540244 scopus 로고    scopus 로고
    • The phosphorylation of eukaryotic initiation factor eIF4E in response to phorbol esters, cell stresses, and cytokines is mediated by distinct MAP kinase pathways
    • Wang X, Flynn A, Waskiewicz AJ, et al. The phosphorylation of eukaryotic initiation factor eIF4E in response to phorbol esters, cell stresses, and cytokines is mediated by distinct MAP kinase pathways. J Biol Chem 1998; 273: 9373-9377
    • (1998) J Biol Chem , vol.273 , pp. 9373-9377
    • Wang, X.1    Flynn, A.2    Waskiewicz, A.J.3
  • 256
    • 0028872649 scopus 로고
    • Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation
    • Marshall CJ. Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation. Cell 1995; 80: 179-185.
    • (1995) Cell , vol.80 , pp. 179-185
    • Marshall, C.J.1
  • 257
    • 0032190629 scopus 로고    scopus 로고
    • Premature senescence involving p53 and p16 is activated in response to constitutive MEK/MAPK mitogenic signaling
    • Lin AW, Barradas M, Stone JC, et al. Premature senescence involving p53 and p16 is activated in response to constitutive MEK/MAPK mitogenic signaling. Genes Dev 1998; 12: 3008-3019.
    • (1998) Genes Dev , vol.12 , pp. 3008-3019
    • Lin, A.W.1    Barradas, M.2    Stone, J.C.3
  • 258
    • 0032535711 scopus 로고    scopus 로고
    • Prolonged activation of the mitogen-activated protein kinase pathway promotes DNA synthesis in primary hepatocytes from p21Cip-1/WAF1-null mice, but not in hepatocytes from p16INK4a-null mice
    • Auer KL, Park JS, Seth P, et al. Prolonged activation of the mitogen-activated protein kinase pathway promotes DNA synthesis in primary hepatocytes from p21Cip-1/WAF1-null mice, but not in hepatocytes from p16INK4a-null mice. Biochem J 1998; 336: 551-560.
    • (1998) Biochem J , vol.336 , pp. 551-560
    • Auer, K.L.1    Park, J.S.2    Seth, P.3
  • 259
    • 0033569726 scopus 로고    scopus 로고
    • The Raf-1/MEK/ERK pathway regulates the expression of the p21(Cip1/Waf1) gene in chondrocytes
    • Beier F, Taylor AC, LuValle P. The Raf-1/MEK/ERK pathway regulates the expression of the p21(Cip1/Waf1) gene in chondrocytes. J Biol Chem 1999; 274: 30273-30279.
    • (1999) J Biol Chem , vol.274 , pp. 30273-30279
    • Beier, F.1    Taylor, A.C.2    LuValle, P.3
  • 260
    • 0034696944 scopus 로고    scopus 로고
    • MAPK-dependent expression of p21(WAF) and p27(kip1) in PMA-induced differentiation of HL60 cells
    • Das D, Pintucci G, Stem A. MAPK-dependent expression of p21(WAF) and p27(kip1) in PMA-induced differentiation of HL60 cells. FEBS Lett 2000; 472: 50-52.
    • (2000) FEBS Lett , vol.472 , pp. 50-52
    • Das, D.1    Pintucci, G.2    Stem, A.3
  • 261
    • 0032521642 scopus 로고    scopus 로고
    • The mitogen-activated protein (MAP) kinase cascade can either stimulate or inhibit DNA synthesis in primary cultures of rat hepatocytes depending upon whether its activation is acute/phasic or chronic
    • Tombes RM, Auer KL, Mikkelsen R, et al. The mitogen-activated protein (MAP) kinase cascade can either stimulate or inhibit DNA synthesis in primary cultures of rat hepatocytes depending upon whether its activation is acute/phasic or chronic. Biochem J 1998; 330: 1451-1460.
    • (1998) Biochem J , vol.330 , pp. 1451-1460
    • Tombes, R.M.1    Auer, K.L.2    Mikkelsen, R.3
  • 262
    • 0028363749 scopus 로고
    • Phosphorylation of the tumor suppressor protein p53 by mitogen- activated protein kinases
    • Milne DM, Campbell DG, Caudwell FB, et al. Phosphorylation of the tumor suppressor protein p53 by mitogen- activated protein kinases. J Biol Chem 1994; 269: 9253-9260.
    • (1994) J Biol Chem , vol.269 , pp. 9253-9260
    • Milne, D.M.1    Campbell, D.G.2    Caudwell, F.B.3
  • 263
    • 0028966941 scopus 로고
    • p53 is phosphorylated in vitro and in vivo by an ultraviolet radiation-induced protein kinase characteristic of the c-Jun kinase, JNK1
    • Milne DM, Campbell LE, Campbell DG, et al. p53 is phosphorylated in vitro and in vivo by an ultraviolet radiation-induced protein kinase characteristic of the c-Jun kinase, JNK1. J Biol Chem 1995; 270: 5511-5518.
    • (1995) J Biol Chem , vol.270 , pp. 5511-5518
    • Milne, D.M.1    Campbell, L.E.2    Campbell, D.G.3
  • 264
    • 0034617077 scopus 로고    scopus 로고
    • ERKs and p38 kinase phosphorylate p53 protein at serine 15 in response to UV radiation
    • She QB, Chen N, Dong Z. ERKs and p38 kinase phosphorylate p53 protein at serine 15 in response to UV radiation. J Biol Chem 2000; 275: 20444-20449.
    • (2000) J Biol Chem , vol.275 , pp. 20444-20449
    • She, Q.B.1    Chen, N.2    Dong, Z.3
  • 265
    • 0033485261 scopus 로고    scopus 로고
    • Phosphorylation of human p53 by p38 kinase coordinates N-terminal phosphorylation and apoptosis in response to UV radiation
    • Bulavin DV, Saito S, Hollander MC, et al. Phosphorylation of human p53 by p38 kinase coordinates N-terminal phosphorylation and apoptosis in response to UV radiation. EMBO J 1999; 18: 6845-6854.
