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Volumn 94, Issue , 2015, Pages 9-25

Src protein-tyrosine kinase structure, mechanism, and small molecule inhibitors This paper is dedicated to the memory of Prof. Donald F. Steiner (1930-2014) - Advisor, mentor, and discoverer of proinsulin.

Author keywords

BCR Abl; Catalytic spine; Regulatory spine; SH2 domain; SH3 domain; Targeted cancer therapy

Indexed keywords

ADENOSINE TRIPHOSPHATE; ANTINEOPLASTIC AGENT; AZD 0424; BOSUTINIB; DASATINIB; MAGNESIUM ION; MEMBRANE PROTEIN; PHOSPHATASE; PONATINIB; PROTEIN SH1; PROTEIN SH2; PROTEIN SH3; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE KINASE INHIBITOR; SARACATINIB; SRC PROTEIN TYROSINE KINASE; UNCLASSIFIED DRUG; VANDETANIB; MAGNESIUM; MOLECULAR LIBRARY; PROTEIN KINASE INHIBITOR;

EID: 84923102615     PISSN: 10436618     EISSN: 10961186     Source Type: Journal    
DOI: 10.1016/j.phrs.2015.01.003     Document Type: Review
Times cited : (436)

References (107)
  • 1
    • 84979948588 scopus 로고
    • A sarcoma of the fowl transmissible by an agent separable from the tumor cells
    • P. Rous A sarcoma of the fowl transmissible by an agent separable from the tumor cells J Exp Med 13 1911 397 411
    • (1911) J Exp Med , vol.13 , pp. 397-411
    • Rous, P.1
  • 2
    • 0017250977 scopus 로고
    • DNA related to the transforming gene(s) of avian sarcoma viruses is present in normal avian DNA
    • D. Stehelin, H.E. Varmus, J.M. Bishop, and P.K. Vogt DNA related to the transforming gene(s) of avian sarcoma viruses is present in normal avian DNA Nature 260 1976 170 173
    • (1976) Nature , vol.260 , pp. 170-173
    • Stehelin, D.1    Varmus, H.E.2    Bishop, J.M.3    Vogt, P.K.4
  • 3
    • 0029896163 scopus 로고    scopus 로고
    • Regulation, substrates and functions of src
    • M.T. Brown, and J.A. Cooper Regulation, substrates and functions of src Biochim Biophys Acta 1287 1996 121 149
    • (1996) Biochim Biophys Acta , vol.1287 , pp. 121-149
    • Brown, M.T.1    Cooper, J.A.2
  • 4
    • 0031439247 scopus 로고    scopus 로고
    • Cellular functions regulated by Src family kinases
    • S.M. Thomas, and J.S. Brugge Cellular functions regulated by Src family kinases Annu Rev Cell Dev Biol 13 1997 513 609
    • (1997) Annu Rev Cell Dev Biol , vol.13 , pp. 513-609
    • Thomas, S.M.1    Brugge, J.S.2
  • 6
    • 84855795110 scopus 로고    scopus 로고
    • MEK1/2 dual-specificity protein kinases: Structure and regulation
    • R. Roskoski Jr. MEK1/2 dual-specificity protein kinases: structure and regulation Biochem Biophys Res Commun 417 2012 5 10
    • (2012) Biochem Biophys Res Commun , vol.417 , pp. 5-10
    • Roskoski, Jr.R.1
  • 8
    • 0028237509 scopus 로고
    • Cloning and characterisation of cDNAs encoding a novel non-receptor tyrosine kinase, brk, expressed in human breast tumours
    • P.J. Mitchell, K.T. Barker, J.E. Martindale, T. Kamalati, P.N. Lowe, and M.J. Page Cloning and characterisation of cDNAs encoding a novel non-receptor tyrosine kinase, brk, expressed in human breast tumours Oncogene 9 1994 2383 2390
    • (1994) Oncogene , vol.9 , pp. 2383-2390
    • Mitchell, P.J.1    Barker, K.T.2    Martindale, J.E.3    Kamalati, T.4    Lowe, P.N.5    Page, M.J.6
  • 10
    • 0024023829 scopus 로고
    • The first seven amino acids encoded by the v-src oncogene act as a myristylation signal: Lysine 7 is a critical determinant
    • J.M. Kaplan, G. Mardon, J.M. Bishop, and H.E. Varmus The first seven amino acids encoded by the v-src oncogene act as a myristylation signal: lysine 7 is a critical determinant Mol Cell Biol 8 1988 2435 2441
    • (1988) Mol Cell Biol , vol.8 , pp. 2435-2441
    • Kaplan, J.M.1    Mardon, G.2    Bishop, J.M.3    Varmus, H.E.4
  • 13
    • 84878259928 scopus 로고    scopus 로고
    • Polyproline-II helix in proteins: Structure and function
    • A.A. Adzhubei, M.J. Sternberg, and A.A. Makarov Polyproline-II helix in proteins: structure and function J Mol Biol 425 2013 2100 2132
    • (2013) J Mol Biol , vol.425 , pp. 2100-2132
    • Adzhubei, A.A.1    Sternberg, M.J.2    Makarov, A.A.3
  • 14
    • 84864622162 scopus 로고    scopus 로고
    • The language of SH2 domain interactions defines phosphotyrosine-mediated signal transduction
    • B.A. Liu, B.W. Engelmann, and P.D. Nash The language of SH2 domain interactions defines phosphotyrosine-mediated signal transduction FEBS Lett 586 2012 2597 2605
    • (2012) FEBS Lett , vol.586 , pp. 2597-2605
    • Liu, B.A.1    Engelmann, B.W.2    Nash, P.D.3
  • 15
    • 0028875162 scopus 로고
    • Recognition and specificity in protein tyrosine kinase-mediated signaling
    • Z. Songyang, and L.C. Cantley Recognition and specificity in protein tyrosine kinase-mediated signaling Trends Biochem Sci 20 1995 470 475
    • (1995) Trends Biochem Sci , vol.20 , pp. 470-475
    • Songyang, Z.1    Cantley, L.C.2
  • 16
    • 2142758178 scopus 로고    scopus 로고
    • Structure and specificity of the SH2 domain
