메뉴 건너뛰기




Volumn 12, Issue 8, 2009, Pages 772-790

Recent developments in isothermal titration calorimetry label free screening

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME; PROTEIN;

EID: 69749120275     PISSN: 13862073     EISSN: None     Source Type: Journal    
DOI: 10.2174/138620709789104889     Document Type: Article
Times cited : (32)

References (52)
  • 1
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman, T.; Williston, S.; Brandts, J.F.; Lin, L.N. Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem., 1989, 179, 131-137
    • (1989) Anal. Biochem. , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.N.4
  • 4
    • 0029645119 scopus 로고
    • Counting the calories to stay in the groove
    • Ladbury, J.E. Counting the calories to stay in the groove. Structure, 1995, 3, 635-639
    • (1995) Structure , vol.3 , pp. 635-639
    • Ladbury, J.E.1
  • 5
    • 0030266484 scopus 로고    scopus 로고
    • Sensing the heat: The application of isothermal titration calorimetry to thermodynamic studies of biomolecular interactions
    • Ladbury, J.E.; Chowdhry, B.Z. Sensing the heat: the application of isothermal titration calorimetry to thermodynamic studies of biomolecular interactions. Chem. Biol., 1996, 3, 791-801.
    • (1996) Chem. Biol. , vol.3 , pp. 791-801
    • Ladbury, J.E.1    Chowdhry, B.Z.2
  • 6
    • 0032901515 scopus 로고    scopus 로고
    • Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition
    • Jelasarov, I.; Bosshard, H.R. Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition. J. Mol. Recogn., 1999, 12, 3-18.
    • (1999) J. Mol. Recogn. , vol.12 , pp. 3-18
    • Jelasarov, I.1    Bosshard, H.R.2
  • 7
    • 0031571628 scopus 로고    scopus 로고
    • Specific binding of Hoechst 3325B to the d(GGCAAATITGCG), duplex: Calorimetric and spectroscopic studies
    • Haq, I.; Ladbury, J.E.; Chowdhry, B.Z.; Jenkins, T.C.; Chaires, J.B. Specific binding of Hoechst 3325B to the d(GGCAAATITGCG), duplex: calorimetric and spectroscopic studies. J. Mol. Biol., 1997, 271, 244-257
    • (1997) J. Mol. Biol. , vol.271 , pp. 244-257
    • Haq, I.1    Ladbury, J.E.2    Chowdhry, B.Z.3    Jenkins, T.C.4    Chaires, J.B.5
  • 9
    • 0345293146 scopus 로고    scopus 로고
    • On the value of c: Can low affinity systems be studied by isothermal titration calorimetry?
    • Turnbull, W.B.; Daranas, A.H. On the value of c: can low affinity systems be studied by isothermal titration calorimetry? J. Am. Chem. Soc., 2003, 125(48), 14859-14866
    • (2003) J. Am. Chem. Soc. , vol.125 , Issue.48 , pp. 14859-14866
    • Turnbull, W.B.1    Daranas, A.H.2
  • 11
    • 24344452953 scopus 로고    scopus 로고
    • Binding thermodynamics of statins to HMG-CoA reductase
    • DOI 10.1021/bi050905v
    • Carbonell, T.; Freire, E. Binding thermodynamics of statins to HMG-CoA reductase. Biochemistry, 2005, 44(35), 11741-11748 (Pubitemid 41262708)
    • (2005) Biochemistry , vol.44 , Issue.35 , pp. 11741-11748
    • Carbonell, T.1    Freire, E.2
  • 12
    • 0035843962 scopus 로고    scopus 로고
    • Structural mechanism for statin inhibition of HMG-CoA reductase
    • Istvan, E.S.; Deisenhofer, J. Structural mechanism for statin inhibition of HMG-CoA reductase. Science, 2001, 292(5519), 1160-1164
    • (2001) Science , vol.292 , Issue.5519 , pp. 1160-1164
    • Istvan, E.S.1    Deisenhofer, J.2
  • 13
    • 0002638463 scopus 로고
    • Heat capacity and entropy changes in processes involving proteins
    • Sturtevant, J.M. Heat capacity and entropy changes in processes involving proteins. Proc. Natl. Acad. Sci. USA, 1977, 74(6), 2236-2240
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , Issue.6 , pp. 2236-2240
    • Sturtevant, J.M.1
  • 14
