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Volumn 9, Issue 25, 2003, Pages 2043-2059

Src family kinases: Potential targets for the treatment of human cancer and leukemia

Author keywords

Cancerogenesis; Leukemogenesis; Protein kinases; Small molecule kinase inhibitor; Src family kinases

Indexed keywords

2,3 DIHYDRO 2 OXO 3 (4,5,6,7 TETRAHYDRO 1H INDOL 2 YLMETHYLENE) 1H INDOLE 5 SULFONIC ACID DIMETHYLAMIDE; 3 DIMETHYLAMINO 1 PHENYL 6 PYRIDAZONE; 4 AMINO 7 TERT BUTYL 5 (4 METHYLPHENYL)PYRAZOLO[3,4 D]PYRIMIDINE; ADENOSINE TRIPHOSPHATE; ANTINEOPLASTIC AGENT; CALPAIN; CGP 76030; IMATINIB; INDOLE DERIVATIVE; ONCOPROTEIN; PDI 180970; PDI 73955; PDI 80970; PHOSPHOTRANSFERASE; PROTEIN KINASE B; PROTEIN KINASE P60; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE KINASE INHIBITOR; PROTEINASE; PYRIMIDINE DERIVATIVE; QUINAZOLINE DERIVATIVE; QUINOLINE DERIVATIVE; SK 1606; STAT3 PROTEIN; UNCLASSIFIED DRUG; UROKINASE; UVOMORULIN;

EID: 0141538143     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/1381612033454126     Document Type: Review
Times cited : (116)

References (186)
  • 1
    • 0035902180 scopus 로고    scopus 로고
    • Oncogenic kinase signalling
    • Blume-Jensen P, Hunter T.Oncogenic kinase signalling. Nature 2001; 411: 355-65.
    • (2001) Nature , vol.411 , pp. 355-365
    • Blume-Jensen, P.1    Hunter, T.2
  • 3
    • 0033786922 scopus 로고    scopus 로고
    • Protein tyrosine kinase structure and function
    • Hubbard SR, Till JH. Protein tyrosine kinase structure and function. Annu Rev Biochem 2000; 69: 373-98.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 373-398
    • Hubbard, S.R.1    Till, J.H.2
  • 4
    • 0029896163 scopus 로고    scopus 로고
    • Regulation, substrates and functions of src
    • 1287
    • Brown MT, Cooper JA. Regulation, substrates and functions of src. Biochim Biophys Acta 1996; 1287: 121-149.
    • (1996) Biochim. Biophys. Acta , pp. 121-149
    • Brown, M.T.1    Cooper, J.A.2
  • 5
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Xu W, Harrison S, Eck M. Three-dimensional structure of the tyrosine kinase c-Src. Nature 1997; 385: 595-602.
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S.2    Eck, M.3
  • 6
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • Sicheri F, Moarefi I, Kuriyan J. Crystal structure of the Src family tyrosine kinase Hck. Nature 1997; 385: 602-609.
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 7
    • 0028941630 scopus 로고
    • Mutational analysis of the Src SH3 domain: The same residues of the ligand binding surface are important for intra- and intermolecular interactions
    • Erpel T, Superti-Furga G, Courtneidge SA. Mutational analysis of the Src SH3 domain: the same residues of the ligand binding surface are important for intra- and intermolecular interactions. Embo J 1995; 14: 963-75.
    • (1995) Embo J. , vol.14 , pp. 963-975
    • Erpel, T.1    Superti-Furga, G.2    Courtneidge, S.A.3
  • 9
    • 0026355723 scopus 로고
    • Csk: A protein-tyrosine kinase involved in regulation of Src family kinases
    • Okada M, Nada S, Yamanashi Y, Yamamoto T, Nakagawa H. Csk: A protein-tyrosine kinase involved in regulation of Src family kinases. J Biol Chem 1991; 266: 24249-24252.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24249-24252
    • Okada, M.1    Nada, S.2    Yamanashi, Y.3    Yamamoto, T.4    Nakagawa, H.5
  • 10
    • 0028107291 scopus 로고
    • Identification and characterization of a novel tyrosine kinase from megakaryocytes
    • Bennett BD, Cowley S, Jiang S, London R, Deng B, Grabarek J, et al. Identification and characterization of a novel tyrosine kinase from megakaryocytes. J Biol Chem 1994; 269: 1068-1074.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1068-1074
    • Bennett, B.D.1    Cowley, S.2    Jiang, S.3    London, R.4    Deng, B.5    Grabarek, J.6
  • 12
    • 0027176228 scopus 로고
    • Constitutive activation of Src family kinases in mouse embryos that lack Csk
    • Nada S, Yagi T, Takeda H, Tokunaga T, Nakagawa H, Ikawa Y, et al. Constitutive activation of Src family kinases in mouse embryos that lack Csk. Cell 1993; 73: 125-135.
    • (1993) Cell , vol.73 , pp. 125-135
    • Nada, S.1    Yagi, T.2    Takeda, H.3    Tokunaga, T.4    Nakagawa, H.5    Ikawa, Y.6
  • 14
    • 0023392494 scopus 로고
    • Activation of the oncogenic potential of the avian cellular src protein by specific structural alterations of the carboxy terminus
    • Reynolds AB, Vila J, Lansing TJ, Potts WM, Weber MJ, Parsons JT. Activation of the oncogenic potential of the avian cellular src protein by specific structural alterations of the carboxy terminus. Embo J 1987; 6: 2359-2364.
    • (1987) Embo J. , vol.6 , pp. 2359-2364
    • Reynolds, A.B.1    Vila, J.2    Lansing, T.J.3    Potts, W.M.4    Weber, M.J.5    Parsons, J.T.6
  • 15
    • 0031464009 scopus 로고    scopus 로고
    • The role of the linker between the SH2 domain and catalytic domain in the regulation and function of Src
    • Gonfloni S, Williams JC, Hattula K, Weijland A, Wierenga RK, Superti-Furga G. The role of the linker between the SH2 domain and catalytic domain in the regulation and function of Src. Embo J 1997; 16: 7261-71.
    • (1997) Embo J. , vol.16 , pp. 7261-7271
    • Gonfloni, S.1    Williams, J.C.2    Hattula, K.3    Weijland, A.4    Wierenga, R.K.5    Superti-Furga, G.6
  • 16
    • 0032769397 scopus 로고    scopus 로고
    • Leucine 255 of Src couples intramolecular interactions to inhibition of catalysis
    • Gonfloni S, Frischknecht F, Way M, Superti-Furga G. Leucine 255 of Src couples intramolecular interactions to inhibition of catalysis. Nat Struct Biol 1999; 6: 760-4.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 760-764
    • Gonfloni, S.1    Frischknecht, F.2    Way, M.3    Superti-Furga, G.4
  • 17
    • 0033543694 scopus 로고    scopus 로고
    • SH2-kinase linker mutations release Hck tyrosine kinase and transforming activities in Rat-2 fibroblasts
    • Briggs SD, Smithgall TE. SH2-kinase linker mutations release Hck tyrosine kinase and transforming activities in Rat-2 fibroblasts. J Biol Chem 1999; 274: 26579-83.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26579-26583
    • Briggs, S.D.1    Smithgall, T.E.2
  • 19
    • 0030792141 scopus 로고    scopus 로고
    • SH3-mediated Hck tyrosine kinase activation and fibroblast transformation by the Nef protein of HIV-1
    • Briggs SD, Sharkey M, Stevenson M, Smithgall TE. SH3-mediated Hck tyrosine kinase activation and fibroblast transformation by the Nef protein of HIV-1. J Biol Chem 1997; 272: 17899-902.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17899-17902
    • Briggs, S.D.1    Sharkey, M.2    Stevenson, M.3    Smithgall, T.E.4
  • 20
    • 0025172811 scopus 로고
    • Association between the PDGF receptor and members of the src family tyrosine kinases
    • Kypta R, Goldberg Y, Ulug E, Courtneidge SA. Association between the PDGF receptor and members of the src family tyrosine kinases. Cell 1990; 62: 481-492.
    • (1990) Cell , vol.62 , pp. 481-492
    • Kypta, R.1    Goldberg, Y.2    Ulug, E.3    Courtneidge, S.A.4
  • 21
    • 0026668932 scopus 로고
    • Association of Fyn with the activated PDGF receptor: Requirements for binding and phosphorylation
    • Twamley GM, Hall B, Kypta R, Courtneidge SA. Association of Fyn with the activated PDGF receptor: requirements for binding and phosphorylation. Oncogene 1992; 7: 1893-1901.
    • (1992) Oncogene , vol.7 , pp. 1893-1901
    • Twamley, G.M.1    Hall, B.2    Kypta, R.3    Courtneidge, S.A.4
  • 22
    • 0028609382 scopus 로고
    • Integrin-mediated signal transduction linked to Ras pathway by Grb2 binding to focal adhesion kinase
    • Schlaepfer DD, Hanks SK, Hunter T, van der Geer P. Integrin-mediated signal transduction linked to Ras pathway by Grb2 binding to focal adhesion kinase. Nature 1994; 372: 786-791.
    • (1994) Nature , vol.372 , pp. 786-791
    • Schlaepfer, D.D.1    Hanks, S.K.2    Hunter, T.3    van der Geer, P.4
  • 23
    • 0029165834 scopus 로고
    • Direct and specific interaction of c-Src with Neu is involved in signaling by the epidermal growth factor receptor
    • Muthuswamy SK, Muller WJ. Direct and specific interaction of c-Src with Neu is involved in signaling by the epidermal growth factor receptor. Oncogene 1995; 11: 271-9.
    • (1995) Oncogene , vol.11 , pp. 271-279
    • Muthuswamy, S.K.1    Muller, W.J.2
  • 24
    • 0028808080 scopus 로고
    • Activation of Src family kinases in Neu-induced mammary tumors correlates with their association with distinct sets of tyrosine phosphorylated proteins in vivo
    • Muthuswamy SK, Muller WJ. Activation of Src family kinases in Neu-induced mammary tumors correlates with their association with distinct sets of tyrosine phosphorylated proteins in vivo. Oncogene 1995; 11: 1801-10.
