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Volumn 6, Issue , 2016, Pages

Function-specific virtual screening for GPCR ligands using a combined scoring method

Author keywords

[No Author keywords available]

Indexed keywords

BETA ADRENERGIC RECEPTOR; BETA ADRENERGIC RECEPTOR BLOCKING AGENT; BETA ADRENERGIC RECEPTOR STIMULATING AGENT; G PROTEIN COUPLED RECEPTOR; HISTAMINE AGONIST; HISTAMINE H1 RECEPTOR; HISTAMINE H1 RECEPTOR ANTAGONIST; LIGAND; PROTEIN BINDING; RECOMBINANT PROTEIN;

EID: 84975721733     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep28288     Document Type: Article
Times cited : (79)

References (69)
  • 1
  • 2
    • 84939818422 scopus 로고    scopus 로고
    • A molecular pharmacologist's guide to G protein-coupled receptor crystallography
    • Piscitelli, C. L., Kean, J., de Graaf, C. & Deupi, X. A Molecular Pharmacologist's Guide to G Protein-Coupled Receptor Crystallography. Mol. Pharmacol. 88, 536-551 (2015).
    • (2015) Mol. Pharmacol. , vol.88 , pp. 536-551
    • Piscitelli, C.L.1    Kean, J.2    De Graaf, C.3    Deupi, X.4
  • 3
    • 84892401045 scopus 로고    scopus 로고
    • Structure-based drug design for g protein-coupled receptors
    • Congreve, M., Dias, J. M. & Marshall, F. H. Structure-based drug design for g protein-coupled receptors. Prog. Med. Chem. 53, 1-63 (2014).
    • (2014) Prog. Med. Chem. , vol.53 , pp. 1-63
    • Congreve, M.1    Dias, J.M.2    Marshall, F.H.3
  • 4
    • 84942133514 scopus 로고    scopus 로고
    • Discovery of GPCR ligands by molecular docking screening: Novel opportunities provided by crystal structures
    • Rodriguez, D., Ranganathan, A. & Carlsson, J. Discovery of GPCR Ligands by Molecular Docking Screening: Novel Opportunities Provided by Crystal Structures. Curr. Top. Med. Chem. 15, 2484-2503 (2015).
    • (2015) Curr. Top. Med. Chem. , vol.15 , pp. 2484-2503
    • Rodriguez, D.1    Ranganathan, A.2    Carlsson, J.3
  • 5
    • 84860513814 scopus 로고    scopus 로고
    • Structure-based drug screening for G-protein-coupled receptors
    • Shoichet, B. K. & Kobilka, B. K. Structure-based drug screening for G-protein-coupled receptors. Trends Pharmacol. Sci. 33, 268-272 (2012).
    • (2012) Trends Pharmacol. Sci. , vol.33 , pp. 268-272
    • Shoichet, B.K.1    Kobilka, B.K.2
  • 6
    • 84934441026 scopus 로고    scopus 로고
    • From three-dimensional GPCR structure to rational ligand discovery
    • Kooistra, A. J., Leurs, R., de Esch, I. J. & de Graaf, C. From three-dimensional GPCR structure to rational ligand discovery. Adv. Exp. Med. Biol. 796, 129-157 (2014).
    • (2014) Adv. Exp. Med. Biol. , vol.796 , pp. 129-157
    • Kooistra, A.J.1    Leurs, R.2    De Esch, I.J.3    De Graaf, C.4
  • 7
    • 84895811180 scopus 로고    scopus 로고
    • Virtual fragment screening on GPCRs: A case study on dopamine D3 and histamine H4 receptors
    • Vass, M., Schmidt, E., Horti, F. & Keseru, G. M. Virtual fragment screening on GPCRs: a case study on dopamine D3 and histamine H4 receptors. Eur. J. Med. Chem. 77, 38-46 (2014).