    • 0032317157 scopus 로고    scopus 로고
    • Tight ligand binding affinities determined from thermodynamic linkage to temperature by titration calorimetry
    • DOI 10.1016/S0076-6879(98)95036-4
    • Doyle, M.L.; Hensley, P. Tight ligand binding affinities determined from thermodynamic linkage to temperature by titration calorimetry. Methods. Enzymol., 1998, 295, 88-99. (Pubitemid 29349910)
    • (1998) Methods in Enzymology , vol.295 , pp. 88-99
    • Doyle, M.L.1    Hensley, P.2
  • 15
    • 0029131539 scopus 로고
    • Tight binding affinities determined from thermodynamic linkage to protons by titration calorimetry
    • Doyle, M.L.; Louie, G.; Dal Monte, P.R.; Sokoloski, T.D. Tight binding affinities determined from thermodynamic linkage to protons by titration calorimetry. Methods. Enzymol., 1995, 259, 183-194
    • (1995) Methods. Enzymol. , vol.259 , pp. 183-194
    • Doyle, M.L.1    Louie, G.2    Dal Monte, P.R.3    Sokoloski, T.D.4
  • 16
    • 0028936571 scopus 로고
    • An exact mathematical expression for describing competitive binding of two different ligands to a protein molecule
    • Wang, Z.X. An exact mathematical expression for describing competitive binding of two different ligands to a protein molecule, FEBS Lett., 1995, 360, 111-114
    • (1995) FEBS Lett. , vol.360 , pp. 111-114
    • Wang, Z.X.1
  • 17
    • 0032144872 scopus 로고    scopus 로고
    • Low-affinity binding determined by titration calorimetry using a high-affinity coupling ligand: A thermodynamic study of ligand binding to protein tyrosine phosphatase IB
    • Zhang, Y.L.; Zhang, Z.Y. Low-affinity binding determined by titration calorimetry using a high-affinity coupling ligand: a thermodynamic study of ligand binding to protein tyrosine phosphatase IB. Anal. Biochem., 1998, 261, 139-148
    • (1998) Anal. Biochem. , vol.261 , pp. 139-148
    • Zhang, Y.L.1    Zhang, Z.Y.2
  • 18
    • 0034650726 scopus 로고    scopus 로고
    • Exact analysis of competition ligand binding by displacement isothermal titration calorimetry
    • Sigurskjold, B.W. Exact analysis of competition ligand binding by displacement isothermal titration calorimetry. Anal. Biochem., 2000, 277, 260-266
    • (2000) Anal. Biochem. , vol.277 , pp. 260-266
    • Sigurskjold, B.W.1
  • 19
    • 14744271960 scopus 로고    scopus 로고
    • ITC in the post-genomic era...? Priceless
    • Velazquez-Campoy, A.; Freire, E. ITC in the post-genomic era...? Priceless. Biophys. Chem., 2005, 115, 115-124
    • (2005) Biophys. Chem. , vol.115 , pp. 115-124
    • Velazquez-Campoy, A.1    Freire, E.2
  • 22
    • 0021763405 scopus 로고
    • A twin titration microcalorimeter for the study of biochemical reactions
    • McKinnon, L.R.; Fall, L.; Parody-Morreale, A.; Gill, S.J. A twin titration microcalorimeter for the study of biochemical reactions. Anal. Biochem., 1984, 139, 134-139
    • (1984) Anal. Biochem. , vol.139 , pp. 134-139
    • McKinnon, L.R.1    Fall, L.2    Parody-Morreale, A.3    Gill, S.J.4
  • 23
    • 0028496039 scopus 로고
    • Description of a new Gill titration calorimeter for the study of biochemical reactions: 1. Basic response of the instrument
    • EI Harrous, M.; Gill, S.J.; Parody-Morreale, A. Description of a new Gill titration calorimeter for the study of biochemical reactions: 1. Basic response of the instrument. Meas. Sci. Technol., 1994, 5, 1065-1070
    • (1994) Meas. Sci. Technol. , vol.5 , pp. 1065-1070
    • Ei Harrous, M.1    Gill, S.J.2    Parody-Morreale, A.3
  • 24
    • 0028495284 scopus 로고
    • Description of a new Gill titration calorimeter for the study of biochemical reactions: II. Operational characterization of the instrument
