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Volumn 42, Issue 26, 1999, Pages 5369-5389

Design and structure-activity relationship of a new class of potent VEGF receptor tyrosine kinase inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN TYROSINE KINASE INHIBITOR; QUINAZOLINE DERIVATIVE; QUINOLINE DERIVATIVE; VASCULOTROPIN RECEPTOR;

EID: 17544387877     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm990345w     Document Type: Article
Times cited : (263)

References (79)
  • 1
    • 0028912119 scopus 로고
    • Controlling the vasculature: Angiogenesis, anti-angiogenesis, and vascular targeting of gene therapy
    • Fan, T. P. D.; Jaggar, R.; Bicknell, R., Controlling the vasculature: angiogenesis, anti-angiogenesis, and vascular targeting of gene therapy. Trends Pharmacol. Sci. 1995, 16, 57-66.
    • (1995) Trends Pharmacol. Sci. , vol.16 , pp. 57-66
    • Fan, T.P.D.1    Jaggar, R.2    Bicknell, R.3
  • 2
    • 0028929803 scopus 로고
    • Angiogenesis in cancer, vascular, rheumatoid and other disease
    • Folkman, J. Angiogenesis in cancer, vascular, rheumatoid and other disease. Nature Medicine 1995, 1, 27-31.
    • (1995) Nature Medicine , vol.1 , pp. 27-31
    • Folkman, J.1
  • 3
    • 0027183674 scopus 로고
    • Vascular endothelial growth factor/vascular permeability factor expression in the rat uterus: Rapid stimulation by estrogen correlates with estrogen-induced increases in uterine capillary permeability and growth
    • Cullinan-Bove, K.; Koos, R. D. Vascular endothelial growth factor/vascular permeability factor expression in the rat uterus: Rapid stimulation by estrogen correlates with estrogen-induced increases in uterine capillary permeability and growth. Endocrinology 1993, 133, 829-837.
    • (1993) Endocrinology , vol.133 , pp. 829-837
    • Cullinan-Bove, K.1    Koos, R.D.2
  • 5
    • 0030576517 scopus 로고    scopus 로고
    • Patterns and emerging mechanisms of the angiogenic switch during tumorigenesis
    • Hananhan, D.; Folkman, J. Patterns and emerging mechanisms of the angiogenic switch during tumorigenesis. Cell 1996, 86, 353-364.
    • (1996) Cell , vol.86 , pp. 353-364
    • Hananhan, D.1    Folkman, J.2
  • 6
    • 0027171960 scopus 로고
    • Developmental expression of binding sites and messenger ribonucleic acid for vascular endothelial growth factor suggests a role for this protein in vasculogenesis and angiogenesis
    • Jakeman, L. B.; Armanmi, M.; Phillips, H. S.; Ferrara, N. Developmental expression of binding sites and messenger ribonucleic acid for vascular endothelial growth factor suggests a role for this protein in vasculogenesis and angiogenesis. Endocrinology 1993, 133, 848-859.
    • (1993) Endocrinology , vol.133 , pp. 848-859
    • Jakeman, L.B.1    Armanmi, M.2    Phillips, H.S.3    Ferrara, N.4
  • 8
    • 0028023922 scopus 로고
    • Receptor tyrosine kinases as targets for drug intervention
    • Plowman, G. D.; Ullrich, A.; Shawver, L. K. Receptor tyrosine kinases as targets for drug intervention. Drug News Perspect. 1994, 7, 334-339.
    • (1994) Drug News Perspect. , vol.7 , pp. 334-339
    • Plowman, G.D.1    Ullrich, A.2    Shawver, L.K.3
  • 9
    • 85017325712 scopus 로고    scopus 로고
    • Tyrosine kinases in disease: Overview of kinase inhibitors as therapeutic agents and current drugs in clinical trials
    • Straw, L. M.; Shawver, L. K. Tyrosine kinases in disease: overview of kinase inhibitors as therapeutic agents and current drugs in clinical trials. Exp. Opin. Invest. Drugs 1998, 7, 553-573.
    • (1998) Exp. Opin. Invest. Drugs , vol.7 , pp. 553-573
    • Straw, L.M.1    Shawver, L.K.2
  • 11
    • 0028941001 scopus 로고
    • Vascular endothelial growth factor in human glioma cell lines: Induced secretion by EGF, PDGF-BB, and bFGF
    • Tsai, J.-C.; Goldman C. K.; Gillespie, G. Y. Vascular endothelial growth factor in human glioma cell lines: induced secretion by EGF, PDGF-BB, and bFGF. J. Neurosurg. 1995, 82, 864-873.
