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Volumn 5, Issue 6, 2004, Pages 464-470

Juxtamembrane autoinhibition in receptor tyrosine kinases

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN TYROSINE KINASE;

EID: 2942594298     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm1399     Document Type: Review
Times cited : (251)

References (56)
  • 1
    • 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
  • 2
    • 0025343230 scopus 로고
    • Signal transduction by receptors with tyrosine kinase activity
    • Ullrich, A. & Schlessinger, J. Signal transduction by receptors with tyrosine kinase activity. Cell 61, 203-212 (1990).
    • (1990) Cell , vol.61 , pp. 203-212
    • Ullrich, A.1    Schlessinger, J.2
  • 3
    • 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
  • 4
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson, T. Protein modules and signalling networks. Nature 373, 573-580 (1995).
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 5
    • 0032493859 scopus 로고    scopus 로고
    • Switching signals on or off by receptor dimerization
    • Weiss, A. & Schlessinger, J. Switching signals on or off by receptor dimerization. Cell 94, 277-280 (1998).
    • (1998) Cell , vol.94 , pp. 277-280
    • Weiss, A.1    Schlessinger, J.2
  • 6
    • 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
  • 7
    • 0033779765 scopus 로고    scopus 로고
    • Single-molecule imaging of EGFR signalling on the surface of living cells
    • Sako, Y., Minoghchi, S. & Yanagida, T. Single-molecule imaging of EGFR signalling on the surface of living cells. Nature Cell Biol. 2, 168-172 (2000).
    • (2000) Nature Cell Biol. , vol.2 , pp. 168-172
    • Sako, Y.1    Minoghchi, S.2    Yanagida, T.3
  • 8
    • 0035979763 scopus 로고    scopus 로고
    • Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain
    • Moriki, T., Maruyama, H. & Maruyama, I. N. Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain. J. Mol. Biol. 311, 1011-1026 (2001). This paper provides evidence for inactive EGF receptor dimers on the cell surface and for the ligand-induced rotation of the transmembrane helices.
    • (2001) J. Mol. Biol. , vol.311 , pp. 1011-1026
    • Moriki, T.1    Maruyama, H.2    Maruyama, I.N.3
  • 9
    • 0031842104 scopus 로고    scopus 로고
    • Activation of Neu (ErbB-2) mediated by disulfide bond-induced dimerization reveals a receptor tyrosine kinase dimer interface
    • Burke, C. L. & Stern, D. F. Activation of Neu (ErbB-2) mediated by disulfide bond-induced dimerization reveals a receptor tyrosine kinase dimer interface. Mol. Cell. Biol. 18, 5371-5379 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5371-5379
    • Burke, C.L.1    Stern, D.F.2
  • 10
    • 0042346447 scopus 로고    scopus 로고
    • Oligomerization-induced modulation of TPR-MET tyrosine kinase activity
    • Hays, J. L. & Watowich, S. J. Oligomerization-induced modulation of TPR-MET tyrosine kinase activity. J. Biol. Chem. 278, 27456-27463 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 27456-27463
    • Hays, J.L.1    Watowich, S.J.2
  • 11
    • 0035960597 scopus 로고    scopus 로고
    • Dimerization-induced activation of soluble insulin/IGF-1 receptor kinases: An alternative mechanism of activation
    • Baer, K. et al. Dimerization-induced activation of soluble insulin/IGF-1 receptor kinases: an alternative mechanism of activation. Biochemistry 40, 14268-14278 (2001).
    • (2001) Biochemistry , vol.40 , pp. 14268-14278
    • Baer, K.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
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: Structural basis for regulation
    • Johnson, L. N., Noble, M. E. M. & Owen, D. J. Active and inactive protein kinases: structural basis for regulation. Cell 85, 149-158 (1996).
    • (1996) Cell , vol.85 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.M.2    Owen, D.J.3
  • 14
    • 0030766163 scopus 로고    scopus 로고
    • Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog
    • Hubbard, S. R. Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog. EMBO J. 16, 5572-5581 (1997).
