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Volumn 411, Issue 6835, 2001, Pages 355-365

Oncogenic kinase signalling

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME INHIBITION; ENZYME KINETICS; ENZYMES; LIPIDS;

EID: 0035902180     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/35077225     Document Type: Review
Times cited : (3278)

References (93)
  • 1
    • 0034614490 scopus 로고    scopus 로고
    • Signaling - 2000 and beyond
    • Hunter, T. Signaling - 2000 and beyond. Cell 100, 113-127 (2000).
    • (2000) Cell , vol.100 , pp. 113-127
    • Hunter, T.1
  • 2
    • 0034193568 scopus 로고    scopus 로고
    • Protein-protein interactions define specificity in signal transduction
    • Pawson, T. & Nash, P. Protein-protein interactions define specificity in signal transduction. Genes Dev. 14, 1027-1047 (2000).
    • (2000) Genes Dev. , vol.14 , pp. 1027-1047
    • Pawson, T.1    Nash, P.2
  • 3
    • 0032877668 scopus 로고    scopus 로고
    • Dysregulation of apoptosis in cancer
    • Reed, J. C. Dysregulation of apoptosis in cancer. J. Clin. Oncol. 17, 2941-2953 (1999).
    • (1999) J. Clin. Oncol. , vol.17 , pp. 2941-2953
    • Reed, J.C.1
  • 4
    • 0032577051 scopus 로고    scopus 로고
    • The Croonian Lecture 1997. The phosphorylation of proteins on tyrosine: Its role in cell growth and disease
    • Hunter, T. The Croonian Lecture 1997. The phosphorylation of proteins on tyrosine: its role in cell growth and disease. Phil. Trans. R. Soc. Lond. B 353, 583-605 (1998).
    • (1998) Phil. Trans. R. Soc. Lond. B , vol.353 , pp. 583-605
    • Hunter, T.1
  • 5
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan, D. & Weinberg, R. A. The hallmarks of cancer. Cell 100, 57-70 (2000).
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 6
    • 0033598830 scopus 로고    scopus 로고
    • The protein kinases of Caenorhabditis elegans: A model for signal transduction in multicellular organisms
    • Plowman, G. D., Sudarsanam, S., Bingham, J., Whyte, D. & Hunter, T. The protein kinases of Caenorhabditis elegans: a model for signal transduction in multicellular organisms. Proc. Natl Acad. Sci. USA 96, 13603-13610 (1999)
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 13603-13610
    • Plowman, G.D.1    Sudarsanam, S.2    Bingham, J.3    Whyte, D.4    Hunter, T.5
  • 7
    • 0034693799 scopus 로고    scopus 로고
    • The protein tyrosine kinase family of the human genome
    • Robinson, D. R., Wu, Y. M. & Lin, S. E. The protein tyrosine kinase family of the human genome Oncogene 19, 5548-5557 (2000).
    • (2000) Oncogene , vol.19 , pp. 5548-5557
    • Robinson, D.R.1    Wu, Y.M.2    Lin, S.E.3
  • 8
    • 0035865465 scopus 로고    scopus 로고
    • Cancer and genomics
    • Futreal, P. A. et al. Cancer and genomics. Nature 409, 850-852 (2001).
    • (2001) Nature , vol.409 , pp. 850-852
    • Futreal, P.A.1
  • 9
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger, J. Cell signaling by receptor tyrosine kinases. Cell 103, 211-225 (2000).
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 11
    • 0028838012 scopus 로고
    • Dimerization of cell surface receptors in signal transduction
    • Heldin, C. H. Dimerization of cell surface receptors in signal transduction. Cell 80, 213-223 (1995).
    • (1995) Cell , vol.80 , pp. 213-223
    • Heldin, C.H.1
  • 12
    • 0033786922 scopus 로고    scopus 로고
    • Protein tyrosine kinase structure and function
    • Hubbard, S. R. & Till, J. H. Protein tyrosine kinase structure and function. Annu. Rev. Biochem. 69, 373-398 (2000).
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 373-398
    • Hubbard, S.R.1    Till, J.H.2
  • 13
    • 0032524350 scopus 로고    scopus 로고
    • Autoregulatory mechanisms in protein-tyrosine kinases
    • Hubbard, S. R., Mohammadi, M. & Schlessinger, J. Autoregulatory mechanisms in protein-tyrosine kinases. J. Biol. Chem. 273, 11987-11990 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 11987-11990
    • Hubbard, S.R.1    Mohammadi, M.2    Schlessinger, J.3
  • 14
    • 0033615077 scopus 로고    scopus 로고
    • Receptor signaling: When dimerization is not enough
    • Jiang, G. & Hunter, T. Receptor signaling: when dimerization is not enough. Curr. Biol. 9, R568-R571 (1999).
    • (1999) Curr. Biol. , vol.9
    • Jiang, G.1    Hunter, T.2
  • 15
    • 0034435424 scopus 로고    scopus 로고
    • Structure of the Tic2 RTK domain. Self-inhibition by the nucleotide binding loop, activation loop, and C-terminal tail
    • Shewchuk, L. M. et al. Structure of the Tic2 RTK domain. Self-inhibition by the nucleotide binding loop, activation loop, and C-terminal tail. Structure Fold. Des. 8, 1105-1113 (2000).
