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Volumn 136, Issue , 2018, Pages 401-410

Muscarinic receptor oligomerization

Author keywords

Dimerization; Ligand regulation; Muscarinic acetylcholine receptor; Oligomerization; Quaternary structure

Indexed keywords

CHAPERONE; G PROTEIN COUPLED RECEPTOR; MUSCARINIC RECEPTOR; PIRENZEPINE; TELENZEPINE;

EID: 85034851232     PISSN: 00283908     EISSN: 18737064     Source Type: Journal    
DOI: 10.1016/j.neuropharm.2017.11.023     Document Type: Review
Times cited : (17)

References (99)
  • 1
    • 77954917965 scopus 로고    scopus 로고
    • Ligand regulation of the quaternary organization of cell surface M3 muscarinic acetylcholine receptors analyzed by fluorescence resonance energy transfer (FRET) imaging and homogeneous time-resolved FRET
    • Alvarez-Curto, E., Ward, R.J., Pediani, J.D., Milligan, G., Ligand regulation of the quaternary organization of cell surface M3 muscarinic acetylcholine receptors analyzed by fluorescence resonance energy transfer (FRET) imaging and homogeneous time-resolved FRET. J. Biol. Chem. 285 (2010), 23318–23330, 10.1074/jbc.M110.122184.
    • (2010) J. Biol. Chem. , vol.285 , pp. 23318-23330
    • Alvarez-Curto, E.1    Ward, R.J.2    Pediani, J.D.3    Milligan, G.4
  • 2
    • 77955982118 scopus 로고    scopus 로고
    • Applications of fluorescence and bioluminescence resonance energy transfer to drug discovery at G protein coupled receptors
    • Alvarez-Curto, E., Pediani, J.D., Milligan, G., Applications of fluorescence and bioluminescence resonance energy transfer to drug discovery at G protein coupled receptors. Anal. Bioanal. Chem. 398 (2010), 167–180, 10.1007/s00216-010-3823-4.
    • (2010) Anal. Bioanal. Chem. , vol.398 , pp. 167-180
    • Alvarez-Curto, E.1    Pediani, J.D.2    Milligan, G.3
  • 3
    • 81555204243 scopus 로고    scopus 로고
    • Developing chemical genetic approaches to explore G protein-coupled receptor function: validation of the use of a receptor activated solely by synthetic ligand (RASSL)
    • Alvarez-Curto, E., Prihandoko, R., Tautermann, C.S., Zwier, J.M., Pediani, J.D., Lohse, M.J., Hoffmann, C., Tobin, A.B., Milligan, G., Developing chemical genetic approaches to explore G protein-coupled receptor function: validation of the use of a receptor activated solely by synthetic ligand (RASSL). Mol. Pharmacol. 80 (2011), 1033–1046, 10.1124/mol.111.074674.
    • (2011) Mol. Pharmacol. , vol.80 , pp. 1033-1046
    • Alvarez-Curto, E.1    Prihandoko, R.2    Tautermann, C.S.3    Zwier, J.M.4    Pediani, J.D.5    Lohse, M.J.6    Hoffmann, C.7    Tobin, A.B.8    Milligan, G.9
  • 4
    • 85007602741 scopus 로고    scopus 로고
    • Targeted Elimination of G proteins and arrestins defines their specific contributions to both intensity and duration of G protein-coupled receptor signalling
    • Alvarez-Curto, E., Inoue, A., Jenkins, L., Raihan, S.Z., Prihandoko, R., Tobin, A.B., Milligan, G., Targeted Elimination of G proteins and arrestins defines their specific contributions to both intensity and duration of G protein-coupled receptor signalling. J. Biol. Chem. 291 (2016), 27147–27159, 10.1074/jbc.M116.754887.
    • (2016) J. Biol. Chem. , vol.291 , pp. 27147-27159
    • Alvarez-Curto, E.1    Inoue, A.2    Jenkins, L.3    Raihan, S.Z.4    Prihandoko, R.5    Tobin, A.B.6    Milligan, G.7
  • 5
    • 84930679031 scopus 로고    scopus 로고
    • Distinct agonist regulation of muscarinic acetylcholine m2-m3 heteromers and their corresponding homomers
    • 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 (2015), 14785–14796, 10.1074/jbc.M115.649079.
    • (2015) J. Biol. Chem. , vol.290 , pp. 14785-14796
    • Aslanoglou, D.1    Alvarez-Curto, E.2    Marsango, S.3    Milligan, G.4
  • 6
    • 0020666568 scopus 로고
    • Oligomeric structure of muscarinic receptors is shown by photoaffinity labeling: subunit assembly may explain high- and low-affinity agonist states
    • Avissar, S., Amitai, G., Sokolovsky, M., Oligomeric structure of muscarinic receptors is shown by photoaffinity labeling: subunit assembly may explain high- and low-affinity agonist states. Proc. Natl. Acad. Sci. U. S. A. 80 (1983), 156–159.
