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Volumn 7, Issue 3, 2010, Pages

The heat is on: Thermodynamic analysis in fragment-based drug discovery

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE A1 RECEPTOR; CAFFEINE; MAJOR URINARY PROTEIN; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE INHIBITOR; PHEROMONE DERIVATIVE; THEOPHYLLINE; UNCLASSIFIED DRUG; XANTHINE DERIVATIVE;

EID: 78650750341     PISSN: 17406749     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ddtec.2010.12.001     Document Type: Review
Times cited : (18)

References (65)
  • 1
    • 67649494337 scopus 로고    scopus 로고
    • Transforming fragments into candidates: Small becomes big in medicinal chemistry
    • G.E. de Kloe Transforming fragments into candidates: small becomes big in medicinal chemistry Drug Discov. Today 14 2009 630 646
    • (2009) Drug Discov. Today , vol.14 , pp. 630-646
    • De Kloe, G.E.1
  • 2
    • 70349425790 scopus 로고    scopus 로고
    • Recent progress in fragment-based lead discovery
    • M.N. Schulz, and R.E. Hubbard Recent progress in fragment-based lead discovery Curr. Opin. Pharmacol. 9 2009 615 621
    • (2009) Curr. Opin. Pharmacol. , vol.9 , pp. 615-621
    • Schulz, M.N.1    Hubbard, R.E.2
  • 3
    • 77953631827 scopus 로고    scopus 로고
    • A medicinal chemist's guide to molecular interactions
    • C. Bissantz A medicinal chemist's guide to molecular interactions J. Med. Chem. 53 2010 5061 5084
    • (2010) J. Med. Chem. , vol.53 , pp. 5061-5084
    • Bissantz, C.1
  • 4
    • 73449087370 scopus 로고    scopus 로고
    • Thermodynamic optimisation in drug discovery: A case study using carbonic anhydrase inhibitors
    • A.D. Scott Thermodynamic optimisation in drug discovery: a case study using carbonic anhydrase inhibitors ChemMedChem 4 2009 1985 1989
    • (2009) ChemMedChem , vol.4 , pp. 1985-1989
    • Scott, A.D.1
  • 5
    • 52049123291 scopus 로고    scopus 로고
    • Do enthalpy and entropy distinguish first in class from best in class?
    • E. Freire Do enthalpy and entropy distinguish first in class from best in class? Drug Discov. Today 13 2008 869 874
    • (2008) Drug Discov. Today , vol.13 , pp. 869-874
    • Freire, E.1
  • 6
    • 56549131177 scopus 로고    scopus 로고
    • The thermodynamics of protein-ligand interaction and solvation: Insights for ligand design
    • T.S. Olsson The thermodynamics of protein-ligand interaction and solvation: insights for ligand design J. Mol. Biol. 384 2008 1002 1017
    • (2008) J. Mol. Biol. , vol.384 , pp. 1002-1017
    • Olsson, T.S.1
  • 7
    • 35748934487 scopus 로고    scopus 로고
    • The influence of drug-like concepts on decision-making in medicinal chemistry
    • P.D. Leeson, and B. Springthorpe The influence of drug-like concepts on decision-making in medicinal chemistry Nat. Rev. Drug Discov. 6 2007 881 890
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 881-890
    • Leeson, P.D.1    Springthorpe, B.2
  • 8
    • 0037468884 scopus 로고    scopus 로고
    • A comparison of physiochemical property profiles of development and marketed oral drugs
    • M.C. Wenlock A comparison of physiochemical property profiles of development and marketed oral drugs J. Med. Chem. 46 2003 1250 1256
    • (2003) J. Med. Chem. , vol.46 , pp. 1250-1256
    • Wenlock, M.C.1
  • 9
    • 0029395478 scopus 로고
    • Win some, lose some: Enthalpy-entropy compensation in weak intermolecular interactions
    • J.D. Dunitz Win some, lose some: enthalpy-entropy compensation in weak intermolecular interactions Chem. Biol. 2 1995 709 712
    • (1995) Chem. Biol. , vol.2 , pp. 709-712
    • Dunitz, J.D.1
  • 12
    • 0842310293 scopus 로고    scopus 로고
    • A survey of the year 2002 literature on applications of isothermal titration calorimetry