    • (2000) Structure Fold. Des. , vol.8 , pp. 1105-1113
    • Shewchuk, L.M.1
  • 16
    • 0034086061 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine residues in the kinase domain and juxtamembrane region regulates the biological and catalytic activities of Eph receptors
    • Binns, K. L., Taylor, P. P., Sicheri, F., Pawson, T. & Holland, S. J. Phosphorylation of tyrosine residues in the kinase domain and juxtamembrane region regulates the biological and catalytic activities of Eph receptors. Mol. Cell. Biol. 20, 4791-4805 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 4791-4805
    • Binns, K.L.1    Taylor, P.P.2    Sicheri, F.3    Pawson, T.4    Holland, S.J.5
  • 17
    • 0032401747 scopus 로고    scopus 로고
    • A single amino acid substitution in a WW-like domain of diverse members of the PDGF receptor subfamily of tyrosine kinases causes constitutive receptor activation
    • Irusta, P. M. & DiMaio, D. A single amino acid substitution in a WW-like domain of diverse members of the PDGF receptor subfamily of tyrosine kinases causes constitutive receptor activation. EMBO J. 17, 6912-6923 (1998).
    • (1998) EMBO J. , vol.17 , pp. 6912-6923
    • Irusta, P.M.1    DiMaio, D.2
  • 18
    • 15644363454 scopus 로고    scopus 로고
    • Gain-of-function mutations of c-kit in human gastrointestinal stromal tumors
    • Hirota, S. et al. Gain-of-function mutations of c-kit in human gastrointestinal stromal tumors. Science 279, 577-580 (1998).
    • (1998) Science , vol.279 , pp. 577-580
    • Hirota, S.1
  • 19
    • 0035168677 scopus 로고    scopus 로고
    • Prevalence and prognostic significance of Flt3 internal tandem duplication in pediatric acute myeloid leukemia
    • Meshinchi, S. et al. Prevalence and prognostic significance of Flt3 internal tandem duplication in pediatric acute myeloid leukemia. Blood 97, 89-94 (2001).
    • (2001) Blood , vol.97 , pp. 89-94
    • Meshinchi, S.1
  • 20
    • 0034638925 scopus 로고    scopus 로고
    • Molecular mechanisms underlying ErbB2/HFR2 action in breast cancer
    • Harari, D. & Yarden, Y. Molecular mechanisms underlying ErbB2/HFR2 action in breast cancer. Oncogene 19, 6102-6114 (2000).
    • (2000) Oncogene , vol.19 , pp. 6102-6114
    • Harari, D.1    Yarden, Y.2
  • 21
    • 0034693757 scopus 로고    scopus 로고
    • The RET proto-oncogene in human cancers
    • Jhiang, S. M. The RET proto-oncogene in human cancers. Oncogene 19, 5590-5597 (2000).
    • (2000) Oncogene , vol.19 , pp. 5590-5597
    • Jhiang, S.M.1
  • 22
    • 0028914683 scopus 로고
    • Activation of RET as a dominant transforming gene by germline mutations of MEN2A and MEN2B
    • Santoro, M. et al. Activation of RET as a dominant transforming gene by germline mutations of MEN2A and MEN2B. Science 267, 381-383 (1995).
    • (1995) Science , vol.267 , pp. 381-383
    • Santoro, M.1
  • 23
    • 0028938721 scopus 로고
    • Catalytics specificity of protein-tyrosine kinases is critical for selective signalling
    • Zhou, S. et al. Catalytics specificity of protein-tyrosine kinases is critical for selective signalling. Nature 373, 536-539 (1995).
    • (1995) Nature , vol.373 , pp. 536-539
    • Zhou, S.1
  • 24
    • 0030663857 scopus 로고    scopus 로고
    • The multiple endocrine neoplasia type 2B point mutation switches the specificity of the Ret tyrosine kinase towards cellular substrates that are susceptible to interact with Crk and Nck
    • Bocciardi, R. et al. The multiple endocrine neoplasia type 2B point mutation switches the specificity of the Ret tyrosine kinase towards cellular substrates that are susceptible to interact with Crk and Nck. Oncogene 15, 2257-2265 (1997).
    • (1997) Oncogene , vol.15 , pp. 2257-2265
    • Bocciardi, R.1
  • 25
    • 0033584474 scopus 로고    scopus 로고
    • Enhanced phosphatidylinositol 3-kinase activity and high phosphorylation state of its downstream signalling molecules mediated by ret with the MEN 2B mutation
    • Murakami, H. et al. Enhanced phosphatidylinositol 3-kinase activity and high phosphorylation state of its downstream signalling molecules mediated by ret with the MEN 2B mutation. Biochem. Biophys. Res. Commun. 262, 68-75 (1999).
