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Volumn , Issue , 2009, Pages 461-483

Fragment-Based Drug Discovery of Kinase Inhibitors

Author keywords

B Raf kinase inhibitor using fragment based methods; Cyclin dependent kinase 2 (CDK2) multiple anticancer drug target in clinics; Fragment based drug discovery of kinase inhibitors

Indexed keywords


EID: 84871551462     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780470524961.ch18     Document Type: Chapter
Times cited : (4)

References (81)
  • 1
    • 17044403086 scopus 로고    scopus 로고
    • Ligand efficiency indices as guideposts for drug discovery
    • Abad-Zapatero, C., and Metz, G. (2005). Ligand efficiency indices as guideposts for drug discovery. Drug Discov Today. 10, 464-469.
    • (2005) Drug Discov Today. , vol.10 , pp. 464-469
    • Abad-Zapatero, C.1    Metz, G.2
  • 2
    • 33747595206 scopus 로고    scopus 로고
    • Structure-activity relationships by interligand NOE-based design and synthesis of antiapoptotic compounds targeting Bid
    • Becattini, B., Culmsee, C., Leone, M., et al. (2006). Structure-activity relationships by interligand NOE-based design and synthesis of antiapoptotic compounds targeting Bid. Proc Natl Acad Sci USA. 103, 12602-12606.
    • (2006) Proc Natl Acad Sci USA. , vol.103 , pp. 12602-12606
    • Becattini, B.1    Culmsee, C.2    Leone, M.3
  • 3
    • 0030039619 scopus 로고    scopus 로고
    • The art and practice of structure-based drug design: a molecular modeling perspective
    • Bohacek, R. S., McMartin, C., and Guida, W. C. (1996). The art and practice of structure-based drug design: a molecular modeling perspective. Med Res Rev. 16, 3-50.
    • (1996) Med Res Rev. , vol.16 , pp. 3-50
    • Bohacek, R.S.1    McMartin, C.2    Guida, W.C.3
  • 4
    • 0026813925 scopus 로고
    • The computer program LUDI: a new method for the de novo design of enzyme inhibitors
    • Bohm, H. J. (1992). The computer program LUDI: a new method for the de novo design of enzyme inhibitors. J Comput Aided Mol Des. 6, 61-78.
    • (1992) J Comput Aided Mol Des. , vol.6 , pp. 61-78
    • Bohm, H.J.1
  • 5
    • 0035818942 scopus 로고    scopus 로고
    • Oxindole-based inhibitors of cyclin-dependent kinase 2 (CDK2): design, synthesis, enzymatic activities, and X-ray crystallographic analysis
    • Bramson, H. N., Corona, J., Davis, S. T., et al. (2001). Oxindole-based inhibitors of cyclin-dependent kinase 2 (CDK2): design, synthesis, enzymatic activities, and X-ray crystallographic analysis. J Med Chem. 44, 4339-4358.
    • (2001) J Med Chem. , vol.44 , pp. 4339-4358
    • Bramson, H.N.1    Corona, J.2    Davis, S.T.3
  • 6
    • 84889829687 scopus 로고    scopus 로고
    • Discovery and development of selective, orally bioavailable tyrosine kinase inhibitors for targeted treatment of human cancers
    • In: CHI's Third Annual Drug Discovery Chemistry 2008: Tools, Targets & Therapies, La Jolla, CA
    • Burley, S. K. (2008). Discovery and development of selective, orally bioavailable tyrosine kinase inhibitors for targeted treatment of human cancers. In: CHI's Third Annual Drug Discovery Chemistry 2008: Tools, Targets & Therapies, La Jolla, CA.
    • (2008)
    • Burley, S.K.1
  • 7
    • 41849092287 scopus 로고    scopus 로고
    • Identification of 4-(4 -aminopiperidin-1-yl)-7 H-pyrrolo[2, 3-d ]pyrimidines as selective inhibitors of protein kinase B through fragment elaboration
    • Caldwell, J. J., Davies, T. G., Donald, A., et al. (2008). Identification of 4-(4 -aminopiperidin-1-yl)-7 H-pyrrolo[2, 3-d ]pyrimidines as selective inhibitors of protein kinase B through fragment elaboration. J Med Chem. 51, 2147-2157.
    • (2008) J Med Chem. , vol.51 , pp. 2147-2157
    • Caldwell, J.J.1    Davies, T.G.2    Donald, A.3
  • 8
    • 47149092363 scopus 로고    scopus 로고
    • Discovery of an Aurora kinase inhibitor through site-specific dynamic combinatorial chemistry
    • Cancilla, M. T., He, M. M., Viswanathan, N., et al. (2008). Discovery of an Aurora kinase inhibitor through site-specific dynamic combinatorial chemistry. Bioorg Med Chem Lett. 18, 3978-3981.
