메뉴 건너뛰기




Volumn 56, Issue 10, 2013, Pages 3889-3903

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

Author keywords

[No Author keywords available]

Indexed keywords

6 [4 (4 ETHYL 1 PIPERAZINYLMETHYL)PHENYL] 4 (ALPHA METHYLBENZYLAMINO) 7H PYRROLO[2,3 D]PYRIMIDINE; AMINO ACID DERIVATIVE; ASPARTIC ACID; ASPARTYLPHENYLALANYLGLYCINE; EPIDERMAL GROWTH FACTOR RECEPTOR; EPIDERMAL GROWTH FACTOR RECEPTOR KINASE INHIBITOR; GEFITINIB; GLYCINE DERIVATIVE; N,N, DIMETHYLAMINO; PHENYL GROUP; PROTEIN KINASE INHIBITOR; SODIUM CHLORIDE; UNCLASSIFIED DRUG;

EID: 84878095831     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm400072p     Document Type: Article
Times cited : (109)

References (71)
  • 2
    • 77950573400 scopus 로고    scopus 로고
    • Through the "gatekeeper door": Exploiting the active kinase conformation
    • Zuccotto, F.; Ardini, E.; Casale, E.; Angiolini, M. Through the "gatekeeper door": exploiting the active kinase conformation J. Med. Chem. 2010, 53, 2681-2694
    • (2010) J. Med. Chem. , vol.53 , pp. 2681-2694
    • Zuccotto, F.1    Ardini, E.2    Casale, E.3    Angiolini, M.4
  • 3
    • 57749188299 scopus 로고    scopus 로고
    • Targeting cancer with small molecule kinase inhibitors
    • Zhang, J.; Yang, P. L.; Gray, N. S. Targeting cancer with small molecule kinase inhibitors Nature Rev. Cancer 2009, 9, 28-39
    • (2009) Nature Rev. Cancer , vol.9 , pp. 28-39
    • Zhang, J.1    Yang, P.L.2    Gray, N.S.3
  • 4
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse, M.; Kuriyan, J. The conformational plasticity of protein kinases Cell 2002, 109, 275-282
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 5
    • 34249818791 scopus 로고    scopus 로고
    • C-Abl tyrosine kinase and inhibition by the cancer drug imatinib (Gleevec/STI-571)
    • Nagar, B. c-Abl tyrosine kinase and inhibition by the cancer drug imatinib (Gleevec/STI-571) J. Nutr. 2007, 137, 1518S-1523S
    • (2007) J. Nutr. , vol.137
    • Nagar, B.1
  • 6
    • 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. 1997, 16, 5572-5581
    • (1997) EMBO J. , vol.16 , pp. 5572-5581
    • Hubbard, S.R.1
  • 7
    • 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 1994, 372, 746-754
    • (1994) Nature , vol.372 , pp. 746-754
    • Hubbard, S.R.1    Wei, L.2    Ellis, L.3    Hendrickson, W.A.4
  • 8
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • Sicheri, F.; Moarefi, I.; Kuriyan, J. Crystal structure of the Src family tyrosine kinase Hck Nature 1997, 385, 602-609
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 9
    • 9444287030 scopus 로고    scopus 로고
    • Common and distinct elements in cellular signaling via EGF and FGF receptors
    • Schlessinger, J. Common and distinct elements in cellular signaling via EGF and FGF receptors Science 2004, 306, 1506-1507
    • (2004) Science , vol.306 , pp. 1506-1507
    • Schlessinger, J.1
  • 10
    • 63749086305 scopus 로고    scopus 로고
    • ErbB receptors and signaling pathways in cancer
    • Hynes, N. E.; MacDonald, G. ErbB receptors and signaling pathways in cancer Curr. Opin. Cell Biol. 2009, 21, 177-184
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 177-184
    • Hynes, N.E.1    MacDonald, G.2
  • 11
    • 0035144559 scopus 로고    scopus 로고
    • Mistletoe for cancer?
