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Volumn 7, Issue 20, 2002, Pages 1047-1055

Structure-based virtual screening: An overview

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD CLOTTING FACTOR 10A; CARBONATE DEHYDRATASE II; DNA TOPOISOMERASE (ATP HYDROLYSING); ESTROGEN RECEPTOR; KINESIN; LIGAND; RETINOIC ACID RECEPTOR; THROMBIN; THYMIDYLATE SYNTHASE; TRANSFERASE; VIRUS RNA;

EID: 0037107887     PISSN: 13596446     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-6446(02)02483-2     Document Type: Review
Times cited : (621)

References (73)
  • 1
    • 0034909257 scopus 로고    scopus 로고
    • Drug discovery - An operating model for a new era
    • Myers S., Baker A. Drug discovery - an operating model for a new era. Nat. Biotechnol. 19:2001;727-730.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 727-730
    • Myers, S.1    Baker, A.2
  • 2
    • 0035709416 scopus 로고    scopus 로고
    • Functional genomics and target validation approaches using antisense oligonucleotide technology
    • Dean N.M. Functional genomics and target validation approaches using antisense oligonucleotide technology. Curr. Opin. Biotechnol. 12:2001;622-625.
    • (2001) Curr. Opin. Biotechnol. , vol.12 , pp. 622-625
    • Dean, N.M.1
  • 3
    • 0033863669 scopus 로고    scopus 로고
    • High-throughput screening: New technology for the 21st century
    • Hertzberg R.P., Pope A.J. High-throughput screening: new technology for the 21st century. Curr. Opin. Chem. Biol. 4:2000;445-451.
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 445-451
    • Hertzberg, R.P.1    Pope, A.J.2
  • 4
    • 0037079609 scopus 로고    scopus 로고
    • Dynamic combinatorial chemistry
    • Otto S., et al. Dynamic combinatorial chemistry. Drug Discov. Today. 7:2002;117-125.
    • (2002) Drug Discov. Today , vol.7 , pp. 117-125
    • Otto, S.1
  • 5
    • 0035313896 scopus 로고    scopus 로고
    • Screening for human ADME/Tox drug properties in drug discovery
    • Li A.P. Screening for human ADME/Tox drug properties in drug discovery. Drug Discov. Today. 6:2001;357-366.
    • (2001) Drug Discov. Today , vol.6 , pp. 357-366
    • Li, A.P.1
  • 7
    • 0036558207 scopus 로고    scopus 로고
    • Structure-based screening of low-affinity compounds
    • Carr R., Jhoti H. Structure-based screening of low-affinity compounds. Drug Discov. Today. 7:2002;522-527.
    • (2002) Drug Discov. Today , vol.7 , pp. 522-527
    • Carr, R.1    Jhoti, H.2
  • 8
    • 0035358813 scopus 로고    scopus 로고
    • Applications of NMR in drug discovery
    • Diercks T.C.M., et al. Applications of NMR in drug discovery. Curr. Opin. Chem. Biol. 5:2001;285-291.
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 285-291
    • Diercks, T.C.M.1
  • 9
    • 0002606755 scopus 로고    scopus 로고
    • Virtual screening - An overview
    • Walters W.P., et al. Virtual screening - an overview. Drug Discov. Today. 3:1998;160-178.
    • (1998) Drug Discov. Today , vol.3 , pp. 160-178
    • Walters, W.P.1
  • 11
    • 0035003352 scopus 로고    scopus 로고
    • 3-D pharmacophores in drug discovery
    • Mason J.S., et al. 3-D pharmacophores in drug discovery. Curr. Pharm. Des. 7:2001;567-597.
    • (2001) Curr. Pharm. Des. , vol.7 , pp. 567-597
    • Mason, J.S.1
  • 12
    • 0037030647 scopus 로고    scopus 로고
    • Evaluation of a novel shape-based computational filter for lead evolution: Application to thrombin inhibitors
    • Srinivasan J., et al. Evaluation of a novel shape-based computational filter for lead evolution: Application to thrombin inhibitors. J. Med. Chem. 45:2002;2494-2500.
