메뉴 건너뛰기




Volumn 15, Issue 2, 2016, Pages 87-95

The drug-target residence time model: A 10-year retrospective

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOOXYGENASE 1; CYCLOOXYGENASE 2; FINASTERIDE; HEAT SHOCK PROTEIN 90; PROTEIN ARGININE METHYLTRANSFERASE; SAQUINAVIR; MACROMOLECULE; PROTEIN BINDING;

EID: 84957845231     PISSN: 14741776     EISSN: 14741784     Source Type: Journal    
DOI: 10.1038/nrd.2015.18     Document Type: Review
Times cited : (540)

References (54)
  • 1
    • 33748325882 scopus 로고    scopus 로고
    • Drug-Target residence time and its implications for lead optimization
    • Copeland, R. A., Pompliano, D. L., & Meek, T. D. Drug-Target residence time and its implications for lead optimization. Nat. Rev. Drug Discov. 5, 730-739 (2006
    • (2006) Nat. Rev. Drug Discov , vol.5 , pp. 730-739
    • Copeland, R.A.1    Pompliano, D.L.2    Meek, T.D.3
  • 2
    • 44049103958 scopus 로고    scopus 로고
    • Residence time of receptor-ligand complexes and its effect on biological function
    • Tummino, P. J., & Copeland, R. A. Residence time of receptor-ligand complexes and its effect on biological function. Biochemistry 47, 5481-5492 (2008
    • (2008) Biochemistry , vol.47 , pp. 5481-5492
    • Tummino, P.J.1    Copeland, R.A.2
  • 3
    • 77950197835 scopus 로고    scopus 로고
    • The dynamics of drug-Target interactions: Drug-Target residence time and its impact on efficacy and safety
    • Copeland, R. A. The dynamics of drug-Target interactions: drug-Target residence time and its impact on efficacy and safety. Expert Opin. Drug Discov. 5, 305-310 (2010
    • (2010) Expert Opin. Drug Discov , vol.5 , pp. 305-310
    • Copeland, R.A.1
  • 4
    • 80052462704 scopus 로고    scopus 로고
    • Conformational adaptation in drug-Target interactions and residence time
    • Copeland, R. A. Conformational adaptation in drug-Target interactions and residence time. Future Med. Chem. 3, 1491-1501 (2011
    • (2011) Future Med. Chem , vol.3 , pp. 1491-1501
    • Copeland, R.A.1
  • 6
    • 84910003834 scopus 로고    scopus 로고
    • A universal homogeneous assay for high-Throughput determination of binding kinetics
    • Schiele, F., Ayaz, P., & Fernandez-Montalvan, A. A universal homogeneous assay for high-Throughput determination of binding kinetics. Anal. Biochem. 468, 42-49 (2014
    • (2014) Anal. Biochem , vol.468 , pp. 42-49
    • Schiele, F.1    Ayaz, P.2    Fernandez-Montalvan, A.3
  • 8
    • 0028139275 scopus 로고
    • Mechanism of selective inhibition of the inducible isoform of prostaglandin G/H synthase
    • Copeland R. A., et al. Mechanism of selective inhibition of the inducible isoform of prostaglandin G/H synthase. Proc. Natl Acad. Sci. USA 91, 11202-11206 (1994
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 11202-11206
    • Copeland, R.A.1
  • 9
    • 0029937631 scopus 로고    scopus 로고
    • Mechanism-based inhibition of human steroid 5α reductase by finasteride: Enzyme catalyzed formation of NADP-dihydrofinasteride a potent bisubstrate analog inhibitor
    • Bull, H. G., et al. Mechanism-based inhibition of human steroid 5α reductase by finasteride: enzyme catalyzed formation of NADP-dihydrofinasteride, a potent bisubstrate analog inhibitor. J. Am. Chem. Soc. USA 118, 2359-2365 (1996
    • (1996) J. Am. Chem. Soc. USA , vol.118 , pp. 2359-2365
    • Bull, H.G.1
  • 10
    • 33646725129 scopus 로고    scopus 로고
    • A biochemical rationale for the anticancer effects of HSP90 inhibitors: Slow tight binding inhibition by geldanamycin and its analogues
