메뉴 건너뛰기




Volumn 53, Issue 12, 2013, Pages 3343-3351

Structural and energetic analyses of SNPs in drug targets and implications for drug therapy

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; BINDING SITES; DISEASE CONTROL;

EID: 84896534505     PISSN: 15499596     EISSN: 1549960X     Source Type: Journal    
DOI: 10.1021/ci400457v     Document Type: Article
Times cited : (24)

References (71)
  • 1
    • 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.; Sawyers, C. L. Clinical resistance to STI-571 cancer therapy caused by BCR-ABL gene mutation or amplification Science 2001, 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
  • 4
    • 84862882308 scopus 로고    scopus 로고
    • A molecular dynamics investigation on the crizotinib resistance mechanism of C1156Y mutation in ALK
    • Sun, H. Y.; Ji, F. Q. A molecular dynamics investigation on the crizotinib resistance mechanism of C1156Y mutation in ALK Biochem. Biophys. Res. Commun. 2012, 423, 319-324
    • (2012) Biochem. Biophys. Res. Commun. , vol.423 , pp. 319-324
    • Sun, H.Y.1    Ji, F.Q.2
  • 5
    • 84884570151 scopus 로고    scopus 로고
    • Insight into crizotinib resistance mechanisms caused by three mutations in ALK tyrosine kinase using free energy calculation approaches
    • Sun, H.; Li, Y.; Li, D.; Hou, T. Insight into crizotinib resistance mechanisms caused by three mutations in ALK tyrosine kinase using free energy calculation approaches J. Chem. Inf. Model. 2013, 53, 2376-2389
    • (2013) J. Chem. Inf. Model. , vol.53 , pp. 2376-2389
    • Sun, H.1    Li, Y.2    Li, D.3    Hou, T.4
  • 7
    • 84874688353 scopus 로고    scopus 로고
    • The promiscuous binding of pharmaceutical drugs and their transporter-mediated uptake into cells: What we (need to) know and how we can do so
    • Kell, D. B.; Dobson, P. D.; Bilsland, E.; Oliver, S. G. The promiscuous binding of pharmaceutical drugs and their transporter-mediated uptake into cells: What we (need to) know and how we can do so Drug Discovery Today 2013, 18, 218-239
    • (2013) Drug Discovery Today , vol.18 , pp. 218-239
    • Kell, D.B.1    Dobson, P.D.2    Bilsland, E.3    Oliver, S.G.4
  • 9
    • 0037421590 scopus 로고    scopus 로고
    • Pharmacogenomics - Drug disposition, drug targets, and side effects
    • Wood, A. J. J.; Evans, W. E.; McLeod, H. L. Pharmacogenomics-Drug disposition, drug targets, and side effects N. Engl. J. Med. 2003, 348, 538-549
    • (2003) N. Engl. J. Med. , vol.348 , pp. 538-549
    • Wood, A.J.J.1    Evans, W.E.2    McLeod, H.L.3
  • 10
    • 84859267371 scopus 로고    scopus 로고
    • Therapeutic target database update 2012: A resource for facilitating target-oriented drug discovery
    • Zhu, F.; Shi, Z.; Qin, C.; Tao, L.; Liu, X.; Xu, F.; Zhang, L.; Song, Y.; Zhang, J. Therapeutic target database update 2012: A resource for facilitating target-oriented drug discovery Nucleic Acids. Res. 2012, 40, 1128-1136
    • (2012) Nucleic Acids. Res. , vol.40 , pp. 1128-1136
    • Zhu, F.1    Shi, Z.2    Qin, C.3    Tao, L.4    Liu, X.5    Xu, F.6    Zhang, L.7    Song, Y.8    Zhang, J.9
  • 15
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • Morris, G. M.; Goodsell, D. S.; Halliday, R. S.; Huey, R.; Hart, W. E.; Belew, R. K.; Olson, A. J. Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function J. Comput. Chem. 1998, 19, 1639-1662
    • (1998) J. Comput. Chem. , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 16
    • 49149147973 scopus 로고
    • Iterative partial equalization of orbital electronegativity - A rapid access to atomic charges
    • Gasteiger, J.; Marsili, M. Iterative partial equalization of orbital electronegativity-a rapid access to atomic charges Tetrahedron 1980, 36, 3219-3228
    • (1980) Tetrahedron , vol.36 , pp. 3219-3228
    • Gasteiger, J.1    Marsili, M.2
  • 18
    • 3042524904 scopus 로고
    • A well-behaved electrostatic potential based method using charge restraints for deriving atomic charges: The RESP model
    • Bayly, C. I.; Cieplak, P.; Cornell, W.; Kollman, P. A. A well-behaved electrostatic potential based method using charge restraints for deriving atomic charges: The RESP model J. Phys. Chem. 1993, 97, 10269-10280
    • (1993) J. Phys. Chem. , vol.97 , pp. 10269-10280
    • Bayly, C.I.1    Cieplak, P.2    Cornell, W.3    Kollman, P.A.4
  • 19
    • 0001398008 scopus 로고    scopus 로고
    • How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules?