    • (1995) J. Neurosurg. , vol.82 , pp. 864-873
    • Tsai, J.-C.1    Goldman, C.K.2    Gillespie, G.Y.3
  • 12
    • 0030031898 scopus 로고    scopus 로고
    • Expression of vascular permeability factor/vascular endothelial growth factor by melanoma cells increases tumour growth, angiogenesis, and experimental metastasis
    • Claffey, K. P.; Brown, L. F.; Del Aguila, L. F.; Tognazzi, K.; Manseau, E. J.; Dvorak, H. F. Expression of vascular permeability factor/vascular endothelial growth factor by melanoma cells increases tumour growth, angiogenesis, and experimental metastasis. Cancer Res. 1996, 56, 172-181.
    • (1996) Cancer Res. , vol.56 , pp. 172-181
    • Claffey, K.P.1    Brown, L.F.2    Del Aguila, L.F.3    Tognazzi, K.4    Manseau, E.J.5    Dvorak, H.F.6
  • 13
    • 0029878789 scopus 로고    scopus 로고
    • Vascular endothelial growth factor and platelet-derived growth factor are potential angiogenic and metastatic factors in human breast cancer
    • Anan, K.; Morosaki, T.; Katano, M. Vascular endothelial growth factor and platelet-derived growth factor are potential angiogenic and metastatic factors in human breast cancer. Surgery 1996, 119, 333-339.
    • (1996) Surgery , vol.119 , pp. 333-339
    • Anan, K.1    Morosaki, T.2    Katano, M.3
  • 14
    • 0029935566 scopus 로고    scopus 로고
    • Expression of vascular endothelial growth factor, its receptor, and other angiogenic factors in human breast cancer
    • Yoshiji H.; Gomez D. E.; Shibuya, M.; Thorgeirsson, U. P. Expression of vascular endothelial growth factor, its receptor, and other angiogenic factors in human breast cancer. Cancer Res. 1996, 56, 2013-2016.
    • (1996) Cancer Res. , vol.56 , pp. 2013-2016
    • Yoshiji, H.1    Gomez, D.E.2    Shibuya, M.3    Thorgeirsson, U.P.4
  • 15
    • 0027482251 scopus 로고
    • Expression of vascular permeability factor (vascular endothelial growth factor) and its receptors in adenocarcinomas of the gastrointestinal tract
    • Brown, L. F.; Berse, B.; Jackman, R. W.; Tognazzi, K.; Manseau, E. J.; Senger, D. R.; Dvorak, H. F. Expression of vascular permeability factor (vascular endothelial growth factor) and its receptors in adenocarcinomas of the gastrointestinal tract. Cancer Res. 1993, 53, 4727-4735.
    • (1993) Cancer Res. , vol.53 , pp. 4727-4735
    • Brown, L.F.1    Berse, B.2    Jackman, R.W.3    Tognazzi, K.4    Manseau, E.J.5    Senger, D.R.6    Dvorak, H.F.7
  • 16
    • 84970070220 scopus 로고
    • Expression of vascular endothelial growth factor and its receptor, KDR correlates with vascularity, metastasis, and proliferation of human colon cancer
    • Takahashi, Y.; Kitadai, Y.; Bucana, C. D.; Cleary, K. R.; Ellis, L. M. Expression of vascular endothelial growth factor and its receptor, KDR correlates with vascularity, metastasis, and proliferation of human colon cancer. Cancer Res. 1995, 55, 3964-3968.
    • (1995) Cancer Res. , vol.55 , pp. 3964-3968
    • Takahashi, Y.1    Kitadai, Y.2    Bucana, C.D.3    Cleary, K.R.4    Ellis, L.M.5
  • 17
    • 0027933191 scopus 로고
    • Markedly increased amounts of messenger RNAs for vascular endothelial growth factor and placenta growth factor in renal cell carcinoma associated with angiogenesis
    • Takahashi, A.; Sasaki, H.; Kim, S. J.; Tobisu, K.-I.; Kakizoe, T.; Tsukamoto, T.; Kumamoto, Y.; Sugimura, T.; Terada, M. Markedly increased amounts of messenger RNAs for vascular endothelial growth factor and placenta growth factor in renal cell carcinoma associated with angiogenesis. Cancer Res. 1994, 54, 4233-4237.
