메뉴 건너뛰기




Volumn 42, Issue 11, 1999, Pages 1908-1920

Quantitative structure-activity relationship of human neutrophil collagenase (MMP-8) inhibitors using comparative molecular field analysis and x-ray structure analysis

Author keywords

[No Author keywords available]

Indexed keywords

MATRIX METALLOPROTEINASE INHIBITOR; NEUTROPHIL COLLAGENASE; TETRAHYDROISOQUINOLINE DERIVATIVE; ZINC;

EID: 0033519654     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm980631s     Document Type: Article
Times cited : (92)

References (70)
  • 1
    • 0025847582 scopus 로고
    • Matrix metalloproteinases and their inhibitors in connective tissue remodeling
    • (a) Woessner, J. F., Jr. Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB J. 1991, 5, 2145-2154.
    • (1991) FASEB J. , vol.5 , pp. 2145-2154
    • Woessner J.F., Jr.1
  • 3
    • 0026903364 scopus 로고
    • The matrix metalloproteinases and their inhibitors
    • (c) Murphy, G.; Docherty, A. J. P. The matrix metalloproteinases and their inhibitors. A. J. Res. Cell. Mol. Biol. 1992, 7, 120-125.
    • (1992) A. J. Res. Cell. Mol. Biol. , vol.7 , pp. 120-125
    • Murphy, G.1    Docherty, A.J.P.2
  • 4
    • 0025230509 scopus 로고
    • Metalloproteinases and their inhibitors in matrix remodeling
    • (d) Matrisian, L. M. Metalloproteinases and their inhibitors in matrix remodeling. Trends Genet. 1990, 6, 121-125.
    • (1990) Trends Genet. , vol.6 , pp. 121-125
    • Matrisian, L.M.1
  • 5
    • 0027450277 scopus 로고
    • Metalloproteinases, tissue inhibitor, and proteoglycan fragments in knee synovial fluid in human osteoarthritis
    • Lohmander, L. S.; Hoerrner, L. A.; Lark, M. W. Metalloproteinases, tissue inhibitor, and proteoglycan fragments in knee synovial fluid in human osteoarthritis. Arthrit. Rheum. 1993, 36, 181-189.
    • (1993) Arthrit. Rheum. , vol.36 , pp. 181-189
    • Lohmander, L.S.1    Hoerrner, L.A.2    Lark, M.W.3
  • 6
    • 0026577352 scopus 로고
    • Proteinases in rheumatoid arthritis
    • Murphy, G.; Hembry, R. M. Proteinases in rheumatoid arthritis. J. Rheumatol. 1992, 19, 61-64.
    • (1992) J. Rheumatol. , vol.19 , pp. 61-64
    • Murphy, G.1    Hembry, R.M.2
  • 7
    • 0028895806 scopus 로고
    • Localization of tissue inhibitor of matrix metalloproteinases in Alzheimer's disease and normal brain
    • Peress, N.; Perillo, E.; Zucker, S. Localization of tissue inhibitor of matrix metalloproteinases in Alzheimer's disease and normal brain. J. Neuropathol. Exp. Neurol. 1995, 54, 16-22.
    • (1995) J. Neuropathol. Exp. Neurol. , vol.54 , pp. 16-22
    • Peress, N.1    Perillo, E.2    Zucker, S.3
  • 8
    • 0028324076 scopus 로고
    • The X-ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity
    • Bode, W.; Reinemer, P.; Huber, R.; Kleine, T.; Schnierer, S.; Tschesche, H. The X-ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity. EMBO J. 1994, 13, 1263-1269.
    • (1994) EMBO J. , vol.13 , pp. 1263-1269
    • Bode, W.1    Reinemer, P.2    Huber, R.3    Kleine, T.4    Schnierer, S.5    Tschesche, H.6
  • 9
    • 0018780188 scopus 로고
    • Design of potent reversible inhibitors for thermolysin. Peptides containing zinc coordinating ligands and their use in affinity chromatography
    • (a) Nishino, N.; Powers, J. C. Design of potent reversible inhibitors for thermolysin. Peptides containing zinc coordinating ligands and their use in affinity chromatography. Biochemistry 1979, 18, 4340-4347.
