메뉴 건너뛰기




Volumn 87, Issue , 2014, Pages 42-59

ErbB/HER protein-tyrosine kinases: Structures and small molecule inhibitors

Author keywords

Catalytic spine; EGFR; Gatekeeper residue; Regulatory spine; Targeted cancer therapy; Transition state inhibitor

Indexed keywords

AFATINIB; CANERTINIB; EPIDERMAL GROWTH FACTOR RECEPTOR; EPIDERMAL GROWTH FACTOR RECEPTOR 2; EPIDERMAL GROWTH FACTOR RECEPTOR 4; ERLOTINIB; GEFITINIB; LAPATINIB; MAGNESIUM ION; NERATINIB; PELITINIB; PROTEIN TYROSINE KINASE; VANDETANIB; VEMURAFENIB; ANTINEOPLASTIC AGENT; PROTEIN KINASE INHIBITOR;

EID: 84903581634     PISSN: 10436618     EISSN: 10961186     Source Type: Journal    
DOI: 10.1016/j.phrs.2014.06.001     Document Type: Review
Times cited : (172)

References (116)
  • 1
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • M.A. Lemmon, and J. Schlessinger Cell signaling by receptor tyrosine kinases Cell 141 2010 1117 1134
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 3
    • 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
  • 4
    • 0037032835 scopus 로고    scopus 로고
    • The protein kinase complement of the human genome
    • DOI 10.1126/science.1075762
    • G. Manning, D.B. Whyte, R. Martinez, T. Hunter, and S. Sudarsanam The protein kinase complement of the human genome Science 298 2002 1912 1934 (Pubitemid 35425239)
    • (2002) Science , vol.298 , Issue.5600 , pp. 1912-1934
    • Manning, G.1    Whyte, D.B.2    Martinez, R.3    Hunter, T.4    Sudarsanam, S.5
  • 6
    • 0036527429 scopus 로고    scopus 로고
    • Protein kinases - The major drug targets of the twenty-first century?
    • P. Cohen Protein kinases - the major drug targets of the twenty-first century? Nat Rev Drug Discov 1 2002 309 315 (Pubitemid 37361447)
    • (2002) Nature Reviews Drug Discovery , vol.1 , Issue.4 , pp. 309-315
    • Cohen, P.1
  • 7
    • 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
  • 8
    • 84891751622 scopus 로고    scopus 로고
    • The druggable genome: Evaluation of drug targets in clinical trials suggests major shifts in molecular class and indication
    • M. Rask-Andersen, S. Masuram, and H.B. Schiöth The druggable genome: evaluation of drug targets in clinical trials suggests major shifts in molecular class and indication Annu Rev Pharmacol Toxicol 54 2014 9 26
    • (2014) Annu Rev Pharmacol Toxicol , vol.54 , pp. 9-26
    • Rask-Andersen, M.1    Masuram, S.2    Schiöth, H.B.3
  • 9
    • 0021688634 scopus 로고
    • The neu oncogene: An erb-B-related gene encoding a 185,000-M(r) tumour antigen
    • DOI 10.1038/312513a0
    • A.L. Schechter, D.F. Stern, L. Vaidyanathan, S.J. Decker, J.A. Drebin, and M.I. Greene et al. The neu oncogene: an erb-B-related gene encoding a 185,000-Mr tumour antigen Nature 312 1984 513 516 (Pubitemid 15182278)
    • (1984) Nature , vol.312 , Issue.5994 , pp. 513-516
    • Schechter, A.L.1    Stern, D.F.2    Vaidyanathan, L.3
  • 10
    • 0021273420 scopus 로고
    • Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells
    • A. Ullrich, L. Coussens, J.S. Hayflick, T.J. Dull, A. Gray, and A.W. Tam et al. Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells Nature 309 1984 418 425 (Pubitemid 14102443)
    • (1984) Nature , vol.309 , Issue.5967 , pp. 418-425
    • Ullrich, A.1    Coussens, L.2    Hayflick, J.S.3
  • 11
    • 79952233837 scopus 로고    scopus 로고
    • Trastuzumab has preferential activity against breast cancers driven by ERBB2 homodimers
    • R. Ghosh, A. Narasanna, S.E. Wang, S. Liu, A. Chakrabarty, and J.M. Balko et al. Trastuzumab has preferential activity against breast cancers driven by ERBB2 homodimers Cancer Res 71 2011 1871 1882
    • (2011) Cancer Res , vol.71 , pp. 1871-1882
    • Ghosh, R.1    Narasanna, A.2    Wang, S.E.3    Liu, S.4    Chakrabarty, A.5    Balko, J.M.6
  • 12
    • 77952338791 scopus 로고    scopus 로고
    • ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation
    • F. Shi, S.E. Telesco, Y. Liu, R. Radhakrishnan, and M.A. Lemmon ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation Proc Natl Acad Sci USA 107 2010 7692 7697
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 7692-7697
    • Shi, F.1    Telesco, S.E.2    Liu, Y.3    Radhakrishnan, R.4    Lemmon, M.A.5
  • 13
    • 0029814271 scopus 로고    scopus 로고
    • A hierarchical network of interreceptor interactions determines signal transduction by Neu differentiation factor/neuregulin and epidermal growth factor
    • E. Tzahar, H. Waterman, X. Chen, G. Levkowitz, D. Karunagaran, and S. Lavi et al. A hierarchical network of interreceptor interactions determines signal transduction by Neu differentiation factor/neuregulin and epidermal growth factor Mol Cell Biol 16 1996 5276 5287 (Pubitemid 26315047)