    • (2014) Eur. J. Med. Chem. , vol.77 , pp. 38-46
    • Vass, M.1    Schmidt, E.2    Horti, F.3    Keseru, G.M.4
  • 8
    • 67650239912 scopus 로고    scopus 로고
    • Analysis of full and partial agonists binding to beta2-adrenergic receptor suggests a role of transmembrane helix v in agonist-specific conformational changes
    • Katritch, V. et al. Analysis of full and partial agonists binding to beta2-adrenergic receptor suggests a role of transmembrane helix V in agonist-specific conformational changes. J. Mol. Recognit. 22, 307-318 (2009).
    • (2009) J. Mol. Recognit. , vol.22 , pp. 307-318
    • Katritch, V.1
  • 9
    • 84961177760 scopus 로고    scopus 로고
    • Single-molecule view of basal activity and activation mechanisms of the G protein-coupled receptor beta2AR
    • Lamichhane, R. et al. Single-molecule view of basal activity and activation mechanisms of the G protein-coupled receptor beta2AR. Proc. Natl. Acad. Sci. USA 112, 14254-14259 (2015).
    • (2015) Proc. Natl. Acad. Sci. USA , vol.112 , pp. 14254-14259
    • Lamichhane, R.1
  • 11
    • 79961241154 scopus 로고    scopus 로고
    • Docking performance of fragments and druglike compounds
    • Verdonk, M. L. et al. Docking performance of fragments and druglike compounds. J. Med. Chem. 54, 5422-5431 (2011).
    • (2011) J. Med. Chem. , vol.54 , pp. 5422-5431
    • Verdonk, M.L.1
  • 12
    • 84925392495 scopus 로고    scopus 로고
    • Molecular docking screening using agonist-bound GPCR structures: Probing the A2A adenosine receptor
    • Rodriguez, D., Gao, Z. G., Moss, S. M., Jacobson, K. A. & Carlsson, J. Molecular docking screening using agonist-bound GPCR structures: Probing the A2A adenosine receptor. J. Chem. Inf. Model. 55, 550-563 (2015).
    • (2015) J. Chem. Inf. Model , vol.55 , pp. 550-563
    • Rodriguez, D.1    Gao, Z.G.2    Moss, S.M.3    Jacobson, K.A.4    Carlsson, J.5
  • 13
    • 84875807317 scopus 로고    scopus 로고
    • Conformation guides molecular efficacy in docking screens of activated beta-2 adrenergic G protein coupled receptor
    • Weiss, D. R. et al. Conformation guides molecular efficacy in docking screens of activated beta-2 adrenergic G protein coupled receptor. ACS Chem. Biol. 8, 1018-1026 (2013).
    • (2013) ACS Chem. Biol. , vol.8 , pp. 1018-1026
    • Weiss, D.R.1
  • 14
    • 69549118627 scopus 로고    scopus 로고
    • Testing assumptions and hypotheses for rescoring success in protein-ligand docking
    • O'Boyle, N. M., Liebeschuetz, J. W. & Cole, J. C. Testing assumptions and hypotheses for rescoring success in protein-ligand docking. J. Chem. Inf. Model. 49, 1871-1878 (2009).
    • (2009) J. Chem. Inf. Model , vol.49 , pp. 1871-1878
    • O'Boyle, N.M.1    Liebeschuetz, J.W.2    Cole, J.C.3
  • 15
    • 84858053438 scopus 로고    scopus 로고
    • Virtual screening data fusion using both structure- and ligand-based methods
    • Svensson, F., Karlen, A. & Skold, C. Virtual screening data fusion using both structure- and ligand-based methods. J. Chem. Inf. Model. 52, 225-232 (2012).
    • (2012) J. Chem. Inf. Model , vol.52 , pp. 225-232
    • Svensson, F.1    Karlen, A.2    Skold, C.3
  • 16
    • 84862291381 scopus 로고    scopus 로고
    • A prospective cross-screening study on G-protein-coupled receptors: Lessons learned in virtual compound library design
    • Sanders, M. P. et al. A prospective cross-screening study on G-protein-coupled receptors: lessons learned in virtual compound library design. J. Med. Chem. 55, 5311-5325 (2012).