    • (2002) J. Med. Chem. , vol.45 , pp. 2494-2500
    • Srinivasan, J.1
  • 13
    • 0036606483 scopus 로고    scopus 로고
    • Principles of docking: An overview of search algorithms and a guide to scoring functions
    • Halperin I., et al. Principles of docking: an overview of search algorithms and a guide to scoring functions. Proteins Struct. Funct. Genet. 47:2002;409-443.
    • (2002) Proteins Struct. Funct. Genet. , vol.47 , pp. 409-443
    • Halperin, I.1
  • 14
    • 0031024171 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • Lipinski C.A., et al. Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv. Drug Discov. Res. 23:1997;3-25.
    • (1997) Adv. Drug Discov. Res. , vol.23 , pp. 3-25
    • Lipinski, C.A.1
  • 15
    • 0030030608 scopus 로고    scopus 로고
    • Correlation of drug absorption with molecular surface properties
    • Palm K., et al. Correlation of drug absorption with molecular surface properties. J. Pharm. Sci. 85:1996;32-39.
    • (1996) J. Pharm. Sci. , vol.85 , pp. 32-39
    • Palm, K.1
  • 16
    • 0030636933 scopus 로고    scopus 로고
    • A hybrid approach for ring flexibility in 3D database searching
    • Sadowski J. A hybrid approach for ring flexibility in 3D database searching. J. Comput.-Aided Mol. Design. 11:1997;53-60.
    • (1997) J. Comput.-Aided Mol. Design , vol.11 , pp. 53-60
    • Sadowski, J.1
  • 17
    • 49149147973 scopus 로고
    • Iterative partial equalization of orbital electronegativity - Rapid access to atomic charges
    • Gasteiger J., Marsili M. Iterative partial equalization of orbital electronegativity - rapid access to atomic charges. Tetrahedron. 36:1980;3219-3288.
    • (1980) Tetrahedron , vol.36 , pp. 3219-3288
    • Gasteiger, J.1    Marsili, M.2
  • 18
    • 0011134241 scopus 로고    scopus 로고
    • Merck molecular force field. 2. MMFF94 van der Waals and electrostatic parameters for intermolecular interations
    • Halgren T.A. Merck molecular force field. 2. MMFF94 van der Waals and electrostatic parameters for intermolecular interations. J. Comput. Chem. 17:1996;520-552.
    • (1996) J. Comput. Chem. , vol.17 , pp. 520-552
    • Halgren, T.A.1
  • 19
    • 0032214649 scopus 로고    scopus 로고
    • Databases for protein-ligand complexes
    • Hendlich M. Databases for protein-ligand complexes. Acta Crystallogr. D. 54:1998;1178-1182.
    • (1998) Acta Crystallogr. D , vol.54 , pp. 1178-1182
    • Hendlich, M.1
  • 20
    • 0344186399 scopus 로고    scopus 로고
    • Errors in protein structures
    • Hooft R.W.W., et al. Errors in protein structures. Nature. 381:1996;272.
    • (1996) Nature , vol.381 , pp. 272
    • Hooft, R.W.W.1
  • 21
    • 0028522982 scopus 로고
    • Flexibases - A way to enhance the use of molecular docking methods
    • Kearsley S.K., et al. Flexibases - a way to enhance the use of molecular docking methods. J. Comput.-Aided Mol. Design. 8:1994;565-582.
    • (1994) J. Comput.-Aided Mol. Design , vol.8 , pp. 565-582
    • Kearsley, S.K.1
  • 22
    • 0031965676 scopus 로고    scopus 로고
    • Flexible ligand docking using configurational ensembles
    • Lomber D.M., Shoichet B.K. Flexible ligand docking using configurational ensembles. Proteins Struct. Funct. Genet. 7:1998;938-950.
    • (1998) Proteins Struct. Funct. Genet. , vol.7 , pp. 938-950
    • Lomber, D.M.1    Shoichet, B.K.2
  • 23
    • 0031181346 scopus 로고    scopus 로고
    • QXP: Powerful, rapid computer algorithms for structure-based drug design
    • McMartin C., Bohacek R.S. QXP: powerful, rapid computer algorithms for structure-based drug design. J. Comput. Aided Mol. Des. 11:1997;333-344.