    • (1999) EMBO J , vol.18 , pp. 6845-6854
    • Bulavin, D.V.1    Saito, S.2    Hollander, M.C.3
  • 266
    • 0034652718 scopus 로고    scopus 로고
    • p53 phosphorylation and association with murine double minute 2, c-Jun NH2-terminal kinase, p14ARF, and p300/CBP during the cell cycle and after exposure to ultraviolet irradiation
    • Buschmann T, Adler V, Matusevich E, et al. p53 phosphorylation and association with murine double minute 2, c-Jun NH2-terminal kinase, p14ARF, and p300/CBP during the cell cycle and after exposure to ultraviolet irradiation. Cancer Res 2000; 60: 896-900.
    • (2000) Cancer Res , vol.60 , pp. 896-900
    • Buschmann, T.1    Adler, V.2    Matusevich, E.3
  • 267
    • 0034745050 scopus 로고    scopus 로고
    • Jun NH2-terminal kinase phosphorylation of p53 on Thr-81 is important for p53 stabilization and transcriptional activities in response to stress
    • Buschmann T, Potapova O, Bar-Shira A, et al. Jun NH2-terminal kinase phosphorylation of p53 on Thr-81 is important for p53 stabilization and transcriptional activities in response to stress. Mol Cell Biol 2001; 21: 2743-2754.
    • (2001) Mol Cell Biol , vol.21 , pp. 2743-2754
    • Buschmann, T.1    Potapova, O.2    Bar-Shira, A.3
  • 268
    • 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 FX, et al. Selective activation of the JNK signaling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs. Cell 1995; 81: 1147-1157.
    • (1995) Cell , vol.81 , pp. 1147-1157
    • Minden, A.1    Lin, A.2    Claret, F.X.3
  • 269
    • 0029055812 scopus 로고
    • The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway
    • Coso OA, Chiariello M, Yu JC, et al. The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway. Cell 1995; 81: 1137-1146.
    • (1995) Cell , vol.81 , pp. 1137-1146
    • Coso, O.A.1    Chiariello, M.2    Yu, J.C.3
  • 270
    • 0028820587 scopus 로고
    • Rho family GTPases regulate p38 mitogen-activated protein kinase through the downstream mediator Pak1
    • Zhang S, Han J, Sells MA, et al. Rho family GTPases regulate p38 mitogen-activated protein kinase through the downstream mediator Pak1. J Biol Chem 1995; 270: 23934-23936.
    • (1995) J Biol Chem , vol.270 , pp. 23934-23936
    • Zhang, S.1    Han, J.2    Sells, M.A.3
  • 271
    • 0032546654 scopus 로고    scopus 로고
    • Activation of G1 progression, JNK mitogen-activated protein kinase, and actin filament assembly by the exchange factor FGD1
    • Nagata K, Driessens M, Lamarche N, et al. Activation of G1 progression, JNK mitogen-activated protein kinase, and actin filament assembly by the exchange factor FGD1. J Biol Chem 1998; 273: 15453-15457.
    • (1998) J Biol Chem , vol.273 , pp. 15453-15457
    • Nagata, K.1    Driessens, M.2    Lamarche, N.3
  • 272
    • 0030298138 scopus 로고    scopus 로고
    • Rac and Cdc42 induce actin polymerization and G1 cell cycle progression independently of p65PAK and the JNK/SAPK MAP kinase cascade
    • Lamarche N, Tapon N, Stowers L, et al. Rac and Cdc42 induce actin polymerization and G1 cell cycle progression independently of p65PAK and the JNK/SAPK MAP kinase cascade. Cell 1996; 87: 519-529.
    • (1996) Cell , vol.87 , pp. 519-529
    • Lamarche, N.1    Tapon, N.2    Stowers, L.3
  • 273
    • 0031009434 scopus 로고    scopus 로고
    • Cdc42Hs, but not Rac1, inhibits serum-stimulated cell cycle progression at G1/S through a mechanism requiting p38/RK
    • Molnar A, Theodoras AM, Zon LI, et al. Cdc42Hs, but not Rac1, inhibits serum-stimulated cell cycle progression at G1/S through a mechanism requiting p38/RK. J Biol Chem 1997; 272: 13229-13235.
    • (1997) J Biol Chem , vol.272 , pp. 13229-13235
    • Molnar, A.1    Theodoras, A.M.2    Zon, L.I.3
  • 274
    • 0032576547 scopus 로고    scopus 로고
    • Regulation of the cell cycle by focal adhesion kinase
    • Zhao JH, Reiske H, Guan JL. Regulation of the cell cycle by focal adhesion kinase. J Cell Biol 1998; 143: 1997-2008.
    • (1998) J Cell Biol , vol.143 , pp. 1997-2008
    • Zhao, J.H.1    Reiske, H.2    Guan, J.L.3
  • 275
    • 0033612572 scopus 로고    scopus 로고
    • Integrin-mediated activation of focal adhesion kinase is required for signaling to Jun NH2-terminal kinase and progression through the G1 phase of the cell cycle
    • Oktay M, Wary KK, Dans M, et al. Integrin-mediated activation of focal adhesion kinase is required for signaling to Jun NH2-terminal kinase and progression through the G1 phase of the cell cycle. J Cell Biol 1999; 145: 1461-1469.
    • (1999) J Cell Biol , vol.145 , pp. 1461-1469
    • Oktay, M.1    Wary, K.K.2    Dans, M.3
  • 276
    • 0032576547 scopus 로고    scopus 로고
    • Regulation of the cell cycle by focal adhesion kinase
    • Zhao JH, Reiske H, Guan JL. Regulation of the cell cycle by focal adhesion kinase. J Cell Biol 1998; 143: 1997-2008.
    • (1998) J Cell Biol , vol.143 , pp. 1997-2008
    • Zhao, J.H.1    Reiske, H.2    Guan, J.L.3
  • 277
    • 0026657460 scopus 로고
    • Biphasic activation of two mitogen-activated protein kinases during the cell cycle in mammalian cells
    • Tamemoto H, Kadowaki T, Tobe K, et al. Biphasic activation of two mitogen-activated protein kinases during the cell cycle in mammalian cells. J Biol Chem 1992; 267: 20293-20297.
