메뉴 건너뛰기




Volumn 7, Issue 7, 2012, Pages 583-595

Radioligand dissociation measurements: Potential interference of rebinding and allosteric mechanisms and physiological relevance of the biological model systems

Author keywords

Allosteric modulation; Avidity; Bivalent ligand; Cell lines; Diffusion; Drug target; Radioligand; Rebinding; Receptors; Residence time

Indexed keywords

EPITOPE; RADIOLIGAND;

EID: 84862847461     PISSN: 17460441     EISSN: 1746045X     Source Type: Journal    
DOI: 10.1517/17460441.2012.687720     Document Type: Review
Times cited : (23)

References (100)
  • 2
    • 78651395471 scopus 로고    scopus 로고
    • Association of candesartan vs losartan with all-cause mortality in patients with heart failure
    • Eklind-Cervenka M, Benson L, Dahlstrom U, et al. Association of candesartan vs losartan with all-cause mortality in patients with heart failure. J Am Med Assoc 2011;305:175-82
    • (2011) J. Am. Med. Assoc. , vol.305 , pp. 175-182
    • Eklind-Cervenka, M.1    Benson, L.2    Dahlstrom, U.3
  • 3
    • 77949875945 scopus 로고    scopus 로고
    • Effects of losartan vs candesartan in reducing cardiovascular events in the primary treatment of hypertension
    • Kjeldsen SE, Stalhammar J, Hasvold P, et al. Effects of losartan vs candesartan in reducing cardiovascular events in the primary treatment of hypertension. J Hum Hypertens 2010;24:263-73
    • (2010) J. Hum. Hypertens. , vol.24 , pp. 263-273
    • Kjeldsen, S.E.1    Stalhammar, J.2    Hasvold, P.3
  • 4
    • 4544381198 scopus 로고    scopus 로고
    • Biochemical mechanisms of drug action: What does it take for success?
    • DOI 10.1038/nrd1500
    • Swinney DC. Biochemical mechanisms of drug action: what does it take for success? Nat Rev Drug Discov 2004;3:801-8 (Pubitemid 39242832)
    • (2004) Nature Reviews Drug Discovery , vol.3 , Issue.9 , pp. 801-808
    • Swinney, D.C.1
  • 5
    • 33646122469 scopus 로고    scopus 로고
    • Biochemical mechanisms of new molecular entities NMEs approved by United States FDA during 2001-2004: Mechanisms leading to optimal efficacy and safety
    • Swinney DC. Biochemical mechanisms of new molecular entities (NMEs) approved by United States FDA during 2001-2004: mechanisms leading to optimal efficacy and safety. Curr Top Med Chem 2006;6:461-78
    • Curr. Top. Med. Chem. , vol.2006 , Issue.6 , pp. 461-478
    • Swinney, D.C.1
  • 6
    • 33749623857 scopus 로고    scopus 로고
    • Can binding kinetics translate to a clinically differentiated drug? From theory to practice
    • DOI 10.2174/157018006778194754
    • Swinney DC. Can binding kinetics translate to a clinically differentiated drug? From theory to practice. Lett Drug Des Discov 2006;3:569-74 (Pubitemid 44544011)
    • (2006) Letters in Drug Design and Discovery , vol.3 , Issue.8 , pp. 569-574
    • Swinney, D.C.1
  • 7
    • 40449118501 scopus 로고    scopus 로고
    • Applications of binding kinetics to drug discovery: Translation of binding mechanisms to clinically differentiated therapeutic responses
    • Swinney DC. Applications of binding kinetics to drug discovery: translation of binding mechanisms to clinically differentiated therapeutic responses. Int J Pharm Med 2008;22:23-34
    • (2008) Int. J. Pharm. Med. , vol.22 , pp. 23-34
    • Swinney, D.C.1
  • 8
    • 58449131873 scopus 로고    scopus 로고
    • The role of binding kinetics in therapeutically useful drug action
    • Swinney DC. The role of binding kinetics in therapeutically useful drug action. Curr Opin Drug Discov Dev 2009;12:31-9
    • (2009) Curr. Opin Drug. Discov. Dev. , vol.12 , pp. 31-39
    • Swinney, D.C.1
  • 9
    • 33748325882 scopus 로고    scopus 로고
    • Drug-target residence time and its implications for lead optimization
    • DOI 10.1038/nrd2082, PII NRD2082
    • Copeland RA, Pompliano DL, Meek TD. Drug-target residence time and its implications for lead optimization. Nat Rev Drug Discov 2006;5:730-9 (Pubitemid 44323700)
    • (2006) Nature Reviews Drug Discovery , vol.5 , Issue.9 , pp. 730-739
    • Copeland, R.A.1    Pompliano, D.L.2    Meek, T.D.3
  • 10
    • 44049103958 scopus 로고    scopus 로고
    • Residence time of receptor - Ligand complexes and its effect on biological function
    • DOI 10.1021/bi8002023
    • Tummino PJ, Copeland RA. Residence time of receptor-ligand complexes and its effect on biological function. Biochemistry 2008;47:5481-92 (Pubitemid 351711169)
    • (2008) Biochemistry , vol.47 , Issue.20 , pp. 5481-5492
    • Tummino, P.J.1    Copeland, R.A.2
  • 11
    • 77950197835 scopus 로고    scopus 로고
    • The dynamics of drug-target interactions: Drug-target residence time and its impact on efficacy and safety
    • Copeland RA. The dynamics of drug-target interactions: drug-target residence time and its impact on efficacy and safety. Expert Opin Drug Discov 2010;5:305-10