    • (1994) Cancer Res. , vol.54 , pp. 4233-4237
    • Takahashi, A.1    Sasaki, H.2    Kim, S.J.3    Tobisu, K.-I.4    Kakizoe, T.5    Tsukamoto, T.6    Kumamoto, Y.7    Sugimura, T.8    Terada, M.9
  • 18
    • 0025343230 scopus 로고
    • Signal transduction by receptor tyrosine kinase activity
    • Ullrich, A.; Schlessinger J. Signal transduction by receptor tyrosine kinase activity. Cell 1990, 61, 203-212.
    • (1990) Cell , vol.61 , pp. 203-212
    • Ullrich, A.1    Schlessinger, J.2
  • 19
    • 0025756650 scopus 로고
    • Growth factors and tyrosine protein kinases in normal and Malignant Melanocytes
    • Halaban, K. Growth factors and tyrosine protein kinases in normal and Malignant Melanocytes. Cancer Met. Rev. 1991, 10, 129-140.
    • (1991) Cancer Met. Rev. , vol.10 , pp. 129-140
    • Halaban, K.1
  • 20
    • 0023145547 scopus 로고
    • The Molecular genetic of cancer
    • Bishop, J. M. The Molecular genetic of cancer. Science 1987, 335, 305-311.
    • (1987) Science , vol.335 , pp. 305-311
    • Bishop, J.M.1
  • 21
    • 0026572345 scopus 로고
    • The fms-like tyrosine kinase, a receptor for vascular endothelial growth factor
    • De Vries, C.; Escobedo, J. A.; Ueno, H.; Houck, K.; Ferrara, N.; Williams, L. T. The fms-like tyrosine kinase, a receptor for vascular endothelial growth factor. Science 1992, 255, 989-991.
    • (1992) Science , vol.255 , pp. 989-991
    • De Vries, C.1    Escobedo, J.A.2    Ueno, H.3    Houck, K.4    Ferrara, N.5    Williams, L.T.6
  • 23
    • 0027197245 scopus 로고
    • Inhibition of vascular endothelial growth factor-induced angiogenesis suppresses tumor growth in vivo
    • Kim, K. L.; Li, B.; Winer, J.; Armanini, M.; Gillett, N.; Phillips, H. S.; Ferrara, N. Inhibition of vascular endothelial growth factor-induced angiogenesis suppresses tumor growth in vivo. Nature 1993, 362, 841-844.
    • (1993) Nature , vol.362 , pp. 841-844
    • Kim, K.L.1    Li, B.2    Winer, J.3    Armanini, M.4    Gillett, N.5    Phillips, H.S.6    Ferrara, N.7
  • 24
    • 0032474915 scopus 로고    scopus 로고
    • Synthesis and Biological Evaluation of 3-substituted Indolin-2-ones: ANovel Class of Tyrosine Kinase Inhibitors That Exhibit Selectivity toward Particular Receptor tyrosine Kinases
    • Sun, L.; Tran, N.; Tang, F.; App, H.; Hirth P.; McMahon G.; Tang, C. Synthesis and Biological Evaluation of 3-substituted Indolin-2-ones: ANovel Class of Tyrosine Kinase Inhibitors That Exhibit Selectivity toward Particular Receptor tyrosine Kinases. J. Med. Chem. 1998, 41, 2588-2603.
    • (1998) J. Med. Chem. , vol.41 , pp. 2588-2603
    • Sun, L.1    Tran, N.2    Tang, F.3    App, H.4    Hirth, P.5    McMahon, G.6    Tang, C.7
  • 25
    • 0030039555 scopus 로고    scopus 로고
    • Tyrosine kinase inhibitors. 8. An unusually steep structure-activity relationship for analogues of 4-(3-bromoanilino)-6,7-dimethoxyquinazoline (PD 153035), a potent inhibitor of the epidermal growth factor receptor
    • Bridges, A. J.; Zhou, H.; Cody, D. R.; Rewcastle, G. W.; McMichael, A.; Showalter, H. D.; Fry, D. W.; Kraker, A. J.; Denny, W. A. Tyrosine kinase inhibitors. 8. An unusually steep structure-activity relationship for analogues of 4-(3-bromoanilino)-6,7-dimethoxyquinazoline (PD 153035), a potent inhibitor of the epidermal growth factor receptor. J. Med. Chem. 1996, 39, 267-276.