    • (1997) J. Comput. Aided Mol. Des. , vol.11 , pp. 333-344
    • McMartin, C.1    Bohacek, R.S.2
  • 24
    • 0032855301 scopus 로고    scopus 로고
    • MCDOCK: A Monte Carlo simulation approach to the molecular docking problem
    • Liu M., Wang S. MCDOCK: a Monte Carlo simulation approach to the molecular docking problem. J. Comput.-Aided Mol. Design. 13:1999;435-451.
    • (1999) J. Comput.-Aided Mol. Design , vol.13 , pp. 435-451
    • Liu, M.1    Wang, S.2
  • 25
    • 0028854034 scopus 로고
    • Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation
    • Jones G., et al. Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation. J. Mol. Biol. 245:1995;43-53.
    • (1995) J. Mol. Biol. , vol.245 , pp. 43-53
    • Jones, G.1
  • 26
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • Morris G.M., et al. Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J. Comput. Chem. 19:1998;1639-1662.
    • (1998) J. Comput. Chem. , vol.19 , pp. 1639-1662
    • Morris, G.M.1
  • 27
    • 84986522918 scopus 로고
    • ICM - a new method for protein modeling and design: Applications to docking and structure prediction from the distorted native conformation
    • Abagyan R.A., et al. ICM - a new method for protein modeling and design: applications to docking and structure prediction from the distorted native conformation. J. Comput. Chem. 15:1994;488-506.
    • (1994) J. Comput. Chem. , vol.15 , pp. 488-506
    • Abagyan, R.A.1
  • 28
    • 0030599010 scopus 로고    scopus 로고
    • A fast flexible docking method using an incremental construction algorithm
    • Rarey M., et al. A fast flexible docking method using an incremental construction algorithm. J. Mol. Biol. 261:1996;470-489.
    • (1996) J. Mol. Biol. , vol.261 , pp. 470-489
    • Rarey, M.1
  • 29
    • 0035025191 scopus 로고    scopus 로고
    • DOCK 4.0: Search strategies for automated molecular docking of flexible molecule databases
    • Ewing T.J.A., et al. DOCK 4.0: Search strategies for automated molecular docking of flexible molecule databases. J. Comput.-Aided Mol. Design. 15:2001;411-428.
    • (2001) J. Comput.-Aided Mol. Design , vol.15 , pp. 411-428
    • Ewing, T.J.A.1
  • 30
    • 0033674405 scopus 로고    scopus 로고
    • Virtual screening with solvation and ligand-induced complementarity
    • Schnecke V., Kuhn L.A. Virtual screening with solvation and ligand-induced complementarity. Perspect. Drug Des. Discov. 20:2000;171-190.
    • (2000) Perspect. Drug Des. Discov. , vol.20 , pp. 171-190
    • Schnecke, V.1    Kuhn, L.A.2
  • 31
    • 0033167995 scopus 로고    scopus 로고
    • Exploring the dynamic information content of a protein NMR structure: Comparison of a molecular dynamics simulation with NMR and X-ray structures of E. coli ribonuclease H1
    • Philippopoulos M., Lim C. Exploring the dynamic information content of a protein NMR structure: Comparison of a molecular dynamics simulation with NMR and X-ray structures of E. coli ribonuclease H1. Proteins Struct. Funct. Genet. 36:1999;87-110.
    • (1999) Proteins Struct. Funct. Genet. , vol.36 , pp. 87-110
    • Philippopoulos, M.1    Lim, C.2
  • 32
    • 0031581852 scopus 로고    scopus 로고
    • Molecular docking to ensembles of protein structures
    • Knegtel R.M.A., et al. Molecular docking to ensembles of protein structures. J. Mol. Biol. 266:1997;424-440.
    • (1997) J. Mol. Biol. , vol.266 , pp. 424-440
    • Knegtel, R.M.A.1
  • 33
    • 0035957528 scopus 로고    scopus 로고
    • Efficient molecular docking considering protein structure variations
    • ClauBen H., et al. Efficient molecular docking considering protein structure variations. J. Mol. Biol. 308:2001;377-395.
    • (2001) J. Mol. Biol. , vol.308 , pp. 377-395
    • ClauBen, H.1
  • 34
    • 0036137713 scopus 로고    scopus 로고
    • Automated docking to multiple target structures: Incorporation of protein mobility and structural water heterogeneity in AutoDock
    • Osterberg F., et al. Automated docking to multiple target structures: incorporation of protein mobility and structural water heterogeneity in AutoDock. Proteins Struct. Funct. Genet. 46:2002;34-40.