    • (2010) Expert. Opin Drug. Discov. , vol.5 , pp. 305-310
    • Copeland, R.A.1
  • 13
    • 77958535230 scopus 로고    scopus 로고
    • Binding kinetics and mechanism of action: Toward the discovery and development of better and best in class drugs
    • Zhang R, Monsma F. Binding kinetics and mechanism of action: toward the discovery and development of better and best in class drugs. Expert Opin Drug Discov 2010;5:1023-9
    • (2010) Expert Opin Drug. Discov. , vol.5 , pp. 1023-1029
    • Zhang, R.1    Monsma, F.2
  • 14
    • 33745511768 scopus 로고    scopus 로고
    • Slow antagonist dissociation and long-lasting in vivo receptor protection
    • Vauquelin G, Van Liefde I. Slow antagonist dissociation and long-lasting in vivo receptor protection. Trends Pharmacol Sci 2006;27:356-9
    • (2006) Trends. Pharmacol. Sci. , vol.27 , pp. 356-359
    • Vauquelin, G.1    Van Liefde, I.2
  • 15
    • 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 2010;5:927-41
    • (2010) Expert. Opin Drug. Discov. , vol.5 , pp. 927-941
    • Vauquelin, G.1
  • 16
    • 77956309074 scopus 로고    scopus 로고
    • Long-lasting target binding and rebinding as mechanisms to prolong in vivo drug action
    • Vauquelin G, Charlton S. Long-lasting target binding and rebinding as mechanisms to prolong in vivo drug action. Br J Pharmacol 2010;161:488-508
    • (2010) Br. J. Pharmacol. , vol.161 , pp. 488-4508
    • Vauquelin, G.1    Charlton, S.2
  • 17
    • 84862869593 scopus 로고    scopus 로고
    • Clozapine atypical antipsychotics and the benefits of fast-off D2 dopamine receptor antagonism
    • 2012 published online Feb 10.1007/s00210-012-0734-2
    • 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 2012, published online Feb 14 2012, doi 10.1007/s00210-012-0734-2
    • (2012) Naunyn Schmiedebergs Arch. Pharmacol. , vol.14
    • Vauquelin, G.1    Bostoen, S.2    Vanderheyden, P.3    Seeman, P.4
  • 18
    • 84862856969 scopus 로고    scopus 로고
    • Determination of drug-receptor residence times by radioligand binding and functional assays: Experimental strategies and physiological relevance
    • 10.1039/C2MD20015E
    • Vauquelin G. Determination of drug-receptor residence times by radioligand binding and functional assays: experimental strategies and physiological relevance. Med Chem Commun 2012;doi 10.1039/C2MD20015E
    • (2012) Med. Chem. Commun.
    • Vauquelin, G.1
  • 19
    • 33749358578 scopus 로고    scopus 로고
    • Quantifying the association and dissociation rates of unlabelled antagonists at the muscarinic M3 receptor
    • Dowling MR, Charlton SJ. Quantifying the association and dissociation rates of unlabelled antagonists at the muscarinic M3 receptor. Br J Pharmacol 2006;148:1134-42
    • (2006) Br. J. Pharmacol. , vol.148 , pp. 1134-1142
    • Dowling, M.R.1    Charlton, S.J.2
  • 20
    • 33847667536 scopus 로고    scopus 로고
    • Scintillation proximity assay as a high-throughput method to identify slowly dissociating nonpeptide ligand binding to the GnRH receptor
    • DOI 10.1177/1087057106297362
    • Heise CE, Sullivan S, Crowe PD. Scintillation proximity assay as high-throughput method to identify slowly dissociating nonpeptide ligand binding to the GnRH receptor. J Biomol Screen 2007;12:235-9 (Pubitemid 46364424)
    • (2007) Journal of Biomolecular Screening , vol.12 , Issue.2 , pp. 235-239
    • Heise, C.E.1    Sullivan, S.K.2    Crowe, P.D.3
  • 21
    • 68949170699 scopus 로고    scopus 로고
    • Analytical method for simultaneously measuring ex vivo drug receptor occupancy and dissociation rate: Application to R-dimethindene occupancy of central histamine H1 receptors
    • Malany S, Hernandez LM, Smith WF, et al. Analytical method for simultaneously measuring ex vivo drug receptor occupancy and dissociation rate: application to (R)-dimethindene occupancy of central histamine H1 receptors. J Recept Signal Transduct Res 2009;29:84-93
    • (2009) J. Recept Signal. Transduct. Res. , vol.29 , pp. 84-93
    • Malany, S.1    Hernandez, L.M.2    Smith, W.F.3
  • 22
    • 77956840539 scopus 로고    scopus 로고
    • Estimation of the dissociation rate of unlabelled ligand-receptor complexes by a two-step competition binding approach
    • Packeu A, Wennerberg M, Ballendran A, Vauquelin G. Estimation of the dissociation rate of unlabelled ligand-receptor complexes by competition binding approach. Br J Pharmacol 2010;161:1311-28
    • (2010) Br. J. Pharmacol. , vol.161 , pp. 1311-1328
    • Packeu, A.1    Wennerberg, M.2    Ballendran, A.3    Vauquelin, G.4
  • 23
    • 0015809277 scopus 로고
    • Insulin interactions with its receptors: Experimental evidence for negative cooperativity
    • De Meyts P, Roth J, Neville DM Jr, et al. Insulin interactions with its receptors: experimental evidence for negative cooperativity. Biochem Biophys Res Commun 1973;55:154-61
