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Volumn 2, Issue 8, 2007, Pages 1103-1114

Thermodynamics of binding interactions in the rational drug design process

Author keywords

DSC; ITC; Ligand binding; Structure based drug design; Thermodynamics

Indexed keywords

AMINOTRANSFERASE; BACTERIAL PROTEIN; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE INHIBITOR; ROSUVASTATIN; WATER;

EID: 34548421643     PISSN: 17460441     EISSN: None     Source Type: Journal    
DOI: 10.1517/17460441.2.8.1103     Document Type: Review
Times cited : (26)

References (70)
  • 1
    • 0002638463 scopus 로고
    • Heat capacity and entropy changes in processes involving proteins
    • STURTEVANT JM: 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
  • 2
    • 34548456428 scopus 로고    scopus 로고
    • Protonation linked equilibria and apparent affinity constants: The thermodynamic profile of the α-chymotrypsin-proflavin interaction
    • Epub ahead of print
    • BRUYLANTS G, WINTJENS K, LOOZE Y et al.: Protonation linked equilibria and apparent affinity constants: the thermodynamic profile of the α-chymotrypsin-proflavin interaction. Eur. Biophys. J. (2007). [Epub ahead of print].
    • (2007) Eur. Biophys. J
    • BRUYLANTS, G.1    WINTJENS, K.2    LOOZE, Y.3
  • 3
    • 0037062633 scopus 로고    scopus 로고
    • MURPHY KP: Van't Hoff and calorimetric enthalpies II: effects of linked equilibria
    • HORN JR, BRANDTS JF, MURPHY KP: van't Hoff and calorimetric enthalpies II: effects of linked equilibria. Biochemistry (2002) 41(23):7501-7507.
    • (2002) Biochemistry , vol.41 , Issue.23 , pp. 7501-7507
    • HORN, J.R.1    BRANDTS, J.F.2
  • 4
    • 14744268745 scopus 로고    scopus 로고
    • Heat capacity effects in protein folding and ligand binding: Are-evaluation of the role of water in biomolecular thermodynamics
    • COOPER A: Heat capacity effects in protein folding and ligand binding: are-evaluation of the role of water in biomolecular thermodynamics. Biophys. Chem. (2005) 115(2-3):89-97.
    • (2005) Biophys. Chem , vol.115 , Issue.2-3 , pp. 89-97
    • COOPER, A.1
  • 5
    • 12344276782 scopus 로고    scopus 로고
    • The effect of water displacement on binding thermodynamics: Concanavalin A
    • LI Z, LAZARIDIS T: The effect of water displacement on binding thermodynamics: concanavalin A. J. Phys. Chem. B (2005) 109(1):662-670.
    • (2005) J. Phys. Chem. B , vol.109 , Issue.1 , pp. 662-670
    • LI, Z.1    LAZARIDIS, T.2
  • 6
    • 33644527925 scopus 로고    scopus 로고
    • Thermodynamics of buried water clusters at a protein-ligand binding interface
    • LI Z, LAZARIDIS T: Thermodynamics of buried water clusters at a protein-ligand binding interface. J. Phys. Chem. B (2006) 110(3):1464-1475.
    • (2006) J. Phys. Chem. B , vol.110 , Issue.3 , pp. 1464-1475
    • LI, Z.1    LAZARIDIS, T.2
  • 7
    • 0141522976 scopus 로고    scopus 로고
    • Uses of enthalpy-entropy compensation in protein research
    • LUMRY R: Uses of enthalpy-entropy compensation in protein research. Biophys. Chem. (2003) 105(2-3):545-557.
    • (2003) Biophys. Chem , vol.105 , Issue.2-3 , pp. 545-557
    • LUMRY, R.1
  • 8
    • 28044466911 scopus 로고    scopus 로고
    • Enthalpy-entropy compensation is not a general feature of weak association
    • FORD DM: Enthalpy-entropy compensation is not a general feature of weak association. J. Am. Chem. Soc. (2005) 127(46):16167-16170.
    • (2005) J. Am. Chem. Soc , vol.127 , Issue.46 , pp. 16167-16170
    • FORD, D.M.1
  • 9
    • 0036120608 scopus 로고    scopus 로고
    • Enthalpy-entropy compensation: A phantom phenomenon
    • CORNISH-BOWDEN A: Enthalpy-entropy compensation: a phantom phenomenon. J. Biosci. (2002) 27(2):121-126.