    • (2008) Bioorg Med Chem Lett. , vol.18 , pp. 3978-3981
    • Cancilla, M.T.1    He, M.M.2    Viswanathan, N.3
  • 9
    • 20844437061 scopus 로고    scopus 로고
    • A family of phosphodiesterase inhibitors discovered by cocrystallography and scaffold-based drug design
    • Card, G. L., Blasdel, L., England, B. P., et al. (2005). A family of phosphodiesterase inhibitors discovered by cocrystallography and scaffold-based drug design. Nat Biotechnol. 23, 201-207.
    • (2005) Nat Biotechnol. , vol.23 , pp. 201-207
    • Card, G.L.1    Blasdel, L.2    England, B.P.3
  • 10
    • 34347375364 scopus 로고    scopus 로고
    • A fragment-based approach for the discovery of isoform-specific p38alpha inhibitors
    • Chen, J., Zhang, Z., Stebbins, J. L., et al. (2007). A fragment-based approach for the discovery of isoform-specific p38alpha inhibitors. ACS Chem Biol. 2, 329-336.
    • (2007) ACS Chem Biol. , vol.2 , pp. 329-336
    • Chen, J.1    Zhang, Z.2    Stebbins, J.L.3
  • 11
    • 27844598284 scopus 로고    scopus 로고
    • The Akt/PKB pathway: molecular target for cancer drug discovery
    • Cheng, J. Q., Lindsley, C. W., Cheng, G. Z., Yang, H., and Nicosia, S. V. (2005). The Akt/PKB pathway: molecular target for cancer drug discovery. Oncogene. 24, 7482-7492.
    • (2005) Oncogene. , vol.24 , pp. 7482-7492
    • Cheng, J.Q.1    Lindsley, C.W.2    Cheng, G.Z.3    Yang, H.4    Nicosia, S.V.5
  • 12
    • 0141670350 scopus 로고    scopus 로고
    • Detection of ligands from a dynamic combinatorial library by X-ray crystallography
    • Congreve, M. S., Davis, D. J., Devine, L., et al. (2003). Detection of ligands from a dynamic combinatorial library by X-ray crystallography. Angew Chem Int Ed Engl. 42, 4479-4482.
    • (2003) Angew Chem Int Ed Engl. , vol.42 , pp. 4479-4482
    • Congreve, M.S.1    Davis, D.J.2    Devine, L.3
  • 13
    • 46849089254 scopus 로고    scopus 로고
    • Recent developments in fragment-based drug discovery
    • Congreve, M., Chessari, G., Tisi, D., and Woodhead, A. J. (2008). Recent developments in fragment-based drug discovery. J Med Chem. 51, 3661-3680.
    • (2008) J Med Chem. , vol.51 , pp. 3661-3680
    • Congreve, M.1    Chessari, G.2    Tisi, D.3    Woodhead, A.J.4
  • 14
    • 35748967909 scopus 로고    scopus 로고
    • The role of the p38 pathway in adaptive immunity
    • Cook, R., Wu, C. C., Kang, Y. J., and Han, J. (2007). The role of the p38 pathway in adaptive immunity. Cell Mol Immunol. 4, 253-259.
    • (2007) Cell Mol Immunol. , vol.4 , pp. 253-259
    • Cook, R.1    Wu, C.C.2    Kang, Y.J.3    Han, J.4
  • 15
    • 0012383568 scopus 로고    scopus 로고
    • PyMOL molecular graphics system on World Wide Web
    • DeLano, W. L. PyMOL molecular graphics system on World Wide Web. http://pymol.sourceforge.net/.
    • DeLano, W.L.1
  • 16
    • 34249069460 scopus 로고    scopus 로고
    • Rapid evolution of 6 -phenylpurine inhibitors of protein kinase B through structure-based design
    • Donald, A., McHardy, T., Rowlands, M. G., et al. (2007). Rapid evolution of 6 -phenylpurine inhibitors of protein kinase B through structure-based design. J Med Chem. 50, 2289-2292.
    • (2007) J Med Chem. , vol.50 , pp. 2289-2292
    • Donald, A.1    McHardy, T.2    Rowlands, M.G.3
  • 17
    • 34548574653 scopus 로고    scopus 로고
    • Carbocyclic 3 ′-deoxyadenosine-based highly potent bisubstrate-analog inhibitor of basophilic protein kinases
    • Enkvist, E., Raidaru, G., Vaasa, A., Pehk, T., Lavogina, D., and Uri, A. (2007). Carbocyclic 3 ′-deoxyadenosine-based highly potent bisubstrate-analog inhibitor of basophilic protein kinases. Bioorg Med Chem Lett. 17, 5336-5339.