    • (1999) Biochem. Biophys. Res. Commun. , vol.262 , pp. 68-75
    • Murakami, H.1
  • 26
    • 0034651526 scopus 로고    scopus 로고
    • C -cell hyperplasia, pheochromocytoma and sympathoadrenal malformation in a mouse model of multiple endocrine neoplasia type 2B
    • Smith-Hicks, C. L., Sizer, K. C., Powers, J. F., Tischler, A. S. & Costantini, F. C -cell hyperplasia, pheochromocytoma and sympathoadrenal malformation in a mouse model of multiple endocrine neoplasia type 2B. EMBO J. 19, 612-622 (2000).
    • (2000) EMBO J. , vol.19 , pp. 612-622
    • Smith-Hicks, C.L.1    Sizer, K.C.2    Powers, J.F.3    Tischler, A.S.4    Costantini, F.5
  • 27
    • 0032241463 scopus 로고    scopus 로고
    • Signal transduction by the receptor tyrosine kinase
    • van Weering, D. H. & Bos, J. L. Signal transduction by the receptor tyrosine kinase Ret. Recent Results Cancer Res. 154, 271-281 (1998).
    • (1998) Ret. Recent Results Cancer Res. , vol.154 , pp. 271-281
    • Van Weering, D.H.1    Bos, J.L.2
  • 28
    • 0032857449 scopus 로고    scopus 로고
    • The biology of stem cell factor and its receptor C-kit
    • Ashman, L. K. The biology of stem cell factor and its receptor C-kit. Int. J. Biochem. Cell Biol. 31, 1037-1051 (1999).
    • (1999) Int. J. Biochem. Cell Biol. , vol.31 , pp. 1037-1051
    • Ashman, L.K.1
  • 29
    • 0026266094 scopus 로고
    • The kit ligand encoded at the murine Steel locus: A pleiotropic growth and differentiation factor
    • Besmer, P. The kit ligand encoded at the murine Steel locus: a pleiotropic growth and differentiation factor. Curr. Opin. Cell Biol. 3, 939-946 (1991).
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 939-946
    • Besmer, P.1
  • 31
    • 0031924794 scopus 로고    scopus 로고
    • SHP-1 binds and negatively modulates the c-Kit receptor by interaction with tyrosine 569 in the c-Kit juxtamembrane domain
    • Kozlowski, M. et al. SHP-1 binds and negatively modulates the c-Kit receptor by interaction with tyrosine 569 in the c-Kit juxtamembrane domain. Mol. Cell. Biol. 18, 2089-2099 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2089-2099
    • Kozlowski, M.1
  • 32
    • 0033619142 scopus 로고    scopus 로고
    • Phosphorylation of Shc by Src family kinases is necessary for stem cell factor receptor/c-kit mediated activation of the Ras/MAP kinase pathway and c-fos induction
    • Lennartsson, J. et al. Phosphorylation of Shc by Src family kinases is necessary for stem cell factor receptor/c-kit mediated activation of the Ras/MAP kinase pathway and c-fos induction. Oncogene 18, 5546-5553 (1999).
    • (1999) Oncogene , vol.18 , pp. 5546-5553
    • Lennartsson, J.1
  • 33
    • 0033199890 scopus 로고    scopus 로고
    • Effect of c-kit mutation on prognosis of gastrointestinal stromal tumors
    • Taniguchi, M. et al. Effect of c-kit mutation on prognosis of gastrointestinal stromal tumors. Cancer Res. 59, 4297-4300 (1999).
    • (1999) Cancer Res. , vol.59 , pp. 4297-4300
    • Taniguchi, M.1
  • 34
    • 17344381429 scopus 로고    scopus 로고
    • Germline and somatic mutations in the tyrosine kinase domain of the MET proto-oncogenic in papillary renal carcinomas
    • Schmidt, L. et al. Germline and somatic mutations in the tyrosine kinase domain of the MET proto-oncogenic in papillary renal carcinomas. Nature Genet. 16, 68-73 (1997).
    • (1997) Nature Genet. , vol.16 , pp. 68-73
    • Schmidt, L.1
  • 35
    • 0000460567 scopus 로고    scopus 로고
    • P13 kinase mediates transformation of hematopoietic cells by the V816 c-kit mutant
    • Chian, R. et al. P13 kinase mediates transformation of hematopoietic cells by the V816 c-kit mutant. Exp. Hematol. 28, 1491 (2000).
    • (2000) Exp. Hematol. , vol.28 , pp. 1491
    • Chian, R.1
  • 36
    • 0032543578 scopus 로고    scopus 로고
    • The kit receptor promotes cell survival via activation of P1 3-kinase and subsequent Akt-mediated phosphorylation of Bad on Ser136
    • Blume-Jensen, P., Janknecht, R. & Hunter T. The kit receptor promotes cell survival via activation of P1 3-kinase and subsequent Akt-mediated phosphorylation of Bad on Ser136. Curr. Biol. 8, 779-782 (1996).
