메뉴 건너뛰기




Volumn 7, Issue OCT, 2016, Pages

Membrane-mediated oligomerization of G protein coupled receptors and its implications for GPCR function

Author keywords

Cholesterol; Dimerization; FRET; GPCR; Membrane; Molecular dynamics simulation; Oligomerization; Palmitoylation

Indexed keywords

G PROTEIN COUPLED RECEPTOR; LIGAND;

EID: 84995912137     PISSN: None     EISSN: 1664042X     Source Type: Journal    
DOI: 10.3389/fphys.2016.00494     Document Type: Review
Times cited : (97)

References (151)
  • 1
    • 33947424778 scopus 로고    scopus 로고
    • G protein-coupled receptor systems and their lipid environment in health disorders during aging
    • Alemany, R., Perona, J. S., Sánchez-Dominguez, J. M., Montero, E., Cañizares, J., Bressani, R., et al. (2007). G protein-coupled receptor systems and their lipid environment in health disorders during aging. Biochim. Biophys. Acta 1768, 964-975. doi: 10.1016/j.bbamem.2006.09.024
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 964-975
    • Alemany, R.1    Perona, J.S.2    Sánchez-Dominguez, J.M.3    Montero, E.4    Cañizares, J.5    Bressani, R.6
  • 2
    • 21744442451 scopus 로고    scopus 로고
    • Ligand modulation of lateral segregation of a G-protein-coupled receptor into lipid microdomains in sphingomyelin/phosphatidylcholine solid-supported bilayers
    • Alves, I. D., Salamon, Z., Hruby, V. J., and Tollin, G. (2005). Ligand modulation of lateral segregation of a G-protein-coupled receptor into lipid microdomains in sphingomyelin/phosphatidylcholine solid-supported bilayers. Biochemistry 44, 9168-9178. doi: 10.1021/bi050207a
    • (2005) Biochemistry , vol.44 , pp. 9168-9178
    • Alves, I.D.1    Salamon, Z.2    Hruby, V.J.3    Tollin, G.4
  • 3
    • 0036174608 scopus 로고    scopus 로고
    • Dimerization: an emerging concept for G protein-coupled receptor ontogeny and function
    • Angers, S., Salahpour, A., and Bouvier, M. (2002). Dimerization: an emerging concept for G protein-coupled receptor ontogeny and function. Annu. Rev. Pharmacol. Toxicol. 42, 409-435. doi: 10.1146/annurev.pharmtox.42.091701.082314
    • (2002) Annu. Rev. Pharmacol. Toxicol , vol.42 , pp. 409-435
    • Angers, S.1    Salahpour, A.2    Bouvier, M.3
  • 4
    • 0034724192 scopus 로고    scopus 로고
    • Detection of β2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET)
    • Angers, S., Salahpour, A., Joly, E., Hilairet, S., Chelsky, D., Dennis, M., et al. (2000). Detection of β2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET). Proc. Natl. Acad. Sci. U.S.A. 97, 3684-3689. doi: 10.1073/pnas.060590697
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 3684-3689
    • Angers, S.1    Salahpour, A.2    Joly, E.3    Hilairet, S.4    Chelsky, D.5    Dennis, M.6
  • 5
    • 72449197630 scopus 로고    scopus 로고
    • Recent advances in bioluminescence resonance energy transfer technologies to study GPCR heteromerization
    • Ayoub, M. A., and Pfleger, K. D. (2010). Recent advances in bioluminescence resonance energy transfer technologies to study GPCR heteromerization. Curr. Opin. Pharm. 10, 44-52. doi: 10.1016/j.coph.2009.09.012
    • (2010) Curr. Opin. Pharm , vol.10 , pp. 44-52
    • Ayoub, M.A.1    Pfleger, K.D.2
  • 6
    • 84860158205 scopus 로고    scopus 로고
    • Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor
    • Baier, C. J., Fantini, J., and Barrantes, F. J. (2011). Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor. Sci. Rep. 1:69. doi: 10.1038/srep00069
    • (2011) Sci. Rep , vol.1 , pp. 69
    • Baier, C.J.1    Fantini, J.2    Barrantes, F.J.3
  • 7
    • 34447509986 scopus 로고    scopus 로고
    • Transducin activation by nanoscale lipid bilayers containing one and two rhodopsins
    • Bayburt, T. H., Leitz, A. J., Xie, G., Oprian, D. D., and Sligar, S. G. (2007). Transducin activation by nanoscale lipid bilayers containing one and two rhodopsins. J. Biol. Chem. 282, 14875-14881. doi: 10.1074/jbc.M701433200
    • (2007) J. Biol. Chem , vol.282 , pp. 14875-14881
    • Bayburt, T.H.1    Leitz, A.J.2    Xie, G.3    Oprian, D.D.4    Sligar, S.G.5
  • 8
    • 4544383544 scopus 로고    scopus 로고
    • Caveolin-1 interacts with 5-HT2A serotonin receptors and profoundly modulates the signaling of selected Gaq-coupled protein receptors
    • Bhatnagar, A., Sheffler, D. J., Kroeze, W. K., Compton-Toth, B., and Roth, B. L. (2004). Caveolin-1 interacts with 5-HT2A serotonin receptors and profoundly modulates the signaling of selected Gaq-coupled protein receptors. J. Biol. Chem. 279, 34614-34623. doi: 10.1074/jbc.M404673200
    • (2004) J. Biol. Chem , vol.279 , pp. 34614-34623
    • Bhatnagar, A.1    Sheffler, D.J.2    Kroeze, W.K.3    Compton-Toth, B.4    Roth, B.L.5
  • 9
    • 0035968261 scopus 로고    scopus 로고
    • Palmitoylation of CCR5 is critical for receptor trafficking and efficient activation of intracellular signaling pathways
    • Blanpain, C., Wittamer, V., Vanderwinden, J. M., Boom, A., Renneboog, B., Lee, B., et al. (2001). Palmitoylation of CCR5 is critical for receptor trafficking and efficient activation of intracellular signaling pathways. J. Biol. Chem. 276, 23795-23804. doi: 10.1074/jbc.M100583200
    • (2001) J. Biol. Chem , vol.276 , pp. 23795-23804
    • Blanpain, C.1    Wittamer, V.2    Vanderwinden, J.M.3    Boom, A.4    Renneboog, B.5    Lee, B.6
  • 10
    • 33845505655 scopus 로고    scopus 로고
    • Curvature and hydrophobic forces drive oligomerization and modulate activity of rhodopsin in membranes
    • Botelho, A. V., Huber, T., Sakmar, T. P., and Brown, M. F. (2006). Curvature and hydrophobic forces drive oligomerization and modulate activity of rhodopsin in membranes. Biophys. J. 91, 4464-4477. doi: 10.1529/biophysj.106.082776
    • (2006) Biophys. J , vol.91 , pp. 4464-4477
    • Botelho, A.V.1    Huber, T.2    Sakmar, T.P.3    Brown, M.F.4
  • 11
    • 84873401872 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer microscopy as demonstrated by measuring the activation of the serine/threonine kinase Akt
    • Broussard, J. A., Rappaz, B., Webb, D. J., and Brown, C. M. (2013). Fluorescence resonance energy transfer microscopy as demonstrated by measuring the activation of the serine/threonine kinase Akt. Nat. Protoc. 8, 265-281. doi: 10.1038/nprot.2012.147
    • (2013) Nat. Protoc , vol.8 , pp. 265-281
    • Broussard, J.A.1    Rappaz, B.2    Webb, D.J.3    Brown, C.M.4
  • 12
    • 0028124422 scopus 로고
    • Modulation of rhodopsin function by properties of the membrane bilayer
    • Brown, M. F. (1994). Modulation of rhodopsin function by properties of the membrane bilayer. Chem. Phys. Lipids 73, 159-180. doi: 10.1016/0009-3084(94)90180-5
    • (1994) Chem. Phys. Lipids , vol.73 , pp. 159-180
    • Brown, M.F.1
  • 13
    • 84872195772 scopus 로고    scopus 로고
    • Single-molecule analysis of fluorescently labeled G-protein-coupled receptors reveals complexes with distinct dynamics and organization
    • Calebiro, D., Rieken, F., Wagner, J., Sungkaworn, T., Zabel, U., Borzi, A., et al. (2013). Single-molecule analysis of fluorescently labeled G-protein-coupled receptors reveals complexes with distinct dynamics and organization. Proc. Natl. Acad. Sci. U.S.A. 110, 743-748. doi: 10.1073/pnas.1205798110
    • (2013) Proc. Natl. Acad. Sci. U.S.A , vol.110 , pp. 743-748
    • Calebiro, D.1    Rieken, F.2    Wagner, J.3    Sungkaworn, T.4    Zabel, U.5    Borzi, A.6
  • 14
    • 84908278525 scopus 로고    scopus 로고
    • Dimerization of the EphA1 receptor tyrosine kinase transmembrane domain: insights into the mechanism of receptor activation
    • Chavent, M., Chetwynd, A. P., Stansfeld, P. J., and Sansom, M. S. (2014). Dimerization of the EphA1 receptor tyrosine kinase transmembrane domain: insights into the mechanism of receptor activation. Biochemistry 53, 6641-6652. doi: 10.1021/bi500800x
    • (2014) Biochemistry , vol.53 , pp. 6641-6652
    • Chavent, M.1    Chetwynd, A.P.2    Stansfeld, P.J.3    Sansom, M.S.4
  • 15
    • 0024452439 scopus 로고
    • Role of the stereochemistry of the hydroxyl group of cholesterol and the formation of nonbilayer structures in phosphatidylethanolamines
    • Cheetham, J. J., Wachtel, E., Bach, D., and Epand, R. M. (1989). Role of the stereochemistry of the hydroxyl group of cholesterol and the formation of nonbilayer structures in phosphatidylethanolamines. Biochemistry 28, 8928-8934. doi: 10.1021/bi00448a036
    • (1989) Biochemistry , vol.28 , pp. 8928-8934
    • Cheetham, J.J.1    Wachtel, E.2    Bach, D.3    Epand, R.M.4
  • 16
    • 36448995359 scopus 로고    scopus 로고
    • High-resolution crystal structure of an engineered human β2-adrenergic G protein-coupled receptor
    • Cherezov, V., Rosenbaum, D. M., Hanson, M. A., Rasmussen, S. G., Thian, F. S., Kobilka, T. S., et al. (2007). High-resolution crystal structure of an engineered human β2-adrenergic G protein-coupled receptor. Science 318, 1258-1265. doi: 10.1126/science.1150577
    • (2007) Science , vol.318 , pp. 1258-1265
    • Cherezov, V.1    Rosenbaum, D.M.2    Hanson, M.A.3    Rasmussen, S.G.4    Thian, F.S.5    Kobilka, T.S.6
  • 17
    • 67649306770 scopus 로고    scopus 로고
    • G-protein-coupled receptors, cholesterol and palmitoylation: facts about fats
    • Chini, B., and Parenti, M. (2009). G-protein-coupled receptors, cholesterol and palmitoylation: facts about fats. J. Mol. Endocrinol. 42, 371-379. doi: 10.1677/JME-08-0114
    • (2009) J. Mol. Endocrinol , vol.42 , pp. 371-379
    • Chini, B.1    Parenti, M.2
  • 18
    • 84942085515 scopus 로고    scopus 로고
    • Structures for G-protein-coupled receptor tetramers in complex with G proteins
