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Volumn 3, Issue 1, 2011, Pages

Prediction of cyclin-dependent kinase 2 inhibitor potency using the fragment molecular orbital method

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EID: 79751471221     PISSN: None     EISSN: 17582946     Source Type: Journal    
DOI: 10.1186/1758-2946-3-2     Document Type: Article
Times cited : (105)

References (88)
  • 1
    • 1642357706 scopus 로고    scopus 로고
    • The Many Roles of Computation in Drug Discovery
    • DOI 10.1126/science.1096361
    • The Many Roles of Computation in Drug Discovery. WL Jorgensen, Science 2004 303 1813 (Pubitemid 38374866)
    • (2004) Science , vol.303 , Issue.5665 , pp. 1813-1818
    • Jorgensen, W.L.1
  • 4
    • 1642540577 scopus 로고    scopus 로고
    • Evaluation of Docking Performance: Comparative Data on Docking Algorithms
    • DOI 10.1021/jm0302997
    • Evaluation of Docking Performance: Comparative Data on Docking Algorithms. M Kontoyianni LM McClellan GS Sokol, J Med Chem 2004 47 558 565 10.1021/jm0302997 14736237 (Pubitemid 38129714)
    • (2004) Journal of Medicinal Chemistry , vol.47 , Issue.3 , pp. 558-565
    • Kontoyianni, M.1    McClellan, L.M.2    Sokol, G.S.3
  • 5
    • 0035966871 scopus 로고    scopus 로고
    • Detailed analysis of scoring functions for virtual screening
    • DOI 10.1021/jm0003992
    • Detailed Analysis of Scoring Functions for Virtual Screening. M Stahl M Rarey, J Med Chem 2001 44 1035 1042 10.1021/jm0003992 11297450 (Pubitemid 32852130)
    • (2001) Journal of Medicinal Chemistry , vol.44 , Issue.7 , pp. 1035-1042
    • Stahl, M.1    Rarey, M.2
  • 7
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
    • 19499576
    • AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. O Trott AJ Olson, J Comput Chem 2010 31 455 461 19499576
    • (2010) J Comput Chem , vol.31 , pp. 455-461
    • Trott, O.1    Olson, A.J.2
  • 8
    • 0037008160 scopus 로고    scopus 로고
    • Approaches to the Description and Prediction of the Binding Affinity of Small-Molecule Ligands to Macromolecular Receptors
    • 10.1002/1521-3773(20020802)41:15<2644::AID-ANIE2644>3.0.CO;2-O
    • Approaches to the Description and Prediction of the Binding Affinity of Small-Molecule Ligands to Macromolecular Receptors. H Gohlke G Klebe, Angew Chem Int Edit 2002 41 2644 2676 10.1002/1521-3773(20020802)41:15<2644::AID- ANIE2644>3.0.CO;2-O
    • (2002) Angew Chem Int Edit , vol.41 , pp. 2644-2676
    • Gohlke, H.1    Klebe, G.2
  • 9
    • 0024578173 scopus 로고
    • Free Energy Via Molecular Simulation: Applications to Chemical and Biomolecular Systems
    • 10.1146/annurev.biophys.18.1.431
    • Free Energy Via Molecular Simulation: Applications to Chemical and Biomolecular Systems. DL Beveridge FM DiCapua, Annu Rev Biophys Bio 1989 18 431 492 10.1146/annurev.biophys.18.1.431
    • (1989) Annu Rev Biophys Bio , vol.18 , pp. 431-492
    • Beveridge, D.L.1    Dicapua, F.M.2
  • 10
    • 0031637651 scopus 로고    scopus 로고
    • Ligand binding affinity prediction by linear interaction energy methods
    • Ligand binding affinity prediction by linear interaction energy methods. T Hansson J Marelius J qvist, J Comput Aided Mol Des 1998 12 27 35 10.1023/A:1007930623000 9570087 (Pubitemid 128513811)
    • (1998) Journal of Computer-Aided Molecular Design , vol.12 , Issue.1 , pp. 27-35
    • Hansson, T.1    Marelius, J.2    Aqvist, J.3
  • 11
    • 0342321950 scopus 로고    scopus 로고
    • Examining methods for calculations of binding free energies: LRA, LIE, PDLD-LRA, and PDLD/S-LRA calculations of ligands binding to an HIV protease
    • Examining Methods for Calculations of Binding Free Energies: LRA, LIE, PDLD-LRA, and PDLD/S-LRA Calculations of Ligands Binding to an HIV Protease. YY Sham Z-T Chu H Tao A Warshel, Proteins: Struct, Funct, Genet 2000 39 393 407 10.1002/(SICI)1097-0134(20000601)39:4<393::AID-PROT120>3.0.CO;2-H (Pubitemid 30414177)
    • (2000) Proteins: Structure, Function and Genetics , vol.39 , Issue.4 , pp. 393-407
    • Sham, Y.Y.1    Chu, Z.T.2    Tao, H.3    Warshel, A.4
  • 12
    • 0026596911 scopus 로고
    • Calculations of antibody-antigen interactions: Microscopic and semi-microscopic evaluation of free energies of binding of phosphorylcholine analogs to McPC603
    • 10.1093/protein/5.3.215. 1409541
    • Calculations of antibody-antigen interactions: microscopic and semi-microscopic evaluation of free energies of binding of phosphorylcholine analogs to McPC603. FS Lee Z-T Chu MB Bolger A Warshel, Protein Eng 1992 5 215 228 10.1093/protein/5.3.215 1409541
    • (1992) Protein Eng , vol.5 , pp. 215-228
    • Lee, F.S.1    Chu, Z.-T.2    Bolger, M.B.3    Warshel, A.4
  • 15
    • 78751641417 scopus 로고    scopus 로고
    • Protein-protein interactions from linear-scaling first-principles quantum-mechanical calculations
    • 10.1209/0295-5075/91/37004