    • G. Waksman, and J. Kuriyan Structure and specificity of the SH2 domain Cell 116 2004 S45 S48
    • (2004) Cell , vol.116 , pp. S45-S48
    • Waksman, G.1    Kuriyan, J.2
  • 17
    • 0034161405 scopus 로고    scopus 로고
    • A phosphotyrosine displacement mechanism for activation of Src by PTPα
    • X.M. Zheng, R.J. Resnick, and D. Shalloway A phosphotyrosine displacement mechanism for activation of Src by PTPα EMBO J 19 2000 964 978
    • (2000) EMBO J , vol.19 , pp. 964-978
    • Zheng, X.M.1    Resnick, R.J.2    Shalloway, D.3
  • 19
    • 0023649672 scopus 로고
    • c-src transforming ability by mutation of its primary sites of tyrosine phosphorylation
    • c-src transforming ability by mutation of its primary sites of tyrosine phosphorylation Cell 49 1987 65 73
    • (1987) Cell , vol.49 , pp. 65-73
    • Kmiecik, T.E.1    Shalloway, D.2
  • 21
    • 84869780894 scopus 로고    scopus 로고
    • Regulation of the Src family kinases by Csk
    • M. Odada Regulation of the Src family kinases by Csk Int J Biol Sci 8 2012 1385 1397
    • (2012) Int J Biol Sci , vol.8 , pp. 1385-1397
    • Odada, M.1
  • 22
    • 0031035740 scopus 로고    scopus 로고
    • Association of Csk-homologous kinase [CHK] [formerly MATK] with HER-2/ErbB-2 in breast cancer cells
    • S. Zrihan-Licht, J. Lim, I. Keydar, M.X. Sliwkowski, J.E. Groopman, and H. Avraham Association of Csk-homologous kinase [CHK] [formerly MATK] with HER-2/ErbB-2 in breast cancer cells J Biol Chem 272 1997 1856 1863
    • (1997) J Biol Chem , vol.272 , pp. 1856-1863
    • Zrihan-Licht, S.1    Lim, J.2    Keydar, I.3    Sliwkowski, M.X.4    Groopman, J.E.5    Avraham, H.6
  • 24
    • 0026342401 scopus 로고
    • Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • D.R. Knighton, J.H. Zheng, L.F. Ten Eyck, V.A. Ashford, N.H. Xuong, and S.S. Taylor Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase Science 253 1991 407 414
    • (1991) Science , vol.253 , pp. 407-414
    • Knighton, D.R.1    Zheng, J.H.2    Ten Eyck, L.F.3    Ashford, V.A.4    Xuong, N.H.5    Taylor, S.S.6
  • 25
    • 0037459341 scopus 로고    scopus 로고
    • Variation on an Src-like theme
    • S.C. Harrison Variation on an Src-like theme Cell 112 2003 737 740
    • (2003) Cell , vol.112 , pp. 737-740
    • Harrison, S.C.1
  • 26
    • 0033001789 scopus 로고    scopus 로고
    • Crystal structures of c-Src reveal features of its autoinhibitory mechanism
    • W. Xu, A. Doshi, M. Lei, M.J. Eck, and S.C. Harrison Crystal structures of c-Src reveal features of its autoinhibitory mechanism Mol Cell 3 1999 629 638
    • (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
  • 27
    • 17444374230 scopus 로고    scopus 로고
    • Src kinase regulation by phosphorylation and dephosphorylation
    • R. Roskoski Jr. Src kinase regulation by phosphorylation and dephosphorylation Biochem Biophys Res Commun 331 2005 1 14
    • (2005) Biochem Biophys Res Commun , vol.331 , pp. 1-14
    • Roskoski, Jr.R.1
  • 28
    • 0036330594 scopus 로고    scopus 로고
    • Effect of autophosphorylation on the catalytic and regulatory properties of protein tyrosine kinase Src
    • G. Sun, L. Ramdas, W. Wang, J. Vinci, J. McMurray, and R.J. Budde Effect of autophosphorylation on the catalytic and regulatory properties of protein tyrosine kinase Src Arch Biochem Biophys 397 2002 11 17
    • (2002) Arch Biochem Biophys , vol.397 , pp. 11-17
    • Sun, G.1    Ramdas, L.2    Wang, W.3    Vinci, J.4    McMurray, J.5    Budde, R.J.6
  • 29
    • 0036241054 scopus 로고    scopus 로고
    • EphrinB phosphorylation and reverse signaling: Regulation by Src kinases and PTP-BL phosphatase
    • A. Palmer, M. Zimmer, K.S. Erdmann, V. Eulenburg, A. Porthin, and R. Heumann EphrinB phosphorylation and reverse signaling: regulation by Src kinases and PTP-BL phosphatase Mol Cell 9 2002 725 737
    • (2002) Mol Cell , vol.9 , pp. 725-737
    • Palmer, A.1    Zimmer, M.2    Erdmann, K.S.3    Eulenburg, V.4    Porthin, A.5    Heumann, R.6
  • 30
    • 13544256790 scopus 로고    scopus 로고
    • Src protein-tyrosine kinase structure and regulation
    • R. Roskoski Jr. Src protein-tyrosine kinase structure and regulation Biochem Biophys Res Commun 324 2004 1155 1164
    • (2004) Biochem Biophys Res Commun , vol.324 , pp. 1155-1164
    • Roskoski, Jr.R.1
  • 31
    • 2442710106 scopus 로고    scopus 로고
    • A novel non-catalytic mechanism employed by the C-terminal Src-homologous kinase to inhibit Src-family kinase activity
    • Y.P. Chong, T.D. Mulhern, H.J. Zhu, D.J. Fujita, J.D. Bjorge, and J.P. Tantiongco A novel non-catalytic mechanism employed by the C-terminal Src-homologous kinase to inhibit Src-family kinase activity J Biol Chem 279 2004 20752 20766
    • (2004) J Biol Chem , vol.279 , pp. 20752-20766
    • Chong, Y.P.1    Mulhern, T.D.2    Zhu, H.J.3    Fujita, D.J.4    Bjorge, J.D.5    Tantiongco, J.P.6
  • 32
    • 0032563970 scopus 로고    scopus 로고
    • Autophosphorylation of Src and Yes blocks their inactivation by Csk phosphorylation