    • (1996) Molecular and Cellular Biology , vol.16 , Issue.10 , pp. 5276-5287
    • Tzahar, E.1    Waterman, H.2    Chen, X.3    Levkowitz, G.4    Karunagaran, D.5    Lavi, S.6    Ratzkin, B.J.7    Yarden, Y.8
  • 14
    • 0030944455 scopus 로고    scopus 로고
    • ErbB-2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signaling
    • DOI 10.1093/emboj/16.7.1647
    • D. Graus-Porta, R.R. Beerli, J.M. Daly, and N.E. Hynes ErbB-2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signaling EMBO J 16 1997 1647 1655 (Pubitemid 27151960)
    • (1997) EMBO Journal , vol.16 , Issue.7 , pp. 1647-1655
    • Graus-Porta, D.1    Beerli, R.R.2    Daly, J.M.3    Hynes, N.E.4
  • 16
    • 0037145061 scopus 로고    scopus 로고
    • Ligand-induced, receptor-mediated dimerization and activation of EGF receptor
    • DOI 10.1016/S0092-8674(02)00966-2
    • J. Schlessinger, and Ligand-induced receptor-mediated dimerization and activation of EGF receptor Cell 110 2002 669 672 (Pubitemid 35283957)
    • (2002) Cell , vol.110 , Issue.6 , pp. 669-672
    • Schlessinger, J.1
  • 21
    • 4444353636 scopus 로고    scopus 로고
    • Regulation of protein kinases: Controlling activity through activation segment conformation
    • DOI 10.1016/j.molcel.2004.08.024, PII S1097276504004800
    • B. Nolen, S. Taylor, and G. Ghosh Regulation of protein kinases; controlling activity through activation segment conformation Mol Cell 15 2004 661 675 (Pubitemid 39194898)
    • (2004) Molecular Cell , vol.15 , Issue.5 , pp. 661-675
    • Nolen, B.1    Taylor, S.2    Ghosh, G.3
  • 22
    • 0033583220 scopus 로고    scopus 로고
    • C-Src-mediated phosphorylation of the epidermal growth factor receptor on Tyr845 and Tyr1101 is associated with modulation of receptor function
    • J.S. Biscardi, M.C. Maa, D.A. Tice, M.E. Cox, T.H. Leu, and S.J. Parsons c-Src-mediated phosphorylation of the epidermal growth factor receptor on Tyr845 and Tyr1101 is associated with modulation of receptor function J Biol Chem 274 1999 8335 8343
    • (1999) J Biol Chem , vol.274 , pp. 8335-8343
    • Biscardi, J.S.1    Maa, M.C.2    Tice, D.A.3    Cox, M.E.4    Leu, T.H.5    Parsons, S.J.6
  • 23
    • 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
    • N. Gotoh, A. Tojo, M. Hino, Y. Yazaki, and M. Shibuya 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 1992 768 774
    • (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
  • 24
    • 33745002702 scopus 로고    scopus 로고
    • An Allosteric Mechanism for Activation of the Kinase Domain of Epidermal Growth Factor Receptor
    • DOI 10.1016/j.cell.2006.05.013, PII S0092867406005848
    • X. Zhang, J. Gureasko, K. Shen, P.A. Cole, and J. Kuriyan An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor Cell 125 2006 1137 1149 (Pubitemid 43866200)
    • (2006) Cell , vol.125 , Issue.6 , pp. 1137-1149
    • Zhang, X.1    Gureasko, J.2    Shen, K.3    Cole, P.A.4    Kuriyan, J.5
  • 25
    • 84891850975 scopus 로고    scopus 로고
    • Targeting protein-protein interaction by small molecules
    • L. Jin, W. Wang, and G. Fang Targeting protein-protein interaction by small molecules Annu Rev Pharmacol Toxicol 54 2014 435 456
    • (2014) Annu Rev Pharmacol Toxicol , vol.54 , pp. 435-456
    • Jin, L.1    Wang, W.2    Fang, G.3
  • 26
    • 77956124562 scopus 로고    scopus 로고
    • RAF protein-serine/threonine kinases: Structure and regulation
    • R. Roskoski Jr. RAF protein-serine/threonine kinases: structure and regulation Biochem Biophys Res Commun 399 2010 313 317
    • (2010) Biochem Biophys Res Commun , vol.399 , pp. 313-317
    • Roskoski, Jr.R.1
  • 27
    • 77949685981 scopus 로고    scopus 로고
    • RAF inhibitors prime wild-type RAF to activate the MAPK pathway and enhance growth
    • G. Hatzivassiliou, K. Song, I. Yen, B.J. Brandhuber, D.J. Anderson, and R. Alvarado et al. RAF inhibitors prime wild-type RAF to activate the MAPK pathway and enhance growth Nature 464 2010 431 435
    • (2010) Nature , vol.464 , pp. 431-435
    • Hatzivassiliou, G.1    Song, K.2    Yen, I.3    Brandhuber, B.J.4    Anderson, D.J.5    Alvarado, R.6
  • 28
    • 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 et al. Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase Science 253 1991 407 414 (Pubitemid 21917165)
    • (1991) Science , vol.253 , Issue.5018 , pp. 407-414
    • Knighton, D.R.1    Zheng, J.2    Ten Eyck, L.F.3    Ashford, V.A.4    Xuong, N.-H.5    Taylor, S.S.6    Sowadski, J.M.7
  • 29