    • (1973) Biochem. Biophys. Res. Commun. , vol.55 , pp. 154-161
    • De Meyts, P.1    Roth, J.2    Neville, Jr.D.M.3
  • 24
    • 10844223660 scopus 로고    scopus 로고
    • Insulin and its receptor: Structure, function and evolution
    • DOI 10.1002/bies.20151
    • De Meyts P. Insulin and its receptor: structure, function and evolution. Bioessays 2004;26:1351-62 (Pubitemid 39664629)
    • (2004) BioEssays , vol.26 , Issue.12 , pp. 1351-1362
    • De Meyts, P.1
  • 25
    • 0036258990 scopus 로고    scopus 로고
    • G protein-coupled receptor allosterism and complexing
    • DOI 10.1124/pr.54.2.323
    • Christopoulos A, Kenakin T. G protein-coupled receptor allosterism and complexing. Pharmacol Rev 2002;54:323-74 (Pubitemid 34575719)
    • (2002) Pharmacological Reviews , vol.54 , Issue.2 , pp. 323-374
    • Christopoulos, A.1    Kenakin, T.2
  • 26
    • 0036490942 scopus 로고    scopus 로고
    • Allosteric binding sites on cell-surface receptors: Novel targets for drug discovery
    • Christopoulos A. Allosteric binding sites on cell-surface receptors: novel targets for drug discovery. Nat Rev Drug Discov 2002;1:198-210 (Pubitemid 37361423)
    • (2002) Nature Reviews Drug Discovery , vol.1 , Issue.3 , pp. 198-210
    • Christopoulos, A.1
  • 28
    • 0001433502 scopus 로고    scopus 로고
    • Composite action of allosteric modulators on ligand binding
    • Kostenis E, Mohr K. Composite action of allosteric modulators on ligand binding. Trends Pharmacol Sci 1996;17:443-4
    • (1996) Trends. Pharmacol. Sci. , vol.17 , pp. 443-444
    • Kostenis, E.1    Mohr, K.2
  • 29
    • 0031009786 scopus 로고    scopus 로고
    • Allosteric binding sites on muscarinic receptors
    • Ellis J. Allosteric binding sites on muscarinic receptors. Drug Dev Res 1997;40:193-204
    • (1997) Drug. Dev. Res. , vol.40 , pp. 193-1204
    • Ellis, J.1
  • 30
    • 0033664285 scopus 로고    scopus 로고
    • Interactions of alcuronium TMB-8 and other allosteric ligands with muscarinic acetylcholine receptors: Studies with chimeric receptors
    • Ellis J, Seidenberg M. Interactions of alcuronium, TMB-8, and other allosteric ligands with muscarinic acetylcholine receptors: studies with chimeric receptors. Mol Pharmacol 2000;58:1451-60
    • (2000) Mol. Pharmacol. , vol.58 , pp. 1451-1460
    • Ellis, J.1    Seidenberg, M.2
  • 31
    • 0033853436 scopus 로고    scopus 로고
    • Dual interaction of agmatine with the rat α(2D)-adrenoceptor: Competitive antagonism and allosteric activation
    • Molderings GJ, Menzel S, Kathmann M, et al. Dual interaction of agmatine with the rat alpha2D-adrenoceptor: competitive antagonism and allosteric activation. Br J Pharmacol 2000;130:1706-12 (Pubitemid 30611952)
    • (2000) British Journal of Pharmacology , vol.130 , Issue.7 , pp. 1706-1712
    • Molderings, G.J.1    Menzel, S.2    Kathmann, M.3    Schlicker, E.4    Gothert, M.5
  • 32
    • 0017190266 scopus 로고
    • Negative cooperativity among beta-adrenergic receptors in frog erythrocyte membrane
    • Limbird LE, Lefkowitz RJ. Negative cooperativity among beta-adrenergic receptors in frog erythrocyte membrane. J Biol Chem 1976;251:5007-14
    • (1976) J. Biol. Chem. , vol.251 , pp. 5007-5014
    • Limbird, L.E.1    Lefkowitz, R.J.2
  • 33
    • 0017224874 scopus 로고
    • Site-site interactions among insulin receptors characterization of the negative cooperativity
    • De Meyts P, Bianco R, Roth J. Site-site interactions among insulin receptors. Characterization of the negative cooperativity. J Biol Chem 1977;251:1877-88
    • (1977) J. Biol. Chem. , vol.251 , pp. 1877-1888
    • De Meyts, P.1    Bianco, R.2    Roth, J.3
  • 34
    • 0018584222 scopus 로고
    • Nerve growth factor receptors. Characterization of two distinct classes of binding sites on chick embryo sensory ganglia cells
    • Sutter A, Riopelle RG, Harris-Warrick RM, Shooter EM. Nerve growth factor receptors. Characterization of two distinct classes of binding sites on chick embryo sensory ganglia cells. J Biol Chem 1979;254:5972-82 (Pubitemid 9242473)
    • (1979) Journal of Biological Chemistry , vol.254 , Issue.13 , pp. 5972-5982
    • Sutter, A.1    Riopelle, R.J.2    Harris-Warrick, R.M.3    Shooter, E.M.4
  • 35
    • 33645802812 scopus 로고    scopus 로고
    • Allosteric modulation of binding properties between units of chemokine receptor homo-and hetero-oligomers
    • Springael JY, Le Minh PN, Urizar E, et al. Allosteric modulation of binding properties between units of chemokine receptor homo- and hetero-oligomers. Mol Pharmacol 2006;69:1652-61
    • (2006) Mol. Pharmacol. , vol.69 , pp. 1652-1661
    • Springael, J.Y.1    Le Minh, P.N.2    Urizar, E.3
  • 36
    • 41149127699 scopus 로고    scopus 로고
    • Dimerization and oligomerization of G-protein-coupled receptors: Debated structures with established and emerging functions
