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Volumn 10, Issue 1, 2015, Pages 190-200

Targeting conformational plasticity of protein kinases

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHOTRANSFERASE INHIBITOR; PROTEIN KINASE; LIGAND; PROTEIN BINDING; PROTEIN KINASE INHIBITOR;

EID: 84921409244     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb500870a     Document Type: Review
Times cited : (87)

References (101)
  • 2
    • 0035413606 scopus 로고    scopus 로고
    • Kinetic and catalytic mechanisms of protein kinases
    • Adams, J. A. (2001) Kinetic and catalytic mechanisms of protein kinases Chem. Rev. 101, 2271-2290
    • (2001) Chem. Rev. , vol.101 , pp. 2271-2290
    • Adams, J.A.1
  • 3
    • 1642323740 scopus 로고    scopus 로고
    • Protein kinase inhibitors: Insights into drug design from structure
    • Noble, M. E., Endicott, J. A., and Johnson, L. N. (2004) Protein kinase inhibitors: insights into drug design from structure Science 303, 1800-1805
    • (2004) Science , vol.303 , pp. 1800-1805
    • Noble, M.E.1    Endicott, J.A.2    Johnson, L.N.3
  • 4
    • 84861859600 scopus 로고    scopus 로고
    • The structural basis for control of eukaryotic protein kinases
    • Endicott, J. A., Noble, M. E., and Johnson, L. N. (2012) The structural basis for control of eukaryotic protein kinases Annu. Rev. Biochem. 81, 587-613
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 587-613
    • Endicott, J.A.1    Noble, M.E.2    Johnson, L.N.3
  • 5
    • 84896920166 scopus 로고    scopus 로고
    • Novel approaches for targeting kinases: Allosteric inhibition, allosteric activation and pseudokinases
    • Cowan-Jacob, S. W., Jahnke, W., and Knapp, S. (2014) Novel approaches for targeting kinases: allosteric inhibition, allosteric activation and pseudokinases Future Med. Chem. 6, 541-561
    • (2014) Future Med. Chem. , vol.6 , pp. 541-561
    • Cowan-Jacob, S.W.1    Jahnke, W.2    Knapp, S.3
  • 6
    • 84905815719 scopus 로고    scopus 로고
    • Recently targeted kinases and their inhibitors-the path to clinical trials
    • Knapp, S. and Sundstrom, M. (2014) Recently targeted kinases and their inhibitors-the path to clinical trials Curr. Opin Pharmacol. 17, 58-63
    • (2014) Curr. Opin Pharmacol. , vol.17 , pp. 58-63
    • Knapp, S.1    Sundstrom, M.2
  • 10
    • 57749188299 scopus 로고    scopus 로고
    • Targeting cancer with small molecule kinase inhibitors
    • Zhang, J., Yang, P. L., and Gray, N. S. (2009) Targeting cancer with small molecule kinase inhibitors Nat. Rev. Cancer 9, 28-39
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 28-39
    • Zhang, J.1    Yang, P.L.2    Gray, N.S.3
  • 11
    • 80755125565 scopus 로고    scopus 로고
    • Comprehensive assay of kinase catalytic activity reveals features of kinase inhibitor selectivity
    • Anastassiadis, T., Deacon, S. W., Devarajan, K., Ma, H., and Peterson, J. R. (2011) Comprehensive assay of kinase catalytic activity reveals features of kinase inhibitor selectivity Nat. Biotechnol. 29, 1039-1045
    • (2011) Nat. Biotechnol. , vol.29 , pp. 1039-1045
    • Anastassiadis, T.1    Deacon, S.W.2    Devarajan, K.3    Ma, H.4    Peterson, J.R.5
  • 13
    • 33745298429 scopus 로고    scopus 로고
    • Rational design of inhibitors that bind to inactive kinase conformations
    • Liu, Y. and Gray, N. S. (2006) Rational design of inhibitors that bind to inactive kinase conformations Nat. Chem. Biol. 2, 358-364
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 358-364
    • Liu, Y.1    Gray, N.S.2
  • 14
    • 84903208494 scopus 로고    scopus 로고
    • Exploration of type II binding mode: A privileged approach for kinase inhibitor focused drug discovery?