    • Protein-protein interactions from linear-scaling first-principles quantum-mechanical calculations. DJ Cole C-K Skylaris E Rajendra AR Venkitaraman MC Payne, EPL 2010 91 37004 10.1209/0295-5075/91/37004
    • (2010) EPL , vol.91 , pp. 37004
    • Cole, D.J.1    Skylaris, C.-K.2    Rajendra, E.3    Venkitaraman, A.R.4    Payne, M.C.5
  • 16
    • 20444377245 scopus 로고    scopus 로고
    • Validation and use of the MM-PBSA approach for drug discovery
    • DOI 10.1021/jm049081q
    • Validation and Use of the MM-PBSA Approach for Drug Discovery. B Kuhn P Gerber T Schulz-Gasch M Stahl, J Med Chem 2005 48 4040 4048 10.1021/jm049081q 15943477 (Pubitemid 40800612)
    • (2005) Journal of Medicinal Chemistry , vol.48 , Issue.12 , pp. 4040-4048
    • Kuhn, B.1    Gerber, P.2    Schulz-Gasch, T.3    Stahl, M.4
  • 17
    • 76249112547 scopus 로고    scopus 로고
    • Fast and accurate predictions of binding free energies using MM-PBSA and MM-GBSA
    • 19569205
    • Fast and accurate predictions of binding free energies using MM-PBSA and MM-GBSA. G Rastelli AD Rio G Degliesposti M Sgobba, J Comput Chem 2010 31 797 810 19569205
    • (2010) J Comput Chem , vol.31 , pp. 797-810
    • Rastelli, G.1    Rio, A.D.2    Degliesposti, G.3    Sgobba, M.4
  • 18
    • 33645400172 scopus 로고    scopus 로고
    • A Multistep Approach to Structure-Based Drug Design:? Studying Ligand Binding at the Human Neutrophil Elastase
    • 10.1021/jm0505720. 16539369
    • A Multistep Approach to Structure-Based Drug Design:? Studying Ligand Binding at the Human Neutrophil Elastase. T Steinbrecher DA Case A Labahn, J Med Chem 2006 49 1837 1844 10.1021/jm0505720 16539369
    • (2006) J Med Chem , vol.49 , pp. 1837-1844
    • Steinbrecher, T.1    Case, D.A.2    Labahn, A.3
  • 19
    • 84961980685 scopus 로고    scopus 로고
    • Binding of a Diverse Set of Ligands to Avidin and Streptavidin: An Accurate Quantitative Prediction of Their Relative Affinities by a Combination of Molecular Mechanics and Continuum Solvent Models
    • 10.1021/jm000241h. 11020294
    • Binding of a Diverse Set of Ligands to Avidin and Streptavidin: An Accurate Quantitative Prediction of Their Relative Affinities by a Combination of Molecular Mechanics and Continuum Solvent Models. B Kuhn PA Kollman, J Med Chem 2000 43 3786 3791 10.1021/jm000241h 11020294
    • (2000) J Med Chem , vol.43 , pp. 3786-3791
    • Kuhn, B.1    Kollman, P.A.2
  • 20
    • 0035846166 scopus 로고    scopus 로고
    • Are free energy calculations useful in practice? A comparison with rapid scoring functions for the p38 MAP kinase protein system
    • DOI 10.1021/jm0100279
    • Are Free Energy Calculations Useful in Practice? A Comparison with Rapid Scoring Functions for the p38 MAP Kinase Protein System. DA Pearlman PS Charifson, J Med Chem 2001 44 3417 3423 10.1021/jm0100279 11585447 (Pubitemid 32947908)
    • (2001) Journal of Medicinal Chemistry , vol.44 , Issue.21 , pp. 3417-3423
    • Pearlman, D.A.1    Charifson, P.S.2
  • 21
    • 0029745052 scopus 로고    scopus 로고
    • Cation-π interactions in aromatics of biological and medicinal interest: Electrostatic potential surfaces as a useful qualitative guide
    • DOI 10.1073/pnas.93.20.10566
    • Cation-pi interactions in aromatics of biological and medicinal interest: electrostatic potential surfaces as a useful qualitative guide. P Mecozzi AP West Jr DA Dougherty, Proc Natl Acad Sci USA 1996 93 10566 10571 10.1073/pnas.93.20.10566 8855218 (Pubitemid 26333027)
    • (1996) Proceedings of the National Academy of Sciences of the United States of America , vol.93 , Issue.20 , pp. 10566-10571
    • Mecozzi, S.1    West Jr., A.P.2    Dougherty, D.A.3
  • 22
    • 0033578302 scopus 로고    scopus 로고
    • Cation- interactions in structural biology
    • 10.1073/pnas.96.17.9459. 10449714
    • Cation- interactions in structural biology. JP Gallivan DA Dougherty, Proc Natl Acad Sci USA 1999 96 9459 9464 10.1073/pnas.96.17.9459 10449714
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9459-9464
    • Gallivan, J.P.1    Dougherty, D.A.2
  • 23
    • 0034703739 scopus 로고    scopus 로고
    • Origin of the Attraction and Directionality of the NH/p Interaction:? Comparison with OH/p and CH/p Interactions
    • 10.1021/ja001901a
    • Origin of the Attraction and Directionality of the NH/p Interaction:? Comparison with OH/p and CH/p Interactions. S Tsuzuki K Honda T Uchimaru M Mikami K Tanabe, J Am Chem Soc 2000 122 11450 11458 10.1021/ja001901a
    • (2000) J Am Chem Soc , vol.122 , pp. 11450-11458
    • Tsuzuki, S.1    Honda, K.2    Uchimaru, T.3    Mikami, M.4    Tanabe, K.5
  • 25
    • 65249083371 scopus 로고    scopus 로고
    • On the Nature of Bonding in Lone Pairp-Electron Complexes: CCSD(T)/Complete Basis Set Limit Calculations
    • 10.1021/ct900036y
    • On the Nature of Bonding in Lone Pairp-Electron Complexes: CCSD(T)/Complete Basis Set Limit Calculations. J Ran P Hobza, J Chem Theory Comput 2009 5 1180 1185 10.1021/ct900036y