    • (2002) J. Biosci , vol.27 , Issue.2 , pp. 121-126
    • CORNISH-BOWDEN, A.1
  • 10
    • 0000866128 scopus 로고
    • Hydrophobic effect in protein folding and other noncovalent processes involving proteins
    • SPOLAR R, HA JH, RECORD MT: Hydrophobic effect in protein folding and other noncovalent processes involving proteins. Proc Natl. Acad. Sci. USA (1989) 86(21):8382-8385.
    • (1989) Proc Natl. Acad. Sci. USA , vol.86 , Issue.21 , pp. 8382-8385
    • SPOLAR, R.1    HA, J.H.2    RECORD, M.T.3
  • 11
    • 0029080864 scopus 로고
    • Thermodynamic mapping of the inhibitor site of the aspartic protease endothiapepsin
    • GOMEZ J, FREIRE E: Thermodynamic mapping of the inhibitor site of the aspartic protease endothiapepsin. J. Mol. Biol. (1995) 252(3):337-350.
    • (1995) J. Mol. Biol , vol.252 , Issue.3 , pp. 337-350
    • GOMEZ, J.1    FREIRE, E.2
  • 12
    • 0034953839 scopus 로고    scopus 로고
    • Making cool drugs hot: Isothermal titration calorimetry as a tool to study binding energetics
    • HOLDGATE GA: Making cool drugs hot: isothermal titration calorimetry as a tool to study binding energetics. Biotechniques (2001) 31(1):164-184.
    • (2001) Biotechniques , vol.31 , Issue.1 , pp. 164-184
    • HOLDGATE, G.A.1
  • 13
    • 3543005385 scopus 로고    scopus 로고
    • Thermodynamics of protein-ligand interactions: History, presence, and future aspects
    • PEROZZO R, FOLKERS G, SCAPOZZA L: Thermodynamics of protein-ligand interactions: history, presence, and future aspects. J. Recept. Signal Transduct. Res. (2004) 24(1-2):1-52.
    • (2004) J. Recept. Signal Transduct. Res , vol.24 , Issue.1-2 , pp. 1-52
    • PEROZZO, R.1    FOLKERS, G.2    SCAPOZZA, L.3
  • 14
    • 21344447247 scopus 로고    scopus 로고
    • Isothermal titration calorimetry
    • LEWIS EA, MURPHY KP: Isothermal titration calorimetry. Methods Mol. Biol. (2005) 305:1-16.
    • (2005) Methods Mol. Biol , vol.305 , pp. 1-16
    • LEWIS, E.A.1    MURPHY, K.P.2
  • 15
    • 27344436962 scopus 로고    scopus 로고
    • Measurements of binding thermodynamics in drug discovery
    • HOLDGATE GA, WARD WHJ: Measurements of binding thermodynamics in drug discovery. Drug Discov. Today (2005) 10(22):1543-1550.
    • (2005) Drug Discov. Today , vol.10 , Issue.22 , pp. 1543-1550
    • HOLDGATE, G.A.1    WARD, W.H.J.2
  • 16
    • 3042828266 scopus 로고    scopus 로고
    • The development of a continuous isothermal titration calorimetric method for equilibrium studies
    • MARKOVA N, HALLEN D: The development of a continuous isothermal titration calorimetric method for equilibrium studies. Anal. Biochem. (2004) 331 (1):77-88.
    • (2004) Anal. Biochem , vol.331 , Issue.1 , pp. 77-88
    • MARKOVA, N.1    HALLEN, D.2
  • 17
    • 0345293146 scopus 로고    scopus 로고
    • On the value of c: Can low affinity systems be studied by isothermal titration calorimetry
    • TURNBULL WB, DARANAS AH: 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
  • 18
    • 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(2-3): 115-124.
    • (2005) Biophys. Chem , vol.115 , Issue.2-3 , pp. 115-124
    • VELAZQUEZ, C.A.1    FREIRE, E.2
  • 19
    • 34250641961 scopus 로고    scopus 로고
    • Isothermal titration calorimetry to determine association constants for high-affinity ligands
    • VELAZQUEZ CAMPOY A, FREIRE E: Isothermal titration calorimetry to determine association constants for high-affinity ligands. Nat. Protoc. (2006) 1(I):186-191.