    • 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 et al. 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
  • 30
    • 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
  • 34
    • 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
  • 35
    • 79956310563 scopus 로고    scopus 로고
    • Structural analysis of the mechanism of inhibition and allosteric activation of the kinase domain of HER2 protein
    • K. Aertgeerts, R. Skene, J. Yano, B.C. Sang, H. Zou, and G. Snell et al. Structural analysis of the mechanism of inhibition and allosteric activation of the kinase domain of HER2 protein J Biol Chem 286 2011 18756 18765
    • (2011) J Biol Chem , vol.286 , pp. 18756-18765
    • Aertgeerts, K.1    Skene, R.2    Yano, J.3    Sang, B.C.4    Zou, H.5    Snell, G.6
  • 36
    • 84886629236 scopus 로고    scopus 로고
    • Deciphering the structural basis of eukaryotic protein kinase regulation
    • H.S. Meharena, P. Chang, M.M. Keshwani, K. Oruganty, A.K. Nene, and N. Kannan et al. Deciphering the structural basis of eukaryotic protein kinase regulation PLoS Biol 11 10 2013 e1001680
    • (2013) PLoS Biol , vol.11 , Issue.10 , pp. 1001680
    • Meharena, H.S.1    Chang, P.2    Keshwani, M.M.3    Oruganty, K.4    Nene, A.K.5    Kannan, N.6
  • 38
    • 0031709073 scopus 로고    scopus 로고
    • A molecular gate which controls unnatural ATP analogue recognition by the tyrosine kinase v-Src
    • DOI 10.1016/S0968-0896(98)00099-6, PII S0968089698000996
    • 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 (Pubitemid 28398957)
    • (1998) Bioorganic and Medicinal Chemistry , vol.6 , Issue.8 , pp. 1219-1226
    • Liu, Y.1    Shah, K.2    Yang, F.3    Witucki, L.4    Shokat, K.M.5
  • 39
    • 0027407640 scopus 로고
    • Autoactivation of catalytic (Cα) subunit of cyclic AMP-dependent protein kinase by phosphorylation of threonine 197
    • 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 (Pubitemid 23097712)
    • (1993) Molecular and Cellular Biology , vol.13 , Issue.4 , pp. 2332-2341
    • Steinberg, R.A.1    Cauthron, R.D.2    Symcox, M.M.3    Shuntoh, H.4
  • 40
    • 84860369376 scopus 로고    scopus 로고
    • Structural basis for the regulation of protein kinase A by activation loop phosphorylation
    • J.M. Steichen, M. Kuchinskas, M.M. Keshwani, J. Yang, J.A. Adams, and S.S. Taylor Structural basis for the regulation of protein kinase A by activation loop phosphorylation J Biol Chem 287 2012 14672 14680
    • (2012) J Biol Chem , vol.287 , pp. 14672-14680
    • Steichen, J.M.1    Kuchinskas, M.2    Keshwani, M.M.3    Yang, J.4    Adams, J.A.5    Taylor, S.S.6
  • 42
    • 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
  • 43
  • 44
    • 0031444107 scopus 로고    scopus 로고
    • Participation of ADP dissociation in the rate-determining step in cAMP- dependent protein kinase
    • DOI 10.1021/bi971438n
    • 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 (Pubitemid 28027372)
    • (1997) Biochemistry , vol.36 , Issue.50 , pp. 15733-15738
    • Zhou, J.1    Adams, J.A.2
  • 45
    • 84856232223 scopus 로고    scopus 로고
    • A conserved Glu-Arg salt bridge connects coevolved motifs that define the eukaryotic protein kinase fold
    • J. Yang, J. Wu, J.M. Steichen, A.P. Kornev, M.S. Deal, and S. Li et al. A conserved Glu-Arg salt bridge connects coevolved motifs that define the eukaryotic protein kinase fold J Mol Biol 415 2012 666 679
    • (2012) J Mol Biol , vol.415 , pp. 666-679
    • Yang, J.1    Wu, J.2    Steichen, J.M.3    Kornev, A.P.4    Deal, M.S.5    Li, S.6
  • 46
    • 33749138745 scopus 로고    scopus 로고
    • Mechanistic studies on enzyme-catalyzed phosphoryl transfer
    • A.C. Hengge Mechanistic studies on enzyme-catalyzed phosphoryl transfer Adv Phys Org Chem 40 2005 49 108
    • (2005) Adv Phys Org Chem , vol.40 , pp. 49-108
    • Hengge, A.C.1
  • 47
    • 0000266761 scopus 로고
    • Stereochemical course of the phospho group transfer catalyzed by cAMP-dependent protein kinase
    • M. Ho, H.N. Bramson, D.E. Hansen, J.R. Knowles, and E.T. Kaiser Stereochemical course of the phospho group transfer catalyzed by cAMP-dependent protein kinase J Am Chem Soc 110 1988 2680 2681
    • (1988) J Am Chem Soc , vol.110 , pp. 2680-2681
    • Ho, M.1    Bramson, H.N.2    Hansen, D.E.3    Knowles, J.R.4    Kaiser, E.T.5
  • 48
    • 33845185675 scopus 로고
    • IUPAC recommendations for the representation of reaction mechanisms
    • R.D. Guthrie, and W.P. Jencks IUPAC recommendations for the representation of reaction mechanisms Acc Chem Res 10 1989 343 349
    • (1989) Acc Chem Res , vol.10 , pp. 343-349