    • (2009) J Chem Theory Comput , vol.5 , pp. 1180-1185
    • Ran, J.1    Hobza, P.2
  • 26
    • 58149491376 scopus 로고    scopus 로고
    • Quantum Chemical Benchmark Energy and Geometry Database for Molecular Clusters and Complex Molecular Systems: A Users Manual and Examples
    • http://www.begdb.com
    • Quantum Chemical Benchmark Energy and Geometry Database for Molecular Clusters and Complex Molecular Systems: A Users Manual and Examples. J Rezc P Jurecka KE Riley J Cern H Valdes K Pluhckov K Berka T Rezc M Pitonk J Vondrek,, et al. Collect Czech Chem Commun 2008 73 1261 1270 http://www.begdb.com
    • (2008) Collect Czech Chem Commun , vol.73 , pp. 1261-1270
    • Rezc, J.1    Jurecka, P.2    Riley, K.E.3    Cern, J.4    Valdes, H.5    Pluhckov, K.6    Berka, K.7    Rezc, T.8    Pitonk, M.9    Vondrek, J.10
  • 27
    • 34548430376 scopus 로고    scopus 로고
    • The role of quantum mechanics in structure-based drug design
    • DOI 10.1016/j.drudis.2007.07.006, PII S1359644607002723
    • The role of quantum mechanics in structure-based drug design. K Raha MB Peters B Wang N Yu AM Wollacott LM Westerhoff KM Merz Jr, Drug Discov Today 2007 12 725 731 10.1016/j.drudis.2007.07.006 17826685 (Pubitemid 47364833)
    • (2007) Drug Discovery Today , vol.12 , Issue.17-18 , pp. 725-731
    • Raha, K.1    Peters, M.B.2    Wang, B.3    Yu, N.4    Wollacott, A.M.5    Westerhoff, L.M.6    Merz Jr., K.M.7
  • 28
    • 0032833998 scopus 로고    scopus 로고
    • The role of polarization and charge transfer in the solvation of biomolecules
    • DOI 10.1021/ja9912325
    • The Role of Polarization and Charge Transfer in the Solvation of Biomolecules. A van der Vaart KM Merz Jr, J Am Chem Soc 1999 121 9182 9190 10.1021/ja9912325 (Pubitemid 29477385)
    • (1999) Journal of the American Chemical Society , vol.121 , Issue.39 , pp. 9182-9190
    • Van Der Vaart, A.1    Merz Jr., K.M.2
  • 29
    • 22244451417 scopus 로고    scopus 로고
    • Large-Scale validation of a quantum mechanics based scoring function: Predicting the binding affinity and the binding mode of a diverse set of protein-ligand complexes
    • DOI 10.1021/jm048973n
    • Large-Scale Validation of a Quantum Mechanics Based Scoring Function:? Predicting the Binding Affinity and the Binding Mode of a Diverse Set of Protein-Ligand Complexes. K Raha KM Merz Jr, J Med Chem 2005 48 4558 4575 10.1021/jm048973n 15999994 (Pubitemid 40993417)
    • (2005) Journal of Medicinal Chemistry , vol.48 , Issue.14 , pp. 4558-4575
    • Raha, K.1    Merz Jr., K.M.2
  • 30
    • 0000721543 scopus 로고    scopus 로고
    • Fragment molecular orbital method: An approximate computational method for large molecules
    • PII S000926149900874X
    • Fragment molecular orbital method: an approximate computational method for large molecules. K Kitaura E Ikeo T Asada T Nakano M Uebayasi, Chem Phys Lett 1999 313 701 706 10.1016/S0009-2614(99)00874-X (Pubitemid 129556715)
    • (1999) Chemical Physics Letters , vol.313 , Issue.3-4 , pp. 701-706
    • Kitaura, K.1    Ikeo, E.2    Asada, T.3    Nakano, T.4    Uebayasi, M.5
  • 31
    • 26444446031 scopus 로고    scopus 로고
    • Quantum computational analysis for drug resistance of HIV-1 reverse transcriptase to nevirapine through point mutations
    • DOI 10.1002/prot.20578
    • Quantum computational analysis for drug resistance of HIV-1 reverse transcriptase to nevirapine through point mutations. X He Y Mei Y Xiang DW Zhang JZH Zhang, Proteins: Struct, Funct, Bioinf 2005 61 423 432 10.1002/prot.20578 (Pubitemid 41430485)
    • (2005) Proteins: Structure, Function and Genetics , vol.61 , Issue.2 , pp. 423-432
    • He, X.1    Mei, Y.2    Xiang, Y.3    Zhang, D.W.4    Zhang, J.Z.H.5
  • 32
    • 33847088301 scopus 로고
    • The Origin of Hydrogen Bonding. An Energy Decomposition Study
    • 10.1021/ja00447a007
    • The Origin of Hydrogen Bonding. An Energy Decomposition Study. H Umeyama K Morokuma, J Am Chem Soc 1977 99 1316 1332 10.1021/ja00447a007
    • (1977) J Am Chem Soc , vol.99 , pp. 1316-1332
    • Umeyama, H.1    Morokuma, K.2
  • 33
    • 43949164521 scopus 로고
    • Computation of charge-transfer energies by perturbation theory
    • 10.1016/0009-2614(93)80058-W
    • Computation of charge-transfer energies by perturbation theory. AJ Stone, J Chem Phys Lett 1993 211 101 109 10.1016/0009-2614(93)80058-W
    • (1993) J Chem Phys Lett , vol.211 , pp. 101-109
    • Stone, A.J.1
  • 34
    • 0034227821 scopus 로고    scopus 로고
    • A general treatment of solvent effects based on screened Coulomb potentials
    • 10.1021/jp993895e
    • A general treatment of solvent effects based on screened Coulomb potentials. SA Hassan, J Phys Chem B 2000 104 6478 6489 10.1021/jp993895e
    • (2000) J Phys Chem B , vol.104 , pp. 6478-6489
    • Hassan, S.A.1
  • 35
    • 0000121375 scopus 로고    scopus 로고
    • Divide and conquer interaction energy decomposition