    • M.J. Cliff, and J.E. Ladbury A survey of the year 2002 literature on applications of isothermal titration calorimetry J. Mol. Recognit. 16 2003 383 391
    • (2003) J. Mol. Recognit. , vol.16 , pp. 383-391
    • Cliff, M.J.1    Ladbury, J.E.2
  • 13
    • 8444250720 scopus 로고    scopus 로고
    • A survey of the year 2003 literature on applications of isothermal titration calorimetry
    • M.J. Cliff A survey of the year 2003 literature on applications of isothermal titration calorimetry J. Mol. Recognit. 17 2004 513 523
    • (2004) J. Mol. Recognit. , vol.17 , pp. 513-523
    • Cliff, M.J.1
  • 14
    • 31144454672 scopus 로고    scopus 로고
    • Survey of the year 2004: Literature on applications of isothermal titration calorimetry
    • A. Ababou, and J.E. Ladbury Survey of the year 2004: literature on applications of isothermal titration calorimetry J. Mol. Recognit. 19 2006 79 89
    • (2006) J. Mol. Recognit. , vol.19 , pp. 79-89
    • Ababou, A.1    Ladbury, J.E.2
  • 15
    • 33846527387 scopus 로고    scopus 로고
    • Survey of the year 2005: Literature on applications of isothermal titration calorimetry
    • A. Ababou, and J.E. Ladbury Survey of the year 2005: literature on applications of isothermal titration calorimetry J. Mol. Recognit. 20 2007 4 14
    • (2007) J. Mol. Recognit. , vol.20 , pp. 4-14
    • Ababou, A.1    Ladbury, J.E.2
  • 16
    • 39749105201 scopus 로고    scopus 로고
    • A survey of the year 2006 literature on applications of isothermal titration calorimetry
    • O. Okhrimenko, and I. Jelesarov A survey of the year 2006 literature on applications of isothermal titration calorimetry J. Mol. Recognit. 21 2008 1 19
    • (2008) J. Mol. Recognit. , vol.21 , pp. 1-19
    • Okhrimenko, O.1    Jelesarov, I.2
  • 17
    • 52649127984 scopus 로고    scopus 로고
    • A survey of the year 2007 literature on applications of isothermal titration calorimetry
    • S. Bjeli A survey of the year 2007 literature on applications of isothermal titration calorimetry J. Mol. Recognit. 21 2008 289 312
    • (2008) J. Mol. Recognit. , vol.21 , pp. 289-312
    • Bjeli, S.1
  • 18
    • 77956404669 scopus 로고    scopus 로고
    • Survey of the year 2008: Applications of isothermal titration calorimetry
    • R.J. Falconer Survey of the year 2008: applications of isothermal titration calorimetry J. Mol. Recognit. 23 2010 395 413
    • (2010) J. Mol. Recognit. , vol.23 , pp. 395-413
    • Falconer, R.J.1
  • 19
    • 33846108633 scopus 로고    scopus 로고
    • BindingDB: A web-accessible database of experimentally determined protein-ligand binding affinities
    • T. Liu BindingDB: a web-accessible database of experimentally determined protein-ligand binding affinities Nucleic Acids Res. 35 Suppl. 1 2007 D198 D201
    • (2007) Nucleic Acids Res. , vol.35 , Issue.SUPPL. 1
    • Liu, T.1
  • 20
    • 43949128085 scopus 로고    scopus 로고
    • PDBcal: A comprehensive dataset for receptor-ligand interactions with three-dimensional structures and binding thermodynamics from isothermal titration calorimetry
    • Liwei Li PDBcal: a comprehensive dataset for receptor-ligand interactions with three-dimensional structures and binding thermodynamics from isothermal titration calorimetry Chem. Biol. Drug Des. 71 2008 529 532
    • (2008) Chem. Biol. Drug Des. , vol.71 , pp. 529-532
    • Li, L.1
  • 21
    • 56549131177 scopus 로고    scopus 로고
    • The thermodynamics of protein-ligand interaction and solvation: Insights for ligand design
    • T.S.G. Olsson The thermodynamics of protein-ligand interaction and solvation: insights for ligand design J. Mol. Biol. 384 2008 1002 1017
    • (2008) J. Mol. Biol. , vol.384 , pp. 1002-1017
    • Olsson, T.S.G.1
  • 22
    • 0345293146 scopus 로고    scopus 로고
    • On the value of c: Can low affinity systems be studied by isothermal titration calorimetry?
