메뉴 건너뛰기




Volumn 7, Issue 10, 2012, Pages 969-988

Ligand-receptor interaction platforms and their applications for drug discovery

Author keywords

Affinity; Backscattering interferometry; Biochemical mechanism of action; Biolayer interferometry; Calorimetry; Conformation; Crystallography; Drugtarget interaction; Fluorescence; in silico screening; Kinetics; Label free; Ligand binding techniques; Microfluidics; Nuclear magnetic resonance; Plasmon waveguide resonance; Polypharmacology; Protein thermal denaturation; Radioligand binding; Rebinding; Residence time; Resonant waveguide grating; Surface acoustic wave; Surface plasmon resonance; Thermodynamics; Whispering gallery mode

Indexed keywords

ADRENALIN; CANDESARTAN; CARAZOLOL; CLOZAPINE; FLUORESCENT DYE; ISOPRENALINE; NEUROLEPTIC AGENT; QUETIAPINE; RADIOLIGAND; SALMETEROL; SPIPERONE; TIOTROPIUM BROMIDE;

EID: 84866875777     PISSN: 17460441     EISSN: 1746045X     Source Type: Journal    
DOI: 10.1517/17460441.2012.715631     Document Type: Review
Times cited : (114)

References (182)
  • 3
    • 8344271026 scopus 로고    scopus 로고
    • Production of recombinant protein therapeutics in cultivated mammalian cells
    • Wurm FM. Production of recombinant protein therapeutics in cultivated mammalian cells. Nat Biotechnol 2004;22:1393-8
    • (2004) Nat Biotechnol , vol.22 , pp. 1393-1398
    • Wurm, F.M.1
  • 5
    • 84855840733 scopus 로고    scopus 로고
    • Target-drug interactions: First principles and their application to drug discovery
    • Nunez S, Venhorst J, Kruse CG. Target-drug interactions: first principles and their application to drug discovery. Drug Discov Today 2012;17:10-22
    • (2012) Drug Discov Today , vol.17 , pp. 10-22
    • Nunez, S.1    Venhorst, J.2    Kruse, C.G.3
  • 6
    • 79952171625 scopus 로고    scopus 로고
    • Probing the links between in vitro potency, ADMET and physicochemical parameters
    • Gleeson M, Hersey A, Montanari D, Overington J. Probing the links between in vitro potency, ADMET and physicochemical parameters. Nat Rev Drug Discov 2011;10:197-208
    • (2011) Nat Rev Drug Discov , vol.10 , pp. 197-208
    • Gleeson, M.1    Hersey, A.2    Montanari, D.3    Overington, J.4
  • 7
    • 33748325882 scopus 로고    scopus 로고
    • Drug-target residence time and its implications for lead optimization
    • Copeland RA, Pompliano DL, Meek TD. Drug-target residence time and its implications for lead optimization. Nat Rev Drug Discov 2006;5:730-9
    • (2006) Nat Rev Drug Discov , vol.5 , pp. 730-739
    • Copeland, R.A.1    Pompliano, D.L.2    Meek, T.D.3
  • 8
    • 34447626644 scopus 로고    scopus 로고
    • GPCR functional selectivity has therapeutic impact
    • Mailman RB. GPCR functional selectivity has therapeutic impact. Trends Pharmacol Sci 2007;28:390-6
    • (2007) Trends Pharmacol Sci , vol.28 , pp. 390-396
    • Mailman, R.B.1
  • 9
    • 77952354490 scopus 로고    scopus 로고
    • Seven transmembrane receptors as shapeshifting proteins: The impact of allosteric modulation and functional selectivity on new drug discovery
    • Kenakin T, Miller LJ. Seven transmembrane receptors as shapeshifting proteins: the impact of allosteric modulation and functional selectivity on new drug discovery. Pharmacol Rev 2010;62:265-304
    • (2010) Pharmacol Rev , vol.62 , pp. 265-304
    • Kenakin, T.1    Miller, L.J.2
  • 10
    • 33846503153 scopus 로고    scopus 로고
    • Both ligand- and cell-specific parameters control ligand agonism in a kinetic model of G protein-coupled receptor signaling
    • Kinzer-Ursem TL, Linderman JJ. Both ligand- and cell-specific parameters control ligand agonism in a kinetic model of G protein-coupled receptor signaling. PLoS Comput Biol 2007;3:e6
    • (2007) PLoS Comput Biol , vol.3
    • Kinzer-Ursem, T.L.1    Linderman, J.J.2
  • 11
    • 77953184143 scopus 로고    scopus 로고
    • Being Mindful of Seven-transmembrane Receptor 'guests' when assessing agonist selectivity
    • Kenakin T. Being mindful of seven-transmembrane receptor 'guests' when assessing agonist selectivity. Br J Pharmacol 2010;160:1045-7
    • (2010) Br J Pharmacol , vol.160 , pp. 1045-1047
    • Kenakin, T.1
  • 12
    • 0018861561 scopus 로고
    • The character of the muscarinic receptors in different regions of the rat brain
    • Birdsall NJ, Hulme EC, Burgen A. The character of the muscarinic receptors in different regions of the rat brain. Proc R Soc Lond B Biol Sci 1980;207:1-12
    • (1980) Proc R Soc Lond B Biol Sci , vol.207 , pp. 1-12
    • Birdsall, N.J.1    Hulme, E.C.2    Burgen, A.3
  • 13
    • 70350340728 scopus 로고    scopus 로고
    • The role of dynamic conformational ensembles in biomolecular recognition
    • Boehr DD, Nussinov R, Wright PE. The role of dynamic conformational ensembles in biomolecular recognition. Nat Chem Biol 2009;5:789-96
    • (2009) Nat Chem Biol , vol.5 , pp. 789-796
    • Boehr, D.D.1    Nussinov, R.2    Wright, P.E.3
  • 14
    • 66249144426 scopus 로고    scopus 로고
    • The structure and function of G-protein-coupled receptors
    • Rosenbaum DM, Rasmussen SG, Kobilka BK. The structure and function of G-protein-coupled receptors. Nature 2009;459:356-63
    • (2009) Nature , vol.459 , pp. 356-363
    • Rosenbaum, D.M.1    Rasmussen, S.G.2    Kobilka, B.K.3
  • 15
    • 80052001378 scopus 로고    scopus 로고
    • Pathway and mechanism of drug binding to G-protein-coupled receptors
    • Dror RO, Pan AC, Arlow DH, et al. Pathway and mechanism of drug binding to G-protein-coupled receptors. Proc Natl Acad Sci USA 2011;108:13118-23
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 13118-13123
    • Dror, R.O.1    Pan, A.C.2    Arlow, D.H.3
  • 16
    • 66149149851 scopus 로고    scopus 로고
    • Structure-based discovery of b2-adrenergic receptor ligands
    • Kolb P, Rosenbaum DM, Irwin JJ, et al. Structure-based discovery of b2-adrenergic receptor ligands. Proc Natl Acad Sci USA 2009;106:6843-8
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 6843-6848
    • Kolb, P.1    Rosenbaum, D.M.2    Irwin, J.J.3
  • 18
    • 4544381198 scopus 로고    scopus 로고
    • Biochemical mechanisms of drug action: What does it take for success?