    • (2012) J. Med. Chem. , vol.55 , pp. 5311-5325
    • Sanders, M.P.1
  • 17
    • 0141992809 scopus 로고    scopus 로고
    • Molecular modeling of the three-dimensional structure of dopamine 3 (D3) subtype receptor: Discovery of novel and potent D3 ligands through a hybrid pharmacophore- and structure-based database searching approach
    • Varady, J. et al. Molecular modeling of the three-dimensional structure of dopamine 3 (D3) subtype receptor: discovery of novel and potent D3 ligands through a hybrid pharmacophore- and structure-based database searching approach. J. Med. Chem. 46, 4377-4392 (2003).
    • (2003) J. Med. Chem. , vol.46 , pp. 4377-4392
    • Varady, J.1
  • 18
    • 84905020680 scopus 로고    scopus 로고
    • Consensus scoring approach to identify the inhibitors of AMP-activated protein kinase alpha2 with virtual screening
    • Park, H., Eom, J. W. & Kim, Y. H. Consensus scoring approach to identify the inhibitors of AMP-activated protein kinase alpha2 with virtual screening. J. Chem. Inf. Model. 54, 2139-2146 (2014).
    • (2014) J. Chem. Inf. Model , vol.54 , pp. 2139-2146
    • Park, H.1    Eom, J.W.2    Kim, Y.H.3
  • 19
    • 62449330667 scopus 로고    scopus 로고
    • Empirical scoring functions for advanced protein-ligand docking with PLANTS
    • Korb, O., Stutzle, T. & Exner, T. E. Empirical scoring functions for advanced protein-ligand docking with PLANTS. J. Chem. Inf. Model. 49, 84-96 (2009).
    • (2009) J. Chem. Inf. Model , vol.49 , pp. 84-96
    • Korb, O.1    Stutzle, T.2    Exner, T.E.3
  • 20
    • 33846933784 scopus 로고    scopus 로고
    • Optimizing fragment and scaffold docking by use of molecular interaction fingerprints
    • Marcou, G. & Rognan, D. Optimizing fragment and scaffold docking by use of molecular interaction fingerprints. J. Chem. Inf. Model. 47, 195-207 (2007).
    • (2007) J. Chem. Inf. Model , vol.47 , pp. 195-207
    • Marcou, G.1    Rognan, D.2
  • 21
    • 82555187387 scopus 로고    scopus 로고
    • Crystal structure-based virtual screening for fragment-like ligands of the human histamine H(1) receptor
    • de Graaf, C. et al. Crystal structure-based virtual screening for fragment-like ligands of the human histamine H(1) receptor. J. Med. Chem. 54, 8195-8206 (2011).
    • (2011) J. Med. Chem. , vol.54 , pp. 8195-8206
    • De Graaf, C.1
  • 22
    • 84930227130 scopus 로고    scopus 로고
    • Structure-based prediction of G-protein-coupled receptor ligand function: A β -adrenoceptor case study
    • Kooistra, A. J., Leurs, R., de Esch, I. J. & de Graaf, C. Structure-Based Prediction of G-Protein-Coupled Receptor Ligand Function: A β -Adrenoceptor Case Study. J. Chem. Inf. Model. 55, 1045-1061 (2015).
    • (2015) J. Chem. Inf. Model , vol.55 , pp. 1045-1061
    • Kooistra, A.J.1    Leurs, R.2    De Esch, I.J.3    De Graaf, C.4
  • 23
    • 79960070651 scopus 로고    scopus 로고
    • Structure of the human histamine H1 receptor complex with doxepin
    • Shimamura, T. et al. Structure of the human histamine H1 receptor complex with doxepin. Nature 475, 65-70 (2011).
    • (2011) Nature , vol.475 , pp. 65-70
    • Shimamura, T.1
  • 24
    • 77952772341 scopus 로고    scopus 로고
    • Extended-connectivity fingerprints
    • Rogers, D. & Hahn, M. Extended-connectivity fingerprints. J. Chem. Inf. Model. 50, 742-754 (2010).
    • (2010) J. Chem. Inf. Model , vol.50 , pp. 742-754
    • Rogers, D.1    Hahn, M.2
  • 25
    • 50249156843 scopus 로고    scopus 로고
    • Selective structure-based virtual screening for full and partial agonists of the beta2 adrenergic receptor
    • de Graaf, C. & Rognan, D. Selective structure-based virtual screening for full and partial agonists of the beta2 adrenergic receptor. J. Med. Chem. 51, 4978-4985 (2008).