    • Cordomí, A., Navarro, G., Aymerich, M. S., and Franco, R. (2015). Structures for G-protein-coupled receptor tetramers in complex with G proteins. Trends Biochem. Sci. 40, 548-551. doi: 10.1016/j.tibs.2015.07.007
    • (2015) Trends Biochem. Sci , vol.40 , pp. 548-551
    • Cordomí, A.1    Navarro, G.2    Aymerich, M.S.3    Franco, R.4
  • 19
    • 84873155972 scopus 로고    scopus 로고
    • BRET and time-resolved FRET strategy to study GPCR oligomerization: from cell lines toward native tissues
    • Cottet, M., Faklaris, O., Maurel, D., Scholler, P., Doumazane, E., Trinquet, E., et al. (2012). BRET and time-resolved FRET strategy to study GPCR oligomerization: from cell lines toward native tissues. Front. Endocrinol. (Lausanne) 3:92. doi: 10.3389/fendo.2012.00092
    • (2012) Front. Endocrinol. (Lausanne) , vol.3 , pp. 92
    • Cottet, M.1    Faklaris, O.2    Maurel, D.3    Scholler, P.4    Doumazane, E.5    Trinquet, E.6
  • 21
    • 62649148289 scopus 로고    scopus 로고
    • Effect of cholesterol on the structure of a phospholipid bilayer
    • de Meyer, F., and Smit, B. (2009). Effect of cholesterol on the structure of a phospholipid bilayer. Proc. Natl. Acad. Sci. U.S.A. 106, 3654-3658. doi: 10.1073/pnas.0809959106
    • (2009) Proc. Natl. Acad. Sci. U.S.A , vol.106 , pp. 3654-3658
    • de Meyer, F.1    Smit, B.2
  • 22
    • 2442438851 scopus 로고    scopus 로고
    • Homo-and hetero-dimeric complex formations of the human oxytocin receptor
    • Devost, D., and Zingg, H. H. (2004). Homo-and hetero-dimeric complex formations of the human oxytocin receptor. J. Neuroendocrinol. 16, 372-377. doi: 10.1111/j.0953-8194.2004.01188.x
    • (2004) J. Neuroendocrinol , vol.16 , pp. 372-377
    • Devost, D.1    Zingg, H.H.2
  • 23
    • 33947431049 scopus 로고    scopus 로고
    • Lipid-protein interactions in GPCR-associated signaling
    • Escribá, P. V., Wedegaertner, P. B., Goñi, F. M., and Vögler, O. (2007). Lipid-protein interactions in GPCR-associated signaling. Biochim. Biophys. Acta 1768, 836-852. doi: 10.1016/j.bbamem.2006.09.001
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 836-852
    • Escribá, P.V.1    Wedegaertner, P.B.2    Goñi, F.M.3    Vögler, O.4
  • 24
    • 68749103465 scopus 로고    scopus 로고
    • Lipid raft-mediated regulation of G-protein coupled receptor signaling by ligands which influence receptor dimerization: a computational study
    • Fallahi-Sichani, M., and Linderman, J. J. (2009). Lipid raft-mediated regulation of G-protein coupled receptor signaling by ligands which influence receptor dimerization: a computational study. PLoS ONE 4:e6604. doi: 10.1371/journal.pone.0006604
    • (2009) PLoS ONE , vol.4
    • Fallahi-Sichani, M.1    Linderman, J.J.2
  • 25
    • 23044483866 scopus 로고    scopus 로고
    • Properties of docosahexaenoic-acid-containing lipids and their influence on the function of rhodopsin
    • Feller, S. E., and Gawrisch, K. (2005). Properties of docosahexaenoic-acid-containing lipids and their influence on the function of rhodopsin. Curr. Opin. Struct. Biol. 15, 416-422. doi: 10.1016/j.sbi.2005.07.002
    • (2005) Curr. Opin. Struct. Biol , vol.15 , pp. 416-422
    • Feller, S.E.1    Gawrisch, K.2
  • 26
    • 0037448883 scopus 로고    scopus 로고
    • Rhodopsin exhibits a preference for solvation by polyunsaturated docosohexaenoic acid
    • Feller, S. E., Gawrisch, K., and Woolf, T. B. (2003). Rhodopsin exhibits a preference for solvation by polyunsaturated docosohexaenoic acid. J. Am. Chem. Soc. 125, 4434-4435. doi: 10.1021/ja0345874
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 4434-4435
    • Feller, S.E.1    Gawrisch, K.2    Woolf, T.B.3
  • 27
    • 84981779372 scopus 로고
    • Zwischenmolekulare Energiewanderung und Fluoreszenz
    • Förster, T. (1948). Zwischenmolekulare Energiewanderung und Fluoreszenz. Annalen Physik 437, 55-75. doi: 10.1002/andp.19484370105
    • (1948) Annalen Physik , vol.437 , pp. 55-75
    • Förster, T.1
  • 28
    • 0037426865 scopus 로고    scopus 로고
    • Atomic-force microscopy: rhodopsin dimers in native disc membranes
    • Fotiadis, D., Liang, Y., Filipek, S., Saperstein, D. A., Engel, A., and Palczewski, K. (2003). Atomic-force microscopy: rhodopsin dimers in native disc membranes. Nature 421, 127-128. doi: 10.1038/421127a
    • (2003) Nature , vol.421 , pp. 127-128
    • Fotiadis, D.1    Liang, Y.2    Filipek, S.3    Saperstein, D.A.4    Engel, A.5    Palczewski, K.6
  • 29
    • 56449120228 scopus 로고    scopus 로고
    • Insights from biophysical studies on the role of polyunsaturated fatty acids for function of G-protein coupled membrane receptors. Prostaglandins Leukot
    • Gawrisch, K., Soubias, O., and Mihailescu, M. (2008). Insights from biophysical studies on the role of polyunsaturated fatty acids for function of G-protein coupled membrane receptors. Prostaglandins Leukot. Essent. Fatty Acids 79, 131-134. doi: 10.1016/j.plefa.2008.09.002
    • (2008) Essent. Fatty Acids , vol.79 , pp. 131-134
    • Gawrisch, K.1    Soubias, O.2    Mihailescu, M.3
  • 30
    • 84923141629 scopus 로고    scopus 로고
    • Methodological advances: the unsung heroes of the GPCR structural revolution
    • Ghosh, E., Kumari, P., Jaiman, D., and Shukla, A. K. (2015). Methodological advances: the unsung heroes of the GPCR structural revolution. Nat. Rev. Mol. Cell Biol. 16, 69-81. doi: 10.1038/nrm3933
    • (2015) Nat. Rev. Mol. Cell Biol , vol.16 , pp. 69-81
    • Ghosh, E.1    Kumari, P.2    Jaiman, D.3    Shukla, A.K.4
  • 31
    • 84975763644 scopus 로고    scopus 로고
    • Interaction of G protein coupled receptors and cholesterol
    • Gimpl, G. (2016). Interaction of G protein coupled receptors and cholesterol. Chem. Phys. Lipids 199, 61-73. doi: 10.1016/j.chemphyslip.2016.04.006
    • (2016) Chem. Phys. Lipids , vol.199 , pp. 61-73
    • Gimpl, G.1
  • 32
    • 0037206131 scopus 로고    scopus 로고
    • Cholesterol as stabilizer of the oxytocin receptor
    • Gimpl, G., and Fahrenholz, F. (2002). Cholesterol as stabilizer of the oxytocin receptor. Biochim. Biophys. Acta 1564, 384-392. doi: 10.1016/S0005-2736(02)00475-3
    • (2002) Biochim. Biophys. Acta , vol.1564 , pp. 384-392
    • Gimpl, G.1    Fahrenholz, F.2
  • 34
    • 84873205676 scopus 로고    scopus 로고
    • Contributions of fluorescence techniques to understanding G protein-coupled receptor dimerisation
    • Goddard, A. D., and Watts, A. (2012a). Contributions of fluorescence techniques to understanding G protein-coupled receptor dimerisation. Biophys. Rev. 4, 291-298. doi: 10.1007/s12551-012-0073-z
    • (2012) Biophys. Rev , vol.4 , pp. 291-298
    • Goddard, A.D.1    Watts, A.2
  • 35
    • 84858326040 scopus 로고    scopus 로고
    • Regulation of G protein-coupled receptors by palmitoylation and cholesterol
    • Goddard, A. D., and Watts, A. (2012b). Regulation of G protein-coupled receptors by palmitoylation and cholesterol. BMC Biol. 10:27. doi: 10.1186/1741-7007-10-27
    • (2012) BMC Biol , vol.10 , pp. 27
    • Goddard, A.D.1    Watts, A.2
  • 36
    • 84865228987 scopus 로고    scopus 로고
    • Computational and experimental analysis of the transmembrane domain 4/5 dimerization interface of the serotonin 5-HT(1A) receptor
    • Gorinski, N., Kowalsman, N., Renner, U., Wirth, A., Reinartz, M. T., Seifert, R., et al. (2012). 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) Mol. Pharmacol , vol.82 , pp. 448-463
    • Gorinski, N.1    Kowalsman, N.2    Renner, U.3    Wirth, A.4    Reinartz, M.T.5    Seifert, R.6
  • 37
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • Griffin, B. A., Adams, S. R., and Tsien, R. Y. (1998). Specific covalent labeling of recombinant protein molecules inside live cells. Science 281, 269-272. doi: 10.1126/science.281.5374.269
    • (1998) Science , vol.281 , pp. 269-272
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 38
    • 33645519597 scopus 로고    scopus 로고
    • A role for direct interactions in the modulation of rhodopsin by omega-3 polyunsaturated lipids
    • Grossfield, A., Feller, S. E., and Pitman, M. C. (2006a). A role for direct interactions in the modulation of rhodopsin by omega-3 polyunsaturated lipids. Proc. Natl. Acad. Sci. U.S.A. 103, 4888-4893. doi: 10.1073/pnas.0508352103
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 4888-4893
    • Grossfield, A.1    Feller, S.E.2    Pitman, M.C.3
  • 39
    • 33744803716 scopus 로고    scopus 로고
    • Contribution of omega-3 fatty acids to the thermodynamics of membrane protein solvation
    • Grossfield, A., Feller, S. E., and Pitman, M. C. (2006b). Contribution of omega-3 fatty acids to the thermodynamics of membrane protein solvation. J. Phys. Chem. B 110, 8907-8909. doi: 10.1021/jp060405r
    • (2006) J. Phys. Chem. B , vol.110 , pp. 8907-8909
    • Grossfield, A.1    Feller, S.E.2    Pitman, M.C.3
  • 40
    • 84955489920 scopus 로고    scopus 로고
    • Membrane omega-3 fatty acids modulate the oligomerisation kinetics of adenosine A2A and dopamine D2 receptors
    • Guixà-González, R., Javanainen, M., Gomez-Soler, M., Cordobilla, B., Domingo, J. C., Sanz, F., et al. (2016). Membrane omega-3 fatty acids modulate the oligomerisation kinetics of adenosine A2A and dopamine D2 receptors. Sci. Rep. 6:19839. doi: 10.1038/srep19839
    • (2016) Sci. Rep , vol.6 , pp. 19839
    • Guixà-González, R.1    Javanainen, M.2    Gomez-Soler, M.3    Cordobilla, B.4    Domingo, J.C.5    Sanz, F.6
  • 41
    • 28444493656 scopus 로고    scopus 로고
    • Crosstalk in G protein-coupled receptors: changes at the transmembrane homodimer interface determine activation