    • (1997) EMBO J. , vol.16 , pp. 5572-5581
    • Hubbard, S.R.1
  • 15
    • 0026701674 scopus 로고
    • A highly conserved tyrosine residue at codon 845 within the kinase domain is not required for the transforming activity of human epidermal growth factor receptor
    • Gotoh, N., Tojo, A., Hino, M., Yazaki, Y. & Shibuya, M. A highly conserved tyrosine residue at codon 845 within the kinase domain is not required for the transforming activity of human epidermal growth factor receptor. Biochem. Biophys. Res. Commun. 186, 768-774 (1992).
    • (1992) Biochem. Biophys. Res. Commun. , vol.186 , pp. 768-774
    • Gotoh, N.1    Tojo, A.2    Hino, M.3    Yazaki, Y.4    Shibuya, M.5
  • 16
    • 0030922714 scopus 로고    scopus 로고
    • Insufficiency of self-phosphorylation for the activation of epidermal growth factor receptor
    • Sherrill, J. M. Insufficiency of self-phosphorylation for the activation of epidermal growth factor receptor. Biochem. 36, 5677-5684 (1997).
    • (1997) Biochem. , vol.36 , pp. 5677-5684
    • Sherrill, J.M.1
  • 17
    • 0141599428 scopus 로고    scopus 로고
    • Structure of the EGF receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor
    • Stamos, J., Sliwkowski, M. X. & Eigenbrot, C. Structure of the EGF receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor. J. Biol. Chem. 277, 46265-46272 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 46265-46272
    • Stamos, J.1    Sliwkowski, M.X.2    Eigenbrot, C.3
  • 18
    • 0034435424 scopus 로고    scopus 로고
    • Structure of the Tie2 RTK domain: Self-inhibition by the nucleotide binding loop, activation loop, and C-terminal tail
    • Shewchuk, L. M. et al. Structure of the Tie2 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
  • 19
    • 0037200045 scopus 로고    scopus 로고
    • Deletion of the carboxy-terminus of Tie2 enhances kinase activity, signaling, and function: Evidence for an autoinhibitory mechanism
    • Niu, X. L., Peters, K. G. & Kontos, C. D. Deletion of the carboxy-terminus of Tie2 enhances kinase activity, signaling, and function: evidence for an autoinhibitory mechanism, J. Biol. Chem. 277, 31768-31773 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 31768-31773
    • Niu, X.L.1    Peters, K.G.2    Kontos, C.D.3
  • 20
    • 0029032394 scopus 로고
    • A recurrent mutation in the tyrosine kinase domain of fibroblast growth factor receptor 3 causes hypochondroplasia
    • Bellus, G. A. et al. A recurrent mutation in the tyrosine kinase domain of fibroblast growth factor receptor 3 causes hypochondroplasia. Nature Genet. 10, 357-359 (1995).
    • (1995) Nature Genet. , vol.10 , pp. 357-359
    • Bellus, G.A.1
  • 21
    • 0028872752 scopus 로고
    • Thanatophoric dysplasia (types I and II) caused by distinct mutations in fibroblast growth factor receptor 3
    • Tavormina, P. L. et al. Thanatophoric dysplasia (types I and II) caused by distinct mutations in fibroblast growth factor receptor 3. Nature Genet. 9, 321-328 (1995).
    • (1995) Nature Genet. , vol.9 , pp. 321-328
    • Tavormina, P.L.1
  • 22
    • 0030297552 scopus 로고    scopus 로고
    • From form to function: Signaling by protein tyrosine phosphatases
    • Tonks, N. K. & Neel, B. G. From form to function: signaling by protein tyrosine phosphatases. Cell 87, 365-368 (1996).