    • Wang, J.; Cieplak, P.; Kollman, P. A. How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules? J. Comput. Chem. 2000, 21, 1049-1074
    • (2000) J. Comput. Chem. , vol.21 , pp. 1049-1074
    • Wang, J.1    Cieplak, P.2    Kollman, P.A.3
  • 21
    • 84865722478 scopus 로고    scopus 로고
    • GAFFlipid: A General Amber Force Field for the accurate molecular dynamics simulation of phospholipid
    • Dickson, C. J.; Rosso, L.; Betz, R. M.; Walker, R. C.; Gould, I. R. GAFFlipid: A General Amber Force Field for the accurate molecular dynamics simulation of phospholipid Soft Matter 2012, 8, 9617-9627
    • (2012) Soft Matter , vol.8 , pp. 9617-9627
    • Dickson, C.J.1    Rosso, L.2    Betz, R.M.3    Walker, R.C.4    Gould, I.R.5
  • 24
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N log(N) method for Ewald sums in large systems
    • Darden, T.; York, D.; Pedersen, L. Particle mesh Ewald: An N log(N) method for Ewald sums in large systems J. Chem. Phys. 1993, 98, 10089-10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 25
    • 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.; Berendsen, H. J. C. Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes J. Comput. Phys. 1977, 23, 327-341
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 26
    • 36449007836 scopus 로고
    • Constant-pressure molecular-dynamics simulation-The Langevin piston method
    • Feller, S. E.; Zhang, Y.; Pastor, R. W.; Brooks, B. R. Constant-pressure molecular-dynamics simulation-the Langevin piston method J. Chem. Phys. 1995, 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
  • 27
    • 84860635411 scopus 로고    scopus 로고
    • Characterization of domain-peptide interaction interface: Prediction of SH3 domain-mediated protein-protein interaction network in yeast by generic structure-based models
    • Hou, T.; Li, N.; Li, Y.; Wang, W. Characterization of domain-peptide interaction interface: Prediction of SH3 domain-mediated protein-protein interaction network in yeast by generic structure-based models J. Proteome Res. 2012, 11, 2982-2995
    • (2012) J. Proteome Res. , vol.11 , pp. 2982-2995
    • Hou, T.1    Li, N.2    Li, Y.3    Wang, W.4
  • 28
    • 79959405623 scopus 로고    scopus 로고
    • Prediction of peptides binding to the PKA RIIα subunit using a hierarchical strategy
    • Hou, T.; Li, Y.; Wang, W. Prediction of peptides binding to the PKA RIIα subunit using a hierarchical strategy Bioinformatics 2011, 27, 1814-1821
    • (2011) Bioinformatics , vol.27 , pp. 1814-1821
    • Hou, T.1    Li, Y.2    Wang, W.3
  • 29
    • 79952588669 scopus 로고    scopus 로고
    • Assessing the performance of the MM/PBSA and MM/GBSA methods: I. The accuracy of binding free energy calculations based on molecular dynamics simulations
    • Hou, T.; Wang, J.; Li, Y.; Wang, W. Assessing the performance of the MM/PBSA and MM/GBSA methods: I. The accuracy of binding free energy calculations based on molecular dynamics simulations J. Chem. Inf. Model. 2011, 51, 69-82
    • (2011) J. Chem. Inf. Model. , vol.51 , pp. 69-82
    • Hou, T.1    Wang, J.2    Li, Y.3    Wang, W.4
  • 30
    • 79951996670 scopus 로고    scopus 로고
    • Assessing the performance of the molecular mechanics/Poisson Boltzmann surface area and molecular mechanics/generalized Born surface area methods. II. The accuracy of ranking poses generated from docking