    • Swinney DC. Biochemical mechanisms of drug action: what does it take for success? Nat Rev Drug Discov 2004;3:801-8
    • (2004) Nat Rev Drug Discov , vol.3 , pp. 801-808
    • Swinney, D.C.1
  • 19
    • 44049103958 scopus 로고    scopus 로고
    • Residence time of receptor-ligand complexes and its effect on biological functions
    • Tummina PJ, Copeland RA. Residence time of receptor-ligand complexes and its effect on biological functions. Biochemistry 2008;47:5481-92
    • (2008) Biochemistry , vol.47 , pp. 5481-5492
    • Tummina, P.J.1    Copeland, R.A.2
  • 20
    • 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 Devel 2009;12:488-96
    • (2009) Curr Opin Drug Discov Devel , vol.12 , pp. 488-496
    • Zhang, R.1    Monsma, F.2
  • 21
    • 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
  • 22
    • 77955329488 scopus 로고    scopus 로고
    • Drug-target residence time: Critical information for lead optimization
    • Lu H, Tonge PJ. Drug-target residence time: critical information for lead optimization. Curr Opin Chem Biol 2010;14:467-74
    • (2010) Curr Opin Chem Biol , vol.14 , pp. 467-474
    • Lu, H.1    Tonge, P.J.2
  • 23
    • 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
  • 25
    • 0033534194 scopus 로고    scopus 로고
    • Tiotropium (Spiriva): Mechanistical considerations and clinical profile in obstructive lung disease
    • Disse B, Speck GA, Rominger KL, et al. Tiotropium (Spiriva): mechanistical considerations and clinical profile in obstructive lung disease. Life Sci 1999;64:457-64
    • (1999) Life Sci , vol.64 , pp. 457-464
    • Disse, B.1    Speck, G.A.2    Rominger, K.L.3
  • 26
    • 0033994636 scopus 로고    scopus 로고
    • The pharmacological properties of tiotropium
    • Barnes PJ. The pharmacological properties of tiotropium. Chest 2000;117:63S-6S
    • (2000) Chest , vol.117
    • Barnes, P.J.1
  • 27
    • 0035094264 scopus 로고    scopus 로고
    • Does fast dissociation from the dopamine D2 receptor explain the action of atypical antipsychotics? A new hypothesis
    • Kapur S, Seeman P. Does fast dissociation from the dopamine D2 receptor explain the action of atypical antipsychotics? A new hypothesis. Am J Psychiatry 2001;158:360-9
    • (2001) Am J Psychiatry , vol.158 , pp. 360-369
    • Kapur, S.1    Seeman, P.2
  • 29
    • 16644394144 scopus 로고    scopus 로고
    • Effects of geometry of the immunological synapse on the delivery of effector molecules
    • Coombs D, Goldstein B. Effects of geometry of the immunological synapse on the delivery of effector molecules. Biophys J 2004;87:2215-20
    • (2004) Biophys J , vol.87 , pp. 2215-2220
    • Coombs, D.1    Goldstein, B.2
  • 30
    • 77956309074 scopus 로고    scopus 로고
    • Long-acting target binding and rebinding as mechanisms to prolong in vivo drug action
    • Vauquelin G, Charlton SJ. Long-acting 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. 488-508
    • Vauquelin, G.1    Charlton, S.J.2
  • 31
    • 0342813129 scopus 로고    scopus 로고
    • Experimental design for the kinetic analysis of protein-protein interactions with surface plasmon resonance biosensors
    • Karlsson R, Falt R. Experimental design for the kinetic analysis of protein-protein interactions with surface plasmon resonance biosensors. J Immunol Method 1997;200:121-33
    • (1997) J Immunol Method , vol.200 , pp. 121-133
    • Karlsson, R.1    Falt, R.2
  • 32
    • 77953631827 scopus 로고    scopus 로고
    • A medicinal chemist's guide to molecular interactions
    • Bissantz C, Kuhn B, Stahl M. A medicinal chemist's guide to molecular interactions. J Med Chem 2010;53:5061-84
    • (2010) J Med Chem , vol.53 , pp. 5061-5084
    • Bissantz, C.1    Kuhn, B.2    Stahl, M.3
  • 34
    • 77957229353 scopus 로고    scopus 로고
    • Thermodynamics guided lead discovery and optimization
    • Ferenczy GG, Keseru GM. Thermodynamics guided lead discovery and optimization. Drug Discov Today 2010;15:919-32
    • (2010) Drug Discov Today , vol.15 , pp. 919-932
    • Ferenczy, G.G.1    Keseru, G.M.2
  • 35
    • 1942453243 scopus 로고    scopus 로고
    • Ligand efficiency: A useful metric for lead selection
    • Hopkins AL, Groom CR, Alex A. Ligand efficiency: a useful metric for lead selection. Drug Discov Today 2004;9:430-1
    • (2004) Drug Discov Today , vol.9 , pp. 430-431
    • Hopkins, A.L.1    Groom, C.R.2    Alex, A.3
  • 37
    • 17044403086 scopus 로고    scopus 로고
    • Ligand efficiency indices as guideposts for drug discovery
    • Abad-Zapatero C, Metz JT. Ligand efficiency indices as guideposts for drug discovery. Drug Discov Today 2005;10:464-9
    • (2005) Drug Discov Today , vol.10 , pp. 464-469
    • Abad-Zapatero, C.1    Metz, J.T.2
  • 38
    • 34447548576 scopus 로고    scopus 로고
    • Ligand efficiency indices for effective drug discovery
    • Abad-Zapatero C. Ligand efficiency indices for effective drug discovery. Expert Opin Drug Discov 2007;2:469-88
    • (2007) Expert Opin Drug Discov , vol.2 , pp. 469-488
    • Abad-Zapatero, C.1
  • 39
    • 77957682613 scopus 로고    scopus 로고
    • Ligand efficiency indices for an effective mapping of chemico-biological space: The concept of an atlas-like representation
    • Abad-Zapatero C, Perisic O, Wass J, et al. Ligand efficiency indices for an effective mapping of chemico-biological space: the concept of an atlas-like representation. Drug Discov Today 2010;15:804-11
    • (2010) Drug Discov Today , vol.15 , pp. 804-811
    • Abad-Zapatero, C.1    Perisic, O.2    Wass, J.3
  • 40
    • 80255131239 scopus 로고    scopus 로고
    • Kinetic efficiency: The missing metric for enhancing compound quality?
    • Holdgate GA. Kinetic efficiency: the missing metric for enhancing compound quality? Drug Discov Today 2011;16:910-13
    • (2011) Drug Discov Today , vol.16 , pp. 910-913
    • Holdgate, G.A.1
  • 41
    • 35748934487 scopus 로고    scopus 로고
    • The influence of drug-like concepts on decision-making in medicinal chemistry
    • Leeson PD, Springthorpe B. The influence of drug-like concepts on decision-making in medicinal chemistry. Nat Rev Drug Discov 2007;6:881-90
    • (2007) Nat Rev Drug Discov , vol.6 , pp. 881-890
    • Leeson, P.D.1    Springthorpe, B.2
  • 42
    • 43049088827 scopus 로고    scopus 로고
    • Ligand binding efficiency: Trends, physical basis, and implications
    • Reynolds CH, Tounge BA, Bembenek SD. Ligand binding efficiency: trends, physical basis, and implications. J Med Chem 2008;51:2432-8
    • (2008) J Med Chem , vol.51 , pp. 2432-2438
    • Reynolds, C.H.1    Tounge, B.A.2    Bembenek, S.D.3
  • 44
    • 67650085841 scopus 로고    scopus 로고
    • Simple size-independent measure of ligand efficiency
    • Nissink JWM. Simple size-independent measure of ligand efficiency. J Chem Inf Model 2009;49:1617-22
    • (2009) J Chem Inf Model , vol.49 , pp. 1617-1622
    • Nissink, J.W.M.1
  • 45
    • 78650742572 scopus 로고    scopus 로고
    • Ligand efficiency as a guide in fragment hit selection and optimization
    • Schultes S, de Graff C, Haaksma EEJ, et al. Ligand efficiency as a guide in fragment hit selection and optimization. Drug Discov Today Technol 2010;7:e157
    • (2010) Drug Discov Today Technol , vol.7
    • Schultes, S.1    De Graff, C.2    Eej, H.3
  • 46
    • 2042538998 scopus 로고    scopus 로고
    • Receptor binding techniques
    • Keen M. Receptor binding techniques. Methods Mol Biol 1999;106:1-290
    • (1999) Methods Mol Biol , vol.106 , pp. 1-290
    • Keen, M.1
  • 47
    • 51149107449 scopus 로고    scopus 로고
    • Scintillation proximity assays in high-throughput screening
    • Glickman JF, Schmid A, Ferrand S. Scintillation proximity assays in high-throughput screening. Assay Drug Dev Technol 2008;6:433-55
    • (2008) Assay Drug Dev Technol , vol.6 , pp. 433-455
    • Glickman, J.F.1    Schmid, A.2    Ferrand, S.3
  • 48
    • 78049403279 scopus 로고    scopus 로고
    • Ligand binding assays at equilibrium: Validation and interpretation
    • Hulme EC, Trevethick MA. Ligand binding assays at equilibrium: validation and interpretation. Br J Pharmacol 2010;161:1219-37
    • (2010) Br J Pharmacol , vol.161 , pp. 1219-1237
    • Hulme, E.C.1    Trevethick, M.A.2
  • 49