    • G. Sun, A.J. Sharma, and R.J. Budde Autophosphorylation of Src and Yes blocks their inactivation by Csk phosphorylation Oncogene 17 1998 1587 1595
    • (1998) Oncogene , vol.17 , pp. 1587-1595
    • Sun, G.1    Sharma, A.J.2    Budde, R.J.3
  • 33
    • 79551594605 scopus 로고    scopus 로고
    • Protein kinases: Evolution of dynamic regulatory proteins
    • S.S. Taylor, and A.P. Kornev Protein kinases: evolution of dynamic regulatory proteins Trends Biochem Sci 36 2011 65 77
    • (2011) Trends Biochem Sci , vol.36 , pp. 65-77
    • Taylor, S.S.1    Kornev, A.P.2
  • 34
    • 33845197964 scopus 로고    scopus 로고
    • Surface comparison of active and inactive protein kinases identifies a conserved activation mechanism
    • A.P. Kornev, N.M. Haste, S.S. Taylor, and L.F. Eyck Surface comparison of active and inactive protein kinases identifies a conserved activation mechanism Proc Natl Acad Sci U S A 103 2006 17783 17788
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 17783-17788
    • Kornev, A.P.1    Haste, N.M.2    Taylor, S.S.3    Eyck, L.F.4
  • 36
    • 0030887842 scopus 로고    scopus 로고
    • Engineering unnatural nucleotide specificity for Rous sarcoma virus tyrosine kinase to uniquely label its direct substrates
    • K. Shah, Y. Liu, C. Deirmengian, and K.M. Shokat Engineering unnatural nucleotide specificity for Rous sarcoma virus tyrosine kinase to uniquely label its direct substrates Proc Natl Acad Sci U S A 94 1997 3565 3570
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 3565-3570
    • Shah, K.1    Liu, Y.2    Deirmengian, C.3    Shokat, K.M.4
  • 37
    • 0031709073 scopus 로고    scopus 로고
    • A molecular gate which controls unnatural ATP analogue recognition by the tyrosine kinase v-Src
    • Y. Liu, K. Shah, F. Yang, L. Witucki, and K.M. Shokat A molecular gate which controls unnatural ATP analogue recognition by the tyrosine kinase v-Src Bioorg Med Chem 6 1998 1219 1226
    • (1998) Bioorg Med Chem , vol.6 , pp. 1219-1226
    • Liu, Y.1    Shah, K.2    Yang, F.3    Witucki, L.4    Shokat, K.M.5
  • 38
    • 65549152514 scopus 로고    scopus 로고
    • Equally potent inhibition of c-Src and Abl by compounds that recognize inactive kinase conformations
    • M.A. Seeliger, P. Ranjitkar, C. Kasap, Y. Shan, D.E. Shaw, and N.P. Shah Equally potent inhibition of c-Src and Abl by compounds that recognize inactive kinase conformations Cancer Res 69 2009 2384 2392
    • (2009) Cancer Res , vol.69 , pp. 2384-2392
    • Seeliger, M.A.1    Ranjitkar, P.2    Kasap, C.3    Shan, Y.4    Shaw, D.E.5    Shah, N.P.6
  • 39
    • 0028818886 scopus 로고
    • How do protein kinases discriminate between serine/threonine and tyrosine? Structural insights from the insulin receptor protein-tyrosine kinase
    • S.S. Taylor, E. Radzio-Andzelm, and T. Hunter How do protein kinases discriminate between serine/threonine and tyrosine? Structural insights from the insulin receptor protein-tyrosine kinase FASEB J 9 1995 1255 1266
    • (1995) FASEB J , vol.9 , pp. 1255-1266
    • Taylor, S.S.1    Radzio-Andzelm, E.2    Hunter, T.3
  • 40
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • W. Xu, S.C. Harrison, and M.J. Eck Three-dimensional structure of the tyrosine kinase c-Src Nature 385 1997 595 602
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 41
    • 0031578579 scopus 로고    scopus 로고
    • The 2.35 crystal structure of the inactivated form of chicken Src: A dynamic molecule with multiple regulatory interactions
    • J.C. Williams, A. Weijland, S. Gonfloni, A. Thompson, S.A. Courtneidge, and G. Superti-Furga The 2.35 crystal structure of the inactivated form of chicken Src: a dynamic molecule with multiple regulatory interactions J Mol Biol 274 1997 757 775
    • (1997) J Mol Biol , vol.274 , pp. 757-775
    • Williams, J.C.1    Weijland, A.2    Gonfloni, S.3    Thompson, A.4    Courtneidge, S.A.5    Superti-Furga, G.6
  • 42
    • 84897114242 scopus 로고    scopus 로고
    • A conserved water-mediated hydrogen bond network defines bosutinib's kinase selectivity
    • N.M. Levinson, and S.G. Boxer A conserved water-mediated hydrogen bond network defines bosutinib's kinase selectivity Nat Chem Biol 10 2014 127 132
    • (2014) Nat Chem Biol , vol.10 , pp. 127-132
    • Levinson, N.M.1    Boxer, S.G.2
  • 43
    • 0023885305 scopus 로고
    • The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains
    • S.K. Hanks, A.M. Quinn, and T. Hunter The protein kinase family: conserved features and deduced phylogeny of the catalytic domains Science 241 1988 42 52
    • (1988) Science , vol.241 , pp. 42-52
    • Hanks, S.K.1    Quinn, A.M.2    Hunter, T.3
  • 44
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • M. Huse, and J. Kuriyan The conformational plasticity of protein kinases Cell 109 2002 275 282
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 45
    • 0027407640 scopus 로고
    • Autoactivation of catalytic [Cα] subunit of cyclic AMP-dependent protein kinase by phosphorylation of threonine 197
