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Volumn 11, Issue 11, 2012, Pages 2394-2400

Mechanism of drug efficacy within the EGF receptor revealed by microsecond molecular dynamics simulation

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR; GEFITINIB;

EID: 84869219081     PISSN: 15357163     EISSN: 15388514     Source Type: Journal    
DOI: 10.1158/1535-7163.MCT-12-0644-T     Document Type: Article
Times cited : (15)

References (38)
  • 3
    • 0023279839 scopus 로고
    • Epidermal-growth-factor receptor status as predictor of early recurrence of and death from breast cancer
    • Sainsbury JRC, Farndon JR, Needham GK, Malcolm AJ, Harris AL. Epidermal-growth-factor receptor status as predictor of early recurrence of and death from breast-cancer. Lancet 1987;1:1398-402. (Pubitemid 17078859)
    • (1987) Lancet , vol.1 , Issue.8547 , pp. 1398-1402
    • Sainsbury, J.R.C.1    Farndon, J.R.2    Needham, G.K.3
  • 4
    • 0034773992 scopus 로고    scopus 로고
    • The EGFR family and its ligands in human cancer: Signalling mechanisms and therapeutic opportunities
    • PII S0959804901002301
    • Yarden Y. The EGFR family and its ligands in human cancer: signalling mechanisms and therapeutic opportunities. Eur J Cancer 2001;37:S3-S8. (Pubitemid 32938123)
    • (2001) European Journal of Cancer , vol.37 , Issue.SUPPL. 4
    • Yarden, Y.1
  • 5
    • 18744415995 scopus 로고    scopus 로고
    • Kinomics: Methods for deciphering the kinome
    • DOI 10.1038/nmeth731
    • Johnson SA, Hunter T. Kinomics: methods for deciphering the kinome. Nat Methods 2005;2:17-25. (Pubitemid 41131053)
    • (2005) Nature Methods , vol.2 , Issue.1 , pp. 17-25
    • Johnson, S.A.1    Hunter, T.2
  • 7
    • 75349091799 scopus 로고    scopus 로고
    • Defining the conserved internal architecture of a protein kinase
    • Kornev AP, Taylor SS. Defining the conserved internal architecture of a protein kinase. Biochim Biophys Acta 2010;1804:440-4.
    • (2010) Biochim Biophys Acta , vol.1804 , pp. 440-444
    • Kornev, A.P.1    Taylor, S.S.2
  • 8
    • 62849097490 scopus 로고    scopus 로고
    • A network of hydrophobic residues impeding helix alpha C rotation maintains latency of kinase Gcn2, which phosphorylates the alpha subunit of translation initiation factor 2
    • Garriz A, Qiu HF, Dey M, Seo EJ, Dever TE, Hinnebusch AG. A network of hydrophobic residues impeding helix alpha C rotation maintains latency of kinase Gcn2, which phosphorylates the alpha subunit of translation initiation factor 2. Mol Cell Biol 2009;29:1592-607.
    • (2009) Mol Cell Biol , vol.29 , pp. 1592-1607
    • Garriz, A.1    Qiu, H.F.2    Dey, M.3    Seo, E.J.4    Dever, T.E.5    Hinnebusch, A.G.6
  • 9
    • 79953726111 scopus 로고    scopus 로고
    • Molecular dynamics analysis of conserved hydrophobic and hydrophilic bond-interaction networks in ErbB family kinases
    • Shin AJ, Telesco SE, Choi SH, Lemmon MA, Radhakrishnan R. Molecular dynamics analysis of conserved hydrophobic and hydrophilic bond-interaction networks in ErbB family kinases. Biochem J 2011;436:241-51.
    • (2011) Biochem J , vol.436 , pp. 241-251
    • Shin, A.J.1    Telesco, S.E.2    Choi, S.H.3    Lemmon, M.A.4    Radhakrishnan, R.5
  • 11
    • 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;53:1413-37.