    • (1996) Curr. Biol. , vol.8 , pp. 779-782
    • Blume-Jensen, P.1    Janknecht, R.2    Hunter, T.3
  • 37
    • 0029891236 scopus 로고    scopus 로고
    • Regulation of colony-stimulating factor 1 receptor signaling by the SH2 domain-containing tyrosine phosphatase. SHPTP1
    • Chen, H. E., Chang, S., Trub, T. & Neel, B. G. Regulation of colony-stimulating factor 1 receptor signaling by the SH2 domain-containing tyrosine phosphatase. SHPTP1. Mol. Cell. Biol. 16, 3685-3697 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3685-3697
    • Chen, H.E.1    Chang, S.2    Trub, T.3    Neel, B.G.4
  • 38
    • 0030014452 scopus 로고    scopus 로고
    • Signalling by the W/Kit receptor tyrosine kinase is negatively regulated in vivo by the protein tyrosine phosphatase Shp1
    • Paulson, R. E., Vesely, S., Siminovitch, K. A. & Bernstein, A. Signalling by the W/Kit receptor tyrosine kinase is negatively regulated in vivo by the protein tyrosine phosphatase Shp1. Nature Genet. 13, 309-315 (1996)
    • (1996) Nature Genet. , vol.13 , pp. 309-315
    • Paulson, R.E.1    Vesely, S.2    Siminovitch, K.A.3    Bernstein, A.4
  • 39
    • 0029907089 scopus 로고    scopus 로고
    • Oncogenic mutation in the Kit receptor tyrosine kinase alters substrate specificity and induces degradation of the protein tyrosine phosphatase SHP-1
    • Piao, X., Paulson, R., van der Geer, P., Pawson, T. & Bernstein, A. Oncogenic mutation in the Kit receptor tyrosine kinase alters substrate specificity and induces degradation of the protein tyrosine phosphatase SHP-1. Proc. Natl Acad. Sci. USA 93, 14665-14669 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 14665-14669
    • Piao, X.1    Paulson, R.2    Van Der Geer, P.3    Pawson, T.4    Bernstein, A.5
  • 40
    • 0034703285 scopus 로고    scopus 로고
    • RNA hyperediting and alternative splicing of hematopoietic cell phosphatase (PTPN6) gene in acute myeloid leukemia
    • Beghini, A. et al. RNA hyperediting and alternative splicing of hematopoietic cell phosphatase (PTPN6) gene in acute myeloid leukemia. Hum. Mol Genet. 9, 2297-2304 (2000).
    • (2000) Hum. Mol Genet. , vol.9 , pp. 2297-2304
    • Beghini, A.1
  • 41
    • 0029947186 scopus 로고    scopus 로고
    • Effects of a selective inhibitor of the Abl tyrosine kinase on the growth of Bcr-Abl positive cells
    • Druker, B. J. et al. Effects of a selective inhibitor of the Abl tyrosine kinase on the growth of Bcr-Abl positive cells. Nature Med. 2, 561-566 (1996).
    • (1996) Nature Med. , vol.2 , pp. 561-566
    • Druker, B.J.1
  • 42
    • 0034254249 scopus 로고    scopus 로고
    • Inhibition of c-kit receptor tyrosine kinase activity by STI 571, a selective tyrosine kinase inhibitor
    • Heinrich, M. C., et al. Inhibition of c-kit receptor tyrosine kinase activity by STI 571, a selective tyrosine kinase inhibitor. Blood 96, 925-932 (2000).
    • (2000) Blood , vol.96 , pp. 925-932
    • Heinrich, M.C.1
  • 43
    • 0017250977 scopus 로고
    • DNA related to the transforming gene(s) of avian sarcoma viruses is present in normal avian DNA
    • Stehelin, D., Varmus, H. E., Bishop, J. M. & Vogt, P. K. DNA related to the transforming gene(s) of avian sarcoma viruses is present in normal avian DNA. Nature 260, 170-173 (1976).
    • (1976) Nature , vol.260 , pp. 170-173
    • Stehelin, D.1    Varmus, H.E.2    Bishop, J.M.3    Vogt, P.K.4
  • 44
    • 0034693806 scopus 로고    scopus 로고
    • Selected glimpses into the activation and function of src kinase
    • Bjorge, J. D., Jakymiw, A & Fujita, D. J. Selected glimpses into the activation and function of src kinase. Oncogene 19, 5620-5635 (2000).
    • (2000) Oncogene , vol.19 , pp. 5620-5635
    • Bjorge, J.D.1    Jakymiw, A.2    Fujita, D.J.3
  • 45
    • 0031452274 scopus 로고    scopus 로고
    • Structures of Src-family tyrosine kinases
    • Sicheri, F. & Kuriyan, J. Structures of Src-family tyrosine kinases. Curr. Opin. Struct. Biol. 7, 777-785 (1997).
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 777-785
    • Sicheri, F.1    Kuriyan, J.2
  • 46
    • 0032932248 scopus 로고    scopus 로고
    • Activating SRC mutation in a subset of advanced human colon cancers
    • Irby, R. B. et al. Activating SRC mutation in a subset of advanced human colon cancers Nature Genet. 21, 187-190 (1999).
    • (1999) Nature Genet. , vol.21 , pp. 187-190
    • Irby, R.B.1
  • 47
    • 0000286732 scopus 로고
    • A minute chromosome in human chronic granulocytic leukemia
    • Nowell, P. & Hungerford, D. A minute chromosome in human chronic granulocytic leukemia. Science 132, 1497 (1960).