    • Guo, W., Shi, L., Filizola, M., Weinstein, H., and Javitch, J. A. (2005). Crosstalk in G protein-coupled receptors: changes at the transmembrane homodimer interface determine activation. Proc. Natl. Acad. Sci. U.S.A. 102, 17495-17500. doi: 10.1073/pnas.0508950102
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 17495-17500
    • Guo, W.1    Shi, L.2    Filizola, M.3    Weinstein, H.4    Javitch, J.A.5
  • 42
    • 84941089766 scopus 로고    scopus 로고
    • Synaptobrevin transmembrane domain dimerization studied by multiscale molecular dynamics simulations
    • Han, J., Pluhackova, K., Wassenaar, T. A., and Böckmann, R. A. (2015). Synaptobrevin transmembrane domain dimerization studied by multiscale molecular dynamics simulations. Biophys. J. 109, 760-771. doi: 10.1016/j.bpj.2015.06.049
    • (2015) Biophys. J , vol.109 , pp. 760-771
    • Han, J.1    Pluhackova, K.2    Wassenaar, T.A.3    Böckmann, R.A.4
  • 43
    • 44649172481 scopus 로고    scopus 로고
    • A specific cholesterol binding site is established by the 2.8 Å structure of the human β2-adrenergic receptor
    • Hanson, M. A., Cherezov, V., Griffith, M. T., Roth, C. B., Jaakola, V. P., Chien, E. Y., et al. (2008). A specific cholesterol binding site is established by the 2.8 Å structure of the human β2-adrenergic receptor. Structure 16, 897-905. doi: 10.1016/j.str.2008.05.001
    • (2008) Structure , vol.16 , pp. 897-905
    • Hanson, M.A.1    Cherezov, V.2    Griffith, M.T.3    Roth, C.B.4    Jaakola, V.P.5    Chien, E.Y.6
  • 44
    • 24144462378 scopus 로고    scopus 로고
    • G-protein-coupled receptor signaling components localize in both sarcolemmal and intracellular caveolin-3-associated microdomains in adult cardiac myocytes
    • Head, B. P., Patel, H. H., Roth, D. M., Lai, N. C., Niesman, I. R., Farquhar, M. G., et al. (2005). G-protein-coupled receptor signaling components localize in both sarcolemmal and intracellular caveolin-3-associated microdomains in adult cardiac myocytes. J. Biol. Chem. 280, 31036-31044. doi: 10.1074/jbc.M502540200
    • (2005) J. Biol. Chem , vol.280 , pp. 31036-31044
    • Head, B.P.1    Patel, H.H.2    Roth, D.M.3    Lai, N.C.4    Niesman, I.R.5    Farquhar, M.G.6
  • 45
    • 77954962222 scopus 로고    scopus 로고
    • Role of antibodies in developing drugs that target G-protein-coupled receptor dimers
    • Hipser, C., Bushlin, I., Gupta, A., Gomes, I., and Devi, L. A. (2010). Role of antibodies in developing drugs that target G-protein-coupled receptor dimers. Mt. Sinai J. Med. 77, 374-380. doi: 10.1002/msj.20199
    • (2010) Mt. Sinai J. Med , vol.77 , pp. 374-380
    • Hipser, C.1    Bushlin, I.2    Gupta, A.3    Gomes, I.4    Devi, L.A.5
  • 46
    • 36348983962 scopus 로고    scopus 로고
    • Agonist treatment did not affect association of mu opioid receptors with lipid rafts and cholesterol reduction had opposite effects on the receptor-mediated signaling in rat brain and CHO cells
    • Huang, P., Xu, W., Yoon, S.-I., Chen, C., Chong, P. L.-G., Unterwald, E. M., et al. (2007). Agonist treatment did not affect association of mu opioid receptors with lipid rafts and cholesterol reduction had opposite effects on the receptor-mediated signaling in rat brain and CHO cells. Brain Res. 1184, 46-56. doi: 10.1016/j.brainres.2007.09.096
    • (2007) Brain Res , vol.1184 , pp. 46-56
    • Huang, P.1    Xu, W.2    Yoon, S.-I.3    Chen, C.4    Chong, P.L.-G.5    Unterwald, E.M.6
  • 48
    • 29244466321 scopus 로고    scopus 로고
    • Imaging nanometer domains of β-adrenergic receptor complexes on the surface of cardiac myocytes
    • Ianoul, A., Grant, D. D., Rouleau, Y., Bani-Yaghoub, M., Johnston, L. J., and Pezacki, J. P. (2005). Imaging nanometer domains of β-adrenergic receptor complexes on the surface of cardiac myocytes. Nat. Chem. Biol. 1, 196-202. doi: 10.1038/nchembio726
    • (2005) Nat. Chem. Biol , vol.1 , pp. 196-202
    • Ianoul, A.1    Grant, D.D.2    Rouleau, Y.3    Bani-Yaghoub, M.4    Johnston, L.J.5    Pezacki, J.P.6
  • 49
    • 27844442717 scopus 로고    scopus 로고
    • Compartmentation of G-protein-coupled receptors and their signalling components in lipid rafts and caveolae
    • Insel, P. A., Head, B. P., Patel, H. H., Roth, D. M., Bundey, R. A., and Swaney, J. S. (2005). Compartmentation of G-protein-coupled receptors and their signalling components in lipid rafts and caveolae. Biochem. Soc. Trans. 33(Pt 5):1131-1134. doi: 10.1042/BST0331131
    • (2005) Biochem. Soc. Trans , vol.33 , pp. 1131-1134
    • Insel, P.A.1    Head, B.P.2    Patel, H.H.3    Roth, D.M.4    Bundey, R.A.5    Swaney, J.S.6
  • 50
    • 0031714513 scopus 로고    scopus 로고
    • Angiotensin II type 1 receptor: relationship with caveolae and caveolin after initial agonist stimulation
    • Ishizaka, N., Griendling, K. K., Lassègue, B., and Alexander, R. W. (1998). Angiotensin II type 1 receptor: relationship with caveolae and caveolin after initial agonist stimulation. Hypertension 32, 459-466. doi: 10.1161/01.HYP.32.3.459
    • (1998) Hypertension , vol.32 , pp. 459-466
    • Ishizaka, N.1    Griendling, K.K.2    Lassègue, B.3    Alexander, R.W.4
  • 51
    • 84887846612 scopus 로고    scopus 로고
    • Stereospecific requirement of cholesterol in the function of the serotonin1A receptor
    • Jafurulla, M., Rao, B. D., Sreedevi, S., Ruysschaert, J. M., Covey, D. F., and Chattopadhyay, A. (2014). Stereospecific requirement of cholesterol in the function of the serotonin1A receptor. Biochim. Biophys. Acta 1838(1 Pt B):158-163. doi: 10.1016/j.bbamem.2013.08.015
    • (2014) Biochim. Biophys. Acta , vol.1838 , Issue.1 , pp. 158-163
    • Jafurulla, M.1    Rao, B.D.2    Sreedevi, S.3    Ruysschaert, J.M.4    Covey, D.F.5    Chattopadhyay, A.6
  • 52
    • 78650919372 scopus 로고    scopus 로고
    • Identification of cholesterol recognition amino acid consensus (CRAC) motif in G-protein coupled receptors
    • Jafurulla, M., Tiwari, S., and Chattopadhyay, A. (2011). Identification of cholesterol recognition amino acid consensus (CRAC) motif in G-protein coupled receptors. Biochem. Biophys. Res. Commun. 404, 569-573. doi: 10.1016/j.bbrc.2010.12.031
    • (2011) Biochem. Biophys. Res. Commun , vol.404 , pp. 569-573
    • Jafurulla, M.1    Tiwari, S.2    Chattopadhyay, A.3
  • 53
    • 84944464034 scopus 로고    scopus 로고
    • Disruption of rhodopsin dimerization with synthetic peptides targeting an interaction interface
    • Jastrzebska, B., Chen, Y., Orban, T., Jin, H., Hofmann, L., and Palczewski, K. (2015). Disruption of rhodopsin dimerization with synthetic peptides targeting an interaction interface. J. Biol. Chem. 290, 25728-25744. doi: 10.1074/jbc.M115.662684
    • (2015) J. Biol. Chem , vol.290 , pp. 25728-25744
    • Jastrzebska, B.1    Chen, Y.2    Orban, T.3    Jin, H.4    Hofmann, L.5    Palczewski, K.6
  • 54
    • 0033578005 scopus 로고    scopus 로고
    • G-protein-coupled receptor heterodimerization modulates receptor function
    • Jordan, B. A., and Devi, L. A. (1999). G-protein-coupled receptor heterodimerization modulates receptor function. Nature 399, 697-700. doi: 10.1038/21441
    • (1999) Nature , vol.399 , pp. 697-700
    • Jordan, B.A.1    Devi, L.A.2
  • 55
    • 84926467217 scopus 로고    scopus 로고
    • Multi-component protein-protein docking based protocol with external scoring for modeling dimers of G protein-coupled receptors
    • Kaczor, A. A., Guixà0-González, R., Carrió, P., Poso, A., Dove, S., Pastor, M., et al. (2015). Multi-component protein-protein docking based protocol with external scoring for modeling dimers of G protein-coupled receptors. Mol. Inform. 34, 246-255. doi: 10.1002/minf.201400088
    • (2015) Mol. Inform , vol.34 , pp. 246-255
    • Kaczor, A.A.1    Guixà-González, R.2    Carrió, P.3    Poso, A.4    Dove, S.5    Pastor, M.6
  • 56
    • 84890612981 scopus 로고    scopus 로고
    • Single-molecule imaging revealed dynamic GPCR dimerization
    • Kasai, R. S., and Kusumi, A. (2014). Single-molecule imaging revealed dynamic GPCR dimerization. Curr. Opin. Cell Biol. 27, 78-86. doi: 10.1016/j.ceb.2013.11.008
    • (2014) Curr. Opin. Cell Biol , vol.27 , pp. 78-86
    • Kasai, R.S.1    Kusumi, A.2
  • 57
    • 84855799592 scopus 로고    scopus 로고
    • Diversity and modularity of G protein-coupled receptor structures
    • Katritsch, V., Cherezov, V., and Stevens, R. C. (2012). Diversity and modularity of G protein-coupled receptor structures. Trends Pharmacol. Sci. 33, 17-27. doi: 10.1016/j.tips.2011.09.003
    • (2012) Trends Pharmacol. Sci , vol.33 , pp. 17-27
    • Katritsch, V.1    Cherezov, V.2    Stevens, R.C.3
  • 58
    • 0031740415 scopus 로고    scopus 로고
    • Hydrophobic mismatch between proteins and lipids in membranes
    • Killian, J. (1998). Hydrophobic mismatch between proteins and lipids in membranes. BBA Rev. Biomembr. 1376, 401-416. doi: 10.1016/s0304-4157(98)00017-3
    • (1998) BBA Rev. Biomembr , vol.1376 , pp. 401-416
    • Killian, J.1
  • 59
    • 84925371859 scopus 로고    scopus 로고
    • Uncovering the triggers for GPCR activation using solid-state NMR spectroscopy
    • Kimata, N., Reeves, P. J., and Smith, S. O. (2015). Uncovering the triggers for GPCR activation using solid-state NMR spectroscopy. J. Magn. Reson. 253, 111-118. doi: 10.1016/j.jmr.2014.12.014
    • (2015) J. Magn. Reson , vol.253 , pp. 111-118
    • Kimata, N.1    Reeves, P.J.2    Smith, S.O.3
  • 60
    • 0028812541 scopus 로고
    • Alteration of the myometrial plasma membrane cholesterol content with beta-cyclodextrin modulates the binding affinity of the oxytocin receptor