    • EI Harrous, M.; Mayorga, O.L.; Parody-Morreale, A. Description of a new Gill titration calorimeter for the study of biochemical reactions: II. Operational characterization of the instrument. Meas. Sci. Technol., 1994, 5, 1071-1077
    • (1994) Meas. Sci. Technol. , vol.5 , pp. 1071-1077
    • Ei Harrous, M.1    Mayorga, O.L.2    Parody-Morreale, A.3
  • 25
    • 0037627322 scopus 로고    scopus 로고
    • Development of an isothermal titration microcalorimetric system with digital control and dynamic power Peltier compensation: I. Description and basic performance
    • Velazquez-Campoy, A.; Lopez-Mayorga, O.; Cabrerizo-Vilchez, M.A. Development of an isothermal titration microcalorimetric system with digital control and dynamic power Peltier compensation: I. Description and basic performance. Rev. Sci. Instrum., 2000, 71, 1824-1831
    • (2000) Rev. Sci. Instrum. , vol.71 , pp. 1824-1831
    • Velazquez-Campoy, A.1    Lopez-Mayorga, O.2    Cabrerizo-Vilchez, M.A.3
  • 26
    • 0345850233 scopus 로고    scopus 로고
    • Development of an isothermal titration rnicrocalorimetric system with digital control and dynamic power Peltier compensation: II. Characterization and operation mode. Myoglobin adsorption onto polymeric latex particles
    • Velazquez-Campoy, A.; Lopez-Mayorga, O.; Cabrerizo-Vilchez, M.A. Development of an isothermal titration rnicrocalorimetric system with digital control and dynamic power Peltier compensation: II. Characterization and operation mode. Myoglobin adsorption onto polymeric latex particles. Rev. Sci. Instrum., 2000, 71, 1832-1840
    • (2000) Rev. Sci. Instrum. , vol.71 , pp. 1832-1840
    • Velazquez-Campoy, A.1    Lopez-Mayorga, O.2    Cabrerizo-Vilchez, M.A.3
  • 27
    • 10044226082 scopus 로고    scopus 로고
    • Application of isothermal titration calorimetry in the biological sciences: Things are heating up
    • Ladbury JE. Application of isothermal titration calorimetry in the biological sciences: things are heating up. Biotechniques, 2004, 37(6), 885-887
    • (2004) Biotechniques , vol.37 , Issue.6 , pp. 885-887
    • Ladbury, J.E.1
  • 30
    • 14744267135 scopus 로고    scopus 로고
    • Isothermal titration calorimetry: Measuring intermolecular interactions
    • Simpson, R., Ed.; New York: Cold Spring Harbor Laboratory Press
    • Velazquez-Campoy, A., E. Freire. Isothermal titration calorimetry: measuring intermolecular interactions. In: Simpson, R., Ed.; Proteins and Proteomics: A Laboratory Manual; New York: Cold Spring Harbor Laboratory Press, 2003; pp. 882-892.
    • (2003) Proteins and Proteomics: A Laboratory Manual , pp. 882-892
    • Velazquez-Campoy, A.1    Freire, E.2
  • 31
    • 3242726206 scopus 로고    scopus 로고
    • Characterization of protein-protein interactions by isothermal titration calorimetry
    • Velazquez-Campoy, A.; Leavitt, S.A.; Freire, E. Characterization of protein-protein interactions by isothermal titration calorimetry. Methods. Mol. Biol., 2004, 261, 35-54.
    • (2004) Methods. Mol. Biol. , vol.261 , pp. 35-54
    • Velazquez-Campoy, A.1    Leavitt, S.A.2    Freire, E.3
  • 32
    • 0032318864 scopus 로고    scopus 로고
    • Structure-based prediction of binding affinities and molecular design of peptide ligands
    • DOI 10.1016/S0076-6879(98)95037-6
    • Luque, I.; Freire, E. Structure-based prediction of binding affinities and molecular design of peptide ligands. Methods Enzymol., 1998, 295, 100-127. (Pubitemid 29349911)
    • (1998) Methods in Enzymology , vol.295 , pp. 100-127
    • Luque, I.1    Freire, E.2
  • 33
    • 0036836538 scopus 로고    scopus 로고
    • Structural parameterization of the binding enthalpy of small ligands
    • Luque, I.; Freire, E. Structural parameterization of the binding enthalpy of small ligands. Proteins, 2002, 49, 181-190.