    • 84862856969 scopus 로고    scopus 로고
    • Determination of drug-receptor residence times by radioligand binding and functional assays: Experimental strategies and physiological relevance
    • Vauquelin G. Determination of drug-receptor residence times by radioligand binding and functional assays: experimental strategies and physiological relevance. Med Chem Commun 2012;3:645-51
    • (2012) Med Chem Commun , vol.3 , pp. 645-651
    • Vauquelin, G.1
  • 50
    • 0033773937 scopus 로고    scopus 로고
    • Fluorescence polarization and anisotropy in high throughput screening: Perspectives and primer
    • Owicki JC. Fluorescence polarization and anisotropy in high throughput screening: perspectives and primer. J Biomol Screen 2000;5:297-306
    • (2000) J Biomol Screen , vol.5 , pp. 297-306
    • Owicki, J.C.1
  • 51
    • 19344375930 scopus 로고    scopus 로고
    • Lanthanide-based luminescent assays for ligand-receptor interactions
    • Handl HL, Gillies RJ. Lanthanide-based luminescent assays for ligand-receptor interactions. Life Sci 2005;77:361-71
    • (2005) Life Sci , vol.77 , pp. 361-371
    • Handl, H.L.1    Gillies, R.J.2
  • 52
    • 78650630819 scopus 로고    scopus 로고
    • Fluorescence polarization assays in small molecule screening
    • Lea WA, Simeonov A. Fluorescence polarization assays in small molecule screening. Expert Opin Drug Discov 2011;6:17-32
    • (2011) Expert Opin Drug Discov , vol.6 , pp. 17-32
    • Lea, W.A.1    Simeonov, A.2
  • 53
    • 79952385103 scopus 로고    scopus 로고
    • Analysis of protein-ligand interactions by fluorescence polarization
    • Rossi AM, Taylor CW. Analysis of protein-ligand interactions by fluorescence polarization. Nat Protoc 2011;6:365-87
    • (2011) Nat Protoc , vol.6 , pp. 365-387
    • Rossi, A.M.1    Taylor, C.W.2
  • 54
    • 84858203893 scopus 로고    scopus 로고
    • Fluorescence/bioluminescence resonance energy transfer techniques to study G-protein-coupled receptor activation and signaling
    • Lohse MJ, Nuber S, Hoffmann C. Fluorescence/bioluminescence resonance energy transfer techniques to study G-protein-coupled receptor activation and signaling. Pharmacol Rev 2012;64:299-336
    • (2012) Pharmacol Rev , vol.64 , pp. 299-336
    • Lohse, M.J.1    Nuber, S.2    Hoffmann, C.3
  • 55
    • 0242385316 scopus 로고    scopus 로고
    • Ligand-receptor kinetics measured by total internal reflection with fluorescence correlation spectroscopy
    • Lieto AM, Cush RC, Thompson NL. Ligand-receptor kinetics measured by total internal reflection with fluorescence correlation spectroscopy. Biophys J 2003;85:3294-302
    • (2003) Biophys J , vol.85 , pp. 3294-3302
    • Lieto, A.M.1    Cush, R.C.2    Thompson, N.L.3
  • 56
    • 0033964118 scopus 로고    scopus 로고
    • High-throughput and ultra-high-throughput screening: Solution- and cell-based approaches
    • Sundberg SA. High-throughput and ultra-high-throughput screening: solution- and cell-based approaches. Curr Opin Biotechnol 2000;11:47-53
    • (2000) Curr Opin Biotechnol , vol.11 , pp. 47-53
    • Sundberg, S.A.1
  • 57
    • 45949106612 scopus 로고    scopus 로고
    • The challenge of selecting protein kinase assays for lead discovery optimization
    • Ma H, Deacon S, Horiuchi K. The challenge of selecting protein kinase assays for lead discovery optimization. Expert Opin Drug Discov 2008;3:607-21
    • (2008) Expert Opin Drug Discov , vol.3 , pp. 607-621
    • Ma, H.1    Deacon, S.2    Horiuchi, K.3
  • 58
    • 80555135906 scopus 로고    scopus 로고
    • Fluorescence labels in kinases: A high-throughput kinase binding assay for the identification of DFG-out binding ligands
    • Simard JR, Rauh D. Fluorescence labels in kinases: a high-throughput kinase binding assay for the identification of DFG-out binding ligands. Methods Mol Biol 2012;800:95-117
    • (2012) Methods Mol Biol , vol.800 , pp. 95-117
    • Simard, J.R.1    Rauh, D.2
  • 59
    • 0037107007 scopus 로고    scopus 로고
    • Novel detection strategies for drug discovery
    • Hemmila IA, Hurskainen P. Novel detection strategies for drug discovery. Drug Discov Today 2002;7:150-6
    • (2002) Drug Discov Today , vol.7 , pp. 150-156
    • Hemmila, I.A.1    Hurskainen, P.2
  • 60
    • 84866881898 scopus 로고    scopus 로고
    • Label-free phenotypic profiling identified D-luciferin as a GPR35 agonist
    • Hu H, Deng H, Fang Y. Label-free phenotypic profiling identified D-luciferin as a GPR35 agonist. PLoS One 2012;7:e34934
    • (2012) PLoS One , vol.7
    • Hu, H.1    Deng, H.2    Fang, Y.3
  • 61
    • 0035860499 scopus 로고    scopus 로고
    • Global analysis of protein activities using proteome chips
    • Zhu H, Bilgin M, Bangham R, et al. Global analysis of protein activities using proteome chips. Science 2001;293:2101-5
    • (2001) Science , vol.293 , pp. 2101-2105
    • Zhu, H.1    Bilgin, M.2    Bangham, R.3
  • 62
    • 0041430941 scopus 로고    scopus 로고
    • G protein-coupled receptor microarrays for drug discovery
    • Fang Y, Lahiri J, Picard L. G protein-coupled receptor microarrays for drug discovery. Drug Discov Today 2003;8:755-61
    • (2003) Drug Discov Today , vol.8 , pp. 755-761
    • Fang, Y.1    Lahiri, J.2    Picard, L.3
  • 63
    • 13444280261 scopus 로고    scopus 로고
    • Protein microarrays as tools for functional proteomics
    • LaBaer J, Ramachandran N. Protein microarrays as tools for functional proteomics. Curr Opin Chem Biol 2005;9:14-19
    • (2005) Curr Opin Chem Biol , vol.9 , pp. 14-19
    • Labaer, J.1    Ramachandran, N.2
  • 64
    • 77950446611 scopus 로고    scopus 로고
    • Screening kinase inhibitors with a microarray-based fluorescent and resonance light scattering assay
    • Li T, Liu D, Wang Z. Screening kinase inhibitors with a microarray-based fluorescent and resonance light scattering assay. Anal Chem 2010;82:3067-72
    • (2010) Anal Chem , vol.82 , pp. 3067-3072
    • Li, T.1    Liu, D.2    Wang, Z.3
  • 65
    • 30044449171 scopus 로고    scopus 로고
    • Air-stable G protein-coupled receptor microarrays and ligand binding characteristics
    • Fang Y, Peng J, Ferrie AM, Burkhalter RS. Air-stable G protein-coupled receptor microarrays and ligand binding characteristics. Anal Chem 2006;78:149-55
    • (2006) Anal Chem , vol.78 , pp. 149-155
    • Fang, Y.1    Peng, J.2    Ferrie, A.M.3    Burkhalter, R.S.4
  • 66
    • 35548958205 scopus 로고
    • Plasma losses by fast electrons in thin films
    • Ritchie RH. Plasma losses by fast electrons in thin films. Phys Rev 1957;106:874-81
    • (1957) Phys Rev , vol.106 , pp. 874-881
    • Ritchie, R.H.1
  • 67
    • 78249249972 scopus 로고    scopus 로고
    • Theory and applications of surface plasmon resonance, resonant mirror, resonant waveguide grating, and dual polarization interferometry biosensors
    • Daghestani HN, Day BW. Theory and applications of surface plasmon resonance, resonant mirror, resonant waveguide grating, and dual polarization interferometry biosensors. Sensors 2010;10:9630-46
    • (2010) Sensors , vol.10 , pp. 9630-9646
    • Daghestani, H.N.1    Day, B.W.2
  • 68
  • 69
    • 0033955735 scopus 로고    scopus 로고
    • Advances in surface plasmon resonance biosensor analysis
    • Rich RL, Myszka DG. Advances in surface plasmon resonance biosensor analysis. Curr Opin Biotechnol 2000;11:54-61
    • (2000) Curr Opin Biotechnol , vol.11 , pp. 54-61
    • Rich, R.L.1    Myszka, D.G.2
  • 70
    • 33845902552 scopus 로고    scopus 로고
    • Higherthroughput, label-free, real-time molecular interaction analysis
    • Rich RL, Myszka DG. Higherthroughput, label-free, real-time molecular interaction analysis. Anal Biochem 2007;361:1-6
    • (2007) Anal Biochem , vol.361 , pp. 1-6
    • Rich, R.L.1    Myszka, D.G.2
  • 71
    • 37549010341 scopus 로고    scopus 로고
    • Survey of the year 2006 commercial optical biosensor literature
    • Rich RL, Myszka DG. Survey of the year 2006 commercial optical biosensor literature. J Mol Recognit 2006;20:300-66
    • (2006) J Mol Recognit , vol.20 , pp. 300-366
    • Rich, R.L.1    Myszka, D.G.2
  • 72
    • 0032693817 scopus 로고    scopus 로고
    • Micropatterned immobilization of a G protein-coupled receptor and direct detection of G protein activation
