메뉴 건너뛰기




Volumn 159, Issue 4, 2010, Pages 738-750

Bimolecular fluorescence complementation: Lighting up seven transmembrane domain receptor signalling networks

Author keywords

Arrestin; Bimolecular fluorescence complementation; Fluorescence correlation spectroscopy; G protein; Receptor dimers; Seven transmembrane domain receptor

Indexed keywords

BETA ARRESTIN; CYAN FLUORESCENT PROTEIN; G PROTEIN COUPLED RECEPTOR; GREEN FLUORESCENT PROTEIN; MEMBRANE RECEPTOR; RED FLUORESCENT PROTEIN; YELLOW FLUORESCENT PROTEIN;

EID: 77249173336     PISSN: 00071188     EISSN: 14765381     Source Type: Journal    
DOI: 10.1111/j.1476-5381.2009.00480.x     Document Type: Review
Times cited : (38)

References (68)
  • 1
    • 34447269248 scopus 로고    scopus 로고
    • In vivo visualization of actin dynamics and actin interactions by BiFC
    • Anderie I, Schmid A (2007). In vivo visualization of actin dynamics and actin interactions by BiFC. Cell Biol Int 31 : 1131 1135.
    • (2007) Cell Biol Int , vol.31 , pp. 1131-1135
    • Anderie, I.1    Schmid, A.2
  • 2
    • 0034724192 scopus 로고    scopus 로고
    • Detection of 2-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 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET). Proc Natl Acad Sci USA 97 : 3684 3689.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3684-3689
    • Angers, S.1    Salahpour, A.2    Joly, E.3    Hilairet, S.4    Chelsky, D.5    Dennis, M.6
  • 3
    • 0038341013 scopus 로고    scopus 로고
    • The use of bioluminescence resonance energy transfer 2 to study neuropeptide y receptor agonist-induced -arrestin 2 interaction
    • Berglund MM, Schober DA, Statnick MA, McDonald PH, Gehlert DR (2003). The use of bioluminescence resonance energy transfer 2 to study neuropeptide Y receptor agonist-induced -arrestin 2 interaction. J Pharmacol Exp Ther 306 : 147 156.
    • (2003) J Pharmacol Exp Ther , vol.306 , pp. 147-156
    • Berglund, M.M.1    Schober, D.A.2    Statnick, M.A.3    McDonald, P.H.4    Gehlert, D.R.5
  • 5
    • 36448965981 scopus 로고    scopus 로고
    • Pharmacology under the microscope: The use of fluorescence correlation spectroscopy to determine the properties of ligand-receptor complexes
    • Briddon SJ, Hill SJ (2007). Pharmacology under the microscope: the use of fluorescence correlation spectroscopy to determine the properties of ligand-receptor complexes. Trends Pharmacol Sci 28 : 637 645.
    • (2007) Trends Pharmacol Sci , vol.28 , pp. 637-645
    • Briddon, S.J.1    Hill, S.J.2
  • 6
    • 33749005086 scopus 로고    scopus 로고
    • In vivo and in vitro protein solubility assays using split GFP
    • Cabantous S, Waldo GS (2006). In vivo and in vitro protein solubility assays using split GFP. Nat Methods 3 : 845 854.
    • (2006) Nat Methods , vol.3 , pp. 845-854
    • Cabantous, S.1    Waldo, G.S.2
  • 8
    • 27144475519 scopus 로고    scopus 로고
    • Characterization of isoprenaline- and salmeterol-stimulated interactions between 2-adrenoceptors and -arrestin 2 using beta-galactosidase complementation in C2C12 cells
    • Carter AA, Hill SJ (2005). Characterization of isoprenaline- and salmeterol-stimulated interactions between 2-adrenoceptors and -arrestin 2 using beta-galactosidase complementation in C2C12 cells. J Pharmacol Exp Ther 315 : 839 848.
    • (2005) J Pharmacol Exp Ther , vol.315 , pp. 839-848
    • Carter, A.A.1    Hill, S.J.2
  • 9
    • 17644391412 scopus 로고    scopus 로고
    • Monitoring agonist-promoted conformational changes of -arrestin in living cells by intramolecular BRET
    • Charest PG, Terrillon S, Bouvier M (2005). Monitoring agonist-promoted conformational changes of -arrestin in living cells by intramolecular BRET. EMBO Rep 6 : 334 340.
