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Volumn 51, Issue 12, 2012, Pages 2390-2406

A water-based mechanism of specificity and resistance for lapatinib with ErbB family kinases

Author keywords

[No Author keywords available]

Indexed keywords

COULOMBIC INTERACTIONS; FREE-ENERGY CALCULATIONS; HIGH AFFINITY; HOMOLOGY MODELING; HYDRATION PATTERNS; KINASE INHIBITORS; LAPATINIB; MOLECULAR BASIS; MOLECULAR DYNAMICS SIMULATIONS; QUANTITATIVE AGREEMENT; RECEPTOR TYROSINE KINASE; SIDE-CHAINS; WATER BASED; WATER MOLECULE; WATER NETWORKS;

EID: 84859166733     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi2016553     Document Type: Article
Times cited : (21)

References (83)
  • 1
    • 84859171349 scopus 로고    scopus 로고
    • American Cancer Society: Breast Cancer Facts & Figures 2011-2012. (accessed Oct 26).
    • American Cancer Society: Breast Cancer Facts & Figures 2011-2012. http://www.cancer.org (accessed Oct 26, 2011).
    • (2011)
  • 3
    • 18344390418 scopus 로고    scopus 로고
    • ERBB receptors and cancer: The complexity of targeted inhibitors
    • Hynes, N. E. and Lane, H. A. (2005) ERBB receptors and cancer: The complexity of targeted inhibitors Nat. Rev. Cancer 5, 341-354
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 341-354
    • Hynes, N.E.1    Lane, H.A.2
  • 4
    • 0026571910 scopus 로고
    • The Clinical Significance of Epidermal Growth Factor Receptor (EGF-R) in Human Breast Cancer: A Review on 5232 Patients
    • Klijn, J. G. M., Berns, P. M. J. J., Schmitz, P. I. M., and Foekens, J. A. (1992) The Clinical Significance of Epidermal Growth Factor Receptor (EGF-R) in Human Breast Cancer: A Review on 5232 Patients Endocr. Rev. 13, 3-17
    • (1992) Endocr. Rev. , vol.13 , pp. 3-17
    • Klijn, J.G.M.1    Berns, P.M.J.J.2    Schmitz, P.I.M.3    Foekens, J.A.4
  • 5
    • 0032445260 scopus 로고    scopus 로고
    • HER-2/neu as a predictive marker of response to breast cancer therapy
    • Pegram, M. D., Pauletti, G., and Slamon, D. J. (1998) HER-2/neu as a predictive marker of response to breast cancer therapy Breast Cancer Res. Treat. 52, 65-77
    • (1998) Breast Cancer Res. Treat. , vol.52 , pp. 65-77
    • Pegram, M.D.1    Pauletti, G.2    Slamon, D.J.3
  • 6
    • 84859174268 scopus 로고    scopus 로고
    • Drugs@FDA website. (accessed Oct 26).
    • Drugs@FDA website. http://www.accessdata.fda.gov/scripts/cder/drugsatfda/ index.cfm (accessed Oct 26, 2011).
