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Volumn 9--11, Issue , 1998, Pages 85-98

Rapid Estimation of Relative Binding Affinities of Enzyme Inhibitors

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EID: 1542739327     PISSN: 09282866     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (7)

References (36)
  • 5
    • 0024365686 scopus 로고
    • Free energy pertubation simulation of the inhibition of thermolysin: Prediction of the free energy of binding of a new inhibitor
    • Merz, K.M., and Kollman, P.A., Free energy pertubation simulation of the inhibition of thermolysin: prediction of the free energy of binding of a new inhibitor, J. Am. Chem. Soc., 111 (1989) 5649-5658.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 5649-5658
    • Merz, K.M.1    Kollman, P.A.2
  • 6
    • 0025720738 scopus 로고
    • Relative free energy differences in the binding free energies of human immunodeficiency virus 1 protease inhibitors: A thermodynamic cycle perturbation approach
    • Rami Reddy, M., Viswanadhan, V.N. and Weinstein, J.N., Relative free energy differences in the binding free energies of human immunodeficiency virus 1 protease inhibitors: A thermodynamic cycle perturbation approach, Proc. Natl. Acad. Sci. USA, 88 (1991) 10287-10291.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10287-10291
    • Rami Reddy, M.1    Viswanadhan, V.N.2    Weinstein, J.N.3
  • 7
    • 0026047763 scopus 로고
    • Determination of the relative binding free energies of peptide inhibitors to the HIV-1 protease
    • Ferguson, D.M., Radmer, R.J. and Kollman, P.A., Determination of the relative binding free energies of peptide inhibitors to the HIV-1 protease, J. Med. Chem., 34 (1991) 2654-2659.
    • (1991) J. Med. Chem. , vol.34 , pp. 2654-2659
    • Ferguson, D.M.1    Radmer, R.J.2    Kollman, P.A.3
  • 8
    • 0026503819 scopus 로고
    • Application of free energy simulations to the binding of a transition state analogue inhibitor to HIV protease
    • Tropshaw, A.J. and Hermans, J., Application of free energy simulations to the binding of a transition state analogue inhibitor to HIV protease, Prot. Eng., 5 (1992) 29-33.
    • (1992) Prot. Eng. , vol.5 , pp. 29-33
    • Tropshaw, A.J.1    Hermans, J.2
  • 9
    • 0026717932 scopus 로고
    • Free energy perturbation studies on inhibitor binding to HIV-1 protease
    • Rao, B.G., Tilton, R.F. and Singh, U.C., Free energy perturbation studies on inhibitor binding to HIV-1 protease, J. Am. Chem. Soc., 114 (1992) 4447-4452.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 4447-4452
    • Rao, B.G.1    Tilton, R.F.2    Singh, U.C.3
  • 10
    • 0040546788 scopus 로고
    • Calculation of relative differences in the binding free energies of HIV-1 protease inhibitors: A thermodynamic cycle perturbation approach
    • Rami Reddy, M., Varney, M.D., Kalish, V., Viswanadhan, V.N. and Appelt, K., Calculation of relative differences in the binding free energies of HIV-1 protease inhibitors: A thermodynamic cycle perturbation approach, J. Med. Chem., 114 (1994) 10117-10122.
    • (1994) J. Med. Chem. , vol.114 , pp. 10117-10122
    • Rami Reddy, M.1    Varney, M.D.2    Kalish, V.3    Viswanadhan, V.N.4    Appelt, K.5
  • 11
    • 0026696669 scopus 로고
    • Definition and display of steric, hydrophobic, and hydrogen-bonding properties of ligand binding sites in proteins using Lee and Richards accessible surface: Validation of a high-resolution graphical tool for drug design
    • Bohacek, R.S. and McMartin, C., Definition and display of steric, hydrophobic, and hydrogen-bonding properties of ligand binding sites in proteins using Lee and Richards accessible surface: Validation of a high-resolution graphical tool for drug design, J. Med. Chem., 35 (1992) 1671-1684.
    • (1992) J. Med. Chem. , vol.35 , pp. 1671-1684
    • Bohacek, R.S.1    McMartin, C.2
  • 13
    • 0021871375 scopus 로고
    • A computational procedure for determining energetically favorable binding sites on biologically important macromolecules
    • Goodford, P.J., A computational procedure for determining energetically favorable binding sites on biologically important macromolecules, J. Med. Chem., 28 (1985) 849-857.