    • Klein, U., Gimpl, G., and Fahrenholz, F. (1995). Alteration of the myometrial plasma membrane cholesterol content with beta-cyclodextrin modulates the binding affinity of the oxytocin receptor. Biochemistry 34, 13784-13793. doi: 10.1021/bi00042a009
    • (1995) Biochemistry , vol.34 , pp. 13784-13793
    • Klein, U.1    Gimpl, G.2    Fahrenholz, F.3
  • 61
    • 79951854466 scopus 로고    scopus 로고
    • Dimers and beyond: the functional puzzles of class C GPCRs
    • Kniazeff, J., Prezeau, L., Rondard, P., Pin, J. P., and Goudet, C. (2011). Dimers and beyond: the functional puzzles of class C GPCRs. Pharmacol. Ther. 130, 9-25. doi: 10.1016/j.pharmthera.2011.01.006
    • (2011) Pharmacol. Ther , vol.130 , pp. 9-25
    • Kniazeff, J.1    Prezeau, L.2    Rondard, P.3    Pin, J.P.4    Goudet, C.5
  • 62
    • 46549088643 scopus 로고    scopus 로고
    • Stimulation-and palmitoylation-dependent changes in oligomeric conformation of serotonin 5-HT1A receptors
    • Kobe, F., Renner, U., Woehler, A., Wlodarczyk, J., Papusheva, E., Bao, G., et al. (2008). Stimulation-and palmitoylation-dependent changes in oligomeric conformation of serotonin 5-HT1A receptors. Biochim. Biophys. Acta 1783, 1503-1516. doi: 10.1016/j.bbamcr.2008.02.021
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 1503-1516
    • Kobe, F.1    Renner, U.2    Woehler, A.3    Wlodarczyk, J.4    Papusheva, E.5    Bao, G.6
  • 63
    • 33947356279 scopus 로고    scopus 로고
    • G protein coupled receptor structure and activation
    • Kobilka, B. K. (2007). G protein coupled receptor structure and activation. Biochim. Biophys. Acta 1768, 794-807. doi: 10.1016/j.bbamem.2006.10.021
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 794-807
    • Kobilka, B.K.1
  • 64
  • 65
    • 84961590011 scopus 로고    scopus 로고
    • The function of the two-pore channel TPC1 depends on dimerization of its carboxy-terminal helix
    • Larisch, N., Kirsch, S. A., Schambony, A., Studtrucker, T., Böckmann, R. A., and Dietrich, P. (2016). The function of the two-pore channel TPC1 depends on dimerization of its carboxy-terminal helix. Cell. Mol. Life Sci. 73, 2565-2581. doi: 10.1007/s00018-016-2131-3
    • (2016) Cell. Mol. Life Sci , vol.73 , pp. 2565-2581
    • Larisch, N.1    Kirsch, S.A.2    Schambony, A.3    Studtrucker, T.4    Böckmann, R.A.5    Dietrich, P.6
  • 66
    • 84855437583 scopus 로고    scopus 로고
    • The role of membrane thickness in charged protein-lipid interactions
    • Li, L. B., Vorobyov, I., and Allen, T. W. (2012). The role of membrane thickness in charged protein-lipid interactions. Biochim. Biophys. Acta 1818, 135-145. doi: 10.1016/j.bbamem.2011.10.026
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 135-145
    • Li, L.B.1    Vorobyov, I.2    Allen, T.W.3
  • 67
    • 0036528357 scopus 로고    scopus 로고
    • Homodimerization of human μ-opioid receptor overexpressed in Sf9 insect cells
    • Li-Wei, C., Can, G., De-He, Z., Qiang, W., Xue-Jun, X., Jie, C., et al. (2002). Homodimerization of human μ-opioid receptor overexpressed in Sf9 insect cells. Protein Pept. Lett. 9, 145-152. doi: 10.2174/0929866023408850
    • (2002) Protein Pept. Lett , vol.9 , pp. 145-152
    • Li-Wei, C.1    Can, G.2    De-He, Z.3    Qiang, W.4    Xue-Jun, X.5    Jie, C.6
  • 68
    • 84862776738 scopus 로고    scopus 로고
    • Biased signaling pathways in β2-adrenergic receptor characterized by 19F-NMR
    • Liu, J. J., Horst, R., Katritch, V., Stevens, R. C., and Wüthrich, K. (2012a). Biased signaling pathways in β2-adrenergic receptor characterized by 19F-NMR. Science 335, 1106-1110. doi: 10.1126/science.1215802
    • (2012) Science , vol.335 , pp. 1106-1110
    • Liu, J.J.1    Horst, R.2    Katritch, V.3    Stevens, R.C.4    Wüthrich, K.5
  • 69
    • 84861961427 scopus 로고    scopus 로고
    • Structural basis for allosteric regulation of GPCRs by sodium ions
    • Liu, W., Chun, E., Thompson, A. A., Chubukov, P., Xu, F., Katritch, V., et al. (2012b). Structural basis for allosteric regulation of GPCRs by sodium ions. Science 337, 232-236. doi: 10.1126/science.1219218
    • (2012) Science , vol.337 , pp. 232-236
    • Liu, W.1    Chun, E.2    Thompson, A.A.3    Chubukov, P.4    Xu, F.5    Katritch, V.6
  • 70
    • 84858203893 scopus 로고    scopus 로고
    • Fluorescence/bioluminescence resonance energy transfer techniques to study G-protein-coupled receptor activation and signaling
    • Lohse, M., Nuber, S., and Hoffmann, C. (2012). Fluorescence/bioluminescence resonance energy transfer techniques to study G-protein-coupled receptor activation and signaling. Pharmacol. Rev. 64, 299-336. doi: 10.1124/pr.110.004309
    • (2012) Pharmacol. Rev , vol.64 , pp. 299-336
    • Lohse, M.1    Nuber, S.2    Hoffmann, C.3
  • 71
    • 71049163000 scopus 로고    scopus 로고
    • A role for a specific cholesterol interaction in stabilizing the Apo configuration of the human A2A adenosine receptor
    • Lyman, E., Higgs, C., Kim, B., Lupyan, D., Shelley, J. C., Farid, R., et al. (2009). A role for a specific cholesterol interaction in stabilizing the Apo configuration of the human A2A adenosine receptor. Structure 17, 1660-1668. doi: 10.1016/j.str.2009.10.010
    • (2009) Structure , vol.17 , pp. 1660-1668
    • Lyman, E.1    Higgs, C.2    Kim, B.3    Lupyan, D.4    Shelley, J.C.5    Farid, R.6
  • 72
    • 48749126827 scopus 로고    scopus 로고
    • Ligand sensitivity in dimeric associations of the serotonin 5HT2c receptor
    • Mancia, F., Assur, Z., Herman, A. G., Siegel, R., and Hendrickson, W. A. (2008). Ligand sensitivity in dimeric associations of the serotonin 5HT2c receptor. EMBO Rep. 9, 363-369. doi: 10.1038/embor.2008.27
    • (2008) EMBO Rep , vol.9 , pp. 363-369
    • Mancia, F.1    Assur, Z.2    Herman, A.G.3    Siegel, R.4    Hendrickson, W.A.5
  • 73
    • 84861096654 scopus 로고    scopus 로고
    • Crystal structure of the μ-opioid receptor bound to a morphinan antagonist
    • Manglik, A., Kruse, A. C., Kobilka, T. S., Thian, F. S., Mathiesen, J. M., Sunahara, R. K., et al. (2012). Crystal structure of the μ-opioid receptor bound to a morphinan antagonist. Nature 485, 321-326. doi: 10.1038/nature10954
    • (2012) Nature , vol.485 , pp. 321-326
    • Manglik, A.1    Kruse, A.C.2    Kobilka, T.S.3    Thian, F.S.4    Mathiesen, J.M.5    Sunahara, R.K.6
  • 74
    • 1642485164 scopus 로고    scopus 로고
    • Coarse grained model for semiquantitative lipid simulations
    • Marrink, S. J., de Vries, A. H., and Mark, A. E. (2004). Coarse grained model for semiquantitative lipid simulations. J. Phys. Chem. B 108, 750-760. doi: 10.1021/jp036508g
    • (2004) J. Phys. Chem. B , vol.108 , pp. 750-760
    • Marrink, S.J.1    de Vries, A.H.2    Mark, A.E.3
  • 75
    • 34547474332 scopus 로고    scopus 로고
    • The MARTINI force field: Coarse grained model for biomolecular simulations
    • Marrink, S. J., Risselada, H. J., Yefimov, S., Tieleman, D. P., and de Vries, A. H. (2007). The MARTINI force field: Coarse grained model for biomolecular simulations. J. Phys. Chem. B 111, 7812-7824. doi: 10.1021/jp071097f
    • (2007) J. Phys. Chem. B , vol.111 , pp. 7812-7824
    • Marrink, S.J.1    Risselada, H.J.2    Yefimov, S.3    Tieleman, D.P.4    de Vries, A.H.5
  • 76
    • 84882398607 scopus 로고    scopus 로고
    • Perspective on the Martini model
    • Marrink, S. J., and Tieleman, D. P. (2013). Perspective on the Martini model. Chem. Soc. Rev. 42, 6801-6822. doi: 10.1039/c3cs60093a
    • (2013) Chem. Soc. Rev , vol.42 , pp. 6801-6822
    • Marrink, S.J.1    Tieleman, D.P.2
  • 77
    • 84930983678 scopus 로고    scopus 로고
    • Computational approaches for modeling GPCR dimerization
    • Meng, X. Y., Mezei, M., and Cui, M. (2014). Computational approaches for modeling GPCR dimerization. Curr. Pharm. Biotechnol. 15, 996-1006. doi: 10.2174/1389201015666141013102515
    • (2014) Curr. Pharm. Biotechnol , vol.15 , pp. 996-1006
    • Meng, X.Y.1    Mezei, M.2    Cui, M.3
  • 78
    • 0031881028 scopus 로고    scopus 로고
    • Molecular order and dynamics in bilayers consisting of highly polyunsaturated phospholipids
    • Mitchell, D. C., and Litman, B. J. (1998). Molecular order and dynamics in bilayers consisting of highly polyunsaturated phospholipids. Biophys. J. 74(2 Pt 1):879-891. doi: 10.1016/S0006-3495(98)74011-1
    • (1998) Biophys. J , vol.74 , Issue.2 , pp. 879-891
    • Mitchell, D.C.1    Litman, B.J.2
  • 79
    • 0037633103 scopus 로고    scopus 로고
    • Enhancement of G protein-coupled signaling by DHA phospholipids
    • Mitchell, D. C., Niu, S. L., and Litman, B. J. (2003). Enhancement of G protein-coupled signaling by DHA phospholipids. Lipids 38, 437-443. doi: 10.1007/s11745-003-1081-1
    • (2003) Lipids , vol.38 , pp. 437-443
    • Mitchell, D.C.1    Niu, S.L.2    Litman, B.J.3
  • 81
    • 80455164853 scopus 로고    scopus 로고
    • Quantitative modeling of membrane deformations by multihelical membrane proteins: application to G-protein coupled receptors
    • Mondal, S., Khelashvili, G., Shan, J., Andersen, O. S., and Weinstein, H. (2011). Quantitative modeling of membrane deformations by multihelical membrane proteins: application to G-protein coupled receptors. Biophys. J. 101, 2092-2101. doi: 10.1016/j.bpj.2011.09.037
    • (2011) Biophys. J , vol.101 , pp. 2092-2101
    • Mondal, S.1    Khelashvili, G.2    Shan, J.3    Andersen, O.S.4    Weinstein, H.5
  • 83
    • 84882754080 scopus 로고    scopus 로고
    • Membrane protein-lipid match and mismatch
    • ed E. H. Egelman (Amsterdam: Humana Press)
    • Mouritsen, O. G. (2013). "Membrane protein-lipid match and mismatch," in Comprehensive Biophysics, Vol. 5, ed E. H. Egelman (Amsterdam: Humana Press), 245-260.