    • (2010) J Med Chem , vol.53 , pp. 1413-1437
    • Morphy, R.1
  • 12
    • 1642323740 scopus 로고    scopus 로고
    • Protein Kinase Inhibitors: Insights into Drug Design from Structure
    • DOI 10.1126/science.1095920
    • Noble MEM, Endicott JA, Johnson LN. Protein kinase inhibitors: insights into drug design from structure. Science 2004;303:1800-5. (Pubitemid 38374863)
    • (2004) Science , vol.303 , Issue.5665 , pp. 1800-1805
    • Noble, M.E.M.1    Endicott, J.A.2    Johnson, L.N.3
  • 13
    • 0036147568 scopus 로고    scopus 로고
    • Multiple diverse ligands binding at a single protein site: A matter of pre-existing populations
    • DOI 10.1110/ps.21302
    • Ma BY, Shatsky M, Wolfson HJ, Nussinov R. Multiple diverse ligands binding at a single protein site: a matter of pre-existing populations. Protein Sci 2002;11:184-97. (Pubitemid 34075781)
    • (2002) Protein Science , vol.11 , Issue.2 , pp. 184-197
    • Ma, B.1    Shatsky, M.2    Wolfson, H.J.3    Nussinov, R.4
  • 14
    • 79960092299 scopus 로고    scopus 로고
    • Rapid and accurate ranking of binding affinities of epidermal growth factor receptor sequences with selected lung cancer drugs
    • Wan S, Coveney PV. Rapid and accurate ranking of binding affinities of epidermal growth factor receptor sequences with selected lung cancer drugs. J R Soc Interface 2011;8:1114-27.
    • (2011) J R Soc Interface , vol.8 , pp. 1114-1127
    • Wan, S.1    Coveney, P.V.2
  • 15
    • 70350340728 scopus 로고    scopus 로고
    • The role of dynamic conformational ensembles in biomolecular recognition
    • Boehr DD, Nussinov R, Wright PE. The role of dynamic conformational ensembles in biomolecular recognition. Nat Chem Biol 2009;5:789-96.
    • (2009) Nat Chem Biol , vol.5 , pp. 789-796
    • Boehr, D.D.1    Nussinov, R.2    Wright, P.E.3
  • 16
    • 0023140044 scopus 로고
    • Multiple conformational states of proteins: A molecular dynamics analysis of myoglobin
    • Elber R, Karplus M. Multiple conformational states of proteins - a molecular-dynamics analysis of myoglobin. Science 1987;235:318-21. (Pubitemid 17232557)
    • (1987) Science , vol.235 , Issue.4786 , pp. 318-321
    • Elber, R.1    Karplus, M.2
  • 17
    • 78651399683 scopus 로고    scopus 로고
    • Structure and function of an irreversible agonist-beta(2) adrenoceptor complex
    • Rosenbaum DM, Zhang C, Lyons JA, Holl R, Aragao D, Arlow DH, et al. Structure and function of an irreversible agonist-beta(2) adrenoceptor complex. Nature 2011;469:236-40.
    • (2011) Nature , vol.469 , pp. 236-240
    • Rosenbaum, D.M.1    Zhang, C.2    Lyons, J.A.3    Holl, R.4    Aragao, D.5    Arlow, D.H.6
  • 18
    • 79960642090 scopus 로고    scopus 로고
    • Molecular dynamics simulation reveals structural and thermodynamic features of kinase activation by cancer mutations within the epidermal growth factor receptor
    • Wan S, Coveney PV. Molecular dynamics simulation reveals structural and thermodynamic features of kinase activation by cancer mutations within the epidermal growth factor receptor. J Comput Chem 2011;32:2843-52.