    • (2007) Bioorg Med Chem Lett. , vol.17 , pp. 5336-5339
    • Enkvist, E.1    Raidaru, G.2    Vaasa, A.3    Pehk, T.4    Lavogina, D.5    Uri, A.6
  • 18
    • 33751204422 scopus 로고    scopus 로고
    • Fragment-based lead discovery: a chemical update
    • Erlanson, D. A. (2006). Fragment-based lead discovery: a chemical update. Curr Opin Biotechnol. 17, 643-652.
    • (2006) Curr Opin Biotechnol. , vol.17 , pp. 643-652
    • Erlanson, D.A.1
  • 19
    • 38649107845 scopus 로고    scopus 로고
    • Fragment-based ligand discovery meets phage display
    • Erlanson, D. A. (2007). Fragment-based ligand discovery meets phage display. ACS Chem Biol. 2, 779-782.
    • (2007) ACS Chem Biol. , vol.2 , pp. 779-782
    • Erlanson, D.A.1
  • 21
    • 0037337035 scopus 로고    scopus 로고
    • In situ assembly of enzyme inhibitors using extended tethering
    • Erlanson, D. A., Lam, J. W., Wiesmann, C., et al. (2003). In situ assembly of enzyme inhibitors using extended tethering. Nat Biotechnol. 21, 308-314.
    • (2003) Nat Biotechnol. , vol.21 , pp. 308-314
    • Erlanson, D.A.1    Lam, J.W.2    Wiesmann, C.3
  • 24
    • 0033213957 scopus 로고    scopus 로고
    • The SHAPES strategy: an NMR-based approach for lead generation in drug discovery
    • Fejzo, J., Lepre, C. A., Peng, J. W., et al. (1999). The SHAPES strategy: an NMR-based approach for lead generation in drug discovery. Chem Biol. 6, 755-769.
    • (1999) Chem Biol. , vol.6 , pp. 755-769
    • Fejzo, J.1    Lepre, C.A.2    Peng, J.W.3
  • 25
    • 0037256273 scopus 로고    scopus 로고
    • Application of NMR screening in drug discovery
    • Fejzo, J., Lepre, C., and Xie, X. (2003). Application of NMR screening in drug discovery. Curr Top Med Chem. 3, 81-97.
    • (2003) Curr Top Med Chem. , vol.3 , pp. 81-97
    • Fejzo, J.1    Lepre, C.2    Xie, X.3
  • 26
    • 16244388286 scopus 로고    scopus 로고
    • Virtual exploration of the small -molecule chemical universe below 160 daltons
    • Fink, T., Bruggesser, H., and Reymond, J. L. (2005). Virtual exploration of the small -molecule chemical universe below 160 daltons. Angew Chem Int Ed Engl. 44, 1504-1508.
    • (2005) Angew Chem Int Ed Engl. , vol.44 , pp. 1504-1508
    • Fink, T.1    Bruggesser, H.2    Reymond, J.L.3
  • 27
    • 13244255220 scopus 로고    scopus 로고
    • The use of CDK inhibitors in oncology: a pharmaceutical perspective
    • Fischer, P. M. (2004). The use of CDK inhibitors in oncology: a pharmaceutical perspective. Cell Cycle. 3, 742-746.
    • (2004) Cell Cycle. , vol.3 , pp. 742-746
    • Fischer, P.M.1
  • 28
    • 0038206479 scopus 로고    scopus 로고
    • Mutants of protein kinase A that mimic the ATP-binding site of protein kinase B (AKT)
    • Gassel, M., Breitenlechner, C. B., Ruger, P., et al. (2003). Mutants of protein kinase A that mimic the ATP-binding site of protein kinase B (AKT). J Mol Biol. 329, 1021-1034.
    • (2003) J Mol Biol. , vol.329 , pp. 1021-1034
    • Gassel, M.1    Breitenlechner, C.B.2    Ruger, P.3
  • 29
    • 2342589483 scopus 로고    scopus 로고
    • New lead generation strategies for protein kinase inhibitors-fragment based screening approaches
    • Gill, A. (2004). New lead generation strategies for protein kinase inhibitors-fragment based screening approaches. Mini Rev Med Chem. 4, 301-311.