    • (2005) EMBO Rep , vol.6 , pp. 334-340
    • Charest, P.G.1    Terrillon, S.2    Bouvier, M.3
  • 10
    • 58149196402 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy in membrane structure elucidation
    • Chiantia S, Ries J, Schwille P (2009). Fluorescence correlation spectroscopy in membrane structure elucidation. Biochim Biophys Acta 1788 : 225 233.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 225-233
    • Chiantia, S.1    Ries, J.2    Schwille, P.3
  • 12
    • 33845926059 scopus 로고    scopus 로고
    • Seven transmembrane receptor core signaling complexes are assembled prior to plasma membrane trafficking
    • Dupre DJ, Robitaille M, Ethier N, Villeneuve LR, Mamarbachi AM, Hebert TE (2006). Seven transmembrane receptor core signaling complexes are assembled prior to plasma membrane trafficking. J Biol Chem 281 : 34561 34573.
    • (2006) J Biol Chem , vol.281 , pp. 34561-34573
    • Dupre, D.J.1    Robitaille, M.2    Ethier, N.3    Villeneuve, L.R.4    Mamarbachi, A.M.5    Hebert, T.E.6
  • 13
    • 38049115791 scopus 로고    scopus 로고
    • Split mCherry as a new red bimolecular fluorescence complementation system for visualizing protein-protein interactions in living cells
    • Fan JY, Cui ZQ, Wei HP, Zhang ZP, Zhou YF, Wang YP et al. (2008). Split mCherry as a new red bimolecular fluorescence complementation system for visualizing protein-protein interactions in living cells. Biochem Biophys Res Commun 367 : 47 53.
    • (2008) Biochem Biophys Res Commun , vol.367 , pp. 47-53
    • Fan, J.Y.1    Cui, Z.Q.2    Wei, H.P.3    Zhang, Z.P.4    Zhou, Y.F.5    Wang, Y.P.6
  • 14
    • 6944227833 scopus 로고    scopus 로고
    • Ubiquitin-mediated fluorescence complementation reveals that Jun ubiquitinated by Itch/AIP4 is localized to lysosomes
    • Fang D, Kerppola TK (2004). Ubiquitin-mediated fluorescence complementation reveals that Jun ubiquitinated by Itch/AIP4 is localized to lysosomes. Proc Natl Acad Sci USA 101 : 14782 14787.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 14782-14787
    • Fang, D.1    Kerppola, T.K.2
  • 15
    • 49849084462 scopus 로고    scopus 로고
    • Detection of higher-order G protein-coupled receptor oligomers by a combined BRET-BiFC technique
    • Gandia J, Galino J, Amaral OB, Soriano A, Lluis C, Franco R et al. (2008). Detection of higher-order G protein-coupled receptor oligomers by a combined BRET-BiFC technique. FEBS Lett 582 : 2979 2984.
    • (2008) FEBS Lett , vol.582 , pp. 2979-2984
    • Gandia, J.1    Galino, J.2    Amaral, O.B.3    Soriano, A.4    Lluis, C.5    Franco, R.6
  • 16
    • 0034647238 scopus 로고    scopus 로고
    • Antiparallel leucine zipper-directed protein reassembly: Application to the green fluorescent protein
    • Ghosh I, Hamilton AD, Regan L (2000). Antiparallel leucine zipper-directed protein reassembly: application to the green fluorescent protein. J Am Chem Soc 122 : 5658 5659.
    • (2000) J Am Chem Soc , vol.122 , pp. 5658-5659
    • Ghosh, I.1    Hamilton, A.D.2    Regan, L.3
  • 17
    • 2942559261 scopus 로고    scopus 로고
    • Visualization of Myc/Max/Mad family dimers and the competition for dimerization in living cells
    • Grinberg AV, Hu CD, Kerppola TK (2004). Visualization of Myc/Max/Mad family dimers and the competition for dimerization in living cells. Mol Cell Biol 24 : 4294 4308.