    • (2013) Comprehensive Biophysics , vol.5 , pp. 245-260
    • Mouritsen, O.G.1
  • 84
    • 79960284935 scopus 로고    scopus 로고
    • Cholesterol-induced conformational changes in the oxytocin receptor
    • Muth, S., Fries, A., and Gimpl, G. (2011). Cholesterol-induced conformational changes in the oxytocin receptor. Biochem. J. 437, 541-553. doi: 10.1042/BJ20101795
    • (2011) Biochem. J , vol.437 , pp. 541-553
    • Muth, S.1    Fries, A.2    Gimpl, G.3
  • 85
    • 84874275263 scopus 로고    scopus 로고
    • Receptor oligomerization: from early evidence to current understanding in class B GPCRs
    • Ng, S. Y., Lee, L. T., and Chow, B. K. (2012). Receptor oligomerization: from early evidence to current understanding in class B GPCRs. Front. Endocrinol. (Lausanne) 3:175. doi: 10.3389/fendo.2012.00175
    • (2012) Front. Endocrinol. (Lausanne) , vol.3 , pp. 175
    • Ng, S.Y.1    Lee, L.T.2    Chow, B.K.3
  • 86
    • 0037090162 scopus 로고    scopus 로고
    • CXCR4 function requires membrane cholesterol: implications for HIV infection
    • Nguyen, D. H., and Taub, D. (2002). CXCR4 function requires membrane cholesterol: implications for HIV infection. J. Immunol. 168, 4121-4126. doi: 10.4049/jimmunol.168.8.4121
    • (2002) J. Immunol , vol.168 , pp. 4121-4126
    • Nguyen, D.H.1    Taub, D.2
  • 87
    • 0242270621 scopus 로고    scopus 로고
    • Inhibition of chemokine receptor function by membrane cholesterol oxidation
    • Nguyen, D. H., and Taub, D. D. (2003). Inhibition of chemokine receptor function by membrane cholesterol oxidation. Exp. Cell Res. 291, 36-45. doi: 10.1016/S0014-4827(03)00345-8
    • (2003) Exp. Cell Res , vol.291 , pp. 36-45
    • Nguyen, D.H.1    Taub, D.D.2
  • 88
    • 3843115666 scopus 로고    scopus 로고
    • Reduced G protein-coupled signaling efficiency in retinal rod outer segments in response to n-3 fatty acid deficiency
    • Niu, S. L., Mitchell, D. C., Lim, S. Y., Wen, Z. M., Kim, H. Y., Salem, N., et al. (2004). Reduced G protein-coupled signaling efficiency in retinal rod outer segments in response to n-3 fatty acid deficiency. J. Biol. Chem. 279, 31098-31104. doi: 10.1074/jbc.M404376200
    • (2004) J. Biol. Chem , vol.279 , pp. 31098-31104
    • Niu, S.L.1    Mitchell, D.C.2    Lim, S.Y.3    Wen, Z.M.4    Kim, H.Y.5    Salem, N.6
  • 89
    • 82955248059 scopus 로고    scopus 로고
    • Uncovering the intimate relationship between lipids, cholesterol and GPCR activation
    • Oates, J., and Watts, A. (2011). Uncovering the intimate relationship between lipids, cholesterol and GPCR activation. Curr. Opin. Struct. Biol. 21, 802-807. doi: 10.1016/j.sbi.2011.09.007
    • (2011) Curr. Opin. Struct. Biol , vol.21 , pp. 802-807
    • Oates, J.1    Watts, A.2
  • 90
    • 4744346615 scopus 로고    scopus 로고
    • The evolving role of lipid rafts and caveolae in G protein-coupled receptor signaling: implications for molecular pharmacology
    • Ostrom, R. S., and Insel, P. A. (2004). The evolving role of lipid rafts and caveolae in G protein-coupled receptor signaling: implications for molecular pharmacology. Br. J. Pharmacol. 143, 235-245. doi: 10.1038/sj.bjp.0705930
    • (2004) Br. J. Pharmacol , vol.143 , pp. 235-245
    • Ostrom, R.S.1    Insel, P.A.2
  • 91
    • 0033943654 scopus 로고    scopus 로고
    • Stoichiometry and compartmentation in G protein-coupled receptor signaling: implications for therapeutic interventions involving G(s)
    • Ostrom, R. S., Post, S. R., and Insel, P. A. (2000). Stoichiometry and compartmentation in G protein-coupled receptor signaling: implications for therapeutic interventions involving G(s). J. Pharmacol. Exp. Ther. 294, 407-412.
    • (2000) J. Pharmacol. Exp. Ther , vol.294 , pp. 407-412
    • Ostrom, R.S.1    Post, S.R.2    Insel, P.A.3
  • 92
    • 80053425487 scopus 로고    scopus 로고
    • Oligomerization of the serotonin(1A) receptor in live cells: a time-resolved fluorescence anisotropy approach
    • Paila, Y. D., Kombrabail, M., Krishnamoorthy, G., and Chattopadhyay, A. (2011). Oligomerization of the serotonin(1A) receptor in live cells: a time-resolved fluorescence anisotropy approach. J. Phys. Chem. B 115, 11439-11447. doi: 10.1021/jp201458h
    • (2011) J. Phys. Chem. B , vol.115 , pp. 11439-11447
    • Paila, Y.D.1    Kombrabail, M.2    Krishnamoorthy, G.3    Chattopadhyay, A.4
  • 93
    • 0034604451 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: a G protein-coupled receptor
    • Palczewski, K., Kumasaka, T., Hori, T., Behnke, C. A., Motoshima, H., Fox, B. A., et al. (2000). Crystal structure of rhodopsin: a G protein-coupled receptor. Science 289, 739-745. doi: 10.1126/science.289.5480.739
    • (2000) Science , vol.289 , pp. 739-745
    • Palczewski, K.1    Kumasaka, T.2    Hori, T.3    Behnke, C.A.4    Motoshima, H.5    Fox, B.A.6
  • 94
    • 0942298112 scopus 로고    scopus 로고
    • The 5-hydroxytryptamine(1A) receptor is stably palmitoylated, and acylation is critical for communication of receptor with Gi protein
    • Papoucheva, E., Dumuis, A., Sebben, M., Richter, D. W., and Ponimaskin, E. G. (2004). The 5-hydroxytryptamine(1A) receptor is stably palmitoylated, and acylation is critical for communication of receptor with Gi protein. J. Biol. Chem. 279, 3280-3291. doi: 10.1074/jbc.M308177200
    • (2004) J. Biol. Chem , vol.279 , pp. 3280-3291
    • Papoucheva, E.1    Dumuis, A.2    Sebben, M.3    Richter, D.W.4    Ponimaskin, E.G.5
  • 95
    • 0041920691 scopus 로고    scopus 로고
    • Multiple determinants for rapid agonist-induced internalization of a nonmammalian gonadotropin-releasing hormone receptor: a putative palmitoylation site and threonine doublet within the carboxyl-terminal tail Are critical
    • Pawson, A. J., Maudsley, S. R., Lopes, J., Katz, A. A., Sun, Y. M., Davidson, J. S., et al. (2003). Multiple determinants for rapid agonist-induced internalization of a nonmammalian gonadotropin-releasing hormone receptor: a putative palmitoylation site and threonine doublet within the carboxyl-terminal tail Are critical. Endocrinology 144, 3860-3871. doi: 10.1210/en.2003-0028
    • (2003) Endocrinology , vol.144 , pp. 3860-3871
    • Pawson, A.J.1    Maudsley, S.R.2    Lopes, J.3    Katz, A.A.4    Sun, Y.M.5    Davidson, J.S.6
  • 96
    • 15444377047 scopus 로고    scopus 로고
    • Bioluminescence resonance energy transfer reveals ligand-induced conformational changes in CXCR4 homo-and heterodimers
    • Percherancier, Y., Berchiche, Y. A., Slight, I., Volkmer-Engert, R., Tamamura, H., Fujii, N., et al. (2005). Bioluminescence resonance energy transfer reveals ligand-induced conformational changes in CXCR4 homo-and heterodimers. J. Biol. Chem. 280, 9895-9903. doi: 10.1210/en.2003-0028
    • (2005) J. Biol. Chem , vol.280 , pp. 9895-9903
    • Percherancier, Y.1    Berchiche, Y.A.2    Slight, I.3    Volkmer-Engert, R.4    Tamamura, H.5    Fujii, N.6
  • 97
    • 84910633308 scopus 로고    scopus 로고
    • A functional selectivity mechanism at the serotonin-2A GPCR involves ligand-dependent conformations of intracellular loop 2
    • Perez-Aguilar, J. M., Shan, J., LeVine, M. V., Khelashvili, G., and Weinstein, H. (2014). A functional selectivity mechanism at the serotonin-2A GPCR involves ligand-dependent conformations of intracellular loop 2. J. Am. Chem. Soc. 136, 16044-16054. doi: 10.1021/ja508394x
    • (2014) J. Am. Chem. Soc , vol.136 , pp. 16044-16054
    • Perez-Aguilar, J.M.1    Shan, J.2    LeVine, M.V.3    Khelashvili, G.4    Weinstein, H.5
  • 98
    • 34548146523 scopus 로고    scopus 로고
    • G protein-coupled receptors self-assemble in dynamics simulations of model bilayers
    • Periole, X., Huber, T., Marrink, S. J., and Sakmar, T. P. (2007). G protein-coupled receptors self-assemble in dynamics simulations of model bilayers. J. Am. Chem. Soc. 129, 10126-10132. doi: 10.1021/ja0706246
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 10126-10132
    • Periole, X.1    Huber, T.2    Marrink, S.J.3    Sakmar, T.P.4
  • 99
    • 42449160533 scopus 로고    scopus 로고
    • Molecular recognition of parathyroid hormone by its G protein-coupled receptor
    • Pioszak, A. A., and Xu, H. E. (2008). Molecular recognition of parathyroid hormone by its G protein-coupled receptor. Proc. Natl. Acad. Sci. U.S.A. 105, 5034-5039. doi: 10.1073/pnas.0801027105
