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Volumn 72, Issue 4, 2008, Pages 237-248

Binding of matrix metalloproteinase inhibitors to extracellular matrix: 3D-QSAR analysis

Author keywords

3 dimensional quantitative structure activity relationship; Comparative Molecular Field Analysis; Disposition; Extracellular matrix; Matrix metalloproteinase inhibitors; Multiple binding modes; Pharmacokinetics; Tissue accumulation

Indexed keywords

3 PYRAZOLIDINONE DERIVATIVE; 4,5 DIHYDROOXAZOLINE DERIVATIVE; ILOMASTAT; MATRIX METALLOPROTEINASE INHIBITOR; N CARBONYLUREA DERIVATIVE; OXAZOLINE DERIVATIVE; PYRAZOLE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 52649150857     PISSN: 17470277     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1747-0285.2008.00710.x     Document Type: Article
Times cited : (9)

References (30)
  • 1
    • 33644545381 scopus 로고    scopus 로고
    • Validating matrix metalloproteinases as drug targets and anti-targets for cancer therapy
    • Overall C.M., Kleifeld O. (2006) Validating matrix metalloproteinases as drug targets and anti-targets for cancer therapy. Nat Rev Cancer 6 : 227 239.
    • (2006) Nat Rev Cancer , vol.6 , pp. 227-239
    • Overall, C.M.1    Kleifeld, O.2
  • 2
    • 33645738383 scopus 로고    scopus 로고
    • Towards third generation matrix metalloproteinase inhibitors for cancer therapy
    • Overall C.M., Kleifeld O. (2006) Towards third generation matrix metalloproteinase inhibitors for cancer therapy. Br J Cancer 94 : 941 946.
    • (2006) Br J Cancer , vol.94 , pp. 941-946
    • Overall, C.M.1    Kleifeld, O.2
  • 3
    • 0037192860 scopus 로고    scopus 로고
    • Design, synthesis, and characterization of potent, slow-binding inhibitors that are selective for gelatinases
    • Bernardo M.M., Brown S., Li Z.H., Fridman R., Mobashery S. (2002) Design, synthesis, and characterization of potent, slow-binding inhibitors that are selective for gelatinases. J Biol Chem 277 : 11201 11207.
    • (2002) J Biol Chem , vol.277 , pp. 11201-11207
    • Bernardo, M.M.1    Brown, S.2    Li, Z.H.3    Fridman, R.4    Mobashery, S.5
  • 7
    • 33646188540 scopus 로고    scopus 로고
    • Quantitative characterization of binding of small molecules to extracellular matrix
    • Zhang Y., Lukacova V., Reindl K., Balaz S. (2006) Quantitative characterization of binding of small molecules to extracellular matrix. J Biochem Biophys Methods 67 : 107 122.
    • (2006) J Biochem Biophys Methods , vol.67 , pp. 107-122
    • Zhang, Y.1    Lukacova, V.2    Reindl, K.3    Balaz, S.4
  • 10
    • 33846253679 scopus 로고    scopus 로고
    • The role of achiral pyrazolidinone templates in enantioselective diels-alder reactions: Scope, limitations, and conformational insights
    • Sibi M.P., Stanely L.M., Nie X., Venkatraman L., Liu M., Jasperse C.P. (2007) The role of achiral pyrazolidinone templates in enantioselective diels-alder reactions: scope, limitations, and conformational insights. J Am Chem Soc 129 : 395 405.
    • (2007) J Am Chem Soc , vol.129 , pp. 395-405
    • Sibi, M.P.1    Stanely, L.M.2    Nie, X.3    Venkatraman, L.4    Liu, M.5    Jasperse, C.P.6
  • 11
    • 33750358157 scopus 로고    scopus 로고
    • Fluxional additives: A second generation control in enantioselective catalysis