    • (1960) Science , vol.132 , pp. 1497
    • Nowell, P.1    Hungerford, D.2
  • 48
    • 0035122485 scopus 로고    scopus 로고
    • Induction of apoptosis in chronic myelogenous leukemia cells through nuclear entrapment of BCR-ABL tyrosine kinase
    • Vigneri, P. & Wang, J. Y. Induction of apoptosis in chronic myelogenous leukemia cells through nuclear entrapment of BCR-ABL tyrosine kinase. Nature Med. 7, 228-234 (2001).
    • (2001) Nature Med. , vol.7 , pp. 228-234
    • Vigneri, P.1    Wang, J.Y.2
  • 49
    • 0034693878 scopus 로고    scopus 로고
    • Regulation of cell death by the abl tyrosine kinase
    • Wang, J. Y. Regulation of cell death by the abl tyrosine kinase. Oncogene 19, 5643-5650 (2000).
    • (2000) Oncogene , vol.19 , pp. 5643-5650
    • Wang, J.Y.1
  • 50
    • 0033666776 scopus 로고    scopus 로고
    • Role of the p53-homologue p73 in F2F1-induced apoptosis
    • Stiewe, T. & Putzer, B. M. Role of the p53-homologue p73 in F2F1-induced apoptosis. Nature Genet. 26, 464-469 (2000).
    • (2000) Nature Genet. , vol.26 , pp. 464-469
    • Stiewe, T.1    Putzer, B.M.2
  • 51
    • 0033568349 scopus 로고    scopus 로고
    • c-Abl is activated by growth factors and Src family kinases and has a role in the cellular response to PDGF
    • Plattner, R., Kadlec, L., DeMali, K. A., Kazlauskas, A. & Pendergast, A. M. c-Abl is activated by growth factors and Src family kinases and has a role in the cellular response to PDGF. Genes Dev. 13, 2400-2411 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 2400-2411
    • Plattner, R.1    Kadlec, L.2    DeMali, K.A.3    Kazlauskas, A.4    Pendergast, A.M.5
  • 52
    • 0027422977 scopus 로고
    • A coiled-coil oligomerization domain of Bcr is essential for the transforming function of Bcr-Abl oncoproteins
    • McWhirter, J. R., Galasso, D. L. & Wang, J. Y. A coiled-coil oligomerization domain of Bcr is essential for the transforming function of Bcr-Abl oncoproteins. Mol. Cell. Biol. 13, 7587-7595 (1993).
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7587-7595
    • McWhirter, J.R.1    Galasso, D.L.2    Wang, J.Y.3
  • 53
    • 0034670036 scopus 로고    scopus 로고
    • The molecular biology of chronic myeloid leukemia
    • Deininger, M. W., Goldman, J. M. & Melo, J. V. The molecular biology of chronic myeloid leukemia. Blood 96, 3343-3356 (2000).
    • (2000) Blood , vol.96 , pp. 3343-3356
    • Deininger, M.W.1    Goldman, J.M.2    Melo, J.V.3
  • 54
    • 8944262829 scopus 로고    scopus 로고
    • Interaction of the receptor tyrosine kinase p145c-kit with the p210bcr/abl kinase in myeloid cells
    • Hallek, M. et al. Interaction of the receptor tyrosine kinase p145c-kit with the p210bcr/abl kinase in myeloid cells. Br. J. Haematol. 94, 5-16 (1996).
    • (1996) Br. J. Haematol. , vol.94 , pp. 5-16
    • Hallek, M.1
  • 55
    • 0034671745 scopus 로고    scopus 로고
    • BCR/ABL regulates expression of the cyclin-dependent kinase inhibitor p27Kip1 through the phosphatidylinositol 3-Kinase/AKT pathway
    • Gesbert, F., Sellers, W. R., Signoretti, S., Loda, M. & Griffin, J. D. BCR/ABL regulates expression of the cyclin-dependent kinase inhibitor p27Kip1 through the phosphatidylinositol 3-Kinase/AKT pathway. J. Biol. Chem. 275, 39223-39230 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 39223-39230
    • Gesbert, F.1    Sellers, W.R.2    Signoretti, S.3    Loda, M.4    Griffin, J.D.5
  • 56
    • 0030710188 scopus 로고    scopus 로고
    • Transformation of hematopoietic cells by BCR/ABL requires activation of a PI-3k/Akt-dependent pathway
    • Skorski, T. et al. Transformation of hematopoietic cells by BCR/ABL requires activation of a PI-3k/Akt-dependent pathway. EMBO J. 16, 6151-6161 (1997).
    • (1997) EMBO J. , vol.16 , pp. 6151-6161
    • Skorski, T.1
  • 57
    • 0034689031 scopus 로고    scopus 로고
    • Blockade of the Bcr-Abl kinase activity induces apoptosis of chronic myelogenous leukemia cells by suppressing signal transducer and activator of transcription 5-dependent expression of Bcl-xL
    • Horita, M. et al. Blockade of the Bcr-Abl kinase activity induces apoptosis of chronic myelogenous leukemia cells by suppressing signal transducer and activator of transcription 5-dependent expression of Bcl-xL. J. Exp. Med. 191, 977-984 (2000).