    • (2008) Proc. Natl. Acad. Sci. U.S.A , vol.105 , pp. 5034-5039
    • Pioszak, A.A.1    Xu, H.E.2
  • 100
    • 16844365398 scopus 로고    scopus 로고
    • Role of cholesterol and polyunsaturated chains in lipid-protein interactions: molecular dynamics simulation of rhodopsin in a realistic membrane environment
    • Pitman, M. C., Grossfield, A., Suits, F., and Feller, S. E. (2005). Role of cholesterol and polyunsaturated chains in lipid-protein interactions: molecular dynamics simulation of rhodopsin in a realistic membrane environment. J. Am. Chem. Soc. 127, 4576-4577. doi: 10.1021/ja042715y
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 4576-4577
    • Pitman, M.C.1    Grossfield, A.2    Suits, F.3    Feller, S.E.4
  • 101
    • 84938152514 scopus 로고    scopus 로고
    • Biomembranes in atomistic and coarse-grained simulations
    • Pluhackova, K., and Böckmann, R. A. (2015). Biomembranes in atomistic and coarse-grained simulations. J. Phys. Condens. Matter 27:323103. doi: 10.1088/0953-8984/27/32/323103
    • (2015) J. Phys. Condens. Matter , vol.27 , pp. 323103
    • Pluhackova, K.1    Böckmann, R.A.2
  • 102
    • 84999683667 scopus 로고    scopus 로고
    • Dynamic cholesterol-conditioned dimerization of the G protein coupled chemokine receptor type 4
    • Pluhackova, K., Gahbauer, S., Kranz, F., Wassenaar, T. A., and Böckmann, R. A. (2016). Dynamic cholesterol-conditioned dimerization of the G protein coupled chemokine receptor type 4. PLoS Comput. Biol. 12:e1005169.
    • (2016) PLoS Comput. Biol , vol.12
    • Pluhackova, K.1    Gahbauer, S.2    Kranz, F.3    Wassenaar, T.A.4    Böckmann, R.A.5
  • 103
    • 84884181332 scopus 로고    scopus 로고
    • Molecular dynamics simulations of membrane proteins
    • eds D. Rapaport and J. M. Herrmann (New York, NY: Humana Press)
    • Pluhackova, K., Wassenaar, T. A., and Böckmann, R. A. (2013). "Molecular dynamics simulations of membrane proteins," in Membrane Biogenesis, Volume 1033 of Methods in Molecular Biology, eds D. Rapaport and J. M. Herrmann (New York, NY: Humana Press), 85-101.
    • (2013) Membrane Biogenesis of Methods in Molecular Biology , vol.1033 , pp. 85-101
    • Pluhackova, K.1    Wassenaar, T.A.2    Böckmann, R.A.3
  • 104
    • 84925957020 scopus 로고    scopus 로고
    • Spontaneous adsorption of coiled-coil model peptides K and E to a mixed lipid bilayer
    • Pluhackova, K., Wassenaar, T. A., Kirsch, S. A., and Böckmann, R. A. (2015). Spontaneous adsorption of coiled-coil model peptides K and E to a mixed lipid bilayer. J. Phys. Chem. B 119, 4396-4408. doi: 10.1021/acs.jpcb.5b00434
    • (2015) J. Phys. Chem. B , vol.119 , pp. 4396-4408
    • Pluhackova, K.1    Wassenaar, T.A.2    Kirsch, S.A.3    Böckmann, R.A.4
  • 105
    • 0037169528 scopus 로고    scopus 로고
    • The 5-hydroxytryptamine(4a) receptor is palmitoylated at two different sites, and acylation is critically involved in regulation of receptor constitutive activity
    • Ponimaskin, E. G., Heine, M., Joubert, L., Sebben, M., Bickmeyer, U., Richter, D. W., et al. (2002). The 5-hydroxytryptamine(4a) receptor is palmitoylated at two different sites, and acylation is critically involved in regulation of receptor constitutive activity. J. Biol. Chem. 277, 2534-2546. doi: 10.1074/jbc.M106529200
    • (2002) J. Biol. Chem , vol.277 , pp. 2534-2546
    • Ponimaskin, E.G.1    Heine, M.2    Joubert, L.3    Sebben, M.4    Bickmeyer, U.5    Richter, D.W.6
  • 106
    • 54049106162 scopus 로고    scopus 로고
    • Cholesterol-dependent separation of the β2-adrenergic receptor from its partners determines signaling efficacy: insight into nanoscale organization of signal transduction
    • Pontier, S. M., Percherancier, Y., Galandrin, S., Breit, A., Gales, C., and Bouvier, M. (2008). Cholesterol-dependent separation of the β2-adrenergic receptor from its partners determines signaling efficacy: insight into nanoscale organization of signal transduction. J. Biol. Chem. 283, 24659-24672. doi: 10.1074/jbc.M800778200
    • (2008) J. Biol. Chem , vol.283 , pp. 24659-24672
    • Pontier, S.M.1    Percherancier, Y.2    Galandrin, S.3    Breit, A.4    Gales, C.5    Bouvier, M.6
  • 107
    • 78649902582 scopus 로고    scopus 로고
    • Self-association of models of transmembrane domains of ErbB receptors in a lipid bilayer
    • Prakash, A., Janosi, L., and Doxastakis, M. (2010). Self-association of models of transmembrane domains of ErbB receptors in a lipid bilayer. Biophys. J. 99, 3657-3665. doi: 10.1016/j.bpj.2010.10.023
    • (2010) Biophys. J , vol.99 , pp. 3657-3665
    • Prakash, A.1    Janosi, L.2    Doxastakis, M.3
  • 108
    • 84896539831 scopus 로고    scopus 로고
    • Cholesterol modulates the dimer interface of the β2-adrenergic receptor via cholesterol occupancy sites
    • Prasanna, X., Chattopadhyay, A., and Sengupta, D. (2014). Cholesterol modulates the dimer interface of the β2-adrenergic receptor via cholesterol occupancy sites. Biophys. J. 106, 1290-1300. doi: 10.1016/j.bpj.2014.02.002
    • (2014) Biophys. J , vol.106 , pp. 1290-1300
    • Prasanna, X.1    Chattopadhyay, A.2    Sengupta, D.3
  • 109
    • 23944501304 scopus 로고    scopus 로고
    • Heterodimerization of G protein-coupled receptors: specificity and functional significance
    • Prinster, S. C., Hague, C., and Hall, R. A. (2005). Heterodimerization of G protein-coupled receptors: specificity and functional significance. Pharmacol. Rev. 57, 289-298. doi: 10.1124/pr.57.3.1
    • (2005) Pharmacol. Rev , vol.57 , pp. 289-298
    • Prinster, S.C.1    Hague, C.2    Hall, R.A.3
  • 110
    • 84926360598 scopus 로고    scopus 로고
    • Preferred supramolecular organization and dimer interfaces of opioid receptors from simulated self-association
    • Provasi, D., Boz, M. B., Johnston, J. M., and Filizola, M. (2015). Preferred supramolecular organization and dimer interfaces of opioid receptors from simulated self-association. PLoS Comput. Biol. 11:e1004148. doi: 10.1371/journal.pcbi.1004148
    • (2015) PLoS Comput. Biol , vol.11
    • Provasi, D.1    Boz, M.B.2    Johnston, J.M.3    Filizola, M.4
  • 111
    • 0038757730 scopus 로고    scopus 로고
    • Role of palmitoylation/depalmitoylation reactions in G-protein-coupled receptor function
    • Qanbar, R., and Bouvier, M. (2003). Role of palmitoylation/depalmitoylation reactions in G-protein-coupled receptor function. Pharmacol. Ther. 97, 1-33. doi: 10.1016/S0163-7258(02)00300-5
    • (2003) Pharmacol. Ther , vol.97 , pp. 1-33
    • Qanbar, R.1    Bouvier, M.2
  • 112
    • 79959292418 scopus 로고    scopus 로고
    • Cholesterol regulates μ-opioid receptor-induced β-arrestin 2 translocation to membrane lipid rafts
    • Qiu, Y., Wang, Y., Law, P. Y., Chen, H. Z., and Loh, H. H. (2011). Cholesterol regulates μ-opioid receptor-induced β-arrestin 2 translocation to membrane lipid rafts. Mol. Pharmacol. 80, 210-218. doi: 10.1124/mol.110.070870
    • (2011) Mol. Pharmacol , vol.80 , pp. 210-218
    • Qiu, Y.1    Wang, Y.2    Law, P.Y.3    Chen, H.Z.4    Loh, H.H.5
  • 113
    • 36248970132 scopus 로고    scopus 로고
    • Crystal structure of the human β2 adrenergic G-protein-coupled receptor
    • Rasmussen, S. G., Choi, H. J., Rosenbaum, D. M., Kobilka, T. S., Thian, F. S., Edwards, P. C., et al. (2007). Crystal structure of the human β2 adrenergic G-protein-coupled receptor. Nature 450, 383-387. doi: 10.1038/nature06325
    • (2007) Nature , vol.450 , pp. 383-387
    • Rasmussen, S.G.1    Choi, H.J.2    Rosenbaum, D.M.3    Kobilka, T.S.4    Thian, F.S.5    Edwards, P.C.6
  • 114
    • 34548303255 scopus 로고    scopus 로고
    • Localization of the mouse 5-hydroxytryptamine(1A) receptor in lipid microdomains depends on its palmitoylation and is involved in receptor-mediated signaling
    • Renner, U., Glebov, K., Lang, T., Papusheva, E., Balakrishnan, S., Keller, B., et al. (2007). Localization of the mouse 5-hydroxytryptamine(1A) receptor in lipid microdomains depends on its palmitoylation and is involved in receptor-mediated signaling. Mol. Pharmacol. 72, 502-513. doi: 10.1124/mol.107.037085
    • (2007) Mol. Pharmacol , vol.72 , pp. 502-513
    • Renner, U.1    Glebov, K.2    Lang, T.3    Papusheva, E.4    Balakrishnan, S.5    Keller, B.6
  • 115
    • 84910019812 scopus 로고    scopus 로고
    • Cholesterol, sphingolipids, and glycolipids: what do we know about their role in raft-like membranes?