    • (1979) Biochemistry , vol.18 , pp. 4340-4347
    • Nishino, N.1    Powers, J.C.2
  • 10
    • 0000049891 scopus 로고
    • Inhibitors of metalloproteinases
    • Barrett, A. J., Salvesen, G., Eds.; Elsevier: Amsterdam, New York, Oxford
    • (b) Powers, J. C.; Harper, J. W. Inhibitors of metalloproteinases. In Proteinase Inhibitors; Barrett, A. J., Salvesen, G., Eds.; Elsevier: Amsterdam, New York, Oxford, 1986; pp 219-298.
    • (1986) Proteinase Inhibitors , pp. 219-298
    • Powers, J.C.1    Harper, J.W.2
  • 11
    • 0023619941 scopus 로고
    • Collagenase inhibitors: Their design and potential therapeutic use
    • (c) Johnson, W. H.; Roberts, N. A.; Borkakoti, N. Collagenase inhibitors: Their design and potential therapeutic use. J. Enzyme Inhib. 1987, 2, 1-22.
    • (1987) J. Enzyme Inhib. , vol.2 , pp. 1-22
    • Johnson, W.H.1    Roberts, N.A.2    Borkakoti, N.3
  • 12
    • 0000647282 scopus 로고    scopus 로고
    • Inhibition of matrix metalloproteinases: Structure based design
    • (d) Zask, A.; Levin, J. I.; Killar, L. M.; Skotnicki, J. S. Inhibition of Matrix Metalloproteinases: Structure Based Design. Curr. Pharm. Des. 1996, 2, 624-661.
    • (1996) Curr. Pharm. Des. , vol.2 , pp. 624-661
    • Zask, A.1    Levin, J.I.2    Killar, L.M.3    Skotnicki, J.S.4
  • 13
  • 15
    • 0028915695 scopus 로고
    • X-ray structures of human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors; implications for substrate binding and rational drug design
    • Grams, F.; Reinemer, P.; Powers, J.; Kleine, T.; Pieper, M.; Tschesche, H.; Huber, R.; Bode, W. X-ray structures of human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors; implications for substrate binding and rational drug design. Eur. J. Biochem. 1995, 228, 830-841. The coordinates were obtained prior to submission to PDB due to a collaboration with this group.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 830-841
    • Grams, F.1    Reinemer, P.2    Powers, J.3    Kleine, T.4    Pieper, M.5    Tschesche, H.6    Huber, R.7    Bode, W.8
  • 16
    • 0028838862 scopus 로고
    • Structure determination and analysis of human collagenase complexed with a hydroxamate inhibitor
    • Grams, F.; Crimmin, M.; Hinnes, L.; Huxley, P.; Pieper, M.; Tschesche, H.; Bode, W. Structure determination and analysis of human collagenase complexed with a hydroxamate inhibitor. Biochemistry 1995, 34, 14012-14020.
    • (1995) Biochemistry , vol.34 , pp. 14012-14020
    • Grams, F.1    Crimmin, M.2    Hinnes, L.3    Huxley, P.4    Pieper, M.5    Tschesche, H.6    Bode, W.7
  • 17
    • 0028841007 scopus 로고
    • 3D-quantitative structure - Activity relationships of human immunodeficiency virus type-1 proteinas inhibitors: Comparative molecular field analysis of 2-heterosubstituted statine derivatives - Implication for the design of novel inhibitors
    • Kroemer, R. T.; Ettmayer, P.; Hecht, P. 3D-Quantitative Structure - Activity Relationships of Human Immunodeficiency Virus Type-1 Proteinas Inhibitors: Comparative Molecular Field Analysis of 2-Heterosubstituted Statine Derivatives - Implication for the Design of Novel Inhibitors. J. Med. Chem. 1995, 38, 4917-4928.