    • (1996) Cell , vol.87 , pp. 365-368
    • Tonks, N.K.1    Neel, B.G.2
  • 23
    • 0021220257 scopus 로고
    • Protein kinase C phosphorylation of the EGF receptor at a threonine residue close to the cytoplasmic face of the plasma membrane
    • Hunter, T., Ling, N. & Cooper, J. A. Protein kinase C phosphorylation of the EGF receptor at a threonine residue close to the cytoplasmic face of the plasma membrane. Nature 311, 480-483 (1984).
    • (1984) Nature , vol.311 , pp. 480-483
    • Hunter, T.1    Ling, N.2    Cooper, J.A.3
  • 24
    • 0025333360 scopus 로고
    • Protein kinase-c activation inhibits tyrosine phosphorylation of the c-met protein
    • Gandino, L., Di Renzo, M. F., Giordano, S., Bussolino, F. & Comoglio, P. M. Protein kinase-c activation inhibits tyrosine phosphorylation of the c-met protein. Oncogene 5, 721-725 (1990).
    • (1990) Oncogene , vol.5 , pp. 721-725
    • Gandino, L.1    Di Renzo, M.F.2    Giordano, S.3    Bussolino, F.4    Comoglio, P.M.5
  • 25
    • 0033016108 scopus 로고    scopus 로고
    • Eph receptors and ephrins: Effectors of morphogenesis
    • Holder, N. & Klein, R. Eph receptors and ephrins: effectors of morphogenesis. Development 126, 2033-2044 (1999).
    • (1999) Development , vol.126 , pp. 2033-2044
    • Holder, N.1    Klein, R.2
  • 26
    • 0034693857 scopus 로고    scopus 로고
    • Eph receptors and ephrin ligands: Embryogenesis to tumorigenesis
    • Dodelet, V. C. & Pasquale, E. B. Eph receptors and ephrin ligands: embryogenesis to tumorigenesis. Oncogene 19, 5614-5619 (2000).
    • (2000) Oncogene , vol.19 , pp. 5614-5619
    • Dodelet, V.C.1    Pasquale, E.B.2
  • 27
    • 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
  • 28
    • 0023814924 scopus 로고
    • Mutation of the insulin receptor at tyrosine 960 inhibits signal transmission but does not affect its tyrosine kinase activity
    • White, M. F. et al. Mutation of the insulin receptor at tyrosine 960 inhibits signal transmission but does not affect its tyrosine kinase activity. Cell 54, 641-649 (1988).
    • (1988) Cell , vol.54 , pp. 641-649
    • White, M.F.1
  • 29
    • 0035929146 scopus 로고    scopus 로고
    • Structural basis for autoinhibition of the Ephb2 receptor tyrosine kinase by the unphosphorylated juxtamembrane region
    • Wybenga-Groot, L. E. Structural basis for autoinhibition of the Ephb2 receptor tyrosine kinase by the unphosphorylated juxtamembrane region. Cell 106, 745-757(2001). The first crystal structure to reveal how the juxtamembrane region of a receptor tyrosine kinase interacts with the kinase domain to suppress catalytic activity.
    • (2001) Cell , vol.106 , pp. 745-757
    • Wybenga-Groot, L.E.1
  • 30
    • 0038168241 scopus 로고    scopus 로고
    • Structural and biochemical evidence for an autoinhibitory role for tyrosine 984 in the juxtamembrane region of the insulin receptor
    • Li, S., Covino, N. D., Stein, E. G., Till, J. H. & Hubbard, S. R. Structural and biochemical evidence for an autoinhibitory role for tyrosine 984 in the juxtamembrane region of the insulin receptor. J. Biol. Chem. 278, 26007-26014 (2003). This work reveals the regulatory role of a non-phosphorylatable Tyr residue in the juxtamembrane region of the insulin receptor and of other receptor tyrosine kinases.