    • Gooljarsingh, L. T., et al. A biochemical rationale for the anticancer effects of HSP90 inhibitors: slow, tight binding inhibition by geldanamycin and its analogues. Proc. Natl Acad. Sci. USA 103, 7625-7630 (2006
    • (2006) Proc Natl Acad. Sci. USA , vol.103 , pp. 7625-7630
    • Gooljarsingh, L.T.1
  • 11
    • 0023728105 scopus 로고
    • The behavior and significance of slow-binding enzyme inhibitors
    • Morrison, J. F., & Walsh, C. T. The behavior and significance of slow-binding enzyme inhibitors. Adv. Enzymol. Relat. Areas Mol. Biol. 61, 201-299 (1988
    • (1988) Adv. Enzymol. Relat. Areas Mol. Biol , vol.61 , pp. 201-299
    • Morrison, J.F.1    Walsh, C.T.2
  • 12
    • 77950278049 scopus 로고    scopus 로고
    • Integrating surface plasmon resonance biosensor-based interaction kinetic analyses into the lead discovery and optimization process
    • Danielson, U. H. Integrating surface plasmon resonance biosensor-based interaction kinetic analyses into the lead discovery and optimization process. Future Med. Chem. 1, 1399-1414 (2009
    • (2009) Future Med. Chem , vol.1 , pp. 1399-1414
    • Danielson, U.H.1
  • 13
    • 84881171375 scopus 로고    scopus 로고
    • Pharmacokinetics and the drug-Target residence time concept
    • Dahl, G., & Akerud, T. Pharmacokinetics and the drug-Target residence time concept. Drug Discov. Today 18, 697-707 (2013
    • (2013) Drug Discov. Today , vol.18 , pp. 697-707
    • Dahl, G.1    Akerud, T.2
  • 14
    • 67649973722 scopus 로고    scopus 로고
    • The importance of drug-Target residence time
    • Zhang, R., & Monsma, F. The importance of drug-Target residence time. Curr. Opin. Drug Discov. 12, 488-496 (2009
    • (2009) Curr. Opin. Drug Discov , vol.12 , pp. 488-496
    • Zhang, R.1    Monsma, F.2
  • 15
    • 77955329488 scopus 로고    scopus 로고
    • Drug-Target residence time: Critical information for lead optimization
    • Lu, H., & Tonge, P. J. Drug-Target residence time: critical information for lead optimization. Curr. Opin. Chem. Biol. 14, 467-474 (2010
    • (2010) Curr. Opin. Chem. Biol , vol.14 , pp. 467-474
    • Lu, H.1    Tonge, P.J.2
  • 16
    • 33644542447 scopus 로고    scopus 로고
    • Cooperative hydrogen bond interactions in the streptavidin-biotin system
    • Hyre D. E., et al. Cooperative hydrogen bond interactions in the streptavidin-biotin system. Protein Sci. 15, 459-467 (2006
    • (2006) Protein Sci , vol.15 , pp. 459-467
    • Hyre, D.E.1
  • 17
    • 0030468331 scopus 로고    scopus 로고
    • Human immunodeficiency virus: Mutations in the viral protease that confer resistance to saquinavir increase the dissociation rate constant of the protease-saquinavir complex
    • Maschera B., et al. Human immunodeficiency virus: mutations in the viral protease that confer resistance to saquinavir increase the dissociation rate constant of the protease-saquinavir complex. J. Biol. Chem. 271, 33231-33235 (1996
    • (1996) J. Biol. Chem , vol.271 , pp. 33231-33235
    • Maschera, B.1
  • 18
    • 84868101932 scopus 로고    scopus 로고
    • Conformational adaption drives potent selective and durable inhibition of the human protein methyltransferase DOT1L
    • Basavapathruni, A., et al. Conformational adaption drives potent, selective and durable inhibition of the human protein methyltransferase DOT1L. Chem. Biol. Drug Des. 80, 971-980 (2012
    • (2012) Chem. Biol. Drug des , vol.80 , pp. 971-980
    • Basavapathruni, A.1
  • 20
    • 84937760506 scopus 로고    scopus 로고
    • Which trails are your drugs taking?