    • Guthrie, R.D.1    Jencks, W.P.2
  • 49
    • 0031688282 scopus 로고    scopus 로고
    • Enzymatic transition states and transition state analog design
    • DOI 10.1146/annurev.biochem.67.1.693
    • V.L. Schramm Enzymatic transition states and transition state analog design Annu Rev Biochem 67 1998 693 720 (Pubitemid 28411142)
    • (1998) Annual Review of Biochemistry , vol.67 , pp. 693-720
    • Schramm, V.L.1
  • 50
    • 84872556816 scopus 로고    scopus 로고
    • Transition states, analogues, and drug development
    • V.L. Schramm Transition states, analogues, and drug development ACS Chem Biol 8 2013 71 81
    • (2013) ACS Chem Biol , vol.8 , pp. 71-81
    • Schramm, V.L.1
  • 51
    • 36949034492 scopus 로고    scopus 로고
    • Phosphorylation reaction in cAPK protein kinase-free energy quantum mechanical/ molecular mechanics simulations
    • DOI 10.1021/jp074853q
    • M. Valiev, J. Yang, J.A. Adams, S.S. Taylor, and J.H. Weare Phosphorylation reaction in cAPK protein kinase-free energy quantum mechanical/molecular mechanics simulations J Phys Chem 111 2007 13455 13464 [Erratum in: J Phys Chem 2010;114:6763] (Pubitemid 350241477)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.47 , pp. 13455-13464
    • Valiev, M.1    Yang, J.2    Adams, J.A.3    Taylor, S.S.4    Weare, J.H.5
  • 52
    • 13444303958 scopus 로고    scopus 로고
    • How does the cAMP-dependent protein kinase catalyze the phosphorylation reaction: An ab Initio QM/MM study
    • DOI 10.1021/ja0464084
    • Y. Cheng, Y. Zhang, and J.A. McCammon How does the cAMP-dependent protein kinase catalyze the phosphorylation reaction: an ab initio QM/MM study J Am Chem Soc 127 2005 1553 1562 (Pubitemid 40204531)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.5 , pp. 1553-1562
    • Cheng, Y.1    Zhang, Y.2    McCammon, J.A.3
  • 53
    • 79955844083 scopus 로고    scopus 로고
    • Briefly bound to activate: Transient binding of a second catalytic magnesium activates the structure and dynamics of CDK2 kinase for catalysis
    • Z.Q. Bao, D.M. Jacobsen, and M.A. Young Briefly bound to activate: transient binding of a second catalytic magnesium activates the structure and dynamics of CDK2 kinase for catalysis Structure 19 2011 675 690
    • (2011) Structure , vol.19 , pp. 675-690
    • Bao, Z.Q.1    Jacobsen, D.M.2    Young, M.A.3
  • 54
    • 84912208190 scopus 로고
    • Chemical achievement and hope for the future
    • L. Pauling Chemical achievement and hope for the future Am Sci 36 1948 51 58
    • (1948) Am Sci , vol.36 , pp. 51-58
    • Pauling, L.1
  • 55
    • 84875636822 scopus 로고    scopus 로고
    • Specificity in transition state binding: The Pauling model revisited
    • T.L. Amyes, and J.P. Richard Specificity in transition state binding: the Pauling model revisited Biochemistry 52 2013 2021 2035
    • (2013) Biochemistry , vol.52 , pp. 2021-2035
    • Amyes, T.L.1    Richard, J.P.2
  • 56
    • 0036050539 scopus 로고    scopus 로고
    • Strategies in the design of antiviral drugs
    • E. De Clercq Strategies in the design of antiviral drugs Nat Rev Drug Discov 1 2002 13 25 (Pubitemid 37361400)
    • (2002) Nature Reviews Drug Discovery , vol.1 , Issue.1 , pp. 13-25
    • De Clercq, E.1
  • 58
    • 84874114410 scopus 로고    scopus 로고
    • Antivirals: Past, present and future
    • E. De Clercq Antivirals: past, present and future Biochem Pharmacol 85 2013 727 744
    • (2013) Biochem Pharmacol , vol.85 , pp. 727-744
    • De Clercq, E.1
  • 59
    • 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
  • 60
    • 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
  • 61
    • 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 III, C.L.4    Young, M.A.5
  • 62
    • 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
  • 63
    • 0037452906 scopus 로고    scopus 로고
    • Physiological concentrations of divalent magnesium ion activate the serine/threonine specific protein kinase ERK2
    • DOI 10.1021/bi027171w
    • 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 (Pubitemid 36331540)
    • (2003) Biochemistry , vol.42 , Issue.10 , pp. 2960-2970
    • Waas, W.F.1    Dalby, K.N.2
  • 64
    • 0031048501 scopus 로고    scopus 로고
    • Requirement for an additional divalent metal cation to activate protein tyrosine kinases
    • DOI 10.1021/bi962291n
    • G. Sun, and R.J. Budde Requirement for an additional divalent metal cation to activate protein tyrosine kinases Biochemistry 36 1997 2139 2146 (Pubitemid 27104705)
    • (1997) Biochemistry , vol.36 , Issue.8 , pp. 2139-2146
    • Sun, G.1    Budde, R.J.A.2
  • 65
