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Volumn 7, Issue 1, 2017, Pages

A molecular basis for selective antagonist destabilization of dopamine D3 receptor quaternary organization

Author keywords

[No Author keywords available]

Indexed keywords

DOPAMINE 3 RECEPTOR; DOPAMINE RECEPTOR BLOCKING AGENT; HALOPERIDOL; PROTEIN BINDING; SPIPERONE;

EID: 85019903749     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/s41598-017-02249-3     Document Type: Article
Times cited : (16)

References (56)
  • 1
    • 84975690668 scopus 로고    scopus 로고
    • Dopamine receptors and neurodegeneration
    • 10.14336/AD.2015.0330 26425390 4567218
    • Rangel-Barajas, C., Coronel, I. & Florán, B. Dopamine Receptors and Neurodegeneration. Aging Dis. 6, 349-368, doi: 10.14336/AD.2015.0330 (2015).
    • (2015) Aging Dis. , vol.6 , pp. 349-368
    • Rangel-Barajas, C.1    Coronel, I.2    Florán, B.3
  • 2
    • 84941314193 scopus 로고    scopus 로고
    • Novel dimensions of D3 receptor function: Focus on heterodimerisation, transactivation and allosteric modulation
    • 10.1016/j.euroneuro.2014.09.016 1:CAS:528:DC%2BC2cXhsl2ltLjJ 25453482
    • Maggio, R., Scarselli, M., Capannolo, M. & Millan, M. J. Novel dimensions of D3 receptor function: Focus on heterodimerisation, transactivation and allosteric modulation. Eur. Neuropsychopharmacol. 25, 1470-1479, doi: 10.1016/j.euroneuro.2014.09.016 (2015).
    • (2015) Eur. Neuropsychopharmacol. , vol.25 , pp. 1470-1479
    • Maggio, R.1    Scarselli, M.2    Capannolo, M.3    Millan, M.J.4
  • 3
    • 79952032110 scopus 로고    scopus 로고
    • The physiology, signaling, and pharmacology of dopamine receptors
    • 10.1124/pr.110.002642 1:CAS:528:DC%2BC3MXjslGis70%3D 21303898
    • Beaulieu, J. M. & Gainetdinov, R. R. The physiology, signaling, and pharmacology of dopamine receptors. Pharmacol. Rev. 63, 182-217, doi: 10.1124/pr.110.002642 (2011).
    • (2011) Pharmacol. Rev. , vol.63 , pp. 182-217
    • Beaulieu, J.M.1    Gainetdinov, R.R.2
  • 4
    • 84893642127 scopus 로고    scopus 로고
    • G protein-coupled receptor oligomerization revisited: Functional and pharmacological perspectives
    • 10.1124/pr.113.008052 24515647 3973609
    • Ferré, S. et al. G protein-coupled receptor oligomerization revisited: functional and pharmacological perspectives. Pharmacol. Rev. 66, 413-434, doi: 10.1124/pr.113.008052 (2014).
    • (2014) Pharmacol. Rev. , vol.66 , pp. 413-434
    • Ferré, S.1
  • 5
    • 0038576278 scopus 로고    scopus 로고
    • The fourth transmembrane segment forms the interface of the dopamine D2 receptor homodimer
    • 10.1074/jbc.C200679200 1:CAS:528:DC%2BD3sXhtVKmtL0%3D 12496294
    • Guo, W., Shi, L. & Javitch, J. A. The fourth transmembrane segment forms the interface of the dopamine D2 receptor homodimer. J. Biol. Chem. 278, 4385-4388, doi: 10.1074/jbc.C200679200 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 4385-4388
    • Guo, W.1    Shi, L.2    Javitch, J.A.3
  • 6
    • 28444493656 scopus 로고    scopus 로고
    • Crosstalk in G protein-coupled receptors: Changes at the transmembrane homodimer interface determine activation
    • 10.1073/pnas.0508950102 2005PNAS.10217495G 1:CAS:528:DC%2BD2MXhtlSqtb3N 16301531 1287488
    • Guo, W., Shi, L., Filizola, M., Weinstein, H. & Javitch, J. A. Crosstalk in G protein-coupled receptors: changes at the transmembrane homodimer interface determine activation. Proc. Natl. Acad. Sci USA 102, 17495-17500, doi: 10.1073/pnas.0508950102 (2005).
