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Volumn 37, Issue 24, 1994, Pages 4130-4146

Molecular Similarity Indices in a Comparative Analysis (CoMSIA) of Drug Molecules To Correlate and Predict Their Biological Activity

Author keywords

[No Author keywords available]

Indexed keywords

17 HYDROXYPREGNENOLONE; ALDOSTERONE; ANDROSTANEDIOL; ANDROSTANOLONE; ANDROSTENEDIOL; ANDROSTENEDIONE; ANDROSTERONE; CORTICOSTERONE; CORTISONE; CORTODOXONE; DEOXYCORTICOSTERONE; ESTRADIOL; ESTRIOL; ESTRONE; ETIOCHOLANOLONE; HYDROCORTISONE; HYDROXYPROGESTERONE; PRASTERONE; PREGNENOLONE; PROGESTERONE; STEROID; TESTOSTERONE; THERMOLYSIN; TRANSCORTIN;

EID: 0027944195     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm00050a010     Document Type: Article
Times cited : (1790)

References (38)
  • 1
    • 85022438335 scopus 로고    scopus 로고
    • Different Approaches Toward an Automatic Alignment of Drug Molecules: Applications to Sterol Mimics, Thrombin and Thermolysin Inhibitors
    • press
    • Klebe, G.; Mietzner, T.; Weber, F. Different Approaches Toward an Automatic Alignment of Drug Molecules: Applications to Sterol Mimics, Thrombin and Thermolysin Inhibitors. J. Comput.-Aided Mol. Design, in press.
    • J. Comput.-Aided Mol. Design
    • Klebe, G.1    Mietzner, T.2    Weber, F.3
  • 2
    • 0028522365 scopus 로고
    • A Fast and Efficient Method to Generate Biologically Relevant Conformations
    • Klebe, G.; Mietzner, T.: A Fast and Efficient Method to Generate Biologically Relevant Conformations. J. Comput.-Aided Mol. Design 1994, 8, 583-606.
    • (1994) J. Comput.-Aided Mol. Design , vol.8 , pp. 583-606
    • Klebe, G.1    Mietzner, T.2
  • 3
    • 44949267284 scopus 로고
    • An Alternative Method for the Alignment of Molecular Structures: Maximizing Electrostatic and Steric Overlap
    • Kearsley, S. K.; Smith, G. M. An Alternative Method for the Alignment of Molecular Structures: Maximizing Electrostatic and Steric Overlap. Tetrahedron Comput. Method. 1990, 3, 615-633.
    • (1990) Tetrahedron Comput. Method. , vol.3 , pp. 615-633
    • Kearsley, S.K.1    Smith, G.M.2
  • 4
    • 0023751431 scopus 로고
    • Comparative Molecular Field Analysis (CoMFA). 1. Effect of Shape on Binding of Steroids to Carrier Proteins
    • Cramer, R. D., III; Patterson, D. E.; Bunce, J. D. Comparative Molecular Field Analysis (CoMFA). 1. Effect of Shape on Binding of Steroids to Carrier Proteins. J. Am. Chem. Soc. 1988, 110, 5959-5967.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 5959-5967
    • Cramer, R.D.1    Patterson, D.E.2    Bunce, J.D.3
  • 5
    • 0026777217 scopus 로고
    • Contribution of the Hydrophobic Effect to Globular Protein Stability
    • Pace, C. N. Contribution of the Hydrophobic Effect to Globular Protein Stability. J. Mol. Biol. 1992, 226, 29-35.
    • (1992) J. Mol. Biol. , vol.226 , pp. 29-35
    • Pace, C.N.1
  • 6
    • 0026076664 scopus 로고
    • Extracting Hydrophobic Free Energies from Experimental Data: Relationship to Protein Folding and Theoretical Models
    • Sharp, K. A.; Nicholls, A.; Friedman, R.; Honig, B. Extracting Hydrophobic Free Energies from Experimental Data: Relationship to Protein Folding and Theoretical Models. Biochemistry 1991, 30, 9686-9697.