    • (2000) J. Exp. Med. , vol.191 , pp. 977-984
    • Horita, M.1
  • 58
    • 0030704646 scopus 로고    scopus 로고
    • Jaks and Stats in cytokine signaling
    • discussion, 112
    • Ihle, J. N., Nosaka, T., Thierfelder, W., Quelle, F. W. & Shimoda, K. Jaks and Stats in cytokine signaling. Stem Cells 15(Suppl. 1), 105-111; discussion, 112 (1997).
    • (1997) Stem Cells , vol.15 , Issue.1 SUPPL. , pp. 105-111
    • Ihle, J.N.1    Nosaka, T.2    Thierfelder, W.3    Quelle, F.W.4    Shimoda, K.5
  • 59
    • 0030840464 scopus 로고    scopus 로고
    • STATs and gene regulation
    • Darnell, J. E. STATs and gene regulation. Science 277, 1630-1635 (1997).
    • (1997) Science , vol.277 , pp. 1630-1635
    • Darnell, J.E.1
  • 60
    • 0035142665 scopus 로고    scopus 로고
    • Activation of STAT proteins and growth control
    • Bromberg, J. F. Activation of STAT proteins and growth control. BioEssays 23, 161-169 (2001).
    • (2001) BioEssays , vol.23 , pp. 161-169
    • Bromberg, J.F.1
  • 62
    • 0033621066 scopus 로고    scopus 로고
    • A nuclear protein tyrosine phosphatase is required for the inactivation of Stat
    • Haspel, R. L. & Darnell, J. E. A nuclear protein tyrosine phosphatase is required for the inactivation of Stat. Proc. Natl Acad Sci. USA 96, 10188-10193 (1999).
    • (1999) Proc. Natl Acad Sci. USA , vol.96 , pp. 10188-10193
    • Haspel, R.L.1    Darnell, J.E.2
  • 63
    • 0034082217 scopus 로고    scopus 로고
    • Negative regulation of cytokine signaling pathways
    • Yasukawa, H., Sasaki, A. & Yoshimura, A. Negative regulation of cytokine signaling pathways. Annu. Rev. Immunol. 18, 143-164 (2000).
    • (2000) Annu. Rev. Immunol. , vol.18 , pp. 143-164
    • Yasukawa, H.1    Sasaki, A.2    Yoshimura, A.3
  • 64
    • 0030852328 scopus 로고    scopus 로고
    • Fusion of TEL, the ETS-variant gene 6 (ETV6), to the receptor-associated kinase JAK2 as a result of t(9;12) in a lymphoid and t(9;15;12) in a myeloid leukemia
    • Peeters, P. et al. Fusion of TEL, the ETS-variant gene 6 (ETV6), to the receptor-associated kinase JAK2 as a result of t(9;12) in a lymphoid and t(9;15;12) in a myeloid leukemia. Blood 90, 2535-2540 (1997).
    • (1997) Blood , vol.90 , pp. 2535-2540
    • Peeters, P.1
  • 65
    • 15444339209 scopus 로고    scopus 로고
    • A TEL-JAK2 fusion protein with constitutive kinase activity in human leukemia
    • Lacronique, V. et al. A TEL-JAK2 fusion protein with constitutive kinase activity in human leukemia. Science 278, 1309-1312 (1997).
    • (1997) Science , vol.278 , pp. 1309-1312
    • Lacronique, V.1
  • 66
    • 0033639119 scopus 로고    scopus 로고
    • Stat5 is essential for the myelo- and lymphoproliferative disease induced by TEL/JAK2
    • Schwaller, J. et al. Stat5 is essential for the myelo- and lymphoproliferative disease induced by TEL/JAK2. Mol. Cell 6, 693-704 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 693-704
    • Schwaller, J.1
  • 67
    • 0034708086 scopus 로고    scopus 로고
    • Cooperation between STATS and phosphatidylinositol 3-kinase in the IL-3-dependent survival of a bone marrow derived cell line
    • Rosa Santos, S. C., Dumon, S., Mayeux, P., Gisselbrecht, S. & Gouilleux, F. Cooperation between STATS and phosphatidylinositol 3-kinase in the IL-3-dependent survival of a bone marrow derived cell line. Oncogene 19, 1164-1172 (2000).
    • (2000) Oncogene , vol.19 , pp. 1164-1172
    • Rosa Santos, S.C.1    Dumon, S.2    Mayeux, P.3    Gisselbrecht, S.4    Gouilleux, F.5
  • 68
    • 0031797243 scopus 로고    scopus 로고
    • Functional cooperation of the interleukin-2 receptor beta chain and Jak1 in phosphatidylinositol 3-kinase recruitment and phosphorylation
    • Migone, T. S. et al. Functional cooperation of the interleukin-2 receptor beta chain and Jak1 in phosphatidylinositol 3-kinase recruitment and phosphorylation. Mol. Cell. Biol. 18, 6416-6422 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6416-6422
    • Migone, T.S.1
  • 69
    • 0030999696 scopus 로고    scopus 로고
    • STAT3 as an adapter to couple phosphatidylinositol 3-kindse to the IFNAR1 chain of the type 1 interferon receptor
    • Pfeffer, L. M. et al. STAT3 as an adapter to couple phosphatidylinositol 3-kindse to the IFNAR1 chain of the type 1 interferon receptor. Science 276, 1418-1420 (1997).
