메뉴 건너뛰기




Volumn 57, Issue 15, 2014, Pages 6834-6844

Pyrrolo[3,2-b ]quinoxaline derivatives as types I1/2 and II Eph tyrosine kinase inhibitors: Structure-based design, synthesis, and in vivo validation

Author keywords

[No Author keywords available]

Indexed keywords

ANTINEOPLASTIC AGENT; PYRROLO[3,2 B]QUINOXALINE DERIVATIVE; QUINOXALINE DERIVATIVE; UNCLASSIFIED DRUG; EPHRIN RECEPTOR A3; EPHRIN RECEPTOR B4; PYRROLE DERIVATIVE;

EID: 84906088551     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm5009242     Document Type: Article
Times cited : (30)

References (60)
  • 2
    • 0036527429 scopus 로고    scopus 로고
    • Protein kinases: The major drug targets of the twenty-first century?
    • Cohen, P. Protein kinases: the major drug targets of the twenty-first century? Nat. Rev. Drug Discovery 2002, 1, 309-315
    • (2002) Nat. Rev. Drug Discovery , vol.1 , pp. 309-315
    • Cohen, P.1
  • 4
    • 84880177115 scopus 로고    scopus 로고
    • Type II kinase inhibitors: An opportunity in cancer for rational design
    • Blanc, J.; Geney, R.; Menet, C. Type II kinase inhibitors: an opportunity in cancer for rational design Anticancer Agents Med. Chem. 2013, 13, 731-747
    • (2013) Anticancer Agents Med. Chem. , vol.13 , pp. 731-747
    • Blanc, J.1    Geney, R.2    Menet, C.3
  • 6
    • 84888094480 scopus 로고    scopus 로고
    • Small molecule kinase inhibitors approved by the FDA from 2000 to 2011: A systematic review of preclinical ADME data
    • O'Brien, Z.; Moghaddam, M. F. Small molecule kinase inhibitors approved by the FDA from 2000 to 2011: a systematic review of preclinical ADME data Expert Opin. Drug Metab. Toxicol. 2013, 9, 1597-1612
    • (2013) Expert Opin. Drug Metab. Toxicol. , vol.9 , pp. 1597-1612
    • O'Brien, Z.1    Moghaddam, M.F.2
  • 7
    • 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 Nat. Rev. Cancer 2009, 9, 28-39
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 28-39
    • Zhang, J.1    Yang, P.L.2    Gray, N.S.3
  • 8
    • 69949151386 scopus 로고    scopus 로고
    • Factors underlying sensitivity of cancers to small-molecule kinase inhibitors
    • Janne, P. A.; Gray, N.; Settleman, J. Factors underlying sensitivity of cancers to small-molecule kinase inhibitors Nat. Rev. Drug Discovery 2009, 8, 709-723
    • (2009) Nat. Rev. Drug Discovery , vol.8 , pp. 709-723
    • Janne, P.A.1    Gray, N.2    Settleman, J.3
  • 10
  • 12
    • 33745298429 scopus 로고    scopus 로고
    • Rational design of inhibitors that bind to inactive kinase conformations
    • Liu, Y.; Gray, N. S. Rational design of inhibitors that bind to inactive kinase conformations Nat. Chem. Biol. 2006, 2, 358-364
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 358-364
    • Liu, Y.1    Gray, N.S.2
  • 13
    • 0033026444 scopus 로고    scopus 로고
    • Strategies toward the design of novel and selective protein tyrosine kinase inhibitors
    • Traxler, P.; Furet, P. Strategies toward the design of novel and selective protein tyrosine kinase inhibitors Pharmacol. Ther. 1999, 82, 195-206
    • (1999) Pharmacol. Ther. , vol.82 , pp. 195-206
    • Traxler, P.1    Furet, P.2
  • 14
    • 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
  • 15
    • 58149102549 scopus 로고    scopus 로고
    • Assessment of chemical coverage of kinome space and its implications for kinase drug discovery
    • Bamborough, P.; Drewry, D.; Harper, G.; Smith, G. K.; Schneider, K. Assessment of chemical coverage of kinome space and its implications for kinase drug discovery J. Med. Chem. 2008, 51, 7898-7914
    • (2008) J. Med. Chem. , vol.51 , pp. 7898-7914
    • Bamborough, P.1    Drewry, D.2    Harper, G.3    Smith, G.K.4    Schneider, K.5
  • 17
    • 77649204688 scopus 로고    scopus 로고