    • (1991) Biochemistry , vol.30 , pp. 9686-9697
    • Sharp, K.A.1    Nicholls, A.2    Friedman, R.3    Honig, B.4
  • 7
    • 0027397374 scopus 로고
    • On the Prediction of Binding Properties of Drug Molecules by Comparative Molecular Field Analysis
    • Klebe, G.; Abraham, U. On the Prediction of Binding Properties of Drug Molecules by Comparative Molecular Field Analysis. J. Med. Chem. 1993, 36, 70-80.
    • (1993) J. Med. Chem. , vol.36 , pp. 70-80
    • Klebe, G.1    Abraham, U.2
  • 8
    • 0027080363 scopus 로고
    • KEY, LOCK, and LOCKSMITH: Complementary Hydrophathic Map Predictions of Drug Structure from a Known Receptor-Receptor Structure from Known Drugs
    • Kellogg, G. E.; Abraham, D. J. KEY, LOCK, and LOCKSMITH: Complementary Hydrophathic Map Predictions of Drug Structure from a Known Receptor-Receptor Structure from Known Drugs. J. Mol. Graph. 1992, 10, 212—217.
    • (1992) J. Mol. Graph. , vol.10 , pp. 212-217
    • Kellogg, G.E.1    Abraham, D.J.2
  • 9
    • 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. 1985, 28, 849-857.
    • (1985) J. Med. Chem. , vol.28 , pp. 849-857
    • Goodford, P.J.1
  • 10
    • 0028411658 scopus 로고
    • Molecular Lipophilicity Potential, a tools in 3D QSAR: Method and Applications
    • Gaiilard, P.; Carrupt, P. A.; Testa, B.; Boudon, A.: Molecular Lipophilicity Potential, a tools in 3D QSAR: Method and Applications. J. Comput.-Aided Mol. Design 1994, 8, 83—96.
    • (1994) J. Comput.-Aided Mol. Design , vol.8 , pp. 83-96
    • Gaiilard, P.1    Carrupt, P.A.2    Testa, B.3    Boudon, A.4
  • 11
    • 0028261516 scopus 로고
    • The Use of the GRID Program in the 3D QSAR Analysis of a Series of Calcium-Channel Agonists
    • Davis, A. M.; Gensmantel, N. P.; Johansson, E.; Marriott, D. P. The Use of the GRID Program in the 3D QSAR Analysis of a Series of Calcium-Channel Agonists. J. Med. Chem. 1994, 37, 963—972.
    • (1994) J. Med. Chem. , vol.37 , pp. 963-972
    • Davis, A.M.1    Gensmantel, N.P.2    Johansson, E.3    Marriott, D.P.4
  • 12
    • 0027232379 scopus 로고
    • Amino Acids Characterization of GRID and Multivariate Data Analysis
    • Cocchi, M.; Johansson, E. Amino Acids Characterization of GRID and Multivariate Data Analysis. Quant. Struct.-Act. Relat. 1993, 12, 1—8.
    • (1993) Quant. Struct.-Act. Relat. , vol.12 , pp. 1-8
    • Cocchi, M.1    Johansson, E.2
  • 13
    • 0000109766 scopus 로고
    • Direct Prediction of Linear Free Energy Substituent Effects from 3D Structures using Comparative Molecular Field Analysis. 1. Electronic Effects of Substituted Benzoid Acids
    • Kim, K. H.; Martin, Y. C. Direct Prediction of Linear Free Energy Substituent Effects from 3D Structures using Comparative Molecular Field Analysis. 1. Electronic Effects of Substituted Benzoid Acids. J. Org. Chem. 1991, 56, 2723-2729.