    • (2006) Nat. Protoc , vol.1 , Issue.I , pp. 186-191
    • VELAZQUEZ, C.A.1    FREIRE, E.2
  • 20
    • 4644222022 scopus 로고    scopus 로고
    • Volume errors in isothermal titration calorimetry
    • TELLINGHUISEN J: Volume errors in isothermal titration calorimetry. Anal. Biochem. (2004) 333(2):405-406.
    • (2004) Anal. Biochem , vol.333 , Issue.2 , pp. 405-406
    • TELLINGHUISEN, J.1
  • 21
    • 0042831474 scopus 로고    scopus 로고
    • A study of statistical error in isothermal titration calorimetry
    • TELLINGHUISEN J: A study of statistical error in isothermal titration calorimetry. Anal. Biochem. (2003) 321(1):79-88.
    • (2003) Anal. Biochem , vol.321 , Issue.1 , pp. 79-88
    • TELLINGHUISEN, J.1
  • 22
    • 22144459822 scopus 로고    scopus 로고
    • Statistical error in isothermal titration calorimetry: Variance function estimation from generalized least squares
    • TELLINGHUISEN J: Statistical error in isothermal titration calorimetry: variance function estimation from generalized least squares. Anal. Biochem. (2005) 343(1):106-115.
    • (2005) Anal. Biochem , vol.343 , Issue.1 , pp. 106-115
    • TELLINGHUISEN, J.1
  • 23
    • 0842303040 scopus 로고    scopus 로고
    • The role of backlash in the "first injection anomaly" in isothermal titration calorimetry
    • MIZOUE LS, TELLINGHUISEN J: The role of backlash in the "first injection anomaly" in isothermal titration calorimetry. Anal Biochem. (2004) 326(1):125-127.
    • (2004) Anal Biochem , vol.326 , Issue.1 , pp. 125-127
    • MIZOUE, L.S.1    TELLINGHUISEN, J.2
  • 24
    • 33845437051 scopus 로고    scopus 로고
    • Calibration in isothermal titration calorimetry: Heat and cell volume from heat of dilution of NaCl (aq)
    • TELLINGHUISEN J: Calibration in isothermal titration calorimetry: heat and cell volume from heat of dilution of NaCl (aq). Anal. Biochem. (2007) 360(1):47-55.
    • (2007) Anal. Biochem , vol.360 , Issue.1 , pp. 47-55
    • TELLINGHUISEN, J.1
  • 25
    • 33645319676 scopus 로고    scopus 로고
    • Overcoming roadblocks in lead optimization: A thermodynamic perspective
    • RUBEN AJ, KISO Y, FREIRE E: Overcoming roadblocks in lead optimization: a thermodynamic perspective. Chem. Biol. Drug Des. (2006) 67(1):2-4.
    • (2006) Chem. Biol. Drug Des , vol.67 , Issue.1 , pp. 2-4
    • RUBEN, A.J.1    KISO, Y.2    FREIRE, E.3
  • 26
    • 0035226253 scopus 로고    scopus 로고
    • Isothermal titration calorimetry in drug discovery
    • WARD WH, HOLDGATE GA: Isothermal titration calorimetry in drug discovery. Prog. Med. Chem. (2001) 38:309-376.
    • (2001) Prog. Med. Chem , vol.38 , pp. 309-376
    • WARD, W.H.1    HOLDGATE, G.A.2
  • 28
    • 4444373877 scopus 로고    scopus 로고
    • High-throughput biochemistry heats up
    • SALEMME FR: High-throughput biochemistry heats up. Nat. Biotech. (2004) 22(9): 1100-1101.
    • (2004) Nat. Biotech , vol.22 , Issue.9 , pp. 1100-1101
    • SALEMME, F.R.1
  • 29
    • 0034581194 scopus 로고    scopus 로고
    • Kinetic, equilibrium, and thermodynamic analysis of macromolecular interactions with BIACORE
    • MYSZKA DG: Kinetic, equilibrium, and thermodynamic analysis of macromolecular interactions with BIACORE. Methods Enzymol. (2000) 323:325-340.