    • (2004) Mini Rev Med Chem. , vol.4 , pp. 301-311
    • Gill, A.1
  • 30
    • 20444451242 scopus 로고    scopus 로고
    • The discovery of novel protein kinase inhibitors by using fragment-based high-throughput X-ray crystallography
    • Gill, A., Cleasby, A., and Jhoti, H. (2005a). The discovery of novel protein kinase inhibitors by using fragment-based high-throughput X-ray crystallography. Chembiochem. 6, 506-512.
    • (2005) Chembiochem , vol.6 , pp. 506-512
    • Gill, A.1    Cleasby, A.2    Jhoti, H.3
  • 31
    • 19944434344 scopus 로고    scopus 로고
    • Identification of novel p38alpha MAP kinase inhibitors using fragment-based lead generation
    • Gill, A. L., Frederickson, M., Cleasby, A., et al. (2005b). Identification of novel p38alpha MAP kinase inhibitors using fragment-based lead generation. J Med Chem. 48, 414-426.
    • (2005) J Med Chem. , vol.48 , pp. 414-426
    • Gill, A.L.1    Frederickson, M.2    Cleasby, A.3
  • 32
    • 34548843943 scopus 로고    scopus 로고
    • A comparison of physicochemical property profiles of marketed oral drugs and orally bioavailable anti -cancer protein kinase inhibitors in clinical development
    • Gill, A. L., Verdonk, M., Boyle, R. G., and Taylor, R. (2007). A comparison of physicochemical property profiles of marketed oral drugs and orally bioavailable anti -cancer protein kinase inhibitors in clinical development. Curr Top Med Chem. 7, 1408-1422.
    • (2007) Curr Top Med Chem. , vol.7 , pp. 1408-1422
    • Gill, A.L.1    Verdonk, M.2    Boyle, R.G.3    Taylor, R.4
  • 33
    • 33847381100 scopus 로고    scopus 로고
    • A decade of fragment-based drug design: strategic advances and lessons learned
    • Hajduk, P. J., and Greer, J. (2007). A decade of fragment-based drug design: strategic advances and lessons learned. Nat Rev Drug Discov. 6, 211-219.
    • (2007) Nat Rev Drug Discov. , vol.6 , pp. 211-219
    • Hajduk, P.J.1    Greer, J.2
  • 34
    • 16944365890 scopus 로고    scopus 로고
    • Discovery of potent nonpeptide inhibitors of stromelysin using SAR by NMR
    • Hajduk, P. J., Sheppard, G., Nettesheim, D. G., et al. (1997). Discovery of potent nonpeptide inhibitors of stromelysin using SAR by NMR. J Am Chem Soc. 119, 5818-5827.
    • (1997) J Am Chem Soc. , vol.119 , pp. 5818-5827
    • Hajduk, P.J.1    Sheppard, G.2    Nettesheim, D.G.3
  • 35
    • 2942564021 scopus 로고    scopus 로고
    • Pursuing the leadlikeness concept in pharmaceutical research
    • Hann, M. M., and Oprea, T. I. (2004). Pursuing the leadlikeness concept in pharmaceutical research. Curr Opin Chem Biol. 8, 255-263.
    • (2004) Curr Opin Chem Biol. , vol.8 , pp. 255-263
    • Hann, M.M.1    Oprea, T.I.2
  • 36
    • 0035324944 scopus 로고    scopus 로고
    • Molecular complexity and its impact on the probability of finding leads for drug discovery
    • Hann, M. M., Leach, A. R., and Harper, G. (2001). Molecular complexity and its impact on the probability of finding leads for drug discovery. J Chem Inf Comput Sci. 41, 856-864.
    • (2001) J Chem Inf Comput Sci. , vol.41 , pp. 856-864
    • Hann, M.M.1    Leach, A.R.2    Harper, G.3
  • 37
    • 1942453243 scopus 로고    scopus 로고
    • Ligand efficiency: a useful metric for lead selection
    • Hopkins, A. L., Groom, C. R., and Alex, A. (2004). Ligand efficiency: a useful metric for lead selection. Drug Discov Today. 9, 430-431.
    • (2004) Drug Discov Today. , vol.9 , pp. 430-431
    • Hopkins, A.L.1    Groom, C.R.2    Alex, A.3
  • 38
    • 36248956723 scopus 로고    scopus 로고
    • The SeeDs approach: integrating fragments into drug discovery
    • Hubbard, R. E., Davis, B., Chen, I., and Drysdale, M. J. (2007). The SeeDs approach: integrating fragments into drug discovery. Curr Top Med Chem. 7, 1568-1581.
