메뉴 건너뛰기




Volumn 53, Issue 10, 2010, Pages 4285-4289

Entropic contribution to the linking coefficient in fragment based drug design: A case study

Author keywords

[No Author keywords available]

Indexed keywords

BENZENESULFONAMIDE DERIVATIVE;

EID: 77952713014     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm901723z     Document Type: Article
Times cited : (64)

References (38)
  • 1
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins: SAR by NMR
    • Shuker, S. B.; Hajduk, P. J.; Meadows, R. P.; Fesik, S. W. Discovering high-affinity ligands for proteins: SAR by NMR Science 1996, 274, 1531-1534
    • (1996) Science , vol.274 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 3
    • 0036835460 scopus 로고    scopus 로고
    • Integration of virtual and high-throughput screening
    • Bajorath, F. Integration of virtual and high-throughput screening Nat. Rev. Drug Discovery 2002, 1, 882-894
    • (2002) Nat. Rev. Drug Discovery , vol.1 , pp. 882-894
    • Bajorath, F.1
  • 5
    • 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
  • 8
  • 10
    • 33847381100 scopus 로고    scopus 로고
    • A decade of fragment-based drug design: Strategic advances and lessons learned
    • Hajduk, P. J.; Greer, J. A decade of fragment-based drug design: strategic advances and lessons learned Nat. Rev. Drug Discovery 2007, 6, 211-219
    • (2007) Nat. Rev. Drug Discovery , vol.6 , pp. 211-219
    • Hajduk, P.J.1    Greer, J.2
  • 11
    • 65349195698 scopus 로고    scopus 로고
    • Molecular docking and ligand specificity in fragment-based inhibitor discovery
    • Chen, Y.; Shoichet, B. K. Molecular docking and ligand specificity in fragment-based inhibitor discovery Nat. Chem. Biol. 2009, 5, 358-364
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 358-364
    • Chen, Y.1    Shoichet, B.K.2
  • 12
    • 33746885488 scopus 로고    scopus 로고
    • Probing hot spots at protein-ligand binding sites: A fragment-based approach using biophysical methods
    • Ciulli, A.; Williams, G.; Smith, A. G.; Blundell, T. L.; Abell, C. Probing hot spots at protein-ligand binding sites: a fragment-based approach using biophysical methods J. Med. Chem. 2006, 49, 4992-5000
    • (2006) J. Med. Chem. , vol.49 , pp. 4992-5000
    • Ciulli, A.1    Williams, G.2    Smith, A.G.3    Blundell, T.L.4    Abell, C.5
  • 13
    • 65349083135 scopus 로고    scopus 로고
    • Fragment-based drug discovery takes a virtual turn
    • Pellecchia, M. Fragment-based drug discovery takes a virtual turn Nat. Chem. Biol. 2009, 5, 274-275
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 274-275
    • Pellecchia, M.1
  • 16
    • 0015101706 scopus 로고
    • Entropic contributions to rate accelerations in enzymic and intramolecular reactions and the chelate effect
    • Page, M. I.; Jencks, W. P. Entropic contributions to rate accelerations in enzymic and intramolecular reactions and the chelate effect Proc. Natl. Acad. Sci. U.S.A. 1971, 68, 1678-1683
    • (1971) Proc. Natl. Acad. Sci. U.S.A. , vol.68 , pp. 1678-1683
    • Page, M.I.1    Jencks, W.P.2
  • 17
    • 0019407381 scopus 로고
    • On the attribution and additivity of binding energies
    • Jencks, W. P. On the attribution and additivity of binding energies Proc. Natl. Acad. Sci. U.S.A. 1981, 78, 4046-4050
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 4046-4050
    • Jencks, W.P.1
  • 18
    • 0036821028 scopus 로고    scopus 로고
    • The consequences of translational and rotational entropy lost by small molecules on binding to proteins
    • Murray, C. W.; Verdonk, M. L. The consequences of translational and rotational entropy lost by small molecules on binding to proteins J. Comput.-Aided Mol. Des. 2002, 16, 741-753
    • (2002) J. Comput.-Aided Mol. Des. , vol.16 , pp. 741-753
    • Murray, C.W.1    Verdonk, M.L.2
  • 19
    • 25144456011 scopus 로고    scopus 로고
    • Solution nuclear magnetic resonance spectroscopy techniques for probing intermolecular interactions
    • Pellecchia, M. Solution nuclear magnetic resonance spectroscopy techniques for probing intermolecular interactions Chem. Biol. 2005, 12, 961-971
    • (2005) Chem. Biol. , vol.12 , pp. 961-971
    • Pellecchia, M.1
  • 21
    • 33751076241 scopus 로고    scopus 로고
    • Deconstructing fragment-based inhibitor discovery
    • Babaoglu, K.; Shoichet, B. K. Deconstructing fragment-based inhibitor discovery Nat. Chem. Biol. 2006, 2, 720-723
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 720-723
    • Babaoglu, K.1    Shoichet, B.K.2
  • 23
    • 70449584752 scopus 로고    scopus 로고
    • Intra- and interdomain flexibility in matrix metalloproteinases: Functional aspects and drug design
    • Bertini, I.; Fragai, M.; Luchinat, C. Intra- and interdomain flexibility in matrix metalloproteinases: functional aspects and drug design Curr. Pharm. Des. 2009, 15, 3592-3605