    • (1995) Oncogene , vol.11 , pp. 1801-1810
    • Muthuswamy, S.K.1    Muller, W.J.2
  • 25
    • 0030833445 scopus 로고    scopus 로고
    • Lyn associates with the juxtamembrane region of c-Kit and is activated by stem cell factor in hematopoietic cell lines and normal progenitor cells
    • Linnekin D, DeBerry CS, Mou S. Lyn associates with the juxtamembrane region of c-Kit and is activated by stem cell factor in hematopoietic cell lines and normal progenitor cells. J Biol Chem 1997; 272: 27450-5.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27450-27455
    • Linnekin, D.1    DeBerry, C.S.2    Mou, S.3
  • 26
    • 0031034681 scopus 로고    scopus 로고
    • The protooncogene product p120(cbl) links c-Src and phosphatidylinositol 3′-kinase to the integrin signaling pathway
    • Ojaniemi M, Martin SS, Dolfi F, Olefsky JM, Vuori K. The protooncogene product p120(cbl) links c-Src and phosphatidylinositol 3′-kinase to the integrin signaling pathway. J Biol Chem 1997; 272: 3780-7.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3780-3787
    • Ojaniemi, M.1    Martin, S.S.2    Dolfi, F.3    Olefsky, J.M.4    Vuori, K.5
  • 27
    • 0031455168 scopus 로고    scopus 로고
    • The Src family kinase Hck interacts with Bcr-Abl by a kinase-independent mechanism and phosphorylates the Grb2-binding site of Bcr
    • Warmuth M, Bergmann M, Prieß A, Häuslmann K, Emmerich B, Hallek M. The Src family kinase Hck interacts with Bcr-Abl by a kinase-independent mechanism and phosphorylates the Grb2-binding site of Bcr. J Biol Chem 1997; 272: 33260-33270.
    • (1997) J. Biol. Chem. , vol.272 , pp. 33260-33270
    • Warmuth, M.1    Bergmann, M.2    Prieß, A.3    Häuslmann, K.4    Emmerich, B.5    Hallek, M.6
  • 28
    • 0034674707 scopus 로고    scopus 로고
    • Transformation of myeloid leukemia cells to cytokine independence by Bcr-Abl is suppressed by kinase-defective Hck
    • Lionberger JM, Wilson MB, Smithgall TE. Transformation of myeloid leukemia cells to cytokine independence by Bcr-Abl is suppressed by kinase-defective Hck. J Biol Chem 2000; 275: 18581-5.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18581-18585
    • Lionberger, J.M.1    Wilson, M.B.2    Smithgall, T.E.3
  • 29
    • 0032987119 scopus 로고    scopus 로고
    • Reduced C-terminal Src kinase (Csk) activities in hepatocellular carcinoma
    • Masaki T, Okada M, Tokuda M, Shiratori Y, Hatase O, Shirai M, et al. Reduced C-terminal Src kinase (Csk) activities in hepatocellular carcinoma. Hepatology 1999; 29: 379-84.
    • (1999) Hepatology , vol.29 , pp. 379-384
    • Masaki, T.1    Okada, M.2    Tokuda, M.3    Shiratori, Y.4    Hatase, O.5    Shirai, M.6
  • 30
    • 0033521886 scopus 로고    scopus 로고
    • Activation of Src in human breast tumor cell lines: Elevated levels of phosphotyrosine phosphatase activity that preferentially recognizes the Src carboxy terminal negative regulatory tyrosine 530
    • Egan C, Pang A, Durda D, Cheng HC, Wang JH, Fujita DJ. Activation of Src in human breast tumor cell lines: elevated levels of phosphotyrosine phosphatase activity that preferentially recognizes the Src carboxy terminal negative regulatory tyrosine 530. Oncogene 1999; 18: 1227-37.
    • (1999) Oncogene , vol.18 , pp. 1227-1237
    • Egan, C.1    Pang, A.2    Durda, D.3    Cheng, H.C.4    Wang, J.H.5    Fujita, D.J.6
  • 32
    • 0033598173 scopus 로고    scopus 로고
    • Ubiquitin-dependent degradation of active Src
    • Hakak Y, Martin GS. Ubiquitin-dependent degradation of active Src. Curr Biol 1999; 9: 1039-42.
    • (1999) Curr. Biol. , vol.9 , pp. 1039-1042
    • Hakak, Y.1    Martin, G.S.2
  • 33
    • 0035860713 scopus 로고    scopus 로고
    • Src-catalyzed phosphorylation of c-Cbl leads to the interdependent ubiquitination of both proteins
    • Yokouchi M, Kondo T, Sanjay A, Houghton A, Yoshimura A, Komiya S, et al. Src-catalyzed phosphorylation of c-Cbl leads to the interdependent ubiquitination of both proteins. J Biol Chem 2001; 276: 35185-93.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35185-35193
    • Yokouchi, M.1    Kondo, T.2    Sanjay, A.3    Houghton, A.4    Yoshimura, A.5    Komiya, S.6
  • 34
    • 0036395180 scopus 로고    scopus 로고
    • Ubiquitin-dependent proteolysis: Its role in human diseases and the design of therapeutic strategies
    • Sakamoto KM. Ubiquitin-dependent proteolysis: its role in human diseases and the design of therapeutic strategies. Mol Genet Metab 2002; 77: 44-56.
    • (2002) Mol. Genet. Metab. , vol.77 , pp. 44-56
    • Sakamoto, K.M.1
  • 35
    • 0029097471 scopus 로고
    • Induction of mammary epithelial hyperplasias and mammary tumors in transgenic mice expressing a murine mammary tumor virus/activated c-src fusion gene
    • Webster MA, Cardiff RD, Muller WJ. Induction of mammary epithelial hyperplasias and mammary tumors in transgenic mice expressing a murine mammary tumor virus/activated c-src fusion gene. Proc Natl Acad Sci USA 1995; 92: 7849-53.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7849-7853
    • Webster, M.A.1    Cardiff, R.D.2    Muller, W.J.3
  • 36
  • 38
    • 0025192786 scopus 로고
    • Activation of the pp60c-src protein kinase is an early event in colonic carcinogenesis
    • Cartwright CA, Meisler AI, Eckhart W. Activation of the pp60c-src protein kinase is an early event in colonic carcinogenesis. Proc Natl Acad Sci USA 1990; 87: 558-62.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 558-562
    • Cartwright, C.A.1    Meisler, A.I.2    Eckhart, W.3
  • 39
    • 0027469402 scopus 로고
    • Increase in activity and level of pp60c-src in progressive stages of human colorectal cancer
    • Talamonti MS, Roh MS, Curley SA, Gallick GE. Increase in activity and level of pp60c-src in progressive stages of human colorectal cancer. J Clin Invest 1993; 91: 53-60.
    • (1993) J. Clin. Invest. , vol.91 , pp. 53-60
    • Talamonti, M.S.1    Roh, M.S.2    Curley, S.A.3    Gallick, G.E.4
  • 41
    • 0037080135 scopus 로고    scopus 로고
    • Activation of Src kinase in primary colorectal carcinoma: An indicator of poor clinical prognosis
    • Allgayer H, Boyd DD, Heiss MM, Abdalla EK, Curley SA, Gallick GE. Activation of Src kinase in primary colorectal carcinoma: an indicator of poor clinical prognosis. Cancer 2002; 94: 344-51.
    • (2002) Cancer , vol.94 , pp. 344-351
    • Allgayer, H.1    Boyd, D.D.2    Heiss, M.M.3    Abdalla, E.K.4    Curley, S.A.5    Gallick, G.E.6
  • 42
    • 18644374835 scopus 로고    scopus 로고
    • Identification of Src transformation fingerprint in human colon cancer
    • Malek RL, Irby RB, Guo QM, Lee K, Wong S, He M, et al. Identification of Src transformation fingerprint in human colon cancer. Oncogene 2002; 21: 7256-65.
    • (2002) Oncogene , vol.21 , pp. 7256-7265
    • Malek, R.L.1    Irby, R.B.2    Guo, Q.M.3    Lee, K.4    Wong, S.5    He, M.6
  • 44
    • 0033603453 scopus 로고    scopus 로고
    • Transcriptional induction of the urokinase receptor gene by a constitutively active Src. Requirement of an upstream motif (-152/-135) bound with Sp1
    • Allgayer H, Wang H, Gallick GE, Crabtree A, Mazar A, Jones T, et al. Transcriptional induction of the urokinase receptor gene by a constitutively active Src. Requirement of an upstream motif (-152/-135) bound with Sp1. J Biol Chem 1999; 274: 18428-37.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18428-18437
    • Allgayer, H.1    Wang, H.2    Gallick, G.E.3    Crabtree, A.4    Mazar, A.5    Jones, T.6
  • 45
    • 0032493871 scopus 로고    scopus 로고
    • Requirement for specific proteases in cancer cell intravasation as revealed by a novel semiquantitative PCR-based assay
    • Kim J, Yu W, Kovalski K, Ossowski L. Requirement for specific proteases in cancer cell intravasation as revealed by a novel semiquantitative PCR-based assay. Cell 1998; 94: 353-62.
    • (1998) Cell , vol.94 , pp. 353-362
    • Kim, J.1    Yu, W.2    Kovalski, K.3    Ossowski, L.4
  • 46
    • 0033824172 scopus 로고    scopus 로고
    • Urokinase receptor and integrin partnership: Coordination of signaling for cell adhesion, migration and growth
    • Ossowski L, Aguirre-Ghiso JA. Urokinase receptor and integrin partnership: coordination of signaling for cell adhesion, migration and growth. Curr Opin Cell Biol 2000; 12: 613-20.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 613-620
    • Ossowski, L.1    Aguirre-Ghiso, J.A.2
  • 47
    • 0034118807 scopus 로고    scopus 로고
    • Identification of a novel nuclear factor-kappaB sequence involved in expression of urokinase-type plasminogen activator receptor
    • Wang Y, Dang J, Wang H, Allgayer H, Murrell GA, Boyd D. Identification of a novel nuclear factor-kappaB sequence involved in expression of urokinase-type plasminogen activator receptor. Eur J Biochem 2000; 267: 3248-54.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 3248-3254
    • Wang, Y.1    Dang, J.2    Wang, H.3    Allgayer, H.4    Murrell, G.A.5    Boyd, D.6
  • 48
    • 0033567413 scopus 로고    scopus 로고
    • A region between -141 and -61 bp containing a proximal AP-1 is essential for constitutive expression of urokinase-type plasminogen activator receptor
    • Dang J, Boyd D, Wang H, Allgayer H, Doe WF, Wang Y. A region between -141 and -61 bp containing a proximal AP-1 is essential for constitutive expression of urokinase-type plasminogen activator receptor. Eur J Biochem 1999; 264: 92-9.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 92-99
    • Dang, J.1    Boyd, D.2    Wang, H.3    Allgayer, H.4    Doe, W.F.5    Wang, Y.6
  • 49
    • 0036631895 scopus 로고    scopus 로고
    • Plasmin/plasminogen system in colorectal cancer
    • Berger DH. Plasmin/plasminogen system in colorectal cancer. World J Surg 2002; 26: 767-71.