    • W.B. Turnbull, and A.H. Daranas On the value of c: can low affinity systems be studied by isothermal titration calorimetry? J. Am. Chem. Soc. 125 2003 14859 14866
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 14859-14866
    • Turnbull, W.B.1    Daranas, A.H.2
  • 23
    • 78650722856 scopus 로고    scopus 로고
    • http://www.microcal.com/products/itc/itc200.asp
  • 24
    • 67649649592 scopus 로고    scopus 로고
    • Titration calorimetry standards and the precision of isothermal titration calorimetry data
    • L. Baranauskiene Titration calorimetry standards and the precision of isothermal titration calorimetry data Int. J. Mol. Sci. 10 2009 2752 2762
    • (2009) Int. J. Mol. Sci. , vol.10 , pp. 2752-2762
    • Baranauskiene, L.1
  • 25
    • 34548421643 scopus 로고    scopus 로고
    • Thermodynamics of binding interactions in the rational drug design process
    • G.A. Holdgate Thermodynamics of binding interactions in the rational drug design process Exp. Opin. Drug Discov. 2 2007 1103 1114
    • (2007) Exp. Opin. Drug Discov. , vol.2 , pp. 1103-1114
    • Holdgate, G.A.1
  • 26
    • 33750565735 scopus 로고    scopus 로고
    • Biomolecular interaction analysis in drug discovery using surface plasmon resonance technology
    • W. Huber, and F. Mueller Biomolecular interaction analysis in drug discovery using surface plasmon resonance technology Curr. Pharm. Des. 12 2006 3999 4021
    • (2006) Curr. Pharm. Des. , vol.12 , pp. 3999-4021
    • Huber, W.1    Mueller, F.2
  • 27
    • 74249116139 scopus 로고    scopus 로고
    • Fragment library screening and lead characterization using SPR biosensors
    • U.H. Danielson Fragment library screening and lead characterization using SPR biosensors Curr. Top. Med. Chem. 9 2009 1725 1735
    • (2009) Curr. Top. Med. Chem. , vol.9 , pp. 1725-1735
    • Danielson, U.H.1
  • 28
    • 0030971891 scopus 로고    scopus 로고
    • Possible origin of differences between van't Hoff and calorimetric enthalpy estimates
    • J.B. Chaires Possible origin of differences between van't Hoff and calorimetric enthalpy estimates Biophys. Chem. 64 1997 15 23
    • (1997) Biophys. Chem. , vol.64 , pp. 15-23
    • Chaires, J.B.1
  • 29
    • 0035852865 scopus 로고    scopus 로고
    • Van't Hoff and calorimetric enthalpies from isothermal titration calorimetry: Are there significant discrepancies?
    • J.R. Horn Van't Hoff and calorimetric enthalpies from isothermal titration calorimetry: are there significant discrepancies? Biochemistry 40 2001 1774 1778
    • (2001) Biochemistry , vol.40 , pp. 1774-1778
    • Horn, J.R.1
  • 30
    • 0037062633 scopus 로고    scopus 로고
    • Van't Hoff and calorimetric enthalpies II: Effects of linked equilibria
    • J.R. Horn van't Hoff and calorimetric enthalpies II: effects of linked equilibria Biochemistry 41 2002 7501 7507
    • (2002) Biochemistry , vol.41 , pp. 7501-7507
    • Horn, J.R.1
  • 31
    • 0028805495 scopus 로고
    • Significant discrepancies between van't Hoff and calorimetric enthalpies. II
    • Y. Liu, and J.M. Sturtevant Significant discrepancies between van't Hoff and calorimetric enthalpies. II Protein Sci. 4 1995 2559 2561
    • (1995) Protein Sci. , vol.4 , pp. 2559-2561
    • Liu, Y.1    Sturtevant, J.M.2
  • 32
    • 0030995171 scopus 로고    scopus 로고
    • Significant discrepancies between van't Hoff and calorimetric enthalpies. III
    • Y. Liu, and J.M. Sturtevant Significant discrepancies between van't Hoff and calorimetric enthalpies. III Biophys. Chem. 64 1-3 1997 121 126
    • (1997) Biophys. Chem. , vol.64 , Issue.13 , pp. 121-126
    • Liu, Y.1    Sturtevant, J.M.2
  • 33
    • 0029064484 scopus 로고
    • Significant discrepancies between van't Hoff and calorimetric enthalpies
    • H. Naghibi Significant discrepancies between van't Hoff and calorimetric enthalpies Proc. Natl. Acad. Sci. U. S. A. 92 12 1995 5597 5599
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , Issue.12 , pp. 5597-5599
    • Naghibi, H.1
  • 34
    • 33644748080 scopus 로고    scopus 로고
    • Van't Hoff analysis of K degrees (T): How good. or bad?