    • (2011)
  • 11
  • 14
    • 54049122600 scopus 로고    scopus 로고
    • Comparison of the EGFR resistance mutation profiles generated by EGFR-targeted tyrosine kinase inhibitors and the impact of drug combinations
    • Avizienyte, E., Ward, R. A., and Garner, A. P. (2008) Comparison of the EGFR resistance mutation profiles generated by EGFR-targeted tyrosine kinase inhibitors and the impact of drug combinations Biochem. J. 415, 197-206
    • (2008) Biochem. J. , vol.415 , pp. 197-206
    • Avizienyte, E.1    Ward, R.A.2    Garner, A.P.3
  • 16
    • 0035553174 scopus 로고    scopus 로고
    • The Effects of the Novel, Reversible Epidermal Growth Factor Receptor/ErbB-2 Tyrosine Kinase Inhibitor, GW2016, on the Growth of Human Normal and Tumor-derived Cell Lines in Vitro and in Vivo
    • Rusnak, D. W., Lackey, K., Affleck, K., Wood, E. R., Alligood, K. J., Rhodes, N., Keith, B. R., Murray, D. M., Knight, W. B., Mullin, R. J., and Gilmer, T. M. (2001) The Effects of the Novel, Reversible Epidermal Growth Factor Receptor/ErbB-2 Tyrosine Kinase Inhibitor, GW2016, on the Growth of Human Normal and Tumor-derived Cell Lines in Vitro and in Vivo Mol. Cancer Ther. 1, 85-94
    • (2001) Mol. Cancer Ther. , vol.1 , pp. 85-94
    • Rusnak, D.W.1    Lackey, K.2    Affleck, K.3    Wood, E.R.4    Alligood, K.J.5    Rhodes, N.6    Keith, B.R.7    Murray, D.M.8    Knight, W.B.9    Mullin, R.J.10    Gilmer, T.M.11
  • 18
    • 33745002702 scopus 로고    scopus 로고
    • An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
    • Zhang, X., Gureasko, J., Shen, K., Cole, P. A., and Kuriyan, J. (2006) An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor Cell 125, 1137-1149
    • (2006) Cell , vol.125 , pp. 1137-1149
    • Zhang, X.1    Gureasko, J.2    Shen, K.3    Cole, P.A.4    Kuriyan, J.5
  • 19
    • 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
  • 20
    • 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
  • 21
    • 33646125891 scopus 로고    scopus 로고
    • Lessons from the drug discovery of lapatinib, a dual ErbB1/2 tyrosine kinase inhibitor
    • Lackey, K. E. (2006) Lessons from the drug discovery of lapatinib, a dual ErbB1/2 tyrosine kinase inhibitor Curr. Top. Med. Chem. 6, 435-460
    • (2006) Curr. Top. Med. Chem. , vol.6 , pp. 435-460
    • Lackey, K.E.1
  • 23
    • 16844369407 scopus 로고    scopus 로고
    • Absence of HER4 expression predicts recurrence of ductal carcinoma in situ of the breast
    • Barnes, N. L., Khavari, S., Boland, G. P., Cramer, A., Knox, W. F., and Bundred, N. J. (2005) Absence of HER4 expression predicts recurrence of ductal carcinoma in situ of the breast Clin. Cancer Res. 11, 2163-2168
    • (2005) Clin. Cancer Res. , vol.11 , pp. 2163-2168
    • Barnes, N.L.1    Khavari, S.2    Boland, G.P.3    Cramer, A.4    Knox, W.F.5    Bundred, N.J.6
  • 26
    • 18244371651 scopus 로고    scopus 로고
    • Acquired resistance of lung adenocarcinomas to gefitinib or erlotinib is associated with a second mutation in the EGFR kinase domain
    • Pao, W., Miller, V. A., Politi, K. A., Riely, G. J., Somwar, R., Zakowski, M. F., Kris, M. G., and Varmus, H. (2005) Acquired resistance of lung adenocarcinomas to gefitinib or erlotinib is associated with a second mutation in the EGFR kinase domain PLoS Med. 2, e73
    • (2005) PLoS Med. , vol.2 , pp. 73
    • Pao, W.1    Miller, V.A.2    Politi, K.A.3    Riely, G.J.4    Somwar, R.5    Zakowski, M.F.6    Kris, M.G.7    Varmus, H.8
  • 28
    • 58149333768 scopus 로고    scopus 로고
    • Acquired resistance to epidermal growth factor receptor kinase inhibitors associated with a novel T854A mutation in a patient with EGFR-mutant lung adenocarcinoma