    • (2007) Curr Top Med Chem. , vol.7 , pp. 1568-1581
    • Hubbard, R.E.1    Davis, B.2    Chen, I.3    Drysdale, M.J.4
  • 39
    • 34547667231 scopus 로고    scopus 로고
    • Treatment for chronic myelogenous leukemia: the long road to imatinib
    • Hunter, T. (2007). Treatment for chronic myelogenous leukemia: the long road to imatinib. J Clin Invest. 117, 2036-2043.
    • (2007) J Clin Invest. , vol.117 , pp. 2036-2043
    • Hunter, T.1
  • 40
    • 84991718926 scopus 로고    scopus 로고
    • Fragment-Based Approaches in Drug Discovery
    • Weinheim, Germany: Wiley-VCH
    • Jahnke, W., and Erlanson, D. A. (eds.) (2006). Fragment-Based Approaches in Drug Discovery, Vol. 34. Weinheim, Germany: Wiley-VCH.
    • (2006) , vol.34
    • Jahnke, W.1    Erlanson, D.A.2
  • 41
    • 0019407381 scopus 로고
    • On the attribution and additivity of binding energies
    • Jencks, W. P. (1981). On the attribution and additivity of binding energies. Proc Natl Acad Sci USA. 78, 4046-4050.
    • (1981) Proc Natl Acad Sci USA. , vol.78 , pp. 4046-4050
    • Jencks, W.P.1
  • 42
    • 33846260566 scopus 로고    scopus 로고
    • Sorafenib for the treatment of advanced renal cell carcinoma
    • Kane, R. C., Farrell, A. T., Saber, H., et al. (2006). Sorafenib for the treatment of advanced renal cell carcinoma. Clin Cancer Res. 12, 7271-7278.
    • (2006) Clin Cancer Res. , vol.12 , pp. 7271-7278
    • Kane, R.C.1    Farrell, A.T.2    Saber, H.3
  • 43
    • 38049018155 scopus 로고    scopus 로고
    • A quantitative analysis of kinase inhibitor selectivity
    • Karaman, M. W., Herrgard, S., Treiber, D. K., et al. (2008). A quantitative analysis of kinase inhibitor selectivity. Nat Biotechnol. 26, 127-132.
    • (2008) Nat Biotechnol. , vol.26 , pp. 127-132
    • Karaman, M.W.1    Herrgard, S.2    Treiber, D.K.3
  • 44
    • 10344236486 scopus 로고    scopus 로고
    • Aurora-kinase inhibitors as anticancer agents
    • Keen, N., and Taylor, S. (2004). Aurora-kinase inhibitors as anticancer agents. Nat Rev Cancer. 4, 927-936.
    • (2004) Nat Rev Cancer. , vol.4 , pp. 927-936
    • Keen, N.1    Taylor, S.2
  • 46
    • 0242439332 scopus 로고    scopus 로고
    • Requirements for specific binding of low affinity inhibitor fragments to the SH2 domain of (pp60)Src are identical to those for high affinity binding of full length inhibitors
    • Lange, G., Lesuisse, D., Deprez, P., et al. (2003). Requirements for specific binding of low affinity inhibitor fragments to the SH2 domain of (pp60)Src are identical to those for high affinity binding of full length inhibitors. J Med Chem. 46, 5184-5195.
    • (2003) J Med Chem. , vol.46 , pp. 5184-5195
    • Lange, G.1    Lesuisse, D.2    Deprez, P.3
  • 47
    • 0037030686 scopus 로고    scopus 로고
    • SAR and X-ray. A new approach combining fragment-based screening and rational drug design: application to the discovery of nanomolar inhibitors of Src SH2
    • Lesuisse, D., Lange, G., Deprez, P., et al. (2002). SAR and X-ray. A new approach combining fragment-based screening and rational drug design: application to the discovery of nanomolar inhibitors of Src SH2. J Med Chem. 45, 2379-2387.
    • (2002) J Med Chem. , vol.45 , pp. 2379-2387
    • Lesuisse, D.1    Lange, G.2    Deprez, P.3
  • 48
    • 33846899405 scopus 로고    scopus 로고
    • Molecular recognition of protein kinase binding pockets for design of potent and selective kinase inhibitors
    • Liao, J. J. (2007). Molecular recognition of protein kinase binding pockets for design of potent and selective kinase inhibitors. J Med Chem. 50, 409-424.
    • (2007) J Med Chem. , vol.50 , pp. 409-424
    • Liao, J.J.1
  • 49
    • 0031024171 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • Lipinski, C. A., Lombardo, F., Dominy, B. W., and Feeney, P. J. (1997). Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv Drug Deliv Rev. 23, 3-25.