    • (2008) J. Med. Chem. , vol.51 , pp. 4978-4985
    • De Graaf, C.1    Rognan, D.2
  • 26
    • 36448995359 scopus 로고    scopus 로고
    • High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor
    • Cherezov, V. et al. High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor. Science 318, 1258-1265 (2007).
    • (2007) Science , vol.318 , pp. 1258-1265
    • Cherezov, V.1
  • 27
    • 36248970132 scopus 로고    scopus 로고
    • Crystal structure of the human beta2 adrenergic G-protein-coupled receptor
    • Rasmussen, S. G. et al. Crystal structure of the human beta2 adrenergic G-protein-coupled receptor. Nature 450, 383-387 (2007).
    • (2007) Nature , vol.450 , pp. 383-387
    • Rasmussen, S.G.1
  • 28
    • 44649172481 scopus 로고    scopus 로고
    • A specific cholesterol binding site is established by the 2.8 A structure of the human beta2-adrenergic receptor
    • Hanson, M. A. et al. A specific cholesterol binding site is established by the 2.8 A structure of the human beta2-adrenergic receptor. Structure 16, 897-905 (2008).
    • (2008) Structure , vol.16 , pp. 897-905
    • Hanson, M.A.1
  • 29
    • 47949129742 scopus 로고    scopus 로고
    • Structure of a beta1-adrenergic G-protein-coupled receptor
    • Warne, T. et al. Structure of a beta1-adrenergic G-protein-coupled receptor. Nature 454, 486-491 (2008).
    • (2008) Nature , vol.454 , pp. 486-491
    • Warne, T.1
  • 30
    • 73849149844 scopus 로고    scopus 로고
    • Ligand-specific regulation of the extracellular surface of a G-protein-coupled receptor
    • Bokoch, M. P. et al. Ligand-specific regulation of the extracellular surface of a G-protein-coupled receptor. Nature 463, 108-112 (2010).
    • (2010) Nature , vol.463 , pp. 108-112
    • Bokoch, M.P.1
  • 31
    • 77955779227 scopus 로고    scopus 로고
    • Conserved binding mode of human beta2 adrenergic receptor inverse agonists and antagonist revealed by X-ray crystallography
    • Wacker, D. et al. Conserved binding mode of human beta2 adrenergic receptor inverse agonists and antagonist revealed by X-ray crystallography. J. Am. Chem. Soc. 132, 11443-11445 (2010).
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 11443-11445
    • Wacker, D.1
  • 32
    • 78651411166 scopus 로고    scopus 로고
    • Structure of a nanobody-stabilized active state of the beta(2) adrenoceptor
    • Rasmussen, S. G. et al. Structure of a nanobody-stabilized active state of the beta(2) adrenoceptor. Nature 469, 175-180 (2011).
    • (2011) Nature , vol.469 , pp. 175-180
    • Rasmussen, S.G.1
  • 33
    • 78651399683 scopus 로고    scopus 로고
    • Structure and function of an irreversible agonist-beta(2) adrenoceptor complex
    • Rosenbaum, D. M. et al. Structure and function of an irreversible agonist-beta(2) adrenoceptor complex. Nature 469, 236-240 (2011).
    • (2011) Nature , vol.469 , pp. 236-240
    • Rosenbaum, D.M.1
  • 34
    • 78651405537 scopus 로고    scopus 로고
    • The structural basis for agonist and partial agonist action on a beta(1)-adrenergic receptor
    • Warne, T. et al. The structural basis for agonist and partial agonist action on a beta(1)-adrenergic receptor. Nature 469, 241-244 (2011).
    • (2011) Nature , vol.469 , pp. 241-244
    • Warne, T.1
  • 35
    • 84881652938 scopus 로고    scopus 로고
    • A structural chemogenomics analysis of aminergic GPCRs: Lessons for histamine receptor ligand design
    • Kooistra, A. J., Kuhne, S., de Esch, I. J., Leurs, R. & de Graaf, C. A structural chemogenomics analysis of aminergic GPCRs: lessons for histamine receptor ligand design. Br. J. Pharmacol. 170, 101-126 (2013).