    • Bean, J., Riely, G. J., Balak, M., Marks, J. L., Ladanyi, M., Miller, V. A., and Pao, W. (2008) Acquired resistance to epidermal growth factor receptor kinase inhibitors associated with a novel T854A mutation in a patient with EGFR-mutant lung adenocarcinoma Clin. Cancer Res. 14, 7519-7525
    • (2008) Clin. Cancer Res. , vol.14 , pp. 7519-7525
    • Bean, J.1    Riely, G.J.2    Balak, M.3    Marks, J.L.4    Ladanyi, M.5    Miller, V.A.6    Pao, W.7
  • 29
    • 0035800507 scopus 로고    scopus 로고
    • Clinical resistance to STI-571 cancer therapy caused by BCR-ABL gene mutation or amplification
    • Gorre, M. E., Mohammed, M., Ellwood, K., Hsu, N., Paquette, R., Rao, P. N., and Sawyers, C. L. (2001) Clinical resistance to STI-571 cancer therapy caused by BCR-ABL gene mutation or amplification Science 293, 876-880
    • (2001) Science , vol.293 , pp. 876-880
    • Gorre, M.E.1    Mohammed, M.2    Ellwood, K.3    Hsu, N.4    Paquette, R.5    Rao, P.N.6    Sawyers, C.L.7
  • 32
    • 26644448460 scopus 로고    scopus 로고
    • Asp746 to Glycine Change May have a Greater Influence than Cys751 to Serine Change in Accounting for Ligand Selectivity between EGFR and HER-2 at the ATP Site
    • Kamath, S. and Buolamwini, J. (2005) Asp746 to Glycine Change May have a Greater Influence than Cys751 to Serine Change in Accounting for Ligand Selectivity between EGFR and HER-2 at the ATP Site J. Comput.-Aided Mol. Des. 19, 287-291
    • (2005) J. Comput.-Aided Mol. Des. , vol.19 , pp. 287-291
    • Kamath, S.1    Buolamwini, J.2
  • 34
    • 0037208314 scopus 로고    scopus 로고
    • Mapping the binding site of a large set of quinazoline type EGF-R inhibitors using molecular field analyses and molecular docking studies
    • Hou, T., Zhu, L., Chen, L., and Xu, X. (2003) Mapping the binding site of a large set of quinazoline type EGF-R inhibitors using molecular field analyses and molecular docking studies J. Chem. Inf. Comput. Sci. 43, 273-287
    • (2003) J. Chem. Inf. Comput. Sci. , vol.43 , pp. 273-287
    • Hou, T.1    Zhu, L.2    Chen, L.3    Xu, X.4
  • 35
    • 42049110178 scopus 로고    scopus 로고
    • Computational study of the binding mode of epidermal growth factor receptor kinase inhibitors
    • Chen, H. F. (2008) Computational study of the binding mode of epidermal growth factor receptor kinase inhibitors Chem. Biol. Drug Des. 71, 434-446
    • (2008) Chem. Biol. Drug Des. , vol.71 , pp. 434-446
    • Chen, H.F.1
  • 36
    • 33144460979 scopus 로고    scopus 로고
    • In silico identification of novel EGFR inhibitors with antiproliferative activity against cancer cells
    • Cavasotto, C. N., Ortiz, M. A., Abagyan, R. A., and Piedrafita, F. J. (2006) In silico identification of novel EGFR inhibitors with antiproliferative activity against cancer cells Bioorg. Med. Chem. Lett. 16, 1969-1974
    • (2006) Bioorg. Med. Chem. Lett. , vol.16 , pp. 1969-1974
    • Cavasotto, C.N.1    Ortiz, M.A.2    Abagyan, R.A.3    Piedrafita, F.J.4
  • 37
    • 33749002274 scopus 로고    scopus 로고
    • Impact of EGFR point mutations on the sensitivity to gefitinib: Insights from comparative structural analyses and molecular dynamics simulations
    • Liu, B., Bernard, B., and Wu, J. H. (2006) Impact of EGFR point mutations on the sensitivity to gefitinib: Insights from comparative structural analyses and molecular dynamics simulations Proteins 65, 331-346
    • (2006) Proteins , vol.65 , pp. 331-346
    • Liu, B.1    Bernard, B.2    Wu, J.H.3
  • 38
    • 34249650622 scopus 로고    scopus 로고
    • A multiscale computational approach to dissect early events in the Erb family receptor mediated activation, differential signaling, and relevance to oncogenic transformations