    • 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 (Pubitemid 18078290)
    • (1988) Archives of Biochemistry and Biophysics , vol.261 , Issue.2 , pp. 336-345
    • Vicario, P.P.1    Saperstein, R.2    Bennun, A.3
  • 66
    • 0032497373 scopus 로고    scopus 로고
    • A second magnesium ion is critical for ATP binding in the kinase domain of the oncoprotein v-Fps
    • DOI 10.1021/bi9812672
    • 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 (Pubitemid 28427547)
    • (1998) Biochemistry , vol.37 , Issue.36 , pp. 12624-12630
    • Saylor, P.1    Wang, C.2    Hirai, T.J.3    Adams, J.A.4
  • 67
    • 0003481596 scopus 로고
    • 2nd ed. W.H. Freeman and Company New York
    • A. Fersht Enzyme structure and mechanism 2nd ed. 1985 W.H. Freeman and Company New York 105 106
    • (1985) Enzyme Structure and Mechanism , pp. 105-106
    • Fersht, A.1
  • 69
    • 84901049654 scopus 로고    scopus 로고
    • Metal-free cAMP-dependent protein kinase can catalyze phosphoryl transfer
    • O. Gerlits, A. Das, M.M. Keshwani, S. Taylor, M.J. Waltman, and P. Langan et al. Metal-free cAMP-dependent protein kinase can catalyze phosphoryl transfer Biochemistry 53 2014 3179 3186
    • (2014) Biochemistry , vol.53 , pp. 3179-3186
    • Gerlits, O.1    Das, A.2    Keshwani, M.M.3    Taylor, S.4    Waltman, M.J.5    Langan, P.6
  • 70
    • 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 et al. Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor Biochemistry 32 1993 2154 2161 (Pubitemid 23094874)
    • (1993) Biochemistry , vol.32 , Issue.9 , pp. 2154-2161
    • Zheng, J.1    Knighton, D.R.2    Ten Eyck, L.F.3    Karlsson, R.4    Xuong, N.-H.5    Taylor, S.S.6    Sowadski, J.M.7
  • 71
    • 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 (Pubitemid 23354720)
    • (1993) Protein Science , vol.2 , Issue.12 , pp. 2177-2186
    • Adams, J.A.1    Taylor, S.S.2
  • 72
    • 0035413606 scopus 로고    scopus 로고
    • Kinetic and catalytic mechanisms of protein kinases
    • DOI 10.1021/cr000230w
    • J.A. Adams Kinetic and catalytic mechanisms of protein kinases Chem Rev 101 2001 2271 2290 (Pubitemid 35373019)
    • (2001) Chemical Reviews , vol.101 , Issue.8 , pp. 2271-2290
    • Adams, J.A.1
  • 73
  • 74
    • 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 et al. 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
  • 79
    • 84877147943 scopus 로고    scopus 로고
    • Uncommon epidermal growth factor receptor mutations in non-small cell lung cancer and their mechanisms of EGFR tyrosine kinase inhibitors sensitivity and resistance
    • E. Massarelli, F.M. Johnson, H.S. Erickson, I.I. Wistuba, and V. Papadimitrakopoulou Uncommon epidermal growth factor receptor mutations in non-small cell lung cancer and their mechanisms of EGFR tyrosine kinase inhibitors sensitivity and resistance Lung Cancer 80 2013 235 241
    • (2013) Lung Cancer , vol.80 , pp. 235-241
    • Massarelli, E.1    Johnson, F.M.2    Erickson, H.S.3    Wistuba, I.I.4    Papadimitrakopoulou, V.5
  • 81
    • 24644458654 scopus 로고    scopus 로고
    • FDA drug approval summary: Erlotinib (Tarceva®) tablets
    • DOI 10.1634/theoncologist.10-7-461
    • M.H. Cohen, J.R. Johnson, Y.F. Chen, R. Sridhara, and R. Pazdur FDA drug approval summary: erlotinib (Tarceva) tablets Oncologist 10 2005 461 466 (Pubitemid 41266326)
    • (2005) Oncologist , vol.10 , Issue.7 , pp. 461-466
    • Cohen, M.H.1    Johnson, J.R.2    Chen, Y.-F.3    Sridhara, R.4    Pazdur, R.5
  • 82
    • 33847406095 scopus 로고    scopus 로고
    • Structures of Lung Cancer-Derived EGFR Mutants and Inhibitor Complexes: Mechanism of Activation and Insights into Differential Inhibitor Sensitivity
    • DOI 10.1016/j.ccr.2006.12.017, PII S1535610807000281
    • C.H. Yun, T.J. Boggon, Y. Li, M.S. Woo, H. Greulich, and M. Meyerson et al. Structures of lung cancer-derived EGFR mutants and inhibitor complexes: mechanism of activation and insights into differential inhibitor sensitivity Cancer Cell 11 2007 217 227 (Pubitemid 46349842)
    • (2007) Cancer Cell , vol.11 , Issue.3 , pp. 217-227
    • Yun, C.-H.1    Boggon, T.J.2    Li, Y.3    Woo, M.S.4    Greulich, H.5    Meyerson, M.6    Eck, M.J.7
  • 83
    • 84884308133 scopus 로고    scopus 로고
    • Mechanism for activation of mutated epidermal growth factor receptors in lung cancer
    • [Erratum in: Proc Natl Acad Sci USA 2013;110(50):20344]
    • M. Red Brewer, C.H. Yun, D. Lai, M.A. Lemmon, M.J. Eck, and W. Pao Mechanism for activation of mutated epidermal growth factor receptors in lung cancer Proc Natl Acad Sci USA 110 2013 E3595 E3604 [Erratum in: Proc Natl Acad Sci USA 2013;110(50):20344]