    • J. Tellinghuisen Van't Hoff analysis of K degrees (T): how good. or bad? Biophys. Chem. 120 2006 114 120
    • (2006) Biophys. Chem. , vol.120 , pp. 114-120
    • Tellinghuisen, J.1
  • 35
    • 33845437051 scopus 로고    scopus 로고
    • Calibration in isothermal titration calorimetry: Heat and cell volume from heat of dilution of NaCl(aq)
    • J. Tellinghuisen Calibration in isothermal titration calorimetry: heat and cell volume from heat of dilution of NaCl(aq) Anal. Biochem. 360 2007 47 55
    • (2007) Anal. Biochem. , vol.360 , pp. 47-55
    • Tellinghuisen, J.1
  • 36
    • 2942552633 scopus 로고    scopus 로고
    • The ABRF-MIRG'02 study: Assembly state, thermodynamic, and kinetic analysis of an enzyme/inhibitor interaction
    • D.G. Myszka The ABRF-MIRG'02 study: assembly state, thermodynamic, and kinetic analysis of an enzyme/inhibitor interaction J. Biomol. Tech. 14 2003 247 269
    • (2003) J. Biomol. Tech. , vol.14 , pp. 247-269
    • Myszka, D.G.1
  • 37
    • 33947666565 scopus 로고    scopus 로고
    • Thermodynamic benchmark study using Biacore technology
    • I. Navratilova Thermodynamic benchmark study using Biacore technology Anal. Biochem. 364 1 2007 67 77
    • (2007) Anal. Biochem. , vol.364 , Issue.1 , pp. 67-77
    • Navratilova, I.1
  • 38
    • 0036228119 scopus 로고    scopus 로고
    • Direct comparison of binding equilibrium, thermodynamic, and rate constants determined by surface- and solution-based biophysical methods
    • S.N. Yasmina, and Day Direct comparison of binding equilibrium, thermodynamic, and rate constants determined by surface- and solution-based biophysical methods Protein Sci. 11 2002 1017 1025
    • (2002) Protein Sci. , vol.11 , pp. 1017-1025
    • Yasmina, S.N.1    Day2
  • 39
    • 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
    • M.A. Wear, and M.D. Walkinshaw 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. 359 2006 285 287
    • (2006) Anal. Biochem. , vol.359 , pp. 285-287
    • Wear, M.A.1    Walkinshaw, M.D.2
  • 40
    • 34250195790 scopus 로고    scopus 로고
    • Histamine H3-receptor agonists and imidazole-based H3-receptor antagonists can be thermodynamically discriminated
    • E.A. Harper, and J.W. Black Histamine H3-receptor agonists and imidazole-based H3-receptor antagonists can be thermodynamically discriminated Br. J. Pharmacol. 151 2007 504 517
    • (2007) Br. J. Pharmacol. , vol.151 , pp. 504-517
    • Harper, E.A.1    Black, J.W.2
  • 41
    • 0029931275 scopus 로고    scopus 로고
    • Distinct thermodynamic parameters of serotonin 5-HT3 agonists and antagonists to displace [3H]granisetron binding
    • G. Maksay Distinct thermodynamic parameters of serotonin 5-HT3 agonists and antagonists to displace [3H]granisetron binding J. Neurochem. 67 1996 407 412
    • (1996) J. Neurochem. , vol.67 , pp. 407-412
    • Maksay, G.1
  • 42
    • 0029670134 scopus 로고    scopus 로고
    • Thermodynamics of 5-HT3 receptor binding discriminates agonistic from antagonistic behaviour
    • P.A. Borea Thermodynamics of 5-HT3 receptor binding discriminates agonistic from antagonistic behaviour Eur. J. Pharmacol. 298 1996 329 334
    • (1996) Eur. J. Pharmacol. , vol.298 , pp. 329-334
    • Borea, P.A.1
  • 43
    • 0032559041 scopus 로고    scopus 로고
    • Structural and thermochemical characterization of lipoxygenase-catechol complexes