    • (2005) Proc. Natl. Acad. Sci USA , vol.102 , pp. 17495-17500
    • Guo, W.1    Shi, L.2    Filizola, M.3    Weinstein, H.4    Javitch, J.A.5
  • 7
    • 51049112029 scopus 로고    scopus 로고
    • Dopamine D2 receptors form higher order oligomers at physiological expression levels
    • 10.1038/emboj.2008.153 1:CAS:528:DC%2BD1cXhtVGkt7jI 18668123 2529367
    • Guo, W. et al. Dopamine D2 receptors form higher order oligomers at physiological expression levels. EMBO J. 27, 2293-2304, doi: 10.1038/emboj.2008.153 (2008).
    • (2008) EMBO J. , vol.27 , pp. 2293-2304
    • Guo, W.1
  • 8
    • 84858607942 scopus 로고    scopus 로고
    • Functional homomers and heteromers of dopamine D2L and D3 receptors co-exist at the cell surface
    • 10.1074/jbc.M111.326678 1:CAS:528:DC%2BC38XjvVehtbw%3D 22291025 3308812
    • Pou, C., la Cour, C. M., Stoddart, L. A., Millan, M. J. & Milligan, G. Functional homomers and heteromers of dopamine D2L and D3 receptors co-exist at the cell surface. J. Biol. Chem. 287, 8864-8878, doi: 10.1074/jbc.M111.326678 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 8864-8878
    • Pou, C.1    La Cour, C.M.2    Stoddart, L.A.3    Millan, M.J.4    Milligan, G.5
  • 9
    • 84930679031 scopus 로고    scopus 로고
    • Distinct agonist regulation of muscarinic acetylcholine M2-M3 heteromers and their corresponding homomers
    • 10.1074/jbc.M115.649079 1:CAS:528:DC%2BC2MXps1emsro%3D 25918156 4505543
    • Aslanoglou, D., Alvarez-Curto, E., Marsango, S. & Milligan, G. Distinct Agonist Regulation of Muscarinic Acetylcholine M2-M3 Heteromers and Their Corresponding Homomers. J. Biol. Chem. 290, 14785-14796, doi: 10.1074/jbc.M115.649079 (2015).
    • (2015) J. Biol. Chem. , vol.290 , pp. 14785-14796
    • Aslanoglou, D.1    Alvarez-Curto, E.2    Marsango, S.3    Milligan, G.4
  • 10
    • 84865228987 scopus 로고    scopus 로고
    • Computational and experimental analysis of the transmembrane domain 4/5 dimerization interface of the serotonin 5-HT(1A) receptor
    • 10.1124/mol.112.079137 1:CAS:528:DC%2BC38XhtlShu7fK 22669805
    • Gorinski, N. et al. Computational and experimental analysis of the transmembrane domain 4/5 dimerization interface of the serotonin 5-HT(1A) receptor. Mol. Pharmacol. 82, 448-463, doi: 10.1124/mol.112.079137 (2012).
    • (2012) Mol. Pharmacol. , vol.82 , pp. 448-463
    • Gorinski, N.1
  • 11
    • 78751527600 scopus 로고    scopus 로고
    • Dopamine receptor homooligomers and heterooligomers in schizophrenia
    • 10.1111/j.1755-5949.2010.00228.x 1:CAS:528:DC%2BC3MXisVCnurY%3D 21199449
    • Perreault, M. L., O'Dowd, B. F. & George, S. R. Dopamine receptor homooligomers and heterooligomers in schizophrenia. CNS Neurosci. Ther. 17, 52-57, doi: 10.1111/j.1755-5949.2010.00228.x (2011).
    • (2011) CNS Neurosci. Ther. , vol.17 , pp. 52-57
    • Perreault, M.L.1    O'Dowd, B.F.2    George, S.R.3
  • 12
    • 72449210611 scopus 로고    scopus 로고
    • Dopamine D2-D3 receptor heteromers: Pharmacological properties and therapeutic significance
    • 10.1016/j.coph.2009.10.001 1:CAS:528:DC%2BD1MXhs1Wgtb3P 19896900
    • Maggio, R. & Millan, M. J. Dopamine D2-D3 receptor heteromers: pharmacological properties and therapeutic significance. Curr. Opin. Pharmacol. 10, 100-107, doi: 10.1016/j.coph.2009.10.001 (2010).
    • (2010) Curr. Opin. Pharmacol. , vol.10 , pp. 100-107
    • Maggio, R.1    Millan, M.J.2
  • 13
    • 84908352984 scopus 로고    scopus 로고
    • A peptide targeting an interaction interface disrupts the dopamine D1-D2 receptor heteromer to block signaling and function in vitro and in vivo: Effective selective antagonism
    • 10.1096/fj.14-254037 1:CAS:528:DC%2BC2cXhvFGiur7F 25063849 4200327
    • Hasbi, A. et al. A peptide targeting an interaction interface disrupts the dopamine D1-D2 receptor heteromer to block signaling and function in vitro and in vivo: effective selective antagonism. FASEB J. 28, 4806-4820, doi: 10.1096/fj.14-254037 (2014).