    • 10.1021/jp9844967
    • Divide and conquer interaction energy decomposition. A van der Vaart KM Merz Jr, J Phys Chem A 1999 103 3321 3329 10.1021/jp9844967
    • (1999) J Phys Chem A , vol.103 , pp. 3321-3329
    • Van Der Vaart, A.1    Merz Jr., K.M.2
  • 36
    • 33744470857 scopus 로고    scopus 로고
    • Benchmark database of accurate (MP2 and CCSD(T) complete basis set limit) interaction energies of small model complexes, DNA base pairs, and amino acid pairs
    • 10.1039/b600027d. 16633685
    • Benchmark database of accurate (MP2 and CCSD(T) complete basis set limit) interaction energies of small model complexes, DNA base pairs, and amino acid pairs. P Jurecka J poner J Cern P Hobza, Phys Chem Chem Phys 2006 8 1985 1993 10.1039/b600027d 16633685
    • (2006) Phys Chem Chem Phys , vol.8 , pp. 1985-1993
    • Jurecka, P.1    Poner, J.2    Cern, J.3    Hobza, P.4
  • 37
    • 36348986753 scopus 로고    scopus 로고
    • On the accurate reproduction of ab initio interaction energies between an enzyme and substrate
    • DOI 10.1016/j.cplett.2007.10.073, PII S0009261407014455
    • On the accurate reproduction of ab initio interaction energies between an enzyme and substrate. RPA Bettens AM Lee, Chem Phys Lett 2007 449 341 346 10.1016/j.cplett.2007.10.073 (Pubitemid 350160609)
    • (2007) Chemical Physics Letters , vol.449 , Issue.4-6 , pp. 341-346
    • Bettens, R.P.A.1    Lee, A.M.2
  • 38
    • 11144302905 scopus 로고    scopus 로고
    • QMQSAR: Utilization of a semiempirical probe potential in a field-based QSAR method
    • DOI 10.1002/jcc.20142
    • QMQSAR: Utilization of a semiempirical probe potential in a field-based QSAR method. S Dixon KM Merz Jr G Lauri JC Ianni, J Comput Chem 2005 26 23 34 10.1002/jcc.20142 15526326 (Pubitemid 40021620)
    • (2005) Journal of Computational Chemistry , vol.26 , Issue.1 , pp. 23-34
    • Dixon, S.1    Merz Jr., K.M.2    Lauri, G.3    Ianni, J.C.4
  • 39
    • 33646888111 scopus 로고    scopus 로고
    • Semiempirical Comparative Binding Energy Analysis (SE-COMBINE) of a Series of Trypsin Inhibitors
    • 10.1021/ct050284j
    • Semiempirical Comparative Binding Energy Analysis (SE-COMBINE) of a Series of Trypsin Inhibitors. MB Peters KM Merz Jr, J Chem Theory Comput 2006 2 383 399 10.1021/ct050284j
    • (2006) J Chem Theory Comput , vol.2 , pp. 383-399
    • Peters, M.B.1    Merz Jr., K.M.2
  • 40
    • 28044438176 scopus 로고    scopus 로고
    • Ab initio fragment molecular orbital (FMO) method applied to analysis of the ligand-protein interaction in a pheromone-binding protein
    • DOI 10.1016/j.compbiolchem.2005.09.005, PII S147692710500099X
    • Ab initio fragment molecular orbital (FMO) method applied to analysis of the ligand-protein interaction in a pheromone-binding protein. T Nemoto DG Fedorov M Uebayasi K Kanazawa K Kitaura Y Komeiji, Comput Biol Chem 2005 29 434 439 10.1016/j.compbiolchem.2005.09.005 16290169 (Pubitemid 41690443)
    • (2005) Computational Biology and Chemistry , vol.29 , Issue.6 , pp. 434-439
    • Nemoto, T.1    Fedorov, D.G.2    Uebayasi, M.3    Kanazawa, K.4    Kitaura, K.5    Komeiji, Y.6
  • 41
    • 1142279661 scopus 로고    scopus 로고
    • Quantum mechanical map for protein-ligand binding with application to -trypsin/benzamidine complex
    • 10.1063/1.1639152. 15268233
    • Quantum mechanical map for protein-ligand binding with application to -trypsin/benzamidine complex. DW Zhang Y Xiang AM Gao JZH Zhang, J Chem Phys 2004 120 1145 1148 10.1063/1.1639152 15268233
    • (2004) J Chem Phys , vol.120 , pp. 1145-1148
    • Zhang, D.W.1    Xiang, Y.2    Gao, A.M.3    Zhang, J.Z.H.4
  • 42
    • 77952337364 scopus 로고    scopus 로고
    • Ligand Affinities Estimated by Quantum Chemical Calculations
    • Ligand Affinities Estimated by Quantum Chemical Calculations. P Söderhjelm J Kongsted U Ryde, J Chem Theory Comput 2010 6 1726 1737
    • (2010) J Chem Theory Comput , vol.6 , pp. 1726-1737
    • Söderhjelm, P.1    Kongsted, J.2    Ryde, U.3
  • 43
    • 77953200013 scopus 로고    scopus 로고
    • Comparison of binding affinity evaluations for FKBP ligands with state-of-the-art computational methods: FMO, QM/MM, MM-PB/SA and MP-CAFEE approaches
    • 10.1273/cbij.10.32
    • Comparison of binding affinity evaluations for FKBP ligands with state-of-the-art computational methods: FMO, QM/MM, MM-PB/SA and MP-CAFEE approaches. H Watanabe S Tanaka N Okimoto A Hasegawa M Taiji Y Tanida T Mitsui M Katsuyama H Fujitani, Chem-Bio Informatics Journal 2010 10 32 45 10.1273/cbij.10.32
    • (2010) Chem-Bio Informatics Journal , vol.10 , pp. 32-45
    • Watanabe, H.1    Tanaka, S.2    Okimoto, N.3    Hasegawa, A.4    Taiji, M.5    Tanida, Y.6    Mitsui, T.7    Katsuyama, M.8    Fujitani, H.9
  • 44
    • 54949153723 scopus 로고    scopus 로고
    • QSAR Study of Cyclic Urea Type HIV-1 PR Inhibitors Using Ab Initio MO Calculation of Their Complex Structures with HIV-1 PR