    • (1995) J. Med. Chem. , vol.38 , pp. 4917-4928
    • Kroemer, R.T.1    Ettmayer, P.2    Hecht, P.3
  • 18
    • 0017411710 scopus 로고
    • The protein data bank: A computer-based archival file for macromolecular structures
    • PDB files obtained from Protein Database (National Brookhaven Laboratories): 1MMB, 1MNC, 1KBC, 1JAN, 1JAO, 1JAP, and 1JAQ (http://www.pdb.bnl.gov). Bernstein, F. C.; Koetzle, T. F.; Williams, G. J. B.; Meyer, E. F.; Brice, M. D.; Rodgers, J. R.; Kennard, O.; Shimanouchi, T.; Tasumi, M. The Protein Data Bank: a computer-based archival file for macromolecular structures. J. Mol. Biol. 1977, 112, 535-542.
    • (1977) J. Mol. Biol. , vol.112 , pp. 535-542
    • Bernstein, F.C.1    Koetzle, T.F.2    Williams, G.J.B.3    Meyer, E.F.4    Brice, M.D.5    Rodgers, J.R.6    Kennard, O.7    Shimanouchi, T.8    Tasumi, M.9
  • 19
    • 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. E. 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. III1    Patterson, D.E.2    Bunce, J.E.3
  • 21
    • 0003476917 scopus 로고
    • Kubinyi, H., Ed.; ESCOM: Leiden
    • 3D-QSAR in Drug Design. Theory, Methods and Applications; Kubinyi, H., Ed.; ESCOM: Leiden, 1993. This includes many applications and cross-references of the CoMFA methodology in medicinal chemistry.
    • (1993) 3D-QSAR in Drug Design. Theory, Methods and Applications
  • 22
    • 0027944195 scopus 로고
    • Molecular Similarity Indices in a Comparative Analysis (CoMSIA) of drug molecules to correlate and predict their biological activity
    • Klebe, G.; Abraham, U.; Mietzner, T. Molecular Similarity Indices in a Comparative Analysis (CoMSIA) of Drug Molecules to Correlate and Predict Their Biological Activity. J. Med. Chem. 1994, 37, 4130-4146.
    • (1994) J. Med. Chem. , vol.37 , pp. 4130-4146
    • Klebe, G.1    Abraham, U.2    Mietzner, T.3
  • 24
    • 0021733924 scopus 로고
    • Multivariate structure - Activity relationshiup between data from a battery of biological tests and an ensemble of structure descriptors: The PLS methodol
    • (b) Dunn, W. J.; Wold, S.; Edlund, U.; Hellberg, S.; Gasteiger, J. Multivariate Structure - Activity Relationshiup Between Data from a Battery of Biological Tests and an Ensemble of Structure Descriptors: The PLS Methodol. Quant. Struct.-Act. Relat. 1984, 3, 31-137.
    • (1984) Quant. Struct.-Act. Relat. , vol.3 , pp. 31-137
    • Dunn, W.J.1    Wold, S.2    Edlund, U.3    Hellberg, S.4    Gasteiger, J.5
  • 25
    • 85152373811 scopus 로고
    • Notes on the history and nature of Partial Least Squares (pls) modelling
    • (c) Geladi, P. Notes on the History and nature of Partial Least Squares (PLS) Modelling. J. Chemom. 1988, 2, 231-246.
    • (1988) J. Chemom. , vol.2 , pp. 231-246
    • Geladi, P.1
  • 26
    • 84951601886 scopus 로고
    • Cross-validatory estimation of the number of component in factor and principal component models
    • (a) Wold, S. Cross-Validatory Estimation of the Number of Component in Factor and Principal Component Models. Technometrics 1978, 4, 397-405.
    • (1978) Technometrics , vol.4 , pp. 397-405
    • Wold, S.1
  • 27
    • 0000484080 scopus 로고
    • Computer-intensive methods for statistics
    • (b) Diaconis, P.; Efron, B. Computer-Intensive Methods for Statistics. Sci. Am. 1984, 116, 96-117.