    • Zhang, R. Which trails are your drugs taking? Nat. Chem. Biol. 11, 382-383 (2015
    • (2015) Nat. Chem. Biol , vol.11 , pp. 382-383
    • Zhang, R.1
  • 21
    • 0037028049 scopus 로고    scopus 로고
    • Relationships between structure and interaction kinetics for HIV-protease inhibitors
    • Markgren P. O., et al. Relationships between structure and interaction kinetics for HIV-protease inhibitors. J. Med. Chem. 45, 5430-5439 (2002
    • (2002) J. Med. Chem , vol.45 , pp. 5430-5439
    • Markgren, P.O.1
  • 22
    • 77956805081 scopus 로고    scopus 로고
    • Rebinding: Or why drugs may act longer in vivo than expected from their in vitro target residence time
    • Vauquelin, G. Rebinding: or why drugs may act longer in vivo than expected from their in vitro target residence time. Expert Opin. Drug Discov. 5, 927-941 (2010
    • (2010) Expert Opin. Drug Discov , vol.5 , pp. 927-941
    • Vauquelin, G.1
  • 23
    • 77956309074 scopus 로고    scopus 로고
    • Long-lasting target binding and rebinding as mechanisms to prolong in vivo drug action
    • Vauquelin, G., & Charlton, S. J. Long-lasting target binding and rebinding as mechanisms to prolong in vivo drug action. Br. J. Pharmacol. 161, 488-508 (2010
    • (2010) Br. J. Pharmacol , vol.161 , pp. 488-508
    • Vauquelin, G.1    Charlton, S.J.2
  • 24
    • 84899111509 scopus 로고    scopus 로고
    • A structural and energetic model for the slow-onset inhibition of the Mycobacterium tuberculosis enoyl-CP reductase InhA
    • Li H. J., et al. A structural and energetic model for the slow-onset inhibition of the Mycobacterium tuberculosis enoyl-CP reductase InhA. ACS Chem. Biol. 9, 986-993 (2014
    • (2014) ACS Chem Biol , vol.9 , pp. 986-993
    • Li, H.J.1
  • 25
    • 84938594669 scopus 로고    scopus 로고
    • Rational modulation of the induced-fit conformational change for slow-onset inhibition of Mycobacterium tuberculosis InhA
    • Lai C. T., et al. Rational modulation of the induced-fit conformational change for slow-onset inhibition of Mycobacterium tuberculosis InhA. Biochemistry 54, 4683-4691 (2015
    • (2015) Biochemistry , vol.54 , pp. 4683-4691
    • Lai, C.T.1
  • 26
    • 84922224593 scopus 로고    scopus 로고
    • Kinetics of protein-ligand unbinding: Predicting pathways, rates and rate-limiting steps
    • Tiwary, P., Limongelli, V., Salvalaglio, M., & Parrinello, M. Kinetics of protein-ligand unbinding: predicting pathways, rates and rate-limiting steps. Proc. Natl Acad. Sci. USA 112, E386-E391 (2009
    • (2009) Proc. Natl Acad. Sci. USA , vol.112 , pp. E386-E391
    • Tiwary, P.1    Limongelli, V.2    Salvalaglio, M.3    Parrinello, M.4
  • 27
    • 84949324412 scopus 로고    scopus 로고
    • Design strategies to address kinetics of drug binding and residence time
    • Cusack K. P., et al. Design strategies to address kinetics of drug binding and residence time. Bioorg. Med. Chem. Lett. 25, 2019-2027 (2015
    • (2015) Bioorg. Med. Chem. Lett , vol.25 , pp. 2019-2027
    • Cusack, K.P.1
  • 28
    • 84896928662 scopus 로고    scopus 로고
    • Long residence time inhibition of EZH2 in activated polycomb repressive complex 2
    • Van Aller G., et al. Long residence time inhibition of EZH2 in activated polycomb repressive complex 2. ACS Chem. Biol. 9, 622-629 (2014
    • (2014) ACS Chem. Biol , vol.9 , pp. 622-629
    • Van Aller, G.1
  • 29
    • 84937397052 scopus 로고    scopus 로고
    • A selective inhibitor of PRMT5 with in vivo and in vitro potency in MCL models