    • (2000) Methods Enzymol , vol.323 , pp. 325-340
    • MYSZKA, D.G.1
  • 30
    • 0347359115 scopus 로고    scopus 로고
    • A Biacore biosensor method for detailed kinetic binding analysis of small moleculeinhibitors of p38α mitogen-activate protein kinase
    • CASPER D, BUKHTIYARIOVA M, SPRINGMAN E: A Biacore biosensor method for detailed kinetic binding analysis of small moleculeinhibitors of p38α mitogen-activate protein kinase. Anal. Biochem. (2004) 325:126-136.
    • (2004) Anal. Biochem , vol.325 , pp. 126-136
    • CASPER, D.1    BUKHTIYARIOVA, M.2    SPRINGMAN, E.3
  • 31
    • 33751534874 scopus 로고    scopus 로고
    • Thermodynamics of the cyclophilin-A/ cyclosporin-A interaction: A direct comparison of parameters determined by surface plasmon resonance using Biacore T100 and isothermal titration calorimetry
    • WEAR MA, WALKINSHAW MD: Thermodynamics of the cyclophilin-A/ cyclosporin-A interaction: a direct comparison of parameters determined by surface plasmon resonance using Biacore T100 and isothermal titration calorimetry. Anal. Biochem. (2006) 359:285-287.
    • (2006) Anal. Biochem , vol.359 , pp. 285-287
    • WEAR, M.A.1    WALKINSHAW, M.D.2
  • 32
    • 0032710475 scopus 로고    scopus 로고
    • NMR techniques for characterization of ligand binding: Utility for lead generation and optimization in drug discovery
    • MOORE JM: NMR techniques for characterization of ligand binding: utility for lead generation and optimization in drug discovery. Biopolymers (1999) 51 (3):221-243.
    • (1999) Biopolymers , vol.51 , Issue.3 , pp. 221-243
    • MOORE, J.M.1
  • 33
    • 33746760388 scopus 로고    scopus 로고
    • Analysis of ligand binidng by bioaffinity mass spectrometry
    • ZHU Y, VALDES R Jr, SIMMONS CQ et al.: Analysis of ligand binidng by bioaffinity mass spectrometry. Clin. Chem. Acta (2006) 371(1-2):71-78.
    • (2006) Clin. Chem. Acta , vol.371 , Issue.1-2 , pp. 71-78
    • ZHU, Y.1    VALDES Jr, R.2    SIMMONS, C.Q.3
  • 34
    • 0344738554 scopus 로고    scopus 로고
    • Frontal affinity chromatography combined on-line with mass spectrometry: A tool for the binding study of different epidermal growth factor receptor inhibitors
    • ZHU L, CHEN L, LUO H et al.: Frontal affinity chromatography combined on-line with mass spectrometry: a tool for the binding study of different epidermal growth factor receptor inhibitors. Anal. Chem. (2003) 75(23):6388-6393.
    • (2003) Anal. Chem , vol.75 , Issue.23 , pp. 6388-6393
    • ZHU, L.1    CHEN, L.2    LUO, H.3
  • 35
    • 1542345535 scopus 로고    scopus 로고
    • Recent advances in the study of biomolecular interactions by capillary electrophoresis
    • HEX, DING Y, LI D et al.: Recent advances in the study of biomolecular interactions by capillary electrophoresis. Electrophoresis (2004) 25:697-711.
    • (2004) Electrophoresis , vol.25 , pp. 697-711
    • HEX, D.Y.1    LI, D.2
  • 36
    • 2942552633 scopus 로고    scopus 로고
    • The ABRF-MIRG'02 study: Assembly state, thermodynamic, and kinetic analysis of an enzyme/ inhibitor interaction
    • MYSZKA DG, ABDICHE YN, ARISAKA F et al.: The ABRF-MIRG'02 study: Assembly state, thermodynamic, and kinetic analysis of an enzyme/ inhibitor interaction. J. Biomol. Tech. (2003) 14(4):247-269.
    • (2003) J. Biomol. Tech , vol.14 , Issue.4 , pp. 247-269
    • MYSZKA, D.G.1    ABDICHE, Y.N.2    ARISAKA, F.3
  • 37
    • 0037081320 scopus 로고    scopus 로고
    • A thermodynamic characerization of the binding of thrombin inhibitors to human thrombin, combining biosensor technology, stopped-flow spectrophotometry, and microcalorimetry
    • DEINUM J, GUSTAVSSON L, GYZANDER E et al.: A thermodynamic characerization of the binding of thrombin inhibitors to human thrombin, combining biosensor technology, stopped-flow spectrophotometry, and microcalorimetry. Anal. Biochem. (2002) 300:152-162.