    • (2002) Proteins Struct. Funct. Genet. , vol.46 , pp. 34-40
    • Osterberg, F.1
  • 35
    • 0029623184 scopus 로고
    • Computational methods to predict binding free energy in ligand-receptor complexes
    • Ajay A., Murcko M.A. Computational methods to predict binding free energy in ligand-receptor complexes. J. Med. Chem. 38:1995;4953-4967.
    • (1995) J. Med. Chem. , vol.38 , pp. 4953-4967
    • Ajay, A.1    Murcko, M.A.2
  • 36
    • 0029011701 scopus 로고
    • A second generation force-field for the simulation of proteins, nucleic acids and organic molecules
    • Cornell W.D., et al. A second generation force-field for the simulation of proteins, nucleic acids and organic molecules. J. Am. Chem. Soc. 117:1995;5179-5197.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 5179-5197
    • Cornell, W.D.1
  • 37
    • 0041784950 scopus 로고    scopus 로고
    • All-atom empirical potential for molecular modeling and dynamics studies of proteins
    • MacKerell A.D., et al. All-atom empirical potential for molecular modeling and dynamics studies of proteins. J. Phys. Chem. B. 102:1998;3586-3616.
    • (1998) J. Phys. Chem. B , vol.102 , pp. 3586-3616
    • MacKerell, A.D.1
  • 38
    • 7044239742 scopus 로고
    • Free energy calculations: Application to chemical and biochemical phenomena
    • Kollman P.A. Free energy calculations: application to chemical and biochemical phenomena. Chem. Rev. 93:1993;2395-2417.
    • (1993) Chem. Rev. , vol.93 , pp. 2395-2417
    • Kollman, P.A.1
  • 39
    • 0028454828 scopus 로고
    • The development of a simple empirical scoring function to estimate the binding constant of a protein-ligand complex of known three-dimensional structure
    • Bohm H.J. The development of a simple empirical scoring function to estimate the binding constant of a protein-ligand complex of known three-dimensional structure. J. Comput.-Aided Mol. Design. 8:1994;243-256.
    • (1994) J. Comput.-Aided Mol. Design , vol.8 , pp. 243-256
    • Bohm, H.J.1
  • 40
    • 0029995624 scopus 로고    scopus 로고
    • VALIDATE: A new method for the receptor-based prediction of binding affinities of novel ligands
    • Head R.D., et al. VALIDATE: a new method for the receptor-based prediction of binding affinities of novel ligands. J. Am. Chem. Soc. 118:1996;3959-3969.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 3959-3969
    • Head, R.D.1
  • 41
    • 0031226772 scopus 로고    scopus 로고
    • Empirical scoring functions. 1. The development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes
    • Eldridge M.D., et al. Empirical scoring functions. 1. The development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes. J. Comput.-Aided Mol. Design. 11:1997;425-445.
    • (1997) J. Comput.-Aided Mol. Design , vol.11 , pp. 425-445
    • Eldridge, M.D.1
  • 42
    • 0026813925 scopus 로고
    • The computer program LUDI: A new method for the de novo design of enzyme inhibitors
    • Bohm H.J. The computer program LUDI: a new method for the de novo design of enzyme inhibitors. J. Comput.-Aided Mol. Design. 6:1992;61-78.
    • (1992) J. Comput.-Aided Mol. Design , vol.6 , pp. 61-78
    • Bohm, H.J.1
  • 43
    • 0029294584 scopus 로고
    • Molecular recognition of the inhibitor AG-1343 by HIV-1 protease - Conformationally flexible docking by evolutionary programming
    • Gehlhaar D.K., et al. Molecular recognition of the inhibitor AG-1343 by HIV-1 protease - conformationally flexible docking by evolutionary programming. Chem. Biol. 2:1995;317-324.