    • (1984) Sci. Am. , vol.116 , pp. 96-117
    • Diaconis, P.1    Efron, B.2
  • 28
    • 84987100711 scopus 로고
    • Crossvalidation, bootstrapping and partial least squares compared wih multile regression in conventional QSAR studies
    • (c) Cramer, R. D., III; Bunce, J. D.; Patterson, D. E. Crossvalidation, Bootstrapping and Partial Least Squares Compared wih Multile Regression in Conventional QSAR Studies. Quant. Struct.-Act. Relat. 1988, 7, 18-25.
    • (1988) Quant. Struct.-act. Relat. , vol.7 , pp. 18-25
    • Cramer R.D. III1    Bunce, J.D.2    Patterson, D.E.3
  • 29
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schlechter, I.; Berger, A. On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 1967, 27, 157-162.
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schlechter, I.1    Berger, A.2
  • 30
    • 0025310828 scopus 로고
    • Human neutrophil collagenase. A distinct gene product with homology to other matrix metalloproteinases
    • Residues and residue numbering rely on the Pro HNC nomenclature: Hasty, K. A.; Pourmotabbed, T. F.; Goldberg, G. I.; Thompson, J. P.; Spinella, D. G.; Stevens, R. M.; Mainardi, C. L. Human neutrophil collagenase. A distinct gene product with homology to other matrix metalloproteinases. J. Biol. Chem. 1990, 265, 11421-11424.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11421-11424
    • Hasty, K.A.1    Pourmotabbed, T.F.2    Goldberg, G.I.3    Thompson, J.P.4    Spinella, D.G.5    Stevens, R.M.6    Mainardi, C.L.7
  • 31
    • 0029003620 scopus 로고
    • Remodeling MMPIs
    • Hodgson, J. Remodeling MMPIs. Bio/Technology 1995, 13, 554-557.
    • (1995) Bio/Technology , vol.13 , pp. 554-557
    • Hodgson, J.1
  • 32
    • 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
  • 33
    • 0022419375 scopus 로고
    • Aromatic-aromatic interaction: A mechanism of protein structure stabilization
    • Burley, S. K.; Petsko, G. A. Aromatic-aromatic interaction: a mechanism of protein structure stabilization. Science 1985, 229, 23-28.
    • (1985) Science , vol.229 , pp. 23-28
    • Burley, S.K.1    Petsko, G.A.2
  • 34
    • 0344275422 scopus 로고    scopus 로고
    • Tetrahydroisoquinoline-3-carboxylate based matrix metalloproteinase inhibitors: Design, synthesis and structure - Activity relationship
    • to be submitted
    • Schwab, W.; Thorwart, W.; Barbier, D.; Billen, G.; Haase, B.; Matter, H.; Neises, B.; Schudok, M.; Weithmann, K. U. Tetrahydroisoquinoline-3-carboxylate based Matrix Metalloproteinase Inhibitors: Design, Synthesis and Structure - Activity Relationship. Bioorg. Med. Chem. 1999, to be submitted.
    • (1999) Bioorg. Med. Chem.
    • Schwab, W.1    Thorwart, W.2    Barbier, D.3    Billen, G.4    Haase, B.5    Matter, H.6    Neises, B.7    Schudok, M.8    Weithmann, K.U.9
  • 36
    • 0030812035 scopus 로고    scopus 로고
    • Effects of tiaprofenic acid on urinary pyridinium cross-links in adjuvant arthritic rats: Comparison with doxycycline
    • Weithmann, K. U.; Schlotte, V.; Jeske, V.; Seiffge, D.; Laber, A.; Haase, B.; Schleyerbach, R. Effects of tiaprofenic acid on urinary pyridinium cross-links in adjuvant arthritic rats: Comparison with doxycycline. Inflamm. Res. 1997, 46, 246-252.
    • (1997) Inflamm. Res. , vol.46 , pp. 246-252
    • Weithmann, K.U.1    Schlotte, V.2    Jeske, V.3    Seiffge, D.4    Laber, A.5    Haase, B.6    Schleyerbach, R.7
  • 37
    • 0026505650 scopus 로고
    • A novel coumarin-labeled peptide for sensitive continuous assays of the matrix metalloproteinases
    • Knight, C. G.; Willenbrock, F.; Murphy, G. A novel coumarin-labeled peptide for sensitive continuous assays of the matrix metalloproteinases. FEBS Lett. 1992, 296, 263-266.