    • (1992) J Biol Chem , vol.267 , pp. 20293-20297
    • Tamemoto, H.1    Kadowaki, T.2    Tobe, K.3
  • 278
    • 0028054929 scopus 로고
    • A 40-kDa myelin basic protein kinase, distinct from erk1 and erk2, is activated in mitotic HeLa cells
    • Heider H, Hug C, Lucocq JM. A 40-kDa myelin basic protein kinase, distinct from erk1 and erk2, is activated in mitotic HeLa cells. Eur J Biochem 1994; 219: 513-520.
    • (1994) Eur J Biochem , vol.219 , pp. 513-520
    • Heider, H.1    Hug, C.2    Lucocq, J.M.3
  • 279
    • 0030029152 scopus 로고    scopus 로고
    • Cell cycle regulation of p70 S6 kinase and p42/p44 mitogen-activated protein kinases in Swiss mouse 3T3 fibroblasts
    • Edelmann HM, Kuhne C, Petritsch C, et al. Cell cycle regulation of p70 S6 kinase and p42/p44 mitogen-activated protein kinases in Swiss mouse 3T3 fibroblasts. J Biol Chem 1996; 271: 963-971.
    • (1996) J Biol Chem , vol.271 , pp. 963-971
    • Edelmann, H.M.1    Kuhne, C.2    Petritsch, C.3
  • 280
    • 0024296405 scopus 로고
    • Altered phosphorylation and activation of pp60c-src during fibroblast mitosis
    • Chackalaparampil I, Shalloway D. Altered phosphorylation and activation of pp60c-src during fibroblast mitosis. Cell 1988; 52: 801-810.
    • (1988) Cell , vol.52 , pp. 801-810
    • Chackalaparampil, I.1    Shalloway, D.2
  • 281
    • 0029093295 scopus 로고
    • Requirement for Src family protein tyrosine kinases in G2 for fibroblast cell division
    • Roche S, Fumagalli S, Courtneidge SA. Requirement for Src family protein tyrosine kinases in G2 for fibroblast cell division. Science 1995; 269: 1567-1569.
    • (1995) Science , vol.269 , pp. 1567-1569
    • Roche, S.1    Fumagalli, S.2    Courtneidge, S.A.3
  • 282
    • 0028787488 scopus 로고
    • Raf-1 is activated during mitosis
    • Laird AD, Taylor SJ, Oberst M, et al. Raf-1 is activated during mitosis. J Biol Chem 1995; 270: 26742-26745.
    • (1995) J Biol Chem , vol.270 , pp. 26742-26745
    • Laird, A.D.1    Taylor, S.J.2    Oberst, M.3
  • 283
    • 0033548072 scopus 로고    scopus 로고
    • Characterization of Raf-1 activation in mitosis
    • Laird AD, Morrison DK, Shalloway D. Characterization of Raf-1 activation in mitosis. J Biol Chem 1999; 274: 4430-4439.
    • (1999) J Biol Chem , vol.274 , pp. 4430-4439
    • Laird, A.D.1    Morrison, D.K.2    Shalloway, D.3
  • 284
    • 0032508532 scopus 로고    scopus 로고
    • Mitotic Raf-1 is stimulated independently of Ras and is active in the cytoplasm
    • Ziogas A, Lorenz IC, Moelling K, et al. Mitotic Raf-1 is stimulated independently of Ras and is active in the cytoplasm. J Biol Chem 1998; 273: 24108-24114.
    • (1998) J Biol Chem , vol.273 , pp. 24108-24114
    • Ziogas, A.1    Lorenz, I.C.2    Moelling, K.3
  • 285
    • 0031985094 scopus 로고    scopus 로고
    • Activated Raf-1 causes growth arrest in human small cell lung cancer cells
    • Ravi RK, Weber E, McMahon M, et al. Activated Raf-1 causes growth arrest in human small cell lung cancer cells. J Clin Invest 1998; 101: 153-159.
    • (1998) J Clin Invest , vol.101 , pp. 153-159
    • Ravi, R.K.1    Weber, E.2    McMahon, M.3
  • 286
    • 0032192153 scopus 로고    scopus 로고
    • Senescence of human fibroblasts induced by oncogenic Raf
    • Zhu J, Woods D, McMahon M, et al. Senescence of human fibroblasts induced by oncogenic Raf. Genes Dev 1998; 12: 2997-3007.
    • (1998) Genes Dev , vol.12 , pp. 2997-3007
    • Zhu, J.1    Woods, D.2    McMahon, M.3
  • 287
    • 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 JH, Munar E, Jameson DR, et al. 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 USA 1999; 96: 11335-11340.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11335-11340
    • Wright, J.H.1    Munar, E.2    Jameson, D.R.3
  • 288
    • 0034644702 scopus 로고    scopus 로고
    • Raf-1/MEK/MAPK pathway is necessary for the G2/M transition induced by nocodazole
    • Hayne C, Tzivion G, Luo Z. Raf-1/MEK/MAPK pathway is necessary for the G2/M transition induced by nocodazole. J Biol Chem 2000; 275: 31876-31882.
    • (2000) J Biol Chem , vol.275 , pp. 31876-31882
    • Hayne, C.1    Tzivion, G.2    Luo, Z.3
  • 289
    • 0033613944 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase kinase 2 activation is essential for progression through the G2/M checkpoint arrest in cells exposed to ionizing radiation
    • Abbott DW, Holt JT. Mitogen-activated protein kinase kinase 2 activation is essential for progression through the G2/M checkpoint arrest in cells exposed to ionizing radiation. J Biol Chem 1999; 274: 2732-2742.
    • (1999) J Biol Chem , vol.274 , pp. 2732-2742
    • Abbott, D.W.1    Holt, J.T.2
  • 290
    • 0032555898 scopus 로고    scopus 로고
    • Active MAP kinase in mitosis: Localization at kinetochores and association with the motor protein CENP-E
    • Zecevic M, Catling AD, Eblen ST, et al. Active MAP kinase in mitosis: localization at kinetochores and association with the motor protein CENP-E. J Cell Biol 1998; 142: 1547-1558.
    • (1998) J Cell Biol , vol.142 , pp. 1547-1558
    • Zecevic, M.1    Catling, A.D.2    Eblen, S.T.3
  • 291
    • 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 PS, Vaisberg E, Hunt A J, et al. 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 1998; 142: 1533-1545.