    • (2014) FASEB J. , vol.28 , pp. 4806-4820
    • Hasbi, A.1
  • 14
    • 78649448729 scopus 로고    scopus 로고
    • Characterization of the A2AR-D2R interface: Focus on the role of the C-terminal tail and the transmembrane helices
    • 10.1016/j.bbrc.2010.10.122 1:CAS:528:DC%2BC3cXhsV2jsrbF 21040702
    • Borroto-Escuela, D. O. et al. Characterization of the A2AR-D2R interface: focus on the role of the C-terminal tail and the transmembrane helices. Biochem. Biophys. Res. Commun. 402, 801-807, doi: 10.1016/j.bbrc.2010.10.122 (2010).
    • (2010) Biochem. Biophys. Res. Commun. , vol.402 , pp. 801-807
    • Borroto-Escuela, D.O.1
  • 15
    • 85024127806 scopus 로고    scopus 로고
    • Heteroreceptor complexes formed by dopamine D1, Histamine H3, and N-Methyl-D-aspartate glutamatereceptors as targets to prevent neuronal death in Alzheimer's disease
    • [Epub ahead of print]
    • Rodríguez-Ruiz, M. et al. Heteroreceptor Complexes Formed by Dopamine D1, Histamine H3, and N-Methyl-D-Aspartate GlutamateReceptors as Targets to Prevent Neuronal Death in Alzheimer's Disease. Mol. Neurobiol. [Epub ahead of print] (2016).
    • (2016) Mol. Neurobiol
    • Rodríguez-Ruiz, M.1
  • 16
    • 84941317804 scopus 로고    scopus 로고
    • Neuronal circuitry underlying the impact of D3 receptor ligands in drug addiction
    • 10.1016/j.euroneuro.2014.08.017 25266821 4362926
    • Le Foll, B. & Di Ciano, P. Neuronal circuitry underlying the impact of D3 receptor ligands in drug addiction. Eur. Neuropsychopharmacol. 25, 1401-1409, doi: 10.1016/j.euroneuro.2014.08.017 (2014).
    • (2014) Eur. Neuropsychopharmacol. , vol.25 , pp. 1401-1409
    • Le Foll, B.1    Di Ciano, P.2
  • 17
    • 84975231527 scopus 로고    scopus 로고
    • Dopamine D3 receptor availability is associated with inflexible decision making
    • 10.1523/JNEUROSCI.3253-15.2016 1:CAS:528:DC%2BC28XhsFGlsrjE 27335404 4916249
    • Groman, S. M. et al. Dopamine D3 Receptor Availability Is Associated with Inflexible Decision Making. J. Neurosci. 36, 6732-6741, doi: 10.1523/JNEUROSCI.3253-15.2016 (2016).
    • (2016) J. Neurosci. , vol.36 , pp. 6732-6741
    • Groman, S.M.1
  • 18
  • 19
    • 0033798153 scopus 로고    scopus 로고
    • The dopamine D3 receptor interacts with itself and the truncated D3 splice variant d3nf: D3-D3nf interaction causes mislocalization of D3 receptors
    • 1:CAS:528:DC%2BD3cXntValur0%3D 10999936
    • Karpa, K. D., Lin, R., Kabbani, N. & Levenson, R. The dopamine D3 receptor interacts with itself and the truncated D3 splice variant d3nf: D3-D3nf interaction causes mislocalization of D3 receptors. Mol. Pharmacol. 58, 677-683 (2000).
    • (2000) Mol. Pharmacol. , vol.58 , pp. 677-683
    • Karpa, K.D.1    Lin, R.2    Kabbani, N.3    Levenson, R.4
  • 20
    • 84931275050 scopus 로고    scopus 로고
    • Analysis of Human Dopamine D3 Receptor Quaternary Structure
    • 10.1074/jbc.M114.630681 1:CAS:528:DC%2BC2MXpvV2nsbo%3D 25931118 4463457
    • Marsango, S., Caltabiano, G., Pou, C., Varela Liste, M. J. & Milligan, G. Analysis of Human Dopamine D3 Receptor Quaternary Structure. J. Biol. Chem. 290, 15146-15162, doi: 10.1074/jbc.M114.630681 (2015).