    • Bieri C, Ernst OP, Heyse S, et al. Micropatterned immobilization of a G protein-coupled receptor and direct detection of G protein activation. Nat Biotechnol 1999;17:1105-8
    • (1999) Nat Biotechnol , vol.17 , pp. 1105-1108
    • Bieri, C.1    Ernst, O.P.2    Heyse, S.3
  • 73
    • 79960398015 scopus 로고    scopus 로고
    • Screening for GPCR ligands using surface plasmon resonance
    • Navratilova I, Besnard J, Hopkins AL. Screening for GPCR ligands using surface plasmon resonance. ACS Med Chem Lett 2011;2:549-54
    • (2011) ACS Med Chem Lett , vol.2 , pp. 549-5554
    • Navratilova, I.1    Besnard, J.2    Hopkins, A.L.3
  • 74
    • 0345550287 scopus 로고    scopus 로고
    • Techniques: Plasmon-waveguide resonance (PWR) spectroscopy as a tool to study ligand-GPCR interactions
    • Tollin G, Salamon Z, Hruby VJ. Techniques: plasmon-waveguide resonance (PWR) spectroscopy as a tool to study ligand-GPCR interactions. Trends Pharmacol Sci 2003;24:655-9
    • (2003) Trends Pharmacol Sci , vol.24 , pp. 655-659
    • Tollin, G.1    Salamon, Z.2    Hruby, V.J.3
  • 75
    • 1942454801 scopus 로고    scopus 로고
    • Graphical analysis of mass and anisotropy changes observed by plasmon-waveguide resonance spectroscopy can provide useful insights into membrane protein function
    • Salamon Z, Tollin G. Graphical analysis of mass and anisotropy changes observed by plasmon-waveguide resonance spectroscopy can provide useful insights into membrane protein function. Biophys J 2004;86:2508-16
    • (2004) Biophys J , vol.86 , pp. 2508-2516
    • Salamon, Z.1    Tollin, G.2
  • 76
    • 2142766875 scopus 로고    scopus 로고
    • Different structural states of the proteolipid membrane are produced by ligand binding to the human -opioid receptor as shown by plasmon-waveguide resonance spectroscopy
    • Alves ID, Cowell SM, Salamon Z, et al. Different structural states of the proteolipid membrane are produced by ligand binding to the human -opioid receptor as shown by plasmon-waveguide resonance spectroscopy. Mol Pharmacol 2004;65:1248-57
    • (2004) Mol Pharmacol , vol.65 , pp. 1248-1257
    • Alves, I.D.1    Cowell, S.M.2    Salamon, Z.3
  • 77
    • 36048969417 scopus 로고    scopus 로고
    • Non-invasive optical biosensor for probing cell signaling
    • Fang Y. Non-invasive optical biosensor for probing cell signaling. Sensors 2007;7:2316-29
    • (2007) Sensors , vol.7 , pp. 2316-2329
    • Fang, Y.1
  • 78
    • 0037021762 scopus 로고    scopus 로고
    • Colorimetric resonant reflection as a direct biochemical assay technique
    • Cunningham B, Li P, Lin B, Pepper J. Colorimetric resonant reflection as a direct biochemical assay technique. Sensors Actuators B Chem 2002;81:316-28
    • (2002) Sensors Actuators B Chem , vol.81 , pp. 316-328
    • Cunningham, B.1    Li, P.2    Lin, B.3    Pepper, J.4
  • 79
    • 33749492783 scopus 로고    scopus 로고
    • Phospho-specific recognition by 14-3-3 proteins and antibodies monitored by a high throughput label-free optical biosensor
    • Wu M, Coblitz B, Shikano S, et al. Phospho-specific recognition by 14-3-3 proteins and antibodies monitored by a high throughput label-free optical biosensor. FEBS Lett 2006;580:5681-9
    • (2006) FEBS Lett , vol.580 , pp. 5681-5689
    • Wu, M.1    Coblitz, B.2    Shikano, S.3
  • 80
    • 79960524751 scopus 로고    scopus 로고
    • High-throughput screening for modulators of protein-protein interactions: Use of photonic crystal biosensors and complementary technologies
    • Heeres JT, Hergenrother PJ. High-throughput screening for modulators of protein-protein interactions: use of photonic crystal biosensors and complementary technologies. Chem Soc Rev 2011;40:4398-410
    • (2011) Chem Soc Rev , vol.40 , pp. 4398-4410
    • Heeres, J.T.1    Hergenrother, P.J.2
  • 81
    • 84856074460 scopus 로고    scopus 로고
    • Label-free detection of G protein-SNARE interactions and screening for small molecule modulators
    • Wells CA, Betke KM, Lindsley CW, Hamm HE. Label-free detection of G protein-SNARE interactions and screening for small molecule modulators. ACS Chem Neurosci 2012;3:69-78
    • (2012) ACS Chem Neurosci , vol.3 , pp. 69-78
    • Wells, C.A.1    Betke, K.M.2    Lindsley, C.W.3    Hamm, H.E.4
  • 82
    • 84860124363 scopus 로고    scopus 로고
    • Application of optical biosensors in small-molecule screening activities
    • Geschwindner S, Carlsson JF, Knecht W. Application of optical biosensors in small-molecule screening activities. Sensors 2012;12:4311-23
    • (2012) Sensors , vol.12 , pp. 4311-4323
    • Geschwindner, S.1    Carlsson, J.F.2    Knecht, W.3
  • 83
    • 80755139203 scopus 로고    scopus 로고
    • Review of transducer principles for label-free biomolecular interaction analysis
    • Nirschl M, Reuter F, Voros J. Review of transducer principles for label-free biomolecular interaction analysis. Biosensors 2011;1:70-92
    • (2011) Biosensors , vol.1 , pp. 70-92
    • Nirschl, M.1    Reuter, F.2    Voros, J.3
  • 84
    • 69749094463 scopus 로고    scopus 로고
    • Label-free detection of biomolecular interactions using BioLayer interferometry for kinetic characterization
    • Concepcion J, Witte K, Wartchow C, et al. Label-free detection of biomolecular interactions using BioLayer interferometry for kinetic characterization. Comb Chem High Throughput Screen 2009;12:791-800
    • (2009) Comb Chem High Throughput Screen , vol.12 , pp. 791-800
    • Concepcion, J.1    Witte, K.2    Wartchow, C.3
  • 85
    • 80051787791 scopus 로고    scopus 로고
    • Biosensor-based small molecule fragment screening with biolayer interferometry
    • Wartchow CA, Podlaski F, Li S, et al. Biosensor-based small molecule fragment screening with biolayer interferometry. J Comput Aided Mol Des 2011;25:669-76
    • (2011) J Comput Aided Mol des , vol.25 , pp. 669-676
    • Wartchow, C.A.1    Podlaski, F.2    Li, S.3
  • 86
    • 71849117804 scopus 로고    scopus 로고
    • Surface plasmon resonance imaging for affinity-based biosensors
    • Scarano S, Mascini M, Turner APF, Minunni M. Surface plasmon resonance imaging for affinity-based biosensors. Biosens Bioelectron 2010;25:957-66
    • (2010) Biosens Bioelectron , vol.25 , pp. 957-966
    • Scarano, S.1    Mascini, M.2    Apf, T.3    Minunni, M.4
  • 88
    • 58349120186 scopus 로고    scopus 로고
    • Detergent screening of a G-protein-coupled receptor using serial and array biosensor technologies
    • Rich RL, Miles AR, Gale BK, Myszka DG. Detergent screening of a G-protein-coupled receptor using serial and array biosensor technologies. Anal Biochem 2009;386:98-104
    • (2009) Anal Biochem , vol.386 , pp. 98-104
    • Rich, R.L.1    Miles, A.R.2    Gale, B.K.3    Myszka, D.G.4
  • 89
    • 27644555518 scopus 로고    scopus 로고
    • Emerging tools for real-time label-free detection of interactions on functional protein microarrays
    • Ramachandran N, Larson DN, Stark PR, Hainsworth E. Emerging tools for real-time label-free detection of interactions on functional protein microarrays. FEBS J 2005;272:5412-25
    • (2005) FEBS J , vol.272 , pp. 5412-5425
    • Ramachandran, N.1    Larson, D.N.2    Stark, P.R.3    Hainsworth, E.4
  • 90
    • 33746742909 scopus 로고    scopus 로고
    • Looking towards label-free biomolecular interaction analysis in a high-throughput format: A review of new surface plasmon resonance technologies
    • Boozer C, Kim G, Cong S, et al. Looking towards label-free biomolecular interaction analysis in a high-throughput format: a review of new surface plasmon resonance technologies. Curr Opin Biotechnol 2006;17:400-5
    • (2006) Curr Opin Biotechnol , vol.17 , pp. 400-40405
    • Boozer, C.1    Kim, G.2    Cong, S.3
  • 91
    • 58149295602 scopus 로고    scopus 로고
    • Quantitative serum proteomics from surface plasmon resonance imaging
    • Lausted C, Hu Z, Hood L. Quantitative serum proteomics from surface plasmon resonance imaging. Mol Cell Proteomics 2008;7:2464-74
    • (2008) Mol Cell Proteomics , vol.7 , pp. 2464-2474
    • Lausted, C.1    Hu, Z.2    Hood, L.3
  • 92
    • 0037613348 scopus 로고    scopus 로고
    • Surface plasmon resonance imaging studies of protein-carbohydrate interactions