    • (2004) Mol Cell Biol , vol.24 , pp. 4294-4308
    • Grinberg, A.V.1    Hu, C.D.2    Kerppola, T.K.3
  • 18
    • 51049112029 scopus 로고    scopus 로고
    • Dopamine D2 receptors form higher order oligomers at physiological expression levels
    • Guo W, Urizar E, Kralikova M, Mobarec JC, Shi L, Filizola M et al. (2008). Dopamine D2 receptors form higher order oligomers at physiological expression levels. EMBO J 27 : 2293 2304.
    • (2008) EMBO J , vol.27 , pp. 2293-2304
    • Guo, W.1    Urizar, E.2    Kralikova, M.3    Mobarec, J.C.4    Shi, L.5    Filizola, M.6
  • 19
    • 33646414189 scopus 로고    scopus 로고
    • The structural basis of arrestin-mediated regulation of G-protein-coupled receptors
    • Gurevich VV, Gurevich EV (2006). The structural basis of arrestin-mediated regulation of G-protein-coupled receptors. Pharmacol Ther 110 : 465 502.
    • (2006) Pharmacol Ther , vol.110 , pp. 465-502
    • Gurevich, V.V.1    Gurevich, E.V.2
  • 20
    • 35748982441 scopus 로고    scopus 로고
    • Functional calcitonin gene-related peptide receptors are formed by the asymmetric assembly of a calcitonin receptor-like receptor homo-oligomer and a monomer of receptor activity-modifying protein-1
    • Heroux M, Hogue M, Lemieux S, Bouvier M (2007). Functional calcitonin gene-related peptide receptors are formed by the asymmetric assembly of a calcitonin receptor-like receptor homo-oligomer and a monomer of receptor activity-modifying protein-1. J Biol Chem 282 : 31610 31620.
    • (2007) J Biol Chem , vol.282 , pp. 31610-31620
    • Heroux, M.1    Hogue, M.2    Lemieux, S.3    Bouvier, M.4
  • 21
    • 84859008521 scopus 로고    scopus 로고
    • Quantitative analysis of neuropeptide y Y1 receptor association with -arrestin2 measured by bimolecular fluorescence complementation (BiFC)
    • Available at. (accessed 1 September 2009).
    • Holliday ND, Kilpatrick L, Briddon SJ, Hill SJ (2008). Quantitative analysis of neuropeptide Y Y1 receptor association with -arrestin2 measured by bimolecular fluorescence complementation (BiFC). Proc Br Pharmacol Soc. Available at http://www.pa2online.org/abstracts/Vol6Issue4abst007P.pdf (accessed 1 September 2009).
    • (2008) Proc Br Pharmacol Soc.
    • Holliday, N.D.1    Kilpatrick, L.2    Briddon, S.J.3    Hill, S.J.4
  • 22
    • 14944381164 scopus 로고    scopus 로고
    • Role of the C terminus in neuropeptide y Y1 receptor desensitization and internalization
    • Holliday ND, Lam CW, Tough IR, Cox HM (2005). Role of the C terminus in neuropeptide Y Y1 receptor desensitization and internalization. Mol Pharmacol 67 : 655 664.
    • (2005) Mol Pharmacol , vol.67 , pp. 655-664
    • Holliday, N.D.1    Lam, C.W.2    Tough, I.R.3    Cox, H.M.4
  • 23
    • 0036241055 scopus 로고    scopus 로고
    • Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation
    • Hu CD, Chinenov Y, Kerppola TK (2002). Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation. Mol Cell 9 : 789 798.
    • (2002) Mol Cell , vol.9 , pp. 789-798
    • Hu, C.D.1    Chinenov, Y.2    Kerppola, T.K.3
  • 24
    • 0037995710 scopus 로고    scopus 로고
    • Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis
    • Hu CD, Kerppola TK (2003). Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis. Nat Biotechnol 21 : 539 545.