    • (1997) Science , vol.276 , pp. 1418-1420
    • Pfeffer, L.M.1
  • 70
    • 0034653608 scopus 로고    scopus 로고
    • The PI3K-PDK1 connection: More than just a road to PKB
    • Vanhaesebroeck, B. & Alessi, D. R. The PI3K-PDK1 connection: more than just a road to PKB. Biochem. J. 346(3), 561-576 (2000).
    • (2000) Biochem. J. , vol.346 , Issue.3 , pp. 561-576
    • Vanhaesebroeck, B.1    Alessi, D.R.2
  • 71
    • 0034644525 scopus 로고    scopus 로고
    • TOR, a central controller of cell growth
    • Schmelzle, T. & Hall, M. N. TOR, a central controller of cell growth. Cell 103, 253-262 (2000).
    • (2000) Cell , vol.103 , pp. 253-262
    • Schmelzle, T.1    Hall, M.N.2
  • 72
    • 0035253411 scopus 로고    scopus 로고
    • Cell-cycle-dependent translational control
    • Pyronnet, S. & Sonenberg, N. Cell-cycle-dependent translational control. Curr. Opin. Gen. Dev. 11, 13-18 (2001).
    • (2001) Curr. Opin. Gen. Dev. , vol.11 , pp. 13-18
    • Pyronnet, S.1    Sonenberg, N.2
  • 73
    • 0033604521 scopus 로고    scopus 로고
    • Ribosomal S6 kinase signaling and the control of translation
    • Dafner, A. & Thomas, G. Ribosomal S6 kinase signaling and the control of translation. Exp. Cell Res. 253, 100-109 (1999).
    • (1999) Exp. Cell Res. , vol.253 , pp. 100-109
    • Dafner, A.1    Thomas, G.2
  • 75
    • 0027470177 scopus 로고
    • Structure, expression and chromosomal mapping of c-akt: Relationship tov-akt and its implications
    • Bellacosa, A. et al. Structure, expression and chromosomal mapping of c-akt: relationship tov-akt and its implications. Oncogene 8, 745-754 (1993).
    • (1993) Oncogene , vol.8 , pp. 745-754
    • Bellacosa, A.1
  • 76
    • 0034644523 scopus 로고    scopus 로고
    • Cellular signaling: Pivoting around PDK-1
    • Toker, A. & Newton, A. C. Cellular signaling: pivoting around PDK-1. Cell 103, 185-188 (2000).
    • (2000) Cell , vol.103 , pp. 185-188
    • Toker, A.1    Newton, A.C.2
  • 78
    • 0034176579 scopus 로고    scopus 로고
    • The role of 3-phosphoinositide-dependent protein kinase 1 in activating AGC kinases defined in embryonic stem cells
    • Williams, M. R. et al. The role of 3-phosphoinositide-dependent protein kinase 1 in activating AGC kinases defined in embryonic stem cells. Curr. Biol. 10, 439-448 (2000).
    • (2000) Curr. Biol. , vol.10 , pp. 439-448
    • Williams, M.R.1
  • 79
    • 0032752063 scopus 로고    scopus 로고
    • Cellular survival: A play in three Akts
    • Datta, S. R., Brunet, A. & Greenburg, M. E. Cellular survival: a play in three Akts. Genes Dev. 13, 2905-2927 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 2905-2927
    • Datta, S.R.1    Brunet, A.2    Greenburg, M.E.3
  • 80
    • 0032533225 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta regulates cyclin D1 proteolysis and subcellular localization
    • Diehl, J. A., Cheng, M., Roussel, M. F. & Sherr, C. J. Glycogen synthase kinase-3beta regulates cyclin D1 proteolysis and subcellular localization. Genes Dev. 12, 3499-3511 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 3499-3511
    • Diehl, J.A.1    Cheng, M.2    Roussel, M.F.3    Sherr, C.J.4
  • 81
    • 0034745353 scopus 로고    scopus 로고
    • Cytoplasmic localization of p21Cip1/WAF1 by Akt-induced phosphorylation in HER-2/neu-overexpressing cells
    • Zhuo, B. P. et al. Cytoplasmic localization of p21Cip1/WAF1 by Akt-induced phosphorylation in HER-2/neu-overexpressing cells. Nature Cell Biol. 3, 245-252 (2001).
    • (2001) Nature Cell Biol. , vol.3 , pp. 245-252
    • Zhuo, B.P.1
  • 82
    • 0000440912 scopus 로고    scopus 로고
    • Transformation of chicken cells by the gene encoding the catalytic subunit of PI 3-kinase
    • Chang, H. W. et al. Transformation of chicken cells by the gene encoding the catalytic subunit of PI 3-kinase. Science 276, 1848-1850 (1997).