    • DOI 10.1677/JOE-07-0573
    • Szidonya L, Cserzo M, Hunyady L. Dimerization and oligomerization of G-protein-coupled receptors: debated structures with established and emerging functions. J Endocrinol 2008;196:435-53 (Pubitemid 351425500)
    • (2008) Journal of Endocrinology , vol.196 , Issue.3 , pp. 435-453
    • Szidonya, L.1    Cserzo, M.2    Hunyady, L.3
  • 37
    • 0017664223 scopus 로고
    • Physics of chemoreception
    • Berg HC, Purcell EM. Physics of chemoreception. Biophys J 1977;20:193-219
    • (1977) Biophys. J. , vol.20 , pp. 193-1219
    • Berg, H.C.1    Purcell, E.M.2
  • 38
    • 0020199402 scopus 로고
    • Role of diffusion in ligand binding to macromolecules and cell-bound receptors
    • Shoup D, Szabo A. Role of diffusion in ligand binding to macromolecules and cell-bound receptors. Biophys J 1982;40:33-9
    • (1982) Biophys. J. , vol.40 , pp. 33-39
    • Shoup, D.1    Szabo, A.2
  • 39
    • 0024760188 scopus 로고
    • Competition between solution and cell surface receptors for ligand dissociation of hapten bound to surface antibody in the presence of solution antibody
    • Goldstein B, Posner RG, Torney DC, et al. Competition between solution and cell surface receptors for ligand. Dissociation of hapten bound to surface antibody in the presence of solution antibody. Biophys J 1989;56:955-66
    • (1989) Biophys. J. , vol.56 , pp. 955-966
    • Goldstein, B.1    Posner, R.G.2    Torney, D.C.3
  • 40
    • 0028960497 scopus 로고
    • Approximating the effects of diffusion on reversible reactions at the cell surface: Ligand-receptor kinetics
    • Goldstein B, Dembo M. Approximating the effects of diffusion on reversible reactions at the cell surface: ligand-receptor kinetics. Biophys J 1995;68:1222-30
    • (1995) Biophys. J. , vol.68 , pp. 1222-1230
    • Goldstein, B.1    Dembo, M.2
  • 43
    • 33646873478 scopus 로고    scopus 로고
    • Diffusion delays and unstirred layer effects at monolayer cultures of Chinese hamster ovary cells: Radioligand binding, confocal microscopy, and mathematical simulations
    • Spivak CE, Oz M, Beglan CL, Shrager RI. Diffusion delays and unstirred layer effects at monolayer cultures of Chinese hamster ovary cells: Radioligand binding, confocal microscopy, and mathematical simulations. Cell Biochem Biophys 2006;45:43-58 (Pubitemid 43780381)
    • (2006) Cell Biochemistry and Biophysics , vol.45 , Issue.1 , pp. 43-58
    • Spivak, C.E.1    Oz, M.2    Beglan, C.L.3    Shrager, R.I.4
  • 44
    • 0041494100 scopus 로고    scopus 로고
    • Lipid rafts: Bringing order to chaos
    • DOI 10.1194/jlr.R200021-JLR200
    • Pike LJ. Lipid rafts: bringing order to chaos. J Lipid Res 2003;44:655-67 (Pubitemid 37279667)
    • (2003) Journal of Lipid Research , vol.44 , Issue.4 , pp. 655-667
    • Pike, L.J.1
  • 45
    • 22244467106 scopus 로고    scopus 로고
    • Serial rebinding of ligands to clustered receptors as exemplified by bacterial chemotaxis
    • DOI 10.1088/1478-3975/2/2/004
    • Andrews SS. Serial rebinding of ligands to clustered receptors as exemplified by bacterial chemotaxis. Phys Biol 2005;2:111-22 (Pubitemid 40991713)
    • (2005) Physical Biology , vol.2 , Issue.2 , pp. 111-122
    • Andrews, S.S.1
  • 46
    • 28444449872 scopus 로고    scopus 로고
    • Effects of receptor clustering on ligand dissociation kinetics: Theory and simulations
    • Gopalakrishnan M, Forsten-Williams K, Nugent MA, Tauber UC. Effects of receptor clustering on ligand dissociation kinetics: theory and simulations. Biophys J 2005;89:3686-700
    • (2005) Biophys. J. , vol.89 , pp. 3686-36700
    • Gopalakrishnan, M.1    Forsten-Williams, K.2    Nugent, M.A.3    Tauber, U.C.4
  • 47
    • 16644394144 scopus 로고    scopus 로고
    • Effects of the geometry of the immunological synapse on the delivery of effector molecules
    • DOI 10.1529/biophysj.104.045674
    • Coombs D, Goldstein B. Effects of geometry of the immunological synapse on the delivery of effector molecules. Biophys J 2004;87:2215-20 (Pubitemid 41071324)
    • (2004) Biophysical Journal , vol.87 , Issue.4 , pp. 2215-2220
    • Coombs, D.1    Goldstein, B.2
  • 48
    • 0018868014 scopus 로고
    • Opiate antagonist receptor binding in vivo: Evidence for a new receptor binding model
    • DOI 10.1016/0006-8993(80)90229-2
    • Perry DC, Mullis KB, Oie S, Sadee W. Opiate antagonist receptor binding in vivo: evidence for a new receptor binding model. Brain Res 1980;199:49-61 (Pubitemid 10052239)
    • (1980) Brain Research , vol.199 , Issue.1 , pp. 49-61
    • Perry, D.C.1    Mullis, K.B.2    Oie, S.3    Sadee, W.4
  • 50
    • 69249205472 scopus 로고    scopus 로고
    • Molecular mechanism of the persistent bronchodilatory effect of the partial beta2-adrenoceptor agonist salmeterol