    • (2003) J. Biol. Chem. , vol.278 , pp. 26007-26014
    • Li, S.1    Covino, N.D.2    Stein, E.G.3    Till, J.H.4    Hubbard, S.R.5
  • 31
    • 0027400467 scopus 로고
    • Muscle-specific trk-related receptor with a kringle domain defines a distinct class of receptor tyrosine kinases
    • Jennings, C. G., Dyer, S. M. & Burden, S. J. Muscle-specific trk-related receptor with a kringle domain defines a distinct class of receptor tyrosine kinases. Proc. Natl Acad. Sci. USA 90, 2895-2899 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2895-2899
    • Jennings, C.G.1    Dyer, S.M.2    Burden, S.J.3
  • 32
    • 15844417385 scopus 로고    scopus 로고
    • The receptor tyrosine kinase MuSK is required for neuromuscular junction formation in vivo
    • DeChiara, T. M. et al. The receptor tyrosine kinase MuSK is required for neuromuscular junction formation in vivo. Cell 85, 501-512 (1996).
    • (1996) Cell , vol.85 , pp. 501-512
    • DeChiara, T.M.1
  • 33
    • 0034602844 scopus 로고    scopus 로고
    • The juxtamembrane region of MuSK has a critical role in agrin-mediated signaling
    • Herbst, R. & Burden, S. J. The juxtamembrane region of MuSK has a critical role in agrin-mediated signaling. EMBO J. 19, 67-77 (2000).
    • (2000) EMBO J. , vol.19 , pp. 67-77
    • Herbst, R.1    Burden, S.J.2
  • 34
    • 0036710123 scopus 로고    scopus 로고
    • Crystal structure of the MuSK tyrosine kinase: Insights into receptor autoregulation
    • Till, J. H. et al. Crystal structure of the MuSK tyrosine kinase: insights into receptor autoregulation. Structure 10, 1187-1196 (2002). This paper shows that MUSK kinase activity is suppressed by the activation segment by a mechanism similar to that used by the insulin receptor, and that the MUSK juxtamembrane region is disordered.
    • (2002) Structure , vol.10 , pp. 1187-1196
    • Till, J.H.1
  • 35
    • 0033524943 scopus 로고    scopus 로고
    • Crystal structure of the cytoplasmic domain of the type I TGFβ receptor in complex with FKBP12
    • Huse, M., Chen, Y. G., Massague, J. & Kuriyan, J. Crystal structure of the cytoplasmic domain of the type I TGFβ receptor in complex with FKBP12. Cell 96, 425-436 (1999).
    • (1999) Cell , vol.96 , pp. 425-436
    • Huse, M.1    Chen, Y.G.2    Massague, J.3    Kuriyan, J.4
  • 36
    • 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
  • 37
    • 0242670019 scopus 로고    scopus 로고
    • PDGFRA activating mutations in gastrointestinal stromal tumors
    • Heinrich, M. C. et al. PDGFRA activating mutations in gastrointestinal stromal tumors. Science 299, 708-710 (2003).
    • (2003) Science , vol.299 , pp. 708-710
    • Heinrich, M.C.1
  • 38
    • 0030451722 scopus 로고    scopus 로고
    • Internal tandem duplication of the flt3 gene found in acute myeloid leukemia
    • Nakao, M. et al. Internal tandem duplication of the flt3 gene found in acute myeloid leukemia. Leukemia 10, 1911-1918 (1996).
    • (1996) Leukemia , vol.10 , pp. 1911-1918
    • Nakao, M.1
  • 39
    • 0027251468 scopus 로고
    • Identification of two juxtamembrane autophosphorylation sites in the PDGFβ-receptor; involvement in the interaction with Src family tyrosine kinases
    • Mori, S. et al. Identification of two juxtamembrane autophosphorylation sites in the PDGFβ-receptor; involvement in the interaction with Src family tyrosine kinases. EMBO J. 12, 2257-2264 (1993).