    • (2002) Proteins , vol.49 , pp. 181-190
    • Luque, I.1    Freire, E.2
  • 34
    • 0034093758 scopus 로고    scopus 로고
    • HIV-1 protease inhibitors: Enthalpic versus entropic optimization of the binding affinity
    • DOI 10.1021/bi992399d
    • Velazquez-Campoy, A.; Todd, M.J.; Freire, E. HIV-l protease inhibitors: enthalpic versus entropic optimization of the binding affinity. Biochemistry, 2000, 39, 2201-2207 (Pubitemid 30130068)
    • (2000) Biochemistry , vol.39 , Issue.9 , pp. 2201-2207
    • Velazquez-Campoy, A.1    Todd, M.J.2    Freire, E.3
  • 35
    • 0034601808 scopus 로고    scopus 로고
    • Thermodynamic basis of resistance to HIV-1 protease inhibition: Calorimetric analysis of the V82F/I84V active site resistant mutant
    • DOI 10.1021/bi001013s
    • Todd, M.J.; Luque, I.; Velazquez-Campoy, A.; Freire, E. Thermodynamic basis of resistance to HIV-1 protease inhibition: calorimetric analysis of the V82F/I84V active site resistant mutant. Biochemistry, 2000, 39, 11876-11883 (Pubitemid 30747292)
    • (2000) Biochemistry , vol.39 , Issue.39 , pp. 11876-11883
    • Todd, M.J.1    Luque, I.2    Velazquez-Campoy, A.3    Freire, E.4
  • 36
    • 0033815251 scopus 로고    scopus 로고
    • Thermodynamic dissection of the binding energetics of KNI-272, a potent HIV-1 protease inhibitor
    • Velazquez-Campoy, A.; Luque, I.; Todd, M.J.; Milutinovich, M.; Kiso, Y.; Freire, E. Thermodynamic dissection of the binding energetics of KNI-272, a potent HIV-l protease inhibitor. Protein. Sci., 2000, 9, 1801-1809 (Pubitemid 30745476)
    • (2000) Protein Science , vol.9 , Issue.9 , pp. 1801-1809
    • Velazquez-Campoy, A.1    Luque, I.2    Todd, M.J.3    Milutinovich, M.4    Kiso, Y.5    Freire, E.6
  • 37
    • 0035876257 scopus 로고    scopus 로고
    • The binding energetics of first- and second-generation HIV-1 protease inhibitors: Implications for drug design
    • DOI 10.1006/abbi.2001.2333
    • Velazquez-Campoy, A.; Kiso, Y.; Freire, E. The binding energetics of first- and second-generation HIV-I protease inhibitors: implications for drug design. Arch. Biochem. Biophys., 2001, 390, 169-175. (Pubitemid 32568478)
    • (2001) Archives of Biochemistry and Biophysics , vol.390 , Issue.2 , pp. 169-175
    • Velazquez-Campoy, A.1    Kiso, Y.2    Freire, E.3
  • 38
  • 39
    • 0036137494 scopus 로고    scopus 로고
    • Designing drugs against heterogeneous targets
    • DOI 10.1038/nbt0102-15
    • Freire, E. Designing drugs against heterogeneous targets. Nat. Biotechnol., 2002, 20, 15-16. (Pubitemid 34044907)
    • (2002) Nature Biotechnology , vol.20 , Issue.1 , pp. 15-16
    • Freire, E.1
  • 40
    • 0037047028 scopus 로고    scopus 로고
    • Amplification of the effects of drug resistance mutations by background polymorphisms in HIV-1 protease from African subtypes
    • DOI 10.1021/bi020160i
    • Velazquez-Campoy, A.; Vega, S.; Freire, E. Amplification of the effects of drug resistance mutations by background polymorphisms in HIV-I protease from African subtypes. Biochemistry, 2002, 41, 8613-8619 (Pubitemid 34743300)
    • (2002) Biochemistry , vol.41 , Issue.27 , pp. 8613-8619
    • Velazquez-Campoy, A.1    Vega, S.2    Freire, E.3
  • 41
    • 0036078615 scopus 로고    scopus 로고
    • Overcoming drug resistance in HIV-l chemotherapy: The binding thermodynamics of Amprenavir and TMC~126 to wild-type and drug-resistant mutants of the HIV-l protease
    • Ohtaka, H.;, Velazquez-Campoy, A.; Xie, D.; Freire, E. Overcoming drug resistance in HIV-l chemotherapy: the binding thermodynamics of Amprenavir and TMC~126 to wild-type and drug-resistant mutants of the HIV-l protease. Protein. Sci., 2002, 11, 1908-1916