    • (1991) J. Org. Chem. , vol.56 , Issue.1 , pp. 2723-2729
    • Kim, K.H.1    Martin, Y.C.2
  • 14
    • 0025816211 scopus 로고
    • Direct Prediction of Dissociation Constants (pKJ of Clonidine-like Imidazoles, 2-substituted Imidazoles and l-Methyl-2-substituted-imidazoles from 3D Structures using a Comparative Molecular Field Analysis (CoMFA)
    • Kim, K. H.; Martin, Y. C. Direct Prediction of Dissociation Constants (pKJ of Clonidine-like Imidazoles, 2-substituted Imidazoles and l-Methyl-2-substituted-imidazoles from 3D Structures using a Comparative Molecular Field Analysis (CoMFA). J. Med. Chem. 1991, 34, 2056-2060.
    • (1991) J. Med. Chem. , vol.34 , pp. 2056-2060
    • Kim, K.H.1    Martin, Y.C.2
  • 15
    • 0026636862 scopus 로고
    • 3D-Quantitative Structure Activity Relationships: Description of Electronic Effects directly from 3D Structures using a GRID-Comparative Molecular Field Analysis (CoMFA) Approach
    • Kim, K. H. 3D-Quantitative Structure Activity Relationships: Description of Electronic Effects directly from 3D Structures using a GRID-Comparative Molecular Field Analysis (CoMFA) Approach. Quant. Struct.-Act. Relat. 1992, 11, 127—134.
    • (1992) Quant. Struct.-Act. Relat. , vol.11 , pp. 127-134
    • Kim, K.H.1
  • 16
    • 0026781450 scopus 로고
    • 3D-Quantitative Structure Activity Relationships: Nonlinear Dependence Described directly from 3D Structures using a GRID-Comparative Molecular Field Analysis (CoMFA) Approach
    • Kim, K. H. 3D-Quantitative Structure Activity Relationships: Nonlinear Dependence Described directly from 3D Structures using a GRID-Comparative Molecular Field Analysis (CoMFA) Approach. Quant. Struct.-Act. Relat. 1992, 11, 453—460.
    • (1992) Quant. Struct.-Act. Relat. , vol.11 , pp. 453-460
    • Kim, K.H.1
  • 17
    • 0011119190 scopus 로고
    • Structural Alignment of Molecules
    • Kubinyi, H., Ed.; ESCOM: Leiden
    • Klebe, G. Structural Alignment of Molecules. In 3D QSAR in Drug Design; Kubinyi, H., Ed.; ESCOM: Leiden, 1993: pp 173-199.
    • (1993) 3D QSAR in Drug Design , pp. 173-199
    • Klebe, G.1
  • 18
    • 0002165646 scopus 로고
    • CoMFA: Scope and Limitations
    • Kubinyi, H., Ed.; ESCOM: Leiden
    • Folkers, G.; Merz, A.; Rognan, D. CoMFA: Scope and Limitations. In 3D QSAR in Drug Design; Kubinyi, H., Ed.; ESCOM: Leiden, 1993; pp 583-618.
    • (1993) 3D QSAR in Drug Design , pp. 583-618
    • Folkers, G.1    Merz, A.2    Rognan, D.3
  • 19
    • 0003146832 scopus 로고
    • The Developing Practice of Comparative Molecular Field Analysis
    • Kubinyi, H., Ed.; ESCOM: Leiden
    • Cramer, R. D., III; DePriest, S. A.; Patterson, D. E.; Hecht, P. The Developing Practice of Comparative Molecular Field Analysis. In 3D QSAR in Drug Design; Kubinyi, H., Ed.; ESCOM: Leiden, 1993; pp 443-485.
    • (1993) 3D QSAR in Drug Design , pp. 443-485
    • Cramer, R.D.1    DePriest, S.A.2    Patterson, D.E.3    Hecht, P.4
  • 20
    • 0024154259 scopus 로고
    • Multivariate Data Analysis and Experimental Design in Biomedical Research
    • Stahle, L.; Wold, S.: Multivariate Data Analysis and Experimental Design in Biomedical Research. Progr. Med. Chem. 1988, 25, 292-334.