    • Zhao, Z., Wu, H., Wang, L., Liu, Y., Knapp, S., Liu, Q., and Gray, N. S. (2014) Exploration of type II binding mode: A privileged approach for kinase inhibitor focused drug discovery? ACS Chem. Biol. 9, 1230-1241
    • (2014) ACS Chem. Biol. , vol.9 , pp. 1230-1241
    • Zhao, Z.1    Wu, H.2    Wang, L.3    Liu, Y.4    Knapp, S.5    Liu, Q.6    Gray, N.S.7
  • 16
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse, M. and Kuriyan, J. (2002) The conformational plasticity of protein kinases Cell 109, 275-282
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 17
    • 79959476700 scopus 로고    scopus 로고
    • The evolution of protein kinase inhibitors from antagonists to agonists of cellular signaling
    • Dar, A. C. and Shokat, K. M. (2011) The evolution of protein kinase inhibitors from antagonists to agonists of cellular signaling Annu. Rev. Biochem. 80, 769-795
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 769-795
    • Dar, A.C.1    Shokat, K.M.2
  • 18
    • 84901330713 scopus 로고    scopus 로고
    • Modulating noncatalytic function with kinase inhibitors
    • Agius, M. P. and Soellner, M. B. (2014) Modulating noncatalytic function with kinase inhibitors Chem. Biol. 21, 569-571
    • (2014) Chem. Biol. , vol.21 , pp. 569-571
    • Agius, M.P.1    Soellner, M.B.2
  • 25
    • 84919832780 scopus 로고    scopus 로고
    • Activation pathway of Src kinase reveals intermediate states as targets for drug design
    • Shukla, D., Meng, Y., Roux, B., and Pande, V. S. (2014) Activation pathway of Src kinase reveals intermediate states as targets for drug design Nat. Commun. 5, 3397
    • (2014) Nat. Commun. , vol.5 , pp. 3397
    • Shukla, D.1    Meng, Y.2    Roux, B.3    Pande, V.S.4
  • 28
    • 33748325882 scopus 로고    scopus 로고
    • Drug-target residence time and its implications for lead optimization
    • Copeland, R. A., Pompliano, D. L., and Meek, T. D. (2006) Drug-target residence time and its implications for lead optimization Nat. Rev. Drug Discovery 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
  • 29
    • 64049102289 scopus 로고    scopus 로고
    • Binding of small-molecule ligands to proteins: "what you see" is not always "what you get"
    • Mobley, D. L. and Dill, K. A. (2009) Binding of small-molecule ligands to proteins: "what you see" is not always "what you get" Structure 17, 489-498
    • (2009) Structure , vol.17 , pp. 489-498
    • Mobley, D.L.1    Dill, K.A.2
  • 32
    • 84860369376 scopus 로고    scopus 로고
    • Structural basis for the regulation of protein kinase A by activation loop phosphorylation
    • Steichen, J. M., Kuchinskas, M., Keshwani, M. M., Yang, J., Adams, J. A., and Taylor, S. S. (2012) Structural basis for the regulation of protein kinase A by activation loop phosphorylation J. Biol. Chem. 287, 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
  • 33
    • 84872511666 scopus 로고    scopus 로고
    • Strategies for the selective regulation of kinases with allosteric modulators: Exploiting exclusive structural features
    • Fang, Z., Grutter, C., and Rauh, D. (2013) Strategies for the selective regulation of kinases with allosteric modulators: exploiting exclusive structural features ACS Chem. Biol. 8, 58-70
    • (2013) ACS Chem. Biol. , vol.8 , pp. 58-70
    • Fang, Z.1    Grutter, C.2    Rauh, D.3
  • 34
    • 33845197964 scopus 로고    scopus 로고
    • Surface comparison of active and inactive protein kinases identifies a conserved activation mechanism
    • Kornev, A. P., Haste, N. M., Taylor, S. S., and Eyck, L. F. (2006) Surface comparison of active and inactive protein kinases identifies a conserved activation mechanism Proc. Natl. Acad. Sci. U. S. A. 103, 17783-17788
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 17783-17788