    • R.A. Steinberg, R.D. Cauthron, M.M. Symcox, and H. Shuntoh Autoactivation of catalytic [Cα] subunit of cyclic AMP-dependent protein kinase by phosphorylation of threonine 197 Mol Cell Biol 13 1993 2332 2341
    • (1993) Mol Cell Biol , vol.13 , pp. 2332-2341
    • Steinberg, R.A.1    Cauthron, R.D.2    Symcox, M.M.3    Shuntoh, H.4
  • 46
    • 84891836984 scopus 로고    scopus 로고
    • Locking the active conformation of c-Src kinase through the phosphorylation of the activation loop
    • Y. Meng, and B. Roux Locking the active conformation of c-Src kinase through the phosphorylation of the activation loop J Mol Biol 426 2014 423 435
    • (2014) J Mol Biol , vol.426 , pp. 423-435
    • Meng, Y.1    Roux, B.2
  • 47
    • 33745298429 scopus 로고    scopus 로고
    • Rational design of inhibitors that bind to inactive kinase conformations
    • Y. Liu, and N.S. Gray Rational design of inhibitors that bind to inactive kinase conformations Nat Chem Biol 2 2006 358 364
    • (2006) Nat Chem Biol , vol.2 , pp. 358-364
    • Liu, Y.1    Gray, N.S.2
  • 48
    • 0003481596 scopus 로고
    • 2nd ed. WH Freeman and Company New York
    • A. Fersht Enzyme structure and mechanism 2nd ed. 1985 WH Freeman and Company New York 105 106
    • (1985) Enzyme Structure and Mechanism , pp. 105-106
    • Fersht, A.1
  • 49
    • 0031048501 scopus 로고    scopus 로고
    • Requirement for an additional divalent metal cation to activate protein tyrosine kinases
    • G. Sun, and R.J. Budde Requirement for an additional divalent metal cation to activate protein tyrosine kinases Biochemistry 36 1997 2139 2146
    • (1997) Biochemistry , vol.36 , pp. 2139-2146
    • Sun, G.1    Budde, R.J.2
  • 50
    • 0020478357 scopus 로고
    • Adenosine cyclic 3′,5′-monophosphate dependent protein kinase: Kinetic mechanism for the bovine skeletal muscle catalytic subunit
    • P.F. Cook, M.E. Neville Jr., K.E. Vrana, F.T. Hartl, and R. Roskoski Jr. Adenosine cyclic 3′,5′-monophosphate dependent protein kinase: kinetic mechanism for the bovine skeletal muscle catalytic subunit Biochemistry 21 1982 5794 5799
    • (1982) Biochemistry , vol.21 , pp. 5794-5799
    • Cook, P.F.1    Neville, Jr.M.E.2    Vrana, K.E.3    Hartl, F.T.4    Roskoski, Jr.R.5
  • 51
    • 77950640166 scopus 로고    scopus 로고
    • Differential effects of divalent manganese and magnesium on the kinase activity of leucine-rich repeat kinase 2 [LRRK2]
    • B. Lovitt, E.C. Vanderporten, Z. Sheng, H. Zhu, J. Drummond, and Y. Liu Differential effects of divalent manganese and magnesium on the kinase activity of leucine-rich repeat kinase 2 [LRRK2] Biochemistry 49 2010 3092 3100
    • (2010) Biochemistry , vol.49 , pp. 3092-3100
    • Lovitt, B.1    Vanderporten, E.C.2    Sheng, Z.3    Zhu, H.4    Drummond, J.5    Liu, Y.6
  • 52
    • 77953243551 scopus 로고    scopus 로고
    • Kinetic mechanistic studies of Cdk5/p25-catalyzed H1P phosphorylation: Metal effect and solvent kinetic isotope effect
    • M. Liu, E. Girma, M.A. Glicksman, and R.L. Stein Kinetic mechanistic studies of Cdk5/p25-catalyzed H1P phosphorylation: metal effect and solvent kinetic isotope effect Biochemistry 49 2010 4921 4929
    • (2010) Biochemistry , vol.49 , pp. 4921-4929
    • Liu, M.1    Girma, E.2    Glicksman, M.A.3    Stein, R.L.4
  • 53
    • 0037452906 scopus 로고    scopus 로고
    • Physiological concentrations of divalent magnesium ion activate the serine/threonine specific protein kinase ERK2
    • W.F. Waas, and K.N. Dalby Physiological concentrations of divalent magnesium ion activate the serine/threonine specific protein kinase ERK2 Biochemistry 42 2003 2960 2970
    • (2003) Biochemistry , vol.42 , pp. 2960-2970
    • Waas, W.F.1    Dalby, K.N.2
  • 55
    • 0023873834 scopus 로고
    • Role of divalent metals in the kinetic mechanism of insulin receptor tyrosine kinase
    • P.P. Vicario, R. Saperstein, and A. Bennun Role of divalent metals in the kinetic mechanism of insulin receptor tyrosine kinase Arch Biochem Biophys 261 1988 336 345
    • (1988) Arch Biochem Biophys , vol.261 , pp. 336-345
    • Vicario, P.P.1    Saperstein, R.2    Bennun, A.3
  • 56
    • 0032497373 scopus 로고    scopus 로고
    • A second magnesium ion is critical for ATP binding in the kinase domain of the oncoprotein v-Fps
    • P. Saylor, C. Wang, T.J. Hirai, and J.A. Adams A second magnesium ion is critical for ATP binding in the kinase domain of the oncoprotein v-Fps Biochemistry 37 1998 12624 12630
    • (1998) Biochemistry , vol.37 , pp. 12624-12630
    • Saylor, P.1    Wang, C.2    Hirai, T.J.3    Adams, J.A.4
  • 57
    • 84866507956 scopus 로고    scopus 로고
    • Price to be paid for two-metal catalysis: Magnesium ions that accelerate chemistry unavoidably limit product release from a protein kinase
    • D.M. Jacobsen, Z.Q. Bao, P. O'Brien, C.L. Brooks 3rd, and M.A. Young Price to be paid for two-metal catalysis: magnesium ions that accelerate chemistry unavoidably limit product release from a protein kinase J Am Chem Soc 134 2012 15357 15370