    • (1988) Progr. Med. Chem. , vol.25 , pp. 292-334
    • Stahle, L.1    Wold, S.2
  • 21
    • 0027518573 scopus 로고
    • Structure-Activity Relationships from Molecular Similarity Matrices
    • Good, A. C.; So, S.-S.; Richards, W. G. Structure-Activity Relationships from Molecular Similarity Matrices. J. Med. Chem. 1993, 36, 433-438.
    • (1993) J. Med. Chem. , vol.36 , pp. 433-438
    • Good, A.C.1    So, S.-S.2    Richards, W.G.3
  • 23
    • 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
  • 24
    • 0024716284 scopus 로고
    • Atomic Physicochemical Parameters for Three Dimensional Structure Directed Quantitative Structure-Activity Relationships. 4. Additional Parameters for Hydrophobic and Dispersive Interactions and Their Application for an Automated Superposition of Certain Naturally Occurring Nucleoside Antibiotics
    • Viswanadhan, V. N.; Ghose, A. K.; Revankar, G. R.; Robins, R. K.: Atomic Physicochemical Parameters for Three Dimensional Structure Directed Quantitative Structure-Activity Relationships. 4. Additional Parameters for Hydrophobic and Dispersive Interactions and Their Application for an Automated Superposition of Certain Naturally Occurring Nucleoside Antibiotics. J. Chem. Inf. Comput. Sci. 1989, 29, 163-172.
    • (1989) J. Chem. Inf. Comput. Sci. , vol.29 , pp. 163-172
    • Viswanadhan, V.N.1    Ghose, A.K.2    Revankar, G.R.3    Robins, R.K.4
  • 25
    • 0027672324 scopus 로고
    • Sample-distance Partial Least-Squares: PLS optimized for many Variables, with Application to CoMFA
    • Bush, B. L.; Nachbar, R. B., Jr.: Sample-distance Partial Least-Squares: PLS optimized for many Variables, with Application to CoMFA. J. Comput.-Aided Mol. Design 1993, 7, 587—619.
    • (1993) J. Comput.-Aided Mol. Design , vol.7 , pp. 587-619
    • Bush, B.L.1    Nachbar, R.B.2
  • 26
    • 0027183015 scopus 로고
    • 3DQSAR 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.; Marshall, G. R. 3DQSAR 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. 1993, 115, 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
  • 28
    • 0024595625 scopus 로고
    • Computed Automated Structure Evaluation (CASE): A Study of Inhibition of the Thermolysin Enzyme
    • Klopman, G.; Bendale, R. D. Computed Automated Structure Evaluation (CASE): A Study of Inhibition of the Thermolysin Enzyme. J. Theor. Biol. 1989, 136, 67-77.
    • (1989) J. Theor. Biol. , vol.136 , pp. 67-77
    • Klopman, G.1    Bendale, R.D.2
  • 29
    • 0027308233 scopus 로고
    • Three-Dimensional Quantitative Structure-Activity Relationship of Angiotensin-Converting Enzyme and Thermolysin Inhibitors. 2. A Comparison of CoMFA Models Incorporating Molecular Orbital Fields and Desolvation Free Energies Based on Active-Analog and Complementary-Receptor-Field Alignment Rules
    • Waller, C. L.; Marshall, G. R. Three-Dimensional Quantitative Structure-Activity Relationship of Angiotensin-Converting Enzyme and Thermolysin Inhibitors. 2. A Comparison of CoMFA Models Incorporating Molecular Orbital Fields and Desolvation Free Energies Based on Active-Analog and Complementary-Receptor-Field Alignment Rules. J. Med. Chem. 1993, 36, 2390-2403.
    • (1993) J. Med. Chem. , vol.36 , Issue.2 , pp. 2390-2403
    • Waller, C.L.1    Marshall, G.R.2
  • 30
    • 33845280830 scopus 로고
    • Structural Basis of the Action of Thermolysin and Related Zinc Peptidases
    • Matthews, B. W. Structural Basis of the Action of Thermolysin and Related Zinc Peptidases. Acc. Chem. Res. 1988, 21, 333-340.