    • (2002) World J. Surg. , vol.26 , pp. 767-771
    • Berger, D.H.1
  • 50
    • 0037021230 scopus 로고    scopus 로고
    • Elevated c-Src is linked to altered cell-matrix adhesion rather than proliferation in KM12C human colorectal cancer cells
    • Jones RJ, Avizienyte E, Wyke AW, Owens DW, Brunton VG, Frame MC. Elevated c-Src is linked to altered cell-matrix adhesion rather than proliferation in KM12C human colorectal cancer cells. Br J Cancer 2002; 87: 1128-35.
    • (2002) Br. J. Cancer , vol.87 , pp. 1128-1135
    • Jones, R.J.1    Avizienyte, E.2    Wyke, A.W.3    Owens, D.W.4    Brunton, V.G.5    Frame, M.C.6
  • 52
    • 0035992434 scopus 로고    scopus 로고
    • Src family kinase inhibitor PP2 restores the E-cadherin/catenin cell adhesion system in human cancer cells and reduces cancer metastasis
    • Nam JS, Ino Y, Sakamoto M, Hirohashi S. Src family kinase inhibitor PP2 restores the E-cadherin/catenin cell adhesion system in human cancer cells and reduces cancer metastasis. Clin Cancer Res 2002; 8: 2430-6.
    • (2002) Clin. Cancer Res. , vol.8 , pp. 2430-2436
    • Nam, J.S.1    Ino, Y.2    Sakamoto, M.3    Hirohashi, S.4
  • 53
    • 0036570080 scopus 로고    scopus 로고
    • Increased Src activity disrupts cadherin/catenin-mediated homotypic adhesion in human colon cancer and transformed rodent cells
    • Irby RB, Yeatman TJ. Increased Src activity disrupts cadherin/catenin-mediated homotypic adhesion in human colon cancer and transformed rodent cells. Cancer Res 2002; 62: 2669-74.
    • (2002) Cancer Res. , vol.62 , pp. 2669-2674
    • Irby, R.B.1    Yeatman, T.J.2
  • 54
    • 0033199696 scopus 로고    scopus 로고
    • Absence of genetic alteration at codon 531 of the human c-src gene in 479 advanced colorectal cancers from Japanese and Caucasian patients
    • Daigo Y, Furukawa Y, Kawasoe T, Ishiguro H, Fujita M, Sugai S, et al. Absence of genetic alteration at codon 531 of the human c-src gene in 479 advanced colorectal cancers from Japanese and Caucasian patients. Cancer Res 1999; 59: 4222-4.
    • (1999) Cancer Res. , vol.59 , pp. 4222-4224
    • Daigo, Y.1    Furukawa, Y.2    Kawasoe, T.3    Ishiguro, H.4    Fujita, M.5    Sugai, S.6
  • 55
    • 0035808252 scopus 로고    scopus 로고
    • SRC transcriptional activation in a subset of human colon cancer cell lines
    • Dehm S, Senger M A, Bonham K. SRC transcriptional activation in a subset of human colon cancer cell lines. FEBS Lett 2001; 487: 367-71.
    • (2001) FEBS Lett. , vol.487 , pp. 367-371
    • Dehm, S.1    Senger, M.A.2    Bonham, K.3
  • 57
    • 6844259884 scopus 로고    scopus 로고
    • Activation of c-Src by receptor tyrosine kinases in human colon cancer cells with high metastatic potential
    • Mao W, Irby R, Coppola D, Fu L, Wloch M, Turner J, et al. Activation of c-Src by receptor tyrosine kinases in human colon cancer cells with high metastatic potential. Oncogene 1997; 15: 3083-90.
    • (1997) Oncogene , vol.15 , pp. 3083-3090
    • Mao, W.1    Irby, R.2    Coppola, D.3    Fu, L.4    Wloch, M.5    Turner, J.6
  • 58
    • 0020645860 scopus 로고
    • Expression of pp60c-src protein kinase in adult and fetal human tissue: High activities in some sarcomas and mammary carcinomas
    • Jacobs C, Rubsamen H. Expression of pp60c-src protein kinase in adult and fetal human tissue: high activities in some sarcomas and mammary carcinomas. Cancer Res 1983; 43: 1696-702.
    • (1983) Cancer Res. , vol.43 , pp. 1696-1702
    • Jacobs, C.1    Rubsamen, H.2
  • 59
  • 61
    • 0031979414 scopus 로고    scopus 로고
    • Characterization of human epidermal growth factor receptor and c-Src interactions in human breast tumor cells
    • Biscardi JS, Bels hes AP, Parsons SJ. Characterization of human epidermal growth factor receptor and c-Src interactions in human breast tumor cells. Mol Carcinog 1998; 21: 261-72.
    • (1998) Mol. Carcinog. , vol.21 , pp. 261-272
    • Biscardi, J.S.1    Belsshes, A.P.2    Parsons, S.J.3
  • 62
    • 0027954475 scopus 로고
    • Activation of the c-Src tyrosine kinase is required for the induction of mammary tumors in transgenic mice
    • Guy CT, Muthuswamy SK, Cardiff RD, Soriano P, Muller WJ. Activation of the c-Src tyrosine kinase is required for the induction of mammary tumors in transgenic mice. Genes Dev 1994; 8: 23-32.
    • (1994) Genes Dev. , vol.8 , pp. 23-32
    • Guy, C.T.1    Muthuswamy, S.K.2    Cardiff, R.D.3    Soriano, P.4    Muller, W.J.5
  • 63
    • 0028047315 scopus 로고
    • Mammary tumors expressing the neu proto-oncogene possess elevated c-Src tyrosine kinase activity
    • Muthuswamy SK, Siegel PM, Dankort DL, Webster MA, Muller WJ. Mammary tumors expressing the neu proto-oncogene possess elevated c-Src tyrosine kinase activity. Mol Cell Biol 1994; 14: 735-43.
    • (1994) Mol. Cell Biol. , vol.14 , pp. 735-743
    • Muthuswamy, S.K.1    Siegel, P.M.2    Dankort, D.L.3    Webster, M.A.4    Muller, W.J.5
  • 66
    • 0032812095 scopus 로고    scopus 로고
    • Decreased Src tyrosine kinase activity inhibits malignant human ovarian cancer tumor growth in a nude mouse model
    • Wiener JR, Nakano K, Kruzelock RP, Bucana CD, Bast RC Jr, Gallick G. E. Decreased Src tyrosine kinase activity inhibits malignant human ovarian cancer tumor growth in a nude mouse model. Clin Cancer Res 1999; 5: 2164-70.
    • (1999) Clin. Cancer Res. , vol.5 , pp. 2164-2170
    • Wiener, J.R.1    Nakano, K.2    Kruzelock, R.P.3    Bucana, C.D.4    Bast R.C., Jr.5    Gallick, G.E.6
  • 68
  • 70
    • 18644380911 scopus 로고    scopus 로고
    • Roles of activated Src and Stat3 signaling in melanoma tumor cell growth
    • Niu G, Bowman T, Huang M, Shivers S, Reintgen D, Daud A, et al. Roles of activated Src and Stat3 signaling in melanoma tumor cell growth. Oncogene 2002; 21: 7001-10.
    • (2002) Oncogene , vol.21 , pp. 7001-7010
    • Niu, G.1    Bowman, T.2    Huang, M.3    Shivers, S.4    Reintgen, D.5    Daud, A.6
  • 71
    • 0025107309 scopus 로고
    • Expression of the neuronal form of pp60c-src in neuroblastoma in relation to clinical stage and prognosis
    • Bjelfman C, Hedborg F, Johansson I, Nordenskjold M, Pahlman S. Expression of the neuronal form of pp60c-src in neuroblastoma in relation to clinical stage and prognosis. Cancer Res 1990; 50: 6908-14.
    • (1990) Cancer Res. , vol.50 , pp. 6908-6914
    • Bjelfman, C.1    Hedborg, F.2    Johansson, I.3    Nordenskjold, M.4    Pahlman, S.5
  • 72
    • 0025012642 scopus 로고
    • Early activation of endogenous pp60src kinase activity during neuronal differentiation of cultured human neuroblastoma cells
    • Bjelfman C, Meyerson G, Cartwright CA, Mellstrom K, Hammerling U, Pahlman S. Early activation of endogenous pp60src kinase activity during neuronal differentiation of cultured human neuroblastoma cells. Mol Cell Biol, 1990; 10: 361-70.
    • (1990) Mol. Cell Biol. , vol.10 , pp. 361-370
    • Bjelfman, C.1    Meyerson, G.2    Cartwright, C.A.3    Mellstrom, K.4    Hammerling, U.5    Pahlman, S.6
  • 73
    • 0033393771 scopus 로고    scopus 로고
    • Selective requirement for Src kinases during VEGF-induced angiogenesis and vascular permeability
    • Eliceiri BP, Paul R, Schwartzberg PL, Hood JD, Leng J, Cheresh DA. Selective requirement for Src kinases during VEGF-induced angiogenesis and vascular permeability. Mol Cell 1999; 4: 915-24.
    • (1999) Mol. Cell , vol.4 , pp. 915-924
    • Eliceiri, B.P.1    Paul, R.2    Schwartzberg, P.L.3    Hood, J.D.4    Leng, J.5    Cheresh, D.A.6
  • 74
    • 0023426279 scopus 로고
    • Nature and specificity of lymphokine independence induced by a selectable retroviral vector expressing v-src
    • Overell RW, Watson JD, Gallis B, Weisser KE, Cosman D, Widmer MB. Nature and specificity of lymphokine independence induced by a selectable retroviral vector expressing v-src. Mol Cell Biol 1987; 7: 3394-401.