    • Ernst, E. Mistletoe for cancer? Eur. J. Cancer 2001, 37, 9-11
    • (2001) Eur. J. Cancer , vol.37 , pp. 9-11
    • Ernst, E.1
  • 12
    • 0033992633 scopus 로고    scopus 로고
    • Biochemical and clinical implications of the ErbB/HER signaling network of growth factor receptors
    • Klapper, L. N.; Kirschbaum, M. H.; Sela, M.; Yarden, Y. Biochemical and clinical implications of the ErbB/HER signaling network of growth factor receptors Adv. Cancer Res. 2000, 77, 25-79
    • (2000) Adv. Cancer Res. , vol.77 , pp. 25-79
    • Klapper, L.N.1    Kirschbaum, M.H.2    Sela, M.3    Yarden, Y.4
  • 13
    • 0034600849 scopus 로고    scopus 로고
    • The ErbB signaling network: Receptor heterodimerization in development and cancer
    • Olayioye, M. A.; Neve, R. M.; Lane, H. A.; Hynes, N. E. The ErbB signaling network: receptor heterodimerization in development and cancer EMBO J. 2000, 19, 3159-3167
    • (2000) EMBO J. , vol.19 , pp. 3159-3167
    • Olayioye, M.A.1    Neve, R.M.2    Lane, H.A.3    Hynes, N.E.4
  • 14
    • 0141599428 scopus 로고    scopus 로고
    • Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor
    • Stamos, J.; Sliwkowski, M. X.; Eigenbrot, C. Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor J. Biol. Chem. 2002, 277, 46265-46272
    • (2002) J. Biol. Chem. , vol.277 , pp. 46265-46272
    • Stamos, J.1    Sliwkowski, M.X.2    Eigenbrot, C.3
  • 15
    • 31544434945 scopus 로고    scopus 로고
    • Cetuximab and irinotecan interact synergistically to inhibit the growth of orthotopic anaplastic thyroid carcinoma xenografts in nude mice
    • Kim, S.; Prichard, C. N.; Younes, M. N.; Yazici, Y. D.; Jasser, S. A.; Bekele, B. N.; Myers, J. N. Cetuximab and irinotecan interact synergistically to inhibit the growth of orthotopic anaplastic thyroid carcinoma xenografts in nude mice Clin. Cancer Res. 2006, 12, 600-607
    • (2006) Clin. Cancer Res. , vol.12 , pp. 600-607
    • Kim, S.1    Prichard, C.N.2    Younes, M.N.3    Yazici, Y.D.4    Jasser, S.A.5    Bekele, B.N.6    Myers, J.N.7
  • 16
    • 0033763084 scopus 로고    scopus 로고
    • ZD1839 ('Iressa') as an anticancer agent
    • Baselga, J.; Averbuch, S. D. ZD1839 ('Iressa') as an anticancer agent Drugs 2000, 60, 33-40
    • (2000) Drugs , vol.60 , pp. 33-40
    • Baselga, J.1    Averbuch, S.D.2
  • 17
    • 33847406095 scopus 로고    scopus 로고
    • Structures of lung cancer-derived EGFR mutants and inhibitor complexes: Mechanism of activation and insights into differential inhibitor sensitivity
    • Yun, C. H.; Boggon, T. J.; Li, Y.; Woo, M. S.; Greulich, H.; Meyerson, M.; Eck, M. J. Structures of lung cancer-derived EGFR mutants and inhibitor complexes: mechanism of activation and insights into differential inhibitor sensitivity Cancer Cell 2007, 11, 217-227
    • (2007) Cancer Cell , vol.11 , 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
  • 18
    • 0035553174 scopus 로고    scopus 로고
    • The effects of the novel, reversible epidermal growth factor receptor/ErbB-2 tyrosine kinase inhibitor, GW2016, on the growth of human normal and tumor-derived cell lines in vitro and in vivo
    • Rusnak, D. W.; Lackey, K.; Affleck, K.; Wood, E. R.; Alligood, K. J.; Rhodes, N.; Keith, B. R.; Murray, D. M.; Knight, W. B.; Mullin, R. J.; Gilmer, T. M. The effects of the novel, reversible epidermal growth factor receptor/ErbB-2 tyrosine kinase inhibitor, GW2016, on the growth of human normal and tumor-derived cell lines in vitro and in vivo Mol. Cancer Ther. 2001, 1, 85-94