    • Hou, T.; Wang, J.; Li, Y.; Wang, W. Assessing the performance of the molecular mechanics/Poisson Boltzmann surface area and molecular mechanics/generalized Born surface area methods. II. The accuracy of ranking poses generated from docking J. Comput. Chem. 2011, 32, 866-877
    • (2011) J. Comput. Chem. , vol.32 , pp. 866-877
    • Hou, T.1    Wang, J.2    Li, Y.3    Wang, W.4
  • 31
    • 33947644064 scopus 로고    scopus 로고
    • Molecular dynamics and free energy studies on the wild-type and double mutant HIV-1 protease complexed with amprenavir and two amprenavir-related inhibitors: Mechanism for binding and drug resistance
    • Hou, T.; Yu, R. Molecular dynamics and free energy studies on the wild-type and double mutant HIV-1 protease complexed with amprenavir and two amprenavir-related inhibitors: mechanism for binding and drug resistance J. Med. Chem. 2007, 50, 1177-1188
    • (2007) J. Med. Chem. , vol.50 , pp. 1177-1188
    • Hou, T.1    Yu, R.2
  • 32
    • 84867759741 scopus 로고    scopus 로고
    • Theoretical studies on the susceptibility of oseltamivir against variants of 2009 A/H1N1 influenza neuraminidase
    • Li, L.; Li, Y.; Zhang, L.; Hou, T. Theoretical studies on the susceptibility of oseltamivir against variants of 2009 A/H1N1 influenza neuraminidase J. Chem. Inf. Model. 2012, 52, 2715-2729
    • (2012) J. Chem. Inf. Model. , vol.52 , pp. 2715-2729
    • Li, L.1    Li, Y.2    Zhang, L.3    Hou, T.4
  • 33
    • 84880541805 scopus 로고    scopus 로고
    • Assessing the performance of MM/PBSA and MM/GBSA methods. 3. The impact of force fields and ligand charge models
    • Xu, L.; Sun, H.; Li, Y.; Wang, J.; Hou, T. Assessing the performance of MM/PBSA and MM/GBSA methods. 3. The impact of force fields and ligand charge models J. Phys. Chem. B 2013, 117, 8408-8421
    • (2013) J. Phys. Chem. B , vol.117 , pp. 8408-8421
    • Xu, L.1    Sun, H.2    Li, Y.3    Wang, J.4    Hou, T.5
  • 34
    • 84873025050 scopus 로고    scopus 로고
    • Exploring the molecular mechanism of cross-resistance to HIV-1 integrase strand transfer inhibitors by molecular dynamics simulation and residue interaction network analysis
    • Xue, W.; Jin, X.; Ning, L.; Wang, M.; Liu, H.; Yao, X. Exploring the molecular mechanism of cross-resistance to HIV-1 integrase strand transfer inhibitors by molecular dynamics simulation and residue interaction network analysis J. Chem. Inf. Model. 2013, 53, 210-222
    • (2013) J. Chem. Inf. Model. , vol.53 , pp. 210-222
    • Xue, W.1    Jin, X.2    Ning, L.3    Wang, M.4    Liu, H.5    Yao, X.6
  • 35
    • 76549102880 scopus 로고    scopus 로고
    • Detecting and understanding combinatorial mutation patterns responsible for HIV drug resistance
    • Zhang, J.; Hou, T.; Wang, W.; Liu, J. S. Detecting and understanding combinatorial mutation patterns responsible for HIV drug resistance Proc. Natl. Acad. Sci. U.S.A. 2010, 107, 1321-1326
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 1321-1326
    • Zhang, J.1    Hou, T.2    Wang, W.3    Liu, J.S.4
  • 36
    • 1842479952 scopus 로고    scopus 로고
    • Exploring protein native states and large-scale conformational changes with a modified generalized born model