    • QSAR Study of Cyclic Urea Type HIV-1 PR Inhibitors Using Ab Initio MO Calculation of Their Complex Structures with HIV-1 PR. T Yoshida K Yamagishi H Chuman, QSAR & Comb Sci 2008 27 694 703
    • (2008) QSAR & Comb Sci , vol.27 , pp. 694-703
    • Yoshida, T.1    Yamagishi, K.2    Chuman, H.3
  • 45
    • 65649135842 scopus 로고    scopus 로고
    • Novel Quantitative Structure-Activity Studies of HIV-1 Protease Inhibitors of the Cyclic Urea Type Using Descriptors Derived from Molecular Dynamics and Molecular Orbital Calculations
    • 10.2174/157340909787580845
    • Novel Quantitative Structure-Activity Studies of HIV-1 Protease Inhibitors of the Cyclic Urea Type Using Descriptors Derived from Molecular Dynamics and Molecular Orbital Calculations. T Yoshida T Fujita H Chuman, Curr Comput Aided Drug Des 2009 5 38 55 10.2174/157340909787580845
    • (2009) Curr Comput Aided Drug des , vol.5 , pp. 38-55
    • Yoshida, T.1    Fujita, T.2    Chuman, H.3
  • 46
    • 77952772108 scopus 로고    scopus 로고
    • Correlation analyses on binding affinity of Substituted benzenesulfonamides with carbonic anhydrase using ab initio MO calculations on their Complex structures
    • 10.1021/ci100068w. 20415451
    • Correlation analyses on binding affinity of Substituted benzenesulfonamides with carbonic anhydrase using ab initio MO calculations on their Complex structures. T Yoshida Y Munei S Hitaoka H Chuman, J Chem Inf Model 2010 50 850 860 10.1021/ci100068w 20415451
    • (2010) J Chem Inf Model , vol.50 , pp. 850-860
    • Yoshida, T.1    Munei, Y.2    Hitaoka, S.3    Chuman, H.4
  • 47
    • 46849089254 scopus 로고    scopus 로고
    • Recent developments in fragment-based drug discovery
    • DOI 10.1021/jm8000373
    • Recent Developments in Fragment-Based Drug Discovery. M Congreve G Chessari D Tisi AJ Woodhead, J Med Chem 2008 51 3661 3680 10.1021/jm8000373 18457385 (Pubitemid 351956496)
    • (2008) Journal of Medicinal Chemistry , vol.51 , Issue.13 , pp. 3661-3680
    • Congreve, M.1    Chessari, G.2    Tisi, D.3    Woodhead, A.J.4
  • 48
    • 50249083873 scopus 로고    scopus 로고
    • Identification of N-(4-Piperidinyl)-4-(2,6-dichlorobenzoylamino)-1H- pyrazole-3-carboxamide (AT7519), a Novel Cyclin Dependent Kinase Inhibitor Using Fragment-Based X-Ray Crystallography and Structure Based Drug Design
    • 10.1021/jm800382h. 18656911
    • Identification of N-(4-Piperidinyl)-4-(2,6-dichlorobenzoylamino)-1H- pyrazole-3-carboxamide (AT7519), a Novel Cyclin Dependent Kinase Inhibitor Using Fragment-Based X-Ray Crystallography and Structure Based Drug Design PG Wyatt AJ Woodhead V Berdini JA Boulstridge MG Carr DM Cross DJ Davis LA Devine TR Early RE Feltell,, et al. J Med Chem 2008 51 4986 4999 10.1021/jm800382h 18656911
    • (2008) J Med Chem , vol.51 , pp. 4986-4999
    • Wyatt, P.G.1    Woodhead, A.J.2    Berdini, V.3    Boulstridge, J.A.4    Carr, M.G.5    Cross, D.M.6    Davis, D.J.7    Devine, L.A.8    Early, T.R.9    Feltell, R.E.10
  • 50
    • 0342645331 scopus 로고    scopus 로고
    • 1010 Sherbrooke Street West, Suite 910, Montreal, Canada H3A 2R7, Chemical Computing Group Inc
    • MOE (The Molecular Operating Environment). (2009.10). 1010 Sherbrooke Street West, Suite 910, Montreal, Canada H3A 2R7, Chemical Computing Group Inc 2009
    • (2009) MOE (The Molecular Operating Environment). (2009.10)
  • 51
    • 0001041959 scopus 로고    scopus 로고
    • Fast, efficient generation of high-quality atomic charges. AM1-BCC model: I. Method
    • 10.1002/(SICI)1096-987X(20000130)21:2<132::AID-JCC5>3.0.CO;2-P
    • Fast, efficient generation of high-quality atomic charges. AM1-BCC model: I. Method. A Jakalian BL Bush DB Jack CI Bayly, J Comput Chem 2000 21 132 146 10.1002/(SICI)1096-987X(20000130)21:2<132::AID-JCC5>3.0.CO;2-P
    • (2000) J Comput Chem , vol.21 , pp. 132-146
    • Jakalian, A.1    Bush, B.L.2    Jack, D.B.3    Bayly, C.I.4
  • 52
    • 0036890178 scopus 로고    scopus 로고
    • Fast, efficient generation of high-quality atomic charges. AM1-BCC model: II. Parameterization and validation
    • DOI 10.1002/jcc.10128
    • Fast, efficient generation of high-quality atomic charges. AM1-BCC model: II. Parameterization and validation. A Jakalian DB Jack CI Bayly, J Comput Chem 2002 23 1623 1641 10.1002/jcc.10128 12395429 (Pubitemid 35330860)
    • (2002) Journal of Computational Chemistry , vol.23 , Issue.16 , pp. 1623-1641
    • Jakalian, A.1    Jack, D.B.2    Bayly, C.I.3
  • 53
    • 33748790698 scopus 로고    scopus 로고
    • Facio: New Computational Chemistry Environment for PC GAMESS
    • 10.2477/jccj.4.25
    • Facio: New Computational Chemistry Environment for PC GAMESS. M Suenaga, J Comput Chem Jpn 2005 4 25 32 10.2477/jccj.4.25
    • (2005) J Comput Chem Jpn , vol.4 , pp. 25-32
    • Suenaga, M.1
  • 54
    • 67650754298 scopus 로고    scopus 로고
    • Development of GUI for GAMESS/FMO Calculation