    • (1997) Science , vol.276 , pp. 1848-1850
    • Chang, H.W.1
  • 83
    • 0032590011 scopus 로고    scopus 로고
    • PIK3CA is implicated as an oncogene in ovarian cancer
    • Shayesteh, I. et al. PIK3CA is implicated as an oncogene in ovarian cancer. Nature Genet. 21, 99-102 (1999).
    • (1999) Nature Genet. , vol.21 , pp. 99-102
    • Shayesteh, I.1
  • 84
    • 0032472913 scopus 로고    scopus 로고
    • Identification and characterization of a new oncogene derived from the regulatory subunit of phosphoinositide 3-kinase
    • Jimenez, C. et al. Identification and characterization of a new oncogene derived from the regulatory subunit of phosphoinositide 3-kinase. EMBO J. 17, 743-753 (1998).
    • (1998) EMBO J. , vol.17 , pp. 743-753
    • Jimenez, C.1
  • 86
    • 0034710675 scopus 로고    scopus 로고
    • Colorectal carcinomas in mice lacking the catalytic subunit of PI(3)Kγ
    • Sasaki, T. et al. Colorectal carcinomas in mice lacking the catalytic subunit of PI(3)Kγ. Nature 406, 897-902 (2000).
    • (2000) Nature , vol.406 , pp. 897-902
    • Sasaki, T.1
  • 87
    • 0033000334 scopus 로고    scopus 로고
    • p70(s6k) integrates phosphatidylinositol 3-kinase and rapamycin-regulated signals for E2F regulation in T lymphocytes
    • Brennan, P., Babbage, J. W., Thomas, G. & Cantrell, D. p70(s6k) integrates phosphatidylinositol 3-kinase and rapamycin-regulated signals for E2F regulation in T lymphocytes. Mol. Cell. Biol. 19, 4729-4738 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4729-4738
    • Brennan, P.1    Babbage, J.W.2    Thomas, G.3    Cantrell, D.4
  • 88
    • 0034682805 scopus 로고    scopus 로고
    • Stem cell factor/c-kit up-regulates cyclin D3 and promotes cell cycle progression via the phosphoinositide 3-kinase/p70 S6 kinase pathway in spermatogonia
    • Feng, L. X., Ravindranath, N. & Dym, M. Stem cell factor/c-kit up-regulates cyclin D3 and promotes cell cycle progression via the phosphoinositide 3-kinase/p70 S6 kinase pathway in spermatogonia. J. Biol. Chem. 275, 25572-25576 (2000)
    • (2000) J. Biol. Chem. , vol.275 , pp. 25572-25576
    • Feng, L.X.1    Ravindranath, N.2    Dym, M.3
  • 89
    • 0035793086 scopus 로고    scopus 로고
    • A role of the kinase mTOR in cellular transformation induced by the oncoproteins P3k and Akt
    • Masahiro, A., Blazek, E. & Vogt, P. K. A role of the kinase mTOR in cellular transformation induced by the oncoproteins P3k and Akt. Proc. Natl Acad. Sci. USA 98, 136-141 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 136-141
    • Masahiro, A.1    Blazek, E.2    Vogt, P.K.3
  • 90
    • 0035936783 scopus 로고    scopus 로고
    • NF1 tumor suppressor gene function: Narrowing the GAP
    • Cichowski, K. & Jacks, T. NF1 tumor suppressor gene function: narrowing the GAP. Cell 104, 593-604 (2001).
    • (2001) Cell , vol.104 , pp. 593-604
    • Cichowski, K.1    Jacks, T.2
  • 91
    • 0035810147 scopus 로고    scopus 로고
    • Efficacy and safety of a specific inhibitor of the BCR-Abl tyrosine kinase in chronic myeloid leukemia
    • Druker, B. J. et al. Efficacy and safety of a specific inhibitor of the BCR-Abl tyrosine kinase in chronic myeloid leukemia. N. Engl. J. Med. 344, 1031-1037 (2001).
    • (2001) N. Engl. J. Med. , vol.344 , pp. 1031-1037
    • Druker, B.J.1
  • 92
    • 0035810142 scopus 로고    scopus 로고
    • Activity of a specific inhibitor of the BCR-Abl tyrosine kinase in the blast crisis of chronic myeloid leukemia and acute lymphoblastic leukemia with the Philadelphia chromosome
    • Druker, B. J. et al. Activity of a specific inhibitor of the BCR-Abl tyrosine kinase in the blast crisis of chronic myeloid leukemia and acute lymphoblastic leukemia with the Philadelphia chromosome. N. Engl. J. Med. 344, 1038-1042 (2001).
    • (2001) N. Engl. J. Med. , vol.344 , pp. 1038-1042
    • Druker, B.J.1
  • 93
    • 0035810148 scopus 로고    scopus 로고
    • Effect of the tyrosine kinase inhibitor STI571 in a patient with a metastatic gastrointestinal stromal tumor
    • Joensuu, H. et al. Effect of the tyrosine kinase inhibitor STI571 in a patient with a metastatic gastrointestinal stromal tumor N. Engl. J. Med. 344, 1052-1056 (2001).
    • (2001) N. Engl. J. Med. , vol.344 , pp. 1052-1056
    • Joensuu, H.1


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