    • Onufriev, A.; Bashford, D.; Case, D. A. Exploring protein native states and large-scale conformational changes with a modified generalized born model Proteins: Struct., Funct., Bioinf. 2004, 55, 383-394
    • (2004) Proteins: Struct., Funct., Bioinf. , vol.55 , pp. 383-394
    • Onufriev, A.1    Bashford, D.2    Case, D.A.3
  • 37
    • 0000408363 scopus 로고    scopus 로고
    • Approximate atomic surfaces from linear combinations of pairwise overlaps (LCPO)
    • Weiser, J.; Shenkin, P. S.; Still, W. C. Approximate atomic surfaces from linear combinations of pairwise overlaps (LCPO) J. Comput. Chem. 1999, 20, 217-230
    • (1999) J. Comput. Chem. , vol.20 , pp. 217-230
    • Weiser, J.1    Shenkin, P.S.2    Still, W.C.3
  • 38
    • 0000991642 scopus 로고
    • Harmonic dynamics of proteins: Normal modes and fluctuations in bovine pancreatic trypsin inhibitor
    • Brooks, B.; Karplus, M. Harmonic dynamics of proteins: Normal modes and fluctuations in bovine pancreatic trypsin inhibitor Proc. Natl. Acad. Sci. U.S.A. 1983, 80, 6571-6575
    • (1983) Proc. Natl. Acad. Sci. U.S.A. , vol.80 , pp. 6571-6575
    • Brooks, B.1    Karplus, M.2
  • 39
    • 84865511407 scopus 로고    scopus 로고
    • The normal-mode entropy in the MM/GBSA method: Effect of system truncation, buffer region, and dielectric constant
    • Genheden, S.; Kuhn, O.; Mikulskis, P.; Hoffmann, D.; Ryde, U. The normal-mode entropy in the MM/GBSA method: Effect of system truncation, buffer region, and dielectric constant J. Chem. Inf. Model. 2012, 52, 2079-2088
    • (2012) J. Chem. Inf. Model. , vol.52 , pp. 2079-2088
    • Genheden, S.1    Kuhn, O.2    Mikulskis, P.3    Hoffmann, D.4    Ryde, U.5
  • 44
    • 84875346781 scopus 로고    scopus 로고
    • Proteome-wide analysis of nonsynonymous single-nucleotide variations in active sites of human proteins
    • Dingerdissen, H.; Motwani, M.; Karagiannis, K.; Simonyan, V.; Mazumder, R. Proteome-wide analysis of nonsynonymous single-nucleotide variations in active sites of human proteins FEBS J. 2013, 280, 1542-1562
    • (2013) FEBS J. , vol.280 , pp. 1542-1562
    • Dingerdissen, H.1    Motwani, M.2    Karagiannis, K.3    Simonyan, V.4    Mazumder, R.5
  • 45
    • 0037763817 scopus 로고    scopus 로고
    • Comparative evaluation of 11 scoring functions for molecular docking
    • Wang, R.; Lu, Y.; Wang, S. Comparative evaluation of 11 scoring functions for molecular docking J. Med. Chem. 2003, 46, 2287-2303
    • (2003) J. Med. Chem. , vol.46 , pp. 2287-2303
    • Wang, R.1    Lu, Y.2    Wang, S.3
  • 46
    • 84873047397 scopus 로고    scopus 로고
    • How to improve docking accuracy of AutoDock4.2: A case study using different electrostatic potentials
    • Hou, x.; Du, J.; Zhang, J.; Du, L.; Fang, H.; Li, M. How to improve docking accuracy of AutoDock4.2: A case study using different electrostatic potentials J. Chem. Inf. Model. 2013, 53, 188-200
    • (2013) J. Chem. Inf. Model. , vol.53 , pp. 188-200
    • Hou, X.1    Du, J.2    Zhang, J.3    Du, L.4    Fang, H.5    Li, M.6
  • 47
    • 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.; Eck, M. J. Structures of lung cancer-derived EGFR mutants and inhibitor complexes: mechanism of activation and insights into differential inhibitor sensitivity Cancer cell 2007, 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