    • (2003) Nat Biotechnol , vol.21 , pp. 539-545
    • Hu, C.D.1    Kerppola, T.K.2
  • 25
    • 6344237493 scopus 로고    scopus 로고
    • Live cell imaging of Gs and the 2-adrenergic receptor demonstrates that both alphas and 17 internalize upon stimulation and exhibit similar trafficking patterns that differ from that of the 2-adrenergic receptor
    • Hynes TR, Mervine SM, Yost EA, Sabo JL, Berlot CH (2004a). Live cell imaging of Gs and the 2-adrenergic receptor demonstrates that both alphas and 17 internalize upon stimulation and exhibit similar trafficking patterns that differ from that of the 2-adrenergic receptor. J Biol Chem 279 : 44101 44112.
    • (2004) J Biol Chem , vol.279 , pp. 44101-44112
    • Hynes, T.R.1    Mervine, S.M.2    Yost, E.A.3    Sabo, J.L.4    Berlot, C.H.5
  • 26
    • 3142766112 scopus 로고    scopus 로고
    • Visualization of G protein dimers using bimolecular fluorescence complementation demonstrates roles for both beta and gamma in subcellular targeting
    • Hynes TR, Tang L, Mervine SM, Sabo JL, Yost EA, Devreotes PN et al. (2004b). Visualization of G protein dimers using bimolecular fluorescence complementation demonstrates roles for both beta and gamma in subcellular targeting. J Biol Chem 279 : 30279 30286.
    • (2004) J Biol Chem , vol.279 , pp. 30279-30286
    • Hynes, T.R.1    Tang, L.2    Mervine, S.M.3    Sabo, J.L.4    Yost, E.A.5    Devreotes, P.N.6
  • 27
    • 58149280817 scopus 로고    scopus 로고
    • Lysosomal localization of ubiquitinated Jun requires multiple determinants in a lysine-27-linked polyubiquitin conjugate
    • Ikeda H, Kerppola TK (2008). Lysosomal localization of ubiquitinated Jun requires multiple determinants in a lysine-27-linked polyubiquitin conjugate. Mol Biol Cell 19 : 4588 4601.
    • (2008) Mol Biol Cell , vol.19 , pp. 4588-4601
    • Ikeda, H.1    Kerppola, T.K.2
  • 28
    • 33746435428 scopus 로고    scopus 로고
    • An improved mRFP1 adds red to bimolecular fluorescence complementation
    • Jach G, Pesch M, Richter K, Frings S, Uhrig JF (2006). An improved mRFP1 adds red to bimolecular fluorescence complementation. Nat Methods 3 : 597 600.
    • (2006) Nat Methods , vol.3 , pp. 597-600
    • Jach, G.1    Pesch, M.2    Richter, K.3    Frings, S.4    Uhrig, J.F.5
  • 29
    • 33751215258 scopus 로고    scopus 로고
    • A rigorous experimental framework for detecting protein oligomerization using bioluminescence resonance energy transfer
    • James JR, Oliveira MI, Carmo AM, Iaboni A, Davis SJ (2006). A rigorous experimental framework for detecting protein oligomerization using bioluminescence resonance energy transfer. Nat Methods 3 : 1001 1006.
    • (2006) Nat Methods , vol.3 , pp. 1001-1006
    • James, J.R.1    Oliveira, M.I.2    Carmo, A.M.3    Iaboni, A.4    Davis, S.J.5
  • 30
    • 48249132926 scopus 로고    scopus 로고
    • Bimolecular fluorescence complementation (BiFC) analysis as a probe of protein interactions in living cells
    • Kerppola TK (2008). Bimolecular fluorescence complementation (BiFC) analysis as a probe of protein interactions in living cells. Annu Rev Biophys 37 : 465 487.
    • (2008) Annu Rev Biophys , vol.37 , pp. 465-487
    • Kerppola, T.K.1
  • 31
    • 84859000379 scopus 로고    scopus 로고
    • Differential association of neuropeptide y Y1 and Y2 receptors with -arrestin2 revealed by bimolecular fluorescence complementation (BiFC)
    • Available at. (accessed 1 September 2009).
    • Kilpatrick L, Briddon SJ, Hill SJ, Holliday ND (2008). Differential association of neuropeptide Y Y1 and Y2 receptors with -arrestin2 revealed by bimolecular fluorescence complementation (BiFC). Proc Br Pharmacol Soc. Available at http://www.pa2online.org/abstracts/Vol6Issue4abst062P.pdf (accessed 1 September 2009).