    • (1996) J. Med. Chem. , vol.39 , pp. 267-276
    • Bridges, A.J.1    Zhou, H.2    Cody, D.R.3    Rewcastle, G.W.4    McMichael, A.5    Showalter, H.D.6    Fry, D.W.7    Kraker, A.J.8    Denny, W.A.9
  • 26
    • 0017349724 scopus 로고
    • Synthesis and identification of the major metabolites of prazosin in dog and rat
    • Althuis, T. H.; Hess, H. J. Synthesis and Identification of the Major Metabolites of Prazosin in dog and Rat. J. Med. Chem. 1977, 20, 146-149.
    • (1977) J. Med. Chem. , vol.20 , pp. 146-149
    • Althuis, T.H.1    Hess, H.J.2
  • 27
    • 13344262678 scopus 로고    scopus 로고
    • Tyrosine kinase inhibitors. 9. Synthesis and evaluation of fused tricyclic quinazoline analogues as ATP site inhibitors of the tyrosine kinase activity of the epidermal growth factor receptor
    • Rewcastle, G. W.; Palmer, B. D.; Bridges, A. J.; Showalter, H. D.; Sun, L. Tyrosine kinase inhibitors. 9. Synthesis and evaluation of fused tricyclic quinazoline analogues as ATP site inhibitors of the tyrosine kinase activity of the epidermal growth factor receptor. J. Med. Chem. 1996, 4, 918-928.
    • (1996) J. Med. Chem. , vol.4 , pp. 918-928
    • Rewcastle, G.W.1    Palmer, B.D.2    Bridges, A.J.3    Showalter, H.D.4    Sun, L.5
  • 28
    • 0343737650 scopus 로고    scopus 로고
    • unpublished data
    • Zeneca, unpublished data.
    • Zeneca1
  • 35
    • 0028106163 scopus 로고
    • Epidermal growth factor receptor tyrosine kinase. Investigation of catalytic mechanism, structure-based searching and discovery of a potent inhibitor
    • Ward, W. H. J.; Cook, P. N.; Slater, A. M.; Davies, D. H.; Holdgate, G. A.; Green, L. R. Epidermal growth factor receptor tyrosine kinase. Investigation of catalytic mechanism, structure-based searching and discovery of a potent inhibitor. Biochem. Pharmacol. 1994, 48(4), 659-666.
    • (1994) Biochem. Pharmacol. , vol.48 , Issue.4 , pp. 659-666
    • Ward, W.H.J.1    Cook, P.N.2    Slater, A.M.3    Davies, D.H.4    Holdgate, G.A.5    Green, L.R.6
  • 36
    • 0029130763 scopus 로고
    • Tyrosine kinase inhibitors. 5. Synthesis and structure-activity relationships for 4-[(phenyl-methyl)amino]- and 4-(phenylamino)quinazolines as potent adenosine 5′-triphosphate binding site inhibitors of the tyrosine kinase domain of the epidermal growth factor receptor
    • Rewcastle, G. W.; Denny, W. A., Bridges, A. J.; Zhou, H.; Cody, D. R.; McMichael, A.; Fry, D. W. Tyrosine kinase inhibitors. 5. Synthesis and structure-activity relationships for 4-[(phenyl-methyl)amino]- and 4-(phenylamino)quinazolines as potent adenosine 5′-triphosphate binding site inhibitors of the tyrosine kinase domain of the epidermal growth factor receptor. J. Med. Chem. 1995, 38, 3482-3487.
    • (1995) J. Med. Chem. , vol.38 , pp. 3482-3487
    • Rewcastle, G.W.1    Denny, W.A.2    Bridges, A.J.3    Zhou, H.4    Cody, D.R.5    McMichael, A.6    Fry, D.W.7
  • 40
    • 0033555270 scopus 로고    scopus 로고
    • Structure of the protein tyrosine kinase domain of the C-terminal Src (CSK) in complex with Staurosporine
    • Lamers, M. B. A. C.; Antson, A. A.; Hubbard, E. E.; Scott, R. K.; Williams, D. H. Structure of the protein tyrosine kinase domain of the C-terminal Src (CSK) in complex with Staurosporine. J. Mol Biol. 1999, 285, 713-725.