    • (1983) Proc. Natl. Acad. Sci. U. S. A. , vol.80 , pp. 156-159
    • Avissar, S.1    Amitai, G.2    Sokolovsky, M.3
  • 7
    • 72449197630 scopus 로고    scopus 로고
    • Recent advances in bioluminescence resonance energy transfer technologies to study GPCR heteromerization
    • Ayoub, M.A., Pfleger, K.D., Recent advances in bioluminescence resonance energy transfer technologies to study GPCR heteromerization. Curr. Opin. Pharmacol. 10 (2010), 44–52, 10.1016/j.coph.2009.09.012.
    • (2010) Curr. Opin. Pharmacol. , vol.10 , pp. 44-52
    • Ayoub, M.A.1    Pfleger, K.D.2
  • 8
    • 84951861644 scopus 로고    scopus 로고
    • Resonance energy transfer-based approaches to study GPCRs
    • Ayoub, M.A., Resonance energy transfer-based approaches to study GPCRs. Methods Cell Biol. 132 (2016), 255–292, 10.1016/bs.mcb.2015.10.008.
    • (2016) Methods Cell Biol. , vol.132 , pp. 255-292
    • Ayoub, M.A.1
  • 9
    • 84873333524 scopus 로고    scopus 로고
    • Quantification of receptor tyrosine kinase activation and transactivation by G-protein-coupled receptors using spatial intensity distribution analysis (SpIDA)
    • Barbeau, A., Godin, A.G., Swift, J.L., De Koninck, Y., Wiseman, P.W., Beaulieu, J.M., Quantification of receptor tyrosine kinase activation and transactivation by G-protein-coupled receptors using spatial intensity distribution analysis (SpIDA). Methods Enzymol. 522 (2013), 109–131, 10.1016/B978-0-12-408143-7.00001-3.
    • (2013) Methods Enzymol. , vol.522 , pp. 109-131
    • Barbeau, A.1    Godin, A.G.2    Swift, J.L.3    De Koninck, Y.4    Wiseman, P.W.5    Beaulieu, J.M.6
  • 11
    • 0018134270 scopus 로고
    • The binding of agonists to brain muscarinic receptors
    • Birdsall, N.J., Burgen, A.S., Hulme, E.C., The binding of agonists to brain muscarinic receptors. Mol. Pharmacol. 14 (1978), 723–736.
    • (1978) Mol. Pharmacol. , vol.14 , pp. 723-736
    • Birdsall, N.J.1    Burgen, A.S.2    Hulme, E.C.3
  • 12
    • 84872195772 scopus 로고    scopus 로고
    • Single-molecule analysis of fluorescently labeled G-protein-coupled receptors reveals complexes with distinct dynamics and organization
    • 110,743–748
    • Calebiro, D., Rieken, F., Wagner, J., Sungkaworn, T., Zabel, U., Borzi, A., Cocucci, E., Zürn, A., Lohse, M.J., Single-molecule analysis of fluorescently labeled G-protein-coupled receptors reveals complexes with distinct dynamics and organization. Proc. Natl. Acad. Sci. U. S. A., 2013, 10.1073/pnas.1205798110 110,743–748.
    • (2013) Proc. Natl. Acad. Sci. U. S. A.
    • Calebiro, D.1    Rieken, F.2    Wagner, J.3    Sungkaworn, T.4    Zabel, U.5    Borzi, A.6    Cocucci, E.7    Zürn, A.8    Lohse, M.J.9
  • 13
    • 0242581698 scopus 로고    scopus 로고
    • Is rhodopsin dimeric in native retinal rods?
    • Chabre, M., Cone, R., Saibil, H., Is rhodopsin dimeric in native retinal rods?. Nature 426 (2003), 30–31.
    • (2003) Nature , vol.426 , pp. 30-31
    • Chabre, M.1    Cone, R.2    Saibil, H.3
  • 15
    • 77955058619 scopus 로고    scopus 로고
    • Lighting up multiprotein complexes: lessons from GPCR oligomerization
    • Ciruela, F., Vilardaga, J.P., Fernández-Dueñas, V., Lighting up multiprotein complexes: lessons from GPCR oligomerization. Trends Biotechnol. 28 (2010), 407–415, 10.1016/j.tibtech.2010.05.002.