    • 10.2477/jccj.H1920
    • Development of GUI for GAMESS/FMO Calculation. M Suenaga, J Comput Chem Jpn 2008 7 33 53 10.2477/jccj.H1920
    • (2008) J Comput Chem Jpn , vol.7 , pp. 33-53
    • Suenaga, M.1
  • 55
    • 0000170061 scopus 로고    scopus 로고
    • Pair interaction molecular orbital method: An approximate computational method for molecular interactions
    • PII S0009261499009379
    • Pair interaction molecular orbital method: an approximate computational method for molecular interactions. K Kitaura T Sawai T Asada T Nakano M Uebayasi, Chem Phys Lett 1999 312 319 324 10.1016/S0009-2614(99)00937-9 (Pubitemid 129556608)
    • (1999) Chemical Physics Letters , vol.312 , Issue.2-4 , pp. 319-324
    • Kitaura, K.1    Sawai, T.2    Asada, T.3    Nakano, T.4    Uebayasi, M.5
  • 56
    • 0001046021 scopus 로고    scopus 로고
    • Fragment molecular orbital method: Application to polypeptides
    • 10.1016/S0009-2614(00)00070-1
    • Fragment molecular orbital method: application to polypeptides. T Nakano T Kaminuma T Sato Y Akiyama M Uebayasi K Kitaura, Chem Phys Lett 2000 318 614 618 10.1016/S0009-2614(00)00070-1
    • (2000) Chem Phys Lett , vol.318 , pp. 614-618
    • Nakano, T.1    Kaminuma, T.2    Sato, T.3    Akiyama, Y.4    Uebayasi, M.5    Kitaura, K.6
  • 57
    • 0037122848 scopus 로고    scopus 로고
    • Fragment molecular orbital method: Use of approximate electrostatic potential
    • 10.1016/S0009-2614(01)01416-6
    • Fragment molecular orbital method: use of approximate electrostatic potential. T Nakano T Kaminuma T Sato K Fukuzawa Y Akiyama M Uebayasi K Kitaura, Chem Phys Lett 2002 351 475 480 10.1016/S0009-2614(01)01416-6
    • (2002) Chem Phys Lett , vol.351 , pp. 475-480
    • Nakano, T.1    Kaminuma, T.2    Sato, T.3    Fukuzawa, K.4    Akiyama, Y.5    Uebayasi, M.6    Kitaura, K.7
  • 60
    • 84885102778 scopus 로고    scopus 로고
    • Advances in electronic structure theory: GAMESS a decade later
    • Amsterdam: Elsevier, Dykstra CE, Frenking G, Kim KS, Scuseria GE
    • Advances in electronic structure theory: GAMESS a decade later. MS Gordon MW Schmidt, Theory and Applications of Computational Chemistry, the first forty years Amsterdam: Elsevier, Dykstra CE, Frenking G, Kim KS, Scuseria GE, 2005 1167 1189 full-text
    • (2005) Theory and Applications of Computational Chemistry, the First Forty Years , pp. 1167-1189
    • Gordon, M.S.1    Schmidt, M.W.2
  • 62
    • 33244464010 scopus 로고    scopus 로고
    • VISCANA: Visualized cluster analysis of protein - Ligand interaction based on the ab initio fragment molecular orbital method for virtual ligand screening
    • DOI 10.1021/ci050262q
    • VISCANA: Visualized Cluster Analysis of Protein-Ligand Interaction Based on the ab Initio Fragment Molecular Orbital Method for Virtual Ligand Screening. S Amari M Aizawa J Zhang K Fukuzawa Y Mochizuki Y Iwasawa K Nakata H Chuman T Nakano, J Chem Inf Model 2006 46 221 230 10.1021/ci050262q 16426058 (Pubitemid 43282117)
    • (2006) Journal of Chemical Information and Modeling , vol.46 , Issue.1 , pp. 221-230
    • Amari, S.1    Aizawa, M.2    Zhang, J.3    Fukuzawa, K.4    Mochizuki, Y.5    Iwasawa, Y.6    Nakata, K.7    Chuman, H.8    Nakano, T.9
  • 63
    • 33646586407 scopus 로고    scopus 로고
    • Intra- and intermolecular interactions between cyclic-AMP receptor protein and DNA: Ab initio fragment molecular orbital study
    • DOI 10.1002/jcc.20399
    • Intra- and intermolecular interactions between cyclic-AMP receptor protein and DNA: Ab initio fragment molecular orbital study. K Fukuzawa Y Komeiji Y Mochizuki A Kato T Nakano S Tanaka, J Comput Chem 2006 27 948 960 10.1002/jcc.20399 16586530 (Pubitemid 43723217)
    • (2006) Journal of Computational Chemistry , vol.27 , Issue.8 , pp. 948-960
    • Fukuzawa, K.1    Komeiji, Y.2    Mochizuki, Y.3    Kato, A.4    Nakano, T.5    Tanaka, S.6
  • 64
    • 33846595219 scopus 로고    scopus 로고
    • Pair interaction energy decomposition analysis
    • DOI 10.1002/jcc.20496
    • Pair interaction energy decomposition analysis. DG Fedorov K Kitaura, J Comput Chem 2007 28 222 237 10.1002/jcc.20496 17109433 (Pubitemid 46180489)
    • (2007) Journal of Computational Chemistry , vol.28 , Issue.1 , pp. 222-237
    • Fedorov, D.G.1    Kitaura, K.2
  • 65
    • 84987133653 scopus 로고
    • A new energy decomposition scheme for molecular interactions within the Hartree-Fock approximation
    • 10.1002/qua.560100211
    • A new energy decomposition scheme for molecular interactions within the Hartree-Fock approximation. K Kitaura K Morokuma, Int J Quantum Chem 1976 10 325 340 10.1002/qua.560100211
    • (1976) Int J Quantum Chem , vol.10 , pp. 325-340
    • Kitaura, K.1    Morokuma, K.2
  • 66
    • 0036722785 scopus 로고    scopus 로고
    • Can the calculation of ligand binding free energies be improved with continuum solvent electrostatics and an ideal-gas entropy correction?