    • (2012) J Am Chem Soc , vol.134 , pp. 15357-15370
    • Jacobsen, D.M.1    Bao, Z.Q.2    O'Brien, P.3    Brooks, C.L.4    Young, M.A.5
  • 58
    • 64549137956 scopus 로고    scopus 로고
    • Activation loop phosphorylation modulates Bruton's tyrosine kinase [Btk] kinase domain activity
    • L. Lin, R. Czerwinski, K. Kelleher, M.M. Siegel, P. Wu, and R. Kriz Activation loop phosphorylation modulates Bruton's tyrosine kinase [Btk] kinase domain activity Biochemistry 48 2009 2021 2032
    • (2009) Biochemistry , vol.48 , pp. 2021-2032
    • Lin, L.1    Czerwinski, R.2    Kelleher, K.3    Siegel, M.M.4    Wu, P.5    Kriz, R.6
  • 59
    • 0037059757 scopus 로고    scopus 로고
    • Comparison of the biochemical and kinetic properties of the type 1 receptor tyrosine kinase intracellular domains. Demonstration of differential sensitivity to kinase inhibitors
    • P.S. Brignola, K. Lackey, S.H. Kadwell, C. Hoffman, E. Horne, and H.L. Carter Comparison of the biochemical and kinetic properties of the type 1 receptor tyrosine kinase intracellular domains. Demonstration of differential sensitivity to kinase inhibitors J Biol Chem 277 2002 1576 1585
    • (2002) J Biol Chem , vol.277 , pp. 1576-1585
    • Brignola, P.S.1    Lackey, K.2    Kadwell, S.H.3    Hoffman, C.4    Horne, E.5    Carter, H.L.6
  • 60
    • 0031239098 scopus 로고    scopus 로고
    • Expression, purification, and initial characterization of human Yes protein tyrosine kinase from a bacterial expression system
    • G. Sun, and R.J. Budde Expression, purification, and initial characterization of human Yes protein tyrosine kinase from a bacterial expression system Arch Biochem Biophys 345 1997 135 142
    • (1997) Arch Biochem Biophys , vol.345 , pp. 135-142
    • Sun, G.1    Budde, R.J.2
  • 61
    • 0032564322 scopus 로고    scopus 로고
    • Characterization and kinetic mechanism of catalytic domain of human vascular endothelial growth factor receptor-2 tyrosine kinase [VEGFR2 TK], a key enzyme in angiogenesis
    • C.V. Parast, B. Mroczkowski, C. Pinko, S. Misialek, G. Khambatta, and K. Appelt Characterization and kinetic mechanism of catalytic domain of human vascular endothelial growth factor receptor-2 tyrosine kinase [VEGFR2 TK], a key enzyme in angiogenesis Biochemistry 37 1998 16788 16801
    • (1998) Biochemistry , vol.37 , pp. 16788-16801
    • Parast, C.V.1    Mroczkowski, B.2    Pinko, C.3    Misialek, S.4    Khambatta, G.5    Appelt, K.6
  • 62
    • 0018780602 scopus 로고
    • Magnetic resonance and kinetic studies of the manganese [II] ion and substrate complexes of the catalytic subunit of adenosine 3′,5′-monophosphate dependent protein kinase from bovine heart
    • R.N. Armstrong, H. Kondo, J. Granot, E.T. Kaiser, and A.S. Mildvan Magnetic resonance and kinetic studies of the manganese [II] ion and substrate complexes of the catalytic subunit of adenosine 3′,5′-monophosphate dependent protein kinase from bovine heart Biochemistry 18 1979 1230 1238
    • (1979) Biochemistry , vol.18 , pp. 1230-1238
    • Armstrong, R.N.1    Kondo, H.2    Granot, J.3    Kaiser, E.T.4    Mildvan, A.S.5
  • 63
    • 0027408171 scopus 로고
    • Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor
    • J. Zheng, D.R. Knighton, L.F. ten Eyck, R. Karlsson, N. Xuong, and S.S. Taylor Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor Biochemistry 32 1993 2154 2161
    • (1993) Biochemistry , vol.32 , pp. 2154-2161
    • Zheng, J.1    Knighton, D.R.2    Ten Eyck, L.F.3    Karlsson, R.4    Xuong, N.5    Taylor, S.S.6
  • 64
    • 0027504169 scopus 로고
    • Divalent metal ions influence catalysis and active-site accessibility in the cAMP-dependent protein kinase
    • J.A. Adams, and S.S. Taylor Divalent metal ions influence catalysis and active-site accessibility in the cAMP-dependent protein kinase Protein Sci 2 1993 2177 2186
    • (1993) Protein Sci , vol.2 , pp. 2177-2186
    • Adams, J.A.1    Taylor, S.S.2
  • 65
    • 0031444107 scopus 로고    scopus 로고
    • Participation of ADP dissociation in the rate-determining step in cAMP-dependent protein kinase
    • J. Zhou, and J.A. Adams Participation of ADP dissociation in the rate-determining step in cAMP-dependent protein kinase Biochemistry 36 1997 15733 15738
    • (1997) Biochemistry , vol.36 , pp. 15733-15738
    • Zhou, J.1    Adams, J.A.2
  • 66
    • 0035413606 scopus 로고    scopus 로고
    • Kinetic and catalytic mechanisms of protein kinases
    • J.A. Adams Kinetic and catalytic mechanisms of protein kinases Chem Rev 101 2001 2271 2290
    • (2001) Chem Rev , vol.101 , pp. 2271-2290
    • Adams, J.A.1
  • 67
  • 70
    • 84878095831 scopus 로고    scopus 로고
    • Protein kinase inhibitor design by targeting the Asp-Phe-Gly [DFG] motif: The role of the DFG motif in the design of epidermal growth factor receptor inhibitors