    • Selectively nonselective kinase inhibition: Striking the right balance
    • Morphy, R. Selectively nonselective kinase inhibition: striking the right balance J. Med. Chem. 2010, 53, 1413-1437
    • (2010) J. Med. Chem. , vol.53 , pp. 1413-1437
    • Morphy, R.1
  • 19
    • 79953658137 scopus 로고    scopus 로고
    • Drug discovery and the human kinome: Recent trends
    • Eglen, R.; Reisine, T. Drug discovery and the human kinome: recent trends Pharmacol. Ther. 2011, 130, 144-156
    • (2011) Pharmacol. Ther. , vol.130 , pp. 144-156
    • Eglen, R.1    Reisine, T.2
  • 20
    • 70350072332 scopus 로고    scopus 로고
    • Structure-based optimization of potent and selective inhibitors of the tyrosine kinase erythropoietin producing human hepatocellular carcinoma receptor B4 (EphB4)
    • Lafleur, K.; Huang, D.; Zhou, T.; Caflisch, A.; Nevado, C. Structure-based optimization of potent and selective inhibitors of the tyrosine kinase erythropoietin producing human hepatocellular carcinoma receptor B4 (EphB4) J. Med. Chem. 2009, 52, 6433-6446
    • (2009) J. Med. Chem. , vol.52 , pp. 6433-6446
    • Lafleur, K.1    Huang, D.2    Zhou, T.3    Caflisch, A.4    Nevado, C.5
  • 21
    • 84867352362 scopus 로고    scopus 로고
    • Discovery of a novel chemotype of tyrosine kinase inhibitors by fragment-based docking and molecular dynamics
    • Zhao, H. T.; Dong, J.; Lafleur, K.; Nevado, C.; Caflisch, A. Discovery of a novel chemotype of tyrosine kinase inhibitors by fragment-based docking and molecular dynamics ACS Med. Chem. Lett. 2012, 3, 834-838
    • (2012) ACS Med. Chem. Lett. , vol.3 , pp. 834-838
    • Zhao, H.T.1    Dong, J.2    Lafleur, K.3    Nevado, C.4    Caflisch, A.5
  • 22
    • 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
  • 23
  • 24
    • 79959222106 scopus 로고    scopus 로고
    • Hydrogen bonding penalty upon ligand binding
    • Zhao, H.; Huang, D. Hydrogen bonding penalty upon ligand binding PLoS One 2011, 6, e19923
    • (2011) PLoS One , vol.6 , pp. 19923
    • Zhao, H.1    Huang, D.2
  • 25
    • 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
  • 34
    • 79952804851 scopus 로고    scopus 로고
    • Improvement in aqueous solubility in small molecule drug discovery programs by disruption of molecular planarity and symmetry
    • Ishikawa, M.; Hashimoto, Y. Improvement in aqueous solubility in small molecule drug discovery programs by disruption of molecular planarity and symmetry J. Med. Chem. 2011, 54, 1539-1554
    • (2011) J. Med. Chem. , vol.54 , pp. 1539-1554
    • Ishikawa, M.1    Hashimoto, Y.2
  • 35
    • 0002621824 scopus 로고
    • Syntheses of indolizino-and dihydroindolizinoquinoxalines
    • Pratt, E. F.; Kereszte, J. Syntheses of indolizino-and dihydroindolizinoquinoxalines J. Org. Chem. 1967, 32, 49-53
    • (1967) J. Org. Chem. , vol.32 , pp. 49-53
    • Pratt, E.F.1    Kereszte, J.2
  • 36
    • 3242775362 scopus 로고    scopus 로고
    • Synthesis and some reactions of 3-chloro-2-(cyanomethylene)-1,2- dihydroquinoxalines
    • Obafemi, C. A.; Pfleiderer, W. Synthesis and some reactions of 3-chloro-2-(cyanomethylene)-1,2-dihydroquinoxalines Molecules 2004, 9, 223-231
    • (2004) Molecules , vol.9 , pp. 223-231
    • Obafemi, C.A.1    Pfleiderer, W.2
  • 37
    • 84998286881 scopus 로고
    • Synthesis of condensed quinoxalines 0.2. A new synthesis of pyrrolo-2,3-b-quinoxalines
    • Otomasu, H.; Ohmiya, S.; Sekuguch, T.; Takahash, H. Synthesis of condensed quinoxalines 0.2. A new synthesis of pyrrolo-2,3-b-quinoxalines Chem. Pharm. Bull. 1970, 18, 2065
    • (1970) Chem. Pharm. Bull. , vol.18 , pp. 2065
    • Otomasu, H.1    Ohmiya, S.2    Sekuguch, T.3    Takahash, H.4
  • 39
    • 34547195268 scopus 로고    scopus 로고
    • An efficient synthesis of nilotinib (AMN107)