    • (1993) EMBO J. , vol.12 , pp. 2257-2264
    • Mori, S.1
  • 40
    • 0032479283 scopus 로고    scopus 로고
    • Full activation of the platelet-derived growth factor β-receptor kinase involves multiple events
    • Baxter, M., Secrist, J. P., Vaillancourt, R. R. & Kazlauskas, A. Full activation of the platelet-derived growth factor β-receptor kinase involves multiple events. J. Biol. Chem. 273, 17050-17055 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 17050-17055
    • Baxter, M.1    Secrist, J.P.2    Vaillancourt, R.R.3    Kazlauskas, A.4
  • 41
    • 0842310394 scopus 로고    scopus 로고
    • The structural basis for autoinhibition of FLT3 by the juxtamembrane domain
    • Griffith, J. et al. The structural basis for autoinhibition of FLT3 by the juxtamembrane domain, Mol. Cell 13, 169-178 (2004). This study provides the structural basis by which the juxtamembrane region of FLT3, and of other PDGF receptor family members, interacts with the kinase domain to suppress catalytic activity.
    • (2004) Mol. Cell , vol.13 , pp. 169-178
    • Griffith, J.1
  • 42
    • 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
  • 43
    • 0037064087 scopus 로고    scopus 로고
    • Definition of an inhibitory juxtamembrane WW-like domain in the platelet-derived growth factor beta receptor
    • Irusta, P. M. et al. Definition of an inhibitory juxtamembrane WW-like domain in the platelet-derived growth factor beta receptor. J. Biol. Chem. 277, 38627-38634 (2002). This paper describes an extensive mutagenesis study of the juxtamembrane region of PDGF receptor-β.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38627-38634
    • Irusta, P.M.1
  • 44
    • 0037138411 scopus 로고    scopus 로고
    • WW and SH3 domains, two different scaffolds to recognize proline-rich ligands
    • Macias, M. J., Wiesner, S. & Sudol, M. WW and SH3 domains, two different scaffolds to recognize proline-rich ligands. FEBS Lett. 513, 30-37 (2002).
    • (2002) FEBS Lett. , vol.513 , pp. 30-37
    • Macias, M.J.1    Wiesner, S.2    Sudol, M.3
  • 45
    • 0037405026 scopus 로고    scopus 로고
    • Autoinhibition of the kit receptor tyrosine kinase by the cytosolic juxtamembrane region
    • Chan, P. M., Ilangumaran, S., La Rose, J., Chakrabartty, A. & Rottapel, R. Autoinhibition of the kit receptor tyrosine kinase by the cytosolic juxtamembrane region. Mol. Cell. Biol. 23, 3067-3078 (2003). This work provides evidence for an autonomously folded domain in the juxtamembrane region of KIT - a result that is not supported by the FLT3 crystal structure.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 3067-3078
    • Chan, P.M.1    Ilangumaran, S.2    La Rose, J.3    Chakrabartty, A.4    Rottapel, R.5
  • 46
    • 0042357240 scopus 로고    scopus 로고
    • Structure of a c-Kit product complex reveals the basis for kinase transactivation
    • Moi, C. D. et al. Structure of a c-Kit product complex reveals the basis for kinase transactivation. J. Biol. Chem. 278, 31461-31464 (2003). This study reveals the structure of the activated KIT kinase domain, in which the juxtamembrane region is Tyr phosphorylated.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31461-31464
    • Moi, C.D.1
  • 47
    • 0026356392 scopus 로고
    • Amino acid sequences Gly-Pro-Leu-Tyr and Asn-Pro-Glu-Tyr in the submembranous domain of the insulin receptor are required for normal endocytosis
    • Rajagopalan, M., Neidigh, J. L. & McClain, D. A. Amino acid sequences Gly-Pro-Leu-Tyr and Asn-Pro-Glu-Tyr in the submembranous domain of the insulin receptor are required for normal endocytosis. J. Biol. Chem. 266, 23068-23073 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 23068-23073
    • Rajagopalan, M.1    Neidigh, J.L.2    McClain, D.A.3