    • (2015) J. Biol. Chem. , vol.290 , pp. 15146-15162
    • Marsango, S.1    Caltabiano, G.2    Pou, C.3    Varela Liste, M.J.4    Milligan, G.5
  • 21
    • 84931288404 scopus 로고    scopus 로고
    • The molecular basis of oligomeric organization of the human M3 muscarinic acetylcholine receptor
    • 10.1124/mol.114.096925 1:CAS:528:DC%2BC2MXns1Wlu7g%3D 25769304
    • Liste, M. J. et al. The molecular basis of oligomeric organization of the human M3 muscarinic acetylcholine receptor. Mol. Pharmacol. 87, 936-953, doi: 10.1124/mol.114.096925 (2015).
    • (2015) Mol. Pharmacol. , vol.87 , pp. 936-953
    • Liste, M.J.1
  • 22
    • 78449305788 scopus 로고    scopus 로고
    • Structure of the human dopamine D3 receptor in complex with a D2/D3 selective antagonist
    • 10.1126/science.1197410 2010Sci.330.1091C 1:CAS:528:DC%2BC3cXhsVahurvM 21097933 3058422
    • Chien, E. Y. et al. Structure of the human dopamine D3 receptor in complex with a D2/D3 selective antagonist. Science 330, 1091-1095, doi: 10.1126/science.1197410 (2010).
    • (2010) Science , vol.330 , pp. 1091-1095
    • Chien, E.Y.1
  • 23
    • 84961116197 scopus 로고    scopus 로고
    • Ligand binding pathways of clozapine and haloperidol in the dopamine D2 and D3 receptors
    • 10.1021/acs.jcim.5b00457 1:CAS:528:DC%2BC2MXitVGiurzO 26690887
    • Thomas, T., Fang, Y., Yuriev, E. & Chalmers, D. K. Ligand Binding Pathways of Clozapine and Haloperidol in the Dopamine D2 and D3 Receptors. J. Chem. Inf. Model. 56, 308-321, doi: 10.1021/acs.jcim.5b00457 (2016).
    • (2016) J. Chem. Inf. Model. , vol.56 , pp. 308-321
    • Thomas, T.1    Fang, Y.2    Yuriev, E.3    Chalmers, D.K.4
  • 24
    • 79955556525 scopus 로고    scopus 로고
    • Revealing protein oligomerization and densities in situ using spatial intensity distribution analysis
    • 10.1073/pnas.1018658108 2011PNAS.108.7010G 1:CAS:528:DC%2BC3MXlslOgtrg%3D 21482753 3084122
    • Godin et al. Revealing protein oligomerization and densities in situ using spatial intensity distribution analysis. Proc. Natl. Acad. Sci USA 108, 7010-7015, doi: 10.1073/pnas.1018658108 (2011).
    • (2011) Proc. Natl. Acad. Sci USA , vol.108 , pp. 7010-7015
    • Godin1
  • 25
    • 84873333524 scopus 로고    scopus 로고
    • Quantification of receptor tyrosine kinase activation and transactivation by G-protein-coupled receptors using spatial intensity distribution analysis (SpIDA)
    • 10.1016/B978-0-12-407865-9.00007-8 1:CAS:528:DC%2BC3sXotFSitL8%3D 23374183
    • Barbeau, A. et al. Quantification of receptor tyrosine kinase activation and transactivation by G-protein-coupled receptors using spatial intensity distribution analysis (SpIDA). Methods Enzymol. 522, 109-131, doi: 10.1016/B978-0-12-407865-9.00007-8 (2013).
    • (2013) Methods Enzymol. , vol.522 , pp. 109-131
    • Barbeau, A.1
  • 26
    • 84941120505 scopus 로고    scopus 로고
    • Spatial intensity distribution analysis reveals abnormal oligomerization of proteins in single cells
    • 10.1016/j.bpj.2015.06.068 2015BpJ.109.710G 1:CAS:528:DC%2BC2MXht1Crt7bM 26287623 4547338
    • Godin, A. G. et al. Spatial Intensity Distribution Analysis reveals abnormal oligomerization of proteins in single cells. Biophys. J. 109, 710-721, doi: 10.1016/j.bpj.2015.06.068 (2015).