    • (1995) Chem. Biol. , vol.2 , pp. 317-324
    • Gehlhaar, D.K.1
  • 44
    • 0029000696 scopus 로고
    • Knowledge-based potentials for proteins
    • Sippl M. Knowledge-based potentials for proteins. Curr. Opin. Struct. Biol. 5:1995;229-235.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 229-235
    • Sippl, M.1
  • 45
    • 0033673508 scopus 로고    scopus 로고
    • A knowledge-based scoring function for protein-ligand interactions: Probing the reference state
    • Muegge I. A knowledge-based scoring function for protein-ligand interactions: probing the reference state. Perspect. Drug Des. Discov. 20:2000;99-114.
    • (2000) Perspect. Drug Des. Discov. , vol.20 , pp. 99-114
    • Muegge, I.1
  • 46
    • 0000882405 scopus 로고    scopus 로고
    • Bleep - Potential of mean force describing protein-ligand interactions: II. Calculation of binding energies and comparison with experimental data
    • Mitchell J.B.O., et al. Bleep - potential of mean force describing protein-ligand interactions: II. Calculation of binding energies and comparison with experimental data. J. Comp. Chem. 20:1999;1177-1185.
    • (1999) J. Comp. Chem. , vol.20 , pp. 1177-1185
    • Mitchell, J.B.O.1
  • 47
    • 0037142298 scopus 로고    scopus 로고
    • Small molecule growth 2001 (SMoG2001): An improved knowledge-based scoring function for protein-ligand interactions
    • Ishchenko A.V., Shakhnovich E.I. Small molecule growth 2001 (SMoG2001): An improved knowledge-based scoring function for protein-ligand interactions. J. Med. Chem. 45:2002;2770-2780.
    • (2002) J. Med. Chem. , vol.45 , pp. 2770-2780
    • Ishchenko, A.V.1    Shakhnovich, E.I.2
  • 48
    • 0034645763 scopus 로고    scopus 로고
    • Knowledge-based scoring function to predict protein-ligand interactions
    • Gohlke H., et al. Knowledge-based scoring function to predict protein-ligand interactions. J. Mol. Biol. 295:2000;337-356.
    • (2000) J. Mol. Biol. , vol.295 , pp. 337-356
    • Gohlke, H.1
  • 49
    • 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
    • Pearlman D.A., Charifson P.S. Are free energy calculations useful in practice? A comparison with rapid scoring functions for the p38 MAP kinase protein system. J. Med. Chem. 44:2001;3417-3423.
    • (2001) J. Med. Chem. , vol.44 , pp. 3417-3423
    • Pearlman, D.A.1    Charifson, P.S.2
  • 50
    • 0037046545 scopus 로고    scopus 로고
    • Docking into knowledge-based potential fields: A comparitive evaluation of DrugScore
    • Sotriffer C.A., et al. Docking into knowledge-based potential fields: a comparitive evaluation of DrugScore. J. Med. Chem. 45:2002;1967-1970.
    • (2002) J. Med. Chem. , vol.45 , pp. 1967-1970
    • Sotriffer, C.A.1
  • 51
    • 0033576680 scopus 로고    scopus 로고
    • Consensus scoring: A method for obtaining improved hit rates from docking databases of three-dimensional structures into proteins
    • Charifson P.S., et al. Consensus scoring: a method for obtaining improved hit rates from docking databases of three-dimensional structures into proteins. J. Med. Chem. 42:1999;5100-5109.
    • (1999) J. Med. Chem. , vol.42 , pp. 5100-5109
    • Charifson, P.S.1
  • 52
    • 0034649618 scopus 로고    scopus 로고
    • Protein-based virtual screening of chemical databases. 1. Evaluation of different docking/scoring combinations
    • Bissantz C., et al. Protein-based virtual screening of chemical databases. 1. Evaluation of different docking/scoring combinations. J. Med. Chem. 43:2000;4759-4767.
    • (2000) J. Med. Chem. , vol.43 , pp. 4759-4767
    • Bissantz, C.1
  • 53
    • 0035966871 scopus 로고    scopus 로고
    • Detailed analysis of scoring functions for virtual screening
    • Stahl M., Rarey M. Detailed analysis of scoring functions for virtual screening. J. Med. Chem. 44:2001;1035-1042.