    • (1988) Acc. Chem. Res. , vol.21 , pp. 333-340
    • Matthews, B.W.1
  • 31
    • 0023040231 scopus 로고
    • Crystallographic structural analysis of phosphoramidates as inhibitors and transition-state analogs of uhermolysin
    • Tronrud, D. E.; Monzingo, A. F.; Matthews, B. W. Crystallographic structural analysis of phosphoramidates as inhibitors and transition-state analogs of uhermolysin. Eur. J. Biochem. 1986, 157, 261-268.
    • (1986) Eur. J. Biochem. , vol.157 , pp. 261-268
    • Tronrud, D.E.1    Monzingo, A.F.2    Matthews, B.W.3
  • 32
    • 0023839658 scopus 로고
    • The Binding of 1-ValyI-ltryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of a Product of Peptide Hvdrolysis
    • Holden, H. M.; Matthews, B. W. The Binding of 1-ValyI-ltryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of a Product of Peptide Hvdrolysis. J. Biol. Chem. 1988, 263, 3256-3260.
    • (1988) J. Biol. Chem. , vol.263 , pp. 3256-3260
    • Holden, H.M.1    Matthews, B.W.2
  • 33
    • 0023121559 scopus 로고
    • Structures of Two Thermolysin-Inhibitor Complexes That Differ by a Single Hydrogen Bond
    • Tronrud, D. E.; Holden, H. M.; Matthews, B. W. Structures of Two Thermolysin-Inhibitor Complexes That Differ by a Single Hydrogen Bond. Science 1987, 235, 571-574.
    • (1987) Science , vol.235 , pp. 571-574
    • Tronrud, D.E.1    Holden, H.M.2    Matthews, B.W.3
  • 34
    • 0023105721 scopus 로고
    • Evaluation of Intrinsic Binding Energy from a Hydrogen Bonding group in an Enzyme Inhibitor
    • Bartlett, P. A.; Marlowe, C. K. Evaluation of Intrinsic Binding Energy from a Hydrogen Bonding group in an Enzyme Inhibitor. Science 1987, 235, 569—571.
    • (1987) Science , vol.235 , pp. 569-571
    • Bartlett, P.A.1    Marlowe, C.K.2
  • 35
    • 0026093346 scopus 로고
    • Differential Binding Energy: A Detailed Evaluation of the Influence of Hydrogen-Bonding and Hydrophobic Groups on the Inhibition of Thermolysin by Phosphorus-Containing Inhibitors
    • Morgan, B. P.; Scholtz, J. M.; Ballinger, M. D.; Zipkin, I. D.; Bartlett, P. A.: Differential Binding Energy: A Detailed Evaluation of the Influence of Hydrogen-Bonding and Hydrophobic Groups on the Inhibition of Thermolysin by Phosphorus-Containing Inhibitors. J. Am. Chem. Soc. 1991, 113, 297-307.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 297-307
    • Morgan, B.P.1    Scholtz, J.M.2    Ballinger, M.D.3    Zipkin, I.D.4    Bartlett, P.A.5
  • 37
    • 85022452020 scopus 로고    scopus 로고
    • available from Biosym Technologies, Inc., 9685 Scranton Road, San Diego, CA
    • DELPHI program, available from Biosym Technologies, Inc., 9685 Scranton Road, San Diego, CA 92121-2777.
    • DELPHI program , pp. 92121-92777
  • 38
    • 38149145182 scopus 로고
    • SHADEMOL: An Algorithm for Presentation of Three-dimensional Structures on a Laser Printer Using Depth-Shading
    • Hahn, M.; Wipke, W. T. SHADEMOL: An Algorithm for Presentation of Three-dimensional Structures on a Laser Printer Using Depth-Shading. Tetrahedron Comput. Method. 1 1988, 81-86.
    • (1988) Tetrahedron Comput. Method. , vol.1 , pp. 81-86
    • Hahn, M.1    Wipke, W.T.2


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