    • Liu, Y., Purvis, J., Shih, A., Weinstein, J., Agrawal, N., and Radhakrishnan, R. (2007) A multiscale computational approach to dissect early events in the Erb family receptor mediated activation, differential signaling, and relevance to oncogenic transformations Ann. Biomed. Eng. 35, 1012-1025
    • (2007) Ann. Biomed. Eng. , vol.35 , pp. 1012-1025
    • Liu, Y.1    Purvis, J.2    Shih, A.3    Weinstein, J.4    Agrawal, N.5    Radhakrishnan, R.6
  • 39
    • 69749120935 scopus 로고    scopus 로고
    • Quantitative Prediction of Fold Resistance for Inhibitors of EGFR
    • Balius, T. E. and Rizzo, R. C. (2009) Quantitative Prediction of Fold Resistance for Inhibitors of EGFR Biochemistry 48, 8435-8448
    • (2009) Biochemistry , vol.48 , pp. 8435-8448
    • Balius, T.E.1    Rizzo, R.C.2
  • 40
    • 70350315092 scopus 로고    scopus 로고
    • Energetics of Displacing Water Molecules from Protein Binding Sites: Consequences for Ligand Optimization
    • Michel, J., Tirado-Rives, J., and Jorgensen, W. L. (2009) Energetics of Displacing Water Molecules from Protein Binding Sites: Consequences for Ligand Optimization J. Am. Chem. Soc. 131, 15403-15411
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 15403-15411
    • Michel, J.1    Tirado-Rives, J.2    Jorgensen, W.L.3
  • 41
    • 10444280878 scopus 로고    scopus 로고
    • Strategies to overcome resistance to targeted protein kinase inhibitors
    • Daub, H., Specht, K., and Ullrich, A. (2004) Strategies to overcome resistance to targeted protein kinase inhibitors Nat. Rev. Drug Discovery 3, 1001-1010
    • (2004) Nat. Rev. Drug Discovery , vol.3 , pp. 1001-1010
    • Daub, H.1    Specht, K.2    Ullrich, A.3
  • 42
    • 4143121554 scopus 로고    scopus 로고
    • Free energy of ligand binding to protein: Evaluation of the contribution of water molecules by computational methods
    • Cozzini, P., Fornabaio, M., Marabotti, A., Abraham, D. J., Kellogg, G. E., and Mozzarelli, A. (2004) Free energy of ligand binding to protein: Evaluation of the contribution of water molecules by computational methods Curr. Med. Chem. 11, 3093-3118
    • (2004) Curr. Med. Chem. , vol.11 , pp. 3093-3118
    • Cozzini, P.1    Fornabaio, M.2    Marabotti, A.3    Abraham, D.J.4    Kellogg, G.E.5    Mozzarelli, A.6
  • 43
    • 34247187356 scopus 로고    scopus 로고
    • Analysis of Ligand-Bound Water Molecules in High-Resolution Crystal Structures of Protein-Ligand Complexes
    • Lu, Y., Wang, R., Yang, C.-Y., and Wang, S. (2007) Analysis of Ligand-Bound Water Molecules in High-Resolution Crystal Structures of Protein-Ligand Complexes J. Chem. Inf. Model. 47, 668-675
    • (2007) J. Chem. Inf. Model. , vol.47 , pp. 668-675
    • Lu, Y.1    Wang, R.2    Yang, C.-Y.3    Wang, S.4
  • 44
    • 33846524439 scopus 로고    scopus 로고
    • Motifs for molecular recognition exploiting hydrophobic enclosure in protein-ligand binding
    • Young, T., Abel, R., Kim, B., Berne, B. J., and Friesner, R. A. (2007) Motifs for molecular recognition exploiting hydrophobic enclosure in protein-ligand binding Proc. Natl. Acad. Sci. U.S.A. 104, 808-813
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 808-813
    • Young, T.1    Abel, R.2    Kim, B.3    Berne, B.J.4    Friesner, R.A.5
  • 46
    • 0029003145 scopus 로고
    • Three-dimensional structure of the complex of 4-guanidino-Neu5Ac2en and influenza virus neuraminidase
    • Varghese, J. N., Epa, V. C., and Colman, P. M. (1995) Three-dimensional structure of the complex of 4-guanidino-Neu5Ac2en and influenza virus neuraminidase Protein Sci. 4, 1081-1087
    • (1995) Protein Sci. , vol.4 , pp. 1081-1087
    • Varghese, J.N.1    Epa, V.C.2    Colman, P.M.3
  • 48