    • (1997) Adv Drug Deliv Rev. , vol.23 , pp. 3-25
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4
  • 50
    • 0036401042 scopus 로고    scopus 로고
    • Design and discovery of small molecules targeting raf-1 kinase
    • Lowinger, T. B., Riedl, B., Dumas, J., and Smith, R. A. (2002). Design and discovery of small molecules targeting raf-1 kinase. Curr Pharm Des. 8, 2269-2278.
    • (2002) Curr Pharm Des. , vol.8 , pp. 2269-2278
    • Lowinger, T.B.1    Riedl, B.2    Dumas, J.3    Smith, R.A.4
  • 51
    • 0034646370 scopus 로고    scopus 로고
    • Combinatorial target-guided ligand assembly: identification of potent subtype-selective c-Src inhibitors
    • Maly, D. J., Choong, I. C., and Ellman, J. A. (2000). Combinatorial target-guided ligand assembly: identification of potent subtype-selective c-Src inhibitors. Proc Natl Acad Sci USA. 97, 2419-2424.
    • (2000) Proc Natl Acad Sci USA. , vol.97 , pp. 2419-2424
    • Maly, D.J.1    Choong, I.C.2    Ellman, J.A.3
  • 52
    • 0037431421 scopus 로고    scopus 로고
    • Kinase inhibitors: not just for kinases anymore
    • McGovern, S. L., and Shoichet, B. K. (2003). Kinase inhibitors: not just for kinases anymore. J Med Chem. 46, 1478-1483.
    • (2003) J Med Chem. , vol.46 , pp. 1478-1483
    • McGovern, S.L.1    Shoichet, B.K.2
  • 53
    • 0037061628 scopus 로고    scopus 로고
    • A common mechanism underlying promiscuous inhibitors from virtual and high-throughput screening
    • McGovern, S. L., Caselli, E., Grigorieff, N., and Shoichet, B. K. (2002). A common mechanism underlying promiscuous inhibitors from virtual and high-throughput screening. J Med Chem. 45, 1712-1722.
    • (2002) J Med Chem. , vol.45 , pp. 1712-1722
    • McGovern, S.L.1    Caselli, E.2    Grigorieff, N.3    Shoichet, B.K.4
  • 54
  • 55
    • 36148932151 scopus 로고    scopus 로고
    • Tethering small molecules to a phage display library: discovery of a selective bivalent inhibitor of protein kinase A
    • Meyer, S. C., Shomin, C. D., Gaj, T., and Ghosh, I. (2007). Tethering small molecules to a phage display library: discovery of a selective bivalent inhibitor of protein kinase A. J Am Chem Soc. 129, 13812-13813.
    • (2007) J Am Chem Soc. , vol.129 , pp. 13812-13813
    • Meyer, S.C.1    Shomin, C.D.2    Gaj, T.3    Ghosh, I.4
  • 57
    • 0036821028 scopus 로고    scopus 로고
    • The consequences of translational and rotational entropy lost by small molecules on binding to proteins
    • Murray, C. W., and Verdonk, M. L. (2002). The consequences of translational and rotational entropy lost by small molecules on binding to proteins. J Comput Aided Mol Des. 16, 741-753.
    • (2002) J Comput Aided Mol Des. , vol.16 , pp. 741-753
    • Murray, C.W.1    Verdonk, M.L.2
  • 58
    • 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., et al. (2002). Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571). Cancer Res. 62, 4236-4243.
    • (2002) Cancer Res. , vol.62 , pp. 4236-4243
    • Nagar, B.1    Bornmann, W.G.2    Pellicena, P.3
  • 59
    • 15744380263 scopus 로고    scopus 로고
    • Structures of human MAP kinase kinase 1 (MEK1) and MEK2 describe novel noncompetitive kinase inhibition
    • Ohren, J. F., Chen, H., Pavlovsky, A., et al. (2004). Structures of human MAP kinase kinase 1 (MEK1) and MEK2 describe novel noncompetitive kinase inhibition. Nat Struct Mol Biol. 11, 1192-1197.
    • (2004) Nat Struct Mol Biol. , vol.11 , pp. 1192-1197
    • Ohren, J.F.1    Chen, H.2    Pavlovsky, A.3
  • 60
    • 18344395134 scopus 로고    scopus 로고
    • Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site
    • Pargellis, C., Tong, L., Churchill, L., et al. (2002). Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site. Nat Struct Biol. 9, 268-272.
    • (2002) Nat Struct Biol. , vol.9 , pp. 268-272
    • Pargellis, C.1    Tong, L.2    Churchill, L.3
  • 61
    • 0036047069 scopus 로고    scopus 로고
    • Drug discovery by dynamic combinatorial libraries
    • Ramstrom, O., and Lehn, J. M. (2002). Drug discovery by dynamic combinatorial libraries. Nat Rev Drug Discov. 1, 26-32.