    • Rog, T., and Vattulainen, I. (2014). Cholesterol, sphingolipids, and glycolipids: what do we know about their role in raft-like membranes? Chem. Phys. Lipids 184, 82-104. doi: 10.1016/j.chemphyslip.2014.10.004
    • (2014) Chem. Phys. Lipids , vol.184 , pp. 82-104
    • Rog, T.1    Vattulainen, I.2
  • 116
    • 66249144426 scopus 로고    scopus 로고
    • The structure and function of G-protein-coupled receptors
    • Rosenbaum, D. M., Rasmussen, S. G. F., and Kobilka, B. K. (2009). The structure and function of G-protein-coupled receptors. Nature 459, 356-363. doi: 10.1038/nature08144
    • (2009) Nature , vol.459 , pp. 356-363
    • Rosenbaum, D.M.1    Rasmussen, S.G.F.2    Kobilka, B.K.3
  • 117
    • 84893370110 scopus 로고    scopus 로고
    • Bridging molecular docking to membrane molecular dynamics to investigate GPCR-ligand recognition: the human A2A adenosine receptor as a key study
    • Sabbadin, D., Ciancetta, A., and Moro, S. (2014). Bridging molecular docking to membrane molecular dynamics to investigate GPCR-ligand recognition: the human A2A adenosine receptor as a key study. J. Chem. Inf. Model 54, 169-183. doi: 10.1021/ci400532b
    • (2014) J. Chem. Inf. Model , vol.54 , pp. 169-183
    • Sabbadin, D.1    Ciancetta, A.2    Moro, S.3
  • 118
    • 0036182481 scopus 로고    scopus 로고
    • Agonist-induced translocation of the kinin B(1) receptor to caveolae-related rafts
    • Sabourin, T., Bastien, L., Bachvarov, D. R., and Marceau, F. (2002). Agonist-induced translocation of the kinin B(1) receptor to caveolae-related rafts. Mol. Pharmacol. 61, 546-553. doi: 10.1124/mol.61.3.546
    • (2002) Mol. Pharmacol , vol.61 , pp. 546-553
    • Sabourin, T.1    Bastien, L.2    Bachvarov, D.R.3    Marceau, F.4
  • 119
  • 120
    • 0037224730 scopus 로고    scopus 로고
    • Biochemical characterization of β2-adrenergic receptor dimers and oligomers
    • Salahpour, A., Bonin, H., Bhalla, S., Petaja-Repo, U., and Bouvier, M. (2003). Biochemical characterization of β2-adrenergic receptor dimers and oligomers. Biol. Chem. 384, 117-123. doi: 10.1515/BC.2003.012
    • (2003) Biol. Chem , vol.384 , pp. 117-123
    • Salahpour, A.1    Bonin, H.2    Bhalla, S.3    Petaja-Repo, U.4    Bouvier, M.5
  • 121
    • 84885935715 scopus 로고    scopus 로고
    • Crystallization of G protein-coupled receptors
    • Salom, D., Padayatti, P. S., and Palczewski, K. (2013). Crystallization of G protein-coupled receptors. Methods Cell Biol. 117, 451-468. doi: 10.1016/B978-0-12-408143-7.00024-4
    • (2013) Methods Cell Biol , vol.117 , pp. 451-468
    • Salom, D.1    Padayatti, P.S.2    Palczewski, K.3
  • 122
    • 84993945227 scopus 로고    scopus 로고
    • The molecular switching mechanism at the conserved D(E)RY motif in class-A GPCRs
    • Sandoval, A., Eichler, S., Madathil, S., Reeves, P. J., Fahmy, K., and Böckmann, R. A. (2016). The molecular switching mechanism at the conserved D(E)RY motif in class-A GPCRs. Biophys. J. 111, 79-89. doi: 10.1016/j.bpj.2016.06.004
    • (2016) Biophys. J , vol.111 , pp. 79-89
    • Sandoval, A.1    Eichler, S.2    Madathil, S.3    Reeves, P.J.4    Fahmy, K.5    Böckmann, R.A.6
  • 123
    • 33746659807 scopus 로고    scopus 로고
    • The active metabolite of Clopidogrel disrupts P2Y12 receptor oligomers and partitions them out of lipid rafts
    • Savi, P., Zachayus, J. L., Delesque-Touchard, N., Labouret, C., Hervé, C., Uzabiaga, M. F., et al. (2006). The active metabolite of Clopidogrel disrupts P2Y12 receptor oligomers and partitions them out of lipid rafts. Proc. Natl. Acad. Sci. U.S.A. 103, 11069-11074. doi: 10.1073/pnas.0510446103
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 11069-11074
    • Savi, P.1    Zachayus, J.L.2    Delesque-Touchard, N.3    Labouret, C.4    Hervé, C.5    Uzabiaga, M.F.6
  • 124
    • 77951055595 scopus 로고    scopus 로고
    • Impact of the DRY motif and the missing "ionic lock" on constitutive activity and G-protein coupling of the human histamine H4 receptor
    • Schneider, E. H., Schnell, D., Strasser, A., Dove, S., and Seifert, R. (2010). Impact of the DRY motif and the missing "ionic lock" on constitutive activity and G-protein coupling of the human histamine H4 receptor. J. Pharmacol. Exp. Ther. 333, 382-392. doi: 10.1124/jpet.109.163220
    • (2010) J. Pharmacol. Exp. Ther , vol.333 , pp. 382-392
    • Schneider, E.H.1    Schnell, D.2    Strasser, A.3    Dove, S.4    Seifert, R.5
  • 125
    • 0033213776 scopus 로고    scopus 로고
    • Colocalization of β-adrenergic receptors and caveolin within the plasma membrane
    • Schwencke, C., Okumura, S., Yamamoto, M., Geng, Y. J., and Ishikawa, Y. (1999). Colocalization of β-adrenergic receptors and caveolin within the plasma membrane. J. Cell. Biochem. 75, 64-72.
    • (1999) J. Cell. Biochem , vol.75 , pp. 64-72
    • Schwencke, C.1    Okumura, S.2    Yamamoto, M.3    Geng, Y.J.4    Ishikawa, Y.5
  • 126
    • 0037416207 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer (FRET) microscopy imaging of live cell protein localizations
    • Sekar, R. B., and Periasamy, A. (2003). Fluorescence resonance energy transfer (FRET) microscopy imaging of live cell protein localizations. J. Cell Biol. 160, 629-633. doi: 10.1083/jcb.200210140
    • (2003) J. Cell Biol , vol.160 , pp. 629-633
    • Sekar, R.B.1    Periasamy, A.2
  • 127
    • 84868234553 scopus 로고    scopus 로고
    • Identification of cholesterol binding sites in the serotonin1A receptor
    • Sengupta, D., and Chattopadhyay, A. (2012). Identification of cholesterol binding sites in the serotonin1A receptor. J. Phys. Chem. B 116, 12991-12996. doi: 10.1021/jp309888u
    • (2012) J. Phys. Chem. B , vol.116 , pp. 12991-12996
    • Sengupta, D.1    Chattopadhyay, A.2
  • 128
    • 84936890311 scopus 로고    scopus 로고
    • Molecular dynamics simulations of GPCR-cholesterol interaction: an emerging paradigm
    • Sengupta, D., and Chattopadhyay, A. (2015). Molecular dynamics simulations of GPCR-cholesterol interaction: an emerging paradigm. Biochim. Biophys. Acta 1848, 1775-1782. doi: 10.1016/j.bbamem.2015.03.018
    • (2015) Biochim. Biophys. Acta , vol.1848 , pp. 1775-1782
    • Sengupta, D.1    Chattopadhyay, A.2
  • 129
    • 34548576414 scopus 로고
    • Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea
    • Shimomura, O., Johnson, F. H., and Saiga, Y. (1962). Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea. J. Cell. Comp. Physiol. 59, 223-239. doi: 10.1002/jcp.1030590302
    • (1962) J. Cell. Comp. Physiol , vol.59 , pp. 223-239
    • Shimomura, O.1    Johnson, F.H.2    Saiga, Y.3
  • 130
    • 84884196122 scopus 로고    scopus 로고
    • Toward optimized potential functions for protein-protein interactions in aqueous solutions: osmotic second virial coefficient calculations using the martini coarse-grained force field
    • Stark, A. C., Andrews, C. T., and Elcock, A. H. (2013). Toward optimized potential functions for protein-protein interactions in aqueous solutions: osmotic second virial coefficient calculations using the martini coarse-grained force field. J. Chem. Theory Comput. 9, 4176-4185. doi: 10.1021/ct400008p
    • (2013) J. Chem. Theory Comput , vol.9 , pp. 4176-4185
    • Stark, A.C.1    Andrews, C.T.2    Elcock, A.H.3
  • 131
    • 41149127699 scopus 로고    scopus 로고
    • Dimerization and oligomerization of G-protein-coupled receptors: debated structures with established and emerging functions
    • Szidonya, L., Cserzo, M., and Hunyady, L. (2008). Dimerization and oligomerization of G-protein-coupled receptors: debated structures with established and emerging functions. J. Endocrinol. 196, 435-453. doi: 10.1677/JOE-07-0573
    • (2008) J. Endocrinol , vol.196 , pp. 435-453
    • Szidonya, L.1    Cserzo, M.2    Hunyady, L.3
  • 132
    • 84937731056 scopus 로고    scopus 로고
    • What can we learn from molecular dynamics simulations for GPCR drug design?