    • (1999) J. Mol Biol. , vol.285 , pp. 713-725
    • Lamers, M.B.A.C.1    Antson, A.A.2    Hubbard, E.E.3    Scott, R.K.4    Williams, D.H.5
  • 41
    • 0029090514 scopus 로고
    • Multiple modes of ligand recognition: Crystal structures of cyclin-dependent protein kinase 2 in complex with ATP and two inhibitors, olomoucine and isopentenyladenine
    • Schulze-Gahmen, U.; Brandsen, J.; Jones, H. D.; Morgan, D. O.; Meijer, L.; Vesely, J.; Kim, S. H. Multiple Modes of Ligand Recognition: Crystal Structures of Cyclin-Dependent Protein Kinase 2 in Complex with ATP and Two Inhibitors, Olomoucine and Isopentenyladenine. Proteins: Struct., Funct., Genet. 1995, 22, 378-391.
    • (1995) Proteins: Struct., Funct., Genet. , vol.22 , pp. 378-391
    • Schulze-Gahmen, U.1    Brandsen, J.2    Jones, H.D.3    Morgan, D.O.4    Meijer, L.5    Vesely, J.6    Kim, S.H.7
  • 42
    • 0029850471 scopus 로고    scopus 로고
    • High-resolution crystal structures of human cyclin-dependent kinase 2 with and without ATP: Bound waters and natural ligand as guides for inhibitor design
    • Schulze-Gahmen, U.; De Bondt, H. L.; Kim, S. H. High-resolution crystal structures of human cyclin-dependent kinase 2 with and without ATP: bound waters and natural ligand as guides for inhibitor design. J. Med. Chem. 1996, 39, 4540-4546.
    • (1996) J. Med. Chem. , vol.39 , pp. 4540-4546
    • Schulze-Gahmen, U.1    De Bondt, H.L.2    Kim, S.H.3
  • 44
    • 0031253655 scopus 로고    scopus 로고
    • Protein kinase inhibition by staurosporine revealed in details of the molecular interaction with CDK2
    • Lawrie, A. M.; Noble, M. E. M.; Tunnah, P.; Brown, N. R.; Johnson, L. N.; Endicott, J. A. Protein kinase inhibition by staurosporine revealed in details of the molecular interaction with CDK2. Nature Struct. Biol. 1997, 4(9), 796-800.
    • (1997) Nature Struct. Biol. , vol.4 , Issue.9 , pp. 796-800
    • Lawrie, A.M.1    Noble, M.E.M.2    Tunnah, P.3    Brown, N.R.4    Johnson, L.N.5    Endicott, J.A.6
  • 45
    • 0029860018 scopus 로고    scopus 로고
    • Crystal structures of catalytic subunit of cAMP-dependent protein kinase in complex with isoquinolinesulfonyl protein kinase inhibitors H7, H8, and H89
    • Engh, R. A.; Girod, A.; Kinzel, V.; Huber R.; Bossemeyer, D. Crystal structures of catalytic subunit of cAMP-dependent protein kinase in complex with isoquinolinesulfonyl protein kinase inhibitors H7, H8, and H89. J. Biol. Chem. 1996, 271(42), 26157-26164.
    • (1996) J. Biol. Chem. , vol.271 , Issue.42 , pp. 26157-26164
    • Engh, R.A.1    Girod, A.2    Kinzel, V.3    Huber, R.4    Bossemeyer, D.5
  • 46
    • 0031574365 scopus 로고    scopus 로고
    • Staurosporine-induced conformational changes of the cAMP-dependent protein kinase catalytic subunit explain inhibitory potential
    • Prade, L.; Engh, R. A.; Girod, A.; Kinzel, V.; Huber R.; Bossemeyer, D. Staurosporine-induced conformational changes of the cAMP-dependent protein kinase catalytic subunit explain inhibitory potential. Structure 1997, 5(12), 1627-1637.
    • (1997) Structure , vol.5 , Issue.12 , pp. 1627-1637
    • Prade, L.1    Engh, R.A.2    Girod, A.3    Kinzel, V.4    Huber, R.5    Bossemeyer, D.6
  • 47
    • 0030766163 scopus 로고    scopus 로고
    • Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analogue
    • Hubbard, S. Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analogue. EMBO J. 1997, 16, 5572-5581.
    • (1997) EMBO J. , vol.16 , pp. 5572-5581
    • Hubbard, S.1
  • 48
    • 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
  • 49
    • 0030945871 scopus 로고    scopus 로고
    • Structures of the tyrosine kinase domain of fibroblast growth factor receptor in complex with inhibitors
    • Mohamadi, M.; McMahon, G.; Sun, L. T.; Tang, C.; Hirth, P.; Yeh, B. K.; Hubbard, S. R.; Schlessinger, J. Structures of the tyrosine kinase domain of fibroblast growth factor receptor in complex with inhibitors. Science 1997, 276, 955-960.