    • (2013) Proc Natl Acad Sci USA , vol.110
    • Red Brewer, M.1    Yun, C.H.2    Lai, D.3    Lemmon, M.A.4    Eck, M.J.5    Pao, W.6
  • 84
    • 84901290217 scopus 로고    scopus 로고
    • FDA drug approval summary: Lapatinib in combination with capecitabine for previously treated metastatic breast cancer that overexpresses HER-2
    • Q. Ryan, A. Ibrahim, M.H. Cohen, J. Johnson, C.W. Ko, and R. Sridhara et al. FDA drug approval summary: lapatinib in combination with capecitabine for previously treated metastatic breast cancer that overexpresses HER-2 Oncologist 13 2008 1114 1119
    • (2008) Oncologist , vol.13 , pp. 1114-1119
    • Ryan, Q.1    Ibrahim, A.2    Cohen, M.H.3    Johnson, J.4    Ko, C.W.5    Sridhara, R.6
  • 85
    • 77951951659 scopus 로고    scopus 로고
    • Clinical outcomes in non-small-cell lung cancer patients with EGFR mutations: Pooled analysis
    • L. Paz-Ares, D. Soulières, I. Melezínek, J. Moecks, L. Keil, and T. Mok et al. Clinical outcomes in non-small-cell lung cancer patients with EGFR mutations: pooled analysis J Cell Mol Med 14 2010 51 69
    • (2010) J Cell Mol Med , vol.14 , pp. 51-69
    • Paz-Ares, L.1    Soulières, D.2    Melezínek, I.3    Moecks, J.4    Keil, L.5    Mok, T.6
  • 87
    • 84867621201 scopus 로고    scopus 로고
    • Target binding properties and cellular activity of afatinib (BIBW 2992), an irreversible ErbB family blocker
    • F. Solca, G. Dahl, A. Zoephel, G. Bader, M. Sanderson, and C. Klein et al. Target binding properties and cellular activity of afatinib (BIBW 2992), an irreversible ErbB family blocker J Pharmacol Exp Ther 343 2012 342 350
    • (2012) J Pharmacol Exp Ther , vol.343 , pp. 342-350
    • Solca, F.1    Dahl, G.2    Zoephel, A.3    Bader, G.4    Sanderson, M.5    Klein, C.6
  • 89
    • 84872288990 scopus 로고    scopus 로고
    • Anaplastic lymphoma kinase (ALK): Structure, oncogenic activation, and pharmacological inhibition
    • R. Roskoski Jr. Anaplastic lymphoma kinase (ALK): structure, oncogenic activation, and pharmacological inhibition Pharmacol Res 68 2013 68 94
    • (2013) Pharmacol Res , vol.68 , pp. 68-94
    • Roskoski, Jr.R.1
  • 91
    • 84868506607 scopus 로고    scopus 로고
    • Clinical perspectives for irreversible tyrosine kinase inhibitors in cancer
    • C. Carmi, M. Mor, P.G. Petronini, and R.R. Alfieri Clinical perspectives for irreversible tyrosine kinase inhibitors in cancer Biochem Pharmacol 84 2012 1388 1399
    • (2012) Biochem Pharmacol , vol.84 , pp. 1388-1399
    • Carmi, C.1    Mor, M.2    Petronini, P.G.3    Alfieri, R.R.4
  • 92
    • 84883017405 scopus 로고    scopus 로고
    • The preclinical profile of crizotinib for the treatment of non-small-cell lung cancer and other neoplastic disorders
    • R. Roskoski Jr. The preclinical profile of crizotinib for the treatment of non-small-cell lung cancer and other neoplastic disorders Expert Opin Drug Discov 8 2013 1165 1179
    • (2013) Expert Opin Drug Discov , vol.8 , pp. 1165-1179
    • Roskoski, Jr.R.1
  • 93
    • 84884640384 scopus 로고    scopus 로고
    • Afatinib: First global approval
    • R.T. Dungo, and G.M. Keating Afatinib: first global approval Drugs 73 2013 1503 1515
    • (2013) Drugs , vol.73 , pp. 1503-1515
    • Dungo, R.T.1    Keating, G.M.2
  • 96
    • 84864539047 scopus 로고    scopus 로고
    • Systematic review of lapatinib in combination with letrozole compared with other first-line treatments for hormone receptor positive (HR+) and HER2+ advanced or metastatic breast cancer (MBC)
    • R. Riemsma, C.A. Forbes, M.M. Amonkar, K. Lykopoulos, J.R. Diaz, and J. Kleijnen et al. Systematic review of lapatinib in combination with letrozole compared with other first-line treatments for hormone receptor positive (HR+) and HER2+ advanced or metastatic breast cancer (MBC) Curr Med Res Opin 28 2012 1263 1279
    • (2012) Curr Med Res Opin , vol.28 , pp. 1263-1279
    • Riemsma, R.1    Forbes, C.A.2    Amonkar, M.M.3    Lykopoulos, K.4    Diaz, J.R.5    Kleijnen, J.6
  • 97
    • 84856331314 scopus 로고    scopus 로고
    • Phase i safety, pharmacokinetic and pharmacodynamic trial of BMS-599626 (AC480), an oral pan-HER receptor tyrosine kinase inhibitor, in patients with advanced solid tumors
    • J.C. Soria, J. Cortes, C. Massard, J.P. Armand, D. De Andreis, and S. Ropert et al. Phase I safety, pharmacokinetic and pharmacodynamic trial of BMS-599626 (AC480), an oral pan-HER receptor tyrosine kinase inhibitor, in patients with advanced solid tumors Ann Oncol 23 2012 463 471
    • (2012) Ann Oncol , vol.23 , pp. 463-471