    • (1992) FEBS Lett. , vol.296 , pp. 263-266
    • Knight, C.G.1    Willenbrock, F.2    Murphy, G.3
  • 38
    • 85046526624 scopus 로고
    • Evaluation of single-crystal X-ray diffraction data from a position sensitive detector
    • Kabsch, W. Evaluation of single-crystal X-ray diffraction data from a position sensitive detector. J. Appl. Crystallogr. 1988, 21, 916-924.
    • (1988) J. Appl. Crystallogr. , vol.21 , pp. 916-924
    • Kabsch, W.1
  • 42
    • 49149147973 scopus 로고    scopus 로고
    • Gasteiger, J.; Marsili, M. Tetrahedron 1980, 36, 3219-3228. Details of the implementation are given in: Sybyl 6.3 Theory Manual; Tripos: St. Louis, MO, 1996; p 67.
    • (1980) Tetrahedron , vol.36 , pp. 3219-3228
    • Gasteiger, J.1    Marsili, M.2
  • 43
    • 49149147973 scopus 로고    scopus 로고
    • Tripos: St. Louis, MO
    • Gasteiger, J.; Marsili, M. Tetrahedron 1980, 36, 3219-3228. Details of the implementation are given in: Sybyl 6.3 Theory Manual; Tripos: St. Louis, MO, 1996; p 67.
    • (1996) Sybyl 6.3 Theory Manual , pp. 67
  • 44
    • 84988109729 scopus 로고
    • Atomic physicochemical parameters for three-dimensional structure-directed quantitative structure - Activity relationships. 1. Partition coefficients as a measure of hydrophobicity
    • (a) Ghose, A.; Crippen, G. Atomic Physicochemical Parameters for Three-Dimensional Structure-Directed Quantitative Structure - Activity Relationships. 1. Partition Coefficients as a Measure of Hydrophobicity. J. Comput. Chem. 1986, 7, 565-577.
    • (1986) J. Comput. Chem. , vol.7 , pp. 565-577
    • Ghose, A.1    Crippen, G.2
  • 45
    • 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
    • (b) 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
  • 46
    • 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
  • 50
    • 0028454829 scopus 로고
    • Extending the trend vector: The trend matrix and sample-based partial least squares
    • Sheridan, R. P.; Nachbar, R. B.; Bush, B. L. Extending the trend vector: The trend matrix and sample-based partial least squares. J. Comput.-Aided Mol. Des. 1994, 8, 323-340.
    • (1994) J. Comput.-Aided Mol. Des. , vol.8 , pp. 323-340
    • Sheridan, R.P.1    Nachbar, R.B.2    Bush, B.L.3
  • 53
    • 0022620276 scopus 로고
    • Comparison of some measures for the determination of intermolecular structural similarity
    • (b) Willett, P.; Winterman, V. A. Comparison of Some Measures for the Determination of Intermolecular Structural Similarity. Quant. Struct.-Act. Relat. 1986, 5, 18-25.
    • (1986) Quant. Struct.-Act. Relat. , vol.5 , pp. 18-25
    • Willett, P.1    Winterman, V.A.2
  • 55
    • 0029233859 scopus 로고
    • Simulation analysis of experimental design strategies for screening random compounds as potential new drugs and agrochemicals
    • Taylor, R. Simulation Analysis of Experimental Design Strategies for Screening Random Compounds as Potential New Drugs and Agrochemicals. J. Chem. Inf. Comput. Sci. 1995, 35, 59-67.
    • (1995) J. Chem. Inf. Comput. Sci. , vol.35 , pp. 59-67
    • Taylor, R.1
  • 56
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A.; MacArthur, M. W.; Moss, D. S.; Thornton, J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 1993, 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 57
    • 0345569448 scopus 로고    scopus 로고
    • note
    • 50 × 100000).
  • 58
    • 0027209171 scopus 로고
    • The probability of chance correlation using Partial Least Squares (PLS)
    • Clark, M.; Cramer, R. D., III. The Probability of Chance Correlation using Partial Least Squares (PLS). Quant. Struct.-Act. Relat. 1993, 12, 137-145.
