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Volumn 10, Issue 4, 2000, Pages 401-404

Recent advances in structure-based rational drug design

Author keywords

[No Author keywords available]

Indexed keywords

ALGORITHM; COMPLEX FORMATION; DRUG DESIGN; DRUG PROTEIN BINDING; PRIORITY JOURNAL; SHORT SURVEY;

EID: 0033915982     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(00)00105-6     Document Type: Review
Times cited : (192)

References (33)
  • 1
    • 0033974667 scopus 로고    scopus 로고
    • Accommodating protein flexibility in computational drug design
    • Carlson H.A., McCammon J.A. Accommodating protein flexibility in computational drug design. Mol Pharmacol. 57:2000;213-218.
    • (2000) Mol Pharmacol , vol.57 , pp. 213-218
    • Carlson, H.A.1    McCammon, J.A.2
  • 2
    • 0001105311 scopus 로고    scopus 로고
    • Method for including the dynamic fluctuations of a protein in computer-aided drug design
    • Carlson H.A., Masukawa K.M., McCammon J.A. Method for including the dynamic fluctuations of a protein in computer-aided drug design. J Phys Chem A. 103:1999;10 213-10 219.
    • (1999) J Phys Chem a , vol.103 , pp. 10213-10219
    • Carlson, H.A.1    Masukawa, K.M.2    McCammon, J.A.3
  • 3
    • 0033135477 scopus 로고    scopus 로고
    • Docking of flexible ligands to flexible receptors in solution by molecular dynamics simulation
    • Mangoni M., Roccatano D., Nola A.D. Docking of flexible ligands to flexible receptors in solution by molecular dynamics simulation. Proteins. 35:1999;153-162.
    • (1999) Proteins , vol.35 , pp. 153-162
    • Mangoni, M.1    Roccatano, D.2    Nola, A.D.3
  • 4
    • 0032738842 scopus 로고    scopus 로고
    • Evaluation of the FLEXX incremental construction algorithm for protein-ligand docking
    • Kramer B., Rarey M., Lengauer T. Evaluation of the FLEXX incremental construction algorithm for protein-ligand docking. Proteins. 37:1999;228-241.
    • (1999) Proteins , vol.37 , pp. 228-241
    • Kramer, B.1    Rarey, M.2    Lengauer, T.3
  • 5
    • 0032718788 scopus 로고    scopus 로고
    • The sensitivity of the results of molecular docking to induced fit effects: Application to thrombin, thermolysin and neuraminidase
    • Murray C.W., Baxter C.A., Frenkel A.D. The sensitivity of the results of molecular docking to induced fit effects: application to thrombin, thermolysin and neuraminidase. J Comput Aided Mol Des. 13:1999;547-562.
    • (1999) J Comput Aided Mol des , vol.13 , pp. 547-562
    • Murray, C.W.1    Baxter, C.A.2    Frenkel, A.D.3
  • 6
    • 0032708785 scopus 로고    scopus 로고
    • Efficacy and selectivity in flexible database docking
    • Knegtel R.M.A., Wagener M. Efficacy and selectivity in flexible database docking. Proteins. 37:1999;334-345.
    • (1999) Proteins , vol.37 , pp. 334-345
    • Knegtel, R.M.A.1    Wagener, M.2
  • 7
    • 0032899364 scopus 로고    scopus 로고
    • The effect of multiple binding modes on empirical modeling of ligand docking to proteins
    • Brem R., Dill K.A. The effect of multiple binding modes on empirical modeling of ligand docking to proteins. Protein Sci. 8:1999;1134-1143.
    • (1999) Protein Sci , vol.8 , pp. 1134-1143
    • Brem, R.1    Dill, K.A.2
  • 8
    • 0032961895 scopus 로고    scopus 로고
    • The particle concept: Placing discrete water molecules during protein-ligand docking predictions
    • Rarey M., Kramer B., Lengauer T. The particle concept: placing discrete water molecules during protein-ligand docking predictions. Proteins. 34:1999;17-28.