    • (2002) Anal. Biochem , vol.300 , pp. 152-162
    • DEINUM, J.1    GUSTAVSSON, L.2    GYZANDER, E.3
  • 38
    • 33845335781 scopus 로고    scopus 로고
    • Towards predictive ligand design with fre energy based computational methods
    • FOLOPPE N, HUBBARD R: Towards predictive ligand design with fre energy based computational methods. Curr. Med. Chem. (2006) 13(29)3583-3608.
    • (2006) Curr. Med. Chem , vol.13 , Issue.29 , pp. 3583-3608
    • FOLOPPE, N.1    HUBBARD, R.2
  • 40
    • 0142028929 scopus 로고    scopus 로고
    • Thermal denaturation: A method to rank slow binding, high-affinity p38 MAP kinase inhibitors
    • KROE RR, REGAN J, PROTO A: Thermal denaturation: a method to rank slow binding, high-affinity p38 MAP kinase inhibitors. J. Med. Chem. (2003) 46(22):4669-4675.
    • (2003) J. Med. Chem , vol.46 , Issue.22 , pp. 4669-4675
    • KROE, R.R.1    REGAN, J.2    PROTO, A.3
  • 41
    • 25644434877 scopus 로고    scopus 로고
    • Ligand binding affinity determined by temperature-dependent circular dichroism: Cyclin-dependent kinase 2 inhibitors
    • MAYHOOD TW, WINDSOR WT: Ligand binding affinity determined by temperature-dependent circular dichroism: cyclin-dependent kinase 2 inhibitors. Anal. Biochem. (2005) 345:187-197.
    • (2005) Anal. Biochem , vol.345 , pp. 187-197
    • MAYHOOD, T.W.1    WINDSOR, W.T.2
  • 42
    • 33751559579 scopus 로고    scopus 로고
    • Screening for ligands using a generic and high-throughput light-scattering-based assay
    • SENISTERRA GA, MARKIN E, YAMAZAKI K, HUI R, VEDADI M, AWREY DE: Screening for ligands using a generic and high-throughput light-scattering-based assay. J. Biomol. Screen. (2006) 11(8):940-948.
    • (2006) J. Biomol. Screen , vol.11 , Issue.8 , pp. 940-948
    • SENISTERRA, G.A.1    MARKIN, E.2    YAMAZAKI, K.3    HUI, R.4    VEDADI, M.5    AWREY, D.E.6
  • 43
    • 33750470057 scopus 로고    scopus 로고
    • Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination
    • VEDADI M, NIESEN FH, ALLALI-HASSANI A et al.: Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination. Proc. Natl. Acad. Sci. USA (2006) 103(43):15835-15840.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , Issue.43 , pp. 15835-15840
    • VEDADI, M.1    NIESEN, F.H.2    ALLALI-HASSANI, A.3
  • 44
    • 33749850046 scopus 로고    scopus 로고
    • Universal screening methods and applications of ThermoFluor
    • CUMMINGS MD, FARNUM MA, HELEN MI: Universal screening methods and applications of ThermoFluor. J. Biomol. Screen. (2006) 11 (7):854-863.
    • (2006) J. Biomol. Screen , vol.11 , Issue.7 , pp. 854-863
    • CUMMINGS, M.D.1    FARNUM, M.A.2    HELEN, M.I.3
  • 45
    • 16344382388 scopus 로고    scopus 로고
    • Thermodynamic stability of carbonic anhydrase: Measurements of binding affinity and stoichiometry using ThermoFluor
    • MATULIS D, KRANZ JK, SALEMME FR, TODD MJ: Thermodynamic stability of carbonic anhydrase: measurements of binding affinity and stoichiometry using ThermoFluor. Biochemistry (2005) 44(13):5258-5266.
    • (2005) Biochemistry , vol.44 , Issue.13 , pp. 5258-5266
    • MATULIS, D.1    KRANZ, J.K.2    SALEMME, F.R.3    TODD, M.J.4
  • 46
    • 33745167708 scopus 로고    scopus 로고
    • Effect of construct design on MAPKAP kinase 2 activity, thermodynamic stability and ligand-binding affinity
    • KERVINEN J, MA H, BAYOUMY S et al.: Effect of construct design on MAPKAP kinase 2 activity, thermodynamic stability and ligand-binding affinity. Arch. Biochem. Biophys. (2006) 449(1-2):47-56.