    • (1997) Science , vol.276 , pp. 955-960
    • Mohamadi, M.1    McMahon, G.2    Sun, L.T.3    Tang, C.4    Hirth, P.5    Yeh, B.K.6    Hubbard, S.R.7    Schlessinger, J.8
  • 53
    • 0029440002 scopus 로고
    • Modeling study of protein kinase inhibitors: Binding mode of staurosporine and origin of the selectivity of CGP 52 411
    • Furet, P.; Caravatti, G.; Priestle, J.; Sowadski, J.; Trinks, U.; Traxler, P. Modeling study of protein kinase inhibitors: binding mode of staurosporine and origin of the selectivity of CGP 52 411. J. Comput.-Aided Mol. Des. 1995, 9, 465-472.
    • (1995) J. Comput.-Aided Mol. Des. , vol.9 , pp. 465-472
    • Furet, P.1    Caravatti, G.2    Priestle, J.3    Sowadski, J.4    Trinks, U.5    Traxler, P.6
  • 54
    • 0030008414 scopus 로고    scopus 로고
    • 4-(phenylamino)pyrrolopyrimidines: Potent and selective, ATP site directed inhibitors of the EGF-receptor protein tyrosine kinase
    • Traxler, P. M.; Furet, P.; Mett, H.; Buchdunger, E.; Meyer, T.; Lydon, N. 4-(phenylamino)pyrrolopyrimidines: potent and selective, ATP site directed inhibitors of the EGF-receptor protein tyrosine kinase. J. Med. Chem. 1996, 39, 2285-2292
    • (1996) J. Med. Chem. , vol.39 , pp. 2285-2292
    • Traxler, P.M.1    Furet, P.2    Mett, H.3    Buchdunger, E.4    Meyer, T.5    Lydon, N.6
  • 55
    • 9844235351 scopus 로고    scopus 로고
    • Use of a Pharmacophore model for the design of EGF-R tyrosine kinase inhibitors: 4-(phenylamino)pyrazolo[3,4-d]pyrimidines
    • Traxler, P. M.; Bold, G.; Frei, J.; Lang, M.; Lydon, N.; Mett, H.; Buchdunger, E.; Meyer, T.; Mueller, M.; Furet, P. Use of a Pharmacophore model for the design of EGF-R tyrosine kinase inhibitors: 4-(phenylamino)pyrazolo[3,4-d]pyrimidines. J. Med. Chem. 1997, 40, 3601-3616.
    • (1997) J. Med. Chem. , vol.40 , pp. 3601-3616
    • Traxler, P.M.1    Bold, G.2    Frei, J.3    Lang, M.4    Lydon, N.5    Mett, H.6    Buchdunger, E.7    Meyer, T.8    Mueller, M.9    Furet, P.10
  • 56
    • 0030907052 scopus 로고    scopus 로고
    • Tyrosine kinase inhibitors. 11. Soluble analogues of pyrrolo- and pyrazoloquinazolines as epidermal growth factor receptor inhibitors: Synthesis, biological evaluation, and modeling of the mode of binding
    • Palmer, B. D.; Trumpp-Kallmeyer, S.; Fry, D. W.; Nelson, J. M..; Showalter, H. D. H.; Denny, W. A. Tyrosine kinase inhibitors. 11. Soluble analogues of pyrrolo- and pyrazoloquinazolines as epidermal growth factor receptor inhibitors: synthesis, biological evaluation, and modeling of the mode of binding. J. Med. Chem. 1997, 40, 1519-1529.
    • (1997) J. Med. Chem. , vol.40 , pp. 1519-1529
    • Palmer, B.D.1    Trumpp-Kallmeyer, S.2    Fry, D.W.3    Nelson, J.M.4    Showalter, H.D.H.5    Denny, W.A.6
  • 57
    • 0032554818 scopus 로고    scopus 로고
    • Development of a binding model to protein tyrosine kinases for substituted pyrido[2,3-d]pyrimidine inhibitors
    • Trumpp-Kallmeyer, S.; Rubin, J. R.; Humblet, C.; Hamby, J. M.; Showalter, H. D. H. Development of a Binding Model to Protein Tyrosine Kinases for Substituted Pyrido[2,3-d]pyrimidine Inhibitors. J. Med. Chem. 1998, 41, 1752-1763.