    • Chan-Penebre E., et al. A selective inhibitor of PRMT5 with in vivo and in vitro potency in MCL models. Nat. Chem. Biol. 11, 432-437 (2015
    • (2015) Nat Chem. Biol , vol.11 , pp. 432-437
    • Chan-Penebre, E.1
  • 30
    • 65249139978 scopus 로고    scopus 로고
    • Slow-onset inhibition of the FabI enoyl reductase from Francisella tularensis: Residence time and in vivo activity
    • Lu H., et al. Slow-onset inhibition of the FabI enoyl reductase from Francisella tularensis: residence time and in vivo activity. ACS Chem. Biol. 4, 221-231 (2009
    • (2009) ACS Chem. Biol , vol.4 , pp. 221-231
    • Lu, H.1
  • 31
    • 84863228021 scopus 로고    scopus 로고
    • Functional efficacy of adenosine A2A receptor agonists is positively correlated to their receptor residence time
    • Guo, D., Mulder-Krieger, T., Ijzerman, A. P., & Heitman, L. H. Functional efficacy of adenosine A2A receptor agonists is positively correlated to their receptor residence time. Br. J. Pharmacol. 166, 1846-1859 (2012
    • (2012) Br. J. Pharmacol , vol.166 , pp. 1846-1859
    • Guo, D.1    Mulder-Krieger, T.2    Ijzerman, A.P.3    Heitman, L.H.4
  • 32
    • 52949089027 scopus 로고    scopus 로고
    • Enzymes with lid-gated active sites must operate by an induced fit mechanism instead of conformational selection
    • Sullivan, S. M., & Holyoak, T. Enzymes with lid-gated active sites must operate by an induced fit mechanism instead of conformational selection. Proc. Natl Acad. Sci. USA 105, 13829-13834 (2008
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 13829-13834
    • Sullivan, S.M.1    Holyoak, T.2
  • 33
    • 61749086407 scopus 로고    scopus 로고
    • Potent inhibitors of HIV 1 integrase display a two-step slow-binding inhibition mechanism which is absent in a drug-resistant T661/M1541 mutant
    • Garvey, E. P., et al. Potent inhibitors of HIV 1 integrase display a two-step, slow-binding inhibition mechanism which is absent in a drug-resistant T661/M1541 mutant. Biochemistry 48, 1644-1653 (2009
    • (2009) Biochemistry , vol.48 , pp. 1644-1653
    • Garvey, E.P.1
  • 34
    • 0034616953 scopus 로고    scopus 로고
    • The crystal structure of tetrameric methionine adenosyltransferase from rat liver reveals the methionine-binding site
    • González B., et al. The crystal structure of tetrameric methionine adenosyltransferase from rat liver reveals the methionine-binding site. J. Mol. Biol. 300, 363-375 (2000
    • (2000) J. Mol. Biol , vol.300 , pp. 363-375
    • González, B.1
  • 35
    • 0042859759 scopus 로고    scopus 로고
    • The relationship between side reactions and slow inhibition of ribulose-bisphosphate carboxylase revealed by a loop 6 mutant of the tobacco enzyme
    • Pearce, F. G., & Andrews, T. J. The relationship between side reactions and slow inhibition of ribulose-bisphosphate carboxylase revealed by a loop 6 mutant of the tobacco enzyme. J. Biol. Chem. 278, 32526-32536 (2003
    • (2003) J. Biol. Chem , vol.278 , pp. 32526-32536
    • Pearce, F.G.1    Andrews, T.J.2
  • 36
    • 0347301743 scopus 로고    scopus 로고
    • Hepatitis C NS3 protease inhibition by peptidyl-α ketoamide inhibitors: Kinetic mechanism and structure
    • Liu Y., et al. Hepatitis C NS3 protease inhibition by peptidyl-α ketoamide inhibitors: kinetic mechanism and structure. Arch. Biochem. Biophys. 421, 207-216 (2004
    • (2004) Arch. Biochem. Biophys , vol.421 , pp. 207-216
    • Liu, Y.1
  • 37
    • 4344567210 scopus 로고    scopus 로고
    • Kinetic and structural analysis of the increased affinity of enoyl-CP (acyl-carrier protein) reductase for triclosan in the presence of NAD