    • Szczuka A, Packeu A, Wennerberg M, Vauquelin G. Molecular mechanism of the persistent bronchodilatory effect of the partial beta2-adrenoceptor agonist salmeterol. Br J Pharmacol 2009;158:183-94
    • (2009) Br. J. Pharmacol. , vol.158 , pp. 183-194
    • Szczuka, A.1    Packeu, A.2    Wennerberg, M.3    Vauquelin, G.4
  • 51
    • 0021186011 scopus 로고
    • Kinetics of binding to opiate receptors in vivo predicted from in vitro parameters
    • DOI 10.1016/0006-8993(84)91113-2
    • Frost JJ, Wagner HR Jr. Kinetics of binding to opiate receptors in vivo predicted from in vitro parameters. Brain Res 1984;305:1-11 (Pubitemid 14117838)
    • (1984) Brain Research , vol.305 , Issue.1 , pp. 1-11
    • Frost, J.J.1    Wagner Jr., H.N.2
  • 52
    • 0030039913 scopus 로고    scopus 로고
    • Competition BIAcore for measuring true affinities: Large differences from values determined from binding kinetics
    • DOI 10.1006/abio.1996.0067
    • Nieba L, Krebber A, Pluckthun A. Competition BIAcore for measuring true affinities: large differences from values determined from binding kinetics. Anal Biochem 1996;234:155-65 (Pubitemid 26063796)
    • (1996) Analytical Biochemistry , vol.234 , Issue.2 , pp. 155-165
    • Nieba, L.1    Krebber, A.2    Pluckthun, A.3
  • 53
    • 0030571002 scopus 로고    scopus 로고
    • Analysis of mass transport-limited binding kinetics in evanescent wave biosensors
    • DOI 10.1006/abio.1996.0356
    • Schuck P, Minton AP. Analysis of mass transport-limited binding kinetics in evanescent wave biosensors. Anal Biochem 1996;240:262-72 (Pubitemid 26304270)
    • (1996) Analytical Biochemistry , vol.240 , Issue.2 , pp. 262-272
    • Schuck, P.1    Minton, A.P.2
  • 54
    • 0031848098 scopus 로고    scopus 로고
    • Extending the range of rate constants available from BIACORE: Interpreting mass transport-influenced binding data
    • Myszka DG, He X, Dembo M, et al. Extending the range of rate constants available from BIACORE: interpreting mass transport-influenced binding data. Biophys J 1998;75:583-94 (Pubitemid 28357501)
    • (1998) Biophysical Journal , vol.75 , Issue.2 , pp. 583-594
    • Myszka, D.G.1    He, X.2    Dembo, M.3    Morton, T.A.4    Goldstein, B.5
  • 55
    • 0023811158 scopus 로고
    • The collisional limit: An important consideration for membrane-associated enzymes and receptors
    • Abbott AJ, Nelsestuen GL. The collisional limit: an important consideration for membrane-associated enzymes and receptors. FASEB J 1988;2:2858-66
    • (1988) FASEB J. , vol.2 , pp. 2858-2866
    • Abbott, A.J.1    Nelsestuen, G.L.2
  • 57
    • 27144432842 scopus 로고    scopus 로고
    • Engineered antibody fragments and the rise of single domains
    • DOI 10.1038/nbt1142, PII N1142
    • Holliger P, Hudson PJ. Engineered antibody fragments and the rise of single domains. Nat Biotechnol 2005;23:1126-36 (Pubitemid 41486394)
    • (2005) Nature Biotechnology , vol.23 , Issue.9 , pp. 1126-1136
    • Holliger, P.1    Hudson, P.J.2
  • 58
    • 79951997039 scopus 로고    scopus 로고
    • THRX-198321 is a bifunctional muscarinic receptor antagonist and beta2-adrenoceptor agonist MABA that binds in a bimodal and multivalent manner
    • Steinfeld T, Hughes AD, Klein U, et al. THRX-198321 is a bifunctional muscarinic receptor antagonist and beta2-adrenoceptor agonist (MABA) that binds in a bimodal and multivalent manner. Mol Pharmacol 2011;79:389-99
    • (2011) Mol. Pharmacol. , vol.79 , pp. 389-399
    • Steinfeld, T.1    Hughes, A.D.2    Klein, U.3
  • 59
    • 0026705890 scopus 로고
    • Effect of bivalent interaction upon apparent antibody affinity: Experimental confirmation of a theory using fluorescence photobleaching and implications for antibody binding assays
    • Kaufman EN, Jain RK. Effect of bivalent interaction upon apparent antibody affinity: experimental confirmation of theory using fluorescence photobleaching and implications for antibody binding assays. Cancer Res 1992;52:4157-67
    • (1992) Cancer Res. , vol.52 , pp. 4157-4167
    • Kaufman, E.N.1    Jain, R.K.2
  • 60
    • 0030738617 scopus 로고    scopus 로고
    • New protein engineering approaches to multivalent and bispecific antibody fragments
    • DOI 10.1016/S1380-2933(97)00067-5, PII S1380293397000675
    • Pluckthun A, Pack P. New protein engineering approaches to multivalent and bispecific antibody fragments. Immunotechnology 1997;3:83-105 (Pubitemid 27356788)
    • (1997) Immunotechnology , vol.3 , Issue.2 , pp. 83-105
    • Pluckthun, A.1    Pack, P.2
  • 61
    • 64549133821 scopus 로고    scopus 로고
    • Structural basis of allosteric ligand-receptor interactions in the insulin-relaxin peptide family: Implications for other receptor tyrosine kinases and G-protein-coupled receptors
    • De Meyts P, Gauguin L, Svendsen AM, et al. Structural basis of allosteric ligand-receptor interactions in the insulin-relaxin peptide family: implications for other receptor tyrosine kinases and G-protein-coupled receptors. Ann NY Acad Sci 2009;1160:45-53