    • Kornev, A.P.1    Haste, N.M.2    Taylor, S.S.3    Eyck, L.F.4
  • 36
    • 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., and Eck, M. J. (2007) Structures of lung cancer-derived EGFR mutants and inhibitor complexes: mechanism of activation and insights into differential inhibitor sensitivity Cancer Cell 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
  • 37
    • 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., and Eigenbrot, C. (2002) Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor J. Biol. Chem. 277, 46265-46272
    • (2002) J. Biol. Chem. , vol.277 , pp. 46265-46272
    • Stamos, J.1    Sliwkowski, M.X.2    Eigenbrot, C.3
  • 42
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Xu, W., Harrison, S. C., and Eck, M. J. (1997) Three-dimensional structure of the tyrosine kinase c-Src Nature 385, 595-602
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 44
    • 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., and Kuriyan, J. (2007) c-Src binds to the cancer drug imatinib with an inactive Abl/c-Kit conformation and a distributed thermodynamic penalty Structure 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
  • 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., and Maly, D. J. (2009) Equally potent inhibition of c-Src and Abl by compounds that recognize inactive kinase conformations Cancer Res. 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
    • 77955792293 scopus 로고    scopus 로고
    • In vitro selection of a DNA-templated small-molecule library reveals a class of macrocyclic kinase inhibitors
    • Kleiner, R. E., Dumelin, C. E., Tiu, G. C., Sakurai, K., and Liu, D. R. (2010) In vitro selection of a DNA-templated small-molecule library reveals a class of macrocyclic kinase inhibitors J. Am. Chem. Soc. 132, 11779-11791
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 11779-11791
    • Kleiner, R.E.1    Dumelin, C.E.2    Tiu, G.C.3    Sakurai, K.4    Liu, D.R.5
  • 47
    • 84862777996 scopus 로고    scopus 로고
    • Highly specific, bisubstrate-competitive Src inhibitors from DNA-templated macrocycles
    • Georghiou, G., Kleiner, R. E., Pulkoski-Gross, M., Liu, D. R., and Seeliger, M. A. (2012) Highly specific, bisubstrate-competitive Src inhibitors from DNA-templated macrocycles Nat. Chem. Biol. 8, 366-374
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 366-374
    • Georghiou, G.1    Kleiner, R.E.2    Pulkoski-Gross, M.3    Liu, D.R.4    Seeliger, M.A.5
  • 55
    • 77950573400 scopus 로고    scopus 로고
    • Through the "gatekeeper door": Exploiting the active kinase conformation
    • Zuccotto, F., Ardini, E., Casale, E., and Angiolini, M. (2010) Through the "gatekeeper door": exploiting the active kinase conformation J. Med. Chem. 53, 2681-2694
    • (2010) J. Med. Chem. , vol.53 , pp. 2681-2694
    • Zuccotto, F.1    Ardini, E.2    Casale, E.3    Angiolini, M.4
  • 56
    • 84879377486 scopus 로고    scopus 로고
    • Sequence determinants of a specific inactive protein kinase conformation
    • Hari, S. B., Merritt, E. A., and Maly, D. J. (2013) Sequence determinants of a specific inactive protein kinase conformation Chem. Biol. 20, 806-815
    • (2013) Chem. Biol. , vol.20 , pp. 806-815
    • Hari, S.B.1    Merritt, E.A.2    Maly, D.J.3
  • 58
    • 77951689893 scopus 로고    scopus 로고
    • Analysis of imatinib and sorafenib binding to p38alpha compared with c-Abl and b-Raf provides structural insights for understanding the selectivity of inhibitors targeting the DFG-out form of protein kinases
    • Namboodiri, H. V., Bukhtiyarova, M., Ramcharan, J., Karpusas, M., Lee, Y., and Springman, E. B. (2010) Analysis of imatinib and sorafenib binding to p38alpha compared with c-Abl and b-Raf provides structural insights for understanding the selectivity of inhibitors targeting the DFG-out form of protein kinases Biochemistry 49, 3611-3618