    • (1987) Mol. Cell Biol. , vol.7 , pp. 3394-3401
    • Overell, R.W.1    Watson, J.D.2    Gallis, B.3    Weisser, K.E.4    Cosman, D.5    Widmer, M.B.6
  • 75
    • 0023176545 scopus 로고
    • Effect of infection with murine recombinant retroviruses containing the v-src oncogene on interleukin 2- and interleukin 3-dependent growth states
    • Watson JD, Eszes M, Overell R, Conlon P, Widmer M, Gillis S. Effect of infection with murine recombinant retroviruses containing the v-src oncogene on interleukin 2- and interleukin 3-dependent growth states. J Immunol 1987; 139: 123-9.
    • (1987) J. Immunol. , vol.139 , pp. 123-129
    • Watson, J.D.1    Eszes, M.2    Overell, R.3    Conlon, P.4    Widmer, M.5    Gillis, S.6
  • 76
    • 0025373759 scopus 로고
    • Abrogation of IL-3 dependent growth requires a functional v-src gene product: Evidence for an autocrine growth cycle
    • Anderson SM, Carroll PM, Lee FD. Abrogation of IL-3 dependent growth requires a functional v-src gene product: evidence for an autocrine growth cycle. Oncogene 1990; 5: 317-25.
    • (1990) Oncogene , vol.5 , pp. 317-325
    • Anderson, S.M.1    Carroll, P.M.2    Lee, F.D.3
  • 77
    • 0025353718 scopus 로고
    • bcr/abl and src but not myc and ras replace v-abl in lymphoid transformation
    • Engelman A, Rosenberg N. bcr/abl and src but not myc and ras replace v-abl in lymphoid transformation. Mol Cell Biol 1990; 10: 4365-9.
    • (1990) Mol. Cell Biol. , vol.10 , pp. 4365-4369
    • Engelman, A.1    Rosenberg, N.2
  • 78
    • 0026029996 scopus 로고
    • The v-src oncogene blocks the differentiation of a murine myeloid progenitor cell line and induces a tumorigenic phenotype
    • Kruger A, Anderson SM. The v-src oncogene blocks the differentiation of a murine myeloid progenitor cell line and induces a tumorigenic phenotype. Oncogene 1991; 6: 245-56.
    • (1991) Oncogene , vol.6 , pp. 245-256
    • Kruger, A.1    Anderson, S.M.2
  • 79
    • 0030992813 scopus 로고    scopus 로고
    • Abrogation of interleukin-3 dependence of myeloid cells by the v-src oncogene requires SH2 and SH3 domains which specify activation of STATs
    • Chaturvedi P, Sharma S, Reddy EP. Abrogation of interleukin-3 dependence of myeloid cells by the v-src oncogene requires SH2 and SH3 domains which specify activation of STATs. Mol Cell Biol 1997; 17: 3295-304.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 3295-3304
    • Chaturvedi, P.1    Sharma, S.2    Reddy, E.P.3
  • 80
    • 0029786988 scopus 로고    scopus 로고
    • Knockouts of Src-family kinases: Stiff bones, wimpy T cells, and bad memories
    • Lowell CA, Soriano P. Knockouts of Src-family kinases: stiff bones, wimpy T cells, and bad memories. Genes Dev 1996; 10: 1845-57.
    • (1996) Genes Dev. , vol.10 , pp. 1845-1857
    • Lowell, C.A.1    Soriano, P.2
  • 81
    • 0030740148 scopus 로고    scopus 로고
    • Characterization of the B lymphocyte populations in Lyn-deficient mice and the role of Lyn in signal initiation and down-regulation
    • Chan VW, Meng F, Soriano P, DeFranco AL, Lowell CA. Characterization of the B lymphocyte populations in Lyn-deficient mice and the role of Lyn in signal initiation and down-regulation. Immunity 1997; 7: 69-81.
    • (1997) Immunity , vol.7 , pp. 69-81
    • Chan, V.W.1    Meng, F.2    Soriano, P.3    DeFranco, A.L.4    Lowell, C.A.5
  • 82
    • 0030067201 scopus 로고    scopus 로고
    • Deficiency of the Hck and Src tyrosine kinases results in extreme levels of extramedullary hematopoiesis
    • Lowell C, Niwa M, Soriano P, Varmus H. Deficiency of the Hck and Src tyrosine kinases results in extreme levels of extramedullary hematopoiesis. Blood 1996; 87: 1780-1792.
    • (1996) Blood , vol.87 , pp. 1780-1792
    • Lowell, C.1    Niwa, M.2    Soriano, P.3    Varmus, H.4
  • 83
    • 0030912071 scopus 로고    scopus 로고
    • Lipopolysaccharide (LPS)-induced macrophage activation and signal transduction in the absence of Src-family kinases Hck, Fgr, and Lyn
    • Meng F, Lowell CA. Lipopolysaccharide (LPS)-induced macrophage activation and signal transduction in the absence of Src-family kinases Hck, Fgr, and Lyn. J Exp Med 1997; 185: 1661-70.
    • (1997) J. Exp. Med. , vol.185 , pp. 1661-1670
    • Meng, F.1    Lowell, C.A.2
  • 84
    • 0032479979 scopus 로고    scopus 로고
    • A beta 1 integrin signaling pathway involving Src-family kinases, Cb1 and PI-3 kinase is required for macrophage spreading and migration
    • Meng F, Lowell CA. A beta 1 integrin signaling pathway involving Src-family kinases, Cb1 and PI-3 kinase is required for macrophage spreading and migration. Embo J 1998; 17: 4391-403.
    • (1998) Embo J. , vol.17 , pp. 4391-4403
    • Meng, F.1    Lowell, C.A.2
  • 85
    • 0033555864 scopus 로고    scopus 로고
    • Adhesion-dependent degranulation of neutrophils requires the Src family kinases Fgr and Hck
    • Mocsai A, Ligeti E, Lowell CA, Berton G. Adhesion-dependent degranulation of neutrophils requires the Src family kinases Fgr and Hck. J Immunol 1999; 162: 1120-6.
    • (1999) J. Immunol. , vol.162 , pp. 1120-1126
    • Mocsai, A.1    Ligeti, E.2    Lowell, C.A.3    Berton, G.4
  • 86
    • 17944381147 scopus 로고    scopus 로고
    • Gain- and loss-of-function Lyn mutant mice define a critical inhibitory role for Lyn in the myeloid lineage
    • Harder KW, Parsons LM, Armes J, Evans N, Kountouri N, Clark R, et al. Gain- and loss-of-function Lyn mutant mice define a critical inhibitory role for Lyn in the myeloid lineage. Immunity 2001; 15: 603-15.
    • (2001) Immunity , vol.15 , pp. 603-615
    • Harder, K.W.1    Parsons, L.M.2    Armes, J.3    Evans, N.4    Kountouri, N.5    Clark, R.6
  • 87
    • 0033568568 scopus 로고    scopus 로고
    • Signaling via Src family kinases is required for normal internalization of the receptor c-Kit
    • Broudy VC, Lin NL, Liles WC, Corey SJ, O'Laughlin B, Mou S, et al. Signaling via Src family kinases is required for normal internalization of the receptor c-Kit. Blood 1999; 94: 1979-86.
    • (1999) Blood , vol.94 , pp. 1979-1986
    • Broudy, V.C.1    Lin, N.L.2    Liles, W.C.3    Corey, S.J.4    O'Laughlin, B.5    Mou, S.6
  • 88
    • 0033525759 scopus 로고    scopus 로고
    • EGF receptor signaling stimulates SRC kinase phosphorylation of clathrin, influencing clathrin redistribution and EGF uptake
    • Wilde A, Beattie EC, Lem L, Riethof DA, Liu SH, Mobley WC, et al. EGF receptor signaling stimulates SRC kinase phosphorylation of clathrin, influencing clathrin redistribution and EGF uptake. Cell 1999; 96: 677-87.
    • (1999) Cell , vol.96 , pp. 677-687
    • Wilde, A.1    Beattie, E.C.2    Lem, L.3    Riethof, D.A.4    Liu, S.H.5    Mobley, W.C.6
  • 89
    • 0037019184 scopus 로고    scopus 로고
    • Analysing c-kit internalization using a functional c-kit-EGFP chimera containing the fluorochrome within the extracellular domain
    • Jahn T, Seipel P, Coutinho S, Urschel S, Schwarz K, Miething C, et al. Analysing c-kit internalization using a functional c-kit-EGFP chimera containing the fluorochrome within the extracellular domain. Oncogene 2002; 21: 4508-20.
    • (2002) Oncogene , vol.21 , pp. 4508-4520
    • Jahn, T.1    Seipel, P.2    Coutinho, S.3    Urschel, S.4    Schwarz, K.5    Miething, C.6
  • 90
    • 0032560522 scopus 로고    scopus 로고
    • Malignant transformation of early lymphoid progenitors in mice expressing an activated Blk tyrosine kinase
    • Malek SN, Dordai DI, ReimJ, Dintzis H, Desiderio S. Malignant transformation of early lymphoid progenitors in mice expressing an activated Blk tyrosine kinase. Proc Natl Acad Sci USA 1998; 95: 7351-6.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7351-7356
    • Malek, S.N.1    Dordai, D.I.2    Reim, J.3    Dintzis, H.4    Desiderio, S.5
  • 92
    • 0024687218 scopus 로고
    • Expression of v-src induces a myeloproliferative disease in bone-marrow- reconstituted mice
    • Keller G, Wagner EF. Expression of v-src induces a myeloproliferative disease in bone-marrow- reconstituted mice. Genes Dev 1989; 3: 827-37.
    • (1989) Genes Dev. , vol.3 , pp. 827-837
    • Keller, G.1    Wagner, E.F.2
  • 93
    • 0032931978 scopus 로고    scopus 로고
    • Src-related protein tyrosine kinases in hematopoiesis
    • Corey SJ, Anderson SM. Src-related protein tyrosine kinases in hematopoiesis. Blood 1999; 93: 1-14.
    • (1999) Blood , vol.93 , pp. 1-14
    • Corey, S.J.1    Anderson, S.M.2
  • 94
    • 0034627767 scopus 로고    scopus 로고
    • Src family tyrosine kinases and growth factor signaling
    • Abram CL, Courtneidge SA. Src family tyrosine kinases and growth factor signaling. Exp Cell Res 2000; 254: 1-13.