    • (1998) J Cell Biol , vol.142 , pp. 1533-1545
    • Shapiro, P.S.1    Vaisberg, E.2    Hunt, A.J.3
  • 292
    • 0023678444 scopus 로고
    • Monoclonal antibodies specific for thiophosphorylated proteins recognize Xenopus MPF
    • Cyert MS, Scherson T, Kirschner MW. Monoclonal antibodies specific for thiophosphorylated proteins recognize Xenopus MPF. Dev Biol 1988; 129: 209-216.
    • (1988) Dev Biol , vol.129 , pp. 209-216
    • Cyert, M.S.1    Scherson, T.2    Kirschner, M.W.3
  • 293
    • 0029069368 scopus 로고
    • Microinjection of mitotic cells with the 3F3/2 anti-phosphoepitope antibody delays the onset of anaphase
    • Campbell MS, Gorbsky GJ. Microinjection of mitotic cells with the 3F3/2 anti-phosphoepitope antibody delays the onset of anaphase. J Cell Biol 1995; 129: 1195-1204.
    • (1995) J Cell Biol , vol.129 , pp. 1195-1204
    • Campbell, M.S.1    Gorbsky, G.J.2
  • 294
    • 0032515149 scopus 로고    scopus 로고
    • Casein kinase II catalyzes a mitotic phosphorylation on threonine 1342 of human DNA topoisomerase IIalpha, which is recognized by the 3F3/2 phosphoepitope antibody
    • Daum JR, Gorbsky GJ. Casein kinase II catalyzes a mitotic phosphorylation on threonine 1342 of human DNA topoisomerase IIalpha, which is recognized by the 3F3/2 phosphoepitope antibody. J Biol Chem 1998; 273: 30622-30629.
    • (1998) J Biol Chem , vol.273 , pp. 30622-30629
    • Daum, J.R.1    Gorbsky, G.J.2
  • 295
    • 0034735915 scopus 로고    scopus 로고
    • The 3F3/2 anti-phosphoepitope antibody binds the mitotically phosphorylated anaphase-promoting complex/cyclosome
    • Daum JR, Tugendreich S, Topper LM, et al. The 3F3/2 anti-phosphoepitope antibody binds the mitotically phosphorylated anaphase-promoting complex/cyclosome. Curr Biol 2000; 10: R850-852.
    • (2000) Curr Biol , vol.10
    • Daum, J.R.1    Tugendreich, S.2    Topper, L.M.3
  • 296
    • 0030943027 scopus 로고    scopus 로고
    • Partitioning of the Golgi apparatus during mitosis in living HeLa cells
    • Shima DT, Haldar K, Pepperkok R, et al. Partitioning of the Golgi apparatus during mitosis in living HeLa cells. J Cell Biol 1997; 137: 1211-1228.
    • (1997) J Cell Biol , vol.137 , pp. 1211-1228
    • Shima, D.T.1    Haldar, K.2    Pepperkok, R.3
  • 297
    • 0032559299 scopus 로고    scopus 로고
    • Signaling via mitogen-activated protein kinase kinase (MEK1) is required for Golgi fragmentation during mitosis
    • Acharya U, Mallabiabarrena A, Acharya JK, et al. Signaling via mitogen-activated protein kinase kinase (MEK1) is required for Golgi fragmentation during mitosis. Cell 1998; 92: 183-192.
    • (1998) Cell , vol.92 , pp. 183-192
    • Acharya, U.1    Mallabiabarrena, A.2    Acharya, J.K.3
  • 298
    • 0034678369 scopus 로고    scopus 로고
    • A specific activation of the mitogen-activated protein kinase kinase 1 (MEK1) is required for Golgi fragmentation during mitosis
    • Colanzi A, Deerinck TJ, Ellisman MH, et al. A specific activation of the mitogen-activated protein kinase kinase 1 (MEK1) is required for Golgi fragmentation during mitosis, J Cell Biol 2000; 149: 331-339.
    • (2000) J Cell Biol , vol.149 , pp. 331-339
    • Colanzi, A.1    Deerinck, T.J.2    Ellisman, M.H.3
  • 299
    • 0032544440 scopus 로고    scopus 로고
    • Cdc2 kinase directly phosphorylates the cis-Golgi matrix protein GM130 and is required for Golgi fragmentation in mitosis
    • Lowe M, Rabouille C, Nakamura N, et al. Cdc2 kinase directly phosphorylates the cis-Golgi matrix protein GM130 and is required for Golgi fragmentation in mitosis. Cell 1998; 94: 783-793.
    • (1998) Cell , vol.94 , pp. 783-793
    • Lowe, M.1    Rabouille, C.2    Nakamura, N.3
  • 300
    • 0034678397 scopus 로고    scopus 로고
    • MEK and Cdc2 kinase are sequentially required for Golgi disassembly in MDCK cells by the mitotic Xenopus extracts
    • Kano F, Takenaka K, Yamamoto A, et al. MEK and Cdc2 kinase are sequentially required for Golgi disassembly in MDCK cells by the mitotic Xenopus extracts. J Cell Biol 2000; 149: 357-368.
    • (2000) J Cell Biol , vol.149 , pp. 357-368
    • Kano, F.1    Takenaka, K.2    Yamamoto, A.3
  • 301
    • 0035954437 scopus 로고    scopus 로고
    • Tyrosine-phosphorylated extracellular signal-regulated kinase associates with the Golgi complex during G2/M phase of the cell cycle. Evidence for regulation of golgi structure
    • Cha H and Shapiro P. Tyrosine-phosphorylated extracellular signal-regulated kinase associates with the Golgi complex during G2/M phase of the cell cycle. Evidence for regulation of golgi structure. J Cell Biol 2001; 153: 1355-1368.
    • (2001) J Cell Biol , vol.153 , pp. 1355-1368
    • Cha, H.1    Shapiro, P.2
  • 302
    • 0030060174 scopus 로고    scopus 로고
    • Modulation of microtubule dynamics during the cell cycle
    • McNally FJ. Modulation of microtubule dynamics during the cell cycle. Curr Opin Cell Biol 1996; 8: 23-29.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 23-29
    • McNally, F.J.1
  • 303
    • 0028799999 scopus 로고
    • Cell cycle-dependent phosphorylation and microtubule binding of tau protein stably transfected into Chinese hamster ovary cells
    • Preuss U, Doring F, Illenberger S, et al. Cell cycle-dependent phosphorylation and microtubule binding of tau protein stably transfected into Chinese hamster ovary cells. Mol Biol Cell 1995; 6: 1397-1410.