    • C. Pham Structural and thermochemical characterization of lipoxygenase-catechol complexes Biochemistry 37 1998 17952 17957
    • (1998) Biochemistry , vol.37 , pp. 17952-17957
    • Pham, C.1
  • 44
    • 34247252410 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli ketopantoate reductase in a ternary complex with NADP + and pantoate bound: Substrate recognition, conformational change, and cooperativity
    • A. Ciulli Crystal structure of Escherichia coli ketopantoate reductase in a ternary complex with NADP + and pantoate bound: substrate recognition, conformational change, and cooperativity J. Biol. Chem. 282 11 2007 8487 8497
    • (2007) J. Biol. Chem. , vol.282 , Issue.11 , pp. 8487-8497
    • Ciulli, A.1
  • 45
    • 67649840628 scopus 로고    scopus 로고
    • Contribution of binding enthalpy and entropy to affinity of antagonist and agonist binding at human and guinea pig histamine h1-receptor
    • H-J. Wittmann Contribution of binding enthalpy and entropy to affinity of antagonist and agonist binding at human and guinea pig histamine h1-receptor Mol. Pharmacol. 76 2009 25 37
    • (2009) Mol. Pharmacol. , vol.76 , pp. 25-37
    • Wittmann, H.-J.1
  • 46
    • 33846698884 scopus 로고    scopus 로고
    • PH-tuneable binding of 2'-phospho-ADP-ribose to ketopantoate reductase: A structural and calorimetric study
    • A. Ciulli pH-tuneable binding of 2'-phospho-ADP-ribose to ketopantoate reductase: a structural and calorimetric study Acta Crystallogr. D: Biol. Crystallogr. 63 Pt 2 2007 171 178
    • (2007) Acta Crystallogr. D: Biol. Crystallogr. , vol.63 , Issue.PART 2 , pp. 171-178
    • Ciulli, A.1
  • 47
    • 0037845104 scopus 로고    scopus 로고
    • Thermodynamic analysis of binding between mouse major urinary protein-I and the pheromone 2-sec-butyl-4,5-dihydrothiazole
    • S.D. Sharrow Thermodynamic analysis of binding between mouse major urinary protein-I and the pheromone 2-sec-butyl-4,5-dihydrothiazole Biochemistry 42 2003 6302 6309
    • (2003) Biochemistry , vol.42 , pp. 6302-6309
    • Sharrow, S.D.1
  • 48
    • 27344436962 scopus 로고    scopus 로고
    • Measurements of binding thermodynamics in drug discovery
    • G.A. Holdgate, and H.J. Ward Measurements of binding thermodynamics in drug discovery Drug Discov. Today 10 2005 1543 1550
    • (2005) Drug Discov. Today , vol.10 , pp. 1543-1550
    • Holdgate, G.A.1    Ward, H.J.2
  • 49
    • 78650717816 scopus 로고    scopus 로고
    • Only unique fragment-protein complexes were incorporated. In cases where complexes were measured under different conditions (concentration of salts, p., temperature, the presence of co-factor, etc.), only the data from one set of conditions were included
    • Only unique fragment-protein complexes were incorporated. In cases where complexes were measured under different conditions (concentration of salts, p., temperature, the presence of co-factor, etc.), only the data from one set of conditions were included
  • 50
    • 13544263437 scopus 로고    scopus 로고
    • Activation of ionotropic receptors and thermodynamics of binding
    • G. Maksay Activation of ionotropic receptors and thermodynamics of binding Neurochem. Int. 46 2005 281 291
    • (2005) Neurochem. Int. , vol.46 , pp. 281-291
    • Maksay, G.1
  • 51
    • 0034571319 scopus 로고    scopus 로고
    • Can thermodynamic measurements of receptor binding yield information on drug affinity and efficacy?