    • (2001) J. Med. Chem. , vol.44 , pp. 1035-1042
    • Stahl, M.1    Rarey, M.2
  • 54
    • 0035438402 scopus 로고    scopus 로고
    • How does consensus scoring work for virtual library screening? An idealized computer experiment
    • Wang R.X., Wang S.M. How does consensus scoring work for virtual library screening? An idealized computer experiment. J. Chem. Inf. Comput. Sci. 41:2001;1422-1426.
    • (2001) J. Chem. Inf. Comput. Sci. , vol.41 , pp. 1422-1426
    • Wang, R.X.1    Wang, S.M.2
  • 55
    • 0031307203 scopus 로고    scopus 로고
    • Evaluation of the CASP2 docking section. Proteins Struct
    • Dixon, J.S. (1997) Evaluation of the CASP2 docking section. Proteins Struct. Funct. Genet. (Suppl. 1), 198-204
    • (1997) Funct. Genet. , Issue.SUPPL. 1 , pp. 198-204
    • Dixon, J.S.1
  • 56
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • Honig B., Nicholls A. Classical electrostatics in biology and chemistry. Science. 268:1995;1144-1149.
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 57
    • 0035971738 scopus 로고    scopus 로고
    • A smooth permitivity function for Poisson-Boltzman solvation methods
    • Grant J.A., et al. A smooth permitivity function for Poisson-Boltzman solvation methods. J. Comp. Chem. 22:2001;608-640.
    • (2001) J. Comp. Chem. , vol.22 , pp. 608-640
    • Grant, J.A.1
  • 58
    • 0032939345 scopus 로고    scopus 로고
    • Ligand solvation in molecular docking
    • Shoichet B.K., et al. Ligand solvation in molecular docking. Proteins Struct. Funct. Genet. 34:1999;4-16.
    • (1999) Proteins Struct. Funct. Genet. , vol.34 , pp. 4-16
    • Shoichet, B.K.1
  • 59
    • 0032226476 scopus 로고    scopus 로고
    • Development of filter functions for protein-ligand docking
    • Stahl M., Bohm H.J. Development of filter functions for protein-ligand docking. J. Mol. Graph. Model. 16:1998;121-132.
    • (1998) J. Mol. Graph. Model. , vol.16 , pp. 121-132
    • Stahl, M.1    Bohm, H.J.2
  • 60
    • 0028057975 scopus 로고
    • Rational design of potent, bioavailable, nonpeptide cyclic ureas as HIV protease inhibitors
    • Lam P.Y.S., et al. Rational design of potent, bioavailable, nonpeptide cyclic ureas as HIV protease inhibitors. Science. 263:1994;380-384.
    • (1994) Science , vol.263 , pp. 380-384
    • Lam, P.Y.S.1
  • 61
    • 0021871375 scopus 로고
    • A computational procedure for determining energetically favourable binding sites on biologically important molecules
    • Goodford P.J. A computational procedure for determining energetically favourable binding sites on biologically important molecules. J. Med. Chem. 28:1985;849-857.
    • (1985) J. Med. Chem. , vol.28 , pp. 849-857
    • Goodford, P.J.1
  • 62
    • 0025916872 scopus 로고
    • Functionality maps of binding sites: A multiple copy simultaneous search method
    • Miranker A., Karplus M. Functionality maps of binding sites: a multiple copy simultaneous search method. Proteins Struct. Funct. Genet. 11:1991;29-34.
    • (1991) Proteins Struct. Funct. Genet. , vol.11 , pp. 29-34
    • Miranker, A.1    Karplus, M.2
  • 63
    • 0033047007 scopus 로고    scopus 로고
    • Superstar: A knowledge-based approach for identifying interaction sites on proteins
    • Verdonk M.L., et al. Superstar: a knowledge-based approach for identifying interaction sites on proteins. J. Mol. Biol. 289:1999;1093-1108.
    • (1999) J. Mol. Biol. , vol.289 , pp. 1093-1108
    • Verdonk, M.L.1
  • 64
    • 0035910596 scopus 로고    scopus 로고
    • Subnanomolar inhibitors from computer screening: A model study using human carbonic anhydrase II
    • Gruneberg S., et al. Subnanomolar inhibitors from computer screening: a model study using human carbonic anhydrase II. Angew. Chem. Int. Ed. Engl. 40:2001;389-393.