    • (1998) J. Med. Chem. , vol.41 , pp. 1752-1763
    • Trumpp-Kallmeyer, S.1    Rubin, J.R.2    Humblet, C.3    Hamby, J.M.4    Showalter, H.D.H.5
  • 58
    • 0000127673 scopus 로고
    • 2.2 A refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor
    • Zheng, J.; Trafny, E. A.; Knighton, D. R.; Xuong, N.-H.; Taylor, S. S.; Ten Eyck, L. F.; Sowadsky, J. M. 2.2 A refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor. Acta Crystallogr. 1993, D49, 362-365.
    • (1993) Acta Crystallogr. , vol.D49 , pp. 362-365
    • Zheng, J.1    Trafny, E.A.2    Knighton, D.R.3    Xuong, N.-H.4    Taylor, S.S.5    Ten Eyck, L.F.6    Sowadsky, J.M.7
  • 60
    • 0342432537 scopus 로고    scopus 로고
    • Effect of the VEGF receptor tyrosine kinase inhibitor ZD4190 on vascular endothelial permeability
    • Abstract 2741. (To be published)
    • (b) Wedge, S. R.; Waterton, J. C.; Tessier, J. J.; Checkley, D.; Dukes, M.; Kendrew, J.; Curry, B. Effect of the VEGF receptor tyrosine kinase inhibitor ZD4190 on vascular endothelial permeability. AACR Philadelphia 1999 Abstract 2741. (To be published).
    • (1999) AACR Philadelphia
    • Wedge, S.R.1    Waterton, J.C.2    Tessier, J.J.3    Checkley, D.4    Dukes, M.5    Kendrew, J.6    Curry, B.7
  • 62
    • 0028157664 scopus 로고
    • Atomic structure of the MAP kinase ERK2 at 2.3 A resolution
    • Zang, F.; Strand, A.; Robbins, D.; Cobb, M. H.; Goldsmith, E. J. Atomic structure of the MAP kinase ERK2 at 2.3 A resolution. Nature 1994, 367, 704-711.
    • (1994) Nature , vol.367 , pp. 704-711
    • Zang, F.1    Strand, A.2    Robbins, D.3    Cobb, M.H.4    Goldsmith, E.J.5
  • 63
    • 0029644732 scopus 로고
    • Two structures of the catalytic domain of phosphorylase kinase: An active protein kinase complexed with substrate analogue and product
    • Owen, D. J.; Noble, M. E. M.; Garman, E. F.; Papageorgiou, A. C.; Johnson, L. N. Two structures of the catalytic domain of phosphorylase kinase: an active protein kinase complexed with substrate analogue and product. Structure 1995, 3, 467-482.
    • (1995) Structure , vol.3 , pp. 467-482
    • Owen, D.J.1    Noble, M.E.M.2    Garman, E.F.3    Papageorgiou, A.C.4    Johnson, L.N.5
  • 64
    • 0028913538 scopus 로고
    • Crystal structure of casein kinase-1, a phosphate-directed protein kinase
    • Xu, R. M.; Carmel, G.; Sweet, R. M.; Kuret, J.; Cheng, X. Crystal structure of casein kinase-1, a phosphate-directed protein kinase. EMBO J. 1995, 14, 1015-1023.
    • (1995) EMBO J. , vol.14 , pp. 1015-1023
    • Xu, R.M.1    Carmel, G.2    Sweet, R.M.3    Kuret, J.4    Cheng, X.5
  • 65
    • 0023885305 scopus 로고
    • The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains
    • (a) Hanks, S. K.; Quinn, A. M.; Hunter, T. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 1988, 241, 42-52.
    • (1988) Science , vol.241 , pp. 42-52
    • Hanks, S.K.1    Quinn, A.M.2    Hunter, T.3
  • 66
    • 0026345394 scopus 로고
    • Protein kinase catalytic domain sequence database: Identification of conserved features of primary structure and classification of family members
    • (b) Hanks, S. K.; Quinn, A. M. Protein kinase catalytic domain sequence database: Identification of conserved features of primary structure and classification of family members. Methods Enzymol. 1991, 200, 38-62.
    • (1991) Methods Enzymol. , vol.200 , pp. 38-62
    • Hanks, S.K.1    Quinn, A.M.2
  • 67
    • 0027429591 scopus 로고
    • Crystal structures of the myristylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformations
    • Zheng, J.; Knighton, D. R.; Xuong, N.-H.; Taylor, S. S.; Sowadsky, J. M.; Ten Eyck, L. F. Crystal structures of the myristylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformations. Protein Sci. 1993, 2, 1559-1573.