    • (2001) Mol. Cancer Ther. , vol.1 , pp. 85-94
    • Rusnak, D.W.1    Lackey, K.2    Affleck, K.3    Wood, E.R.4    Alligood, K.J.5    Rhodes, N.6    Keith, B.R.7    Murray, D.M.8    Knight, W.B.9    Mullin, R.J.10    Gilmer, T.M.11
  • 20
    • 20944433324 scopus 로고    scopus 로고
    • Dual inhibition of epidermal growth factor receptor and vascular endothelial growth factor receptor phosphorylation by AEE788 reduces growth and metastasis of human colon carcinoma in an orthotopic nude mouse model
    • Yokoi, K.; Thaker, P. H.; Yazici, S.; Rebhun, R. R.; Nam, D. H.; He, J.; Kim, S. J.; Abbruzzese, J. L.; Hamilton, S. R.; Fidler, I. J. Dual inhibition of epidermal growth factor receptor and vascular endothelial growth factor receptor phosphorylation by AEE788 reduces growth and metastasis of human colon carcinoma in an orthotopic nude mouse model Cancer Res. 2005, 65, 3716-3725
    • (2005) Cancer Res. , vol.65 , pp. 3716-3725
    • Yokoi, K.1    Thaker, P.H.2    Yazici, S.3    Rebhun, R.R.4    Nam, D.H.5    He, J.6    Kim, S.J.7    Abbruzzese, J.L.8    Hamilton, S.R.9    Fidler, I.J.10
  • 27
    • 38049038935 scopus 로고    scopus 로고
    • A phase i dose escalation study of BIBW 2992, an irreversible dual inhibitor of epidermal growth factor receptor 1 (EGFR) and 2 (HER2) tyrosine kinase in a 2-week on, 2-week off schedule in patients with advanced solid tumours
    • Eskens, F. A.; Mom, C. H.; Planting, A. S.; Gietema, J. A.; Amelsberg, A.; Huisman, H.; van Doorn, L.; Burger, H.; Stopfer, P.; Verweij, J.; de Vries, E. G. A phase I dose escalation study of BIBW 2992, an irreversible dual inhibitor of epidermal growth factor receptor 1 (EGFR) and 2 (HER2) tyrosine kinase in a 2-week on, 2-week off schedule in patients with advanced solid tumours Br. J. Cancer 2008, 98, 80-85
    • (2008) Br. J. Cancer , vol.98 , pp. 80-85
    • Eskens, F.A.1    Mom, C.H.2    Planting, A.S.3    Gietema, J.A.4    Amelsberg, A.5    Huisman, H.6    Van Doorn, L.7    Burger, H.8    Stopfer, P.9    Verweij, J.10    De Vries, E.G.11
  • 32
    • 38049025794 scopus 로고    scopus 로고
    • Review: Side effects of approved molecular targeted therapies in solid cancers
    • Widakowich, C.; de Castro, G., Jr.; de Azambuja, E.; Dinh, P.; Awada, A. Review: side effects of approved molecular targeted therapies in solid cancers Oncologist 2007, 12, 1443-1455
    • (2007) Oncologist , vol.12 , pp. 1443-1455
    • Widakowich, C.1    De Castro Jr., G.2    De Azambuja, E.3    Dinh, P.4    Awada, A.5
  • 34
    • 84870840686 scopus 로고    scopus 로고
    • Strategies for Overcoming EGFR Resistance in the Treatment of Advanced-Stage NSCLC
    • Lovly, C. M.; Horn, L. Strategies for Overcoming EGFR Resistance in the Treatment of Advanced-Stage NSCLC Curr. Treat. Options Oncol. 2012, 13, 516-526
    • (2012) Curr. Treat. Options Oncol. , vol.13 , pp. 516-526
    • Lovly, C.M.1    Horn, L.2
  • 35
    • 80051974226 scopus 로고    scopus 로고
    • Off-target serine/threonine kinase 10 inhibition by erlotinib enhances lymphocytic activity leading to severe skin disorders
    • Yamamoto, N.; Honma, M.; Suzuki, H. Off-target serine/threonine kinase 10 inhibition by erlotinib enhances lymphocytic activity leading to severe skin disorders Mol. Pharmacol. 2011, 80, 466-475