    • DOI 10.1002/jcc.10112
    • Can the calculation of ligand binding free energies be improved with continuum solvent electrostatics and an ideal-gas entropy correction? SM Schwarzl TB Tschopp JC Smith S Fischer, J Comput Chem 2002 23 1143 1149 10.1002/jcc.10112 12116383 (Pubitemid 34854445)
    • (2002) Journal of Computational Chemistry , vol.23 , Issue.12 , pp. 1143-1149
    • Schwarzl, S.M.1    Tschopp, T.B.2    Smith, J.C.3    Fischer, S.4
  • 67
    • 0036821028 scopus 로고    scopus 로고
    • The consequences of translational and rotational entropy lost by small molecules on binding to proteins
    • DOI 10.1023/A:1022446720849
    • The consequences of translational and rotational entropy lost by small molecules on binding to proteins. CW Murray ML Verdonk, J Comput Aided Mol Des 2002 16 741 753 10.1023/A:1022446720849 12650591 (Pubitemid 36336183)
    • (2002) Journal of Computer-Aided Molecular Design , vol.16 , Issue.10 , pp. 741-753
    • Murray, C.W.1    Verdonk, M.L.2
  • 68
    • 33749242759 scopus 로고    scopus 로고
    • Contribution of conformer focusing to the uncertainty in predicting free energies for protein-ligand binding
    • DOI 10.1021/jm060763i
    • Contribution of Conformer Focusing to the Uncertainty in Predicting Free Energies for Protein-Ligand Binding. J Tirado-Rives WL Jorgensen, J Med Chem 2006 49 5880 5884 10.1021/jm060763i 17004703 (Pubitemid 44484934)
    • (2006) Journal of Medicinal Chemistry , vol.49 , Issue.20 , pp. 5880-5884
    • Tirado-Rives, J.1    Jorgensen, W.L.2
  • 69
    • 0031226772 scopus 로고    scopus 로고
    • Empirical scoring functions: I. The development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes
    • Empirical scoring functions: I. The development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes. MD Eldridge CW Murray TR Auton GV Paolini RP Mee, J Comput Aided Mol Des 1997 11 425 445 10.1023/A:1007996124545 9385547 (Pubitemid 127505895)
    • (1997) Journal of Computer-Aided Molecular Design , vol.11 , Issue.5 , pp. 425-445
    • Eldridge, M.D.1    Murray, C.W.2    Auton, T.R.3    Paolini, G.V.4    Mee, R.P.5
  • 70
    • 0028454828 scopus 로고
    • The development of a simple empirical scoring function to estimate the binding constant for a protein-ligand complex of known three-dimensional structure
    • 7964925
    • The development of a simple empirical scoring function to estimate the binding constant for a protein-ligand complex of known three-dimensional structure. H-J Böhm, J Comput Aided Mol Des 1994 8 243 256 7964925
    • (1994) J Comput Aided Mol des , vol.8 , pp. 243-256
    • Böhm, H.-J.1
  • 71
    • 0037142298 scopus 로고    scopus 로고
    • SMall Molecule Growth 2001 (SMoG2001): An improved knowledge-based scoring function for protein-ligand interactions
    • DOI 10.1021/jm0105833
    • SMall Molecule Growth 2001 (SMoG2001): An Improved Knowledge-Based Scoring Function for Protein-Ligand Interactions. AV Ishchenko EI Shakhnovich, J Med Chem 2002 45 2770 2780 10.1021/jm0105833 12061879 (Pubitemid 34627647)
    • (2002) Journal of Medicinal Chemistry , vol.45 , Issue.13 , pp. 2770-2780
    • Ishchenko, A.V.1    Shakhnovich, E.I.2
  • 72
    • 0942276314 scopus 로고    scopus 로고
    • A Quantum Mechanics-Based Scoring Function: Study of Zinc Ion-Mediated Ligand Binding
    • DOI 10.1021/ja038496i
    • A Quantum Mechanics-Based Scoring Function:? Study of Zinc Ion-Mediated Ligand Binding. K Raha KM Merz Jr, J Am Chem Soc 2004 126 1020 1021 10.1021/ja038496i 14746460 (Pubitemid 38140722)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.4 , pp. 1020-1021
    • Raha, K.1    Merz Jr., K.M.2
  • 73
    • 77957954013 scopus 로고    scopus 로고
    • Mixed Quantum Mechanics/Molecular Mechanics Scoring Function to Predict Protein-Ligand Binding Affinity
    • 10.1021/ct100315g. 21221417
    • Mixed Quantum Mechanics/Molecular Mechanics Scoring Function To Predict Protein-Ligand Binding Affinity. SA Hayik R Dunbrack Jr KM Merz Jr, J Chem Theory Comput 2010 6 3079 3091 10.1021/ct100315g 21221417
    • (2010) J Chem Theory Comput , vol.6 , pp. 3079-3091
    • Hayik, S.A.1    Dunbrack Jr., R.2    Merz Jr., K.M.3
  • 74
    • 0000598486 scopus 로고    scopus 로고
    • Using a Convenient, Quantitative Model for Torsional Entropy to Establish Qualitative Trends for Molecular Processes That Restrict Conformational Freedom
    • Using a Convenient, Quantitative Model for Torsional Entropy To Establish Qualitative Trends for Molecular Processes That Restrict Conformational Freedom. M Mammen EI Shakhnovich GM Whitesides, J Org Chem 1998 63 3168 3175 10.1021/jo970943n (Pubitemid 128500459)
    • (1998) Journal of Organic Chemistry , vol.63 , Issue.10 , pp. 3168-3175
    • Mammen, M.1    Shakhnovich, E.I.2    Whitesides, G.M.3
  • 75
    • 0011930746 scopus 로고
    • Theory of hydrophobic bonding. II. Correlation of hydrocarbon solubility in water with solvent cavity surface area
    • 10.1021/j100663a023
    • Theory of hydrophobic bonding. II. Correlation of hydrocarbon solubility in water with solvent cavity surface area. RB Hermann, J Phys Chem 1972 76 2754 2759 10.1021/j100663a023
    • (1972) J Phys Chem , vol.76 , pp. 2754-2759
    • Hermann, R.B.1
  • 76
    • 33751385054 scopus 로고
    • Macroscopic models of aqueous solutions: Biological and chemical applications
    • 10.1021/j100108a002
    • Macroscopic models of aqueous solutions: biological and chemical applications. B Honig K Sharp AS Yang, J Phys Chem 1993 97 1101 1109 10.1021/j100108a002
    • (1993) J Phys Chem , vol.97 , pp. 1101-1109
    • Honig, B.1    Sharp, K.2    Yang, A.S.3