    • (2013) Br. J. Pharmacol. , vol.170 , pp. 101-126
    • Kooistra, A.J.1    Kuhne, S.2    De Esch, I.J.3    Leurs, R.4    De Graaf, C.5
  • 36
    • 4544367743 scopus 로고    scopus 로고
    • Comparative evaluation of eight docking tools for docking and virtual screening accuracy
    • Kellenberger, E., Rodrigo, J., Muller, P. & Rognan, D. Comparative evaluation of eight docking tools for docking and virtual screening accuracy. Proteins 57, 225-242 (2004).
    • (2004) Proteins , vol.57 , pp. 225-242
    • Kellenberger, E.1    Rodrigo, J.2    Muller, P.3    Rognan, D.4
  • 37
    • 84875151295 scopus 로고    scopus 로고
    • Discovery of novel Trypanosoma brucei phosphodiesterase B1 inhibitors by virtual screening against the unliganded TbrPDEB1 crystal structure
    • Jansen, C. et al. Discovery of novel Trypanosoma brucei phosphodiesterase B1 inhibitors by virtual screening against the unliganded TbrPDEB1 crystal structure. J. Med. Chem. 56, 2087-2096 (2013).
    • (2013) J. Med. Chem. , vol.56 , pp. 2087-2096
    • Jansen, C.1
  • 38
    • 84859881146 scopus 로고    scopus 로고
    • Diazepam-bound GABAA receptor models identify new benzodiazepine binding-site ligands
    • Richter, L. et al. Diazepam-bound GABAA receptor models identify new benzodiazepine binding-site ligands. Nat. Chem. Biol. 8, 455-464 (2012).
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 455-464
    • Richter, L.1
  • 39
    • 84976892909 scopus 로고    scopus 로고
    • KLIFS: A structural kinase-ligand interaction database
    • Kooistra, A. J. et al. KLIFS: a structural kinase-ligand interaction database. Nucleic Acids Res. 44, D365-371 (2016).
    • (2016) Nucleic Acids Res. , vol.44 , pp. D365-371
    • Kooistra, A.J.1
  • 40
    • 84982084049 scopus 로고    scopus 로고
    • PDEStrIAn: A phosphodiesterase structure and ligand interaction annotated database as a tool for structure-based drug design
    • Jansen, C. et al. PDEStrIAn: A Phosphodiesterase Structure and Ligand Interaction Annotated Database As a Tool for Structure-Based Drug Design. J. Med. Chem. doi: 10.1021/acs.jmedchem.5b01813 (2016).
    • (2016) J. Med. Chem.
    • Jansen, C.1
  • 41
    • 84905730759 scopus 로고    scopus 로고
    • Structure-based discovery of selective serotonin 5-HT1B receptor ligands
    • Rodriguez, D., Brea, J., Loza, M. I. & Carlsson, J. Structure-Based Discovery of Selective Serotonin 5-HT1B Receptor Ligands. Structure 22, 1140-1151 (2014).
    • (2014) Structure , vol.22 , pp. 1140-1151
    • Rodriguez, D.1    Brea, J.2    Loza, M.I.3    Carlsson, J.4
  • 42
    • 39149097541 scopus 로고    scopus 로고
    • Discovery of novel agonists and antagonists of the free fatty acid receptor 1 (FFAR1) using virtual screening
    • Tikhonova, I. G. et al. Discovery of novel agonists and antagonists of the free fatty acid receptor 1 (FFAR1) using virtual screening. J. Med. Chem. 51, 625-633 (2008).