    • (2000) Exp. Cell Res. , vol.254 , pp. 1-13
    • Abram, C.L.1    Courtneidge, S.A.2
  • 95
    • 0031985198 scopus 로고    scopus 로고
    • Multiple myeloma: Increasing evidence for a multistep transformation process
    • Hallek M, Leif Bergsagel P, Anderson KC. Multiple myeloma: increasing evidence for a multistep transformation process. Blood 1998; 91: 3-21.
    • (1998) Blood , vol.91 , pp. 3-21
    • Hallek, M.1    Leif Bergsagel, P.2    Anderson, K.C.3
  • 96
    • 0031456720 scopus 로고    scopus 로고
    • Signal transduction of interleukin-6 involves tyrosine phosphorylation of multiple cytosolic proteins and activation of Src-family kinases Fyn, Hck, and Lyn in multiple myeloma cell lines
    • Hallek M, Neumann C, Schaeffer M, Danhauser-Riedl S, von Bubnoff N, de Vos G, et al. Signal transduction of interleukin-6 involves tyrosine phosphorylation of multiple cytosolic proteins and activation of Src-family kinases Fyn, Hck, and Lyn in multiple myeloma cell lines. Exp Hematol 1997; 25: 1367-77.
    • (1997) Exp. Hematol. , vol.25 , pp. 1367-1377
    • Hallek, M.1    Neumann, C.2    Schaeffer, M.3    Danhauser-Riedl, S.4    von Bubnoff, N.5    de Vos, G.6
  • 97
    • 0035158029 scopus 로고    scopus 로고
    • Signaling through a Novel Domain of gp130 Mediates Cell Proliferation and Activation of Hck and Erk Kinases
    • Schaeffer M, Schneiderbauer M, Weidler S, Tavares R, Warmuth M, de Vos G, et al. Signaling through a Novel Domain of gp130 Mediates Cell Proliferation and Activation of Hck and Erk Kinases. Mol Cell Biol 2001; 21: 8068-81.
    • (2001) Mol. Cell Biol. , vol.21 , pp. 8068-8081
    • Schaeffer, M.1    Schneiderbauer, M.2    Weidler, S.3    Tavares, R.4    Warmuth, M.5    de Vos, G.6
  • 98
    • 0037085809 scopus 로고    scopus 로고
    • Requirements of src family kinase activity associated with CD45 for myeloma cell proliferation by interleukin-6
    • Ishikawa H, Tsuyama N, Abroun S, Liu S, Li FJ, Taniguchi O, et al. Requirements of src family kinase activity associated with CD45 for myeloma cell proliferation by interleukin-6. Blood 2002; 99: 2172-8.
    • (2002) Blood , vol.99 , pp. 2172-2178
    • Ishikawa, H.1    Tsuyama, N.2    Abroun, S.3    Liu, S.4    Li, F.J.5    Taniguchi, O.6
  • 99
    • 0029683347 scopus 로고    scopus 로고
    • Activation of Src kinases p53/56lyn and p59hck by p210bcr-abl in myeloid cells
    • Danhauser-Riedl S, Warmuth M, Druker BJ, Emmerich B, Hallek M. Activation of Src kinases p53/56lyn and p59hck by p210bcr-abl in myeloid cells. Cancer Res 1996; 56: 3589-3596.
    • (1996) Cancer Res. , vol.56 , pp. 3589-3596
    • Danhauser-Riedl, S.1    Warmuth, M.2    Druker, B.J.3    Emmerich, B.4    Hallek, M.5
  • 100
    • 0037438513 scopus 로고    scopus 로고
    • Dual-specific Src and Abl kinase inhibitors, PP1 and CGP76030, inhibit growth and survival of cells expressing imatinib mesylate-resistant Bcr- Abl kinases
    • Warmuth M, Simon N, Mitina O, Mathes R, Fabbro D, Manley PW, et al. Dual-specific Src and Abl kinase inhibitors, PP1 and CGP76030, inhibit growth and survival of cells expressing imatinib mesylate-resistant Bcr- Abl kinases. Blood 2003; 101: 664-72.
    • (2003) Blood , vol.101 , pp. 664-672
    • Warmuth, M.1    Simon, N.2    Mitina, O.3    Mathes, R.4    Fabbro, D.5    Manley, P.W.6
  • 103
    • 0033816156 scopus 로고    scopus 로고
    • Abl protein-tyrosine kinase inhibitor STI571 inhibits in vitro signal transduction mediated by c-kit and platelet-derived growth factor receptors
    • Buchdunger E, Cioffi CL, Law N, Stover D, Ohno-Jones S, Druker BJ, et al. Abl protein-tyrosine kinase inhibitor STI571 inhibits in vitro signal transduction mediated by c-kit and platelet-derived growth factor receptors. J Pharmacol Exp Ther 2000; 295: 139-45.
    • (2000) J. Pharmacol. Exp. Ther. , vol.295 , pp. 139-145
    • Buchdunger, E.1    Cioffi, C.L.2    Law, N.3    Stover, D.4    Ohno-Jones, S.5    Druker, B.J.6
  • 104
    • 0035871874 scopus 로고    scopus 로고
    • ARG tyrosine kinase activity is inhibited by STI571
    • Okuda K, Weisberg E, Gilliland DG, Griffin JD. ARG tyrosine kinase activity is inhibited by STI571. Blood 2001; 97: 2440-8.
    • (2001) Blood , vol.97 , pp. 2440-2448
    • Okuda, K.1    Weisberg, E.2    Gilliland, D.G.3    Griffin, J.D.4
  • 106
    • 0037199996 scopus 로고    scopus 로고
    • Analysis of the structural basis of specificity of inhibition of the Abl kinase by STI571
    • Corbin AS, Buchdunger E, Pascal F, Druker BJ. Analysis of the structural basis of specificity of inhibition of the Abl kinase by STI571. J Biol Chem 2002; 277: 32214-9.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32214-32219
    • Corbin, A.S.1    Buchdunger, E.2    Pascal, F.3    Druker, B.J.4
  • 107
    • 85081431917 scopus 로고    scopus 로고
    • A single amino acid exchange inverts susceptibility of related receptor tyrosine kinases for the ATP-site inhibitor STI-571
    • Bohmer FD, Karagyozov L, Uecker A, Serve H, Botzki A, Mahboobi S, et al. A single amino acid exchange inverts susceptibility of related receptor tyrosine kinases for the ATP-site inhibitor STI-571. J Biol Chem 2002; 14: 14.
    • (2002) J. Biol. Chem. , vol.14 , pp. 14
    • Bohmer, F.D.1    Karagyozov, L.2    Uecker, A.3    Serve, H.4    Botzki, A.5    Mahboobi, S.6
  • 108
    • 16144364951 scopus 로고    scopus 로고
    • Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation
    • Yamaguchi H, Hendrickson WA. Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation. Nature 1996; 384: 484-489.
    • (1996) Nature , vol.384 , pp. 484-489
    • Yamaguchi, H.1    Hendrickson, W.A.2
  • 109
    • 0033001789 scopus 로고    scopus 로고
    • Crystal structures of c-Src reveal features of its autoinhibitory mechanism
    • Xu W, Doshi A, Lei M, Eck MJ, Harrison SC. Crystal structures of c-Src reveal features of its autoinhibitory mechanism. Mol Cell 1999; 3: 629-38.
    • (1999) Mol. Cell , vol.3 , pp. 629-638
    • Xu, W.1    Doshi, A.2    Lei, M.3    Eck, M.J.4    Harrison, S.C.5
  • 110
    • 0033063429 scopus 로고    scopus 로고
    • Crystal structure of Hck in complex with a Src family-selective tyrosine kinase inhibitor
    • Schindler T, Sicheri F, Pico A, Gazit A, Levitzki A, Kuriyan J. Crystal structure of Hck in complex with a Src family-selective tyrosine kinase inhibitor. Mol Cell 1999; 3: 639-48.
    • (1999) Mol. Cell , vol.3 , pp. 639-648
    • Schindler, T.1    Sicheri, F.2    Pico, A.3    Gazit, A.4    Levitzki, A.5    Kuriyan, J.6
  • 111
    • 0030598848 scopus 로고    scopus 로고
    • Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism
    • Mohammadi M, Schlessinger J, Hubbard SR. Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism. Cell 1996; 86: 577-87.
    • (1996) Cell , vol.86 , pp. 577-587
    • Mohammadi, M.1    Schlessinger, J.2    Hubbard, S.R.3
  • 112
    • 0035929146 scopus 로고    scopus 로고
    • Structural basis for autoinhibition of the Ephb2 receptor tyrosine kinase by the unphosphorylated juxtamembrane region
    • Wybenga-Groot LE, Baskin B, Ong SH, Tong J, Pawson T, Sicheri F. Structural basis for autoinhibition of the Ephb2 receptor tyrosine kinase by the unphosphorylated juxtamembrane region. Cell 2001; 106: 745-57.
    • (2001) Cell , vol.106 , pp. 745-757
    • Wybenga-Groot, L.E.1    Baskin, B.2    Ong, S.H.3    Tong, J.4    Pawson, T.5    Sicheri, F.6
  • 113
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse M, Kuriyan J. The conformational plasticity of protein kinases. Cell 2002; 109: 275-82.
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 114
    • 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 BJ, Sawyers CL, Kantarjian H, Resta DJ, Reese SF, Ford JM, 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 2001; 344: 1038-42.
    • (2001) N. Engl. J. Med. , vol.344 , pp. 1038-1042
    • Druker, B.J.1    Sawyers, C.L.2    Kantarjian, H.3    Resta, D.J.4    Reese, S.F.5    Ford, J.M.6
  • 115
    • 0035810147 scopus 로고    scopus 로고
    • Efficacy and safety of a specific inhibitor of the BCR-ABL tyrosine kinase in chronic myeloid leukemia
    • Druker BJ, Talpaz M, Resta DJ, Peng B, Buchdunger E, Ford JM, et al. Efficacy and safety of a specific inhibitor of the BCR-ABL tyrosine kinase in chronic myeloid leukemia. N Engl J Med 2001; 344: 1031-7.
    • (2001) N. Engl. J. Med. , vol.344 , pp. 1031-1037
    • Druker, B.J.1    Talpaz, M.2    Resta, D.J.3    Peng, B.4    Buchdunger, E.5    Ford, J.M.6
  • 116
    • 0036216405 scopus 로고    scopus 로고
    • STI571 (Gleevec) as a paradigm for cancer therapy
    • Druker BJ. STI571 (Gleevec) as a paradigm for cancer therapy. Trends Mol Med 2002; 8: S14-8.