    • (2009) Ann. NY. Acad. Sci. , vol.1160 , pp. 45-53
    • De Meyts, P.1    Gauguin, L.2    Svendsen, A.M.3
  • 62
    • 48149095486 scopus 로고    scopus 로고
    • The insulin receptor: A prototype for dimeric allosteric membrane receptors
    • De Meyts P. The insulin receptor: a prototype for dimeric, allosteric membrane receptors? Trends Biochem Sci 2008;33:376-84
    • (2008) Trends. Biochem. Sci. , vol.33 , pp. 376-384
    • De Meyts, P.1
  • 63
    • 0030944020 scopus 로고    scopus 로고
    • Kinetic studies of co-operativity at atrial muscarinic M2 receptors with an infinite dilution procedure
    • Christopoulos A, Lunzafame A, Ziegler A, Mitchelson F. Kinetic studies of co-operativity at atrial muscarinic M2 receptors with an ''infinite dilution'' procedure. Biochem Pharmacol 1997;53:795-800
    • (1997) Biochem. Pharmacol. , vol.53 , pp. 795-7800
    • Christopoulos, A.1    Lunzafame, A.2    Ziegler, A.3    Mitchelson, F.4
  • 64
    • 43049137653 scopus 로고    scopus 로고
    • Antagonist- dopamine D2L- receptor interactions in intact cells
    • Packeu A, De Backer J-P, Van Liefde I, et al. Antagonist- dopamine D2L- receptor interactions in intact cells. Biochem Pharmacol 2008;75:2192-203
    • (2008) Biochem. Pharmacol. , vol.75 , pp. 2192-2103
    • Packeu, A.1    De Backer, J.-P.2    Van Liefde, I.3
  • 65
    • 79952404677 scopus 로고    scopus 로고
    • Binding properties of antagonists to cannabinoid receptors in intact cells
    • Wennerberg M, Cheng L, Hjorth S, et al. Binding properties of antagonists to cannabinoid receptors in intact cells. Fundam Clin Pharmacol 2010;25:200-10
    • (2010) Fundam. Clin. Pharmacol. , vol.25 , pp. 200-210
    • Wennerberg, M.1    Cheng, L.2    Hjorth, S.3
  • 66
    • 0028146822 scopus 로고
    • The structural basis of insulin and insulin-like growth factor-I receptor binding and negative co-operativity, and its relevance to mitogenic versus metabolic signalling
    • De Meyts P. The structural basis of insulin and insulin-like growth factor- (IGF-I) receptor binding and negative cooperativity, and its relevance to mitogenic versus metabolic signaling. Diabetologia 1994;37:S135-48 (Pubitemid 24288803)
    • (1994) Diabetologia , vol.37 , Issue.SUPPL. 2
    • De Meyts, P.1
  • 67
    • 38349190632 scopus 로고    scopus 로고
    • Heterogeneity in EGF-binding affinities arises from negative cooper- ativity in an aggregating system
    • USA
    • Macdonald JL, Pike LJ. Heterogeneity in EGF-binding affinities arises from negative cooper- ativity in an aggregating system. Proc Natl Acad Sci USA 2008;105:112-17
    • (2008) Proc. Natl. Acad. Sci. , vol.105 , pp. 112-117
    • Macdonald, J.L.1    Pike, L.J.2
  • 68
    • 0029550774 scopus 로고
    • Mechanism of insulin and IGF-I receptor activation and signal transduction specificity receptor dimer crosslinking bell-shaped curves and sustained versus transient signaling
    • De Meyts P, Urso B, Christoffersen CT, Shymko RM. Mechanism of insulin and IGF-I receptor activation and signal transduction specificity. Receptor dimer crosslinking, bell-shaped curves, and sustained versus transient signaling. Ann NY Acad Sci 1995;766:388-401
    • (1995) Ann. NY. Acad. Sci. , vol.766 , pp. 388-3401
    • De Meyts, P.1    Urso, B.2    Christoffersen, C.T.3    Shymko, R.M.4
  • 69
    • 60749092852 scopus 로고    scopus 로고
    • Harmonic oscillator model of the insulin and IGF1 receptors allosteric binding and activation
    • Kiselyov VV, Versteyhe S, Gauguin L, De Meyts P. Harmonic oscillator model of the insulin and IGF1 receptors' allosteric binding and activation. Mol Syst Biol 2009;5:243
    • (2009) Mol. Syst. Biol. , vol.5 , pp. 243
    • Kiselyov, V.V.1    Versteyhe, S.2    Gauguin, L.3    De Meyts, P.4
  • 70
    • 82455186745 scopus 로고    scopus 로고
    • Insight into the molecular basis for the kinetic differences between the two insulin receptor isoforms
    • Knudsen L, De Meyts P, Kiselyov VV. Insight into the molecular basis for the kinetic differences between the two insulin receptor isoforms. Biochem J 2011;440:397-403
    • (2011) Biochem. J. , vol.440 , pp. 397-3403
    • Knudsen, L.1    De Meyts, P.2    Kiselyov, V.V.3
  • 72
    • 80052462704 scopus 로고    scopus 로고
    • Conformational adaptation in drug-target interactions and residence time
    • Copeland RA. Conformational adaptation in drug-target interactions and residence time. Future Med Chem 2011;3:1491-501
    • (2011) Future Med. Chem. , vol.3 , pp. 1491-1501
    • Copeland, R.A.1
  • 73
    • 14644387575 scopus 로고    scopus 로고
    • Emerging role of homo- and heterodimerization in G-protein-coupled receptor biosynthesis and maturation
    • DOI 10.1016/j.tips.2005.01.004