    • (2015) Biophys. J. , vol.109 , pp. 710-721
    • Godin, A.G.1
  • 27
    • 84975092952 scopus 로고    scopus 로고
    • Dynamic regulation of quaternary organization of the M1 muscarinic receptor by subtype-selective antagonist drugs
    • 10.1074/jbc.M115.712562 1:CAS:528:DC%2BC28XhtVSksLjJ 27080256 4933229
    • Pediani, J. D., Ward, R. J., Godin, A. G., Marsango, S. & Milligan, G. Dynamic Regulation of Quaternary Organization of the M1 Muscarinic Receptor by Subtype-selective Antagonist Drugs. J. Biol. Chem. 291, 13132-13146, doi: 10.1074/jbc.M115.712562 (2016).
    • (2016) J. Biol. Chem. , vol.291 , pp. 13132-13146
    • Pediani, J.D.1    Ward, R.J.2    Godin, A.G.3    Marsango, S.4    Milligan, G.5
  • 29
    • 80052811601 scopus 로고    scopus 로고
    • Using the Flp-In T-Rex system to regulate GPCR expression
    • 10.1007/978-1-61779-126-0-2 1:CAS:528:DC%2BC38XjvVakt78%3D 21607850
    • Ward, R. J., Alvarez-Curto, E. & Milligan, G. Using the Flp-In T-Rex system to regulate GPCR expression. Methods Mol. Biol. 746, 21-37, doi: 10.1007/978-1-61779-126-0-2 (2011).
    • (2011) Methods Mol. Biol. , vol.746 , pp. 21-37
    • Ward, R.J.1    Alvarez-Curto, E.2    Milligan, G.3
  • 30
    • 0031953613 scopus 로고    scopus 로고
    • Agonistic properties of alniditan, sumatriptan and dihydroergotamine on human 5-HT1B and 5-HT1D receptors expressed in various mammalian cell lines
    • 10.1038/sj.bjp.0701766 1:CAS:528:DyaK1cXislarsLY%3D 9605573 1565323
    • Lesage, A. S. et al. Agonistic properties of alniditan, sumatriptan and dihydroergotamine on human 5-HT1B and 5-HT1D receptors expressed in various mammalian cell lines. Br. J. Pharmacol. 123, 1655-1665, doi: 10.1038/sj.bjp.0701766 (1998).
    • (1998) Br. J. Pharmacol. , vol.123 , pp. 1655-1665
    • Lesage, A.S.1
  • 31
    • 0032701195 scopus 로고    scopus 로고
    • Receptor density as a factor governing the efficacy of the dopamine D4 receptor ligands, L-745,870 and U-101958 at human recombinant D4.4 receptors expressed in CHO cells
    • 10.1038/sj.bjp.0702849 1:CAS:528:DyaK1MXntV2qsbY%3D 10516640 1571689
    • Gazi, L. et al. Receptor density as a factor governing the efficacy of the dopamine D4 receptor ligands, L-745,870 and U-101958 at human recombinant D4.4 receptors expressed in CHO cells. Br. J. Pharmacol. 128, 613-20, doi: 10.1038/sj.bjp.0702849 (1999).
    • (1999) Br. J. Pharmacol. , vol.128 , pp. 613-620
    • Gazi, L.1
  • 32
    • 78549284860 scopus 로고    scopus 로고
    • Interaction of novel hybrid compounds with the D3 dopamine receptor: Site-directed mutagenesis and homology modeling studies
    • 10.1016/j.bcp.2010.08.026 1:CAS:528:DC%2BC3cXhsVGrsbvL 20833147
    • Kortagere, S. et al. Interaction of novel hybrid compounds with the D3 dopamine receptor: Site-directed mutagenesis and homology modeling studies. Biochem. Pharmacol. 81, 157-163, doi: 10.1016/j.bcp.2010.08.026 (2011).
    • (2011) Biochem. Pharmacol. , vol.81 , pp. 157-163
    • Kortagere, S.1
  • 33
    • 41149164277 scopus 로고    scopus 로고
    • G protein coupling and ligand selectivity of the D2L and D3 dopamine receptors
    • 10.1124/jpet.107.134296 1:CAS:528:DC%2BD1cXktFGjur0%3D 18218829
    • Lane, J. R., Powney, B., Wise, A., Rees, S. & Milligan, G. G protein coupling and ligand selectivity of the D2L and D3 dopamine receptors. J. Pharmacol. Exp. Ther. 325, 319-330, doi: 10.1124/jpet.107.134296 (2008).
    • (2008) J. Pharmacol. Exp. Ther. , vol.325 , pp. 319-330
    • Lane, J.R.1    Powney, B.2    Wise, A.3    Rees, S.4    Milligan, G.5
  • 34
    • 77957055780 scopus 로고
    • Integrated methods for modelling G-protein coupled receptors
    • Ballesteros, J. A. & Weinstein, H. Integrated methods for modelling G-protein coupled receptors. Methods Neurosci. 366-428 (1995).