    • (1993) Protein Sci. , vol.2 , pp. 1559-1573
    • Zheng, J.1    Knighton, D.R.2    Xuong, N.-H.3    Taylor, S.S.4    Sowadsky, J.M.5    Ten Eyck, L.F.6
  • 68
    • 0027319145 scopus 로고
    • Structural features that specify tyrosine kinase activity deduced from homology modeling of the epidermal growth factor receptor
    • Knighton, D. R.; Cadena, D. L.; Zheng, J.; Ten Eyck, L. F.; Taylor, S. S.; Sowadski, J. M.; Gill, G. N. Structural features that specify tyrosine kinase activity deduced from homology modeling of the epidermal growth factor receptor. Proc. Natl. Acad. Sci. U.S.A. 1993, 90(11), 5001-5005.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , Issue.11 , pp. 5001-5005
    • Knighton, D.R.1    Cadena, D.L.2    Zheng, J.3    Ten Eyck, L.F.4    Taylor, S.S.5    Sowadski, J.M.6    Gill, G.N.7
  • 69
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A.; Blundell, T. L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 1993, 234, 779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 70
    • 0342867000 scopus 로고    scopus 로고
    • Quanta; Molecular Simulations, Incorporated, 9685 Scranton Rd, San Diego, CA 92121-3752
    • Quanta; Molecular Simulations, Incorporated, 9685 Scranton Rd, San Diego, CA 92121-3752.
  • 72
    • 84986505827 scopus 로고
    • Validation of the general purpose QUANTA3.2/CHARMm force field
    • Momany, F. A.; Rone, R. Validation of the general purpose QUANTA3.2/CHARMm force field. J. Comput. Chem. 1992, 13, 888-900.
    • (1992) J. Comput. Chem. , vol.13 , pp. 888-900
    • Momany, F.A.1    Rone, R.2
  • 74
    • 0342432536 scopus 로고
    • Heterocyclic basic compounds. IV. 2-aminoalkylamino-pyrimidines
    • Adams, R. R.; Whitmore, F. C. Heterocyclic basic compounds. IV. 2-aminoalkylamino-pyrimidines. J. Am. Chem. Soc. 1945, 67, 735-738.
    • (1945) J. Am. Chem. Soc. , vol.67 , pp. 735-738
    • Adams, R.R.1    Whitmore, F.C.2
  • 76
  • 77
    • 33947463964 scopus 로고
    • Isomeric and nuclear-substituted β-aminoethyl-1,2,4-triazoles
    • Ainsworth, C.; Jones, R. G. Isomeric and Nuclear-substituted β-Aminoethyl-1,2,4-triazoles. J. Am. Chem. Soc. 1955, 77, 621-622.
    • (1955) J. Am. Chem. Soc. , vol.77 , pp. 621-622
    • Ainsworth, C.1    Jones, R.G.2
  • 78
    • 0027473861 scopus 로고
    • Orally active cephalosporins ii. synthesis and structure-activity relationships of new 7β-[(Z)-2-(2-aminothiazol-4-yl)-2-hydroxyiminoacetamido]-cephalosporins with 1,2,3-triazole in C-3 side chain
    • Kume, M.; Kubota, T.; Kunura, Y.; Nakashimizu, H.; Motokawa, K.; Nakano M. Orally Active Cephalosporins II. Synthesis and Structure-Activity Relationships of New 7β-[(Z)-2-(2-Aminothiazol-4-yl)-2-Hydroxyiminoacetamido]-Cephalosporins with 1,2,3-Triazole in C-3 Side Chain. J. Antibio. 1993, 46, 177-195.
    • (1993) J. Antibio , vol.46 , pp. 177-195
    • Kume, M.1    Kubota, T.2    Kunura, Y.3    Nakashimizu, H.4    Motokawa, K.5    Nakano, M.6
  • 79
    • 0343737617 scopus 로고    scopus 로고
    • Substituted Isoindoles. US Patent 1978, 4, 120, 693. CA: 90: 38788
    • Goddard, S. J.; Levitt, G. Substituted Isoindoles. US Patent 1978, 4, 120, 693. CA: 90: 38788.
    • Goddard, S.J.1    Levitt, G.2


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