    • Kapoor M., et al. Kinetic and structural analysis of the increased affinity of enoyl-CP (acyl-carrier protein) reductase for triclosan in the presence of NAD. Biochem. J. 381, 725-733 (2004
    • (2004) Biochem. J. , vol.381 , pp. 725-733
    • Kapoor, M.1
  • 38
    • 84857190619 scopus 로고    scopus 로고
    • Evidence for dynamics in proteins as a mechanism for ligand dissociation
    • Carroll M. J., et al. Evidence for dynamics in proteins as a mechanism for ligand dissociation. Nat. Chem. Biol. 8, 246-252 (2012
    • (2012) Nat. Chem. Biol , vol.8 , pp. 246-252
    • Carroll, M.J.1
  • 39
    • 77951987627 scopus 로고    scopus 로고
    • A slow tight binding inhibitor of InhA, the enoyl-cyl carrier protein reductase from Mycobacterium tuberculosis
    • Luckner, S. R., et al. A slow, tight binding inhibitor of InhA, the enoyl-cyl carrier protein reductase from Mycobacterium tuberculosis. J. Biol. Chem. 285, 14330-14337 (2010
    • (2010) J. Biol Chem , vol.285 , pp. 14330-14337
    • Luckner, S.R.1
  • 40
    • 63749101636 scopus 로고    scopus 로고
    • Structural biology contributions to tyrosine kinase drug discovery
    • Cowan-Jacob, S. W., Mobitz, H., & Fabbro, D. Structural biology contributions to tyrosine kinase drug discovery. Curr. Opin. Cell Biol. 21, 280-287 (2009
    • (2009) Curr. Opin. Cell Biol , vol.21 , pp. 280-287
    • Cowan-Jacob, S.W.1    Mobitz, H.2    Fabbro, D.3
  • 41
    • 0029911267 scopus 로고    scopus 로고
    • Flexibility of the NSAID binding site in the structure of human cyclooxygenase 2
    • Luong C., et al. Flexibility of the NSAID binding site in the structure of human cyclooxygenase 2. Nat. Struct. Biol. 3, 927-933 (1996
    • (1996) Nat. Struct. Biol , vol.3 , pp. 927-933
    • Luong, C.1
  • 42
    • 83055179348 scopus 로고    scopus 로고
    • Shielded hydrogen bonds as structural determinants of binding kinetics: Application in drug design
    • Schmidtke, P., Luque, F. J., Murray, J. B., & Barril, X. Shielded hydrogen bonds as structural determinants of binding kinetics: application in drug design. J. Am. Chem. Soc. 133, 18903-18910 (2011
    • (2011) J. Am. Chem. Soc , vol.133 , pp. 18903-18910
    • Schmidtke, P.1    Luque, F.J.2    Murray, J.B.3    Barril, X.4
  • 43
    • 84931572829 scopus 로고    scopus 로고
    • Prolonged and tunable residence time using reversible covalent kinase inhibitors
    • Bradshaw J. M., et al. Prolonged and tunable residence time using reversible covalent kinase inhibitors. Nat. Chem. Biol. 11, 525-531 (2015
    • (2015) Nat. Chem. Biol , vol.11 , pp. 525-531
    • Bradshaw, J.M.1
  • 44
    • 84937760572 scopus 로고    scopus 로고
    • Translating slow-binding inhibition kinetics into cellular and in vivo effects
    • Walkup G. K., et al. Translating slow-binding inhibition kinetics into cellular and in vivo effects. Nat.Chem. Biol. 11, 416-423 (2015
    • (2015) Nat.Chem. Biol , vol.11 , pp. 416-423
    • Walkup, G.K.1
  • 45
    • 0037093079 scopus 로고    scopus 로고
    • Evidence that thrombocytopenia observed in humans treated with orally bioavailable glycoprotein IIb/IIIa antagonists is immune mediated
    • Billheimer J. T., et al. Evidence that thrombocytopenia observed in humans treated with orally bioavailable glycoprotein IIb/IIIa antagonists is immune mediated. Blood 99, 3540-3546 (2002
    • (2002) Blood , vol.99 , pp. 3540-3546
    • Billheimer, J.T.1
  • 46
    • 0037222079 scopus 로고    scopus 로고