    • (2010) Trends Biotechnol. , vol.28 , pp. 407-415
    • Ciruela, F.1    Vilardaga, J.P.2    Fernández-Dueñas, V.3
  • 17
    • 77749320196 scopus 로고    scopus 로고
    • Directed molecular evolution of DREADDs: a generic approach to creating next-generation RASSLs
    • Dong, S., Rogan, S.C., Roth, B.L., Directed molecular evolution of DREADDs: a generic approach to creating next-generation RASSLs. Nat. Protoc 5 (2010), 561–573, 10.1038/nprot.2009.239.
    • (2010) Nat. Protoc , vol.5 , pp. 561-573
    • Dong, S.1    Rogan, S.C.2    Roth, B.L.3
  • 18
    • 0022408262 scopus 로고
    • The relationship between muscarinic receptor occupancy and adenylate cyclase inhibition in the rabbit myocardium
    • Ehlert, F.J., The relationship between muscarinic receptor occupancy and adenylate cyclase inhibition in the rabbit myocardium. Mol. Pharmacol. 28 (1985), 410–421.
    • (1985) Mol. Pharmacol. , vol.28 , pp. 410-421
    • Ehlert, F.J.1
  • 19
    • 85009351664 scopus 로고    scopus 로고
    • An update on the physiological and therapeutic relevance of GPCR oligomers
    • Farran, B., An update on the physiological and therapeutic relevance of GPCR oligomers. Pharmacol. Res. 117 (2017), 303–327, 10.1016/j.phrs.2017.01.008.
    • (2017) Pharmacol. Res. , vol.117 , pp. 303-327
    • Farran, B.1
  • 20
    • 85029363558 scopus 로고    scopus 로고
    • Receptor quaternary organization explains G protein-coupled receptor family structure
    • Felce, J.H., Latty, S.L., Knox, R.G., Mattick, S.R., Lui, Y., Lee, S.F., Klenerman, D., Davis, S.J., Receptor quaternary organization explains G protein-coupled receptor family structure. Cell Rep. 20 (2017), 2654–2665, 10.1016/j.celrep.2017.08.072.
    • (2017) Cell Rep. , vol.20 , pp. 2654-2665
    • Felce, J.H.1    Latty, S.L.2    Knox, R.G.3    Mattick, S.R.4    Lui, Y.5    Lee, S.F.6    Klenerman, D.7    Davis, S.J.8
  • 23
    • 84973091661 scopus 로고    scopus 로고
    • Basic pharmacological and structural evidence for class A G-protein-coupled receptor heteromerisation
    • Franco, R., Martinez-Pinilla, E., Lanciego, J.L., Navarro, G., Basic pharmacological and structural evidence for class A G-protein-coupled receptor heteromerisation. Front. Pharmacol., 7, 2016, 76, 10.3389/fphar.2016.00076.
    • (2016) Front. Pharmacol. , vol.7 , pp. 76
    • Franco, R.1    Martinez-Pinilla, E.2    Lanciego, J.L.3    Navarro, G.4
  • 24
    • 84995912137 scopus 로고    scopus 로고
    • Membrane-mediated oligomerisation of G protein coupled receptors and its implications for GPCR function
    • Gahbauer, S., Böckmann, R.A., Membrane-mediated oligomerisation of G protein coupled receptors and its implications for GPCR function. Front. Pharmacol., 7, 2016, 494, 10.3389/fphar.2016.00494.
    • (2016) Front. Pharmacol. , vol.7 , pp. 494
    • Gahbauer, S.1    Böckmann, R.A.2
  • 25
    • 0023585043 scopus 로고
    • Muscarinic cholinergic receptors in the embryonic chick heart: interaction of agonist, receptor, and guanine nucleotides studied by an improved assay for direct binding of the muscarinic agonist [3H]cismethyldioxolane
    • Galper, J.B., Haigh, L.S., Hart, A.C., O'Hara, D.S., Livingston, D.J., Muscarinic cholinergic receptors in the embryonic chick heart: interaction of agonist, receptor, and guanine nucleotides studied by an improved assay for direct binding of the muscarinic agonist [3H]cismethyldioxolane. Mol. Pharmacol. 32 (1987), 230–240.
    • (1987) Mol. Pharmacol. , vol.32 , pp. 230-240
    • Galper, J.B.1    Haigh, L.S.2    Hart, A.C.3    O'Hara, D.S.4    Livingston, D.J.5
  • 28
    • 84941120505 scopus 로고    scopus 로고
    • Spatial Intensity Distribution Analysis reveals abnormal oligomerization of proteins in single cells
    • Godin, A.G., Rappaz, B., Potvin-Trottier, L., Kennedy, T.E., De Koninck, Y., Wiseman, P.W., Spatial Intensity Distribution Analysis reveals abnormal oligomerization of proteins in single cells. Biophys. J. 109 (2015), 710–721, 10.1016/j.bpj.2015.06.068.