    • 42949149763 scopus 로고    scopus 로고
    • 6-Ethynylthieno[3,2-d]- and 6-ethynylthieno[2,3-d]pyrimidin-4-anilines as tunable covalent modifiers of ErbB kinases
    • Wood, E. R., Shewchuk, L. M., Ellis, B., Brignola, P., and Brashear, R. L. 2008, 6-Ethynylthieno[3,2-d]- and 6-ethynylthieno[2,3-d]pyrimidin-4-anilines as tunable covalent modifiers of ErbB kinases Proc. Natl. Acad. Sci. U.S.A. 105, 2773-2778
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 2773-2778
    • Wood, E.R.1    Shewchuk, L.M.2    Ellis, B.3    Brignola, P.4    Brashear, R.L.5
  • 50
    • 0027136282 scopus 로고
    • Comparative Protein Modelling by Satisfaction of Spatial Restraints
    • Sali, A. and Blundell, T. L. (1993) Comparative Protein Modelling by Satisfaction of Spatial Restraints J. Mol. Biol. 234, 779-815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 51
    • 0027968068 scopus 로고
    • Clustal W: Improving the Sensitivity of Progressive Multiple Sequence Alignment through Sequence Weighting, Position-Specific Gap Penalties and Weight Matrix Choice
    • Thompson, J. D., Higgins, D. G., and Gibson, T. J. (1994) Clustal W: Improving the Sensitivity of Progressive Multiple Sequence Alignment through Sequence Weighting, Position-Specific Gap Penalties and Weight Matrix Choice Nucleic Acids Res. 22, 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 52
    • 33749578940 scopus 로고    scopus 로고
    • Statistical potential for assessment and prediction of protein structures
    • Shen, M.-Y. and Sali, A. (2006) Statistical potential for assessment and prediction of protein structures Protein Sci. 15, 2507-2524
    • (2006) Protein Sci. , vol.15 , pp. 2507-2524
    • Shen, M.-Y.1    Sali, A.2
  • 53
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: A program to check the stereochemical quality of protein structures J. Appl. Crystallogr. 26, 283-291
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 54
    • 84859200212 scopus 로고    scopus 로고
    • Chemical Computing Group Inc. Montreal.
    • MOE (2008) Chemical Computing Group Inc., Montreal.
    • (2008) MOE
  • 60
    • 84986513567 scopus 로고
    • Determining Atom-Centered Monopoles from Molecular Electrostatic Potentials: The Need for High Sampling Density in Formamide Conformational Analysis
    • Breneman, C. M. and Wiberg, K. B. (1990) Determining Atom-Centered Monopoles from Molecular Electrostatic Potentials: The Need for High Sampling Density in Formamide Conformational Analysis J. Comput. Chem. 11, 361-373
    • (1990) J. Comput. Chem. , vol.11 , pp. 361-373
    • Breneman, C.M.1    Wiberg, K.B.2
  • 62
    • 36449007836 scopus 로고
    • Constant pressure molecular dynamics simulation: The Langevin piston method
    • Feller, S. E., Zhang, Y., Pastor, R. W., and Brooks, B. R. (1995) Constant pressure molecular dynamics simulation: The Langevin piston method J. Chem. Phys. 103, 4613-4621
    • (1995) J. Chem. Phys. , vol.103 , pp. 4613-4621
    • Feller, S.E.1    Zhang, Y.2    Pastor, R.W.3    Brooks, B.R.4
  • 63
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert, J.-P., Ciccotti, G., and Berendsen, H. J. C. (1977) Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes J. Comput. Phys. 23, 327-341
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.-P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 64
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N log(N) method for Ewald sums in large systems
    • Darden, T., York, D., and Pedersen, L. (1993) Particle mesh Ewald: An N log(N) method for Ewald sums in large systems J. Chem. Phys. 98, 10089-10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 65
    • 0032560959 scopus 로고    scopus 로고