    • Y.H. Peng, H.Y. Shiao, C.H. Tu, P.M. Liu, J.T. Hsu, and P.K. Amancha Protein kinase inhibitor design by targeting the Asp-Phe-Gly [DFG] motif: the role of the DFG motif in the design of epidermal growth factor receptor inhibitors J Med Chem 56 2013 3889 3903
    • (2013) J Med Chem , vol.56 , pp. 3889-3903
    • Peng, Y.H.1    Shiao, H.Y.2    Tu, C.H.3    Liu, P.M.4    Hsu, J.T.5    Amancha, P.K.6
  • 71
    • 84890041471 scopus 로고    scopus 로고
    • The ErbB/HER family of protein-tyrosine kinases and cancer
    • R. Roskoski Jr. The ErbB/HER family of protein-tyrosine kinases and cancer Pharmacol Res 79 2014 34 74
    • (2014) Pharmacol Res , vol.79 , pp. 34-74
    • Roskoski, Jr.R.1
  • 72
    • 84903581634 scopus 로고    scopus 로고
    • ErbB/HER protein-tyrosine kinases: Structures and small molecule inhibitors
    • R. Roskoski Jr. ErbB/HER protein-tyrosine kinases: structures and small molecule inhibitors Pharmacol Res 87 2014 42 59
    • (2014) Pharmacol Res , vol.87 , pp. 42-59
    • Roskoski, Jr.R.1
  • 73
    • 84902449207 scopus 로고    scopus 로고
    • Targeting receptor tyrosine kinase MET in cancer: Small molecule inhibitors and clinical progress
    • J.J. Cui Targeting receptor tyrosine kinase MET in cancer: small molecule inhibitors and clinical progress J Med Chem 57 2014 4427 4453
    • (2014) J Med Chem , vol.57 , pp. 4427-4453
    • Cui, J.J.1
  • 74
    • 84856020870 scopus 로고    scopus 로고
    • Targeting c-Met as a promising strategy for the treatment of hepatocellular carcinoma
    • J. Gao, Y. Inagaki, P. Song, X. Qu, N. Kokudo, and W. Tang Targeting c-Met as a promising strategy for the treatment of hepatocellular carcinoma Pharmacol Res 65 2012 23 30
    • (2012) Pharmacol Res , vol.65 , pp. 23-30
    • Gao, J.1    Inagaki, Y.2    Song, P.3    Qu, X.4    Kokudo, N.5    Tang, W.6
  • 75
    • 84890467312 scopus 로고    scopus 로고
    • Targeting the PDGF signaling pathway in tumor treatment
    • C.H. Heldin Targeting the PDGF signaling pathway in tumor treatment Cell Commun Signal 11 2013 97
    • (2013) Cell Commun Signal , vol.11 , pp. 97
    • Heldin, C.H.1
  • 77
    • 84881523535 scopus 로고    scopus 로고
    • Targeting the insulin-like growth factor-1 receptor in human cancer
    • A. Arcaro Targeting the insulin-like growth factor-1 receptor in human cancer Front Pharmacol 4 2013 30
    • (2013) Front Pharmacol , vol.4 , pp. 30
    • Arcaro, A.1
  • 78
    • 79959713140 scopus 로고    scopus 로고
    • Fibroblast growth factors and their receptors in cancer
    • J. Wesche, K. Haglund, and E.M. Haugsten Fibroblast growth factors and their receptors in cancer Biochem J 437 2011 199 213
    • (2011) Biochem J , vol.437 , pp. 199-213
    • Wesche, J.1    Haglund, K.2    Haugsten, E.M.3
  • 79
    • 84857916018 scopus 로고    scopus 로고
    • Targeting Src family kinases in anti-cancer therapies: Turning promise into triumph
    • S. Zhang, and D. Yu Targeting Src family kinases in anti-cancer therapies: turning promise into triumph Trends Pharmacol Sci 33 2012 122 128
    • (2012) Trends Pharmacol Sci , vol.33 , pp. 122-128
    • Zhang, S.1    Yu, D.2
  • 80
    • 0037470819 scopus 로고    scopus 로고
    • Protein prenylation: A pivotal posttranslational process
    • R. Roskoski Jr. Protein prenylation: a pivotal posttranslational process Biochem Biophys Res Commun 303 2003 1 7
    • (2003) Biochem Biophys Res Commun , vol.303 , pp. 1-7
    • Roskoski, Jr.R.1
  • 81
    • 79956283619 scopus 로고    scopus 로고
    • Current status of SRC inhibitors in solid tumor malignancies
    • L.N. Puls, M. Eadens, and W. Messersmith Current status of SRC inhibitors in solid tumor malignancies Oncologist 16 2011 566 578
    • (2011) Oncologist , vol.16 , pp. 566-578
    • Puls, L.N.1    Eadens, M.2    Messersmith, W.3
  • 82
    • 84857090723 scopus 로고    scopus 로고
    • Phase i study of bosutinib, a src/abl tyrosine kinase inhibitor, administered to patients with advanced solid tumors
    • A.I. Daud, S.S. Krishnamurthi, M.N. Saleh, B.J. Gitlitz, M.J. Borad, and P.J. Gold Phase I study of bosutinib, a src/abl tyrosine kinase inhibitor, administered to patients with advanced solid tumors Clin Cancer Res 18 2012 1092 1100
    • (2012) Clin Cancer Res , vol.18 , pp. 1092-1100
    • Daud, A.I.1    Krishnamurthi, S.S.2    Saleh, M.N.3    Gitlitz, B.J.4    Borad, M.J.5    Gold, P.J.6
  • 83
    • 84898449429 scopus 로고    scopus 로고
    • Bosutinib in combination with the aromatase inhibitor letrozole: A phase II trial in postmenopausal women evaluating first-line endocrine therapy in locally advanced or metastatic hormone receptor-positive/HER2-negative breast cancer
    • B. Moy, P. Neven, F. Lebrun, M. Bellet, B. Xu, and T. Sarosiek Bosutinib in combination with the aromatase inhibitor letrozole: a phase II trial in postmenopausal women evaluating first-line endocrine therapy in locally advanced or metastatic hormone receptor-positive/HER2-negative breast cancer Oncologist 19 2014 348 349
    • (2014) Oncologist , vol.19 , pp. 348-349
    • Moy, B.1    Neven, P.2    Lebrun, F.3    Bellet, M.4    Xu, B.5    Sarosiek, T.6