  • 48
    • 69749120935 scopus 로고    scopus 로고
    • Quantitative prediction of fold resistance for inhibitors of EGFR
    • Balius, T. E.; Rizzo, R. C. Quantitative prediction of fold resistance for inhibitors of EGFR Biochemistry 2009, 48, 8435-8448
    • (2009) Biochemistry , vol.48 , pp. 8435-8448
    • Balius, T.E.1    Rizzo, R.C.2
  • 49
    • 0029073127 scopus 로고
    • Specific mutations in the estrogen receptor change the properties of antiestrogens to full agonists
    • Mahfoudi, A.; Roulet, E.; Dauvois, S.; Parker, M. G.; Wahli, W. Specific mutations in the estrogen receptor change the properties of antiestrogens to full agonists Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 4206-4210
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 4206-4210
    • Mahfoudi, A.1    Roulet, E.2    Dauvois, S.3    Parker, M.G.4    Wahli, W.5
  • 50
    • 0028831226 scopus 로고
    • Mutation of an arginine residue in the human glycine receptor transforms β-alanine and taurine from agonists into competitive antagonists
    • Rajendra, S.; Lynch, J. W.; Pierce, K. D.; French, C. R.; Barry, P. H.; Schofield, P. R. Mutation of an arginine residue in the human glycine receptor transforms β-alanine and taurine from agonists into competitive antagonists Neuron 1995, 14, 169-175
    • (1995) Neuron , vol.14 , pp. 169-175
    • Rajendra, S.1    Lynch, J.W.2    Pierce, K.D.3    French, C.R.4    Barry, P.H.5    Schofield, P.R.6
  • 51
    • 0029836349 scopus 로고    scopus 로고
    • Myocardial signaling defects and impaired cardiac function of a human beta 2-adrenergic receptor polymorphism expressed in transgenic mice
    • Turki, J.; Lorenz, J. N.; Green, S. A.; Donnelly, E. T.; Jacinto, M.; Liggett, S. B. Myocardial signaling defects and impaired cardiac function of a human beta 2-adrenergic receptor polymorphism expressed in transgenic mice Proc. Natl. Acad. Sci. U.S.A. 1996, 93, 10483-10488
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 10483-10488
    • Turki, J.1    Lorenz, J.N.2    Green, S.A.3    Donnelly, E.T.4    Jacinto, M.5    Liggett, S.B.6
  • 52
    • 0037143619 scopus 로고    scopus 로고
    • Closure of the Venus flytrap module of mGlu8 receptor and the activation process: Insights from mutations converting antagonists into agonists
    • Bessis, A.-S.; Rondard, P.; Gaven, F.; Brabet, I.; Triballeau, N.; Prézeau, L.; Acher, F.; Pin, J.-P. Closure of the Venus flytrap module of mGlu8 receptor and the activation process: Insights from mutations converting antagonists into agonists Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 11097-11102
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 11097-11102
    • Bessis, A.-S.1    Rondard, P.2    Gaven, F.3    Brabet, I.4    Triballeau, N.5    Prézeau, L.6    Acher, F.7    Pin, J.-P.8
  • 53
    • 4143117785 scopus 로고    scopus 로고
    • Beta2-adrenoceptor Thr164Ile polymorphism is associated with markedly decreased vasodilator and increased vasoconstrictor sensitivity in vivo
    • Dishy, V.; Landau, R.; Sofowora, G. G.; Xie, H.-G.; Smiley, R. M.; Kim, R. B.; Byrne, D. W.; Wood, A. J.; Stein, C. M. Beta2-adrenoceptor Thr164Ile polymorphism is associated with markedly decreased vasodilator and increased vasoconstrictor sensitivity in vivo Pharmacogenetics 2004, 14, 517-522