    • (2008) J. Med. Chem. , vol.51 , pp. 625-633
    • Tikhonova, I.G.1
  • 43
    • 84859460667 scopus 로고    scopus 로고
    • Structure-based ligand discovery for the protein-protein interface of chemokine receptor CXCR4
    • Mysinger, M. M. et al. Structure-based ligand discovery for the protein-protein interface of chemokine receptor CXCR4. Proc. Natl. Acad. Sci. USA 109, 5517-5522 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 5517-5522
    • Mysinger, M.M.1
  • 44
    • 80054868459 scopus 로고    scopus 로고
    • Ligand discovery from a dopamine D3 receptor homology model and crystal structure
    • Carlsson, J. et al. Ligand discovery from a dopamine D3 receptor homology model and crystal structure. Nat. Chem. Biol. 7, 769-778 (2011).
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 769-778
    • Carlsson, J.1
  • 45
    • 77649204282 scopus 로고    scopus 로고
    • Structure-based discovery of novel chemotypes for adenosine A(2A) receptor antagonists
    • Katritch, V. et al. Structure-based discovery of novel chemotypes for adenosine A(2A) receptor antagonists. J. Med. Chem. 53, 1799-1809 (2010).
    • (2010) J. Med. Chem. , vol.53 , pp. 1799-1809
    • Katritch, V.1
  • 46
    • 66149149851 scopus 로고    scopus 로고
    • Structure-based discovery of beta2-adrenergic receptor ligands
    • Kolb, P. et al. Structure-based discovery of beta2-adrenergic receptor ligands. Proc. Natl. Acad. Sci. USA 106, 6843-6848 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 6843-6848
    • Kolb, P.1
  • 47
    • 33947727830 scopus 로고    scopus 로고
    • Identification of nonpeptide CCR5 receptor agonists by structure-based virtual screening
    • Kellenberger, E. et al. Identification of nonpeptide CCR5 receptor agonists by structure-based virtual screening. J. Med. Chem. 50, 1294-1303 (2007).
    • (2007) J. Med. Chem. , vol.50 , pp. 1294-1303
    • Kellenberger, E.1
  • 48
    • 13944255377 scopus 로고    scopus 로고
    • Structure-based drug discovery using GPCR homology modeling: Successful virtual screening for antagonists of the alpha1A adrenergic receptor
    • Evers, A. & Klabunde, T. Structure-based drug discovery using GPCR homology modeling: successful virtual screening for antagonists of the alpha1A adrenergic receptor. J. Med. Chem. 48, 1088-1097 (2005).
    • (2005) J. Med. Chem. , vol.48 , pp. 1088-1097
    • Evers, A.1    Klabunde, T.2
  • 49
    • 84877716938 scopus 로고    scopus 로고
    • Biophysical fragment screening of the beta1-adrenergic receptor: Identification of high affinity arylpiperazine leads using structure-based drug design
    • Christopher, J. A. et al. Biophysical fragment screening of the beta1-adrenergic receptor: identification of high affinity arylpiperazine leads using structure-based drug design. J. Med. Chem. 56, 3446-3455 (2013).
    • (2013) J. Med. Chem. , vol.56 , pp. 3446-3455
    • Christopher, J.A.1
  • 50
    • 65049089399 scopus 로고    scopus 로고
    • Identifying conformational changes of the beta(2) adrenoceptor that enable accurate prediction of ligand/receptor interactions and screening for GPCR modulators
    • Reynolds, K. A., Katritch, V. & Abagyan, R. Identifying conformational changes of the beta(2) adrenoceptor that enable accurate prediction of ligand/receptor interactions and screening for GPCR modulators. J. Comput. Aided Mol. Des. 23, 273-288 (2009).
    • (2009) J. Comput. Aided Mol. Des. , vol.23 , pp. 273-288
    • Reynolds, K.A.1    Katritch, V.2    Abagyan, R.3
  • 51
    • 84862776738 scopus 로고    scopus 로고
    • Biased signaling pathways in beta2-adrenergic receptor characterized by 19F-NMR
    • Liu, J. J., Horst, R., Katritch, V., Stevens, R. C. & Wuthrich, K. Biased signaling pathways in beta2-adrenergic receptor characterized by 19F-NMR. Science 335, 1106-1110 (2012).