    • (1985) J. Med. Chem. , vol.28 , pp. 849-857
    • Goodford, P.J.1
  • 14
    • 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
    • Boehm, H.-J., The development of a simple empirical scoring function to estimate the binding constant for 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
    • Boehm, H.-J.1
  • 15
    • 0026438932 scopus 로고
    • Molecular mechanics analysis of inhibitor binding to HIV-1 protease
    • Sansom, C.E., Wu, J. and Weber, I.T., Molecular mechanics analysis of inhibitor binding to HIV-1 protease, Protein Eng., 5 (1992) 659-667.
    • (1992) Protein Eng. , vol.5 , pp. 659-667
    • Sansom, C.E.1    Wu, J.2    Weber, I.T.3
  • 17
    • 0027135793 scopus 로고
    • Structure-based design of inhibitors of purine nucleoside phosphorylase. 3. 9-arylmenthyl derivatives of 9-deazaguanine substituted on the methylene-group
    • Erion, M.D., Montgomery, J.A., Niwas, S., Rose, J.D., Ananthan, S., Allen, M., Secrist, J.A., Babu, S.Y., Bugg, C.E., Guida, W.C. and Ealick, S.E., Structure-based design of inhibitors of purine nucleoside phosphorylase. 3. 9-arylmenthyl derivatives of 9-deazaguanine substituted on the methylene-group, J. Med. Chem., 36 (1993) 3771-3783.
    • (1993) J. Med. Chem. , vol.36 , pp. 3771-3783
    • Erion, M.D.1    Montgomery, J.A.2    Niwas, S.3    Rose, J.D.4    Ananthan, S.5    Allen, M.6    Secrist, J.A.7    Babu, S.Y.8    Bugg, C.E.9    Guida, W.C.10    Ealick, S.E.11
  • 18
    • 0027235716 scopus 로고
    • Structure-based design of inhibitors of purine nucleoside phosphorylase. 2. 9-alicyclic and 9-heteroalicyclic derivatives of 9-deazaguanine
    • Secrist, J.A.I., Niwas, S., Rose, J.D., Babu, S.Y., Bugg, C.E., Erion, M.D., Guida, W.C., Ealick, S.E. and Montgomery, J.A., Structure-based design of inhibitors of purine nucleoside phosphorylase. 2. 9-alicyclic and 9-heteroalicyclic derivatives of 9-deazaguanine, J. Med. Chem., 36 (1993) 1847-1854.
    • (1993) J. Med. Chem. , vol.36 , pp. 1847-1854
    • Secrist, J.A.I.1    Niwas, S.2    Rose, J.D.3    Babu, S.Y.4    Bugg, C.E.5    Erion, M.D.6    Guida, W.C.7    Ealick, S.E.8    Montgomery, J.A.9
  • 19
    • 13344282748 scopus 로고    scopus 로고
    • An approach to rapid estimation of relative binding affinities of enzyme inhibitors: Application to peptidomimetic inhibitors of the human immunodeficiency virus type 1 protease
    • Viswanadhan, V.N., Rami Redy, M, Wlodawer, A., Varney, M.D. and Weinstein, J.N., An approach to rapid estimation of relative binding affinities of enzyme inhibitors: application to peptidomimetic inhibitors of the human immunodeficiency virus type 1 protease, J. Med. Chem., 39 (1996) 705-712.
    • (1996) J. Med. Chem. , vol.39 , pp. 705-712
    • Viswanadhan, V.N.1    Rami Redy, M.2    Wlodawer, A.3    Varney, M.D.4    Weinstein, J.N.5
  • 21
    • 0023751431 scopus 로고
    • Comparative molecular field analysis (CoMFA). I. Effect of shape on binding of steroids to carrier proteins
    • Cramer, R.D., Patterson, D.E. and Bunce, J.D., Comparative molecular field analysis (CoMFA). I. Effect of shape on binding of steroids to carrier proteins, J. Am. Chem. Soc., 110 (1988) 5959-5967.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 5959-5967
    • Cramer, R.D.1    Patterson, D.E.2    Bunce, J.D.3
  • 22
    • 0025286882 scopus 로고
    • Mapping the binding site of the nucleoside transporter protein: A 3D-QSAR study
    • Viswanadhan, V.N., Gnose, A.K. and Weinstein,J.N., Mapping the binding site of the nucleoside transporter protein: A 3D-QSAR study, Biochim. Biophys. Acta, 1039 (1991) 356-366.
    • (1991) Biochim. Biophys. Acta , vol.1039 , pp. 356-366
    • Viswanadhan, V.N.1    Gnose, A.K.2    Weinstein, J.N.3
  • 23
    • 0027266850 scopus 로고
    • Mechanistic interpretation of the genotoxicity of nitrofurans (antibacterial agents) using quantitative structure-activity relationships and comparative molecular field analysis
    • Debnath, A.K.,Hansch, C., Kim, K.H. and Martin, Y.C., Mechanistic interpretation of the genotoxicity of nitrofurans (antibacterial agents) using quantitative structure-activity relationships and comparative molecular field analysis, J. Med. Chem., 36 (1993) 1007-1016.