    • (2015) Biophys. J. , vol.109 , pp. 710-721
    • Godin, A.G.1    Rappaz, B.2    Potvin-Trottier, L.3    Kennedy, T.E.4    De Koninck, Y.5    Wiseman, P.W.6
  • 29
    • 33646500642 scopus 로고    scopus 로고
    • Quantitative analysis of muscarinic acetylcholine receptor homo- and heterodimerization in live cells: regulation of receptor down-regulation by heterodimerization
    • Goin, J.C., Nathanson, N.M., Quantitative analysis of muscarinic acetylcholine receptor homo- and heterodimerization in live cells: regulation of receptor down-regulation by heterodimerization. J. Biol. Chem. 281 (2006), 5416–5425.
    • (2006) J. Biol. Chem. , vol.281 , pp. 5416-5425
    • Goin, J.C.1    Nathanson, N.M.2
  • 32
  • 33
    • 84884683292 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy analysis of serotonin, adrenergic, muscarinic, and dopamine receptor dimerization: the oligomer number puzzle
    • 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 (2013), 630–642, 10.1124/mol.113.087072.
    • (2013) Mol. Pharmacol. , vol.84 , pp. 630-642
    • Herrick-Davis, K.1    Grinde, E.2    Cowan, A.3    Mazurkiewicz, J.E.4
  • 34
    • 0028007135 scopus 로고
    • A kinetic model for oxotremorine M binding to recombinant porcine m2 muscarinic receptors expressed in Chinese hamster ovary cells
    • Hirschberg, B.T., Schimerlik, M.I., A kinetic model for oxotremorine M binding to recombinant porcine m2 muscarinic receptors expressed in Chinese hamster ovary cells. J. Biol. Chem. 269 (1994), 26127–26135.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26127-26135
    • Hirschberg, B.T.1    Schimerlik, M.I.2
  • 37
    • 84889006104 scopus 로고    scopus 로고
    • Novel structural and functional insights into M3 muscarinic receptor dimer/oligomer formation
    • Hu, J., Hu, K., Liu, T., Stern, M.K., Mistry, R., Challiss, R.A., Costanzi, S., Wess, J., Novel structural and functional insights into M3 muscarinic receptor dimer/oligomer formation. J. Biol. Chem. 288 (2013), 34777–34790, 10.1074/jbc.M113.503714.
    • (2013) J. Biol. Chem. , vol.288 , pp. 34777-34790
    • Hu, J.1    Hu, K.2    Liu, T.3    Stern, M.K.4    Mistry, R.5    Challiss, R.A.6    Costanzi, S.7    Wess, J.8
  • 38
    • 84876197291 scopus 로고    scopus 로고
    • Crystal structure of oligomeric β1-adrenergic G protein–coupled receptors in ligand-free basal state
    • 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 (2013), 419–425, 10.1038/nsmb.2504.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 419-425
    • Huang, J.1    Chen, S.2    Zhang, J.J.3    Huang, X.Y.4
  • 39
    • 84881363451 scopus 로고    scopus 로고
    • SNAP-tag technology: a powerful tool for site specific conjugation of therapeutic and imaging agents
    • Hussain, A.F., Amoury, M., Barth, S., SNAP-tag technology: a powerful tool for site specific conjugation of therapeutic and imaging agents. Curr. Pharm. Des. 19 (2013), 5437–5442.
    • (2013) Curr. Pharm. Des. , vol.19 , pp. 5437-5442
    • Hussain, A.F.1    Amoury, M.2    Barth, S.3
  • 40
    • 67749116459 scopus 로고    scopus 로고
    • Pirenzepine promotes the dimerization of muscarinic M1 receptors through a three-step binding process
    • Ilien, B., Glasser, N., Clamme, J.P., Didier, P., Piemont, E., Chinnappan, R., Daval, S.B., Galzi, J.L., Mely, Y., Pirenzepine promotes the dimerization of muscarinic M1 receptors through a three-step binding process. J. Biol. Chem. 284 (2009), 19533–19543, 10.1074/jbc.M109.017145.
    • (2009) J. Biol. Chem. , vol.284 , pp. 19533-19543
    • Ilien, B.1    Glasser, N.2    Clamme, J.P.3    Didier, P.4    Piemont, E.5    Chinnappan, R.6    Daval, S.B.7    Galzi, J.L.8    Mely, Y.9
  • 42
    • 0033578005 scopus 로고    scopus 로고
    • G-protein-coupled receptor heterodimerisation modulates receptor function
    • Jordan, B.A., Devi, L.A., G-protein-coupled receptor heterodimerisation modulates receptor function. Nature 399 (1999), 697–700.