    • (2004) Pharmacogenetics , vol.14 , pp. 517-522
    • Dishy, V.1    Landau, R.2    Sofowora, G.G.3    Xie, H.-G.4    Smiley, R.M.5    Kim, R.B.6    Byrne, D.W.7    Wood, A.J.8    Stein, C.M.9
  • 54
    • 0036188425 scopus 로고    scopus 로고
    • Naturally occurring mutation, Asp70His, in human butyrylcholinesterase
    • Boeck, A. T.; Fry, D. L.; Sastre, A.; Lockridge, O. Naturally occurring mutation, Asp70His, in human butyrylcholinesterase Ann. Clin. Biochem. 2002, 39, 154-156
    • (2002) Ann. Clin. Biochem. , vol.39 , pp. 154-156
    • Boeck, A.T.1    Fry, D.L.2    Sastre, A.3    Lockridge, O.4
  • 55
    • 0030764030 scopus 로고    scopus 로고
    • Importance of aspartate-70 in organophosphate inhibition, oxime re-activation and aging of human butyrylcholinesterase
    • Masson, P.; Froment, M.; Bartels, C.; Lockridge, O. Importance of aspartate-70 in organophosphate inhibition, oxime re-activation and aging of human butyrylcholinesterase Biochem. J. 1997, 325, 53-61
    • (1997) Biochem. J. , vol.325 , pp. 53-61
    • Masson, P.1    Froment, M.2    Bartels, C.3    Lockridge, O.4
  • 57
    • 13444266370 scopus 로고    scopus 로고
    • Online Mendelian Inheritance in Man (OMIM), a knowledgebase of human genes and genetic disorders
    • Hamosh, A.; Scott, A. F.; Amberger, J. S.; Bocchini, C. A.; McKusick, V. A. Online Mendelian Inheritance in Man (OMIM), a knowledgebase of human genes and genetic disorders Nucleic Acids. Res. 2005, 33, 514-517
    • (2005) Nucleic Acids. Res. , vol.33 , pp. 514-517
    • Hamosh, A.1    Scott, A.F.2    Amberger, J.S.3    Bocchini, C.A.4    McKusick, V.A.5
  • 58
    • 33645127443 scopus 로고    scopus 로고
    • Genetic medicines: Treatment strategies for hereditary disorders
    • O'Connor, T. P.; Crystal, R. G. Genetic medicines: Treatment strategies for hereditary disorders Nat. Rev. Genet. 2006, 7, 261-276
    • (2006) Nat. Rev. Genet. , vol.7 , pp. 261-276
    • O'Connor, T.P.1    Crystal, R.G.2
  • 59
    • 44849140430 scopus 로고    scopus 로고
    • Gene therapy of inherited diseases
    • Fischer, A.; Cavazzana-Calvo, M. Gene therapy of inherited diseases Lancet 2008, 371, 2044-2047
    • (2008) Lancet , vol.371 , pp. 2044-2047
    • Fischer, A.1    Cavazzana-Calvo, M.2
  • 60
    • 84859326107 scopus 로고    scopus 로고
    • Rare diseases and orphan drugs
    • Melnikova, I. Rare diseases and orphan drugs Nat. Rev. Drug Discovery 2012, 11, 267-268
    • (2012) Nat. Rev. Drug Discovery , vol.11 , pp. 267-268
    • Melnikova, I.1
  • 64
    • 0041629450 scopus 로고    scopus 로고
    • Status of epidermal growth factor receptor antagonists in the biology and treatment of cancer
    • Mendelsohn, J.; Baselga, J. Status of epidermal growth factor receptor antagonists in the biology and treatment of cancer J. Clin. Oncol. 2003, 21, 2787-2799
    • (2003) J. Clin. Oncol. , vol.21 , pp. 2787-2799
    • Mendelsohn, J.1    Baselga, J.2
  • 65
    • 84865184491 scopus 로고    scopus 로고
    • Phase II study of gefitinib adaptive dose escalation to skin toxicity in recurrent or metastatic squamous cell carcinoma of the head and neck