  • 84
    • 77956072809 scopus 로고    scopus 로고
    • Dasatinib: A potent SRC inhibitor in clinical development for the treatment of solid tumors
    • J. Araujo, and C. Logothetis Dasatinib: a potent SRC inhibitor in clinical development for the treatment of solid tumors Cancer Treat Rev 36 2010 492 500
    • (2010) Cancer Treat Rev , vol.36 , pp. 492-500
    • Araujo, J.1    Logothetis, C.2
  • 86
    • 84890451764 scopus 로고    scopus 로고
    • The discovery and development of vandetanib for the treatment of thyroid cancer
    • M.W. Sim, and M.S. Cohen The discovery and development of vandetanib for the treatment of thyroid cancer Expert Opin Drug Discov 9 2014 105 114
    • (2014) Expert Opin Drug Discov , vol.9 , pp. 105-114
    • Sim, M.W.1    Cohen, M.S.2
  • 87
    • 84899049029 scopus 로고    scopus 로고
    • Phase II randomized study of vandetanib plus gemcitabine or gemcitabine plus placebo as first-line treatment of advanced non-small-cell lung cancer in elderly patients
    • C. Gridelli, S. Novello, N. Zilembo, A. Luciani, A.G. Favaretto, and F. De Marinis Phase II randomized study of vandetanib plus gemcitabine or gemcitabine plus placebo as first-line treatment of advanced non-small-cell lung cancer in elderly patients J Thorac Oncol 9 2014 733 737
    • (2014) J Thorac Oncol , vol.9 , pp. 733-737
    • Gridelli, C.1    Novello, S.2    Zilembo, N.3    Luciani, A.4    Favaretto, A.G.5    De Marinis, F.6
  • 88
    • 84887617202 scopus 로고    scopus 로고
    • A randomized, phase II study of vandetanib maintenance for advanced or metastatic non-small-cell lung cancer following first-line platinum-doublet chemotherapy
    • J.S. Ahn, K.H. Lee, J.M. Sun, K. Park, E.S. Kang, and E.K. Cho A randomized, phase II study of vandetanib maintenance for advanced or metastatic non-small-cell lung cancer following first-line platinum-doublet chemotherapy Lung Cancer 82 2013 455 460
    • (2013) Lung Cancer , vol.82 , pp. 455-460
    • Ahn, J.S.1    Lee, K.H.2    Sun, J.M.3    Park, K.4    Kang, E.S.5    Cho, E.K.6
  • 89
    • 84891830024 scopus 로고    scopus 로고
    • A phase II trial of saracatinib, an inhibitor of src kinases, in previously-treated advanced non-small-cell lung cancer: The Princess Margaret Hospital phase II consortium
    • S.A. Laurie, G.D. Goss, F.A. Shepherd, M.N. Reaume, G. Nicholas, and L. Philip A phase II trial of saracatinib, an inhibitor of src kinases, in previously-treated advanced non-small-cell lung cancer: the Princess Margaret Hospital phase II consortium Clin Lung Cancer 15 2014 52 57
    • (2014) Clin Lung Cancer , vol.15 , pp. 52-57
    • Laurie, S.A.1    Goss, G.D.2    Shepherd, F.A.3    Reaume, M.N.4    Nicholas, G.5    Philip, L.6
  • 90
    • 1642339546 scopus 로고    scopus 로고
    • 7-Alkoxy-4-phenylamino-3-quinolinecarbonitriles as dual inhibitors of Src and Abl kinases
    • D.H. Boschelli, Y.D. Wang, S. Johnson, B. Wu, F. Ye, and A.C. Barrios Sosa 7-Alkoxy-4-phenylamino-3-quinolinecarbonitriles as dual inhibitors of Src and Abl kinases J Med Chem 47 2004 1599 1601
    • (2004) J Med Chem , vol.47 , pp. 1599-1601
    • Boschelli, D.H.1    Wang, Y.D.2    Johnson, S.3    Wu, B.4    Ye, F.5    Barrios Sosa, A.C.6
  • 91
    • 19944428353 scopus 로고    scopus 로고
    • Discovery of N-(2-chloro-6-methyl-phenyl)-2-(6-(4-(2-hydroxyethyl)- piperazin-1-yl)-2-methylpyrimidin-4-ylamino)thiazole-5-carboxamide (BMS-354825), a dual Src/Abl kinase inhibitor with potent antitumor activity in preclinical assays
    • L.J. Lombardo, F.Y. Lee, P. Chen, D. Norris, J.C. Barrish, and K. Behnia Discovery of N-(2-chloro-6-methyl-phenyl)-2-(6-(4-(2-hydroxyethyl)- piperazin-1-yl)-2-methylpyrimidin-4-ylamino)thiazole-5-carboxamide (BMS-354825), a dual Src/Abl kinase inhibitor with potent antitumor activity in preclinical assays J Med Chem 47 2004 6658 6661
    • (2004) J Med Chem , vol.47 , pp. 6658-6661
    • Lombardo, L.J.1    Lee, F.Y.2    Chen, P.3    Norris, D.4    Barrish, J.C.5    Behnia, K.6
  • 92
    • 77953790762 scopus 로고    scopus 로고
    • Discovery of 3-[2-(imidazo[1,2-b]pyridazin-3-yl)ethynyl]-4-methyl-N-{4-[(4-methylpiperazin-1-yl)methyl]-3-(trifluoromethyl)phenyl}benzamide (AP24534), a potent, orally active pan-inhibitor of breakpoint cluster region-abelson (BCR-ABL) kinase including the T315I gatekeeper mutant
    • W.S. Huang, C.A. Metcalf, R. Sundaramoorthi, Y. Wang, D. Zou, and R.M. Thomas Discovery of 3-[2-(imidazo[1,2-b]pyridazin-3-yl)ethynyl]-4-methyl-N-{4-[(4-methylpiperazin-1-yl)methyl]-3-(trifluoromethyl)phenyl}benzamide (AP24534), a potent, orally active pan-inhibitor of breakpoint cluster region-abelson (BCR-ABL) kinase including the T315I gatekeeper mutant J Med Chem 53 2010 4701 4719
    • (2010) J Med Chem , vol.53 , pp. 4701-4719
    • Huang, W.S.1    Metcalf, C.A.2    Sundaramoorthi, R.3    Wang, Y.4    Zou, D.5    Thomas, R.M.6
  • 93
    • 33750491945 scopus 로고    scopus 로고