    • Bulenger S, Marullo S, Bouvier M. Emerging role of homo- and heterodimerization in G- protein-coupled receptor biosynthesis and maturation. Trends Pharmacol Sci 2005;26:131-7 (Pubitemid 40313592)
    • (2005) Trends in Pharmacological Sciences , vol.26 , Issue.3 , pp. 131-137
    • Bulenger, S.1    Marullo, S.2    Bouvier, M.3
  • 77
    • 40849119953 scopus 로고    scopus 로고
    • Cooperative binding of insulin-like peptide 3 to a dimeric relaxin family peptide receptor 2
    • Svendsen AM, Vrecl M, Ellis TM, et al. Cooperative binding of insulin-like peptide 3 to a dimeric relaxin family peptide receptor 2. Endocrinology 2008;149:113-20
    • (2008) Endocrinology , vol.149 , pp. 113-120
    • Svendsen, A.M.1    Vrecl, M.2    Ellis, T.M.3
  • 78
    • 0043235844 scopus 로고    scopus 로고
    • Ligand-selective receptor conformations revisited: The promise and the problem
    • DOI 10.1016/S0165-6147(03)00167-6
    • Kenakin T. Ligand-selective receptor conformations revisited: the promise and the problem. Trends Pharmacol Sci 2003;24:346-54 (Pubitemid 37315526)
    • (2003) Trends in Pharmacological Sciences , vol.24 , Issue.7 , pp. 346-354
    • Kenakin, T.1
  • 80
    • 65449161390 scopus 로고    scopus 로고
    • Ligand binding and micro-switches in 7TM receptor structures
    • Nygaard R, Frimurer TM, Holst B, et al. Ligand binding and micro-switches in 7TM receptor structures. Trends Pharmacol Sci 2009;30:249-59
    • (2009) Trends. Pharmacol. Sci. , vol.30 , pp. 249-259
    • Nygaard, R.1    Frimurer, T.M.2    Holst, B.3
  • 81
    • 58149193205 scopus 로고    scopus 로고
    • Allosteric modulators of GPCRs: A novel approach for the treatment of CNS disorders
    • Conn PJ, Christopoulos A, Lindsley CW. Allosteric modulators of GPCRs: a novel approach for the treatment of CNS disorders. Nat Rev Drug Discov 2009;8:41-54
    • (2009) Nat. Rev. Drug. Discov. , vol.8 , pp. 41-54
    • Conn, P.J.1    Christopoulos, A.2    Lindsley, C.W.3
  • 82
    • 33751195311 scopus 로고    scopus 로고
    • Probing the existence of G protein-coupled receptor dimers by positive and negative ligand-dependent cooperative binding
    • Albizu L, Balestre MN, Breton C, et al. Probing the existence of G protein-coupled receptor dimers by positive and negative ligand-dependent cooperative binding. Mol Pharmacol 2006;70:1783-91
    • (2006) Mol. Pharmacol. , vol.70 , pp. 1783-1791
    • Albizu, L.1    Balestre, M.N.2    Breton, C.3
  • 84
    • 33744544180 scopus 로고
    • Fractal reaction kinetics
    • Kopelman R. Fractal reaction kinetics. Science 1988;241:1620-6
    • (1988) Science , vol.241 , pp. 1620-1626
    • Kopelman, R.1
  • 85
    • 0031194188 scopus 로고    scopus 로고
    • Theoretical analysis of protein concentration determination using biosensor technology under conditions of partial mass transport limitation
    • DOI 10.1006/abio.1997.2182
    • Christensen LLH. Theoretical analysis of protein concentration determination using biosensor technology under conditions of partial mass transport limitation. Anal Biochem 1997;249:153-64 (Pubitemid 27291095)
    • (1997) Analytical Biochemistry , vol.249 , Issue.2 , pp. 153-164
    • Christensen, L.L.H.1
  • 86
    • 0024433856 scopus 로고
    • 2, and Fab in tumors
    • Fujimori K, Covell DC, Fletcher JE, Weinstein JN. Modeling analysis of the global and microscopic distribution of immunoglobulin G, F(ab)2, and Fab in tumors. Cancer Res 1989;49:5656-63 (Pubitemid 19256448)
    • (1989) Cancer Research , vol.49 , Issue.20 , pp. 5656-5663
    • Fujimori, K.1    Covell, D.G.2    Fletcher, J.E.3    Weinstein, J.N.4
  • 87
    • 68249113457 scopus 로고    scopus 로고
    • Cellular assays as portals to seven-transmembrane receptor-based drug discovery
    • Kenakin TP. Cellular assays as portals to seven-transmembrane receptor-based drug discovery. Nat Rev Drug Discov 2009;8:617-26
    • (2009) Nat. Rev. Drug. Discov. , vol.8 , pp. 617-626
    • Kenakin, T.P.1
  • 88
    • 0032568305 scopus 로고    scopus 로고
    • Endothelin ET(B) receptors show different binding profiles in intact cells and cell membrane preparations
    • DOI 10.1016/S0014-2999(98)00016-8, PII S0014299998000168
    • Hara M, Tozawa F, Itazaki K, et al. Endothelin ET(B) receptors show different binding profiles in intact cells and cell membrane preparations. Eur J Pharmacol 1998;345:339-42 (Pubitemid 28179577)
    • (1998) European Journal of Pharmacology , vol.345 , Issue.3 , pp. 339-342
    • Hara, M.1    Tozawa, F.2    Itazaki, K.3    Mihara, S.-I.4    Fujimoto, M.5
  • 90
    • 69249210978 scopus 로고    scopus 로고
    • Ligands their receptors and plasma membranes
    • Vauquelin G, Packeu A. Ligands, their receptors and plasma membranes. Mol Cell Endocrinol 2009;311:1-10
    • (2009) Mol. Cell. Endocrinol. , vol.311 , pp. 1-10
    • Vauquelin, G.1    Packeu, A.2
  • 91
    • 84862856969 scopus 로고    scopus 로고