    • (2002) Trends Mol. Med. , vol.8
    • Druker, B.J.1
  • 117
    • 0035210658 scopus 로고    scopus 로고
    • Imatinib mesylate: Clinical results in Philadelphia chromosome-positive leukemias
    • Kantarjian HM, Talpaz M. Imatinib mesylate: clinical results in Philadelphia chromosome-positive leukemias. Semin Oncol 2001; 28: 9-18.
    • (2001) Semin. Oncol. , vol.28 , pp. 9-18
    • Kantarjian, H.M.1    Talpaz, M.2
  • 119
    • 0037085785 scopus 로고    scopus 로고
    • Imatinib induces durable hematologic and cytogenetic responses in patients with accelerated phase chronic myeloid leukemia: Results of a phase 2 study
    • Talpaz M, Silver RT, Druker BJ, Goldman JM, Gambacorti-Passerini C, Guilhot F, et al. Imatinib induces durable hematologic and cytogenetic responses in patients with accelerated phase chronic myeloid leukemia: results of a phase 2 study. Blood 2002; 99: 1928-37.
    • (2002) Blood , vol.99 , pp. 1928-1937
    • Talpaz, M.1    Silver, R.T.2    Druker, B.J.3    Goldman, J.M.4    Gambacorti-Passerini, C.5    Guilhot, F.6
  • 120
    • 0035800507 scopus 로고    scopus 로고
    • Clinical resistance to STI-571 cancer therapy caused by BCR-ABL gene mutation or amplification
    • Gorre ME, Mohammed M, Ellwood K, Hsu N, Paquette R, Rao PN, et al. Clinical resistance to STI-571 cancer therapy caused by BCR-ABL gene mutation or amplification. Science 2001; 293: 876-80.
    • (2001) Science , vol.293 , pp. 876-880
    • Gorre, M.E.1    Mohammed, M.2    Ellwood, K.3    Hsu, N.4    Paquette, R.5    Rao, P.N.6
  • 121
    • 0001686739 scopus 로고    scopus 로고
    • Multiple BCR-ABL kinase domain mutations confer polyclonal resistance to the tyrosine kinase inhibitor imatinib (STI571) in chronic phase and blast crisis chronic myeloid leukemia
    • Shah NP, Nicoll JM, Nagar B, Gorre ME, Paquette RL, Kuriyan J, et al. Multiple BCR-ABL kinase domain mutations confer polyclonal resistance to the tyrosine kinase inhibitor imatinib (STI571) in chronic phase and blast crisis chronic myeloid leukemia. Cancer Cell 2002; 2: 117-25.
    • (2002) Cancer Cell , vol.2 , pp. 117-125
    • Shah, N.P.1    Nicoll, J.M.2    Nagar, B.3    Gorre, M.E.4    Paquette, R.L.5    Kuriyan, J.6
  • 122
    • 0037045583 scopus 로고    scopus 로고
    • BCR-ABL gene mutations in relation to clinical resistance of Philadelphia-chromosome-positive leukaemia to STI571: A prospective study
    • von Bubnoff N, Schneller F, Peschel C, Duyster J. BCR-ABL gene mutations in relation to clinical resistance of Philadelphia-chromosome-positive leukaemia to STI571: a prospective study. Lancet 2002; 359: 487-91.
    • (2002) Lancet , vol.359 , pp. 487-491
    • von Bubnoff, N.1    Schneller, F.2    Peschel, C.3    Duyster, J.4
  • 123
    • 0036493544 scopus 로고    scopus 로고
    • Ph(+) acute lymphoblastic leukemia resistant to the tyrosine kinase inhibitor STI571 has a unique BCR-ABL gene mutation
    • Hofmann WK, Jones LC, Lemp NA, de Vos S, Gschaidmeier H, Hoelzer D, et al. Ph(+) acute lymphoblastic leukemia resistant to the tyrosine kinase inhibitor STI571 has a unique BCR-ABL gene mutation. Blood 2002; 99: 1860-2.
    • (2002) Blood , vol.99 , pp. 1860-1862
    • Hofmann, W.K.1    Jones, L.C.2    Lemp, N.A.3    de Vos, S.4    Gschaidmeier, H.5    Hoelzer, D.6
  • 124
    • 0037045589 scopus 로고    scopus 로고
    • Relation between resistance of Philadelphia-chromosome-positive acute lymphoblastic leukaemia to the tyrosine kinase inhibitor STI571 and gene-expression profiles: A gene-expression study
    • Hofmann WK, de Vos S, Elashoff D, Gschaidmeier H, Hoelzer D, Koeffler HP, et al. Relation between resistance of Philadelphia-chromosome-positive acute lymphoblastic leukaemia to the tyrosine kinase inhibitor STI571 and gene-expression profiles: a gene-expression study. Lancet 2002; 359: 481-6.
    • (2002) Lancet , vol.359 , pp. 481-486
    • Hofmann, W.K.1    de Vos, S.2    Elashoff, D.3    Gschaidmeier, H.4    Hoelzer, D.5    Koeffler, H.P.6
  • 125
    • 0036850514 scopus 로고    scopus 로고
    • Molecular and chromosomal mechanisms of resistance to imatinib (STI571) therapy
    • Hochhaus A, Kreil S, Corbin AS, La Rosee P, Muller MC, Lahaye T, et al. Molecular and chromosomal mechanisms of resistance to imatinib (STI571) therapy. Leukemia 2002; 16: 2190-6.
    • (2002) Leukemia , vol.16 , pp. 2190-2196
    • Hochhaus, A.1    Kreil, S.2    Corbin, A.S.3    La Rosee, P.4    Muller, M.C.5    Lahaye, T.6
  • 126
    • 0037438640 scopus 로고    scopus 로고
    • BCR-ABL independence and LYN kinase overexpression in chronic myelogenous leukemia cells selected for resistance to STI571
    • Donato NJ, Wu JY, Stapley J, Gallick G, Lin H, Arlinghaus R, et al. BCR-ABL independence and LYN kinase overexpression in chronic myelogenous leukemia cells selected for resistance to STI571. Blood 2003; 101: 690-8.
    • (2003) Blood , vol.101 , pp. 690-698
    • Donato, N.J.1    Wu, J.Y.2    Stapley, J.3    Gallick, G.4    Lin, H.5    Arlinghaus, R.6
  • 127
    • 0034095603 scopus 로고    scopus 로고
    • The pyrido[2,3-d]pyrimidine derivative PD180970 inhibits p210Bcr-Abl tyrosine kinase and induces apoptosis of K562 leukemic cells
    • Dorsey JF, Jove R, Kraker AJ, Wu J. The pyrido[2,3-d]pyrimidine derivative PD180970 inhibits p210Bcr-Abl tyrosine kinase and induces apoptosis of K562 leukemic cells. Cancer Res 2000: 60; 3127-31.
    • (2000) Cancer Res. , vol.60 , pp. 3127-3131
    • Dorsey, J.F.1    Jove, R.2    Kraker, A.J.3    Wu, J.4
  • 128
    • 0037115644 scopus 로고    scopus 로고
    • Activity of the Bcr-Abl kinase inhibitor PD180970 against clinically relevant Bcr-Abl isoforms that cause resistance to imatinib mesylate (Gleevec, STI571)
    • La Rosee P, Corbin AS, Stoffregen EP, Deininger MW, Druker BJ. Activity of the Bcr-Abl kinase inhibitor PD180970 against clinically relevant Bcr-Abl isoforms that cause resistance to imatinib mesylate (Gleevec, STI571). Cancer Res 2002; 62: 7149-53.
    • (2002) Cancer Res. , vol.62 , pp. 7149-7153
    • La Rosee, P.1    Corbin, A.S.2    Stoffregen, E.P.3    Deininger, M.W.4    Druker, B.J.5
  • 129
    • 0037153476 scopus 로고    scopus 로고
    • Selective pyrrolo-pyrimidine inhibitors reveal a necessary role for Src family kinases in Bcr-Abl signal transduction and oncogenesis
    • Wilson MB, Schreiner SJ, Choi HJ, Kamens J, Smithgall TE. Selective pyrrolo-pyrimidine inhibitors reveal a necessary role for Src family kinases in Bcr-Abl signal transduction and oncogenesis. Oncogene 2002; 21: 8075-88.
    • (2002) Oncogene , vol.21 , pp. 8075-8088
    • Wilson, M.B.1    Schreiner, S.J.2    Choi, H.J.3    Kamens, J.4    Smithgall, T.E.5
  • 130
    • 0141586702 scopus 로고    scopus 로고
    • The Src-selective kinase inhibitor PP1 also inhibits kit and Bcr-Abl tyrosine kinases
    • Tatton L, Morley GM, Chopra R, Khwaja A. The Src-selective kinase inhibitor PP1 also inhibits kit and Bcr-Abl tyrosine kinases. J Biol Chem 2002; 9: 9.
    • (2002) J. Biol. Chem. , vol.9 , pp. 9
    • Tatton, L.1    Morley, G.M.2    Chopra, R.3    Khwaja, A.4
  • 131
    • 0037439689 scopus 로고    scopus 로고
    • SKI-606, a 4-Anilino-3-quinolinecarbonitrile Dual Inhibitor of Src and Abl Kinases, Is a Potent Antiproliferative Agent against Chronic Myelogenous Leukemia Cells in Culture and Causes Regression of K562 Xenografts in Nude Mice
    • Golas JM, Arndt K, Etienne C, Lucas J, Nardin D, Gibbons J, et al. SKI-606, a 4-Anilino-3-quinolinecarbonitrile Dual Inhibitor of Src and Abl Kinases, Is a Potent Antiproliferative Agent against Chronic Myelogenous Leukemia Cells in Culture and Causes Regression of K562 Xenografts in Nude Mice. Cancer Res 2003; 63: 375-81.
    • (2003) Cancer Res. , vol.63 , pp. 375-381
    • Golas, J.M.1    Arndt, K.2    Etienne, C.3    Lucas, J.4    Nardin, D.5    Gibbons, J.6
  • 132
    • 0036682301 scopus 로고    scopus 로고
    • Crystal Structures of the Kinase Domain of c-Abl in Complex with the Small Molecule Inhibitorsnag and Imatinib (STI-571)
    • Nagar B, Bornmann WG, Pellicena P, Schindler T, Veach DR, Miller WT, et al. Crystal Structures of the Kinase Domain of c-Abl in Complex with the Small Molecule Inhibitorsnag and Imatinib (STI-571). Cancer Res 2002; 62: 4236-43.