    • Tautermann, C. S., Seeliger, D., and Kriegl, J. M. (2015). What can we learn from molecular dynamics simulations for GPCR drug design? Comput. Struct. Biotechnol. J. 13, 111-121. doi: 10.1016/j.csbj.2014.12.002
    • (2015) Comput. Struct. Biotechnol. J , vol.13 , pp. 111-121
    • Tautermann, C.S.1    Seeliger, D.2    Kriegl, J.M.3
  • 133
    • 84940478169 scopus 로고    scopus 로고
    • Conformational dynamics of a class C G-protein-coupled receptor
    • Vafabakhsh, R., Levitz, J., and Isacoff, E. Y. (2015). Conformational dynamics of a class C G-protein-coupled receptor. Nature 524, 497-501. doi: 10.1038/nature14679
    • (2015) Nature , vol.524 , pp. 497-501
    • Vafabakhsh, R.1    Levitz, J.2    Isacoff, E.Y.3
  • 135
    • 84939812854 scopus 로고    scopus 로고
    • G protein-coupled receptor multimers: a question still open despite the use of novel approaches
    • Vischer, H. F., Castro, M., and Pin, J. P. (2015). G protein-coupled receptor multimers: a question still open despite the use of novel approaches. Mol. Pharmacol. 88, 561-571. doi: 10.1124/mol.115.099440
    • (2015) Mol. Pharmacol , vol.88 , pp. 561-571
    • Vischer, H.F.1    Castro, M.2    Pin, J.P.3
  • 136
    • 0034604399 scopus 로고    scopus 로고
    • Crystallographic and energetic analysis of binding of selected anions to the yellow variants of green fluorescent protein
    • Wachter, R. M., Yarbrough, D., Kallio, K., and Remington, S. J. (2000). Crystallographic and energetic analysis of binding of selected anions to the yellow variants of green fluorescent protein. J. Mol. Biol. 301, 157-171. doi: 10.1006/jmbi.2000.3905
    • (2000) J. Mol. Biol , vol.301 , pp. 157-171
    • Wachter, R.M.1    Yarbrough, D.2    Kallio, K.3    Remington, S.J.4
  • 137
    • 84877631485 scopus 로고    scopus 로고
    • Structural features for functional selectivity at serotonin receptors
    • Wacker, D., Wang, C., Katritch, V., Han, G. W., Huang, X. P., Vardy, E., et al. (2013). Structural features for functional selectivity at serotonin receptors. Science 340, 615-619. doi: 10.1126/science.1232808
    • (2013) Science , vol.340 , pp. 615-619
    • Wacker, D.1    Wang, C.2    Katritch, V.3    Han, G.W.4    Huang, X.P.5    Vardy, E.6
  • 138
    • 33750447940 scopus 로고    scopus 로고
    • Dimerization of CXCR4 in living malignant cells: control of cell migration by a synthetic peptide that reduces homologous CXCR4 interactions
    • Wang, J., He, L., Combs, C. A., Roderiquez, G., and Norcross, M. A. (2006). Dimerization of CXCR4 in living malignant cells: control of cell migration by a synthetic peptide that reduces homologous CXCR4 interactions. Mol. Cancer Ther. 5, 2474-2483. doi: 10.1158/1535-7163.MCT-05-0261
    • (2006) Mol. Cancer Ther , vol.5 , pp. 2474-2483
    • Wang, J.1    He, L.2    Combs, C.A.3    Roderiquez, G.4    Norcross, M.A.5
  • 139
    • 84925062589 scopus 로고    scopus 로고
    • Computational lipidomics with insane: a versatile tool for generating custom membranes for molecular simulations
    • Wassenaar, T. A., Ingólfsson, H. I., Böckmann, R. A., Tieleman, D. P., and Marrink, S. J. (2015a). Computational lipidomics with insane: a versatile tool for generating custom membranes for molecular simulations. J. Chem. Theory Comput. 11, 2144-2155. doi: 10.1021/acs.jctc.5b00209
    • (2015) J. Chem. Theory Comput , vol.11 , pp. 2144-2155
    • Wassenaar, T.A.1    Ingólfsson, H.I.2    Böckmann, R.A.3    Tieleman, D.P.4    Marrink, S.J.5
  • 140
    • 84929203814 scopus 로고    scopus 로고
    • High-throughput simulations of dimer and trimer assembly of membrane proteins The DAFT approach
    • Wassenaar, T. A., Pluhackova, K., Moussatova, A., Sengupta, D., Marrink, S. J., Tieleman, D. P., et al. (2015b). High-throughput simulations of dimer and trimer assembly of membrane proteins. The DAFT approach. J. Chem. Theory Comput. 11, 2278-2291. doi: 10.1021/ct5010092
    • (2015) J. Chem. Theory Comput , vol.11 , pp. 2278-2291
    • Wassenaar, T.A.1    Pluhackova, K.2    Moussatova, A.3    Sengupta, D.4    Marrink, S.J.5    Tieleman, D.P.6
  • 141
    • 34250666273 scopus 로고    scopus 로고
    • A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein
    • Whorton, M. R., Bokoch, M. P., Rasmussen, S. G., Huang, B., Zare, R. N., Kobilka, B., et al. (2007). A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein. Proc. Natl. Acad. Sci. U.S.A. 104, 7682-7687. doi: 10.1073/pnas.0611448104
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 7682-7687
    • Whorton, M.R.1    Bokoch, M.P.2    Rasmussen, S.G.3    Huang, B.4    Zare, R.N.5    Kobilka, B.6
  • 142
    • 85027927015 scopus 로고    scopus 로고
    • Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists
    • Wu, B., Chien, E. Y., Mol, C. D., Fenalti, G., Liu, W., Katritch, V., et al. (2010). Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists. Science 330, 1066-1071. doi: 10.1126/science.1194396
    • (2010) Science , vol.330 , pp. 1066-1071
    • Wu, B.1    Chien, E.Y.2    Mol, C.D.3    Fenalti, G.4    Liu, W.5    Katritch, V.6
  • 143
    • 84897580006 scopus 로고    scopus 로고
    • Structure of a class C GPCR metabotropic glutamate receptor 1 bound to an allosteric modulator
    • Wu, H., Wang, C., Gregory, K. J., Han, G. W., Cho, H. P., Xia, Y., et al. (2014). Structure of a class C GPCR metabotropic glutamate receptor 1 bound to an allosteric modulator. Science 344, 58-64. doi: 10.1126/science.1249489
    • (2014) Science , vol.344 , pp. 58-64
    • Wu, H.1    Wang, C.2    Gregory, K.J.3    Han, G.W.4    Cho, H.P.5    Xia, Y.6
  • 144
    • 0037072884 scopus 로고    scopus 로고
    • Caveolar localization dictates physiologic signaling of β2-adrenoceptors in neonatal cardiac myocytes
    • Xiang, Y., Rybin, V. O., Steinberg, S. F., and Kobilka, B. (2002). Caveolar localization dictates physiologic signaling of β2-adrenoceptors in neonatal cardiac myocytes. J. Biol. Chem. 277, 34280-34286. doi: 10.1074/jbc.M201644200
    • (2002) J. Biol. Chem , vol.277 , pp. 34280-34286
    • Xiang, Y.1    Rybin, V.O.2    Steinberg, S.F.3    Kobilka, B.4
  • 145
    • 33646783322 scopus 로고    scopus 로고
    • Localization of the κ opioid receptor in lipid rafts
    • Xu, W., Yoon, S. I., Huang, P., Wang, Y., Chen, C., Chong, P. L., et al. (2006). Localization of the κ opioid receptor in lipid rafts. J. Pharmacol. Exp. Ther. 317, 1295-1306. doi: 10.1124/jpet.105.099507
    • (2006) J. Pharmacol. Exp. Ther , vol.317 , pp. 1295-1306
    • Xu, W.1    Yoon, S.I.2    Huang, P.3    Wang, Y.4    Chen, C.5    Chong, P.L.6
  • 146
    • 40349110968 scopus 로고    scopus 로고
    • The A2A-adenosine receptor: a GPCR with unique features?
    • Zezula, J., and Freissmuth, M. (2008). The A2A-adenosine receptor: a GPCR with unique features? Br. J. Pharmacol. 153(Suppl. 1):S184-S190. doi: 10.1038/sj.bjp.0707674
    • (2008) Br. J. Pharmacol , vol.153 , pp. S184-S190
    • Zezula, J.1    Freissmuth, M.2
  • 147
    • 84928469118 scopus 로고    scopus 로고
    • Two disparate ligand-binding sites in the human P2Y1 receptor
    • Zhang, D., Gao, Z. G., Zhang, K., Kiselev, E., Crane, S., Wang, J., et al. (2015). Two disparate ligand-binding sites in the human P2Y1 receptor. Nature 520, 317-321. doi: 10.1038/nature14287
    • (2015) Nature , vol.520 , pp. 317-321
    • Zhang, D.1    Gao, Z.G.2    Zhang, K.3    Kiselev, E.4    Crane, S.5    Wang, J.6
  • 148
    • 84899755031 scopus 로고    scopus 로고
    • Structure of the human P2Y12 receptor in complex with an antithrombotic drug
    • Zhang, K., Zhang, J., Gao, Z. G., Zhang, D., Zhu, L., Han, G. W., et al. (2014). Structure of the human P2Y12 receptor in complex with an antithrombotic drug. Nature 509, 115-118. doi: 10.1038/nature13083
    • (2014) Nature , vol.509 , pp. 115-118
    • Zhang, K.1    Zhang, J.2    Gao, Z.G.3    Zhang, D.4    Zhu, L.5    Han, G.W.6
  • 149
    • 84858319313 scopus 로고    scopus 로고
    • Palmitoylation and membrane cholesterol stabilize μ-opioid receptor homodimerization and G protein coupling
    • Zheng, H., Pearsall, E. A., Hurst, D. P., Zhang, Y., Chu, J., Zhou, Y., et al. (2012a). Palmitoylation and membrane cholesterol stabilize μ-opioid receptor homodimerization and G protein coupling. BMC Cell Biol. 13:6. doi: 10.1186/1471-2121-13-6
    • (2012) BMC Cell Biol , vol.13 , pp. 6
    • Zheng, H.1    Pearsall, E.A.2    Hurst, D.P.3    Zhang, Y.4    Chu, J.5    Zhou, Y.6
  • 150
    • 84861452611 scopus 로고    scopus 로고
    • Cholesterol level influences opioid signaling in cell models and analgesia in mice and humans
    • Zheng, H., Zou, H., Liu, X., Chu, J., Zhou, Y., Loh, H. H., et al. (2012b). Cholesterol level influences opioid signaling in cell models and analgesia in mice and humans. J. Lipid Res. 53, 1153-1162. doi: 10.1194/jlr.M024455
    • (2012) J. Lipid Res , vol.53 , pp. 1153-1162
    • Zheng, H.1    Zou, H.2    Liu, X.3    Chu, J.4    Zhou, Y.5    Loh, H.H.6
  • 151
    • 84870896671 scopus 로고    scopus 로고
    • Cholesterol increases kinetic, energetic, and mechanical stability of the human β2-adrenergic receptor
    • Zocher, M., Zhang, C., Rasmussen, S. G., Kobilka, B. K., and Muller, D. J. (2012). Cholesterol increases kinetic, energetic, and mechanical stability of the human β2-adrenergic receptor. Proc. Natl. Acad. Sci. U.S.A. 109, E3463-E3472. doi: 10.1073/pnas.1210373109
    • (2012) Proc. Natl. Acad. Sci. U.S.A , vol.109 , pp. E3463-E3472
    • Zocher, M.1    Zhang, C.2    Rasmussen, S.G.3    Kobilka, B.K.4    Muller, D.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.