    • (2010) Biochemistry , vol.49 , pp. 3611-3618
    • Namboodiri, H.V.1    Bukhtiyarova, M.2    Ramcharan, J.3    Karpusas, M.4    Lee, Y.5    Springman, E.B.6
  • 59
    • 67649995940 scopus 로고    scopus 로고
    • Development of a fluorescent-tagged kinase assay system for the detection and characterization of allosteric kinase inhibitors
    • Simard, J. R., Getlik, M., Grutter, C., Pawar, V., Wulfert, S., Rabiller, M., and Rauh, D. (2009) Development of a fluorescent-tagged kinase assay system for the detection and characterization of allosteric kinase inhibitors J. Am. Chem. Soc. 131, 13286-13296
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 13286-13296
    • Simard, J.R.1    Getlik, M.2    Grutter, C.3    Pawar, V.4    Wulfert, S.5    Rabiller, M.6    Rauh, D.7
  • 62
    • 84863634917 scopus 로고    scopus 로고
    • Fluorophore labeled kinase detects ligands that bind within the MAPK insert of p38alpha kinase
    • Getlik, M., Simard, J. R., Termathe, M., Grutter, C., Rabiller, M., van Otterlo, W. A., and Rauh, D. (2012) Fluorophore labeled kinase detects ligands that bind within the MAPK insert of p38alpha kinase PLoS One 7, e39713
    • (2012) PLoS One , vol.7 , pp. 39713
    • Getlik, M.1    Simard, J.R.2    Termathe, M.3    Grutter, C.4    Rabiller, M.5    Van Otterlo, W.A.6    Rauh, D.7
  • 66
    • 84893873004 scopus 로고    scopus 로고
    • Quick evaluation of kinase inhibitors by surface plasmon resonance using single-site specifically biotinylated kinases
    • Kitagawa, D., Gouda, M., and Kirii, Y. (2014) Quick evaluation of kinase inhibitors by surface plasmon resonance using single-site specifically biotinylated kinases J. Biomol. Screening 19, 453-461
    • (2014) J. Biomol. Screening , vol.19 , pp. 453-461
    • Kitagawa, D.1    Gouda, M.2    Kirii, Y.3
  • 67
    • 33747597796 scopus 로고    scopus 로고
    • Detection of protein conformational change by optical second-harmonic generation
    • Salafsky, J. S. (2006) Detection of protein conformational change by optical second-harmonic generation J. Chem. Phys. 125, 074701
    • (2006) J. Chem. Phys. , vol.125 , pp. 074701
    • Salafsky, J.S.1
  • 68
    • 35448970955 scopus 로고    scopus 로고
    • Second-harmonic generation for studying structural motion of biological molecules in real time and space
    • Salafsky, J. S. (2007) Second-harmonic generation for studying structural motion of biological molecules in real time and space Phys. Chem. Chem. Phys. 9, 5704-5711
    • (2007) Phys. Chem. Chem. Phys. , vol.9 , pp. 5704-5711
    • Salafsky, J.S.1
  • 70
    • 84880806523 scopus 로고    scopus 로고
    • Cracking the molecular origin of intrinsic tyrosine kinase activity through analysis of pathogenic gain-of-function mutations
    • Chen, H., Huang, Z., Dutta, K., Blais, S., Neubert, T. A., Li, X., Cowburn, D., Traaseth, N. J., and Mohammadi, M. (2013) Cracking the molecular origin of intrinsic tyrosine kinase activity through analysis of pathogenic gain-of-function mutations Cell Rep. 4, 376-384
    • (2013) Cell Rep. , vol.4 , pp. 376-384
    • Chen, H.1    Huang, Z.2    Dutta, K.3    Blais, S.4    Neubert, T.A.5    Li, X.6    Cowburn, D.7    Traaseth, N.J.8    Mohammadi, M.9
  • 72
    • 84898003608 scopus 로고    scopus 로고
    • Extracellular-regulated kinase 2 is activated by the enhancement of hinge flexibility
    • Sours, K. M., Xiao, Y., and Ahn, N. G. (2014) Extracellular-regulated kinase 2 is activated by the enhancement of hinge flexibility J. Mol. Biol. 426, 1925-1935
    • (2014) J. Mol. Biol. , vol.426 , pp. 1925-1935
    • Sours, K.M.1    Xiao, Y.2    Ahn, N.G.3
  • 74
    • 49649108911 scopus 로고    scopus 로고