    • (1995) Methods Neurosci , pp. 366-428
    • Ballesteros, J.A.1    Weinstein, H.2
  • 35
    • 77249150932 scopus 로고    scopus 로고
    • Formation and dissociation of M1 muscarinic receptor dimers seen by total internal reflection fluorescence imaging of single molecules
    • 10.1073/pnas.0907915107 2010PNAS.107.2693H 1:CAS:528:DC%2BC3cXit1Srs7k%3D 20133736 2823895
    • Hern, J. A. et al. Formation and dissociation of M1 muscarinic receptor dimers seen by total internal reflection fluorescence imaging of single molecules. Proc. Natl. Acad. Sci. USA 107, 2693-2698, doi: 10.1073/pnas.0907915107 (2010).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 2693-2698
    • Hern, J.A.1
  • 36
    • 84874183639 scopus 로고    scopus 로고
    • 2 muscarinic acetylcholine receptors in live cardiac muscle
    • 10.1016/j.yjmcc.2013.01.009 1:CAS:528:DC%2BC3sXjvFCmtLc%3D 23357106 3605596
    • 2 muscarinic acetylcholine receptors in live cardiac muscle. J. Mol. Cell Cardiol. 57, 129-136, doi: 10.1016/j.yjmcc.2013.01.009 (2013).
    • (2013) J. Mol. Cell Cardiol. , vol.57 , pp. 129-136
    • Nenasheva, T.A.1
  • 37
    • 84987824806 scopus 로고    scopus 로고
    • Visualization and ligand-induced modulation of dopamine receptor dimerization at the single molecule level
    • doi: 10.1038/srep33233
    • Tabor, A. et al. Visualization and ligand-induced modulation of dopamine receptor dimerization at the single molecule level. Sci. Rep. 6, doi: 10.1038/srep33233 (2016).
    • (2016) Sci. Rep. , vol.6
    • Tabor, A.1
  • 38
    • 79551711208 scopus 로고    scopus 로고
    • Full characterization of GPCR monomer-dimer dynamic equilibrium by single molecule imaging
    • 10.1083/jcb.201009128 1:CAS:528:DC%2BC3MXitVCjt7g%3D 21300851 3101103
    • Kasai, R. S. et al. Full characterization of GPCR monomer-dimer dynamic equilibrium by single molecule imaging. J. Cell Biol. 192, 463-80, doi: 10.1083/jcb.201009128 (2011).
    • (2011) J. Cell Biol. , vol.192 , pp. 463-480
    • Kasai, R.S.1
  • 39
    • 84902772267 scopus 로고    scopus 로고
    • Tracking single molecules at work in living cells
    • 10.1038/nchembio.1558 1:CAS:528:DC%2BC2cXpvFWksL4%3D 24937070
    • Kusumi, A., Tsunoyama, T. A., Hirosawa, K. M., Kasai, R. S. & Fujiwara, T. K. Tracking single molecules at work in living cells. Nat. Chem. Biol. 10, 524-32, doi: 10.1038/nchembio.1558 (2014).
    • (2014) Nat. Chem. Biol. , vol.10 , pp. 524-532
    • Kusumi, A.1    Tsunoyama, T.A.2    Hirosawa, K.M.3    Kasai, R.S.4    Fujiwara, T.K.5
  • 40
    • 84872195772 scopus 로고    scopus 로고
    • Single-molecule analysis of fluorescently labeled G-protein-coupled receptors reveals complexes with distinct dynamics and organization
    • 10.1073/pnas.1205798110 2013PNAS.110.743C 1:CAS:528:DC%2BC3sXhtFOgsrY%3D 23267088
    • Calebiro, D. et al. Single-molecule analysis of fluorescently labeled G-protein-coupled receptors reveals complexes with distinct dynamics and organization. Proc. Natl. Acad. Sci. USA 110, 743-748, doi: 10.1073/pnas.1205798110 (2013).
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 743-748
    • Calebiro, D.1
  • 41
    • 84929377388 scopus 로고    scopus 로고
    • Regulation of oligomeric organization of the serotonin 5-hydroxytryptamine 2C (5-HT2C) receptor observed by spatial intensity distribution analysis
    • 10.1074/jbc.M115.644724 1:CAS:528:DC%2BC2MXosVamsLo%3D 25825490 4432300
    • Ward, R. J., Pediani, J. D., Godin, A. G. & Milligan, G. Regulation of oligomeric organization of the serotonin 5-hydroxytryptamine 2C (5-HT2C) receptor observed by spatial intensity distribution analysis. J. Biol. Chem. 290, 12844-12857, doi: 10.1074/jbc.M115.644724 (2015).