    • (1995) Mol Biol Cell , vol.6 , pp. 1397-1410
    • Preuss, U.1    Doring, F.2    Illenberger, S.3
  • 304
    • 0031928259 scopus 로고    scopus 로고
    • Mitotic phosphorylation of tau protein in neuronal cell lines resembles phosphorylation in Alzheimer's disease
    • Preuss U, Mandelkow EM. Mitotic phosphorylation of tau protein in neuronal cell lines resembles phosphorylation in Alzheimer's disease. Eur J Cell Biol 1998; 76: 176-184
    • (1998) Eur J Cell Biol , vol.76 , pp. 176-184
    • Preuss, U.1    Mandelkow, E.M.2
  • 305
    • 17044461433 scopus 로고    scopus 로고
    • The endogenous and cell cycle-dependent phosphorylation of tau protein in living cells: Implications for Alzheimer's disease
    • Illenberger S, Zheng-Fischhofer Q, Preuss U, et al. The endogenous and cell cycle-dependent phosphorylation of tau protein in living cells: implications for Alzheimer's disease. Mol Biol Cell 1998; 9: 1495-1512.
    • (1998) Mol Biol Cell , vol.9 , pp. 1495-1512
    • Illenberger, S.1    Zheng-Fischhofer, Q.2    Preuss, U.3
  • 306
    • 0030048731 scopus 로고    scopus 로고
    • Identification of a protein that interacts with tubulin dimers and increases the catastrophe rate of microtubules
    • Belmont LD, Mitchison TJ. Identification of a protein that interacts with tubulin dimers and increases the catastrophe rate of microtubules. Cell 1996; 84: 623-631.
    • (1996) Cell , vol.84 , pp. 623-631
    • Belmont, L.D.1    Mitchison, T.J.2
  • 307
    • 0031745447 scopus 로고    scopus 로고
    • The stathmin phosphoprotein family: Intracellular localization and effects on the microtubule network
    • Gavet O, Ozon S, Manceau V, et al. The stathmin phosphoprotein family: intracellular localization and effects on the microtubule network. J Cell Sci 1998; 111: 3333-3346.
    • (1998) J Cell Sci , vol.111 , pp. 3333-3346
    • Gavet, O.1    Ozon, S.2    Manceau, V.3
  • 308
    • 0030748898 scopus 로고    scopus 로고
    • Mitotic chromatin regulates phosphorylation of Stathmin/Op18
    • Andersen SS, Ashford AJ, Tournebize R, et al. Mitotic chromatin regulates phosphorylation of Stathmin/Op18. Nature 1997; 389: 640-4543.
    • (1997) Nature , vol.389 , pp. 640-4543
    • Andersen, S.S.1    Ashford, A.J.2    Tournebize, R.3
  • 309
    • 0035155824 scopus 로고    scopus 로고
    • Stathmin/Op18 phosphorylation is regulated by microtubule assembly
    • Kuntziger T, Gavet O, Manceau V, et al. Stathmin/Op18 phosphorylation is regulated by microtubule assembly. Mol Biol Cell 2001; 12: 437-448.
    • (2001) Mol Biol Cell , vol.12 , pp. 437-448
    • Kuntziger, T.1    Gavet, O.2    Manceau, V.3
  • 310
    • 0035057461 scopus 로고    scopus 로고
    • Effects of stathmin inhibition on the mitotic spindle
    • Iancu C, Mistry SJ, Arkin S, et al. Effects of stathmin inhibition on the mitotic spindle. J Cell Sci 2001; 114: 909-916.
    • (2001) J Cell Sci , vol.114 , pp. 909-916
    • Iancu, C.1    Mistry, S.J.2    Arkin, S.3
  • 311
    • 0027751577 scopus 로고
    • The phosphorylation of stathmin by MAP kinase
    • Leighton IA, Curmi P, Campbell DG, et al. The phosphorylation of stathmin by MAP kinase. Mol Cell Biochem 1993; 127-128: 151-156.
    • (1993) Mol Cell Biochem , vol.127 , pp. 151-156
    • Leighton, I.A.1    Curmi, P.2    Campbell, D.G.3
  • 312
    • 0031779645 scopus 로고    scopus 로고
    • Phosphorylation of stathmin modulates its function as a microtubule depolymerizing factor
    • Moreno FJ, Avila J. Phosphorylation of stathmin modulates its function as a microtubule depolymerizing factor. Mol Cell Biochem 1998; 183: 201-209.
    • (1998) Mol Cell Biochem , vol.183 , pp. 201-209
    • Moreno, F.J.1    Avila, J.2
  • 313
    • 0034647733 scopus 로고    scopus 로고
    • ERKs and p38 Kinases Mediate UVB-induced Phosphorylation of Histone H3 at Serine 10
    • Zhong SP, Ma WY, Dong Z. ERKs and p38 Kinases Mediate UVB-induced Phosphorylation of Histone H3 at Serine 10. J Biol Chem 2000.
    • (2000) J Biol Chem
    • Zhong, S.P.1    Ma, W.Y.2    Dong, Z.3
  • 314
    • 0032560517 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 at serine 10 is correlated with chromosome condensation during mitosis and meiosis in Tetrahymena
    • Wei Y, Mizzen CA, Cook RG, et al. Phosphorylation of histone H3 at serine 10 is correlated with chromosome condensation during mitosis and meiosis in Tetrahymena. Proc Natl Acad Sci USA 1998; 95: 7480-7484.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7480-7484
    • Wei, Y.1    Mizzen, C.A.2    Cook, R.G.3
  • 315
    • 0033515426 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 is required for proper chromosome condensation and segregation
    • Wei Y, Yu L, Bowen J, et al. Phosphorylation of histone H3 is required for proper chromosome condensation and segregation. Cell 1999; 97: 99-109.
    • (1999) Cell , vol.97 , pp. 99-109
    • Wei, Y.1    Yu, L.2    Bowen, J.3
  • 316
    • 0032530154 scopus 로고    scopus 로고
    • Mitotic inactivation of a human SWI/SNF chromatin remodeling complex
    • Sif S, Stukenberg PT, Kirschner MW, et al. Mitotic inactivation of a human SWI/SNF chromatin remodeling complex. Genes Dev 1998; 12: 2842-2851.