    • Solution conformations and dynamics of ABL kinase-inhibitor complexes determined by NMR substantiate the different binding modes of imatinib/nilotinib and dasatinib
    • Vajpai, N., Strauss, A., Fendrich, G., Cowan-Jacob, S. W., Manley, P. W., Grzesiek, S., and Jahnke, W. (2008) Solution conformations and dynamics of ABL kinase-inhibitor complexes determined by NMR substantiate the different binding modes of imatinib/nilotinib and dasatinib J. Biol. Chem. 283, 18292-18302
    • (2008) J. Biol. Chem. , vol.283 , pp. 18292-18302
    • Vajpai, N.1    Strauss, A.2    Fendrich, G.3    Cowan-Jacob, S.W.4    Manley, P.W.5    Grzesiek, S.6    Jahnke, W.7
  • 77
    • 84921403151 scopus 로고    scopus 로고
    • Druggable sensors of the unfolded protein response
    • Maly, D. J. and Papa, F. R. (2014) Druggable sensors of the unfolded protein response Nat. Chem. Biol. 10, 892-901
    • (2014) Nat. Chem. Biol. , vol.10 , pp. 892-901
    • Maly, D.J.1    Papa, F.R.2
  • 80
    • 84858236398 scopus 로고    scopus 로고
    • Working without kinase activity: Phosphotransfer-independent functions of extracellular signal-regulated kinases
    • Rodriguez, J. and Crespo, P. (2011) Working without kinase activity: phosphotransfer-independent functions of extracellular signal-regulated kinases Sci. Signal 4, re3
    • (2011) Sci. Signal , vol.4 , pp. 3
    • Rodriguez, J.1    Crespo, P.2
  • 81
    • 84901295552 scopus 로고    scopus 로고
    • Conformation-selective ATP-competitive inhibitors control regulatory interactions and noncatalytic functions of mitogen-activated protein kinases
    • Hari, S. B., Merritt, E. A., and Maly, D. J. (2014) Conformation-selective ATP-competitive inhibitors control regulatory interactions and noncatalytic functions of mitogen-activated protein kinases Chem. Biol. 21, 628-635
    • (2014) Chem. Biol. , vol.21 , pp. 628-635
    • Hari, S.B.1    Merritt, E.A.2    Maly, D.J.3
  • 83
    • 84888104464 scopus 로고    scopus 로고
    • NMR reveals the allosteric opening and closing of Abelson tyrosine kinase by ATP-site and myristoyl pocket inhibitors
    • Skora, L., Mestan, J., Fabbro, D., Jahnke, W., and Grzesiek, S. (2013) NMR reveals the allosteric opening and closing of Abelson tyrosine kinase by ATP-site and myristoyl pocket inhibitors Proc. Natl. Acad. Sci. U. S. A. 110, E4437-4445
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 4437-4445
    • Skora, L.1    Mestan, J.2    Fabbro, D.3    Jahnke, W.4    Grzesiek, S.5
  • 85
    • 33144464795 scopus 로고    scopus 로고
    • EKB-569, a new irreversible epidermal growth factor receptor tyrosine kinase inhibitor, with clinical activity in patients with non-small cell lung cancer with acquired resistance to gefitinib
    • Yoshimura, N., Kudoh, S., Kimura, T., Mitsuoka, S., Matsuura, K., Hirata, K., Matsui, K., Negoro, S., Nakagawa, K., and Fukuoka, M. (2006) EKB-569, a new irreversible epidermal growth factor receptor tyrosine kinase inhibitor, with clinical activity in patients with non-small cell lung cancer with acquired resistance to gefitinib Lung Cancer 51, 363-368
    • (2006) Lung Cancer , vol.51 , pp. 363-368
    • Yoshimura, N.1    Kudoh, S.2    Kimura, T.3    Mitsuoka, S.4    Matsuura, K.5    Hirata, K.6    Matsui, K.7    Negoro, S.8    Nakagawa, K.9    Fukuoka, M.10
  • 90
    • 84859388604 scopus 로고    scopus 로고
    • Investigation of the effect of molecular properties on the binding kinetics of a ligand to its biological target
    • Miller, D. C., Lunn, G., Jones, P., Sabnis, Y., Davies, N. L., and Driscoll, P. (2012) Investigation of the effect of molecular properties on the binding kinetics of a ligand to its biological target Medchemcomm 3, 449-452
    • (2012) Medchemcomm , vol.3 , pp. 449-452
    • Miller, D.C.1    Lunn, G.2    Jones, P.3    Sabnis, Y.4    Davies, N.L.5    Driscoll, P.6