    • (1993) Quant. Struct.-act. Relat. , vol.12 , pp. 137-145
    • Clark, M.1    Cramer R.D. III2
  • 60
    • 0344275417 scopus 로고
    • Design of more informative molecules for QSAR study in a series of juvenile hormones
    • Wermuth, C.-G., Ed.; ESCOM: Leiden, The Netherlands
    • Carpignano, R.; Dolci, M.; Scarfi, D. Design of more informative molecules for QSAR study in a series of juvenile hormones. In Trends QSAR Mol. Modelling 92, Proc. Eur. Symp. Struct.-Act. Relat.; Wermuth, C.-G., Ed.; ESCOM: Leiden, The Netherlands, 1993.
    • (1993) Trends QSAR Mol. Modelling 92, Proc. Eur. Symp. Struct.-Act. Relat.
    • Carpignano, R.1    Dolci, M.2    Scarfi, D.3
  • 61
    • 0026842407 scopus 로고
    • PLS-based quantitative structure -activity relationship for substituted benazmides of clebopride type. Application of experimental design in drug research
    • (a) Norinder, U.; Hoegberg, T. PLS-based quantitative structure -activity relationship for substituted benazmides of clebopride type. Application of experimental design in drug research. Acta Chem. Scand. 1992, 46, 363-366.
    • (1992) Acta Chem. Scand. , vol.46 , pp. 363-366
    • Norinder, U.1    Hoegberg, T.2
  • 62
    • 0026558044 scopus 로고
    • Experimental design-based quantitative structure-toxicity relationship of some local anestetics using the PLS method
    • (b) Norinder, U. Experimental design-based quantitative structure-toxicity relationship of some local anestetics using the PLS method. J. Appl. Toxicol. 1992, 12, 143-147.
    • (1992) J. Appl. Toxicol. , vol.12 , pp. 143-147
    • Norinder, U.1
  • 63
    • 0026349358 scopus 로고
    • An experimental design based quantitative structure - Activity relationship study on β-adrenergic blocking agents using PLS
    • (c) Norinder, U. An experimental design based quantitative structure - activity relationship study on β-adrenergic blocking agents using PLS. Drug Des. Discov. 1991, 8, 127-136.
    • (1991) Drug Des. Discov. , vol.8 , pp. 127-136
    • Norinder, U.1
  • 64
    • 0025617054 scopus 로고
    • Experimental design based 3D QSAR analysis of steroid-protein interaction: Application to human CBG complexes
    • (d) Norinder, U. Experimental design based 3D QSAR analysis of steroid-protein interaction: application to human CBG complexes. J. Comput.-Aided Mol. Des. 1990, 4, 381-389.
    • (1990) J. Comput.-Aided Mol. Des. , vol.4 , pp. 381-389
    • Norinder, U.1
  • 65
    • 0032509984 scopus 로고    scopus 로고
    • Random or rational design ? Evaluation of diverse compound subsets from chemical structure databases
    • Pötter, T.; Matter, H. Random or Rational Design ? Evaluation of Diverse Compound Subsets from Chemical Structure Databases. J. Med. Chem. 1998, 41, 478-488.
    • (1998) J. Med. Chem. , vol.41 , pp. 478-488
    • Pötter, T.1    Matter, H.2
  • 66
    • 0030609810 scopus 로고    scopus 로고
    • 1.8-A crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate primed-side inhibitor with a distinct selectivity profile
    • Betz, M.; Huxley, P.; Davies, S. J.; Mushtaq, Y.; Pieper, M.; Tschesche, H.; Bode, W.; Gomis-Rüth, F. X. 1.8-A crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate primed-side inhibitor with a distinct selectivity profile. Eur. J. Biochem. 1997, 247, 356-363.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 356-363
    • Betz, M.1    Huxley, P.2    Davies, S.J.3    Mushtaq, Y.4    Pieper, M.5    Tschesche, H.6    Bode, W.7    Gomis-Rüth, F.X.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.