    • (2002) Cancer Res. , vol.62 , pp. 4236-4243
    • Nagar, B.1    Bornmann, W.G.2    Pellicena, P.3    Schindler, T.4    Veach, D.R.5    Miller, W.T.6
  • 133
    • 0034693877 scopus 로고    scopus 로고
    • Role of Src expression and activation in human cancer
    • Irby RB, Yeatman TJ. Role of Src expression and activation in human cancer. Oncogene 2000; 19: 5636-42.
    • (2000) Oncogene , vol.19 , pp. 5636-5642
    • Irby, R.B.1    Yeatman, T.J.2
  • 135
    • 0037150728 scopus 로고    scopus 로고
    • Src in cancer: Deregulation and consequences for cell behaviour
    • 1602
    • Frame MC. Src in cancer: deregulation and consequences for cell behaviour. Biochim Biophys Acta 2002; 1602: 114-30.
    • (2002) Biochim. Biophys. Acta , pp. 114-130
    • Frame, M.C.1
  • 137
    • 0033546315 scopus 로고    scopus 로고
    • ErbB receptor-induced activation of stat transcription factors is mediated by Src tyrosine kinases
    • Olayioye MA, Beuvink I, Horsch K, Daly JM, Hynes NE. ErbB receptor-induced activation of stat transcription factors is mediated by Src tyrosine kinases. J Biol Chem 1999; 274: 17209-18.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17209-17218
    • Olayioye, M.A.1    Beuvink, I.2    Horsch, K.3    Daly, J.M.4    Hynes, N.E.5
  • 138
    • 0034614695 scopus 로고    scopus 로고
    • Stat3-mediated transformation of NIH-3T3 cells by the constitutively active Q205L Galphao protein
    • Ram PT, Horvath CM, Iyengar R. Stat3-mediated transformation of NIH-3T3 cells by the constitutively active Q205L Galphao protein. Science 2000; 287: 142-4.
    • (2000) Science , vol.287 , pp. 142-144
    • Ram, P.T.1    Horvath, C.M.2    Iyengar, R.3
  • 139
    • 0035952638 scopus 로고    scopus 로고
    • G protein coupled receptor signaling through the Src and Stat3 pathway: Role in proliferation and transformation
    • Ram PT, Iyengar R. G protein coupled receptor signaling through the Src and Stat3 pathway: role in proliferation and transformation. Oncogene 2001; 20: 1601-6.
    • (2001) Oncogene , vol.20 , pp. 1601-1606
    • Ram, P.T.1    Iyengar, R.2
  • 141
    • 0037064121 scopus 로고    scopus 로고
    • ErbB-2 activates Stat3 alpha in a Src- and JAK2-dependent manner
    • Ren Z, Schaefer TS. ErbB-2 activates Stat3 alpha in a Src- and JAK2-dependent manner. J Biol Chem 2002; 277: 38486-93.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38486-38493
    • Ren, Z.1    Schaefer, T.S.2
  • 142
    • 0029916933 scopus 로고    scopus 로고
    • Activation and association of Stat3 with Src in v-Src-transformed cell lines
    • Cao X, Tay A, Guy GR, Tan YH. Activation and association of Stat3 with Src in v-Src-transformed cell lines. Mol Cell Biol 1996; 16: 1595-603.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 1595-1603
    • Cao, X.1    Tay, A.2    Guy, G.R.3    Tan, Y.H.4
  • 143
    • 0031953831 scopus 로고    scopus 로고
    • Stat3 activation by Src induces specific gene regulation and is required for cell transformation
    • Turkson J, Bowman T, Garcia R, Caldenhoven E, De Groot RP, Jove R. Stat3 activation by Src induces specific gene regulation and is required for cell transformation. Mol Cell Biol 1998; 18: 2545-52.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 2545-2552
    • Turkson, J.1    Bowman, T.2    Garcia, R.3    Caldenhoven, E.4    De Groot, R.P.5    Jove, R.6
  • 145
    • 0035799531 scopus 로고    scopus 로고
    • Constitutive activation of Stat3 by the Src and JAK tyrosine kinases participates in growth regulation of human breast carcinoma cells
    • Garcia R, Bowman TL, Niu G, Yu H, Minton S, Muro-Cacho CA, et al. Constitutive activation of Stat3 by the Src and JAK tyrosine kinases participates in growth regulation of human breast carcinoma cells. Oncogene, 2001, 20, 2499-513.
    • (2001) Oncogene , vol.20 , pp. 2499-2513
    • Garcia, R.1    Bowman, T.L.2    Niu, G.3    Yu, H.4    Minton, S.5    Muro-Cacho, C.A.6
  • 146
    • 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: 2905-27.
    • (1999) Genes Dev. , vol.13 , pp. 2905-2927
    • Datta, S.R.1    Brunet, A.2    Greenberg, M.E.3
  • 147
    • 0036185848 scopus 로고    scopus 로고
    • The protein kinase B/Akt signalling pathway in human malignancy
    • Nicholson KM, Anderson NG. The protein kinase B/Akt signalling pathway in human malignancy. Cell Signal 2002; 14: 381-95.
    • (2002) Cell Signal , vol.14 , pp. 381-395
    • Nicholson, K.M.1    Anderson, N.G.2
  • 148
    • 0036632368 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-Kinase AKT pathway in human cancer
    • Vivanco I, Sawyers CL. The phosphatidylinositol 3-Kinase AKT pathway in human cancer. Nat Rev Cancer 2002; 2: 489-501.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 489-501
    • Vivanco, I.1    Sawyers, C.L.2
  • 150
    • 0035813230 scopus 로고    scopus 로고
    • Identification of tyrosine phosphorylation sites on 3-phosphoinositide-dependent protein kinase-1 and their role in regulating kinase activity
    • Park J, Hill MM, Hess D, Brazil DP, Hofsteenge J, Hemmings BA. Identification of tyrosine phosphorylation sites on 3-phosphoinositide-dependent protein kinase-1 and their role in regulating kinase activity. J Biol Chem 2001; 276: 37459-71.
    • (2001) J. Biol. Chem. , vol.276 , pp. 37459-37471
    • Park, J.1    Hill, M.M.2    Hess, D.3    Brazil, D.P.4    Hofsteenge, J.5    Hemmings, B.A.6
  • 152
    • 0034212787 scopus 로고    scopus 로고
    • No requirement for src family kinases for PDGF signaling in fibroblasts expressing SV40 large T antigen
    • Broome MA, Courtneidge SA. No requirement for src family kinases for PDGF signaling in fibroblasts expressing SV40 large T antigen. Oncogene 2000; 19: 2867-9.
    • (2000) Oncogene , vol.19 , pp. 2867-2869
    • Broome, M.A.1    Courtneidge, S.A.2
  • 153
    • 0033522510 scopus 로고    scopus 로고
    • Src family kinases are required for integrin but not PDGFR signal transduction
    • Klinghoffer RA, Sachsenmaier C, Cooper JA, Soriano P. Src family kinases are required for integrin but not PDGFR signal transduction. Embo J 1999; 18: 2459-71.
    • (1999) Embo J. , vol.18 , pp. 2459-2471
    • Klinghoffer, R.A.1    Sachsenmaier, C.2    Cooper, J.A.3    Soriano, P.4
  • 155
    • 0033538676 scopus 로고    scopus 로고
    • A dual inhibitor of platelet-derived growth factor beta-receptor and Src kinase activity potently interferes with motogenic and mitogenic responses to PDGF in vascular smooth muscle cells. A novel candidate for prevention of vascular remodeling
    • Waltenberger J, Uecker A, Krol J, Frank H, Mayr U, Bjorge JD, et al. A dual inhibitor of platelet-derived growth factor beta-receptor and Src kinase activity potently interferes with motogenic and mitogenic responses to PDGF in vascular smooth muscle cells. A novel candidate for prevention of vascular remodeling. Circ Res 1999; 85: 12-22.
    • (1999) Circ. Res. , vol.85 , pp. 12-22
    • Waltenberger, J.1    Uecker, A.2    Krol, J.3    Frank, H.4    Mayr, U.5    Bjorge, J.D.6
  • 156
  • 157
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies SP, Reddy H, Caivano M, Cohen P. 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    Cohen, P.4
  • 158
  • 159
    • 0032901378 scopus 로고    scopus 로고
    • Use of a drug-resistant mutant of stress-activated protein kinase 2a/p38 to validate the in vivo specificity of SB 203580
    • Eyers PA, van den IP, Quinlan RA, Goedert M, Cohen P. Use of a drug-resistant mutant of stress-activated protein kinase 2a/p38 to validate the in vivo specificity of SB 203580. FEBS Lett 1999; 451: 191-6.
    • (1999) FEBS Lett. , vol.451 , pp. 191-196
    • Eyers, P.A.1    van den, I.P.2    Quinlan, R.A.3    Goedert, M.4    Cohen, P.5
  • 160
    • 0032008085 scopus 로고    scopus 로고
    • Engineering Src family protein kinases with unnatural nucleotide specificity
    • Liu Y, Shah K, Yang F, Witucki L, Shokat KM. Engineering Src family protein kinases with unnatural nucleotide specificity. Chem Biol 1998; 5: 91-101.
    • (1998) Chem. Biol. , vol.5 , pp. 91-101
    • Liu, Y.1    Shah, K.2    Yang, F.3    Witucki, L.4    Shokat, K.M.5
  • 163
    • 0035947671 scopus 로고    scopus 로고
    • Identification of new JNK substrate using ATP pocket mutant JNK and a corresponding ATP analogue
    • Habelhah H, Shah K, Huang L, Burlingame AL, Shokat KM, Ronai Z. Identification of new JNK substrate using ATP pocket mutant JNK and a corresponding ATP analogue. J Biol Chem 2001; 276: 18090-5.
    • (2001) J. Biol. Chem. , vol.276 , pp. 18090-18095
    • Habelhah, H.1    Shah, K.2    Huang, L.3    Burlingame, A.L.4    Shokat, K.M.5    Ronai, Z.6
  • 165
    • 0036008093 scopus 로고    scopus 로고
    • A Chemical Genetic Screen for Direct v-Src Substrates Reveals Ordered Assembly of a Retrograde Signaling Pathway
    • Shah K, Shokat KM. A Chemical Genetic Screen for Direct v-Src Substrates Reveals Ordered Assembly of a Retrograde Signaling Pathway. Chem Biol 2002; 9: 35-47.