    • Perez, C. A.; Song, H.; Raez, L. E.; Agulnik, M.; Grushko, T. A.; Dekker, A.; Stenson, K.; Blair, E. A.; Olopade, O. I.; Seiwert, T. Y. Phase II study of gefitinib adaptive dose escalation to skin toxicity in recurrent or metastatic squamous cell carcinoma of the head and neck Oral Oncol. 2012, 48, 887-892
    • (2012) Oral Oncol. , vol.48 , pp. 887-892
    • Perez, C.A.1    Song, H.2    Raez, L.E.3    Agulnik, M.4    Grushko, T.A.5    Dekker, A.6    Stenson, K.7    Blair, E.A.8    Olopade, O.I.9    Seiwert, T.Y.10
  • 66
    • 0037674062 scopus 로고    scopus 로고
    • Phase II trial of ZD1839 in recurrent or metastatic squamous cell carcinoma of the head and neck
    • Cohen, E. E.; Rosen, F.; Stadler, W. M.; Recant, W.; Stenson, K.; Huo, D.; Vokes, E. E. Phase II trial of ZD1839 in recurrent or metastatic squamous cell carcinoma of the head and neck J. Clin. Oncol. 2003, 21, 1980-1987
    • (2003) J. Clin. Oncol. , vol.21 , pp. 1980-1987
    • Cohen, E.E.1    Rosen, F.2    Stadler, W.M.3    Recant, W.4    Stenson, K.5    Huo, D.6    Vokes, E.E.7
  • 68
    • 85027926988 scopus 로고    scopus 로고
    • BIM induction of apoptosis triggered by EGFR-sensitive and resistance cell lines of non-small-cell lung cancer
    • Li, Z.; Zhou, S.; Zhang, L.; Su, C.; Hang, J.; Zhao, Y.; Su, B.; Zhou, C. BIM induction of apoptosis triggered by EGFR-sensitive and resistance cell lines of non-small-cell lung cancer Med. Oncol. 2011, 28, 572-577
    • (2011) Med. Oncol. , vol.28 , pp. 572-577
    • Li, Z.1    Zhou, S.2    Zhang, L.3    Su, C.4    Hang, J.5    Zhao, Y.6    Su, B.7    Zhou, C.8
  • 69
    • 0037109014 scopus 로고    scopus 로고
    • ZD1839 (Iressa) an orally active inhibitor of epidermal growth factor signaling with potential for cancer therapy
    • Wakeling, A. E.; Guy, S. P.; Woodburn, J. R.; Ashton, S. E.; Curry, B. J.; Barker, A. J.; Gibson, K. H. ZD1839 (Iressa) an orally active inhibitor of epidermal growth factor signaling with potential for cancer therapy Cancer Res. 2002, 62, 5749-5754
    • (2002) Cancer Res. , vol.62 , pp. 5749-5754
    • Wakeling, A.E.1    Guy, S.P.2    Woodburn, J.R.3    Ashton, S.E.4    Curry, B.J.5    Barker, A.J.6    Gibson, K.H.7
  • 70
    • 20644433937 scopus 로고    scopus 로고
    • Establishment of a human non-small cell lung cancer cell line resistant to gefitinib
    • Koizumi, F.; Shimoyama, T.; Taguchi, F.; Saijo, N.; Nishio, K. Establishment of a human non-small cell lung cancer cell line resistant to gefitinib Int. J. Cancer 2005, 116, 36-44
    • (2005) Int. J. Cancer , vol.116 , pp. 36-44
    • Koizumi, F.1    Shimoyama, T.2    Taguchi, F.3    Saijo, N.4    Nishio, K.5
  • 71
    • 78651540936 scopus 로고    scopus 로고
    • Molecular mechanism of the schedule-dependent synergistic interaction in EGFR-mutant non-small cell lung cancer cell lines treated with paclitaxel and gefitinib
    • Cheng, H.; An, S. J.; Dong, S.; Zhang, Y. F.; Zhang, X. C.; Chen, Z. H.; Su, J.; Wu, Y. L. Molecular mechanism of the schedule-dependent synergistic interaction in EGFR-mutant non-small cell lung cancer cell lines treated with paclitaxel and gefitinib J. Hematol. Oncol. 2011, 4, 5-17
    • (2011) J. Hematol. Oncol. , vol.4 , pp. 5-17
    • Cheng, H.1    An, S.J.2    Dong, S.3    Zhang, Y.F.4    Zhang, X.C.5    Chen, Z.H.6    Su, J.7    Wu, Y.L.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.