    • Continuum solvent studies of the stability of DNA, RNA, and phosphoramidate-DNA helices
    • Srinivasan, J., Cheatham, T. E., III, Cieplak, P., Kollman, P. A., and Case, D. A. (1998) Continuum solvent studies of the stability of DNA, RNA, and phosphoramidate-DNA helices J. Am. Chem. Soc. 120, 9401-9409
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 9401-9409
    • Srinivasan, J.1    Cheatham III, T.E.2    Cieplak, P.3    Kollman, P.A.4    Case, D.A.5
  • 67
    • 34247219622 scopus 로고    scopus 로고
    • Binding of antifusion peptides with HIVgp41 from molecular dynamics simulations: Quantitative correlation with experiment
    • Strockbine, B. and Rizzo, R. C. (2007) Binding of antifusion peptides with HIVgp41 from molecular dynamics simulations: Quantitative correlation with experiment Proteins: Struct., Funct., Bioinf. 67, 630-642
    • (2007) Proteins: Struct., Funct., Bioinf. , vol.67 , pp. 630-642
    • Strockbine, B.1    Rizzo, R.C.2
  • 68
    • 57749118013 scopus 로고    scopus 로고
    • Origins of Resistance Conferred by the R292K Neuraminidase Mutation via Molecular Dynamics and Free Energy Calculations
    • Chachra, R. and Rizzo, R. C. (2008) Origins of Resistance Conferred by the R292K Neuraminidase Mutation via Molecular Dynamics and Free Energy Calculations J. Chem. Theory Comput. 4, 1526-1540
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 1526-1540
    • Chachra, R.1    Rizzo, R.C.2
  • 69
    • 57749100107 scopus 로고    scopus 로고
    • Calculation of binding free energies for non-zinc chelating pyrimidine dicarboxamide inhibitors with MMP-13
    • Carrascal, N. and Rizzo, R. C. (2009) Calculation of binding free energies for non-zinc chelating pyrimidine dicarboxamide inhibitors with MMP-13 Bioorg. Med. Chem. Lett. 19, 47-50
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 47-50
    • Carrascal, N.1    Rizzo, R.C.2
  • 70
    • 77951670043 scopus 로고    scopus 로고
    • Origins of Resistance to the HIVgp41 Viral Entry Inhibitor T20
    • McGillick, B. E., Balius, T. E., Mukherjee, S., and Rizzo, R. C. (2010) Origins of Resistance to the HIVgp41 Viral Entry Inhibitor T20 Biochemistry 49, 3575-3592
    • (2010) Biochemistry , vol.49 , pp. 3575-3592
    • McGillick, B.E.1    Balius, T.E.2    Mukherjee, S.3    Rizzo, R.C.4
  • 71
    • 1842479952 scopus 로고    scopus 로고
    • Exploring protein native states and large-scale conformational changes with a modified generalized born model
    • Onufriev, A., Bashford, D., and Case, D. A. (2004) Exploring protein native states and large-scale conformational changes with a modified generalized born model Proteins: Struct., Funct., Bioinf. 55, 383-394
    • (2004) Proteins: Struct., Funct., Bioinf. , vol.55 , pp. 383-394
    • Onufriev, A.1    Bashford, D.2    Case, D.A.3
  • 72
    • 32844457567 scopus 로고
    • Accurate Calculation of Hydration Free-Energies Using Macroscopic Solvent Models
    • Sitkoff, D., Sharp, K. A., and Honig, B. (1994) Accurate Calculation of Hydration Free-Energies Using Macroscopic Solvent Models J. Phys. Chem. 98, 1978-1988
    • (1994) J. Phys. Chem. , vol.98 , pp. 1978-1988
    • Sitkoff, D.1    Sharp, K.A.2    Honig, B.3
  • 73
    • 69349101503 scopus 로고    scopus 로고
    • Quantifying uncertainty and sampling quality in biomolecular simulations
    • Grossfield, A. and Zuckerman, D. M. (2009) Quantifying uncertainty and sampling quality in biomolecular simulations Annu. Rep. Comput. Chem. 5, 23-48
    • (2009) Annu. Rep. Comput. Chem. , vol.5 , pp. 23-48
    • Grossfield, A.1    Zuckerman, D.M.2
  • 74
    • 0036140611 scopus 로고    scopus 로고
    • Determining the shear viscosity of model liquids from molecular dynamics simulations