    • (2011) Mol. Pharmacol. , vol.80 , pp. 466-475
    • Yamamoto, N.1    Honma, M.2    Suzuki, H.3
  • 39
    • 19944426858 scopus 로고    scopus 로고
    • High frequency of epidermal growth factor receptor mutations with complex patterns in non-small cell lung cancers related to gefitinib responsiveness in Taiwan
    • Huang, S. F.; Liu, H. P.; Li, L. H.; Ku, Y. C.; Fu, Y. N.; Tsai, H. Y.; Chen, Y. T.; Lin, Y. F.; Chang, W. C.; Kuo, H. P.; Wu, Y. C.; Chen, Y. R.; Tsai, S. F. High frequency of epidermal growth factor receptor mutations with complex patterns in non-small cell lung cancers related to gefitinib responsiveness in Taiwan Clin. Cancer Res. 2004, 10, 8195-8203
    • (2004) Clin. Cancer Res. , vol.10 , pp. 8195-8203
    • Huang, S.F.1    Liu, H.P.2    Li, L.H.3    Ku, Y.C.4    Fu, Y.N.5    Tsai, H.Y.6    Chen, Y.T.7    Lin, Y.F.8    Chang, W.C.9    Kuo, H.P.10    Wu, Y.C.11    Chen, Y.R.12    Tsai, S.F.13
  • 40
    • 0036682301 scopus 로고    scopus 로고
    • Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571)
    • Nagar, B.; Bornmann, W. G.; Pellicena, P.; Schindler, T.; Veach, D. R.; Miller, W. T.; Clarkson, B.; Kuriyan, J. Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571) Cancer Res. 2002, 62, 4236-4243
    • (2002) Cancer Res. , vol.62 , pp. 4236-4243
    • Nagar, B.1    Bornmann, W.G.2    Pellicena, P.3    Schindler, T.4    Veach, D.R.5    Miller, W.T.6    Clarkson, B.7    Kuriyan, J.8
  • 42
    • 77955664248 scopus 로고    scopus 로고
    • X-ray crystal structure of JNK2 complexed with the p38alpha inhibitor BIRB796: Insights into the rational design of DFG-out binding MAP kinase inhibitors
    • Kuglstatter, A.; Ghate, M.; Tsing, S.; Villasenor, A. G.; Shaw, D.; Barnett, J. W.; Browner, M. F. X-ray crystal structure of JNK2 complexed with the p38alpha inhibitor BIRB796: insights into the rational design of DFG-out binding MAP kinase inhibitors Bioorg. Med. Chem. Lett. 2010, 20, 5217-5220
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , pp. 5217-5220
    • Kuglstatter, A.1    Ghate, M.2    Tsing, S.3    Villasenor, A.G.4    Shaw, D.5    Barnett, J.W.6    Browner, M.F.7
  • 45
    • 65549152514 scopus 로고    scopus 로고
    • Equally potent inhibition of c-Src and Abl by compounds that recognize inactive kinase conformations
    • Seeliger, M. A.; Ranjitkar, P.; Kasap, C.; Shan, Y.; Shaw, D. E.; Shah, N. P.; Kuriyan, J.; Maly, D. J. Equally potent inhibition of c-Src and Abl by compounds that recognize inactive kinase conformations Cancer Res. 2009, 69, 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    Kuriyan, J.7    Maly, D.J.8
  • 46
    • 33847659183 scopus 로고    scopus 로고
    • C-Src binds to the cancer drug imatinib with an inactive Abl/c-Kit conformation and a distributed thermodynamic penalty
    • Seeliger, M. A.; Nagar, B.; Frank, F.; Cao, X.; Henderson, M. N.; Kuriyan, J. c-Src binds to the cancer drug imatinib with an inactive Abl/c-Kit conformation and a distributed thermodynamic penalty Structure 2007, 15, 299-311
    • (2007) Structure , vol.15 , pp. 299-311
    • Seeliger, M.A.1    Nagar, B.2    Frank, F.3    Cao, X.4    Henderson, M.N.5    Kuriyan, J.6
  • 50
    • 84865527163 scopus 로고    scopus 로고
    • An integrated chemical biology approach provides insight into Cdk2 functional redundancy and inhibitor sensitivity