    • (2008) Proc Br Pharmacol Soc.
    • Kilpatrick, L.1    Briddon, S.J.2    Hill, S.J.3    Holliday, N.D.4
  • 32
    • 35748946937 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy in living cells
    • Kim SA, Heinze KG, Schwille P (2007). Fluorescence correlation spectroscopy in living cells. Nat Methods 4 : 963 973.
    • (2007) Nat Methods , vol.4 , pp. 963-973
    • Kim, S.A.1    Heinze, K.G.2    Schwille, P.3
  • 34
    • 33947362780 scopus 로고    scopus 로고
    • The 1b-adrenoceptor exists as a higher-order oligomer: Effective oligomerization is required for receptor maturation, surface delivery, and function
    • Lopez-Gimenez JF, Canals M, Pediani JD, Milligan G (2007). The 1b-adrenoceptor exists as a higher-order oligomer: effective oligomerization is required for receptor maturation, surface delivery, and function. Mol Pharmacol 71 : 1015 1029.
    • (2007) Mol Pharmacol , vol.71 , pp. 1015-1029
    • Lopez-Gimenez, J.F.1    Canals, M.2    Pediani, J.D.3    Milligan, G.4
  • 35
    • 49049108182 scopus 로고    scopus 로고
    • Imaging CXCR4 signaling with firefly luciferase complementation
    • Luker KE, Gupta M, Luker GD (2008). Imaging CXCR4 signaling with firefly luciferase complementation. Anal Chem 80 : 5565 5573.
    • (2008) Anal Chem , vol.80 , pp. 5565-5573
    • Luker, K.E.1    Gupta, M.2    Luker, G.D.3
  • 36
    • 61449217021 scopus 로고    scopus 로고
    • Imaging chemokine receptor dimerization with firefly luciferase complementation
    • Luker KE, Gupta M, Luker GD (2009). Imaging chemokine receptor dimerization with firefly luciferase complementation. FASEB J 23 : 823 834.
    • (2009) FASEB J , vol.23 , pp. 823-834
    • Luker, K.E.1    Gupta, M.2    Luker, G.D.3
  • 38
    • 33646365380 scopus 로고    scopus 로고
    • A -arrestin binding determinant common to the second intracellular loops of rhodopsin family G protein-coupled receptors
    • Marion S, Oakley RH, Kim KM, Caron MG, Barak LS (2006). A -arrestin binding determinant common to the second intracellular loops of rhodopsin family G protein-coupled receptors. J Biol Chem 281 : 2932 2938.
    • (2006) J Biol Chem , vol.281 , pp. 2932-2938
    • Marion, S.1    Oakley, R.H.2    Kim, K.M.3    Caron, M.G.4    Barak, L.S.5
  • 39
    • 44449096254 scopus 로고    scopus 로고
    • Cell-surface protein-protein interaction analysis with time-resolved FRET and snap-tag technologies: Application to GPCR oligomerization
    • Maurel D, Comps-Agrar L, Brock C, Rives ML, Bourrier E, Ayoub MA et al. (2008). Cell-surface protein-protein interaction analysis with time-resolved FRET and snap-tag technologies: application to GPCR oligomerization. Nat Methods 5 : 561 567.
    • (2008) Nat Methods , vol.5 , pp. 561-567
    • Maurel, D.1    Comps-Agrar, L.2    Brock, C.3    Rives, M.L.4    Bourrier, E.5    Ayoub, M.A.6
  • 40
    • 33745234272 scopus 로고    scopus 로고
    • Analysis of G protein dimer formation in live cells using multicolor bimolecular fluorescence complementation demonstrates preferences of beta1 for particular gamma subunits
    • Mervine SM, Yost EA, Sabo JL, Hynes TR, Berlot CH (2006). Analysis of G protein dimer formation in live cells using multicolor bimolecular fluorescence complementation demonstrates preferences of beta1 for particular gamma subunits. Mol Pharmacol 70 : 194 205.