    • (1999) Nature , vol.399 , pp. 697-700
    • Jordan, B.A.1    Devi, L.A.2
  • 43
    • 79951854466 scopus 로고    scopus 로고
    • Dimers and beyond: the functional puzzles of class C GPCRs
    • Kniazeff, J., Prézeau, L., Rondard, P., Pin, J.P., Goudet, C., Dimers and beyond: the functional puzzles of class C GPCRs. Pharmacol. Ther. 130 (2011), 9–25, 10.1016/j.pharmthera.2011.01.006.
    • (2011) Pharmacol. Ther. , vol.130 , pp. 9-25
    • Kniazeff, J.1    Prézeau, L.2    Rondard, P.3    Pin, J.P.4    Goudet, C.5
  • 48
    • 70350381113 scopus 로고    scopus 로고
    • Purification and functional reconstitution of monomeric mu-opioid receptors: allosteric modulation of agonist binding by Gi2
    • Kuzak, A.J., Pitchiaya, S., Anand, J.P., Mosberg, H.I., Walter, N.G., Sunahara, R.K., Purification and functional reconstitution of monomeric mu-opioid receptors: allosteric modulation of agonist binding by Gi2. J. Biol. Chem. 284 (2009), 26732–26741, 10.1074/jbc.M109.026922.
    • (2009) J. Biol. Chem. , vol.284 , pp. 26732-26741
    • Kuzak, A.J.1    Pitchiaya, S.2    Anand, J.P.3    Mosberg, H.I.4    Walter, N.G.5    Sunahara, R.K.6
  • 49
    • 84869749433 scopus 로고    scopus 로고
    • Sequential conformational rearrangements dictate the dynamics of class C GPCR activation
    • Lane, J.R., Canals, M., Sequential conformational rearrangements dictate the dynamics of class C GPCR activation. Sci. Signal., 5, 2012, pe51, 10.1126/scisignal.2003503.
    • (2012) Sci. Signal. , vol.5 , pp. pe51
    • Lane, J.R.1    Canals, M.2
  • 50
    • 0038159530 scopus 로고    scopus 로고
    • Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes
    • Liang, Y., Fotiadis, D., Filipek, S., Saperstein, D.A., Palczewski, K., Engel, A., Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes. J. Biol. Chem. 278 (2003), 21655–21662.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21655-21662
    • Liang, Y.1    Fotiadis, D.2    Filipek, S.3    Saperstein, D.A.4    Palczewski, K.5    Engel, A.6
  • 51
    • 84931288404 scopus 로고    scopus 로고
    • The molecular basis of oligomeric organization of the human M3 muscarinic acetylcholine receptor
    • Liste, M.J., Caltabiano, G., Ward, R.J., Alvarez-Curto, E., Marsango, S., Milligan, G., The molecular basis of oligomeric organization of the human M3 muscarinic acetylcholine receptor. Mol. Pharmacol. 87 (2015), 936–953, 10.1124/mol.114.096925.
    • (2015) Mol. Pharmacol. , vol.87 , pp. 936-953
    • Liste, M.J.1    Caltabiano, G.2    Ward, R.J.3    Alvarez-Curto, E.4    Marsango, S.5    Milligan, G.6
  • 52
    • 0027467848 scopus 로고
    • Coexpression studies with mutant muscarinic/adrenergic receptors provide evidence for intermolecular “cross-talk” between G-protein-linked receptors
    • Maggio, R., Vogel, Z., Wess, J., Coexpression studies with mutant muscarinic/adrenergic receptors provide evidence for intermolecular “cross-talk” between G-protein-linked receptors. Proc. Natl. Acad. Sci. U. S. A. 90 (1993), 3103–3107.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 3103-3107
    • Maggio, R.1    Vogel, Z.2    Wess, J.3
  • 53
    • 0029955946 scopus 로고    scopus 로고
    • Functional role of the third cytoplasmic loop in muscarinic receptor dimerization
    • Maggio, R., Barbier, P., Fornai, F., Corsini, G.U., Functional role of the third cytoplasmic loop in muscarinic receptor dimerization. J. Biol. Chem. 271 (1996), 31055–31060.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31055-31060
    • Maggio, R.1    Barbier, P.2    Fornai, F.3    Corsini, G.U.4
  • 56
    • 0033667466 scopus 로고    scopus 로고
    • A trafficking checkpoint controls GABA(B) receptor heterodimerization
    • Margeta-Mitrovic, M., Jan, Y.N., Jan, L.Y., A trafficking checkpoint controls GABA(B) receptor heterodimerization. Neuron 27 (2000), 97–106.
    • (2000) Neuron , vol.27 , pp. 97-106
    • Margeta-Mitrovic, M.1    Jan, Y.N.2    Jan, L.Y.3
  • 58
    • 84931275050 scopus 로고    scopus 로고
    • Analysis of human dopamine D3 receptor quaternary structure
    • Marsango, S., Caltabiano, G., Pou, C., Liste, M.J., Milligan, G., Analysis of human dopamine D3 receptor quaternary structure. J. Biol. Chem. 290 (2015), 15146–15162, 10.1074/jbc.M114.630681.