    • Echalier, A.; Cot, E.; Camasses, A.; Hodimont, E.; Hoh, F.; Jay, P.; Sheinerman, F.; Krasinska, L.; Fisher, D. An integrated chemical biology approach provides insight into Cdk2 functional redundancy and inhibitor sensitivity Chem. Biol. 2012, 19, 1028-1040
    • (2012) Chem. Biol. , vol.19 , pp. 1028-1040
    • Echalier, A.1    Cot, E.2    Camasses, A.3    Hodimont, E.4    Hoh, F.5    Jay, P.6    Sheinerman, F.7    Krasinska, L.8    Fisher, D.9
  • 51
    • 84873908358 scopus 로고    scopus 로고
    • Comparative Structural and Functional Studies of 4-(Thiazol-5-yl)-2- (phenylamino)pyrimidine-5-carbonitrile CDK9 Inhibitors Suggest the Basis for Isotype Selectivity
    • Hole, A. J.; Baumli, S.; Shao, H.; Shi, S.; Huang, S.; Pepper, C.; Fischer, P. M.; Wang, S.; Endicott, J. A.; Noble, M. E. Comparative Structural and Functional Studies of 4-(Thiazol-5-yl)-2-(phenylamino)pyrimidine-5- carbonitrile CDK9 Inhibitors Suggest the Basis for Isotype Selectivity J. Med. Chem. 2013, 56, 660-670
    • (2013) J. Med. Chem. , vol.56 , pp. 660-670
    • Hole, A.J.1    Baumli, S.2    Shao, H.3    Shi, S.4    Huang, S.5    Pepper, C.6    Fischer, P.M.7    Wang, S.8    Endicott, J.A.9    Noble, M.E.10
  • 52
    • 84872309000 scopus 로고    scopus 로고
    • Optimization of inhibitors of the tyrosine kinase EphB4. 2. Cellular potency improvement and binding mode validation by X-ray crystallography
    • Lafleur, K.; Dong, J.; Huang, D.; Caflisch, A.; Nevado, C. Optimization of inhibitors of the tyrosine kinase EphB4. 2. Cellular potency improvement and binding mode validation by X-ray crystallography J. Med. Chem. 2013, 56, 84-96
    • (2013) J. Med. Chem. , vol.56 , pp. 84-96
    • Lafleur, K.1    Dong, J.2    Huang, D.3    Caflisch, A.4    Nevado, C.5
  • 62
    • 61349149899 scopus 로고    scopus 로고
    • Dissecting specificity in the Janus kinases: The structures of JAK-specific inhibitors complexed to the JAK1 and JAK2 protein tyrosine kinase domains
    • Williams, N. K.; Bamert, R. S.; Patel, O.; Wang, C.; Walden, P. M.; Wilks, A. F.; Fantino, E.; Rossjohn, J.; Lucet, I. S. Dissecting specificity in the Janus kinases: the structures of JAK-specific inhibitors complexed to the JAK1 and JAK2 protein tyrosine kinase domains J. Mol. Biol. 2009, 387, 219-232
    • (2009) J. Mol. Biol. , vol.387 , pp. 219-232
    • Williams, N.K.1    Bamert, R.S.2    Patel, O.3    Wang, C.4    Walden, P.M.5    Wilks, A.F.6    Fantino, E.7    Rossjohn, J.8    Lucet, I.S.9
  • 63
    • 77950473958 scopus 로고    scopus 로고
    • Kinase selectivity potential for inhibitors targeting the ATP binding site: A network analysis
    • Huang, D.; Zhou, T.; Lafleur, K.; Nevado, C.; Caflisch, A. Kinase selectivity potential for inhibitors targeting the ATP binding site: a network analysis Bioinformatics 2010, 26, 198-204
    • (2010) Bioinformatics , vol.26 , pp. 198-204
    • Huang, D.1    Zhou, T.2    Lafleur, K.3    Nevado, C.4    Caflisch, A.5
  • 66
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin, A.; Teplyakov, A. MOLREP: an automated program for molecular replacement J. Appl. Crystallogr. 1997, 30, 1022-1025
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 69
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A.; Zou, J. Y.; Cowan, S. W.; Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallogr., Sect. A: Found. Crystallogr. 1991, 47, 110-119
    • (1991) Acta Crystallogr., Sect. A: Found. Crystallogr. , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.