    • Hess, B. (2002) Determining the shear viscosity of model liquids from molecular dynamics simulations J. Chem. Phys. 116, 209-217
    • (2002) J. Chem. Phys. , vol.116 , pp. 209-217
    • Hess, B.1
  • 75
    • 0037442584 scopus 로고    scopus 로고
    • Molecular dynamics simulations and thermodynamics analysis of DNA-drug complexes. Minor groove binding between 4′,6-diamidino-2-phenylindole and DNA duplexes in solution
    • Spackova, N., Cheatham, T. E., III, Ryjacek, F., Lankas, F., Van Meervelt, L., Hobza, P., and Sponer, J. (2003) Molecular dynamics simulations and thermodynamics analysis of DNA-drug complexes. Minor groove binding between 4′,6-diamidino-2-phenylindole and DNA duplexes in solution J. Am. Chem. Soc. 125, 1759-1769
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 1759-1769
    • Spackova, N.1    Cheatham III, T.E.2    Ryjacek, F.3    Lankas, F.4    Van Meervelt, L.5    Hobza, P.6    Sponer, J.7
  • 76
    • 0346996361 scopus 로고    scopus 로고
    • Investigation of Neuraminidase-Substrate Recognition Using Molecular Dynamics and Free Energy Calculations
    • Masukawa, K. M., Kollman, P. A., and Kuntz, I. D. (2003) Investigation of Neuraminidase-Substrate Recognition Using Molecular Dynamics and Free Energy Calculations J. Med. Chem. 46, 5628-5637
    • (2003) J. Med. Chem. , vol.46 , pp. 5628-5637
    • Masukawa, K.M.1    Kollman, P.A.2    Kuntz, I.D.3
  • 77
    • 65249187243 scopus 로고    scopus 로고
    • MM-PBSA Captures Key Role of Intercalating Water Molecules at a Protein-Protein Interface
    • Wong, S., Amaro, R. E., and McCammon, J. A. (2009) MM-PBSA Captures Key Role of Intercalating Water Molecules at a Protein-Protein Interface J. Chem. Theory Comput. 5, 422-429
    • (2009) J. Chem. Theory Comput. , vol.5 , pp. 422-429
    • Wong, S.1    Amaro, R.E.2    McCammon, J.A.3
  • 78
    • 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
  • 79
    • 33846552656 scopus 로고    scopus 로고
    • Escape from HER-family tyrosine kinase inhibitor therapy by the kinase-inactive HER3
    • Sergina, N. V., Rausch, M., Wang, D., Blair, J., Hann, B., Shokat, K. M., and Moasser, M. M. (2007) Escape from HER-family tyrosine kinase inhibitor therapy by the kinase-inactive HER3 Nature 445, 437-441
    • (2007) Nature , vol.445 , pp. 437-441
    • Sergina, N.V.1    Rausch, M.2    Wang, D.3    Blair, J.4    Hann, B.5    Shokat, K.M.6    Moasser, M.M.7
  • 80
    • 34547871259 scopus 로고    scopus 로고
    • Targeting HER proteins in cancer therapy and the role of the non-target HER3
    • Hsieh, A. C. and Moasser, M. M. (2007) Targeting HER proteins in cancer therapy and the role of the non-target HER3 Br. J. Cancer 97, 453-457
    • (2007) Br. J. Cancer , vol.97 , pp. 453-457
    • Hsieh, A.C.1    Moasser, M.M.2
  • 82
    • 77952338791 scopus 로고    scopus 로고
    • ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation
    • Shi, F., Telesco, S. E., Liu, Y., Radhakrishnan, R., and Lemmon, M. A. (2010) ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation Proc. Natl. Acad. Sci. U.S.A. 107, 7692-7697
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 7692-7697
    • Shi, F.1    Telesco, S.E.2    Liu, Y.3    Radhakrishnan, R.4    Lemmon, M.A.5
  • 83
    • 76049128717 scopus 로고    scopus 로고
    • Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3
    • Jura, N., Shan, Y., Cao, X., Shaw, D. E., and Kuriyan, J. (2009) Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3 Proc. Natl. Acad. Sci. U.S.A. 106, 21608-21613
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 21608-21613
    • Jura, N.1    Shan, Y.2    Cao, X.3    Shaw, D.E.4    Kuriyan, J.5


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