    • (1998) Genes Dev , vol.12 , pp. 2842-2851
    • Sif, S.1    Stukenberg, P.T.2    Kirschner, M.W.3
  • 317
    • 0032562716 scopus 로고    scopus 로고
    • Activation of the protein kinase p38 in the spindle assembly checkpoint and mitotic arrest
    • Takenaka K, Moriguchi T, Nishida E. Activation of the protein kinase p38 in the spindle assembly checkpoint and mitotic arrest. Science 1998; 280: 599-602.
    • (1998) Science , vol.280 , pp. 599-602
    • Takenaka, K.1    Moriguchi, T.2    Nishida, E.3
  • 318
    • 0034604540 scopus 로고    scopus 로고
    • Selective activation of p38 MAPK cascade and mitotic arrest caused by low level oxidative stress
    • Kurata S. Selective activation of p38 MAPK cascade and mitotic arrest caused by low level oxidative stress. J Biol Chem 2000; 275: 23413-23416.
    • (2000) J Biol Chem , vol.275 , pp. 23413-23416
    • Kurata, S.1
  • 319
    • 0035799557 scopus 로고    scopus 로고
    • Initiation of a G2/M checkpoint after ultraviolet radiation requires p38 kinase
    • Bulavin DV, Higashimoto Y, Popoff IJ, et al. Initiation of a G2/M checkpoint after ultraviolet radiation requires p38 kinase. Nature 2001; 411: 102-107.
    • (2001) Nature , vol.411 , pp. 102-107
    • Bulavin, D.V.1    Higashimoto, Y.2    Popoff, I.J.3
  • 320
    • 15644381250 scopus 로고    scopus 로고
    • Bcl-2 undergoes phosphorylation by c-Jun N-terminal kinase/stress- activated protein kinases in the presence of the constitutively active GTP-binding protein Racl
    • Maundrell K, Antonsson B, Magnenat E, et al. Bcl-2 undergoes phosphorylation by c-Jun N-terminal kinase/stress- activated protein kinases in the presence of the constitutively active GTP-binding protein Racl. J Biol Chem 1997; 272: 25238-25242.
    • (1997) J Biol Chem , vol.272 , pp. 25238-25242
    • Maundrell, K.1    Antonsson, B.2    Magnenat, E.3
  • 321
    • 0033499801 scopus 로고    scopus 로고
    • BCL-2 is phosphorylated and inactivated by an ASK1/Jun N-terminal protein kinase pathway normally activated at G(2)/M
    • Yamamoto K, Ichijo H, Korsmeyer SJ. BCL-2 is phosphorylated and inactivated by an ASK1/Jun N-terminal protein kinase pathway normally activated at G(2)/M. Mol Cell Biol 1999; 19: 8469-8478.
    • (1999) Mol Cell Biol , vol.19 , pp. 8469-8478
    • Yamamoto, K.1    Ichijo, H.2    Korsmeyer, S.J.3
  • 322
    • 0032563202 scopus 로고    scopus 로고
    • Phosphorylation of Bcl-2 is a marker of M phase events and not a determinant of apoptosis
    • Ling YH, Tornos C, Perez-Soler R. Phosphorylation of Bcl-2 is a marker of M phase events and not a determinant of apoptosis. J Biol Chem 1998; 273: 18984-18991
    • (1998) J Biol Chem , vol.273 , pp. 18984-18991
    • Ling, Y.H.1    Tornos, C.2    Perez-Soler, R.3
  • 323
    • 0033617405 scopus 로고    scopus 로고
    • MEK kinase 1 (MEKK1) transduces c-Jun NH2-terminal kinase activation in response to changes in the microtubule cytoskeleton
    • Yujiri T, Fanger GR, Garrington TP, et al. MEK kinase 1 (MEKK1) transduces c-Jun NH2-terminal kinase activation in response to changes in the microtubule cytoskeleton. J Biol Chem 1999; 274: 12605-12610.
    • (1999) J Biol Chem , vol.274 , pp. 12605-12610
    • Yujiri, T.1    Fanger, G.R.2    Garrington, T.P.3
  • 324
    • 0035902166 scopus 로고    scopus 로고
    • Cancer genetics
    • Ponder BA. Cancer genetics. Nature 2001; 411: 336-341.
    • (2001) Nature , vol.411 , pp. 336-341
    • Ponder, B.A.1
  • 325
    • 0033551070 scopus 로고    scopus 로고
    • New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway
    • Cantley LC, Neel BG. New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway. Proc Natl Acad Sci USA 1999; 96: 4240-4245.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 4240-4245
    • Cantley, L.C.1    Neel, B.G.2
  • 326
    • 0034598796 scopus 로고    scopus 로고
    • Inhibition of H-Ras transformation by the PTEN/MMAC1/TEP1 tumor suppressor gene
    • Tolkacheva T, Chan AM. Inhibition of H-Ras transformation by the PTEN/MMAC1/TEP1 tumor suppressor gene. Oncogene 2000; 19: 680-689.
    • (2000) Oncogene , vol.19 , pp. 680-689
    • Tolkacheva, T.1    Chan, A.M.2
  • 327
    • 0032530850 scopus 로고    scopus 로고
    • Repression of yeast Ste12 transcription factor by direct binding of unphosphorylated Kss1 MAPK and its regulation by the Ste7 MEK
    • Bardwell L, Cook JG, Voora D, et al. Repression of yeast Ste12 transcription factor by direct binding of unphosphorylated Kss1 MAPK and its regulation by the Ste7 MEK. Genes Dev 1998; 12: 2887-2898.
    • (1998) Genes Dev , vol.12 , pp. 2887-2898
    • Bardwell, L.1    Cook, J.G.2    Voora, D.3
  • 328
    • 0032961902 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase activates topoisomerase IIalpha through a mechanism independent of phosphorylation
    • Shapiro PS, Whalen AM, Tolwinski NS, et al. Extracellular signal-regulated kinase activates topoisomerase IIalpha through a mechanism independent of phosphorylation. Mol Cell Biol 1999; 19: 3551-3560.