    • (1999) Proteins , vol.34 , pp. 17-28
    • Rarey, M.1    Kramer, B.2    Lengauer, T.3
  • 9
    • 0033214412 scopus 로고    scopus 로고
    • Exhaustive docking of molecular fragments with electrostatic solvation
    • Majeux N., Scarsi M., Apostolakis J., Ehrhardt C., Caflisch A. Exhaustive docking of molecular fragments with electrostatic solvation. Proteins. 37:1999;88-105.
    • (1999) Proteins , vol.37 , pp. 88-105
    • Majeux, N.1    Scarsi, M.2    Apostolakis, J.3    Ehrhardt, C.4    Caflisch, A.5
  • 10
    • 0032993815 scopus 로고    scopus 로고
    • Scoring functions: A view from the bench
    • Tame J.R.H. Scoring functions: a view from the bench. J Comput Aided Mol Des. 13:1999;99-108.
    • (1999) J Comput Aided Mol des , vol.13 , pp. 99-108
    • Tame, J.R.H.1
  • 11
    • 0034645763 scopus 로고    scopus 로고
    • Knowledge-based scoring function to predict protein-ligand interactions
    • Gohlke H., Hendlich M., Klebe G. 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    Hendlich, M.2    Klebe, G.3
  • 12
    • 0033545622 scopus 로고    scopus 로고
    • A general and fast scoring function for protein-ligand interactions: A simplified potential approach
    • Muegge I., Martin Y.C. A general and fast scoring function for protein-ligand interactions: a simplified potential approach. J Med Chem. 42:1999;791-804.
    • (1999) J Med Chem , vol.42 , pp. 791-804
    • Muegge, I.1    Martin, Y.C.2
  • 13
    • 0000823044 scopus 로고    scopus 로고
    • BLEEP - potential of mean force describing protein-ligand interactions: I. Generating potential
    • Mitchell J.B.O., Laskowski R.A., Alex A., Thornton J.M. BLEEP - potential of mean force describing protein-ligand interactions: I. Generating potential. J Comput Chem. 20:1999;1165-1176.
    • (1999) J Comput Chem , vol.20 , pp. 1165-1176
    • Mitchell, J.B.O.1    Laskowski, R.A.2    Alex, A.3    Thornton, J.M.4
  • 14
    • 0000823044 scopus 로고    scopus 로고
    • BLEEP - potential of mean force describing protein-ligand interactions: 11. Calculation of binding energies and comparison with experimental data
    • Mitchell J.B.O., Laskowski R.A., Alex A., Forster M.J., Thornton J.M. BLEEP - potential of mean force describing protein-ligand interactions: 11. Calculation of binding energies and comparison with experimental data. J Comput Chem. 20:1999;1165-1176.
    • (1999) J Comput Chem , vol.20 , pp. 1165-1176
    • Mitchell, J.B.O.1    Laskowski, R.A.2    Alex, A.3    Forster, M.J.4    Thornton, J.M.5
  • 15
    • 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 Des. 13:1999;435-451.
    • (1999) J Comput Aided Mol des , vol.13 , pp. 435-451
    • Liu, M.1    Wang, S.2
  • 16
    • 0345483185 scopus 로고    scopus 로고
    • Prodock: Software package for protein modeling and docking
    • Trosset J.Y., Scheraga H.A. Prodock: software package for protein modeling and docking. J Comput Chem. 20:1999;412-427.
    • (1999) J Comput Chem , vol.20 , pp. 412-427
    • Trosset, J.Y.1    Scheraga, H.A.2
  • 17
    • 0032840569 scopus 로고    scopus 로고
    • DREAM++: Flexible docking program for virtual combinatorial libraries
    • Makino S., Ewing T.J.A., Kuntz I.D. DREAM++: flexible docking program for virtual combinatorial libraries. J Comput Aided Mol Des. 13:1999;513-532.
    • (1999) J Comput Aided Mol des , vol.13 , pp. 513-532
    • Makino, S.1    Ewing, T.J.A.2    Kuntz, I.D.3
  • 18
    • 0033044392 scopus 로고    scopus 로고
