메뉴 건너뛰기




Volumn 47, Issue 2, 2004, Pages 337-344

Structural Interaction Fingerprint (SIFt): A Novel Method for Analyzing Three-Dimensional Protein-Ligand Binding Interactions

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN KINASE INHIBITOR;

EID: 0346962971     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm030331x     Document Type: Article
Times cited : (510)

References (32)
  • 2
    • 0036051992 scopus 로고    scopus 로고
    • High-throughput crystallography for lead discovery in drug design
    • Blundell, T. L.; Jhoti, H.; Abell, C. High-throughput crystallography for lead discovery in drug design. Nat. Rev. Drug Discovery 2002, 1, 45-54.
    • (2002) Nat. Rev. Drug Discovery , vol.1 , pp. 45-54
    • Blundell, T.L.1    Jhoti, H.2    Abell, C.3
  • 3
    • 0037107887 scopus 로고    scopus 로고
    • Structure-based virtual screening: An overview
    • Lyne, P. Structure-based virtual screening: an overview. Drug Discovery Today 2002, 7 (20), 1047-1055.
    • (2002) Drug Discovery Today , vol.7 , Issue.20 , pp. 1047-1055
    • Lyne, P.1
  • 4
    • 0028922586 scopus 로고
    • LIGPLOT a program to generate schematic diagrams of protein-ligand interactions
    • Wallace, A. C.; Laskowski, R. A.; Thornton, J. M. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 1995, 8, 127-134.
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 7
    • 0030599010 scopus 로고    scopus 로고
    • A fast flexible docking method using an incremental construction algorithm
    • Rarey, M.; Kramer, B.; Lengauer, T.; Klebe, G. A fast flexible docking method using an incremental construction algorithm. J. Mol. Biol. 1996, 261, 470-489.
    • (1996) J. Mol. Biol. , vol.261 , pp. 470-489
    • Rarey, M.1    Kramer, B.2    Lengauer, T.3    Klebe, G.4
  • 8
    • 0003797555 scopus 로고    scopus 로고
    • Tripos, Inc.: St. Louis, Missouri
    • SYBYL, version 6.8; Tripos, Inc.: St. Louis, Missouri.
    • SYBYL, Version 6.8
  • 9
    • 0031226772 scopus 로고    scopus 로고
    • Empirical scoring functions: I. The development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes
    • Eldridge, M.; Murray, C. W.; Auton, T. A.; Paolini, G. V.; Lee, R. P. Empirical scoring functions: I. The development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes. J. Comput.-Aided Mol. Des. 1997, 11, 425-445.
    • (1997) J. Comput.-Aided Mol. Des. , vol.11 , pp. 425-445
    • Eldridge, M.1    Murray, C.W.2    Auton, T.A.3    Paolini, G.V.4    Lee, R.P.5
  • 10
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • Jones, G.; Willett, P.; Glen, R. C.; Leach, A. R.; Taylor, R. Development and validation of a genetic algorithm for flexible docking. J. Mol. Biol. 1997, 267, 727-748.
    • (1997) J. Mol. Biol. , vol.267 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 11
    • 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. 1999, 42 (5), 791-804.
    • (1999) J. Med. Chem. , vol.42 , Issue.5 , pp. 791-804
    • Muegge, I.1    Martin, Y.C.2
  • 12
    • 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. 2000, 295, 337-356.
    • (2000) J. Mol. Biol. , vol.295 , pp. 337-356
    • Gohlke, H.1    Hendlich, M.2    Klebe, G.3
  • 13
    • 0033576680 scopus 로고    scopus 로고
    • Consensus scoring: A method for obtaining improved hit rates from docking databases of three-dimensional structures into protein
    • Charifson, P. S.; Corkery, J. J.; Murcko, M. A.; Walter, W. P. Consensus scoring: a method for obtaining improved hit rates from docking databases of three-dimensional structures into protein. J. Med. Chem. 1999, 42 (25), 5100-5109.
    • (1999) J. Med. Chem. , vol.42 , Issue.25 , pp. 5100-5109
    • Charifson, P.S.1    Corkery, J.J.2    Murcko, M.A.3    Walter, W.P.4
  • 14
    • 0032945648 scopus 로고    scopus 로고
    • Recent progress towards the identification of selective inhibitors of serine/threonine protein kinases
    • Adams, J. L.; Lee, D. Recent progress towards the identification of selective inhibitors of serine/threonine protein kinases. Curr. Opin. Drug Discovery Dev. 1999, 2, 96-109.
    • (1999) Curr. Opin. Drug Discovery Dev. , vol.2 , pp. 96-109