    • (2012) Science , vol.335 , pp. 1106-1110
    • Liu, J.J.1    Horst, R.2    Katritch, V.3    Stevens, R.C.4    Wuthrich, K.5
  • 52
    • 0017655199 scopus 로고
    • Distortion of cyclic AMP responses to catecholamine due to destruction of the hormone
    • Barber, R., Kelly, L. A., McGuire, R. F. & Butcher, R. W. Distortion of cyclic AMP responses to catecholamine due to destruction of the hormone. J. Cyclic Nucleotide Res. 3, 249-261 (1977).
    • (1977) J. Cyclic Nucleotide Res. , vol.3 , pp. 249-261
    • Barber, R.1    Kelly, L.A.2    McGuire, R.F.3    Butcher, R.W.4
  • 53
    • 84855798366 scopus 로고    scopus 로고
    • Cell-based and in-silico studies on the high intrinsic activity of two boron-containing salbutamol derivatives at the human beta(2)-adrenoceptor
    • Soriano-Ursua, M. A. et al. Cell-based and in-silico studies on the high intrinsic activity of two boron-containing salbutamol derivatives at the human beta(2)-adrenoceptor. Bioorg. Med. Chem. 20, 933-941 (2012).
    • (2012) Bioorg. Med. Chem. , vol.20 , pp. 933-941
    • Soriano-Ursua, M.A.1
  • 54
    • 33846876695 scopus 로고    scopus 로고
    • Relating protein pharmacology by ligand chemistry
    • Keiser, M. J. et al. Relating protein pharmacology by ligand chemistry. Nat. Biotechnol. 25, 197-206 (2007).
    • (2007) Nat. Biotechnol. , vol.25 , pp. 197-206
    • Keiser, M.J.1
  • 55
    • 84892751031 scopus 로고    scopus 로고
    • MyChEMBL: A virtual machine implementation of open data and cheminformatics tools
    • Ochoa, R., Davies, M., Papadatos, G., Atkinson, F. & Overington, J. P. myChEMBL: a virtual machine implementation of open data and cheminformatics tools. Bioinformatics 30, 298-300 (2014).
    • (2014) Bioinformatics , vol.30 , pp. 298-300
    • Ochoa, R.1    Davies, M.2    Papadatos, G.3    Atkinson, F.4    Overington, J.P.5
  • 56
    • 85027927015 scopus 로고    scopus 로고
    • Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists
    • Wu, B. et al. Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists. Science 330, 1066-1071 (2010).
    • (2010) Science , vol.330 , pp. 1066-1071
    • Wu, B.1
  • 57
    • 84884673669 scopus 로고    scopus 로고
    • Structure of the CCR5 chemokine receptor-HIV entry inhibitor maraviroc complex
    • Tan, Q. et al. Structure of the CCR5 chemokine receptor-HIV entry inhibitor maraviroc complex. Science 341, 1387-1390 (2013).
    • (2013) Science , vol.341 , pp. 1387-1390
    • Tan, Q.1
  • 58
    • 84925606909 scopus 로고    scopus 로고
    • Identifying modulators of CXC receptors 3 and 4 with tailored selectivity using multi-target docking
    • Schmidt, D., Bernat, V., Brox, R., Tschammer, N. & Kolb, P. Identifying modulators of CXC receptors 3 and 4 with tailored selectivity using multi-target docking. ACS Chem. Biol. 10, 715-724 (2015).
    • (2015) ACS Chem. Biol. , vol.10 , pp. 715-724
    • Schmidt, D.1    Bernat, V.2    Brox, R.3    Tschammer, N.4    Kolb, P.5
  • 59
    • 84948440927 scopus 로고    scopus 로고
    • Allosteric ligands for the pharmacologically dark receptors GPR68 and GPR65
    • Huang, X. P. et al. Allosteric ligands for the pharmacologically dark receptors GPR68 and GPR65. Nature 527, 477-483 (2015).
    • (2015) Nature , vol.527 , pp. 477-483
    • Huang, X.P.1
  • 60
    • 79954782236 scopus 로고    scopus 로고
    • Structure of an agonist-bound human A2A adenosine receptor
    • Xu, F. et al. Structure of an agonist-bound human A2A adenosine receptor. Science 332, 322-327 (2011).