    • Prospective testing for drug-dependent antibodies reduces the incidence of thrombocytopenia observed with the small molecule glycoprotein IIb/IIIa antagonist roxifiban: Implications for the etiology of thrombocytopenia
    • Seiffert D., et al. Prospective testing for drug-dependent antibodies reduces the incidence of thrombocytopenia observed with the small molecule glycoprotein IIb/IIIa antagonist roxifiban: implications for the etiology of thrombocytopenia. Blood 101, 58-63 (2003
    • (2003) Blood , vol.101 , pp. 58-63
    • Seiffert, D.1
  • 47
    • 0345874610 scopus 로고    scopus 로고
    • Steroid-hormone rapid actions, membrane receptors and a conformational ensemble model
    • Norman, A. W., Mizwicki, M. T., & Norman, D. P. Steroid-hormone rapid actions, membrane receptors and a conformational ensemble model. Nat. Rev. Drug Discov. 3, 27-41 (2004
    • (2004) Nat. Rev. Drug Discov , vol.3 , pp. 27-41
    • Norman, A.W.1    Mizwicki, M.T.2    Norman, D.P.3
  • 48
    • 0034109940 scopus 로고    scopus 로고
    • Antipsychotic agents differ in how fast they come off the dopamine D2 receptors Implications for atypical antipsychotic action
    • Kapur, S., & Seeman, P. Antipsychotic agents differ in how fast they come off the dopamine D2 receptors. Implications for atypical antipsychotic action. J. Psychiatry Neurosci. 25, 161-166 (2000
    • (2000) J. Psychiatry Neurosci , vol.25 , pp. 161-166
    • Kapur, S.1    Seeman, P.2
  • 49
    • 84862869593 scopus 로고    scopus 로고
    • Clozapine, atypical antipsychotics, and the benefits of fast-off D2 dopamine receptor antagonism
    • Vauquelin, G., Bostoen, S., Vanderheyden, P., & Seeman, P. Clozapine, atypical antipsychotics, and the benefits of fast-off D2 dopamine receptor antagonism. Naunyn Schmiedebergs Arch. Pharmacol. 385, 337-372 (2012
    • (2012) Naunyn Schmiedebergs Arch. Pharmacol , vol.385 , pp. 337-372
    • Vauquelin, G.1    Bostoen, S.2    Vanderheyden, P.3    Seeman, P.4
  • 50
    • 4544381198 scopus 로고    scopus 로고
    • Biochemical mechanisms of drug action: What does it take for success?
    • Swinney, D. C. Biochemical mechanisms of drug action: what does it take for success? Nat. Rev. Drug Discov. 3, 801-808 (2004
    • (2004) Nat. Rev. Drug Discov , vol.3 , pp. 801-808
    • Swinney, D.C.1
  • 51
    • 80054093004 scopus 로고    scopus 로고
    • Molecular mechanism of action (MMoA) in drug discovery
    • Swinney, D. C. Molecular mechanism of action (MMoA) in drug discovery. Annu. Reports Med. Chem. 46, 301-317 (2011
    • (2011) Annu. Reports Med. Chem , vol.46 , pp. 301-317
    • Swinney, D.C.1
  • 53
    • 84969440623 scopus 로고    scopus 로고
    • Incorporating receptor theory in mechanism-based pharmacokinetic-pharmacodynamic (PK PD) modeling
    • Ploeger, B. A., van der Graaf, P. H., & Danhof, M. Incorporating receptor theory in mechanism-based pharmacokinetic-pharmacodynamic (PK PD) modeling. Drug Metab. Pharmacokinet. 29, 84-93 (2009
    • (2009) Drug Metab. Pharmacokinet , vol.29 , pp. 84-93
    • Ploeger, B.A.1    Van Der Graaf, P.H.2    Danhof, M.3
  • 54
    • 78650057776 scopus 로고    scopus 로고
    • Hsp90 (heat shock protein 90) inhibitor occupancy is a direct determinant of client protein degradation and tumor growth arrest in vivo
    • Tillotson B., et al. Hsp90 (heat shock protein 90) inhibitor occupancy is a direct determinant of client protein degradation and tumor growth arrest in vivo. J. Biol. Chem. 285, 39835-39843 (2010
    • (2010) J. Biol. Chem , vol.285 , pp. 39835-39843
    • Tillotson, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.