    • Adams, J.L.1    Lee, D.2
  • 15
    • 0035865781 scopus 로고    scopus 로고
    • Improved scoring of ligand-protein interactions using OWFEG free energy grids
    • Pearlman, D. A.; Charifson, P. S. Improved scoring of ligand-protein interactions using OWFEG free energy grids. J. Med. Chem. 2001, 44, 502-511.
    • (2001) J. Med. Chem. , vol.44 , pp. 502-511
    • Pearlman, D.A.1    Charifson, P.S.2
  • 16
    • 0346048989 scopus 로고    scopus 로고
    • OpenEye Scientific Software, Inc.: Santa Fe, New Mexico
    • OMEGA; OpenEye Scientific Software, Inc.: Santa Fe, New Mexico.
    • OMEGA
  • 17
    • 0029020282 scopus 로고
    • The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • Hanks, S. K.; Hunter, T. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 1995, 9, 576-596.
    • (1995) FASEB J. , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 18
    • 0026345394 scopus 로고
    • Protein kinase catalytic domain sequence database: Identification of conserved features of primary structure and classification of family members
    • Hanks, S. K.; Quinn, A. M. Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. Methods Enzymol. 1991, 200, 38-62.
    • (1991) Methods Enzymol. , vol.200 , pp. 38-62
    • Hanks, S.K.1    Quinn, A.M.2
  • 19
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee, B.; Richards, F. M. The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 1971, 55, 379-400.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 20
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. 1994, D50, 760-763.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 21
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald, I. K.; Thornton, J. M. Satisfying hydrogen bonding potential in proteins. J. Mol. Biol. 1994, 238, 777-793.
    • (1994) J. Mol. Biol. , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 22
    • 0000127673 scopus 로고
    • 2.2 Å refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with Mn-ATP and a peptide inhibitor
    • Zheng, J. H.; Tranfny, E. A.; Knighton, D. R.; Xuong, N. H.; Taylor, S. S.; Teneyck, L. F.; Sowadski, J. M. 2.2 Å refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with Mn-ATP and a peptide inhibitor. Acta Crystallogr. 1993, D49, 362-365.
    • (1993) Acta Crystallogr. , vol.D49 , pp. 362-365
    • Zheng, J.H.1    Tranfny, E.A.2    Knighton, D.R.3    Xuong, N.H.4    Taylor, S.S.5    Teneyck, L.F.6    Sowadski, J.M.7
  • 24
    • 84906381446 scopus 로고    scopus 로고
    • Accelrys Inc.: San Diego, CA
    • Insight II; Accelrys Inc.: San Diego, CA.
    • Insight II
  • 25
    • 5344244908 scopus 로고    scopus 로고
    • Chemical similarity searching
    • Willet, P. Chemical similarity searching. J. Chem. Inf. Comput. Sci. 1998, 38, 983-996.
    • (1998) J. Chem. Inf. Comput. Sci. , vol.38 , pp. 983-996
    • Willet, P.1
  • 26
    • 0019280022 scopus 로고
    • Clustering methodologies in exploratory data analysis
    • Dubes, R.; Jain, A. K. Clustering methodologies in exploratory data analysis. Adv. Comput. 1980, 19, 113-228.
    • (1980) Adv. Comput. , vol.19 , pp. 113-228
    • Dubes, R.1    Jain, A.K.2
  • 27
    • 0013157535 scopus 로고    scopus 로고
    • The MathWorks, Inc.: Natick, MA
    • MATLAB, version 6.5; The MathWorks, Inc.: Natick, MA.
    • MATLAB, Version 6.5
  • 29
    • 0034649618 scopus 로고    scopus 로고
    • Protein-based virtual screening of chemical databases: 1. Evaluation of different docking/scoring combinations
    • Bissantz, C.; Folkers, G.; Rognan, D. Protein-based virtual screening of chemical databases: 1. Evaluation of different docking/scoring combinations. J. Med. Chem. 2000, 43, 4759-4767.
    • (2000) J. Med. Chem. , vol.43 , pp. 4759-4767
    • Bissantz, C.1    Folkers, G.2    Rognan, D.3
  • 30
    • 0028773477 scopus 로고
    • Three protein kinase structures define a common motif
    • Taylor, S. S.; Radzio-Andzelm, E. Three protein kinase structures define a common motif. Structure 1994, 2, 345-355.
    • (1994) Structure , vol.2 , pp. 345-355
    • Taylor, S.S.1    Radzio-Andzelm, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.