    • (2002) Protein. Sci. , vol.11 , pp. 1908-1916
    • Ohtaka, H.1    Velazquez-Campoy, A.2    Xie, D.3    Freire, E.4
  • 42
    • 0037780064 scopus 로고    scopus 로고
    • High-affinity inhibition of a family of Plasmodium falciparum proteases by a designed adaptive inhibitor
    • DOI 10.1021/bi034131z
    • Nezami, A.; Kimura, T.; Hidaka, K.; Kiso, A.; Liu, J.; Kiso, Y.; Goldberg, D.E.; Freire, E. High-affinity inhibition of a family of Plasmodium falciparum proteases by a designed adaptive inhibitor. Biochemistry, 2003, 42, 8459-8464 (Pubitemid 36875411)
    • (2003) Biochemistry , vol.42 , Issue.28 , pp. 8459-8464
    • Nezami, A.1    Kimura, T.2    Hidaka, K.3    Kiso, A.4    Liu, J.5    Kiso, Y.6    Goldberg, D.E.7    Freire, E.8
  • 45
    • 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
    • DOI 10.1016/j.biocel.2004.02.021, PII S1357272504000998, Molecular Biology of HIV
    • Ohtaka, H.; Muzammil, S.; Schon, A.; Velazquez-Campoy, A.; Vega, S.; Freire, E. 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., 2004, 36, 1787-1799. (Pubitemid 38748533)
    • (2004) International Journal of Biochemistry and Cell Biology , vol.36 , Issue.9 , pp. 1787-1799
    • Ohtaka, H.1    Muzammil, S.2    Schon, A.3    Velazquez-Campoy, A.4    Vega, S.5    Freire, E.6
  • 46
    • 0036166136 scopus 로고    scopus 로고
    • Incorporating target heterogeneity in drug design
    • Velazquez-Campoy, A.; Freire, E. Incorporating target heterogeneity in drug design. J. Cell. Biochem., 2001, S37, 82-88.
    • (2001) J. Cell. Biochem. , vol.37 , pp. 82-88
    • Velazquez-Campoy, A.1    Freire, E.2
  • 47
    • 0035876257 scopus 로고    scopus 로고
    • The binding energetics of first- and second-generation HIV-1 protease inhibitors: Implications for drug design
    • DOI 10.1006/abbi.2001.2333
    • Velazquez-Campoy, A.; Kiso, Y.; Freire, E. The binding energetics of first and second-generation HIV-1 protease inhibitors: implications for drug design. Arch. Biochem. Biophys., 2001, 390, 169-175. (Pubitemid 32568478)
    • (2001) Archives of Biochemistry and Biophysics , vol.390 , Issue.2 , pp. 169-175
    • Velazquez-Campoy, A.1    Kiso, Y.2    Freire, E.3
  • 48
    • 0344823654 scopus 로고    scopus 로고
    • Multidrug Resistance to HIV-1 Protease Inhibition Requires Cooperative Coupling between Distal Mutations
    • DOI 10.1021/bi0350405
    • Ohtaka, H.; Schon, A.; Xie, D.; Freire, E. Multidrug resistance to HIV-I protease inhibition requires cooperative coupling between distal mutations. Biochemistry, 2003, 42, 13659-13666 (Pubitemid 37444916)
    • (2003) Biochemistry , vol.42 , Issue.46 , pp. 13659-13666
    • Ohtaka, H.1    Schon, A.2    Freire, E.3
  • 49
    • 0037047028 scopus 로고    scopus 로고
    • Amplification of the effects of drug resistance mutations by background polymorphisms in HIV-1 protease from African subtypes
    • Velazquez-Campoy, A.; Vega, S.; Freirem, E. Amplification of the effects of drug resistance mutations by background polymorphisms in HIV-1 protease from African subtypes. Biochemistry, 2002, 41, 8613-8619.
    • (2002) Biochemistry , vol.41 , pp. 8613-8619
    • Velazquez-Campoy, A.1    Vega, S.2    Freirem, E.3
  • 50
  • 51
    • 33645319676 scopus 로고    scopus 로고
    • Overcoming roadblocks in lead optimization: A thermodynamic perspective
    • DOI 10.1111/j.1747-0285.2005.00314.x
    • Ruben, A.J.; Kiso, Y.; Freire, E. Overcoming roadblocks in lead optimization: a thermodynamic perspective. Chem. Biol. Drug. Des., 2006, 67(1), 2-4. (Pubitemid 43881382)
    • (2006) Chemical Biology and Drug Design , vol.67 , Issue.1 , pp. 2-4
    • Ruben, A.J.1    Kiso, Y.2    Freire, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.