    • Soria, J.C.1    Cortes, J.2    Massard, C.3    Armand, J.P.4    De Andreis, D.5    Ropert, S.6
  • 98
    • 84886296148 scopus 로고    scopus 로고
    • An update on molecularly targeted therapies in second- and third-line treatment in non-small cell lung cancer: Focus on EGFR inhibitors and anti-angiogenic agents
    • M. Majem, and C. Pallarès An update on molecularly targeted therapies in second- and third-line treatment in non-small cell lung cancer: focus on EGFR inhibitors and anti-angiogenic agents Clin Transl Oncol 15 2013 343 357
    • (2013) Clin Transl Oncol , vol.15 , pp. 343-357
    • Majem, M.1    Pallarès, C.2
  • 100
    • 84874644488 scopus 로고    scopus 로고
    • Second-generation epidermal growth factor receptor tyrosine kinase inhibitors in lung cancers
    • H.A. Yu, and G.J. Riely Second-generation epidermal growth factor receptor tyrosine kinase inhibitors in lung cancers J Natl Compr Cancer Netw 11 2013 161 169
    • (2013) J Natl Compr Cancer Netw , vol.11 , pp. 161-169
    • Yu, H.A.1    Riely, G.J.2
  • 101
    • 84899645435 scopus 로고    scopus 로고
    • Role of human epidermal growth factor receptor 2 in gastric cancer: Biological and pharmacological aspects
    • J.T. Jørgensen Role of human epidermal growth factor receptor 2 in gastric cancer: biological and pharmacological aspects World J Gastroenterol 20 2014 4526 4535
    • (2014) World J Gastroenterol , vol.20 , pp. 4526-4535
    • Jørgensen, J.T.1
  • 102
    • 84878846850 scopus 로고    scopus 로고
    • Promising new molecular targeted therapies in head and neck cancer
    • K. Dorsey, and M. Agulnik Promising new molecular targeted therapies in head and neck cancer Drugs 73 2013 315 325
    • (2013) Drugs , vol.73 , pp. 315-325
    • Dorsey, K.1    Agulnik, M.2
  • 103
    • 84860730675 scopus 로고    scopus 로고
    • Effects of icotinib, a novel epidermal growth factor receptor tyrosine kinase inhibitor, in EGFR-mutated non-small cell lung cancer
    • G. Yang, Y. Yao, J. Zhou, and Q. Zhao Effects of icotinib, a novel epidermal growth factor receptor tyrosine kinase inhibitor, in EGFR-mutated non-small cell lung cancer Oncol Rep 27 2012 2066 2072
    • (2012) Oncol Rep , vol.27 , pp. 2066-2072
    • Yang, G.1    Yao, Y.2    Zhou, J.3    Zhao, Q.4
  • 104
    • 84903619064 scopus 로고    scopus 로고
    • Current challenges and clinical investigations of epidermal growth factor receptor (EGFR)- and ErbB family-targeted agents in the treatment of head and neck squamous cell carcinoma (HNSCC)
    • S0305-7372(13)00206-5
    • R.B. Cohen Current challenges and clinical investigations of epidermal growth factor receptor (EGFR)- and ErbB family-targeted agents in the treatment of head and neck squamous cell carcinoma (HNSCC) Cancer Treat Rev 2013 S0305-7372(13)00206-5
    • (2013) Cancer Treat Rev
    • Cohen, R.B.1
  • 105
    • 79960035905 scopus 로고    scopus 로고
    • Phase i study of icotinib hydrochloride (BPI-2009H), an oral EGFR tyrosine kinase inhibitor, in patients with advanced NSCLC and other solid tumors
    • Q. Zhao, J. Shentu, N. Xu, J. Zhou, G. Yang, and Y. Yao et al. Phase I study of icotinib hydrochloride (BPI-2009H), an oral EGFR tyrosine kinase inhibitor, in patients with advanced NSCLC and other solid tumors Lung Cancer 73 2011 195 202
    • (2011) Lung Cancer , vol.73 , pp. 195-202
    • Zhao, Q.1    Shentu, J.2    Xu, N.3    Zhou, J.4    Yang, G.5    Yao, Y.6
  • 106
    • 84895765218 scopus 로고    scopus 로고
    • Network meta-analysis of erlotinib, gefitinib, afatinib and icotinib in patients with advanced non-small-cell lung cancer harboring EGFR mutations
    • 8524
    • W. Liang, X. Wu, W. Fang, Y. Zhao, Y. Yang, and Z. Hu et al. Network meta-analysis of erlotinib, gefitinib, afatinib and icotinib in patients with advanced non-small-cell lung cancer harboring EGFR mutations PLoS ONE 9 2014 e5 8524
    • (2014) PLoS ONE , vol.9 , pp. 5
    • Liang, W.1    Wu, X.2    Fang, W.3    Zhao, Y.4    Yang, Y.5    Hu, Z.6
  • 107
    • 84888004978 scopus 로고    scopus 로고
    • A phase two randomised trial of neratinib monotherapy versus lapatinib plus capecitabine combination therapy in patients with HER2+ advanced breast cancer
    • M. Martin, M. Martin, C.E. Geyer Jr., Y. Ito, J. Ro, and I. Lang et al. A phase two randomised trial of neratinib monotherapy versus lapatinib plus capecitabine combination therapy in patients with HER2+ advanced breast cancer Eur J Cancer 49 2013 3763 3772
    • (2013) Eur J Cancer , vol.49 , pp. 3763-3772
    • Martin, M.1    Martin, M.2    Geyer, Jr.C.E.3    Ito, Y.4    Ro, J.5    Lang, I.6
  • 108
    • 84894807977 scopus 로고    scopus 로고