  • 77
    • 84884674606 scopus 로고    scopus 로고
    • SIMCAP (11.0.0.0)
    • Umeå, Sweden, Umetrics AB
    • SIMCAP (11.0.0.0). Box 7960, SE90719 Umeå, Sweden, Umetrics AB 2005
    • (2005) Box 7960, SE90719
  • 78
    • 0035965476 scopus 로고    scopus 로고
    • PLS-regression: A basic tool of chemometrics
    • DOI 10.1016/S0169-7439(01)00155-1, PII S0169743901001551
    • PLS-regression: a basic tool of chemometrics. S Wold M Sjöström L Eriksson, Chemom Intell Lab Syst 2001 58 109 130 10.1016/S0169-7439(01)00155- 1 (Pubitemid 33033283)
    • (2001) Chemometrics and Intelligent Laboratory Systems , vol.58 , Issue.2 , pp. 109-130
    • Wold, S.1    Sjostrom, M.2    Eriksson, L.3
  • 79
    • 77958551314 scopus 로고    scopus 로고
    • Correlation Analyses on Binding Affinity of Sialic Acid Analogues with Influenza Virus Neuraminidase-1 Using ab Initio MO Calculations on Their Complex Structures
    • 10.1021/ci100225b. 20863103
    • Correlation Analyses on Binding Affinity of Sialic Acid Analogues with Influenza Virus Neuraminidase-1 Using ab Initio MO Calculations on Their Complex Structures. S Hitaoka M Harada T Yoshida H Chuman, J Chem Inf Model 2010 50 1796 1805 10.1021/ci100225b 20863103
    • (2010) J Chem Inf Model , vol.50 , pp. 1796-1805
    • Hitaoka, S.1    Harada, M.2    Yoshida, T.3    Chuman, H.4
  • 80
    • 2342586724 scopus 로고    scopus 로고
    • Conformational Analysis of Drug-Like Molecules Bound to Proteins: An Extensive Study of Ligand Reorganization upon Binding
    • DOI 10.1021/jm030563w
    • Conformational Analysis of Drug-Like Molecules Bound to Proteins:? An Extensive Study of Ligand Reorganization upon Binding. E Perola PS Charifson, J Med Chem 2004 47 2499 2510 10.1021/jm030563w 15115393 (Pubitemid 38580088)
    • (2004) Journal of Medicinal Chemistry , vol.47 , Issue.10 , pp. 2499-2510
    • Perola, E.1    Charifson, P.S.2
  • 81
    • 34347224684 scopus 로고    scopus 로고
    • Calculation of protein-ligand binding affinities
    • DOI 10.1146/annurev.biophys.36.040306.132550
    • Calculation of Protein-Ligand Binding Affinities. MK Gilson H-X Zhou, Annu Rev Biophys Biomol Struct 2007 36 21 42 10.1146/annurev.biophys.36.040306. 132550 17201676 (Pubitemid 46998108)
    • (2007) Annual Review of Biophysics and Biomolecular Structure , vol.36 , pp. 21-42
    • Gilson, M.K.1    Zhou, H.-X.2
  • 82
    • 70350349240 scopus 로고    scopus 로고
    • A Study of CDK2 Inhibitors Using a Novel 3D-QSAR Method Exploiting Receptor Flexibility
    • A Study of CDK2 Inhibitors Using a Novel 3D-QSAR Method Exploiting Receptor Flexibility. MP Mazanetz IM Withers CA Laughton PM Fischer, QSAR & Comb Sci 2009 28 878 884
    • (2009) QSAR & Comb Sci , vol.28 , pp. 878-884
    • Mazanetz, M.P.1    Withers, I.M.2    Laughton, C.A.3    Fischer, P.M.4
  • 83
    • 52149095458 scopus 로고    scopus 로고
    • The effect of MM polarization on the QM/MM transition state stabilization: Application to chorismate mutase
    • 10.1080/00268970802077850
    • The effect of MM polarization on the QM/MM transition state stabilization: application to chorismate mutase. CJR Illingworth KE Parkes CR Snell S Marti V Moliner CA Reynolds, Mol Phys 2008 106 1511 1515 10.1080/00268970802077850
    • (2008) Mol Phys , vol.106 , pp. 1511-1515
    • Illingworth, C.J.R.1    Parkes, K.E.2    Snell, C.R.3    Marti, S.4    Moliner, V.5    Reynolds, C.A.6
  • 84
    • 34250745809 scopus 로고    scopus 로고
    • Compensating enthalpic and entropic changes hinder binding affinity optimization
    • DOI 10.1111/j.1747-0285.2007.00519.x
    • Compensating Enthalpic and Entropic Changes Hinder Binding Affinity Optimization. V Lafont AA Armstrong H Ohtaka Y Kiso LM Amzel E Freire, Chem Biol Drug Des 2007 69 413 422 10.1111/j.1747-0285.2007.00519.x 17581235 (Pubitemid 46955533)
    • (2007) Chemical Biology and Drug Design , vol.69 , Issue.6 , pp. 413-422
    • Lafont, V.1    Armstrong, A.A.2    Ohtaka, H.3    Kiso, Y.4    Mario Amzel, L.5    Freire, E.6
  • 85
    • 52049123291 scopus 로고    scopus 로고
    • Do enthalpy and entropy distinguish first in class from best in class?
    • 10.1016/j.drudis.2008.07.005. 18703160
    • Do enthalpy and entropy distinguish first in class from best in class? E Freire, Drug Discov Today 2008 13 869 874 10.1016/j.drudis.2008.07.005 18703160
    • (2008) Drug Discov Today , vol.13 , pp. 869-874
    • Freire, E.1
  • 87
    • 33646565044 scopus 로고    scopus 로고
    • The polarizable continuum model (PCM) interfaced with the fragment molecular orbital method (FMO)
    • DOI 10.1002/jcc.20406
    • The polarizable continuum model (PCM) interfaced with the fragment molecular orbital method (FMO). DG Fedorov K Kitaura H Li JH Jensen MS Gordon, J Comput Chem 2006 27 976 985 10.1002/jcc.20406 16604514 (Pubitemid 43723220)
    • (2006) Journal of Computational Chemistry , vol.27 , Issue.8 , pp. 976-985
    • Fedorov, D.G.1    Kitaura, K.2    Li, H.3    Jensen, J.H.4    Gordon, M.S.5
  • 88
    • 78649965861 scopus 로고    scopus 로고
    • Incorporation of solvation effects into the fragment molecular orbital calculations with the Poisson-Boltzmann equation
    • 10.1016/j.cplett.2010.10.017
    • Incorporation of solvation effects into the fragment molecular orbital calculations with the Poisson-Boltzmann equation. H Watanabe Y Okiyama T Nakano S Tanaka, Chem Phys Lett 2010 500 116 119 10.1016/j.cplett.2010.10.017
    • (2010) Chem Phys Lett , vol.500 , pp. 116-119
    • Watanabe, H.1    Okiyama, Y.2    Nakano, T.3    Tanaka, S.4


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