    • (2006) Arch. Biochem. Biophys , vol.449 , Issue.1-2 , pp. 47-56
    • KERVINEN, J.1    MA, H.2    BAYOUMY, S.3
  • 47
    • 33748929006 scopus 로고    scopus 로고
    • Thermofluor-based high-throughput stability optimization of proteins for structural studies
    • ERICSSON UB, HALLBERG BM, DETITTA GT, DEKKER N, NORDLUND P: Thermofluor-based high-throughput stability optimization of proteins for structural studies. Anal. Biochem. (2006) 357(2):289-298.
    • (2006) Anal. Biochem , vol.357 , Issue.2 , pp. 289-298
    • ERICSSON, U.B.1    HALLBERG, B.M.2    DETITTA, G.T.3    DEKKER, N.4    NORDLUND, P.5
  • 48
    • 20144384268 scopus 로고    scopus 로고
    • Decrypting the biochemical function of an essential gene from Streptococcus pneumoniae using ThermoFluor technology
    • CARVER TE, BORDEAU B, CUMMINGS MD et al.: Decrypting the biochemical function of an essential gene from Streptococcus pneumoniae using ThermoFluor technology. J. Biol. Chem. (2005) 280(12): 11704-11712.
    • (2005) J. Biol. Chem , vol.280 , Issue.12 , pp. 11704-11712
    • CARVER, T.E.1    BORDEAU, B.2    CUMMINGS, M.D.3
  • 49
    • 33644873086 scopus 로고    scopus 로고
    • Benzodiazepinedione inhibitors of the Hdm2:p53 complex suppress human tumor cell proliferation in vitro and sensitize tumors to doxorubicin in vivo
    • KOBLISH HK, ZHAO S, FRANKS CF et al.: Benzodiazepinedione inhibitors of the Hdm2:p53 complex suppress human tumor cell proliferation in vitro and sensitize tumors to doxorubicin in vivo. Mol. Cancer Ther. (2006) 5(1):160-169.
    • (2006) Mol. Cancer Ther , vol.5 , Issue.1 , pp. 160-169
    • KOBLISH, H.K.1    ZHAO, S.2    FRANKS, C.F.3
  • 50
    • 0033586726 scopus 로고    scopus 로고
    • Calorimetric examination of high-affinity src SH2 domain-tyrosyl phosphopeptide binding: Dissection of the phosphopeptide sequence specificity and coupling energetics
    • BRADSHAW JM, WAKSMAN G: Calorimetric examination of high-affinity src SH2 domain-tyrosyl phosphopeptide binding: dissection of the phosphopeptide sequence specificity and coupling energetics. Biochemistry (1999) 38(16):5145-5154.
    • (1999) Biochemistry , vol.38 , Issue.16 , pp. 5145-5154
    • BRADSHAW, J.M.1    WAKSMAN, G.2
  • 51
    • 27344439152 scopus 로고    scopus 로고
    • The application of isothermal titration calorimetry to drug discovery
    • Ladbury JE, Doyle ML Eds, John Wiley & Sons Ltd, West Sussex
    • HOLDGATE G, FISHER S, WARD W: The application of isothermal titration calorimetry to drug discovery. In: Biocalorimetry 2: Applications of Calorimetry in the Biological Sciences. Ladbury JE, Doyle ML (Eds), John Wiley & Sons Ltd, West Sussex (2004):59-79.
    • (2004) Biocalorimetry 2: Applications of Calorimetry in the Biological Sciences , pp. 59-79
    • HOLDGATE, G.1    FISHER, S.2    WARD, W.3
  • 52
    • 22544442178 scopus 로고    scopus 로고
    • Differential scanning calorimetry in life science: Thermodynamics, molecular recognition and application in drug design
    • BRUYLANTS G, WOUTERS J, MICHAUX C: Differential scanning calorimetry in life science: thermodynamics, molecular recognition and application in drug design. Curr. Med. Chem. (2005) 12(17):2011-2020.