    • (2006) Mol Pharmacol , vol.70 , pp. 194-205
    • Mervine, S.M.1    Yost, E.A.2    Sabo, J.L.3    Hynes, T.R.4    Berlot, C.H.5
  • 41
    • 34347374044 scopus 로고    scopus 로고
    • Universal strategies in research and drug discovery based on protein-fragment complementation assays
    • Michnick SW, Ear PH, Manderson EN, Remy I, Stefan E (2007). Universal strategies in research and drug discovery based on protein-fragment complementation assays. Nat Rev Drug Discov 6 : 569 582.
    • (2007) Nat Rev Drug Discov , vol.6 , pp. 569-582
    • Michnick, S.W.1    Ear, P.H.2    Manderson, E.N.3    Remy, I.4    Stefan, E.5
  • 42
    • 33751057231 scopus 로고    scopus 로고
    • Chemical genetic strategies to delineate MAP kinase signaling pathways using protein-fragment complementation assays (PCA)
    • Michnick SW, MacDonald ML, Westwick JK (2006). Chemical genetic strategies to delineate MAP kinase signaling pathways using protein-fragment complementation assays (PCA). Methods 40 : 287 293.
    • (2006) Methods , vol.40 , pp. 287-293
    • Michnick, S.W.1    MacDonald, M.L.2    Westwick, J.K.3
  • 43
    • 21344433619 scopus 로고    scopus 로고
    • Methods to monitor the quaternary structure of G protein-coupled receptors
    • DOI 10.1111/j.1742-4658.2005.04731.x
    • Milligan G, Bouvier M (2005). Methods to monitor the quaternary structure of G protein-coupled receptors. FEBS J 272 : 2914 2925. (Pubitemid 40904680)
    • (2005) FEBS Journal , vol.272 , Issue.12 , pp. 2914-2925
    • Milligan, G.1    Bouvier, M.2
  • 44
    • 34247525991 scopus 로고    scopus 로고
    • Detection of transient protein-protein interactions by bimolecular fluorescence complementation: The Abl-SH3 case
    • Morell M, Espargaro A, Aviles FX, Ventura S (2007). Detection of transient protein-protein interactions by bimolecular fluorescence complementation: the Abl-SH3 case. Proteomics 7 : 1023 1036.
    • (2007) Proteomics , vol.7 , pp. 1023-1036
    • Morell, M.1    Espargaro, A.2    Aviles, F.X.3    Ventura, S.4
  • 45
    • 0036138908 scopus 로고    scopus 로고
    • A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications
    • Nagai T, Ibata K, Park ES, Kubota M, Mikoshiba K, Miyawaki A (2002). A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nat Biotechnol 20 : 87 90.
    • (2002) Nat Biotechnol , vol.20 , pp. 87-90
    • Nagai, T.1    Ibata, K.2    Park, E.S.3    Kubota, M.4    Mikoshiba, K.5    Miyawaki, A.6
  • 46
    • 0035853040 scopus 로고    scopus 로고
    • Circularly permuted green fluorescent proteins engineered to sense Ca2+
    • Nagai T, Sawano A, Park ES, Miyawaki A (2001). Circularly permuted green fluorescent proteins engineered to sense Ca2+. Proc Natl Acad Sci USA 98 : 3197 3202.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 3197-3202
    • Nagai, T.1    Sawano, A.2    Park, E.S.3    Miyawaki, A.4
  • 47
    • 55549147195 scopus 로고    scopus 로고
    • Detection of heteromers formed by cannabinoid CB1, dopamine D2, and adenosine A2A G-protein-coupled receptors by combining bimolecular fluorescence complementation and bioluminescence energy transfer
    • Navarro G, Carriba P, Gandia J, Ciruela F, Casado V, Cortes A et al. (2008). Detection of heteromers formed by cannabinoid CB1, dopamine D2, and adenosine A2A G-protein-coupled receptors by combining bimolecular fluorescence complementation and bioluminescence energy transfer. Sci World J 8 : 1088 1097.