    • (2002) Chem. Biol. , vol.9 , pp. 35-47
    • Shah, K.1    Shokat, K.M.2
  • 166
    • 0032904762 scopus 로고    scopus 로고
    • A novel inhibitor of the tyrosine kinase Src suppresses phosphorylation of its major cellular substrates and reduces bone resorption in vitro and in rodent models in vivo
    • Missbach M, Jeschke M, Feyen J, Muller K, Glatt M, Green J, Susa M. A novel inhibitor of the tyrosine kinase Src suppresses phosphorylation of its major cellular substrates and reduces bone resorption in vitro and in rodent models in vivo. Bone 1999; 24: 437-49.
    • (1999) Bone , vol.24 , pp. 437-449
    • Missbach, M.1    Jeschke, M.2    Feyen, J.3    Muller, K.4    Glatt, M.5    Green, J.6    Susa, M.7
  • 167
    • 0034193789 scopus 로고    scopus 로고
    • Substituted 5,7-diphenyl-pyrrolo[2,3d] pyrimidines: Potent inhibitors of the tyrosine kinase c-Src
    • Missbach M, Altmann E, Widler L, Susa M, Buchdunger E, Mett, H, et al. Substituted 5,7-diphenyl-pyrrolo[2,3d] pyrimidines: potent inhibitors of the tyrosine kinase c-Src. Bioorg Med Chem Lett 2000; 10: 945-9.
    • (2000) Bioorg. Med. Chem. Lett. , vol.10 , pp. 945-949
    • Missbach, M.1    Altmann, E.2    Widler, L.3    Susa, M.4    Buchdunger, E.5    Mett, H.6
  • 168
    • 0035953060 scopus 로고    scopus 로고
    • 7-Pyrrolidinyl- and 7-piperidinyl-5-aryl-pyrrolo[2,3d]pyrimidines- potent inhibitors of the tyrosine kinase c-Src
    • Altmann E, Missbach M, Green J, Susa M, Wagenknecht HA, Widler L. 7-Pyrrolidinyl- and 7-piperidinyl-5-aryl-pyrrolo[2,3d]pyrimidines- potent inhibitors of the tyrosine kinase c-Src. Bioorg Med Chem Lett 2001; 11: 853-6.
    • (2001) Bioorg. Med. Chem. Lett. , vol.11 , pp. 853-856
    • Altmann, E.1    Missbach, M.2    Green, J.3    Susa, M.4    Wagenknecht, H.A.5    Widler, L.6
  • 169
    • 15644374929 scopus 로고    scopus 로고
    • Synthesis and tyrosine kinase inhibitory activity of a series of 2- amino-8H-pyrido[2,3-d] pyrimidines: Identification of potent, selective platelet-derived growth factor receptor tyrosine kinase inhibitors
    • Boschelli DH, Wu Z, Klutchko SR, Showalter HD, Hamby JM, Lu GH, et al. Synthesis and tyrosine kinase inhibitory activity of a series of 2- amino-8H-pyrido[2,3-d] pyrimidines: identification of potent, selective platelet-derived growth factor receptor tyrosine kinase inhibitors. J Med Chem 1998; 41: 4365-77.
    • (1998) J. Med. Chem. , vol.41 , pp. 4365-4377
    • Boschelli, D.H.1    Wu, Z.2    Klutchko, S.R.3    Showalter, H.D.4    Hamby, J.M.5    Lu, G.H.6
  • 170
    • 15444353988 scopus 로고    scopus 로고
    • 2-Substituted aminopyrido[2,3-d] pyrimidin-7(8H)-ones. structure- activity relationships against selected tyrosine kinases and in vitro and in vivo anticancer activity
    • Klutchko SR, Hamby JM, Boschelli DH, Wu Z, Kraker AJ, Amar AM, et al. 2-Substituted aminopyrido[2,3-d] pyrimidin-7(8H)-ones.
    • (1998) J. Med. Chem. , vol.41 , pp. 3276-3292
    • Klutchko, S.R.1    Hamby, J.M.2    Boschelli, D.H.3    Wu, Z.4    Kraker, A.J.5    Amar, A.M.6
  • 175
    • 0035829463 scopus 로고    scopus 로고
    • Optimization of 4-phenylamino-3-quinolinecarbo-nitriles as potent inhibitors of Src kinase activity
    • Boschelli DH, Ye F, Wang YD, Dutia M, Johnson SL, Wu B, et al. Optimization of 4-phenylamino-3-quinolinecarbo-nitriles as potent inhibitors of Src kinase activity. J Med Chem 2001; 44: 3965-77.
    • (2001) J. Med. Chem. , vol.44 , pp. 3965-3977
    • Boschelli, D.H.1    Ye, F.2    Wang, Y.D.3    Dutia, M.4    Johnson, S.L.5    Wu, B.6
  • 176
    • 0035282974 scopus 로고    scopus 로고
    • Synthesis and Src kinase inhibitory activity of a series of 4-phenylamino-3-quinolinecarbonitriles
    • Boschelli DH, Wang YD, Ye F, Wu B, Zhang N, Dutia M, et al. Synthesis and Src kinase inhibitory activity of a series of 4-phenylamino-3-quinolinecarbonitriles. J Med Chem 2001; 44: 822-33.
    • (2001) J. Med. Chem. , vol.44 , pp. 822-833
    • Boschelli, D.H.1    Wang, Y.D.2    Ye, F.3    Wu, B.4    Zhang, N.5    Dutia, M.6
  • 177
    • 0034613645 scopus 로고    scopus 로고
    • Inhibitors of src tyrosine kinase: The preparation and structure-activity relationship of 4-anilino-3-cyanoquino-lines and 4-anilinoquinazolines
    • Wang YD, Miller K, Boschelli DH, Ye F, Wu B, Floyd MB, et al. Inhibitors of src tyrosine kinase: the preparation and structure-activity relationship of 4-anilino-3-cyanoquino-lines and 4-anilinoquinazolines. Bioorg Med Chem Lett 2000; 10: 2477-80.
    • (2000) Bioorg. Med. Chem. Lett. , vol.10 , pp. 2477-2480
    • Wang, Y.D.1    Miller, K.2    Boschelli, D.H.3    Ye, F.4    Wu, B.5    Floyd, M.B.6
  • 178
    • 0035912929 scopus 로고    scopus 로고
    • Structural determinants for potent, selective dual site inhibition of human pp60c-src by 4-anilinoquinazolines
    • Tian G, Cory M, Smith AA, Knight WB. Structural determinants for potent, selective dual site inhibition of human pp60c-src by 4-anilinoquinazolines. Biochemistry 2001; 40: 7084-91.
    • (2001) Biochemistry , vol.40 , pp. 7084-7091
    • Tian, G.1    Cory, M.2    Smith, A.A.3    Knight, W.B.4
  • 179
    • 18344373265 scopus 로고    scopus 로고
    • Discovery and initial SAR of imidazoquinoxa-lines as inhibitors of the Src-family kinase p56(Lck)
    • Chen P, Norris D, Iwanowicz EJ, Spergel SH, Lin J, Gu HH, et al. Discovery and initial SAR of imidazoquinoxa-lines as inhibitors of the Src-family kinase p56(Lck). Bioorg Med Chem Lett 2002; 12: 1361-4.
    • (2002) Bioorg. Med. Chem. Lett. , vol.12 , pp. 1361-1364
    • Chen, P.1    Norris, D.2    Iwanowicz, E.J.3    Spergel, S.H.4    Lin, J.5    Gu, H.H.6
  • 180
    • 0034458943 scopus 로고    scopus 로고
    • SU6656, a selective src family kinase inhibitor, used to probe growth factor signaling
    • Blake RA, Broome MA, Liu X, Wu J, Gishizky M, Sun L, et al. SU6656, a selective src family kinase inhibitor, used to probe growth factor signaling. Mol Cell Biol 2000; 20: 9018-27.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 9018-9027
    • Blake, R.A.1    Broome, M.A.2    Liu, X.3    Wu, J.4    Gishizky, M.5    Sun, L.6
  • 182
    • 0033152210 scopus 로고    scopus 로고
    • Structural analysis of the lymphocyte-specific kinase Lck in complex with non-selective and Src family selective kinase inhibitors
    • Zhu X, Kim JL, Newcomb JR, Rose PE, Stover DR, Toledo LM, et al. Structural analysis of the lymphocyte-specific kinase Lck in complex with non-selective and Src family selective kinase inhibitors. Structure Fold Des 1999; 7: 651-61.
    • (1999) Structure Fold Des. , vol.7 , pp. 651-661
    • Zhu, X.1    Kim, J.L.2    Newcomb, J.R.3    Rose, P.E.4    Stover, D.R.5    Toledo, L.M.6
  • 184
    • 0034776809 scopus 로고    scopus 로고
    • Protein kinase C isozymes novel phorbol ester receptors and cancer chemotherapy
    • Barry OP, Kazanietz MG. Protein kinase C isozymes novel phorbol ester receptors and cancer chemotherapy. Curr Pharm Des 2001, 7(17): 1725-44.
    • (2001) Curr. Pharm. Des. , vol.7 , Issue.17 , pp. 1725-1744
    • Barry, O.P.1    Kazanietz, M.G.2
  • 185
    • 0036240794 scopus 로고    scopus 로고
    • The use of hematopoietic growth factors in the treatment of acute leukemia
    • Bradstock KF. The use of hematopoietic growth factors in the treatment of acute leukemia. Curr Pharm Des 2002; 8(5): 343-55.
    • (2002) Curr. Pharm. Des. , vol.8 , Issue.5 , pp. 343-355
    • Bradstock, K.F.1
  • 186
    • 0036372416 scopus 로고    scopus 로고
    • Targeting protein kinases for bone disease: Discovery and development of Src inhibitors
    • Metcalf CA 3rd, van Schravendijk MR, Dalgarno DC, Sawyer TK. Targeting protein kinases for bone disease: discovery and development of Src inhibitors. Curr Pharm Des 2002; 8(23): 2049-75.
    • (2002) Curr. Pharm. Des. , vol.8 , Issue.23 , pp. 2049-2075
    • Metcalf C.A. III1    van Schravendijk, M.R.2    Dalgarno, D.C.3    Sawyer, T.K.4


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