    • (2011) Science , vol.332 , pp. 322-327
    • Xu, F.1
  • 61
    • 84889564886 scopus 로고    scopus 로고
    • Activation and allosteric modulation of a muscarinic acetylcholine receptor
    • Kruse, A. C. et al. Activation and allosteric modulation of a muscarinic acetylcholine receptor. Nature 504, 101-106 (2013).
    • (2013) Nature , vol.504 , pp. 101-106
    • Kruse, A.C.1
  • 62
    • 84899751079 scopus 로고    scopus 로고
    • Agonist-bound structure of the human P2Y12 receptor
    • Zhang, J. et al. Agonist-bound structure of the human P2Y12 receptor. Nature 509, 119-122 (2014).
    • (2014) Nature , vol.509 , pp. 119-122
    • Zhang, J.1
  • 63
    • 84939795137 scopus 로고    scopus 로고
    • Structural insights into micro-opioid receptor activation
    • Huang, W. et al. Structural insights into micro-opioid receptor activation. Nature 524, 315-321 (2015).
    • (2015) Nature , vol.524 , pp. 315-321
    • Huang, W.1
  • 64
    • 80052967337 scopus 로고    scopus 로고
    • Multiple ligand-specific conformations of the beta2-adrenergic receptor
    • Kahsai, A. W. et al. Multiple ligand-specific conformations of the beta2-adrenergic receptor. Nat. Chem. Biol. 7, 692-700 (2011).
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 692-700
    • Kahsai, A.W.1
  • 65
    • 84956677842 scopus 로고    scopus 로고
    • Drugging specific conformational states of GPCRs: Challenges and opportunities for computational chemistry
    • Marti-Solano, M., Schmidt, D., Kolb, P. & Selent, J. Drugging specific conformational states of GPCRs: challenges and opportunities for computational chemistry. Drug Discov. Today 21, 625-631 (2016).
    • (2016) Drug Discov. Today , vol.21 , pp. 625-631
    • Marti-Solano, M.1    Schmidt, D.2    Kolb, P.3    Selent, J.4
  • 66
    • 84894090269 scopus 로고    scopus 로고
    • Quantification of ligand bias for clinically relevant beta2-adrenergic receptor ligands: Implications for drug taxonomy
    • van der Westhuizen, E. T., Breton, B., Christopoulos, A. & Bouvier, M. Quantification of ligand bias for clinically relevant beta2-adrenergic receptor ligands: implications for drug taxonomy. Mol. Pharmacol. 85, 492-509 (2014).
    • (2014) Mol. Pharmacol. , vol.85 , pp. 492-509
    • Van-Der-Westhuizen, E.T.1    Breton, B.2    Christopoulos, A.3    Bouvier, M.4
  • 67
    • 77957055780 scopus 로고
    • Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations of G protein-coupled receptors
    • Ballesteros, J. A. & Weinstein, H. Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations of G protein-coupled receptors. Methods Neurosci. 25, 366-428 (1995).
    • (1995) Methods Neurosci. , vol.25 , pp. 366-428
    • Ballesteros, J.A.1    Weinstein, H.2
  • 68
    • 77953185520 scopus 로고    scopus 로고
    • The selectivity of beta-adrenoceptor agonists at human beta1-, beta2- and beta3-adrenoceptors
    • Baker, J. G. The selectivity of beta-adrenoceptor agonists at human beta1-, beta2- and beta3-adrenoceptors. Br. J. Pharmacol. 160, 1048-1061 (2010).
    • (2010) Br. J. Pharmacol. , vol.160 , pp. 1048-1061
    • Baker, J.G.1
  • 69
    • 0001109246 scopus 로고    scopus 로고
    • A fast method of molecular shape comparison: A simple application of a Gaussian description of molecular shape
    • Grant, J. A., Gallardo, M. A. & Pickup, B. T. A fast method of molecular shape comparison: A simple application of a Gaussian description of molecular shape. J. Comput. Chem. 17, 1653-1666 (1996).
    • (1996) J. Comput. Chem. , vol.17 , pp. 1653-1666
    • Grant, J.A.1    Gallardo, M.A.2    Pickup, B.T.3


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