    • Smith EA, Thomas WD, Kiessling LL, Corn RM. Surface plasmon resonance imaging studies of protein-carbohydrate interactions. J Am Chem Soc 2003;125:6140-8
    • (2003) J Am Chem Soc , vol.125 , pp. 6140-6148
    • Smith, E.A.1    Thomas, W.D.2    Kiessling, L.L.3    Corn, R.M.4
  • 93
    • 34547790172 scopus 로고    scopus 로고
    • Development of a surface plasmon resonance mass spectrometry array platform
    • Nedelkov D. Development of a surface plasmon resonance mass spectrometry array platform. Anal Chem 2007;79:5987-90
    • (2007) Anal Chem , vol.79 , pp. 5987-5990
    • Nedelkov, D.1
  • 94
    • 33845893375 scopus 로고    scopus 로고
    • Fabrication and characterization of RNA aptamer microarrays for the study of protein-aptamer interactions with SPR imaging
    • Li Y, Lee HJ, Corn RM. Fabrication and characterization of RNA aptamer microarrays for the study of protein-aptamer interactions with SPR imaging. Nucleic Acids Res 2006;34:6416-24
    • (2006) Nucleic Acids Res , vol.34 , pp. 6416-6424
    • Li, Y.1    Lee, H.J.2    Corn, R.M.3
  • 95
    • 33750486181 scopus 로고    scopus 로고
    • Attomole detection of microRNAs by nanoparticle-amplified SPR imaging measurements of surface polyadenylation reactions
    • Fang S, Lee HJ, Wark AW, Corn RM. Attomole detection of microRNAs by nanoparticle-amplified SPR imaging measurements of surface polyadenylation reactions. J Am Chem Soc 2006;128:14044-6
    • (2006) J Am Chem Soc , vol.128 , pp. 14044-14046
    • Fang, S.1    Lee, H.J.2    Wark, A.W.3    Corn, R.M.4
  • 96
    • 65449147042 scopus 로고    scopus 로고
    • Proteins and proteomics: Life on the surface
    • Blow N. Proteins and proteomics: life on the surface. Nat Methods 2009;6:389-93
    • (2009) Nat Methods , vol.6 , pp. 389-393
    • Blow, N.1
  • 97
    • 79955991249 scopus 로고    scopus 로고
    • Protein detection by optical shift of a resonant microcavity
    • Vollmer F, Braun D, Libchaber A, et al. Protein detection by optical shift of a resonant microcavity. Appl Phys Lett 2002;80:4057-9
    • (2002) Appl Phys Lett , vol.80 , pp. 4057-4059
    • Vollmer, F.1    Braun, D.2    Libchaber, A.3
  • 98
    • 0037440564 scopus 로고    scopus 로고
    • Shift of whispering-gallery modes in microspheres by protein adsorption
    • Arnold S, Khoshsima M, Teraoka I, et al. Shift of whispering-gallery modes in microspheres by protein adsorption. Opt Lett 2003;28:272-4
    • (2003) Opt Lett , vol.28 , pp. 272-274
    • Arnold, S.1    Khoshsima, M.2    Teraoka, I.3
  • 99
    • 33947642687 scopus 로고    scopus 로고
    • Photoinduced transformations in bacteriorhodopsin membrane monitored with optical microcavities
    • Topolancik J, Vollmer F. Photoinduced transformations in bacteriorhodopsin membrane monitored with optical microcavities. Biophys J 2007;92:2223-9
    • (2007) Biophys J , vol.92 , pp. 2223-2229
    • Topolancik, J.1    Vollmer, F.2
  • 100
    • 58549114502 scopus 로고    scopus 로고
    • Single virus detection from the reactive shift, of a whispering-gallery mode
    • Vollmer F, Arnold S, Keng D. Single virus detection from the reactive shift, of a whispering-gallery mode. Proc Natl Acad Sci USA 2008;105:20701-4
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 20701-20704
    • Vollmer, F.1    Arnold, S.2    Keng, D.3
  • 101
    • 46249089703 scopus 로고    scopus 로고
    • Whispering-gallery-mode biosensing: Label-free detection down to single molecules
    • Vollmer F, Arnold S. Whispering-gallery-mode biosensing: label-free detection down to single molecules. Nat Methods 2008;5:591-6
    • (2008) Nat Methods , vol.5 , pp. 591-596
    • Vollmer, F.1    Arnold, S.2
  • 102
    • 34547865680 scopus 로고    scopus 로고
    • Label-free, single-molecule detection with optical microcavities
    • Armani AM, Kulkarni RP, Fraser SE, et al. Label-free, single-molecule detection with optical microcavities. Science 2007;317:783-7
    • (2007) Science , vol.317 , pp. 783-787
    • Armani, A.M.1    Kulkarni, R.P.2    Fraser, S.E.3
  • 103
    • 2642574048 scopus 로고    scopus 로고
    • Concentration of IL-2, IL-6, IL-8, IL-10 and TNF-alpha in children with acute lymphoblastic leukemia after cessation of chemotherapy
    • Mazur B, Mertas A, Son'ta-Jakimczyk D, et al. Concentration of IL-2, IL-6, IL-8, IL-10 and TNF-alpha in children with acute lymphoblastic leukemia after cessation of chemotherapy. Hematol Oncol 2004;22:27-34
    • (2004) Hematol Oncol , vol.22 , pp. 27-34
    • Mazur, B.1    Mertas, A.2    Son'Ta-Jakimczyk, D.3
  • 104
    • 79953240309 scopus 로고    scopus 로고
    • Whispering gallery microresonators for second harmonic light generation from a low number of small molecules
    • Dominguez-Juarez JL, Kozyreff G, Martorell J. Whispering gallery microresonators for second harmonic light generation from a low number of small molecules. Nat Commun 2011;2:254
    • (2011) Nat Commun , vol.2 , pp. 254
    • Dominguez-Juarez, J.L.1    Kozyreff, G.2    Martorell, J.3
  • 105
    • 34648815160 scopus 로고    scopus 로고
    • Free-solution, label-free molecular interactions studied by back-scattering interferometry
    • Bornhop DJ, Latham JC, Kussrow A, et al. Free-solution, label-free molecular interactions studied by back-scattering interferometry. Science 2007;317:1732-6
    • (2007) Science , vol.317 , pp. 1732-1736
    • Bornhop, D.J.1    Latham, J.C.2    Kussrow, A.3
  • 106
    • 64749106155 scopus 로고    scopus 로고
    • Free-solution label-free detection of alpha-crystallin chaperone interactions by back-scattering interferometry
    • Latham JC, Stein RA, Bornhop DJ, Mchaourab HS. Free-solution label-free detection of alpha-crystallin chaperone interactions by back-scattering interferometry. Anal Chem 2009;81:1865-71
    • (2009) Anal Chem , vol.81 , pp. 1865-1871
    • Latham, J.C.1    Stein, R.A.2    Bornhop, D.J.3    McHaourab, H.S.4
  • 107
    • 78449231796 scopus 로고    scopus 로고
    • Free-solution interaction assay of carbonic anhydrase to its inhibitors using back-scattering interferometry
    • Morcos EF, Kussrow A, Enders C, Bornhop D. Free-solution interaction assay of carbonic anhydrase to its inhibitors using back-scattering interferometry. Electrophoresis 2010;31:3691-5
    • (2010) Electrophoresis , vol.31 , pp. 3691-3695
    • Morcos, E.F.1    Kussrow, A.2    Enders, C.3    Bornhop, D.4
  • 108
    • 79953839803 scopus 로고    scopus 로고
    • Label-free quantification of membrane-ligand interactions using backscattering interferometry
    • Baksh MM, Kussrow AK, Mileni M, et al. Label-free quantification of membrane-ligand interactions using backscattering interferometry. Nat Biotechnol 2011;29:357-60
    • (2011) Nat Biotechnol , vol.29 , pp. 357-360
    • Baksh, M.M.1    Kussrow, A.K.2    Mileni, M.3
  • 109
    • 0037418476 scopus 로고    scopus 로고
    • Ganglioside microarrays for toxin detection
    • Fang Y, Frutos A, Lahiri J. Ganglioside Microarrays for Toxin Detection. Langmuir 2003;19:1500
    • (2003) Langmuir , vol.19 , pp. 1500
    • Fang, Y.1    Frutos, A.2    Lahiri, J.3
  • 110
    • 78049417719 scopus 로고    scopus 로고
    • Higher throughput calorimetry: Opportunities, approaches and challenges
    • Torres FE, Recht MI, Coyle JE, et al. Higher throughput calorimetry: opportunities, approaches and challenges. Curr Opin Struct Biol 2010;20:598-605
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 598-605
    • Torres, F.E.1    Recht, M.I.2    Coyle, J.E.3
  • 111
    • 37249005205 scopus 로고    scopus 로고
    • The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability
    • Niesen FH, Berglund H, Vedadi M. The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability. Nat Protoc 2007;2:2212-21
    • (2007) Nat Protoc , vol.2 , pp. 2212-2221
    • Niesen, F.H.1    Berglund, H.2    Vedadi, M.3
  • 112
    • 33751559579 scopus 로고    scopus 로고
    • Screening for ligands using a generic and high-throughput light-scattering-based assay
    • Senisterra GA, Markin E, Yamazaki K, et al. Screening for ligands using a generic and high-throughput light-scattering-based assay. J Biomol Screen 2006;11:940-8
    • (2006) J Biomol Screen , vol.11 , pp. 940-948