    • P.A. Borea Can thermodynamic measurements of receptor binding yield information on drug affinity and efficacy? Biochem. Pharmacol. 60 2000 1549 1556
    • (2000) Biochem. Pharmacol. , vol.60 , pp. 1549-1556
    • Borea, P.A.1
  • 52
    • 0029684422 scopus 로고    scopus 로고
    • Binding thermodynamics at A1 and A2A adenosine receptors
    • P.A. Borea Binding thermodynamics at A1 and A2A adenosine receptors Life Sci. 59 1996 1373 1388
    • (1996) Life Sci. , vol.59 , pp. 1373-1388
    • Borea, P.A.1
  • 53
    • 0032523119 scopus 로고    scopus 로고
    • Binding thermodynamics at the human neuronal nicotine receptor
    • P.A. Borea Binding thermodynamics at the human neuronal nicotine receptor Biochem. Pharmacol. 55 1998 1189 1197
    • (1998) Biochem. Pharmacol. , vol.55 , pp. 1189-1197
    • Borea, P.A.1
  • 54
    • 0027093347 scopus 로고
    • Binding thermodynamics of A1 adenosine receptor ligands
    • P.A. Borea Binding thermodynamics of A1 adenosine receptor ligands Mol. Neuropharmacol. 2 1992 273 281
    • (1992) Mol. Neuropharmacol. , vol.2 , pp. 273-281
    • Borea, P.A.1
  • 55
    • 42549142092 scopus 로고    scopus 로고
    • An update on the mechanisms of the psychostimulant effects of caffeine
    • S. Ferre An update on the mechanisms of the psychostimulant effects of caffeine J. Neurochem. 105 2008 1067 1079
    • (2008) J. Neurochem. , vol.105 , pp. 1067-1079
    • Ferre, S.1
  • 56
    • 33847677634 scopus 로고    scopus 로고
    • Exploring the subtleties of drug-receptor interactions: The case of matrix metalloproteinases
    • I. Bertini Exploring the subtleties of drug-receptor interactions: the case of matrix metalloproteinases J. Am. Chem. Soc. 129 2007 2466 2475
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 2466-2475
    • Bertini, I.1
  • 57
    • 77952713014 scopus 로고    scopus 로고
    • Entropic contribution to the linking coefficient in fragment based drug design: A case study
    • V. Borsi Entropic contribution to the linking coefficient in fragment based drug design: a case study J. Med. Chem. 53 2010 4285 4289
    • (2010) J. Med. Chem. , vol.53 , pp. 4285-4289
    • Borsi, V.1
  • 58
    • 67349171544 scopus 로고    scopus 로고
    • Impact of linker strain and flexibility in the design of a fragment-based inhibitor
    • S. Chung Impact of linker strain and flexibility in the design of a fragment-based inhibitor Nat. Chem. Biol. 5 2009 407 413
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 407-413
    • Chung, S.1
  • 59
    • 33144470698 scopus 로고    scopus 로고
    • Application of fragment screening and fragment linking to the discovery of novel thrombin inhibitors
    • N. Howard Application of fragment screening and fragment linking to the discovery of novel thrombin inhibitors J. Med. Chem. 49 2006 1346 1355
    • (2006) J. Med. Chem. , vol.49 , pp. 1346-1355
    • Howard, N.1
  • 60
    • 23944481864 scopus 로고    scopus 로고
    • Van der Waals interactions dominate ligand-protein association in a protein binding site occluded from solvent water
    • E. Barratt Van der Waals interactions dominate ligand-protein association in a protein binding site occluded from solvent water J. Am. Chem. Soc. 127 2005 11827 11834
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 11827-11834
    • Barratt, E.1
  • 61
    • 10744231573 scopus 로고    scopus 로고
    • Thermodynamics of binding of 2-methoxy-3-isopropylpyrazine and 2-methoxy-3-isobutylpyrazine to the major urinary protein
    • R.J. Bingham Thermodynamics of binding of 2-methoxy-3-isopropylpyrazine and 2-methoxy-3-isobutylpyrazine to the major urinary protein J. Am. Chem. Soc. 126 2004 1675 1681
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 1675-1681
    • Bingham, R.J.1
  • 62
    • 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
    • J.D. Taylor Identification of novel fragment compounds targeted against the pY pocket of v-Src SH2 by computational and NMR screening and thermodynamic evaluation Proteins 67 2007 981 990
    • (2007) Proteins , vol.67 , pp. 981-990
    • Taylor, J.D.1
  • 63
    • 0033451033 scopus 로고    scopus 로고
    • Estimating binding constants - The hydrophobic effect and cooperativity
    • D.H. Williams, and B. Bardsley Estimating binding constants - the hydrophobic effect and cooperativity Perspect. Drug Discov. Des. 17 1999 43 59
    • (1999) Perspect. Drug Discov. Des. , vol.17 , pp. 43-59
    • Williams, D.H.1    Bardsley, B.2
  • 64
    • 1942453243 scopus 로고    scopus 로고
    • Ligand efficiency: A useful metric for lead selection
    • A.L. Hopkins Ligand efficiency: a useful metric for lead selection Drug Discov. Today 9 2004 430 431
    • (2004) Drug Discov. Today , vol.9 , pp. 430-431
    • Hopkins, A.L.1
  • 65
    • 74149083849 scopus 로고    scopus 로고
    • Adding calorimetric data to decision making in lead discovery: A hot tip
    • J.E. Ladbury Adding calorimetric data to decision making in lead discovery: a hot tip Nat. Rev. Drug Discov. 9 2010 23 27
    • (2010) Nat. Rev. Drug Discov. , vol.9 , pp. 23-27
    • Ladbury, J.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.