    • (2009) Curr. Pharm. Des. , vol.15 , pp. 3592-3605
    • Bertini, I.1    Fragai, M.2    Luchinat, C.3
  • 24
    • 51949118486 scopus 로고    scopus 로고
    • Residual ligand entropy in the binding of p-substituted benzenesulfonamide ligands to bovine carbonic anhydrase II
    • Stockmann, H.; Bronowska, A.; Syme, N. R.; Thompson, G. S.; Kalverda, A. P.; Warriner, S. L.; Homans, S. W. Residual ligand entropy in the binding of p-substituted benzenesulfonamide ligands to bovine carbonic anhydrase II J. Am. Chem. Soc. 2008, 130, 12420-12426
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 12420-12426
    • Stockmann, H.1    Bronowska, A.2    Syme, N.R.3    Thompson, G.S.4    Kalverda, A.P.5    Warriner, S.L.6    Homans, S.W.7
  • 28
    • 0842289659 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of human matrix metyalloproteinase 10
    • Bertini, I.; Calderone, V.; Fragai, M.; Luchinat, C.; Mangani, S.; Terni, B. Crystal structure of the catalytic domain of human matrix metyalloproteinase 10 J. Mol. Biol. 2004, 336, 707-716
    • (2004) J. Mol. Biol. , vol.336 , pp. 707-716
    • Bertini, I.1    Calderone, V.2    Fragai, M.3    Luchinat, C.4    Mangani, S.5    Terni, B.6
  • 31
    • 0028228418 scopus 로고
    • The entropic cost of bound water in crystals and biomolecules
    • Dunitz, J. D. The entropic cost of bound water in crystals and biomolecules Science 1994, 264, 670
    • (1994) Science , vol.264 , pp. 670
    • Dunitz, J.D.1
  • 32
    • 47649098600 scopus 로고    scopus 로고
    • Cooperativity and biological complexity
    • Whitty, A. Cooperativity and biological complexity Nat. Chem. Biol. 2008, 4, 435-439
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 435-439
    • Whitty, A.1
  • 33
    • 0031439461 scopus 로고    scopus 로고
    • Site-directed mutagenesis of the active site glutamate in human matrilysin: Investigation of its role in catalysis
    • Cha, J.; Auld, D. S. Site-directed mutagenesis of the active site glutamate in human matrilysin: investigation of its role in catalysis Biochemistry 1997, 36, 16019-16024
    • (1997) Biochemistry , vol.36 , pp. 16019-16024
    • Cha, J.1    Auld, D.S.2
  • 34
    • 0033550047 scopus 로고    scopus 로고
    • Analysis of the binding of hydroxamic acid and carboxylic acid inhibitors to the stromelysin-1 (matrix metalloproteinase-3) catalytic domain by isothermal titration calorimetry
    • Parker, M. H.; Lunney, E. A.; Ortwine, D. F.; Pavlovsky, A. G.; Humblet, C.; Brouillette, C. G. Analysis of the binding of hydroxamic acid and carboxylic acid inhibitors to the stromelysin-1 (matrix metalloproteinase-3) catalytic domain by isothermal titration calorimetry Biochemistry 1999, 38, 13592-13601
    • (1999) Biochemistry , vol.38 , pp. 13592-13601
    • Parker, M.H.1    Lunney, E.A.2    Ortwine, D.F.3    Pavlovsky, A.G.4    Humblet, C.5    Brouillette, C.G.6
  • 35
    • 0033547831 scopus 로고    scopus 로고
    • Role of His-224 in the anomalous pH dependence of human stromelysin-1
    • Holman, C. M.; Kan, C. C.; Gehring, M. R.; Van Wart, H. E. Role of His-224 in the anomalous pH dependence of human stromelysin-1 Biochemistry 1999, 38, 677-681
    • (1999) Biochemistry , vol.38 , pp. 677-681
    • Holman, C.M.1    Kan, C.C.2    Gehring, M.R.3    Van Wart, H.E.4
  • 36
    • 37549048176 scopus 로고    scopus 로고
    • Fragment-based approaches to enzyme inhibition
    • Ciulli, A.; Abell, C. Fragment-based approaches to enzyme inhibition Curr. Opin. Biotechnol. 2007, 18, 489-496
    • (2007) Curr. Opin. Biotechnol. , vol.18 , pp. 489-496
    • Ciulli, A.1    Abell, C.2
  • 37
    • 67349171544 scopus 로고    scopus 로고
    • Impact of linker strain and flexibility in the design of a fragment-based inhibitor
    • Chung, S.; Parker, J. B.; Bianchet, M.; Amzel, L. M.; Stivers, J. T. Impact of linker strain and flexibility in the design of a fragment-based inhibitor Nat. Chem. Biol. 2009, 5, 407-413
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 407-413
    • Chung, S.1    Parker, J.B.2    Bianchet, M.3    Amzel, L.M.4    Stivers, J.T.5
  • 38
    • 70350346470 scopus 로고    scopus 로고
    • Application of fragment growing and fragment linking to the discovery of inhibitors of Mycobacterium tuberculosis pantothenate synthetase
    • Hung, A. W.; Silvestre, H. L.; Wen, S.; Ciulli, A.; Blundell, T. L.; Abell, C. Application of fragment growing and fragment linking to the discovery of inhibitors of Mycobacterium tuberculosis pantothenate synthetase Angew. Chem., Int. Ed. 2009, 8452-8456
    • (2009) Angew. Chem., Int. Ed. , pp. 8452-8456
    • Hung, A.W.1    Silvestre, H.L.2    Wen, S.3    Ciulli, A.4    Blundell, T.L.5    Abell, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.