    • (2015) J. Biol. Chem. , vol.290 , pp. 15146-15162
    • Marsango, S.1    Caltabiano, G.2    Pou, C.3    Liste, M.J.4    Milligan, G.5
  • 59
    • 84938845592 scopus 로고    scopus 로고
    • Approaches to characterize and quantify oligomerization of GPCRs
    • Marsango, S., Varela, M.J., Milligan, G., Approaches to characterize and quantify oligomerization of GPCRs. Methods Mol. Biol. 1335 (2015), 95–105, 10.1007/978-1-4939-2914-6_7.
    • (2015) Methods Mol. Biol. , vol.1335 , pp. 95-105
    • Marsango, S.1    Varela, M.J.2    Milligan, G.3
  • 61
    • 0021824455 scopus 로고
    • Guanine nucleotide regulation of a mammalian myocardial muscarinic receptor system. Evidence for homo- and heterotropic cooperativity in ligand binding analyzed by computer-assisted curve fitting
    • Mattera, R., Pitts, B.J., Entman, M.L., Birnbaumer, L., Guanine nucleotide regulation of a mammalian myocardial muscarinic receptor system. Evidence for homo- and heterotropic cooperativity in ligand binding analyzed by computer-assisted curve fitting. J. Biol. Chem. 260 (1985), 7410–7421.
    • (1985) J. Biol. Chem. , vol.260 , pp. 7410-7421
    • Mattera, R.1    Pitts, B.J.2    Entman, M.L.3    Birnbaumer, L.4
  • 63
    • 80051480604 scopus 로고    scopus 로고
    • Structural basis of M3 muscarinic receptor dimer/oligomer formation
    • McMillin, S.M., Heusel, M., Liu, T., Costanzi, S., Wess, J., Structural basis of M3 muscarinic receptor dimer/oligomer formation. J. Biol. Chem. 286 (2011), 28584–28598, 10.1007/978-1-4939-2914-6_7.
    • (2011) J. Biol. Chem. , vol.286 , pp. 28584-28598
    • McMillin, S.M.1    Heusel, M.2    Liu, T.3    Costanzi, S.4    Wess, J.5
  • 64
    • 84988672537 scopus 로고    scopus 로고
    • Accelerated structure-based design of chemically diverse allosteric modulators of a muscarinic G protein-coupled receptor
    • Miao, Y., Goldfeld, D.A., Von Moo, E., Sexton, P.M., Christopoulos, A., McCammon, J.A., Valant, C., Accelerated structure-based design of chemically diverse allosteric modulators of a muscarinic G protein-coupled receptor. Proc. Natl. Acad. Sci. U. S. A. 113 (2016), E5675–E5684, 10.1073/pnas.1612353113.
    • (2016) Proc. Natl. Acad. Sci. U. S. A. , vol.113 , pp. E5675-E5684
    • Miao, Y.1    Goldfeld, D.A.2    Von Moo, E.3    Sexton, P.M.4    Christopoulos, A.5    McCammon, J.A.6    Valant, C.7
  • 65
    • 3042663287 scopus 로고    scopus 로고
    • G protein-coupled receptor dimerization: function and ligand pharmacology
    • Milligan, G., G protein-coupled receptor dimerization: function and ligand pharmacology. Mol. Pharm. 66 (2004), 1–7.
    • (2004) Mol. Pharm. , vol.66 , pp. 1-7
    • Milligan, G.1
  • 66
    • 69249206623 scopus 로고    scopus 로고
    • G protein-coupled receptor hetero-dimerization: contribution to pharmacology and function
    • Milligan, G., G protein-coupled receptor hetero-dimerization: contribution to pharmacology and function. Br. J. Pharmacol. 158 (2009), 5–14, 10.1111/j.1476-5381.2009.00169.
    • (2009) Br. J. Pharmacol. , vol.158 , pp. 5-14
    • Milligan, G.1
  • 67
    • 84879121186 scopus 로고    scopus 로고
    • The prevalence, maintenance and relevance of G protein-coupled receptor oligomerisation
    • Milligan, G., The prevalence, maintenance and relevance of G protein-coupled receptor oligomerisation. Mol. Pharm. 84 (2013), 158–169, 10.1124/mol.113.084780.