    • Determination of drug-receptor residence times by radioligand binding and functional assays: Experimental strategies and physiological relevance
    • 2012, published online March 10.1039/C2MD20015E
    • Vauquelin G. Determination of drug-receptor residence times by radioligand binding and functional assays: experimental strategies and physiological relevance. Med Chem Commun 2012, published online March 27 2012, doi:10.1039/C2MD20015E
    • (2012) Med. Chem. Commun. , vol.27
    • Vauquelin, G.1
  • 92
    • 2942534217 scopus 로고    scopus 로고
    • Contribution of dead-space microdomains to tortuosity of brain extracellular space
    • DOI 10.1016/j.neuint.2003.11.011, PII S0197018603002511, Role of Non-synaptic Communication in Information Processing
    • Hrabctova S, Nicholson C. Contribution of dead-space microdomains to tortuosity of brain extracellular space. Neurochem Int 2004;45:467-77 (Pubitemid 38739473)
    • (2004) Neurochemistry International , vol.45 , Issue.4 , pp. 467-477
    • Hrabetova, S.1    Nicholson, C.2
  • 94
    • 0003064682 scopus 로고
    • Reduction of dimensionality in biological diffusion processes
    • Rich A Davidson R editors W.H. Freeman & Co., San Francisco
    • Adam G, Delbruck M. Reduction of dimensionality in biological diffusion processes. In: Rich A, Davidson R, editors, Structural Chemistry and Molecular Biology. W.H. Freeman & Co., San Francisco; 1968. p. 198-215
    • (1968) Structural Chemistry and Molecular Biology , pp. 198-215
    • Adam, G.1    Delbruck, M.2
  • 95
    • 84862877299 scopus 로고    scopus 로고
    • Pharmacology of JNJ-37822681 a specific and fast-dissociating D2 antagonist for the treatment of schizophrenia poster presented at the 23nd congress of european college of neuropsychopharmacology amsterdam 9 2010
    • Langlois X, Megens A, Lavreysen H, et al. Pharmacology of JNJ-37822681, specific and fast-dissociating D2 antagonist for the treatment of schizophrenia. Poster presented at the 23nd Congress of European College of Neuropsychopharmacology; Amsterdam 9/2010. Eur Neuropsychopharmacol 2010;20:S502
    • (2010) Eur. Neuropsychopharmacol. , vol.20
    • Langlois, X.1    Megens, A.2    Lavreysen, H.3
  • 96
    • 0025941654 scopus 로고
    • Positron emission tomography with 18F methylspipcronc demonstrates D2 dopamine receptor binding differences of clozapine and haloperidol
    • Karbe H, Wienhard K, Haniacher K, et al. Positron emission tomography with [18F]methylspipcronc demonstrates D2 dopamine receptor binding differences of clozapine and haloperidol. J Neural Transm 1991;86:163-73
    • (1991) J. Neural. Transm. , vol.86 , pp. 163-173
    • Karbe, H.1    Wienhard, K.2    Haniacher, K.3
  • 97
    • 0026612906 scopus 로고
    • Time course of D2-dopamine receptor occupancy examined by PET after single oral doses of haloperidol
    • Nordstrom A-L, Farde L, Halldin C. Time course of D2-dopamine receptor occupancy examined by PET after single oral doses of haloperidol. Psychopharmacology 1992;106:433-8
    • (1992) Psychopharmacology , vol.106 , pp. 433-8
    • Nordstrom, A.-L.1    Farde, L.2    Halldin, C.3
  • 98
    • 0021699902 scopus 로고
    • 2 receptor, application of an original filter method
    • Leysen JE, Gommeren WJ. The dissociation of unlabelled dopamine antagonists and agonists from the dopamine D2-receptor. Implication of an original filter method. J Recept Res 1984;4:817-45 (Pubitemid 15155105)
    • (1984) Journal of Receptor Research , vol.4 , Issue.7 , pp. 817-845
    • Leysen, J.E.1    Gommeren, W.2
  • 99
    • 0035254652 scopus 로고    scopus 로고
    • A two-state receptor model for the interaction between angiotensin II type 1 receptors and non-peptide antagonists
    • DOI 10.1016/S0006-2952(00)00546-3, PII S0006295200005463
    • Vauquelin G, Morsing P, Fierens FLP, et al. A two-state receptor model for the interaction between angiotensin II AT1 receptors and their non-peptide antagonists. Biochem Pharmacol 2001;61:277-84 (Pubitemid 32126665)
    • (2001) Biochemical Pharmacology , vol.61 , Issue.3 , pp. 277-284
    • Vauquelin, G.1    Morsing, P.2    Fierens, F.L.P.3    De Backer, J.-P.4    Vanderheyden, P.M.L.5
  • 100
    • 0029126526 scopus 로고
    • Detection quantitation and verification of allosteric interactions of agents with labeled and unlabeled ligands at G protein coupled receptors: Interactions of strychnine and acetylcholine at muscarinic receptors
    • Lazareno S, Birdsall NJM. Detection, quantitation and verification of allosteric interactions of agents with labeled and unlabeled ligands at G protein coupled receptors: interactions of strychnine and acetylcholine at muscarinic receptors. Mol Pharmacol 1995;48:362-78
    • (1995) Mol. Pharmacol. , vol.48 , pp. 362-378
    • Lazareno, S.1    Birdsall, N.J.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.