    • (2002) Nat Rev Drug Discov. , vol.1 , pp. 26-32
    • Ramstrom, O.1    Lehn, J.M.2
  • 63
    • 43049088827 scopus 로고    scopus 로고
    • Ligand binding effi-ciency: trends, physical basis, and implications
    • Reynolds, C. H., Tounge, B. A., and Bembenek, S. D. (2008). Ligand binding effi-ciency: trends, physical basis, and implications. J Med Chem. 51, 2432-2438.
    • (2008) J Med Chem. , vol.51 , pp. 2432-2438
    • Reynolds, C.H.1    Tounge, B.A.2    Bembenek, S.D.3
  • 64
    • 0026063670 scopus 로고
    • Design of potent protein kinase inhibitors using the bisubstrate approach
    • Ricouart, A., Gesquiere, J. C., Tartar, A., and Sergheraert, C. (1991). Design of potent protein kinase inhibitors using the bisubstrate approach. J Med Chem. 34, 73-78.
    • (1991) J Med Chem. , vol.34 , pp. 73-78
    • Ricouart, A.1    Gesquiere, J.C.2    Tartar, A.3    Sergheraert, C.4
  • 65
    • 0037439447 scopus 로고    scopus 로고
    • Nonleadlikeness and leadlikeness in biochemical screening
    • Rishton, G. M. (2003). Nonleadlikeness and leadlikeness in biochemical screening. Drug Discov Today. 8, 86-96.
    • (2003) Drug Discov Today. , vol.8 , pp. 86-96
    • Rishton, G.M.1
  • 67
    • 0041842684 scopus 로고    scopus 로고
    • Effect of detergent on " promiscuous " inhibitors
    • Ryan, A. J., Gray, N. M., Lowe, P. N., and Chung, C. W. (2003). Effect of detergent on " promiscuous " inhibitors. J Med Chem. 46, 3448-3451.
    • (2003) J Med Chem. , vol.46 , pp. 3448-3451
    • Ryan, A.J.1    Gray, N.M.2    Lowe, P.N.3    Chung, C.W.4
  • 68
    • 34249050729 scopus 로고    scopus 로고
    • Identification of inhibitors of protein kinase B using fragment-based lead discovery
    • Saxty, G., Woodhead, S. J., Berdini, V., et al. (2007). Identification of inhibitors of protein kinase B using fragment-based lead discovery. J Med Chem. 50, 2293-2296.
    • (2007) J Med Chem. , vol.50 , pp. 2293-2296
    • Saxty, G.1    Woodhead, S.J.2    Berdini, V.3
  • 70
    • 18844441430 scopus 로고    scopus 로고
    • Increasing the kinase specificity of k252a by protein surface recognition
    • Schneider, T. L., Mathew, R. S., Rice, K. P., Tamaki, K., Wood, J. L., and Schepartz, A. (2005). Increasing the kinase specificity of k252a by protein surface recognition. Org Lett. 7, 1695-1698.
    • (2005) Org Lett. , vol.7 , pp. 1695-1698
    • Schneider, T.L.1    Mathew, R.S.2    Rice, K.P.3    Tamaki, K.4    Wood, J.L.5    Schepartz, A.6
  • 71
    • 33644756429 scopus 로고    scopus 로고
    • Oral p38 mitogen-activated protein kinase inhibition with BIRB 796 for active Crohn ' s disease: a randomized, double-blind, placebo-controlled trial
    • Schreiber, S., Feagan, B., D ' Haens, G., et al. (2006). Oral p38 mitogen-activated protein kinase inhibition with BIRB 796 for active Crohn ' s disease: a randomized, double-blind, placebo-controlled trial. Clin Gastroenterol Hepatol. 4, 325-334.
    • (2006) Clin Gastroenterol Hepatol. , vol.4 , pp. 325-334
    • Schreiber, S.1    Feagan, B.2    D'Haens, G.3
  • 72
    • 85017466994 scopus 로고    scopus 로고
    • NMR-guided fragment assembly
    • In: W. Jahnke and D. A. Erlanson (eds.). Fragment-Based Approaches in Drug Discovery, Weinheim, Germany: Wiley-VCH
    • Sem, D. S. (2006). NMR-guided fragment assembly. In: W. Jahnke and D. A. Erlanson (eds.). Fragment-Based Approaches in Drug Discovery, Vol. 34. Weinheim, Germany: Wiley-VCH, pp. 149-180.