    • (2013) Mol. Pharm. , vol.84 , pp. 158-169
    • Milligan, G.1
  • 72
    • 84877737677 scopus 로고    scopus 로고
    • The muscarinic M3 acetylcholine receptor exists as two differently sized complexes at the plasma membrane
    • Patowary, S., Alvarez-Curto, E., Xu, T.R., Holz, J.D., Oliver, J.A., Milligan, G., Raicu, V., The muscarinic M3 acetylcholine receptor exists as two differently sized complexes at the plasma membrane. Biochem. J. 452 (2013), 303–312, 10.1042/BJ20121902.
    • (2013) Biochem. J. , vol.452 , pp. 303-312
    • Patowary, S.1    Alvarez-Curto, E.2    Xu, T.R.3    Holz, J.D.4    Oliver, J.A.5    Milligan, G.6    Raicu, V.7
  • 73
    • 3343026033 scopus 로고    scopus 로고
    • Oligomeric potential of the M2 muscarinic cholinergic receptor
    • Park, P.S., Wells, J.W., Oligomeric potential of the M2 muscarinic cholinergic receptor. J. Neurochem. 90 (2004), 537–548.
    • (2004) J. Neurochem. , vol.90 , pp. 537-548
    • Park, P.S.1    Wells, J.W.2
  • 74
    • 84975092952 scopus 로고    scopus 로고
    • Dynamic regulation of quaternary organization of the M1 muscarinic receptor by subtype-selective antagonist drugs
    • 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 (2016), 13132–13146, 10.1074/jbc.M115.712562.
    • (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
  • 75
    • 85030622484 scopus 로고    scopus 로고
    • Spatial intensity distribution analysis: studies of G Protein-coupled receptor oligomerisation
    • Pediani, J.D., Ward, R.J., Marsango, S., Milligan, G., Spatial intensity distribution analysis: studies of G Protein-coupled receptor oligomerisation. Trends Pharmacol. Sci. 1465 (2017), 30180–30183, 10.1016/j.tips.2017.09.001.
    • (2017) Trends Pharmacol. Sci. , vol.1465 , pp. 30180-30183
    • Pediani, J.D.1    Ward, R.J.2    Marsango, S.3    Milligan, G.4
  • 76
    • 57749114392 scopus 로고    scopus 로고
    • Engineered GPCRs as tools to modulate signal transduction
    • Pei, Y., Rogan, S.C., Yan, F., Roth, B.L., Engineered GPCRs as tools to modulate signal transduction. Physiol. (Bethesda). 23 (2008), 313–321, 10.1152/physiol.00025.2008.
    • (2008) Physiol. (Bethesda). , vol.23 , pp. 313-321
    • Pei, Y.1    Rogan, S.C.2    Yan, F.3    Roth, B.L.4
  • 77
    • 77952757509 scopus 로고    scopus 로고
    • Oligomeric size of the m2 muscarinic receptor in live cells as determined by quantitative fluorescence resonance energy transfer
    • Pisterzi, L.F., Jansma, D.B., Georgiou, J., Woodside, M.J., Chou, J.T., Angers, S., Raicu, V., Wells, J.W., Oligomeric size of the m2 muscarinic receptor in live cells as determined by quantitative fluorescence resonance energy transfer. J. Biol. Chem. 285 (2010), 16723–16738, 10.1074/jbc.M109.069443.
    • (2010) J. Biol. Chem. , vol.285 , pp. 16723-16738
    • Pisterzi, L.F.1    Jansma, D.B.2    Georgiou, J.3    Woodside, M.J.4    Chou, J.T.5    Angers, S.6    Raicu, V.7    Wells, J.W.8
  • 80
    • 84886787864 scopus 로고    scopus 로고
    • Efficacy as an intrinsic property of the M(2) muscarinic receptor in its tetrameric state
    • Redka, D.S., Heerklotz, H., Wells, J.W., Efficacy as an intrinsic property of the M(2) muscarinic receptor in its tetrameric state. Biochemistry 52 (2013), 7405–7427, 10.1021/bi4003869.
    • (2013) Biochemistry , vol.52 , pp. 7405-7427
    • Redka, D.S.1    Heerklotz, H.2    Wells, J.W.3
  • 84
    • 78650147139 scopus 로고    scopus 로고
    • Allostery at G protein-coupled receptor homo- and heteromers: uncharted pharmacological landscapes
    • Smith, N.J., Milligan, G., Allostery at G protein-coupled receptor homo- and heteromers: uncharted pharmacological landscapes. Pharmacol. Rev. 62 (2010), 701–725, 10.1124/pr.110.002667.
    • (2010) Pharmacol. Rev. , vol.62 , pp. 701-725
    • Smith, N.J.1    Milligan, G.2
  • 85
    • 84912051951 scopus 로고    scopus 로고
    • Identification of transmembrane domains that regulate spatial arrangements and activity of prokineticin receptor 2 dimers
    • Sposini, S., Caltabiano, G., Hanyaloglu, A.C., Miele, R., Identification of transmembrane domains that regulate spatial arrangements and activity of prokineticin receptor 2 dimers. Mol. Cell. Endocrinol. 399 (2015), 362–372, 10.1016/j.mce.2014.10.024.