    • Senisterra, G.A.1    Markin, E.2    Yamazaki, K.3
  • 113
    • 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;103:15835-40
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 15835-15840
    • Vedadi, M.1    Niesen, F.H.2    Allali-Hassani, A.3
  • 115
    • 22544461068 scopus 로고    scopus 로고
    • Recent applications of protein crystallography and structure-guided drug design
    • Williams SP, Kuyper LF, Pearce KH. Recent applications of protein crystallography and structure-guided drug design. Curr Opin Chem Biol 2005;9:371-80
    • (2005) Curr Opin Chem Biol , vol.9 , pp. 371-380
    • Williams, S.P.1    Kuyper, L.F.2    Pearce, K.H.3
  • 116
    • 0036051992 scopus 로고    scopus 로고
    • High-throughput crystallography for lead discovery in drug design
    • Blundell TL, Jhoti H, Abell C. High-throughput crystallography for lead discovery in drug design. Nat Rev Drug Discov 2002;1:45-54
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 45-54
    • Blundell, T.L.1    Jhoti, H.2    Abell, C.3
  • 117
    • 0037107887 scopus 로고    scopus 로고
    • Structure-based virtual screening: An overview
    • Lyne PD. Structure-based virtual screening: an overview. Drug Discov Today 2002;7:1047-55
    • (2002) Drug Discov Today , vol.7 , pp. 1047-1055
    • Lyne, P.D.1
  • 118
    • 8844263008 scopus 로고    scopus 로고
    • Docking and scoring in virtual screening for drug discovery: Methods and applications
    • Kitchen DB, Decornez H, Furr JR, Bajorath J. Docking and scoring in virtual screening for drug discovery: methods and applications. Nat Rev Drug Discov 2004;3:935-49
    • (2004) Nat Rev Drug Discov , vol.3 , pp. 935-949
    • Kitchen, D.B.1    Decornez, H.2    Furr, J.R.3    Bajorath, J.4
  • 119
    • 13844312649 scopus 로고    scopus 로고
    • ZINC - A free database of commercially available compounds for virtual screening
    • Irwin JJ, Shoichet BK. ZINC - a free database of commercially available compounds for virtual screening. J Chem Inf Model 2005;45:177-82
    • (2005) J Chem Inf Model , vol.45 , pp. 177-182
    • Irwin, J.J.1    Shoichet, B.K.2
  • 120
    • 11144323163 scopus 로고    scopus 로고
    • Virtual screening of chemical libraries
    • Shoichet BK. Virtual screening of chemical libraries. Nature 2004;432:862-5
    • (2004) Nature , vol.432 , pp. 862-865
    • Shoichet, B.K.1
  • 122
    • 51249121331 scopus 로고    scopus 로고
    • Perspectives on NMR in drug discovery: A technique comes of age
    • Pellecchia M, Bertini I, Cowburn D, et al. Perspectives on NMR in drug discovery: a technique comes of age. Nat Rev Drug Discov 2008;7:738-45
    • (2008) Nat Rev Drug Discov , vol.7 , pp. 738-745
    • Pellecchia, M.1    Bertini, I.2    Cowburn, D.3
  • 123
    • 70350422335 scopus 로고    scopus 로고
    • NMR methods in fragment screening: Theory and a comparison with other biophysical techniques
    • Dalvit C. NMR methods in fragment screening: theory and a comparison with other biophysical techniques. Drug Discov Today 2009;14:1051-7
    • (2009) Drug Discov Today , vol.14 , pp. 1051-1057
    • Dalvit, C.1
  • 124
    • 0034604451 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: A G protein-coupled receptor
    • Palczewski K, Kumasaka T, Hori T, et al. Crystal structure of rhodopsin: a G protein-coupled receptor. Science 2000;289:739-45
    • (2000) Science , vol.289 , pp. 739-745
    • Palczewski, K.1    Kumasaka, T.2    Hori, T.3
  • 125
    • 36248970132 scopus 로고    scopus 로고
    • Crystal structure of the human b2 adrenergic G-protein-coupled receptor
    • Rasmussen SG, Choi HJ, Rosenbaum DM, et al. Crystal structure of the human b2 adrenergic G-protein-coupled receptor. Nature 2007;450:383-7
    • (2007) Nature , vol.450 , pp. 383-387
    • Rasmussen, S.G.1    Choi, H.J.2    Rosenbaum, D.M.3
  • 126
    • 47949129742 scopus 로고    scopus 로고
    • Structure of b1-adrenergic G-protein-coupled receptor
    • Warne T, Serrano-Vega MJ, Baker JG, et al. Structure of b1-adrenergic G-protein-coupled receptor. Nature 2008;454:486-91
    • (2008) Nature , vol.454 , pp. 486-491
    • Warne, T.1    Serrano-Vega, M.J.2    Baker, J.G.3
  • 127
    • 56749103466 scopus 로고    scopus 로고
    • The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist
    • Jaakola VP, Griffith MT, Hanson MA, et al. The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist. Science 2008;322:1211-17
    • (2008) Science , vol.322 , pp. 1211-1217
    • Jaakola, V.P.1    Griffith, M.T.2    Ma, H.3
  • 128
    • 85027927015 scopus 로고    scopus 로고
    • Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists
    • Wu B, Chien EY, Mol CD, et al. Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists. Science 2010;330:1066-71
    • (2010) Science , vol.330 , pp. 1066-1071
    • Wu, B.1    Chien, E.Y.2    Mol, C.D.3
  • 129
    • 78449305788 scopus 로고    scopus 로고
    • Structure of the human dopamine D3 receptor in complex with a D2/D3 selective antagonist
    • Chien EY, Liu W, Zhao Q, et al. Structure of the human dopamine D3 receptor in complex with a D2/D3 selective antagonist. Science 2010;330:1091-5
    • (2010) Science , vol.330 , pp. 1091-1095
    • Chien, E.Y.1    Liu, W.2    Zhao, Q.3
  • 130
    • 79960070651 scopus 로고    scopus 로고
    • Structure of the human histamine H1 receptor complex with doxepin
    • Shimamura T, Shiroishi M, Weyand S, et al. Structure of the human histamine H1 receptor complex with doxepin. Nature 2011;475:65-70
    • (2011) Nature , vol.475 , pp. 65-70
    • Shimamura, T.1    Shiroishi, M.2    Weyand, S.3
  • 131
    • 84857254248 scopus 로고    scopus 로고
    • Crystal structure of a lipid G protein-coupled receptor
    • Hanson MA, Roth CB, Jo E, et al. Crystal structure of a lipid G protein-coupled receptor. Science 2012;335:851-5
    • (2012) Science , vol.335 , pp. 851-855
    • Ma, H.1    Roth, C.B.2    Jo, E.3
  • 132
    • 84863115467 scopus 로고    scopus 로고
    • Structure and dynamics of the M3 muscarinic acetylcholine receptor
    • Kruse AC, Hu J, Pan AC, et al. Structure and dynamics of the M3 muscarinic acetylcholine receptor. Nature 2012;482:552-6
    • (2012) Nature , vol.482 , pp. 552-556
    • Kruse, A.C.1    Hu, J.2    Pan, A.C.3
  • 133
    • 84862777405 scopus 로고    scopus 로고
    • Structure of the human M2 muscarinic acetylcholine receptor bound to an antagonist
    • Haga K, Kruse AC, Asada H, et al. Structure of the human M2 muscarinic acetylcholine receptor bound to an antagonist. Nature 2012;482:547-51
    • (2012) Nature , vol.482 , pp. 547-551
    • Haga, K.1    Kruse, A.C.2    Asada, H.3
  • 134
    • 84862777742 scopus 로고    scopus 로고
    • Structure of the human k-opioid receptor in complex with JDTic
    • Wu H, Wacker D, Mileni M, et al. Structure of the human k-opioid receptor in complex with JDTic. Nature 2012;485:327-32
    • (2012) Nature , vol.485 , pp. 327-332
    • Wu, H.1    Wacker, D.2    Mileni, M.3
  • 135
    • 84861096654 scopus 로고    scopus 로고
    • Crystal structure of the μ-opioid receptor bound to a morphine antagonist
    • Manglik A, Kruse AC, Kobilka TS, et al. Crystal structure of the μ-opioid receptor bound to a morphine antagonist. Nature 2012;485:321-6
    • (2012) Nature , vol.485 , pp. 321-326
    • Manglik, A.1    Kruse, A.C.2    Kobilka, T.S.3
  • 136
    • 84861019261 scopus 로고    scopus 로고
    • Structure of the nociceptin/orphanin FQ receptor in complex with a peptide mimetic
    • Thompson AA, Liu W, Chun E, et al. Structure of the nociceptin/orphanin FQ receptor in complex with a peptide mimetic. Nature 2012;485:395-9
    • (2012) Nature , vol.485 , pp. 395-399
    • Thompson, A.A.1    Liu, W.2    Chun, E.3
  • 137
    • 84861075468 scopus 로고    scopus 로고
    • Structure of the d-opioid receptor bound to naltrindole
    • Granier S, Manglik A, Kruse AC, et al. Structure of the d-opioid receptor bound to naltrindole. Nature 2012;485:400-4
    • (2012) Nature , vol.485 , pp. 400-404
    • Granier, S.1    Manglik, A.2    Kruse, A.C.3
  • 138
    • 80051658642 scopus 로고    scopus 로고
    • Crystal structure of the b2 adrenergic receptor-Gs protein complex
    • Rasmussen SG, DeVree BT, Zou Y, et al. Crystal structure of the b2 adrenergic receptor-Gs protein complex. Nature 2011;477:549-55