    • N-(5-chloro-1,3-benzodioxol-4-yl)-7-[2-(4-methylpiperazin-1-yl)ethoxy]-5-(tetrahydro-2H-pyran-4-yloxy)quinazolin-4-amine, a novel, highly selective, orally available, dual-specific c-Src/Abl kinase inhibitor
    • L.F. Hennequin, J. Allen, J. Breed, J. Curwen, M. Fennell, and T.P. Green N-(5-chloro-1,3-benzodioxol-4-yl)-7-[2-(4-methylpiperazin-1-yl)ethoxy]-5-(tetrahydro-2H-pyran-4-yloxy)quinazolin-4-amine, a novel, highly selective, orally available, dual-specific c-Src/Abl kinase inhibitor J Med Chem 49 2006 6465 6488
    • (2006) J Med Chem , vol.49 , pp. 6465-6488
    • Hennequin, L.F.1    Allen, J.2    Breed, J.3    Curwen, J.4    Fennell, M.5    Green, T.P.6
  • 94
    • 34548086185 scopus 로고    scopus 로고
    • Src kinase inhibitors induce apoptosis and mediate cell cycle arrest in lymphoma cells
    • D. Nowak, S. Boehrer, S. Hochmuth, B. Trepohl, W. Hofmann, and D. Hoelzer Src kinase inhibitors induce apoptosis and mediate cell cycle arrest in lymphoma cells Anticancer Drugs 18 2007 981 995
    • (2007) Anticancer Drugs , vol.18 , pp. 981-995
    • Nowak, D.1    Boehrer, S.2    Hochmuth, S.3    Trepohl, B.4    Hofmann, W.5    Hoelzer, D.6
  • 95
    • 0037075812 scopus 로고    scopus 로고
    • Novel 4-anilinoquinazolines with C-7 basic side chains: Design and structure activity relationship of a series of potent, orally active, VEGF receptor tyrosine kinase inhibitors
    • L.F. Hennequin, E.S. Stokes, A.P. Thomas, C. Johnstone, P.A. Plé, and D.J. Ogilvie Novel 4-anilinoquinazolines with C-7 basic side chains: design and structure activity relationship of a series of potent, orally active, VEGF receptor tyrosine kinase inhibitors J Med Chem 45 2002 1300 1312
    • (2002) J Med Chem , vol.45 , pp. 1300-1312
    • Hennequin, L.F.1    Stokes, E.S.2    Thomas, A.P.3    Johnstone, C.4    Plé, P.A.5    Ogilvie, D.J.6
  • 97
  • 98
    • 84862294189 scopus 로고    scopus 로고
    • ERK1/2 MAP kinases: Structure, function, and regulation
    • R. Roskoski Jr. ERK1/2 MAP kinases: structure, function, and regulation Pharmacol Res 66 2012 105 143
    • (2012) Pharmacol Res , vol.66 , pp. 105-143
    • Roskoski, Jr.R.1
  • 100
    • 0018580807 scopus 로고
    • An activity phosphorylating tyrosine in polyoma T antigen immunoprecipitates
    • W. Eckhart, M.A. Hutchinson, and T. Hunter An activity phosphorylating tyrosine in polyoma T antigen immunoprecipitates Cell 18 1979 925 933
    • (1979) Cell , vol.18 , pp. 925-933
    • Eckhart, W.1    Hutchinson, M.A.2    Hunter, T.3
  • 101
    • 0000109995 scopus 로고
    • Transforming gene product of Rous sarcoma virus phosphorylates tyrosine
    • T. Hunter, and B.M. Sefton Transforming gene product of Rous sarcoma virus phosphorylates tyrosine Proc Natl Acad Sci U S A 77 1980 1311 1315
    • (1980) Proc Natl Acad Sci U S A , vol.77 , pp. 1311-1315
    • Hunter, T.1    Sefton, B.M.2
  • 102
    • 0019311793 scopus 로고
    • Nucleotide sequence of an avian sarcoma virus oncogene (src) and proposed amino acid sequence for gene product
    • A.P. Czernilofsky, A.D. Levinson, H.E. Varmus, J.M. Bishop, E. Tischer, and H.M. Goodman Nucleotide sequence of an avian sarcoma virus oncogene (src) and proposed amino acid sequence for gene product Nature 287 1980 198 203
    • (1980) Nature , vol.287 , pp. 198-203
    • Czernilofsky, A.P.1    Levinson, A.D.2    Varmus, H.E.3    Bishop, J.M.4    Tischer, E.5    Goodman, H.M.6
  • 104
    • 2642618791 scopus 로고
    • Complete amino acid sequence of the catalytic subunit of bovine cardiac muscle cyclic AMP-dependent protein kinase
    • S. Shoji, D.C. Parmelee, R.D. Wade, S. Kumar, L.H. Ericsson, and K.A. Walsh Complete amino acid sequence of the catalytic subunit of bovine cardiac muscle cyclic AMP-dependent protein kinase Proc Natl Acad Sci U S A 78 1981 848 851
    • (1981) Proc Natl Acad Sci U S A , vol.78 , pp. 848-851
    • Shoji, S.1    Parmelee, D.C.2    Wade, R.D.3    Kumar, S.4    Ericsson, L.H.5    Walsh, K.A.6
  • 105
    • 0011627561 scopus 로고
    • Viral src gene products are related to the catalytic chain of mammalian cAMP-dependent protein kinase
    • W.C. Barker, and M.O. Dayhoff Viral src gene products are related to the catalytic chain of mammalian cAMP-dependent protein kinase Proc Natl Acad Sci U S A 79 1982 2836 2839
    • (1982) Proc Natl Acad Sci U S A , vol.79 , pp. 2836-2839
    • Barker, W.C.1    Dayhoff, M.O.2
  • 106
    • 0018787251 scopus 로고
    • 14C]benzoyl 5′-adenosine. Identification of a modified lysine residue
    • 14C]benzoyl 5′-adenosine. Identification of a modified lysine residue J Biol Chem 1979 254 1979 8363 8368
    • (1979) J Biol Chem 1979 , vol.254 , pp. 8363-8368
    • Zoller, M.J.1    Taylor, S.S.2
  • 107
    • 84872515516 scopus 로고    scopus 로고
    • Kinase drug discovery - What's next in the field?
    • P. Cohen, and D.R. Alessi Kinase drug discovery - what's next in the field? ACS Chem Biol 8 2013 96 104
    • (2013) ACS Chem Biol , vol.8 , pp. 96-104
    • Cohen, P.1    Alessi, D.R.2


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