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Volumn 1, Issue 3, 2004, Pages 295-299

Isothermal titration calorimetry: Controlling binding forces in lead optimization

Author keywords

[No Author keywords available]

Indexed keywords

PROTEINASE INHIBITOR; SAQUINAVIR; TMC 126; UNCLASSIFIED DRUG;

EID: 13344284025     PISSN: 17406749     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ddtec.2004.11.016     Document Type: Review
Times cited : (58)

References (12)
  • 1
    • 0031024171 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • C.A. Lipinski et al. Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings Adv. Drug Deliv. Rev. 23 1997 3-25
    • (1997) Adv. Drug Deliv. Rev. , vol.23 , pp. 3-25
    • Lipinski, C.A.1
  • 2
    • 0034461768 scopus 로고    scopus 로고
    • Drug-like properties and the causes of poor solubility and poor permeability
    • C.A. Lipinski Drug-like properties and the causes of poor solubility and poor permeability J. Pharmacol. Toxicol. Methods 44 2000 235-249
    • (2000) J. Pharmacol. Toxicol. Methods , vol.44 , pp. 235-249
    • Lipinski, C.A.1
  • 3
    • 84888003088 scopus 로고    scopus 로고
    • Physicochemical properties and the discovery of orally active drugs: Technical and people issues
    • Proceedings of the Beilstein Institute Workshop, 13th-16th May 2002 (Kettner, M.G.Ha.C., ed.) Logos Verlag
    • Lipinski, C.A. (2003) Physicochemical properties and the discovery of orally active drugs: Technical and people issues. In Molecular Informatics Confronting Complexity. Proceedings of the Beilstein Institute Workshop, 13th-16th May 2002 (Kettner, M.G.Ha.C., ed.), pp. 59-78, Logos Verlag
    • (2003) Molecular Informatics Confronting Complexity , pp. 59-78
    • Lipinski, C.A.1
  • 4
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • T. Wiseman et al. Rapid measurement of binding constants and heats of binding using a new titration calorimeter Anal. Biochem. 179 1989 131-135
    • (1989) Anal. Biochem. , vol.179 , pp. 131-135
    • Wiseman, T.1
  • 5
    • 0035442411 scopus 로고    scopus 로고
    • Direct measurement of protein binding energetics by isothermal titration calorimetry
    • S. Leavitt E. Freire Direct measurement of protein binding energetics by isothermal titration calorimetry Curr. Opin. Struct. Biol. 11 2001 560-566
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 560-566
    • Leavitt, S.1    Freire, E.2
  • 6
    • 0037310209 scopus 로고    scopus 로고
    • Applications of calorimetric methods to drug discovery and the study of protein interactions
    • P.C. Weber F.R. Salemme Applications of calorimetric methods to drug discovery and the study of protein interactions Curr. Opin. Struct. Biol. 13 2003 115-121
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 115-121
    • Weber, P.C.1    Salemme, F.R.2
  • 7
    • 3242726206 scopus 로고    scopus 로고
    • Characterization of protein-protein interactions by isothermal titration calorimetry
    • A. Velazquez-Campoy et al. Characterization of protein-protein interactions by isothermal titration calorimetry Methods Mol. Biol. 261 2004 35-54
    • (2004) Methods Mol. Biol. , vol.261 , pp. 35-54
    • Velazquez-Campoy, A.1
  • 8
    • 0034601808 scopus 로고    scopus 로고
    • The thermodynamic basis of resistance to HIV-1 protease inhibition mutant
    • M.J. Todd et al. The thermodynamic basis of resistance to HIV-1 protease inhibition mutant Biochemistry 39 2000 11876-11883
    • (2000) Biochemistry , vol.39 , pp. 11876-11883
    • Todd, M.J.1
  • 9
    • 0035876257 scopus 로고    scopus 로고
    • The binding energetics of first and second generation HIV-1 protease inhibitors: Implications for drug design
    • A. Velazquez-Campoy et al. The binding energetics of first and second generation HIV-1 protease inhibitors: Implications for drug design Arch. Biochim. Biophys. 390 2001 169-175
    • (2001) Arch. Biochim. Biophys. , vol.390 , pp. 169-175
    • Velazquez-Campoy, A.1
  • 10
    • 9944232242 scopus 로고
    • Group contributions to the thermodynamic properties of non-ionic organic solutes in dilute aqueous solution
    • S. Cabani et al. Group contributions to the thermodynamic properties of non-ionic organic solutes in dilute aqueous solution J. Solution Chem. 10 1981 563-595
    • (1981) J. Solution Chem. , vol.10 , pp. 563-595
    • Cabani, S.1
  • 11
    • 0347513233 scopus 로고    scopus 로고
    • Structural and thermodynamic basis of resistance to HIV-1 protease inhibition: Implications for inhibitor design
    • A. Velazquez-Campoy et al. Structural and thermodynamic basis of resistance to HIV-1 protease inhibition: Implications for inhibitor design Curr. Drug Targets Infect. Disord. 3 2003 311-328
    • (2003) Curr. Drug Targets Infect. Disord. , vol.3 , pp. 311-328
    • Velazquez-Campoy, A.1
  • 12
    • 2942557079 scopus 로고    scopus 로고
    • Thermodynamic rules for the design of high affinity HIV-1 protease inhibitors with adaptability to mutations and high selectivity towards unwanted targets
    • H. Ohtaka et al. Thermodynamic rules for the design of high affinity HIV-1 protease inhibitors with adaptability to mutations and high selectivity towards unwanted targets Int. J. Biochem. Cell Biol. 36 2004 1787-1799
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 1787-1799
    • Ohtaka, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.