    • (1999) Mol Cell Biol , vol.19 , pp. 3551-3560
    • Shapiro, P.S.1    Whalen, A.M.2    Tolwinski, N.S.3
  • 329
    • 0032932912 scopus 로고    scopus 로고
    • MAP kinases, phosphatidylinositol 3-kinase, and p70 S6 kinase mediate the mitogenic response of human endothelial cells to vascular endothelial growth factor
    • Yu Y, Sato JD. MAP kinases, phosphatidylinositol 3-kinase, and p70 S6 kinase mediate the mitogenic response of human endothelial cells to vascular endothelial growth factor. J Cell Physiol 1999; 178: 235-246.
    • (1999) J Cell Physiol , vol.178 , pp. 235-246
    • Yu, Y.1    Sato, J.D.2
  • 330
    • 0034699326 scopus 로고    scopus 로고
    • Hypoxia-induced VEGF enhances tumor survivability via suppression of selum deprivation-induced apoptosis
    • Baek JH, Jang JE, Kang CM, et al. Hypoxia-induced VEGF enhances tumor survivability via suppression of selum deprivation-induced apoptosis. Oncogene 2000; 19: 4621-4631.
    • (2000) Oncogene , vol.19 , pp. 4621-4631
    • Baek, J.H.1    Jang, J.E.2    Kang, C.M.3
  • 331
    • 0030713446 scopus 로고    scopus 로고
    • Activator-protein-1 binding potentiates the hypoxia-inducible factor-1-mediated hypoxia-induced transcriptional activation of vascular- endothelial growth factor expression in C6 glioma cells
    • Damert A, Ikeda E, Risau W. Activator-protein-1 binding potentiates the hypoxia-inducible factor-1-mediated hypoxia-induced transcriptional activation of vascular- endothelial growth factor expression in C6 glioma cells. Biochem J 1997; 327: 419-423.
    • (1997) Biochem J , vol.327 , pp. 419-423
    • Damert, A.1    Ikeda, E.2    Risau, W.3
  • 332
    • 0033215389 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase activation is required for up- regulation of vascular endothelial growth factor by serum starvation in human colon carcinoma cells
    • Jung YD, Nakano K, Liu W, et al. Extracellular signal-regulated kinase activation is required for up- regulation of vascular endothelial growth factor by serum starvation in human colon carcinoma cells. Cancer Res 1999; 59: 4804-4807.
    • (1999) Cancer Res , vol.59 , pp. 4804-4807
    • Jung, Y.D.1    Nakano, K.2    Liu, W.3
  • 333
    • 0034668187 scopus 로고    scopus 로고
    • Signaling angiogenesis via p42/p44 MAP kinase and hypoxia
    • Berra E, Milanini J, Richard DE, et al. Signaling angiogenesis via p42/p44 MAP kinase and hypoxia. Biochem Pharmacol 2000; 60: 1171-1178.
    • (2000) Biochem Pharmacol , vol.60 , pp. 1171-1178
    • Berra, E.1    Milanini, J.2    Richard, D.E.3
  • 334
    • 0034488898 scopus 로고    scopus 로고
    • The angiogenesis inhibitor SU5416 has long-lasting effects on vascular endothelial growth factor receptor phosphorylation and function
    • Mendel DB, Schreck RE, West DC, et al. The angiogenesis inhibitor SU5416 has long-lasting effects on vascular endothelial growth factor receptor phosphorylation and function. Clin Cancer Res 2000; 4848-4858.
    • (2000) Clin Cancer Res , pp. 4848-4858
    • Mendel, D.B.1    Schreck, R.E.2    West, D.C.3
  • 335
    • 0033994955 scopus 로고    scopus 로고
    • Clinical strategy for the development of angiogenesis inhibitors
    • Carter SK. Clinical strategy for the development of angiogenesis inhibitors. Oncologist 2000; 51-54.
    • (2000) Oncologist , pp. 51-54
    • Carter, S.K.1
  • 336
    • 0034652716 scopus 로고    scopus 로고
    • ZD4190: An orally active inhibitor of vascular endothelial growth factor signaling with broad-spectrum antitumor efficacy
    • Wedge SR, Ogilvie DJ, Dukes M, et al. ZD4190: an orally active inhibitor of vascular endothelial growth factor signaling with broad-spectium antitumor efficacy. Cancer Res 2000; 60: 970-975.
    • (2000) Cancer Res , vol.60 , pp. 970-975
    • Wedge, S.R.1    Ogilvie, D.J.2    Dukes, M.3
  • 337
    • 0034471773 scopus 로고    scopus 로고
    • Inhibition of VEGF signal transduction. Identification of ZD4190
    • Wedge SR and Ogilvie DJ. Inhibition of VEGF signal transduction. Identification of ZD4190. Adv Exp Med Biol 2000; 476: 307-310.
    • (2000) Adv Exp Med Biol , vol.476 , pp. 307-310
    • Wedge, S.R.1    Ogilvie, D.J.2
  • 339
    • 0032127350 scopus 로고    scopus 로고
    • Recombinant humanized anti-HER2 antibody (Herceptin) enhances the antitumor activity of paclitaxel and doxorubicin against HER2/neu overcxpressing human breast cancer xenografts
    • Baselga J, Norton L, Albanell J, et al. Recombinant humanized anti-HER2 antibody (Herceptin) enhances the antitumor activity of paclitaxel and doxorubicin against HER2/neu overcxpressing human breast cancer xenografts. Cancer Res 1998; 58: 2825-2831.
    • (1998) Cancer Res , vol.58 , pp. 2825-2831
    • Baselga, J.1    Norton, L.2    Albanell, J.3
  • 340
    • 0035257549 scopus 로고    scopus 로고
    • Rationale for trastuzumab (Herceptin) in adjuvant breast cartcer trials
    • Slamon D, Pegram M. Rationale for trastuzumab (Herceptin) in adjuvant breast cartcer trials. Semin Oncol 2001; 28: 13-19.
    • (2001) Semin Oncol , vol.28 , pp. 13-19
    • Slamon, D.1    Pegram, M.2
  • 341
    • 0034722889 scopus 로고    scopus 로고
    • The EGF receptor family as targets for cancer therapy
    • Mendelsohn J, Baselga J. The EGF receptor family as targets for cancer therapy. Oncogene 2000; 19: 6550-6565.