    • (2015) Mol. Cell. Endocrinol. , vol.399 , pp. 362-372
    • Sposini, S.1    Caltabiano, G.2    Hanyaloglu, A.C.3    Miele, R.4
  • 86
    • 11144301981 scopus 로고    scopus 로고
    • The supramolecular structure of the GPCR rhodopsin in solution and native disc membranes
    • Suda, K., Filipek, S., Palczewski, K., Engel, A., Fotiadis, D., The supramolecular structure of the GPCR rhodopsin in solution and native disc membranes. Mol. Membr. Biol. 21 (2004), 435–446.
    • (2004) Mol. Membr. Biol. , vol.21 , pp. 435-446
    • Suda, K.1    Filipek, S.2    Palczewski, K.3    Engel, A.4    Fotiadis, D.5
  • 90
    • 84940478169 scopus 로고    scopus 로고
    • Conformational dynamics of a class C G-protein-coupled receptor
    • Vafabakhsh, R., Levitz, J., Isacoff, E.Y., Conformational dynamics of a class C G-protein-coupled receptor. Nature 524 (2015), 497–501, 10.1038/nature14679.
    • (2015) Nature , vol.524 , pp. 497-501
    • Vafabakhsh, R.1    Levitz, J.2    Isacoff, E.Y.3
  • 92
    • 79951963422 scopus 로고    scopus 로고
    • 1 receptors assessed via N-terminal SNAP and CLIP-tagging
    • 1 receptors assessed via N-terminal SNAP and CLIP-tagging. Brt. J. Pharm. 162 (2010), 1439–1452, 10.1111/j.1476-5381.2010.01156.
    • (2010) Brt. J. Pharm. , vol.162 , pp. 1439-1452
    • Ward, R.J.1    Pediani, J.D.2    Milligan, G.3
  • 93
    • 84929377388 scopus 로고    scopus 로고
    • Regulation of oligomeric organization of the serotonin 5-hydroxytryptamine 2C (5-HT2C) receptor observed by spatial intensity distribution analysis
    • 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 (2015), 12844–12857, 10.1074/jbc.M115.644724.
    • (2015) J. Biol. Chem. , vol.290 , pp. 12844-12857
    • Ward, R.J.1    Pediani, J.D.2    Godin, A.G.3    Milligan, G.4
  • 94
    • 85019854752 scopus 로고    scopus 로고
    • Spatial Intensity Distribution Analysis quantifies the extent and regulation of homo-dimerization of the secretin receptor
    • Ward, R.J., Pediani, J.D., Harikumar, K.G., Miller, L.J., Milligan, G., Spatial Intensity Distribution Analysis quantifies the extent and regulation of homo-dimerization of the secretin receptor. Biochem. J. 474 (2017), 1879–1895, 10.1042/BCJ20170184.
    • (2017) Biochem. J. , vol.474 , pp. 1879-1895
    • Ward, R.J.1    Pediani, J.D.2    Harikumar, K.G.3    Miller, L.J.4    Milligan, G.5
  • 96
    • 0029083945 scopus 로고
    • Cooperativity manifest in the binding properties of purified cardiac muscarinic receptors
    • Wreggett, K.A., Wells, J.W., Cooperativity manifest in the binding properties of purified cardiac muscarinic receptors. J. Biol. Chem. 270 (1995), 22488–22499.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22488-22499
    • Wreggett, K.A.1    Wells, J.W.2
  • 97
    • 84902340888 scopus 로고    scopus 로고
    • Roundabout 1 exists predominantly as a basal dimeric complex and this is unaffected by binding of the ligand Slit2
    • Zakrys, L., Ward, R.J., Pediani, J.D., Godin, A.G., Graham, G.J., Milligan, G., Roundabout 1 exists predominantly as a basal dimeric complex and this is unaffected by binding of the ligand Slit2. Biochem. J. 461 (2014), 61–73, 10.1042/BJ20140190.
    • (2014) Biochem. J. , vol.461 , pp. 61-73
    • Zakrys, L.1    Ward, R.J.2    Pediani, J.D.3    Godin, A.G.4    Graham, G.J.5    Milligan, G.6
  • 98
    • 0033516576 scopus 로고    scopus 로고
    • Identification and molecular characterization of m3 muscarinic receptor dimers
    • Zeng, F.Y., Wess, J., Identification and molecular characterization of m3 muscarinic receptor dimers. J. Biol. Chem. 274 (1999), 19487–19497.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19487-19497
    • Zeng, F.Y.1    Wess, J.2


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