    • (1993) J. Med. Chem. , vol.36 , pp. 1007-1016
    • Debnath, A.K.1    Hansch, C.2    Kim, K.H.3    Martin, Y.C.4
  • 24
    • 0027183015 scopus 로고
    • 3D QSAR of angiotensin-converting enzyme and thermolysin inhibitors: A comparison of CoMFA models based on deduced and experimentally determined active site geometries
    • Depriest, S.A., Mayer, D., Naylor, C.B. and Marshall, G.R., 3D QSAR of angiotensin-converting enzyme and thermolysin inhibitors: A comparison of CoMFA models based on deduced and experimentally determined active site geometries, J. Am. Chem. Soc., 115 (1993) 5372-5384.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 5372-5384
    • Depriest, S.A.1    Mayer, D.2    Naylor, C.B.3    Marshall, G.R.4
  • 26
    • 0027548454 scopus 로고
    • A fast new approach to pharmacophore mapping and its application to dopaminergic and benzodiazepine agonists
    • Martin, Y.C., A fast new approach to pharmacophore mapping and its application to dopaminergic and benzodiazepine agonists, J. Comput.-Aided Mol. Design, 7 (1993) 83-102.
    • (1993) J. Comput.-Aided Mol. Design , vol.7 , pp. 83-102
    • Martin, Y.C.1
  • 27
    • 0027762073 scopus 로고
    • Three-dimensional QSAR of human immunodeficiency virus (I) protease inhibitors: 1. A study employing experimentally-determined alignment rules
    • Waller, C., Oprea, T.I., Giolitti, A. and Marshall, G.R., Three-dimensional QSAR of human immunodeficiency virus (I) protease inhibitors: 1. A study employing experimentally-determined alignment rules, J. Med. Chem., 36 (1993) 4152-4160.
    • (1993) J. Med. Chem. , vol.36 , pp. 4152-4160
    • Waller, C.1    Oprea, T.I.2    Giolitti, A.3    Marshall, G.R.4
  • 28
    • 0027978699 scopus 로고
    • 3D-QSAR of human immunodeficiency virus (I) protease inhibitors III: Interpretation of CoMFA results
    • Oprea, T.I., Waller, C.L. and Marshall, G.R., 3D-QSAR of human immunodeficiency virus (I) protease inhibitors III: Interpretation of CoMFA results, Drug Design and Discovery, 12 (1994) 29-51.
    • (1994) Drug Design and Discovery , vol.12 , pp. 29-51
    • Oprea, T.I.1    Waller, C.L.2    Marshall, G.R.3
  • 31
    • 0029995624 scopus 로고    scopus 로고
    • VALIDATE: A new method for the receptor-based prediction of binding affinities of novel ligands
    • Head, R.D., Smythe, M.L., Oprea, T.I., Waller, C.L., Green, .S.M. and Marshall, G.R., 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    Smythe, M.L.2    Oprea, T.I.3    Waller, C.L.4    Green, S.M.5    Marshall, G.R.6
  • 32
    • 84988098098 scopus 로고
    • Atomic charges derived from electrostatic potentials: A detailed study
    • Chirlian, L.E. and Francl, M.M., Atomic charges derived from electrostatic potentials: A detailed study, J. Comp. Chem., 8 (1987) 894-905.
    • (1987) J. Comp. Chem. , vol.8 , pp. 894-905
    • Chirlian, L.E.1    Francl, M.M.2
  • 35
    • 45149145779 scopus 로고
    • Dielectric constant of SPC/E water
    • Rami Reddy, M. and Berkowitz, M., Dielectric constant of SPC/E water, Chem. Phys. Lett., 155 (1989) 173-176.
    • (1989) Chem. Phys. Lett. , vol.155 , pp. 173-176
    • Rami Reddy, M.1    Berkowitz, M.2
  • 36
    • 1542706555 scopus 로고    scopus 로고
    • Rapid estimation of relative binding affinities of enzyme inhibitors: Application to inhibitors of Fructose-1,6-bisphosphatase
    • to be submitted
    • Rami Reddy, M., Viswanadhan, V.N. and Erion, M.D., Rapid estimation of relative binding affinities of enzyme inhibitors: Application to inhibitors of Fructose-1,6-bisphosphatase, J. Med. Chem. (to be submitted).
    • J. Med. Chem.
    • Rami Reddy, M.1    Viswanadhan, V.N.2    Erion, M.D.3


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