  • 91
    • 0023364022 scopus 로고
    • Computer simulations of the diffusion of a substrate to an active site of an enzyme
    • Sharp, K., Fine, R., and Honig, B. (1987) Computer simulations of the diffusion of a substrate to an active site of an enzyme Science 236, 1460-1463
    • (1987) Science , vol.236 , pp. 1460-1463
    • Sharp, K.1    Fine, R.2    Honig, B.3
  • 94
    • 84885131303 scopus 로고    scopus 로고
    • Computational analysis of the binding specificity of Gleevec to Abl, c-Kit, Lck, and c-Src tyrosine kinases
    • Lin, Y. L. and Roux, B. (2013) Computational analysis of the binding specificity of Gleevec to Abl, c-Kit, Lck, and c-Src tyrosine kinases J. Am. Chem. Soc. 135, 14741-14753
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 14741-14753
    • Lin, Y.L.1    Roux, B.2
  • 95
    • 84873135773 scopus 로고    scopus 로고
    • Explaining why Gleevec is a specific and potent inhibitor of Abl kinase
    • Lin, Y. L., Meng, Y., Jiang, W., and Roux, B. (2013) Explaining why Gleevec is a specific and potent inhibitor of Abl kinase Proc. Natl. Acad. Sci. U. S. A. 110, 1664-1669
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 1664-1669
    • Lin, Y.L.1    Meng, Y.2    Jiang, W.3    Roux, B.4
  • 96
    • 77951557992 scopus 로고    scopus 로고
    • Molecular dynamics simulations show that conformational selection governs the binding preferences of imatinib for several tyrosine kinases
    • Aleksandrov, A. and Simonson, T. (2010) Molecular dynamics simulations show that conformational selection governs the binding preferences of imatinib for several tyrosine kinases J. Biol. Chem. 285, 13807-13815
    • (2010) J. Biol. Chem. , vol.285 , pp. 13807-13815
    • Aleksandrov, A.1    Simonson, T.2
  • 97
    • 84890823201 scopus 로고    scopus 로고
    • Conformation-selective inhibitors reveal differences in the activation and phosphate-binding loops of the tyrosine kinases Abl and Src
    • Hari, S. B., Perera, B. G., Ranjitkar, P., Seeliger, M. A., and Maly, D. J. (2013) Conformation-selective inhibitors reveal differences in the activation and phosphate-binding loops of the tyrosine kinases Abl and Src ACS Chem. Biol. 8, 2734-2743
    • (2013) ACS Chem. Biol. , vol.8 , pp. 2734-2743
    • Hari, S.B.1    Perera, B.G.2    Ranjitkar, P.3    Seeliger, M.A.4    Maly, D.J.5
  • 99
    • 84866449140 scopus 로고    scopus 로고
    • A novel approach to the discovery of small-molecule ligands of CDK2
    • Martin, M. P., Alam, R., Betzi, S., Ingles, D. J., Zhu, J. Y., and Schonbrunn, E. (2012) A novel approach to the discovery of small-molecule ligands of CDK2 Chembiochem 13, 2128-2136
    • (2012) Chembiochem , vol.13 , pp. 2128-2136
    • Martin, M.P.1    Alam, R.2    Betzi, S.3    Ingles, D.J.4    Zhu, J.Y.5    Schonbrunn, E.6
  • 100
    • 84921364228 scopus 로고    scopus 로고
    • A dynamically coupled allosteric network underlies binding cooperativity in Src kinase
    • (In press)
    • Foda, Z. H., Shan, Y., Kim, E., Shaw, D. E., and Seeliger, M. A. (In press) A dynamically coupled allosteric network underlies binding cooperativity in Src kinase, Nat. Commun.
    • Nat. Commun.
    • Foda, Z.H.1    Shan, Y.2    Kim, E.3    Shaw, D.E.4    Seeliger, M.A.5
  • 101
    • 37649004940 scopus 로고    scopus 로고
    • Structure of the dual enzyme Ire1 reveals the basis for catalysis and regulation in nonconventional RNA splicing
    • Lee, K. P., Dey, M., Neculai, D., Cao, C., Dever, T. E., and Sicheri, F. (2008) Structure of the dual enzyme Ire1 reveals the basis for catalysis and regulation in nonconventional RNA splicing Cell 132, 89-100
    • (2008) Cell , vol.132 , pp. 89-100
    • Lee, K.P.1    Dey, M.2    Neculai, D.3    Cao, C.4    Dever, T.E.5    Sicheri, F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.