    • (2005) Curr. Med. Chem , vol.12 , Issue.17 , pp. 2011-2020
    • BRUYLANTS, G.1    WOUTERS, J.2    MICHAUX, C.3
  • 53
    • 0037310209 scopus 로고    scopus 로고
    • Applications of calorimetric methods to drug discovery and the study of protein interactions
    • WEBER PC, SALEMME FR: Applications of calorimetric methods to drug discovery and the study of protein interactions. Curr. Opin. Struct. Biol. (2003) 13(1):115-121.
    • (2003) Curr. Opin. Struct. Biol , vol.13 , Issue.1 , pp. 115-121
    • WEBER, P.C.1    SALEMME, F.R.2
  • 54
    • 33646252015 scopus 로고    scopus 로고
    • Rapid and simple protein-stability screens:application to membrane proteins
    • YEH AP, MCMILLAN A, STOWELL MHB: Rapid and simple protein-stability screens:application to membrane proteins. Acta Cryst. (2006) D62(4):451-457.
    • (2006) Acta Cryst , vol.D62 , Issue.4 , pp. 451-457
    • YEH, A.P.1    MCMILLAN, A.2    STOWELL, M.H.B.3
  • 55
    • 33846419564 scopus 로고    scopus 로고
    • The use of biophysical methods increases success in obtaining liganded crystal structures
    • CHUNG CW: The use of biophysical methods increases success in obtaining liganded crystal structures. Acta Cryst. (2007) D63(1):62-71.
    • (2007) Acta Cryst , vol.D63 , Issue.1 , pp. 62-71
    • CHUNG, C.W.1
  • 56
    • 0038333283 scopus 로고    scopus 로고
    • Stabilization of proteins by ligand binding: Application to drug screening and determination of unfolding energetics
    • WALDRON TT, MURPHY KP: Stabilization of proteins by ligand binding: application to drug screening and determination of unfolding energetics. Biochemistry (2003) 42(17):5058-5064.
    • (2003) Biochemistry , vol.42 , Issue.17 , pp. 5058-5064
    • WALDRON, T.T.1    MURPHY, K.P.2
  • 57
    • 4143121255 scopus 로고    scopus 로고
    • Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery
    • LO MC, AULABAUGH A, JIN G et al.: Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery. Anal. Biochem. (2004) 332(1):153-159.
    • (2004) Anal. Biochem , vol.332 , Issue.1 , pp. 153-159
    • MC, L.O.1    AULABAUGH, A.2    JIN, G.3
  • 58
    • 33845929089 scopus 로고    scopus 로고
    • Protein flexibility and ligand rigidity: A thermodynamic and kinetic study of ITAM based ligand binding to Syk tandem SH2
    • DE MOL NJ, CATALINA MI, DEKKER FJ et al.: Protein flexibility and ligand rigidity: a thermodynamic and kinetic study of ITAM based ligand binding to Syk tandem SH2. Chem. Bio. Chem. (2005) 6:2261-2270.
    • (2005) Chem. Bio. Chem , vol.6 , pp. 2261-2270
    • DE MOL, N.J.1    CATALINA, M.I.2    DEKKER, F.J.3
  • 59
  • 60
    • 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
    • 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(9):1787-1799.
    • (2004) Int. J. Biochem. Cell Biol , 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
  • 61
    • 33645319676 scopus 로고    scopus 로고
    • Overcoming roadblocks in lead optimization: A thermodynamic perspective
    • RUBEN AJ, KISO Y, FREIRE E: Overcoming roadblocks in lead optimization: a thermodynamic perspective. Chem. Biol. Drug Des. (2006) 67(1):2-4.
    • (2006) Chem. Biol. Drug Des , vol.67 , Issue.1 , pp. 2-4
    • RUBEN, A.J.1    KISO, Y.2    FREIRE, E.3
  • 62
    • 0035833985 scopus 로고    scopus 로고
    • Biochemical characterization of a phosphinate inhibitor of Escherichia coli MurC
    • MARMOR S, PETERSEN CP, RECK F, YANG W, GAO N, FISHER SL: Biochemical characterization of a phosphinate inhibitor of Escherichia coli MurC. Biochemistry (2001) 40 (40): 12207-12214.