    • (2001) Angew. Chem. Int. Ed. Engl. , vol.40 , pp. 389-393
    • Gruneberg, S.1
  • 65
    • 0037161605 scopus 로고    scopus 로고
    • Molecular docking and high throughput screening for novel inhibitors of protein tyrosine phosphatase 1B
    • Doman T.N., et al. Molecular docking and high throughput screening for novel inhibitors of protein tyrosine phosphatase 1B. J. Med. Chem. 45:2002;2213-2221.
    • (2002) J. Med. Chem. , vol.45 , pp. 2213-2221
    • Doman, T.N.1
  • 66
    • 0001750717 scopus 로고    scopus 로고
    • New approach to molecular docking and its application to virtual screening of chemical databases
    • Baxter C.A., et al. New approach to molecular docking and its application to virtual screening of chemical databases. J. Chem. Inf. Comput. Sci. 40:2000;254-262.
    • (2000) J. Chem. Inf. Comput. Sci. , vol.40 , pp. 254-262
    • Baxter, C.A.1
  • 67
    • 0033133969 scopus 로고    scopus 로고
    • Structure-based discovery and in-parallel optimization of novel competitive inhibitors of thymidylate synthase
    • Tondi D., et al. Structure-based discovery and in-parallel optimization of novel competitive inhibitors of thymidylate synthase. Chem. Biol. 6:1999;319-331.
    • (1999) Chem. Biol. , vol.6 , pp. 319-331
    • Tondi, D.1
  • 68
    • 0033965389 scopus 로고    scopus 로고
    • Rational discovery of novel nuclear hormone receptor antagonists
    • Schapira M., et al. Rational discovery of novel nuclear hormone receptor antagonists. Proc. Natl. Acad. Sci. U. S. A. 97:2000;1008-1013.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 1008-1013
    • Schapira, M.1
  • 69
    • 0034628541 scopus 로고    scopus 로고
    • Successful virtual screening of a chemical database for farnesyltransferase inhibitor leads
    • Perola E., et al. Successful virtual screening of a chemical database for farnesyltransferase inhibitor leads. J. Med. Chem. 43:2000;401-408.
    • (2000) J. Med. Chem. , vol.43 , pp. 401-408
    • Perola, E.1
  • 70
    • 0034646180 scopus 로고    scopus 로고
    • Inhibitors of kinesin activity from structure-based computer screening
    • Hopkins S.C., et al. Inhibitors of kinesin activity from structure-based computer screening. Biochemistry. 39:2000;2805-2814.
    • (2000) Biochemistry , vol.39 , pp. 2805-2814
    • Hopkins, S.C.1
  • 71
    • 0034712714 scopus 로고    scopus 로고
    • Rational design of selective submicromolar inhibitors of Tritrichmonas foetus hypoxanthine-guanine-xanthine phosphoribosyltransferase
    • Aronov A.M., et al. Rational design of selective submicromolar inhibitors of Tritrichmonas foetus hypoxanthine-guanine-xanthine phosphoribosyltransferase. Biochemistry. 39:2000;4684-4691.
    • (2000) Biochemistry , vol.39 , pp. 4684-4691
    • Aronov, A.M.1
  • 72
    • 1642288258 scopus 로고    scopus 로고
    • Novel inhibitors of DNA gyrase: 3D structure based biased needle screening. Hit validation by biophysical methods, and 3D guided optimization. A promising alternative to random screening
    • Boehm H-J., et al. Novel inhibitors of DNA gyrase: 3D structure based biased needle screening. Hit validation by biophysical methods, and 3D guided optimization. A promising alternative to random screening. J. Med. Chem. 43:2000;2664-2674.
    • (2000) J. Med. Chem. , vol.43 , pp. 2664-2674
    • Boehm, H.-J.1
  • 73
    • 0033949057 scopus 로고    scopus 로고
    • Identification of ligands for RNA targets via structure-based virtual screening: HIV-1 TAR
    • Filikov A.V., et al. Identification of ligands for RNA targets via structure-based virtual screening: HIV-1 TAR. J. Comput.-Aided Mol. Design. 14:2000;593-610.
    • (2000) J. Comput.-Aided Mol. Design , vol.14 , pp. 593-610
    • Filikov, A.V.1


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