    • Sibi M.P., Manyem S., Palencia H.J. (2006) Fluxional additives: a second generation control in enantioselective catalysis. J Am Chem Soc 128 : 13660 13661.
    • (2006) J Am Chem Soc , vol.128 , pp. 13660-13661
    • Sibi, M.P.1    Manyem, S.2    Palencia, H.J.3
  • 14
    • 49149147973 scopus 로고
    • Iterative partial equalization of orbital electronegativity: A rapid access to atomic charges
    • Gasteiger J., Marsili M. (1980) Iterative partial equalization of orbital electronegativity: a rapid access to atomic charges. Tetrahedron 36 : 3219 3228.
    • (1980) Tetrahedron , vol.36 , pp. 3219-3228
    • Gasteiger, J.1    Marsili, M.2
  • 16
    • 0032488013 scopus 로고    scopus 로고
    • FLEXS: A method for fast flexible ligand superposition
    • Lemmen C., Lengauer T., Klebe G. (1998) FLEXS: a method for fast flexible ligand superposition. J Med Chem 41 : 4502 4520.
    • (1998) J Med Chem , vol.41 , pp. 4502-4520
    • Lemmen, C.1    Lengauer, T.2    Klebe, G.3
  • 18
    • 33846883939 scopus 로고    scopus 로고
    • Structural determinants of binding of aromates to extracellular matrix: A multi-species multi-mode CoMFA study
    • Zhang Y., Lukacova V., Bartus V., Balaz S. (2006) Structural determinants of binding of aromates to extracellular matrix: a multi-species multi-mode CoMFA study. Chem Res Toxicol 20 : 11 19.
    • (2006) Chem Res Toxicol , vol.20 , pp. 11-19
    • Zhang, Y.1    Lukacova, V.2    Bartus, V.3    Balaz, S.4
  • 19
    • 0028844980 scopus 로고
    • Calculation of relative binding free energies and configurational entropies: A structural and thermodynamic analysis of the nature of non-polar binding of thrombin inhibitors based on hirudin 55-65
    • Wang J., Szewczuk Z., Yue S.Y., Tsuda Y., Konishi Y., Purisima E.O. (1995) Calculation of relative binding free energies and configurational entropies: a structural and thermodynamic analysis of the nature of non-polar binding of thrombin inhibitors based on hirudin 55-65. J Mol Biol 253 : 473 492.
    • (1995) J Mol Biol , vol.253 , pp. 473-492
    • Wang, J.1    Szewczuk, Z.2    Yue, S.Y.3    Tsuda, Y.4    Konishi, Y.5    Purisima, E.O.6
  • 20
    • 0028064402 scopus 로고
    • Receptor mapping with multiple binding modes: Binding site of PCB-degrading dioxygenase
    • Balaz S., Hornak V., Haluska L. (1994) Receptor mapping with multiple binding modes: binding site of PCB-degrading dioxygenase. Chemom Intell Lab Syst 24 : 185 191.
    • (1994) Chemom Intell Lab Syst , vol.24 , pp. 185-191
    • Balaz, S.1    Hornak, V.2    Haluska, L.3
  • 21
    • 19244377973 scopus 로고    scopus 로고
    • Multiple binding modes in 3D-QSAR: Microbial degradation of polychlorinated biphenyls
    • Hornak V., Balaz S., Schaper K.J., Seydel J.K. (1998) Multiple binding modes in 3D-QSAR: microbial degradation of polychlorinated biphenyls. Quant Struct Act Relat 17 : 427 436.
    • (1998) Quant Struct Act Relat , vol.17 , pp. 427-436
    • Hornak, V.1    Balaz, S.2    Schaper, K.J.3    Seydel, J.K.4
  • 22
    • 0039784723 scopus 로고    scopus 로고
    • How does the Gibbs free energy evolve in a system undergoing coupled competitive reactions?
    • Jullien L., Proust A., LeMenn J.C. (1998) How does the Gibbs free energy evolve in a system undergoing coupled competitive reactions? J Chem Educ 75 : 194 199.