    • (2015) J. Biol. Chem. , vol.290 , pp. 12844-12857
    • Ward, R.J.1    Pediani, J.D.2    Godin, A.G.3    Milligan, G.4
  • 42
    • 85009370641 scopus 로고    scopus 로고
    • Quaternary structures of opsin in live cells revealed by FRET spectrometry
    • 10.1042/BCJ20160422 1:CAS:528:DC%2BC2sXhs1Omt7g%3D 27623775
    • Mishra, A. K. et al. Quaternary structures of opsin in live cells revealed by FRET spectrometry. Biochem J. 473, 3819-3836, doi: 10.1042/BCJ20160422 (2016).
    • (2016) Biochem J. , vol.473 , pp. 3819-3836
    • Mishra, A.K.1
  • 43
    • 84884683292 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy analysis of serotonin, adrenergic, muscarinic, and dopamine receptor dimerization: The oligomer number puzzle
    • 10.1124/mol.113.087072 1:CAS:528:DC%2BC3sXhsVygt7zK 23907214 3781380
    • Herrick-Davis, K., Grinde, E., Cowan, A. & Mazurkiewicz, J. E. Fluorescence correlation spectroscopy analysis of serotonin, adrenergic, muscarinic, and dopamine receptor dimerization: the oligomer number puzzle. Mol. Pharmacol. 84, 630-642, doi: 10.1124/mol.113.087072 (2013).
    • (2013) Mol. Pharmacol. , vol.84 , pp. 630-642
    • Herrick-Davis, K.1    Grinde, E.2    Cowan, A.3    Mazurkiewicz, J.E.4
  • 44
    • 3042663287 scopus 로고    scopus 로고
    • G protein-coupled receptor dimerization: Function and ligand pharmacology
    • 10.1124/mol.104.000497 1:CAS:528:DC%2BD2cXlsVOjtbY%3D
    • Milligan, G. G protein-coupled receptor dimerization: function and ligand pharmacology. Mol. Pharm. 66, 1-7, doi: 10.1124/mol.104.000497 (2004).
    • (2004) Mol. Pharm. , vol.66 , pp. 1-7
    • Milligan, G.1
  • 45
    • 69249206623 scopus 로고    scopus 로고
    • G protein-coupled receptor hetero-dimerisation: Contribution to pharmacology and function
    • 10.1111/j.1476-5381.2009.00169.x 1:CAS:528:DC%2BD1MXhsVKmu7nO 19309353 2795239
    • Milligan, G. G protein-coupled receptor hetero-dimerisation: contribution to pharmacology and function. Br. J. Pharmacol. 158, 5-14, doi: 10.1111/j.1476-5381.2009.00169.x (2009).
    • (2009) Br. J. Pharmacol. , vol.158 , pp. 5-14
    • Milligan, G.1
  • 46
    • 84879121186 scopus 로고    scopus 로고
    • The prevalence, maintenance and relevance of G protein-coupled receptor oligomerisation
    • 10.1124/mol.113.084780 1:CAS:528:DC%2BC3sXhtVajsbnI
    • Milligan, G. The prevalence, maintenance and relevance of G protein-coupled receptor oligomerisation. Mol. Pharm. 84, 158-169, doi: 10.1124/mol.113.084780 (2013).
    • (2013) Mol. Pharm. , vol.84 , pp. 158-169
    • Milligan, G.1
  • 47
    • 77951668878 scopus 로고    scopus 로고
    • Heterodimerisation of G protein-coupled receptors: Implications for drug design and ligand screening
    • 10.1517/17460441003720467 22823130
    • Saenz del Burgo, L. & Milligan, G. Heterodimerisation of G protein-coupled receptors: implications for drug design and ligand screening. Expert. Opin. Drug Discov. 5, 461-474, doi: 10.1517/17460441003720467 (2010).