    • (2011) J Comput Chem , vol.32 , pp. 2843-2852
    • Wan, S.1    Coveney, P.V.2
  • 20
    • 0029912748 scopus 로고    scopus 로고
    • Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids
    • DOI 10.1021/ja9621760, PII S0002786396021762
    • Jorgensen WL, Maxwell DS, Tirado-Rives J. Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids. J Am Chem Soc 1996;118:11225-36. (Pubitemid 26399746)
    • (1996) Journal of the American Chemical Society , vol.118 , Issue.45 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tirado-Rives, J.3
  • 21
  • 24
    • 18744373865 scopus 로고    scopus 로고
    • Crystal structure of an activated Akt/Protein Kinase B ternary complex with GSK3-peptide and AMP-PNP
    • DOI 10.1038/nsb870
    • Yang J, Cron P, Good VM, Thompson V, Hemmings BA, Barford D. Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-PNP. Nat Struct Biol 2002;9:940-4. (Pubitemid 35417064)
    • (2002) Nature Structural Biology , vol.9 , Issue.12 , pp. 940-944
    • Yang, J.1    Cron, P.2    Good, V.M.3    Thompson, V.4    Hemmings, B.A.5    Barford, D.6
  • 25
    • 77952786003 scopus 로고    scopus 로고
    • Accurate ensemble molecular dynamics binding free energy ranking of multidrug-resistant HIV-1 proteases
    • Sadiq SK, Wright DW, Kenway OA, Coveney PV. Accurate ensemble molecular dynamics binding free energy ranking of multidrug-resistant HIV-1 proteases. J Chem Inf Model 2010;50:890-905.
    • (2010) J Chem Inf Model , vol.50 , pp. 890-905
    • Sadiq, S.K.1    Wright, D.W.2    Kenway, O.A.3    Coveney, P.V.4
  • 28
    • 77957231785 scopus 로고    scopus 로고
    • Induced fit, conformational selection and independent dynamic segments: An extended view of binding events
    • Csermely P, Palotai R, Nussinov R. Induced fit, conformational selection and independent dynamic segments: an extended view of binding events. Trends Biochem Sci 2010;35:539-46.
    • (2010) Trends Biochem Sci , vol.35 , pp. 539-546
    • Csermely, P.1    Palotai, R.2    Nussinov, R.3
  • 29
    • 0036680063 scopus 로고    scopus 로고
    • Protein flexibility and drug design: How to hit a moving target
    • DOI 10.1016/S1367-5931(02)00341-1
    • Carlson HA. Protein flexibility and drug design: how to hit a moving target. Curr Opin Chem Biol 2002;6:447-52. (Pubitemid 34804766)
    • (2002) Current Opinion in Chemical Biology , vol.6 , Issue.4 , pp. 447-452
    • Carlson, H.A.1
  • 32
    • 80051965827 scopus 로고    scopus 로고
    • Relative abundance of EGFR mutations predicts benefit from gefitinib treatment for advanced non-small-cell lung cancer
    • Zhou Q, Zhang XC, Chen ZH, Yin XL, Yang JJ, Xu CR, et al. Relative abundance of EGFR mutations predicts benefit from gefitinib treatment for advanced non-small-cell lung cancer. J Clin Oncol 2011;29:3316-21.
    • (2011) J Clin Oncol , vol.29 , pp. 3316-3321
    • Zhou, Q.1    Zhang, X.C.2    Chen, Z.H.3    Yin, X.L.4    Yang, J.J.5    Xu, C.R.6
  • 36
    • 84867585198 scopus 로고    scopus 로고
    • From base pair to bedside: Molecular simulation and the translation of genomics to personalized medicine
    • doi: 10.1002/wsbm.1186. [Epub ahead of print]
    • Wright DW, Wan S, Shublaq N, Zesada S, Coveney PV. From base pair to bedside: molecular simulation and the translation of genomics to personalized medicine. WIREs Syst Biol Med 2012. doi: 10.1002/wsbm.1186. [Epub ahead of print].
    • (2012) WIREs Syst Biol Med
    • Wright, D.W.1    Wan, S.2    Shublaq, N.3    Zesada, S.4    Coveney, P.V.5
  • 37
    • 33847406095 scopus 로고    scopus 로고
    • Structures of Lung Cancer-Derived EGFR Mutants and Inhibitor Complexes: Mechanism of Activation and Insights into Differential Inhibitor Sensitivity
    • DOI 10.1016/j.ccr.2006.12.017, PII S1535610807000281
    • Yun CH, Boggon TJ, Li YQ, Woo MS, Greulich H, Meyerson M, et al. Structures of lung cancer-derived EGFR mutants and inhibitor complexes: mechanism of activation and insights into differential inhibitor sensitivity. Cancer Cell 2007;11:217-27. (Pubitemid 46349842)
    • (2007) Cancer Cell , vol.11 , Issue.3 , 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.