    • (1998) J Chem Educ , vol.75 , pp. 194-199
    • Jullien, L.1    Proust, A.2    Lemenn, J.C.3
  • 24
    • 0031079364 scopus 로고    scopus 로고
    • "mining Minima": Direct computation of conformational free energy
    • Head M.S., Given J.A., Gilson M.K. (1997) "Mining Minima": direct computation of conformational free energy. J Phys Chem A 101 : 1609 1618.
    • (1997) J Phys Chem a , vol.101 , pp. 1609-1618
    • Head, M.S.1    Given, J.A.2    Gilson, M.K.3
  • 25
    • 0345117314 scopus 로고    scopus 로고
    • Multimode ligand binding in receptor site modeling: Implementation in CoMFA
    • Lukacova V., Balaz S. (2003) Multimode ligand binding in receptor site modeling: implementation in CoMFA. J Chem Inf Comput Sci 43 : 2093 2105.
    • (2003) J Chem Inf Comput Sci , vol.43 , pp. 2093-2105
    • Lukacova, V.1    Balaz, S.2
  • 26
    • 0013851951 scopus 로고
    • The role of substituents in the hydrophobic bonding of phenols by serum and mitochondrial proteins
    • Hansch C., Kiehs K., Lawrence G.L. (1965) The role of substituents in the hydrophobic bonding of phenols by serum and mitochondrial proteins. J Am Chem Soc 87 : 5770 5773.
    • (1965) J Am Chem Soc , vol.87 , pp. 5770-5773
    • Hansch, C.1    Kiehs, K.2    Lawrence, G.L.3
  • 27
    • 0025828219 scopus 로고
    • A quantitative structure-activity relationship approach to the minimization of albumin binding
    • Hersey A., Hyde R.M., Livingstone D.J., Rahr E. (1991) A quantitative structure-activity relationship approach to the minimization of albumin binding. J Pharm Sci 80 : 333 337.
    • (1991) J Pharm Sci , vol.80 , pp. 333-337
    • Hersey, A.1    Hyde, R.M.2    Livingstone, D.J.3    Rahr, E.4
  • 28
    • 0035818919 scopus 로고    scopus 로고
    • Cheminformatic models to predict binding affinities to human serum albumin
    • Colmenarejo G., Alvarez-Pedraglio A., Lavandera J.L. (2001) Cheminformatic models to predict binding affinities to human serum albumin. J Med Chem 44 : 4370 4378.
    • (2001) J Med Chem , vol.44 , pp. 4370-4378
    • Colmenarejo, G.1    Alvarez-Pedraglio, A.2    Lavandera, J.L.3
  • 29
    • 0242290408 scopus 로고    scopus 로고
    • Fast gradient HPLC method to determine compounds binding to human serum albumin. Relationships with octanol/water and immobilized artificial membrane lipophilicity
    • Valko K., Nunhuck S., Bevan C., Abraham M.H., Reynolds D.P. (2003) Fast gradient HPLC method to determine compounds binding to human serum albumin. Relationships with octanol/water and immobilized artificial membrane lipophilicity. J Pharm Sci 92 : 2236 2248.
    • (2003) J Pharm Sci , vol.92 , pp. 2236-2248
    • Valko, K.1    Nunhuck, S.2    Bevan, C.3    Abraham, M.H.4    Reynolds, D.P.5
  • 30
    • 3242757468 scopus 로고    scopus 로고
    • Contribution of ionization and lipophilicity to drug binding to albumin: A preliminary step toward biodistribution prediction
    • Ermondi G., Lorenti M., Caron G. (2004) Contribution of ionization and lipophilicity to drug binding to albumin: a preliminary step toward biodistribution prediction. J Med Chem 47 : 3949 3961.
    • (2004) J Med Chem , vol.47 , pp. 3949-3961
    • Ermondi, G.1    Lorenti, M.2    Caron, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.