    • (2000) Oncogene , vol.19 , pp. 6550-6565
    • Mendelsohn, J.1    Baselga, J.2
  • 342
    • 19244366949 scopus 로고    scopus 로고
    • Phase I studies of anti-epidermal growth factor receptor chimeric antibody C225 alone and in combination with cisplatin
    • Baselga J, Pfister D, Cooper MR, et al. Phase I studies of anti-epidermal growth factor receptor chimeric antibody C225 alone and in combination with cisplatin. J Clin Oncol 2000; 18: 904-914.
    • (2000) J Clin Oncol , vol.18 , pp. 904-914
    • Baselga, J.1    Pfister, D.2    Cooper, M.R.3
  • 343
    • 0028893444 scopus 로고
    • Single-chain antibody-mediated intracellular retention of ErbB-2 impairs Neu differentiation factor and epidermal growth factor signaling
    • Graus-Porta D, Beerli RR, Hynes NE. Single-chain antibody-mediated intracellular retention of ErbB-2 impairs Neu differentiation factor and epidermal growth factor signaling. Mol Cell Biol 1995; 15: 1182-1191.
    • (1995) Mol Cell Biol , vol.15 , pp. 1182-1191
    • Graus-Porta, D.1    Beerli, R.R.2    Hynes, N.E.3
  • 344
    • 0033993508 scopus 로고    scopus 로고
    • Adenovirus-mediated ribozyme targeting of HER-2/neu inhibits in vivo growth of breast cancer cells
    • Suzuki T, Ohkawa T, et al. Adenovirus-mediated ribozyme targeting of HER-2/neu inhibits in vivo growth of breast cancer cells. Gene Ther 2000; 241-248.
    • (2000) Gene Ther , pp. 241-248
    • Suzuki, T.1    Ohkawa, T.2
  • 345
    • 0035290919 scopus 로고    scopus 로고
    • Angiozyme: A novel angiogenesis inhibitor
    • Weng DE, Usman N. Angiozyme: a novel angiogenesis inhibitor. Curr Oncol Rep 2001; 141-146.
    • (2001) Curr Oncol Rep , pp. 141-146
    • Weng, D.E.1    Usman, N.2
  • 346
    • 0032008099 scopus 로고    scopus 로고
    • Novel therapeutic strategies to selectively kill cancer cells
    • Panchal RG. Novel therapeutic strategies to selectively kill cancer cells. Biochem Pharmacol 1998; 55: 247-252.
    • (1998) Biochem Pharmacol , vol.55 , pp. 247-252
    • Panchal, R.G.1
  • 347
    • 0035874504 scopus 로고    scopus 로고
    • Targeting of the CD33-calicheamicin immunoconjugate Mylotarg (CMA-676) in acute myeloid leukemia: In vivo and in vitro saturation and internalization by leukemic and normal myeloid cells
    • van Der Velden VH, te Marvelde JG, Hoogeveen PG, et al. Targeting of the CD33-calicheamicin immunoconjugate Mylotarg (CMA-676) in acute myeloid leukemia: in vivo and in vitro saturation and internalization by leukemic and normal myeloid cells. Blood 2001; 97: 3197-3204.
    • (2001) Blood , vol.97 , pp. 3197-3204
    • Van Der Velden, V.H.1    Te Marvelde, J.G.2    Hoogeveen, P.G.3
  • 348
    • 0030926774 scopus 로고    scopus 로고
    • Focal adhesion kinase overexpression enhances ras-dependent integrin signaling to ERK2/mitogen-activated protein kinase through interactions with and activation of c-Src
    • Schlaepfer DD, Hunter T. Focal adhesion kinase overexpression enhances ras-dependent integrin signaling to ERK2/mitogen-activated protein kinase through interactions with and activation of c-Src. J Biol Chem 1997; 272: 13189-13195.
    • (1997) J Biol Chem , vol.272 , pp. 13189-13195
    • Schlaepfer, D.D.1    Hunter, T.2
  • 349
    • 0032541613 scopus 로고    scopus 로고
    • Rho family proteins and Ras transformation: The RHOad less traveled gets congested
    • Zohn IM, Campbell SL, Khosravi-Far R, et al. Rho family proteins and Ras transformation: the RHOad less traveled gets congested. Oncogene 1998; 17: 1415-1438.
    • (1998) Oncogene , vol.17 , pp. 1415-1438
    • Zohn, I.M.1    Campbell, S.L.2    Khosravi-Far, R.3
  • 350
    • 0343618673 scopus 로고    scopus 로고
    • Checkpoints controlling mitosis
    • Clarke D J, Gimenez-Abian JF. Checkpoints controlling mitosis. Bioessays 2000; 22: 351-363.
    • (2000) Bioessays , vol.22 , pp. 351-363
    • Clarke, D.J.1    Gimenez-Abian, J.F.2
  • 351
    • 0030023116 scopus 로고    scopus 로고
    • Src and the control of cell division
    • Taylor SJ, Shalloway D. Src and the control of cell division. Bioessays 1996; 18: 9-11
    • (1996) Bioessays , vol.18 , pp. 9-11
    • Taylor, S.J.1    Shalloway, D.2
  • 352
    • 0034896362 scopus 로고    scopus 로고
    • Inhibition of growth factor production and angiogenesis in human cancer cells by ZD1839 (Iressa), a selective epidermal growth factor receptor tyrosine kinase inhibitor
    • Ciardiello F, Caputo R, Bianco R, et al. Inhibition of growth factor production and angiogenesis in human cancer cells by ZD1839 (Iressa), a selective epidermal growth factor receptor tyrosine kinase inhibitor. Clin Cancer Res 2001; 1459-1465.
    • (2001) Clin Cancer Res , pp. 1459-1465
    • Ciardiello, F.1    Caputo, R.2    Bianco, R.3
  • 353
    • 0035125614 scopus 로고    scopus 로고
    • Clinical trials of Herceptin(trastuzumab)
    • Baselga J. Clinical trials of Herceptin(trastuzumab). Eur J Cancer 2001; 37 Suppl S18-24.
    • (2001) Eur J Cancer , vol.37 , Issue.SUPPL.
    • Baselga, J.1


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