    • Phase i study of neratinib in combination with temsirolimus in patients with human epidermal growth factor receptor 2-dependent and other solid tumors
    • L. Gandhi, R. Bahleda, S.M. Tolaney, E.L. Kwak, J.M. Cleary, and S.S. Pandya et al. Phase I study of neratinib in combination with temsirolimus in patients with human epidermal growth factor receptor 2-dependent and other solid tumors J Clin Oncol 32 2014 68 75
    • (2014) J Clin Oncol , vol.32 , pp. 68-75
    • Gandhi, L.1    Bahleda, R.2    Tolaney, S.M.3    Kwak, E.L.4    Cleary, J.M.5    Pandya, S.S.6
  • 109
    • 84863274596 scopus 로고    scopus 로고
    • Antitumor activity of HM781-36B, a pan-HER tyrosine kinase inhibitor, in HER2-amplified breast cancer cells
    • H.J. Kim, H.P. Kim, Y.K. Yoon, M.S. Kim, G.S. Lee, and S.W. Han et al. Antitumor activity of HM781-36B, a pan-HER tyrosine kinase inhibitor, in HER2-amplified breast cancer cells Anticancer Drugs 23 2012 288 297
    • (2012) Anticancer Drugs , vol.23 , pp. 288-297
    • Kim, H.J.1    Kim, H.P.2    Yoon, Y.K.3    Kim, M.S.4    Lee, G.S.5    Han, S.W.6
  • 110
    • 84859100127 scopus 로고    scopus 로고
    • Antitumor activity of HM781-36B, a highly effective pan-HER inhibitor in erlotinib-resistant NSCLC and other EGFR-dependent cancer models
    • M.Y. Cha, K.O. Lee, M. Kim, J.Y. Song, K.H. Lee, and J. Park et al. Antitumor activity of HM781-36B, a highly effective pan-HER inhibitor in erlotinib-resistant NSCLC and other EGFR-dependent cancer models Int J Cancer 130 2012 2445 2454
    • (2012) Int J Cancer , vol.130 , pp. 2445-2454
    • Cha, M.Y.1    Lee, K.O.2    Kim, M.3    Song, J.Y.4    Lee, K.H.5    Park, J.6
  • 111
    • 79951580512 scopus 로고    scopus 로고
    • Antitumor activity of HM781-36B, an irreversible Pan-HER inhibitor, alone or in combination with cytotoxic chemotherapeutic agents in gastric cancer
    • H.J. Nam, H.P. Kim, Y.K. Yoon, H.S. Hur, S.H. Song, and M.S. Kim et al. Antitumor activity of HM781-36B, an irreversible Pan-HER inhibitor, alone or in combination with cytotoxic chemotherapeutic agents in gastric cancer Cancer Lett 302 2011 155 165
    • (2011) Cancer Lett , vol.302 , pp. 155-165
    • Nam, H.J.1    Kim, H.P.2    Yoon, Y.K.3    Hur, H.S.4    Song, S.H.5    Kim, M.S.6
  • 112
    • 84856822581 scopus 로고    scopus 로고
    • Phase i first-in-human study of TAK-285, a novel investigational dual HER2/EGFR inhibitor, in cancer patients
    • T. Doi, H. Takiuchi, A. Ohtsu, N. Fuse, M. Goto, and M. Yoshida et al. Phase I first-in-human study of TAK-285, a novel investigational dual HER2/EGFR inhibitor, in cancer patients Br J Cancer 106 2012 666 672
    • (2012) Br J Cancer , vol.106 , pp. 666-672
    • Doi, T.1    Takiuchi, H.2    Ohtsu, A.3    Fuse, N.4    Goto, M.5    Yoshida, M.6
  • 113
    • 84899105729 scopus 로고    scopus 로고
    • Phase 1 dose-escalation, pharmacokinetic, and cerebrospinal fluid distribution study of TAK-285, an investigational inhibitor of EGFR and HER2
    • P. Lorusso, K. Venkatakrishnan, E.G. Chiorean, D. Noe, J.T. Wu, and S. Sankoh et al. Phase 1 dose-escalation, pharmacokinetic, and cerebrospinal fluid distribution study of TAK-285, an investigational inhibitor of EGFR and HER2 Invest New Drugs 32 2014 160 170
    • (2014) Invest New Drugs , vol.32 , pp. 160-170
    • Lorusso, P.1    Venkatakrishnan, K.2    Chiorean, E.G.3    Noe, D.4    Wu, J.T.5    Sankoh, S.6
  • 114
    • 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
  • 115
    • 84857716200 scopus 로고    scopus 로고
    • WZ4002, a third-generation EGFR inhibitor, can overcome anoikis resistance in EGFR-mutant lung adenocarcinomas more efficiently than Src inhibitors
    • Y. Sakuma, Y. Yamazaki, Y. Nakamura, M. Yoshihara, S. Matsukuma, and H. Nakayama et al. WZ4002, a third-generation EGFR inhibitor, can overcome anoikis resistance in EGFR-mutant lung adenocarcinomas more efficiently than Src inhibitors Lab Invest 92 2012 371 383
    • (2012) Lab Invest , vol.92 , pp. 371-383
    • Sakuma, Y.1    Yamazaki, Y.2    Nakamura, Y.3    Yoshihara, M.4    Matsukuma, S.5    Nakayama, H.6
  • 116
    • 84860216901 scopus 로고    scopus 로고
    • Differential action of small molecule HER kinase inhibitors on receptor heterodimerization: Therapeutic implications
    • M. Sánchez-Martín, and A. Pandiella Differential action of small molecule HER kinase inhibitors on receptor heterodimerization: therapeutic implications Int J Cancer 131 2012 244 252
    • (2012) Int J Cancer , vol.131 , pp. 244-252
    • Sánchez-Martín, M.1    Pandiella, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.