    • (2001) Biochemistry , vol.40 , Issue.40 , pp. 12207-12214
    • MARMOR, S.1    PETERSEN, C.P.2    RECK, F.3    YANG, W.4    GAO, N.5    FISHER, S.L.6
  • 63
    • 0036199409 scopus 로고    scopus 로고
    • Determination of ligand-MurB interactions by isothermal denaturation: Application as a secondary assay to complement high throughput screening
    • SARVER RW, ROGERS JM, EPPS DE: Determination of ligand-MurB interactions by isothermal denaturation: application as a secondary assay to complement high throughput screening. J. Biomol. Screen. (2002) 7(1):21-28.
    • (2002) J. Biomol. Screen , vol.7 , Issue.1 , pp. 21-28
    • SARVER, R.W.1    ROGERS, J.M.2    EPPS, D.E.3
  • 64
    • 0037527704 scopus 로고    scopus 로고
    • Molecular mechanism for inhibition of 3-hydroxy-3-methylglutarylCoA (HMG-CoA) reductase by rosuvastatin
    • HOLDGATE GA, WARD WH, MCTAGGART F: Molecular mechanism for inhibition of 3-hydroxy-3-methylglutarylCoA (HMG-CoA) reductase by rosuvastatin. Biochem. Soc. Trans. (2003) 31(3):528-531.
    • (2003) Biochem. Soc. Trans , vol.31 , Issue.3 , pp. 528-531
    • HOLDGATE, G.A.1    WARD, W.H.2    MCTAGGART, F.3
  • 65
    • 24344452953 scopus 로고    scopus 로고
    • Binding thermodynamics of statins binding to HMG-CoA Reductase
    • CARBONELL T, FREIRE E: Binding thermodynamics of statins binding to HMG-CoA Reductase. Biochemistry (2005) 44(35):11741-11748.
    • (2005) Biochemistry , vol.44 , Issue.35 , pp. 11741-11748
    • CARBONELL, T.1    FREIRE, E.2
  • 66
    • 3142567042 scopus 로고    scopus 로고
    • Advances in membrane receptor screening and analysis
    • COOPER MA: Advances in membrane receptor screening and analysis. J. Mol. Recognit. (2004) 17(4):286-315.
    • (2004) J. Mol. Recognit , vol.17 , Issue.4 , pp. 286-315
    • COOPER, M.A.1
  • 67
    • 11244254913 scopus 로고    scopus 로고
    • Investigation of ligand binding to the multidrug resistance protein EmrE by isothermal titration calorimetry
    • SIKORA CW, TURNER RJ: Investigation of ligand binding to the multidrug resistance protein EmrE by isothermal titration calorimetry. Biophys. J. (2005) 88(1):475-482.
    • (2005) Biophys. J , vol.88 , Issue.1 , pp. 475-482
    • SIKORA, C.W.1    TURNER, R.J.2
  • 68
    • 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 AG, BLUNDELL TL, ABELL C: Probing hot spots at protein-ligand binding sites: a fragment-based approach using biophysical methods. J. Med. Chem. (2006) 49(16):4992-5000.
    • (2006) J. Med. Chem , vol.49 , Issue.16 , pp. 4992-5000
    • CIULLI, A.1    WILLIAMS, G.2    SMITH, A.G.3    BLUNDELL, T.L.4    ABELL, C.5
  • 69
    • 33846433192 scopus 로고    scopus 로고
    • Measurement of the formation of complexes in tyrosine kinase-mediated signal transduction
    • LADBURY JE: Measurement of the formation of complexes in tyrosine kinase-mediated signal transduction. Acta Cryst. (2007) D63(1):26-31.
    • (2007) Acta Cryst , vol.D63 , Issue.1 , pp. 26-31
    • LADBURY, J.E.1
  • 70
    • 34248581436 scopus 로고    scopus 로고
    • Identification of novel fragment compounds targeted against the pY pocket of v-Src SH2 by computational and NMR screening and thermodynamic evaluation
    • Epub ahead of print
    • TAYLOR JD, GILBERT PJ, WILLIAMS MA, PITT WR, LADBURY JE: Identification of novel fragment compounds targeted against the pY pocket of v-Src SH2 by computational and NMR screening and thermodynamic evaluation. Proteins (2007). [Epub ahead of print].
    • (2007) Proteins
    • TAYLOR, J.D.1    GILBERT, P.J.2    WILLIAMS, M.A.3    PITT, W.R.4    LADBURY, J.E.5


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