    • (2006) , vol.34 , pp. 149-180
    • Sem, D.S.1
  • 73
    • 0346434146 scopus 로고    scopus 로고
    • Conversion of a tyrosine kinase protein substrate to a high affinity ligand by ATP linkage
    • Shen, K., and Cole, P. A. (2003). Conversion of a tyrosine kinase protein substrate to a high affinity ligand by ATP linkage. J Am Chem Soc. 125, 16172-16173.
    • (2003) J Am Chem Soc. , vol.125 , pp. 16172-16173
    • Shen, K.1    Cole, P.A.2
  • 74
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins: SAR by NMR
    • Shuker, S. B., Hajduk, P. J., Meadows, R. P., and Fesik, S. W. (1996). Discovering high-affinity ligands for proteins: SAR by NMR. Science. 274, 1531-1534.
    • (1996) Science. , vol.274 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 76
    • 42949149240 scopus 로고    scopus 로고
    • Discovery of a selective inhibitor of oncogenic B-Raf kinase with potent antimelanoma activity
    • Tsai, J., Lee, J. T., Wang, W., et al. (2008). Discovery of a selective inhibitor of oncogenic B-Raf kinase with potent antimelanoma activity. Proc Natl Acad Sci USA. 105, 3041-3046.
    • (2008) Proc Natl Acad Sci USA. , vol.105 , pp. 3041-3046
    • Tsai, J.1    Lee, J.T.2    Wang, W.3
  • 77
    • 45749113037 scopus 로고    scopus 로고
    • Development of paramagnetic probes for molecular recognition studies in protein kinases
    • Vazquez, J., De, S. K., Chen, L. H., et al. (2008). Development of paramagnetic probes for molecular recognition studies in protein kinases. J Med Chem. 51, 3460-3465.
    • (2008) J Med Chem. , vol.51 , pp. 3460-3465
    • Vazquez, J.1    De, S.K.2    Chen, L.H.3
  • 78
    • 34548822459 scopus 로고    scopus 로고
    • Recent advances of MEK inhibitors and their clinical progress
    • Wang, J. Y., Wilcoxen, K. M., Nomoto, K., and Wu, S. (2007). Recent advances of MEK inhibitors and their clinical progress. Curr Top Med Chem. 7, 1364-1378.
    • (2007) Curr Top Med Chem. , vol.7 , pp. 1364-1378
    • Wang, J.Y.1    Wilcoxen, K.M.2    Nomoto, K.3    Wu, S.4
  • 79
    • 33748299545 scopus 로고    scopus 로고
    • Identification of a lead small-molecule inhibitor of the Aurora kinases using a structure-assisted, fragment -based approach
    • Warner, S. L., Bashyam, S., Vankayalapati, H., et al. (2006). Identification of a lead small-molecule inhibitor of the Aurora kinases using a structure-assisted, fragment -based approach. Mol Cancer Ther. 5, 1764-1773.
    • (2006) Mol Cancer Ther. , vol.5 , pp. 1764-1773
    • Warner, S.L.1    Bashyam, S.2    Vankayalapati, H.3
  • 80
    • 50249083873 scopus 로고    scopus 로고
    • Identification of N-(4 -piperidinyl)-4-(2, 6-dichlorobenzoylamino)-1 H-pyrazole-3-carboxamide (AT7519), a novel cyclin dependent kinase inhibitor using fragment-based X-ray crystallography and structure based drug design
    • Wyatt, P. G., Woodhead, A. J., Berdini, V., et al. (2008). Identification of N-(4 -piperidinyl)-4-(2, 6-dichlorobenzoylamino)-1 H-pyrazole-3-carboxamide (AT7519), a novel cyclin dependent kinase inhibitor using fragment-based X-ray crystallography and structure based drug design. J Med Chem. 51, 4986-4999.
    • (2008) J Med Chem. , vol.51 , pp. 4986-4999
    • Wyatt, P.G.1    Woodhead, A.J.2    Berdini, V.3
  • 81
    • 33746771005 scopus 로고    scopus 로고
    • Discovery of potent, highly selective, and orally bioavailable pyridine carboxamide c-Jun NH(2)-terminal kinase inhibitors
    • Zhao, H., Serby, M. D., Xin, Z., et al. (2006). Discovery of potent, highly selective, and orally bioavailable pyridine carboxamide c-Jun NH(2)-terminal kinase inhibitors. J Med Chem. 49, 4455-4458.
    • (2006) J Med Chem. , vol.49 , pp. 4455-4458
    • Zhao, H.1    Serby, M.D.2    Xin, Z.3


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