    • (2011) Nature , vol.477 , pp. 549-555
    • Rasmussen, S.G.1    Devree, B.T.2    Zou, Y.3
  • 139
    • 77952050479 scopus 로고    scopus 로고
    • Structure-based discovery of A2A adenosine receptor ligands
    • Carlsson J, Yoo L, Gao ZG, et al. Structure-based discovery of A2A adenosine receptor ligands. J Med Chem 2010;53:3748-55
    • (2010) J Med Chem , vol.53 , pp. 3748-3755
    • Carlsson, J.1    Yoo, L.2    Gao, Z.G.3
  • 140
    • 80054868459 scopus 로고    scopus 로고
    • Ligand discovery from a dopamine D3 receptor homology model and crystal structure
    • Carlsson J, Coleman RG, Setola V, et al. Ligand discovery from a dopamine D3 receptor homology model and crystal structure. Nat Chem Biol 2011;7:769-78
    • (2011) Nat Chem Biol , vol.7 , pp. 769-778
    • Carlsson, J.1    Coleman, R.G.2    Setola, V.3
  • 141
    • 84859460667 scopus 로고    scopus 로고
    • Structure-based ligand discovery for the protein-protein interface of chemokine receptor CXCR4
    • Mysinger MM, Weiss DR, Ziarek JJ, et al. Structure-based ligand discovery for the protein-protein interface of chemokine receptor CXCR4. Proc Natl Acad Sci USA 2012;109:5517-22
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 5517-5522
    • Mysinger, M.M.1    Weiss, D.R.2    Ziarek, J.J.3
  • 142
    • 85126151667 scopus 로고    scopus 로고
    • Surface generated acoustic wave biosensors for the detection of pathogens: A review
    • Rocha-Gaso MI, March-Iborra C, Montoya-Baides A, Arnau-Vives A. Surface generated acoustic wave biosensors for the detection of pathogens: a review. Sensors 2009;9:5740-69
    • (2009) Sensors , vol.9 , pp. 5740-5769
    • Rocha-Gaso, M.I.1    March-Iborra, C.2    Montoya-Baides, A.3    Arnau-Vives, A.4
  • 143
    • 45849085364 scopus 로고    scopus 로고
    • Surface acoustic wave biosensors: A review
    • Länge K, Rapp BE, Rapp M. Surface acoustic wave biosensors: a review. Anal Bioanal Chem 2008;391:1509-19
    • (2008) Anal Bioanal Chem , vol.391 , pp. 1509-1519
    • Länge, K.1    Rapp, B.E.2    Rapp, M.3
  • 144
    • 22544463110 scopus 로고    scopus 로고
    • Probing cytoskeleton modulation by optical biosensors
    • Fang Y, Ferrie AM, Li G. Probing cytoskeleton modulation by optical biosensors. FEBS Lett 2005;579:4175-80
    • (2005) FEBS Lett , vol.579 , pp. 4175-4180
    • Fang, Y.1    Ferrie, A.M.2    Li, G.3
  • 145
    • 24644496122 scopus 로고    scopus 로고
    • Characteristics of dynamic mass redistribution of EGF receptor signaling in living cells measured with label free optical biosensors
    • Fang Y, Ferrie AM, Fontaine NH, Yuen PK. Characteristics of dynamic mass redistribution of EGF receptor signaling in living cells measured with label free optical biosensors. Anal Chem 2005;77:5720-5
    • (2005) Anal Chem , vol.77 , pp. 5720-5725
    • Fang, Y.1    Ferrie, A.M.2    Fontaine, N.H.3    Yuen, P.K.4
  • 146
    • 27744501166 scopus 로고    scopus 로고
    • Optical biosensor provides insights for bradykinin B2 receptor signaling in A431 cells
    • Fang Y, Li G, Peng J. Optical biosensor provides insights for bradykinin B2 receptor signaling in A431 cells. FEBS Lett 2005;579:6365-74
    • (2005) FEBS Lett , vol.579 , pp. 6365-6374
    • Fang, Y.1    Li, G.2    Peng, J.3
  • 147
    • 33748469378 scopus 로고    scopus 로고
    • Resonant waveguide grating biosensor for living cell sensing
    • Fang Y, Ferrie AM, Fontaine NH, et al. Resonant waveguide grating biosensor for living cell sensing. Biophys J 2006;91:1925-40
    • (2006) Biophys J , vol.91 , pp. 1925-1940
    • Fang, Y.1    Ferrie, A.M.2    Fontaine, N.H.3
  • 148
    • 33947217218 scopus 로고    scopus 로고
    • Non-invasive optical biosensor for assaying endogenous G protein-coupled receptors in adherent cells
    • Fang Y, Li G, Ferrie AM. Non-invasive optical biosensor for assaying endogenous G protein-coupled receptors in adherent cells. J Pharamcol Toxicol Methods 2007;55:314-22
    • (2007) J Pharamcol Toxicol Methods , vol.55 , pp. 314-322
    • Fang, Y.1    Li, G.2    Ferrie, A.M.3
  • 149
    • 39649108870 scopus 로고    scopus 로고
    • Label-free optical biosensor for ligand-directed functional selectivity of acting on b2 adrenoceptor in living cells
    • Fang Y, Ferrie AM. Label-free optical biosensor for ligand-directed functional selectivity of acting on b2 adrenoceptor in living cells. FEBS Lett 2008;582:558-64
    • (2008) FEBS Lett , vol.582 , pp. 558-564
    • Fang, Y.1    Ferrie, A.M.2
  • 150
    • 79958142575 scopus 로고    scopus 로고
    • Tyrphostin analogs are GPR35 agonists
    • Deng H, Hu H, Fang Y. Tyrphostin analogs are GPR35 agonists. FEBS Lett 2011;585:1957-62
    • (2011) FEBS Lett , vol.585 , pp. 1957-1962
    • Deng, H.1    Hu, H.2    Fang, Y.3
  • 151
    • 81355148507 scopus 로고    scopus 로고
    • GPCRs regulate the assembly of a multienzyme complex for purine biosynthesis
    • Verrier F, An S, Ferrie AM, et al. GPCRs regulate the assembly of a multienzyme complex for purine biosynthesis. Nat Chem Biol 2011;7:909-15
    • (2011) Nat Chem Biol , vol.7 , pp. 909-915
    • Verrier, F.1    An, S.2    Ferrie, A.M.3
  • 153
    • 83455169708 scopus 로고    scopus 로고
    • The development of label-free cellular assays for drug discovery
    • Fang Y. The development of label-free cellular assays for drug discovery. Expert Opin Drug Discov 2011;6:1285-98
    • (2011) Expert Opin Drug Discov , vol.6 , pp. 1285-1298
    • Fang, Y.1
  • 154
    • 59449089513 scopus 로고    scopus 로고
    • The C-terminal tail of CRTH2 is a key molecular determinant that constrains Gi- and downstream-signaling cascade activation
    • Schroeder R, Merten N, Mathiesen JM, et al. The C-terminal tail of CRTH2 is a key molecular determinant that constrains Gi- and downstream-signaling cascade activation. J Biol Chem 2009;284:1324-36
    • (2009) J Biol Chem , vol.284 , pp. 1324-1336
    • Schroeder, R.1    Merten, N.2    Mathiesen, J.M.3
  • 155
    • 70349775115 scopus 로고    scopus 로고
    • Real-time quantitation of viral replication and inhibitor potency using a label-free optical biosensor
    • Owens RM, Wang C, You JA, et al. Real-time quantitation of viral replication and inhibitor potency using a label-free optical biosensor. J Recept Signal Transduct Res 2009;29:195-201
    • (2009) J Recept Signal Transduct Res , vol.29 , pp. 195-201
    • Owens, R.M.1    Wang, C.2    You, J.A.3
  • 156
    • 70349781296 scopus 로고    scopus 로고
    • An optical dynamic mass redistribution assay reveals biased signaling of dualsteric GPCR activators
    • Kebig A, Kostenis E, Mohr K, Mohr-Andr M. An optical dynamic mass redistribution assay reveals biased signaling of dualsteric GPCR activators. J Recept Signal Transduct Res 2009;29:140-5
    • (2009) J Recept Signal Transduct Res , vol.29 , pp. 140-145
    • Kebig, A.1    Kostenis, E.2    Mohr, K.3    Mohr-Andr, M.4
  • 157
    • 77956657852 scopus 로고    scopus 로고
    • Deconvolution of complex G protein-coupled receptor signaling in live cells using dynamic mass redistribution measurements
    • Schröder R, Janssen N, Schmidt J, et al. Deconvolution of complex G protein-coupled receptor signaling in live cells using dynamic mass redistribution measurements. Nat Biotechnol 2010;28:943-9
    • (2010) Nat Biotechnol , vol.28 , pp. 943-949
    • Schröder, R.1    Janssen, N.2    Schmidt, J.3
  • 158
    • 84860389995 scopus 로고    scopus 로고
    • Dynamic mass redistribution as a means to measure and differentiate signaling via opioid and cannabinoid receptors
    • Codd EE, Mabus JR, Murray BS, et al. Dynamic mass redistribution as a means to measure and differentiate signaling via opioid and cannabinoid receptors. Assay Drug Dev Technol 2011;9:362-72
    • (2011) Assay Drug Dev Technol , vol.9 , pp. 362-372
    • Codd, E.E.1    Mabus, J.R.2    Murray, B.S.3
  • 159
    • 84862214350 scopus 로고    scopus 로고
    • Development of a label-free assay for sodium-dependent phosphate transporter NaPi-IIb
    • Wong SH, Gao A, Ward S, et al. Development of a label-free assay for sodium-dependent phosphate transporter NaPi-IIb. J Biomol Screen 2012;17:829-34
    • (2012) J Biomol Screen , vol.17 , pp. 829-834