    • (2010) Expert. Opin. Drug Discov. , vol.5 , pp. 461-474
    • Saenz Del Burgo, L.1    Milligan, G.2
  • 48
    • 67749116459 scopus 로고    scopus 로고
    • Pirenzepine promotes the dimerization of muscarinic M1 receptors through a three-step binding process
    • 10.1074/jbc.M109.017145 1:CAS:528:DC%2BD1MXot12ku7g%3D 19451648 2740579
    • Ilien, B. et al. Pirenzepine promotes the dimerization of muscarinic M1 receptors through a three-step binding process. J. Biol. Chem. 284, 19533-19543, doi: 10.1074/jbc.M109.017145 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 19533-19543
    • Ilien, B.1
  • 49
    • 77956478769 scopus 로고    scopus 로고
    • Schizophrenia, amphetamine-induced sensitized state and acute amphetamine exposure all show a common alteration: Increased dopamine D2 receptor dimerization
    • 10.1186/1756-6606-3-25 20813060 2942879
    • Wang, M. et al. Schizophrenia, amphetamine-induced sensitized state and acute amphetamine exposure all show a common alteration: increased dopamine D2 receptor dimerization. Mol. Brain 3, 25-34, doi: 10.1186/1756-6606-3-25 (2010).
    • (2010) Mol. Brain , vol.3 , pp. 25-34
    • Wang, M.1
  • 50
    • 84884203363 scopus 로고    scopus 로고
    • Schizophrenia and dopamine receptors
    • 10.1016/j.euroneuro.2013.06.005 1:CAS:528:DC%2BC3sXhtFSlsLbJ 23860356
    • Seeman, P. Schizophrenia and dopamine receptors. Eur. Neuropsychopharmacol. 23, 999-1009, doi: 10.1016/j.euroneuro.2013.06.005 (2013).
    • (2013) Eur. Neuropsychopharmacol. , vol.23 , pp. 999-1009
    • Seeman, P.1
  • 51
    • 43749107283 scopus 로고    scopus 로고
    • Comparative protein structure modeling using Modeller
    • doi: 10.1002/0471250953.bi0506s15 (Chapter 5, 5.6.1-5.6.30)
    • Eswar, N. et al. Comparative protein structure modeling using Modeller. Curr. Protoc. bioinformatics Chapter 5, doi: 10.1002/0471250953.bi0506s15 (Chapter 5, 5.6.1-5.6.30) (2006).
    • (2006) Curr. Protoc. Bioinformatics Chapter , vol.5
    • Eswar, N.1
  • 52
    • 84876197291 scopus 로고    scopus 로고
    • Y. Crystal structure of oligomeric β1-adrenergic G protein-coupled receptors in ligand-free basal state
    • 10.1038/nsmb.2504 1:CAS:528:DC%2BC3sXivF2jur8%3D 23435379 3618578
    • Huang, J., Chen, S., Zhang, J. J. & Huang, X. Y. Crystal structure of oligomeric β1-adrenergic G protein-coupled receptors in ligand-free basal state. Nat. Struct. Mol. Biol. 20, 419-25, doi: 10.1038/nsmb.2504 (2013).
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 419-425
    • Huang, J.1    Chen, S.2    Zhang, J.J.3    Huang, X.4
  • 53
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
    • 10.1002/jcc.21334
    • Trott, O. & Olson, A. J. AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J. Comput. Chem. 30, 455-61, doi: 10.1002/jcc.21334 (2010).
    • (2010) J. Comput. Chem. , vol.30 , pp. 455-461
    • Trott, O.1    Olson, A.J.2
  • 54
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation. in
    • 10.1021/ct700301q 1:CAS:528:DC%2BD1cXhsVSqurc%3D 26620784
    • Hess, B., Kutzner, C., van der Spoel, D. & Lindahl, E. GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation. in. J. Chem. Theory Comput. 4, 435-47, doi: 10.1021/ct700301q (2008).
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 55
    • 84858311167 scopus 로고    scopus 로고
    • Membrane protein simulations using AMBER force field and berger lipid parameters
    • 10.1021/ct200491c 26593357
    • Cordomí, A., Caltabiano, G. & Pardo, L. Membrane Protein Simulations Using AMBER Force Field and Berger Lipid Parameters. J. Chem. Theory Comput. 8, 948-958, doi: 10.1021/ct200491c (2012).
    • (2012) J. Chem. Theory Comput. , vol.8 , pp. 948-958
    • Cordomí, A.1    Caltabiano, G.2    Pardo, L.3
  • 56
    • 0029878720 scopus 로고    scopus 로고
    • VMD - Visual molecular dynamics
    • 10.1016/0263-7855(96)00018-5
    • Humphrey, W., Dalke, A. & Schulten, K. VMD - Visual Molecular Dynamics. J. Mol. Graph. 14(33-38), 27-28, doi: 10.1016/0263-7855(96)00018-5 (1996).
    • (1996) J. Mol. Graph. , vol.14 , Issue.33-38 , pp. 27-28
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3


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