    • Huang, W. S.; Shakespeare, W. C. An efficient synthesis of nilotinib (AMN107) Synthesis-Stuttgart 2007, 2121-2124
    • (2007) Synthesis-Stuttgart , pp. 2121-2124
    • Huang, W.S.1    Shakespeare, W.C.2
  • 40
    • 77950574393 scopus 로고    scopus 로고
    • Structure-activity relationship for thiohydantoin androgen receptor antagonists for castration-resistant prostate cancer (CRPC)
    • Jung, M. E.; Ouk, S.; Yoo, D.; Sawyers, C. L.; Chen, C.; Tran, C.; Wongvipat, J. Structure-activity relationship for thiohydantoin androgen receptor antagonists for castration-resistant prostate cancer (CRPC) J. Med. Chem. 2010, 53, 2779-2796
    • (2010) J. Med. Chem. , vol.53 , pp. 2779-2796
    • Jung, M.E.1    Ouk, S.2    Yoo, D.3    Sawyers, C.L.4    Chen, C.5    Tran, C.6    Wongvipat, J.7
  • 41
    • 37249005205 scopus 로고    scopus 로고
    • The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability
    • Niesen, F. H.; Berglund, H.; Vedadi, M. The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability Nat. Protoc. 2007, 2, 2212-2221
    • (2007) Nat. Protoc. , vol.2 , pp. 2212-2221
    • Niesen, F.H.1    Berglund, H.2    Vedadi, M.3
  • 48
    • 58149102648 scopus 로고    scopus 로고
    • Type-II kinase inhibitor docking, screening, and profiling using modified structures of active kinase states
    • Kufareva, I.; Abagyan, R. Type-II kinase inhibitor docking, screening, and profiling using modified structures of active kinase states J. Med. Chem. 2008, 51, 7921-7932
    • (2008) J. Med. Chem. , vol.51 , pp. 7921-7932
    • Kufareva, I.1    Abagyan, R.2
  • 50
    • 33748325882 scopus 로고    scopus 로고
    • Drug-target residence time and its implications for lead optimization
    • Copeland, R. A.; Pompliano, D. L.; Meek, T. D. Drug-target residence time and its implications for lead optimization Nat. Rev. Drug Discovery 2006, 5, 730-739
    • (2006) Nat. Rev. Drug Discovery , vol.5 , pp. 730-739
    • Copeland, R.A.1    Pompliano, D.L.2    Meek, T.D.3
  • 52
    • 84893873004 scopus 로고    scopus 로고
    • Quick evaluation of kinase inhibitors by surface plasmon resonance using single-site specifically biotinylated kinases
    • Kitagawa, D.; Gouda, M.; Kirii, Y. Quick evaluation of kinase inhibitors by surface plasmon resonance using single-site specifically biotinylated kinases J. Biomol. Screening 2014, 19, 453-461
    • (2014) J. Biomol. Screening , vol.19 , pp. 453-461
    • Kitagawa, D.1    Gouda, M.2    Kirii, Y.3
  • 57
    • 33845318922 scopus 로고    scopus 로고
    • New potential ligand-receptor signaling loops in ovarian cancer identified in multiple gene expression studies
    • Castellano, G.; Reid, J. F.; Alberti, P.; Carcangiu, M. L.; Tomassetti, A.; Canevari, S. New potential ligand-receptor signaling loops in ovarian cancer identified in multiple gene expression studies Cancer Res. 2006, 66, 10709-10719
    • (2006) Cancer Res. , vol.66 , pp. 10709-10719
    • Castellano, G.1    Reid, J.F.2    Alberti, P.3    Carcangiu, M.L.4    Tomassetti, A.5    Canevari, S.6
  • 58
    • 0036445885 scopus 로고    scopus 로고
    • Vascular patterning by Eph receptor tyrosine kinases and ephrins
    • Adams, R. H. Vascular patterning by Eph receptor tyrosine kinases and ephrins Semin. Cell Dev. Biol. 2002, 13, 55-60
    • (2002) Semin. Cell Dev. Biol. , vol.13 , pp. 55-60
    • Adams, R.H.1
  • 60
    • 0032748089 scopus 로고    scopus 로고
    • Tensional forces in fibrillar extracellular matrices control directional capillary sprouting
    • Korff, T.; Augustin, H. G. Tensional forces in fibrillar extracellular matrices control directional capillary sprouting J. Cell Sci. 1999, 112 (Pt 19) 3249-3258
    • (1999) J. Cell Sci. , vol.112 , Issue.PART 19 , pp. 3249-3258
    • Korff, T.1    Augustin, H.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.