    • Integration of combinatorial chemistry and structure based drug design
    • Antel J. Integration of combinatorial chemistry and structure based drug design. Curr Opin Drug Discov Dev. 2:1999;224-233.
    • (1999) Curr Opin Drug Discov Dev , vol.2 , pp. 224-233
    • Antel, J.1
  • 19
    • 0033559918 scopus 로고    scopus 로고
    • Hydrogen bonding, hydrophobic interactions, and failure of the rigid receptor hypothesis
    • Davis A.M., Teague S.J. Hydrogen bonding, hydrophobic interactions, and failure of the rigid receptor hypothesis. Angew Chem Int Ed Engl. 38:1999;736-749.
    • (1999) Angew Chem Int Ed Engl , vol.38 , pp. 736-749
    • Davis, A.M.1    Teague, S.J.2
  • 20
    • 0033574397 scopus 로고    scopus 로고
    • The discovery of steroids and other novel FKBP inhibitors using a molecular docking program
    • Burkhard P., Hommel U., Sanner M., Walkinshaw M.D. The discovery of steroids and other novel FKBP inhibitors using a molecular docking program. J Mol Biol. 287:1999;853-858.
    • (1999) J Mol Biol , vol.287 , pp. 853-858
    • Burkhard, P.1    Hommel, U.2    Sanner, M.3    Walkinshaw, M.D.4
  • 21
    • 84991422777 scopus 로고    scopus 로고
    • DockCrunch on World Wide Web URL
    • DockCrunch on World Wide Web URL: http://www.protherics.com/crunch.
  • 22
    • 0033967525 scopus 로고    scopus 로고
    • Theoretical investigation of substrate specificity for cytochromes P450 IA2, P450 IID6 and P450 IIIA4
    • De Rienzo F., Fanelli F., Menziani M.C., De Benedetti P.G. Theoretical investigation of substrate specificity for cytochromes P450 IA2, P450 IID6 and P450 IIIA4. J Comput Aided Mol Des. 14:2000;93-116.
    • (2000) J Comput Aided Mol des , vol.14 , pp. 93-116
    • De Rienzo, F.1    Fanelli, F.2    Menziani, M.C.3    De Benedetti, P.G.4
  • 27
    • 0344731437 scopus 로고    scopus 로고
    • Structure-based design, synthesis, and X-ray crystallography of a high-affinity antagonist of the Grb2-SH2 domain containing an asparagine mimetic
    • Furet P., García-Echeverría C., Gay B., Schoepfer J., Zeller M., Rahuel J. Structure-based design, synthesis, and X-ray crystallography of a high-affinity antagonist of the Grb2-SH2 domain containing an asparagine mimetic. J Med Chem. 42:1999;2358-2363.
    • (1999) J Med Chem , vol.42 , pp. 2358-2363
    • Furet, P.1    García-Echeverría, C.2    Gay, B.3    Schoepfer, J.4    Zeller, M.5    Rahuel, J.6
  • 30
    • 0033047131 scopus 로고    scopus 로고
    • Structure-based discovery of tipranavir disodium (PNU-140690E): A potent, oral bio-available, non-peptidic HIV protease inhibitor
    • Thaisrivongs S., Strohbach J.W. Structure-based discovery of tipranavir disodium (PNU-140690E): a potent, oral bio-available, non-peptidic HIV protease inhibitor. Biopolymers. 51:1999;51-58.
    • (1999) Biopolymers , vol.51 , pp. 51-58
    • Thaisrivongs, S.1    Strohbach, J.W.2
  • 33
    • 0034629461 scopus 로고    scopus 로고
    • Re-engineering of human urokinase provides a system for structure-based drug design at high resolution and reveals a novel structural subsite
    • Nienaber V., Wang J., Davidson D., Henkin J. Re-engineering of human urokinase provides a system for structure-based drug design at high resolution and reveals a novel structural subsite. J Biol Chem. 275:2000;7239-7248.
    • (2000) J Biol Chem , vol.275 , pp. 7239-7248
    • Nienaber, V.1    Wang, J.2    Davidson, D.3    Henkin, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.