    • Wong, S.H.1    Gao, A.2    Ward, S.3
  • 160
    • 84859949278 scopus 로고    scopus 로고
    • Differential signaling by splice variants of the human free fatty acid receptor GPR120
    • Watson SJ, Brown AJ, Holliday ND. Differential signaling by splice variants of the human free fatty acid receptor GPR120. Mol Pharmacol 2012;81:631-42
    • (2012) Mol Pharmacol , vol.81 , pp. 631-642
    • Watson, S.J.1    Brown, A.J.2    Holliday, N.D.3
  • 161
    • 84863414075 scopus 로고    scopus 로고
    • Dynamic mass redistribution assays decodes surface influence on signaling of endogenous purinergic receptors
    • Tran E, Sun H, Fang Y. Dynamic mass redistribution assays decodes surface influence on signaling of endogenous purinergic receptors. Assays Drug Dev Technol 2012;10:37-45
    • (2012) Assays Drug Dev Technol , vol.10 , pp. 37-45
    • Tran, E.1    Sun, H.2    Fang, Y.3
  • 162
    • 79955631465 scopus 로고    scopus 로고
    • Agonist-directed desensitization of the b2-adrenergic receptor
    • Goral V, Jin Y, Sun H, et al. Agonist-directed desensitization of the b2-adrenergic receptor. PLoS One 2011;6:e19282
    • (2011) PLoS One , vol.6
    • Goral, V.1    Jin, Y.2    Sun, H.3
  • 163
    • 79953235353 scopus 로고    scopus 로고
    • Label-free optical biosensor with microfluidics for sensing ligand-directed functional selectivity on trafficking of thrombin receptor
    • Goral V, Wu Q, Sun H, Fang Y. Label-free optical biosensor with microfluidics for sensing ligand-directed functional selectivity on trafficking of thrombin receptor. FEBS Lett 2011;585:1054-60
    • (2011) FEBS Lett , vol.585 , pp. 1054-1060
    • Goral, V.1    Wu, Q.2    Sun, H.3    Fang, Y.4
  • 164
    • 79955397068 scopus 로고    scopus 로고
    • Microfluidic resonant waveguide grating biosensor system for whole cell sensing
    • Zaytseva N, Miller W, Goral V, et al. Microfluidic resonant waveguide grating biosensor system for whole cell sensing. Appl Phys Lett 2011;96:163703
    • (2011) Appl Phys Lett , vol.96 , pp. 163703
    • Zaytseva, N.1    Miller, W.2    Goral, V.3
  • 165
    • 78650667671 scopus 로고    scopus 로고
    • Resonant waveguide grating imager for live cell sensing
    • Ferrie AM, Wu Q, Fang Y. Resonant waveguide grating imager for live cell sensing. Appl Phys Lett 2010;97:223704
    • (2010) Appl Phys Lett , vol.97 , pp. 223704
    • Ferrie, A.M.1    Wu, Q.2    Fang, Y.3
  • 166
    • 84862115332 scopus 로고    scopus 로고
    • High resolution resonant waveguide grating imager for cell cluster analysis under physiological condition
    • Ferrie AM, Deichmann OD, Wu Q, Fang Y. High resolution resonant waveguide grating imager for cell cluster analysis under physiological condition. Appl Phys Lett 2012;100:223701
    • (2012) Appl Phys Lett , vol.100 , pp. 223701
    • Ferrie, A.M.1    Deichmann, O.D.2    Wu, Q.3    Fang, Y.4
  • 167
    • 84858034356 scopus 로고    scopus 로고
    • Discovery of 1,2,4-triazine derivatives as adenosine A2A antagonists using structure based drug design
    • Congreve M, Andrews SP, Doré AS, et al. Discovery of 1,2,4-triazine derivatives as adenosine A2A antagonists using structure based drug design. J Med Chem 2012;55:1898-903
    • (2012) J Med Chem , vol.55 , pp. 1898-1903
    • Congreve, M.1    Andrews, S.P.2    Doré, A.S.3
  • 168
    • 79956024496 scopus 로고    scopus 로고
    • Learning lessons from drugs that have recently entered the market
    • Teague SJ. Learning lessons from drugs that have recently entered the market. Drug Discov Today 2011;16:398-411
    • (2011) Drug Discov Today , vol.16 , pp. 398-411
    • Teague, S.J.1
  • 169
    • 84859388604 scopus 로고    scopus 로고
    • Investigation of the effect of molecular properties on the binding kinetics of a ligand to its biological target
    • Miller DC, Lunn G, Jones P, et al. Investigation of the effect of molecular properties on the binding kinetics of a ligand to its biological target. Med Chem Commun 2012;3:449-52
    • (2012) Med Chem Commun , vol.3 , pp. 449-452
    • Miller, D.C.1    Lunn, G.2    Jones, P.3
  • 171
    • 0347361638 scopus 로고    scopus 로고
    • Characteristic physical properties and structural fragments of marketed oral drugs
    • Vieth M, Siegel MG, Higgs RE, et al. Characteristic physical properties and structural fragments of marketed oral drugs. J Med Chem 2004;47:224-32
    • (2004) J Med Chem , vol.47 , pp. 224-232
    • Vieth, M.1    Siegel, M.G.2    Higgs, R.E.3
  • 173
    • 84859268097 scopus 로고    scopus 로고
    • Can biochemistry drive drug discovery beyond simple potency measurements?
    • Chene P. Can biochemistry drive drug discovery beyond simple potency measurements? Drug Discov Today 2012;17:388-95
    • (2012) Drug Discov Today , vol.17 , pp. 388-395
    • Chene, P.1
  • 174
    • 79961007102 scopus 로고    scopus 로고
    • The need for high throughput kinetics early in the drug discovery process
    • Keighley W. The need for high throughput kinetics early in the drug discovery process. Drug Discov World 2011;12(3):39-45
    • (2011) Drug Discov World , vol.12 , Issue.3 , pp. 39-45
    • Keighley, W.1
  • 175
    • 54249155522 scopus 로고    scopus 로고
    • Network pharmacology: The next paradigm in drug discovery
    • Hopkins AL. Network pharmacology: the next paradigm in drug discovery. Nat Chem Biol 2008;4:682-90
    • (2008) Nat Chem Biol , vol.4 , pp. 682-690
    • Hopkins, A.L.1
  • 176
    • 47249146126 scopus 로고    scopus 로고
    • Drug target identification using side-effect similarity
    • Campillos M, Kuhn M, Gavin AC, et al. Drug target identification using side-effect similarity. Science 2008;321:263-6
    • (2008) Science , vol.321 , pp. 263-266
    • Campillos, M.1    Kuhn, M.2    Gavin, A.C.3
  • 177
    • 70449634957 scopus 로고    scopus 로고
    • Predicting new molecular targets for known drugs
    • Keiser MJ, Setola V, Irwin JJ, et al. Predicting new molecular targets for known drugs. Nature 2009;462:175-81
    • (2009) Nature , vol.462 , pp. 175-181
    • Keiser, M.J.1    Setola, V.2    Irwin, J.J.3
  • 178
    • 77956040404 scopus 로고    scopus 로고
    • Predicting polypharmacology by binding site similarity: From kinetics to the protein universe
    • Milletti F, Vulpetti A. Predicting polypharmacology by binding site similarity: from kinetics to the protein universe. J Chem Inf Model 2010;50:1418-31
    • (2010) J Chem Inf Model , vol.50 , pp. 1418-1431
    • Milletti, F.1    Vulpetti, A.2
  • 179
    • 12244275244 scopus 로고    scopus 로고
    • Biological spectra analysis: Linking biological activity profiles to molecular structures
    • Fliri AF, Loging WT, Thadeio PF, Volkmann RA. Biological spectra analysis: linking biological activity profiles to molecular structures. Proc Natl Acad Sci USA 2005;102:261-6
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 261-266
    • Fliri, A.F.1    Loging, W.T.2    Thadeio, P.F.3    Volkmann, R.A.4
  • 180
    • 80755125565 scopus 로고    scopus 로고
    • Comprehensive assay of kinase catalytic activity reveals features of kinase inhibitor selectivity
    • Anastassiadis T, Deacon SW, Devarajan K, et al. Comprehensive assay of kinase catalytic activity reveals features of kinase inhibitor selectivity. Nat Biotechnol 2011;29:1039-45
    • (2011) Nat Biotechnol , vol.29 , pp. 1039-1045
    • Anastassiadis, T.1    Deacon, S.W.2    Devarajan, K.3
  • 181
    • 80755125575 scopus 로고    scopus 로고
    • Comprehensive analysis of kinase inhibitor selectivity
    • Davis MI, Hunt JP, Herrgard S, et al. Comprehensive analysis of kinase inhibitor selectivity. Nat Biotechnol 2011;29:1046-51
    • (2011) Nat Biotechnol , vol.29 , pp. 1046-1051
    • Davis, M.I.1    Hunt, J.P.2    Herrgard, S.3
  • 182
    • 54249162351 scopus 로고    scopus 로고
    • Targeted polypharmacology: Discovery of dual inhibitors of tyrosine and phosphoinositide kinases
    • Apsel B, Blair JA, Gonzalez B, et al. Targeted polypharmacology: discovery of dual inhibitors of tyrosine and phosphoinositide kinases. Nat Chem Biol 2008;4:691-9
    • (2008) Nat Chem Biol , vol.4 , pp. 691-699
    • Apsel, B.1    Blair, J.A.2    Gonzalez, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.