  • 48
    • 0028912999 scopus 로고
    • Phosphotyrosine-dependent interaction of SHC and insulin receptor substrate 1 with the NPEY motif of the insulin receptor via a novel non-SH2 domain
    • Gustafson, T. A., He, W., Craparo, A., Schaub, C. D. & O'Neill, T. J. Phosphotyrosine-dependent interaction of SHC and insulin receptor substrate 1 with the NPEY motif of the insulin receptor via a novel non-SH2 domain. Mol. Cell. Biol. 15, 2500-2508 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2500-2508
    • Gustafson, T.A.1    He, W.2    Craparo, A.3    Schaub, C.D.4    O'Neill, T.J.5
  • 49
    • 0024997853 scopus 로고
    • Receptor-mediated internalization of insulin requires a 12-amino acid sequence in the juxtamembrane region of the insulin receptor β-subunit
    • Backer, J. M., Kahn, C. R., Cahill, D. A., Ullrich, A. White, M. F. Receptor-mediated internalization of insulin requires a 12-amino acid sequence in the juxtamembrane region of the insulin receptor β-subunit. J. Biol. Chem. 265, 16450-16454 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 16450-16454
    • Backer, J.M.1    Kahn, C.R.2    Cahill, D.A.3    Ullrich, A.4    White, M.F.5
  • 50
    • 0030598848 scopus 로고    scopus 로고
    • Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism
    • Mohammadi, M., Schlessinger, J. & Hubbard, S. R. Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism. Cell 186, 577-587 (1996).
    • (1996) Cell , vol.186 , pp. 577-587
    • Mohammadi, M.1    Schlessinger, J.2    Hubbard, S.R.3
  • 51
    • 0033103867 scopus 로고    scopus 로고
    • Crystal structure of the kinase domain of human vascular endothelial growth factor receptor 2: A key enzyme in angiogenesis
    • McTigue, M. A. et al. Crystal structure of the kinase domain of human vascular endothelial growth factor receptor 2: a key enzyme in angiogenesis. Structure Fold. Des. 7, 319-330 (1999).
    • (1999) Structure Fold. Des. , vol.7 , pp. 319-330
    • McTigue, M.A.1
  • 52
    • 0035902180 scopus 로고    scopus 로고
    • Oncogenic kinase signalling
    • Blume-Jensen, P. & Hunter, T. Oncogenic kinase signalling. Nature 411, 355-365 (2001).
    • (2001) Nature , vol.411 , pp. 355-365
    • Blume-Jensen, P.1    Hunter, T.2
  • 53
    • 0034665713 scopus 로고    scopus 로고
    • Structural mechanism for STI-571 inhibition of Abelson tyrosine kinase
    • Schindler, T. et al. Structural mechanism for STI-571 inhibition of Abelson tyrosine kinase. Science 289, 1938-1942 (2000).
    • (2000) Science , vol.289 , pp. 1938-1942
    • Schindler, T.1
  • 54
    • 0036909260 scopus 로고    scopus 로고
    • Protein tyrosine kinases: Autoregulation and small-molecule inhibition
    • Hubbard, S. R. Protein tyrosine kinases: autoregulation and small-molecule inhibition. Curr. Opin. Struct. Biol. 12, 735-741 (2002).
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 735-741
    • Hubbard, S.R.1
  • 55
    • 0028582185 scopus 로고
    • Crystal structure of the tyrosine kinase domain of the human insulin receptor
    • Hubbard, S. R., Wei, L., Ellis, L. & Hendrickson, W. A. Crystal structure of the tyrosine kinase domain of the human insulin receptor, Nature 372, 746-754 (1994).
    • (1994) Nature , vol.372 , pp. 746-754
    • Hubbard, S.R.1    Wei, L.2    Ellis, L.3    Hendrickson, W.A.4
  • 56
    • 2942542387 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition and STI-571 Inhibition of c-Kit tyrosine kinase
    • 29 April (doi: 10.1074/jbc.M 403319200)
    • Mol C. D. et al. Structural basis for the autoinhibition and STI-571 Inhibition of c-Kit tyrosine kinase. J. Biol. Chem. 29 April 2004 (doi: 10.1074/jbc.M403319200).
    • (2004) J. Biol. Chem.
    • Mol, C.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.