    • (2008) Sci World J , vol.8 , pp. 1088-1097
    • Navarro, G.1    Carriba, P.2    Gandia, J.3    Ciruela, F.4    Casado, V.5    Cortes, A.6
  • 48
    • 18144394763 scopus 로고    scopus 로고
    • Capturing protein interactions in the secretory pathway of living cells
    • Nyfeler B, Michnick SW, Hauri HP (2005). Capturing protein interactions in the secretory pathway of living cells. Proc Natl Acad Sci USA 102 : 6350 6355.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 6350-6355
    • Nyfeler, B.1    Michnick, S.W.2    Hauri, H.P.3
  • 49
    • 0035374624 scopus 로고    scopus 로고
    • Molecular determinants underlying the formation of stable intracellular G protein-coupled receptor--arrestin complexes after receptor endocytosis
    • Oakley RH, Laporte SA, Holt JA, Barak LS, Caron MG (2001). Molecular determinants underlying the formation of stable intracellular G protein-coupled receptor--arrestin complexes after receptor endocytosis. J Biol Chem 276 : 19452 19460.
    • (2001) J Biol Chem , vol.276 , pp. 19452-19460
    • Oakley, R.H.1    Laporte, S.A.2    Holt, J.A.3    Barak, L.S.4    Caron, M.G.5
  • 50
    • 58249120533 scopus 로고    scopus 로고
    • Applicability of superfolder YFP bimolecular fluorescence complementation in vitro
    • Ottmann C, Weyand M, Wolf A, Kuhlmann J (2009). Applicability of superfolder YFP bimolecular fluorescence complementation in vitro. Biol Chem 390 : 81 90.
    • (2009) Biol Chem , vol.390 , pp. 81-90
    • Ottmann, C.1    Weyand, M.2    Wolf, A.3    Kuhlmann, J.4
  • 51
    • 38849196399 scopus 로고    scopus 로고
    • Distinct motifs of neuropeptide y receptors differentially regulate trafficking and desensitization
    • Ouedraogo M, Lecat S, Rochdi MD, Hachet-Haas M, Matthes H, Gicquiaux H et al. (2008). Distinct motifs of neuropeptide Y receptors differentially regulate trafficking and desensitization. Traffic 9 : 305 324.
    • (2008) Traffic , vol.9 , pp. 305-324
    • Ouedraogo, M.1    Lecat, S.2    Rochdi, M.D.3    Hachet-Haas, M.4    Matthes, H.5    Gicquiaux, H.6
  • 52
    • 0032514623 scopus 로고    scopus 로고
    • Oligomerization domain-directed reassembly of active dihydrofolate reductase from rationally designed fragments
    • Pelletier JN, Campbell-Valois FX, Michnick SW (1998). Oligomerization domain-directed reassembly of active dihydrofolate reductase from rationally designed fragments. Proc Natl Acad Sci USA 95 : 12141 12146.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12141-12146
    • Pelletier, J.N.1    Campbell-Valois, F.X.2    Michnick, S.W.3
  • 53
    • 33746871075 scopus 로고    scopus 로고
    • Heterotrimeric G proteins form stable complexes with adenylyl cyclase and Kir3.1 channels in living cells
    • Rebois RV, Robitaille M, Gales C, Dupre DJ, Baragli A, Trieu P et al. (2006). Heterotrimeric G proteins form stable complexes with adenylyl cyclase and Kir3.1 channels in living cells. J Cell Sci 119 : 2807 2818.
    • (2006) J Cell Sci , vol.119 , pp. 2807-2818
    • Rebois, R.V.1    Robitaille, M.2    Gales, C.3    Dupre, D.J.4    Baragli, A.5    Trieu, P.6
  • 54
    • 0034976147 scopus 로고    scopus 로고
    • From fixed to FRAP: Measuring protein mobility and activity in living cells
    • Reits EA, Neefjes JJ (2001). From fixed to FRAP: measuring protein mobility and activity in living cells. Nat Cell Biol 3 : E145 E147.
    • (2001) Nat Cell Biol , vol.3
    • Reits, E.A.1    Neefjes, J.J.2
  • 55
    • 33751208345 scopus 로고    scopus 로고
    • A highly sensitive protein-protein interaction assay based on Gaussia luciferase
    • Remy I, Michnick SW (2006). A highly sensitive protein-protein interaction assay based on Gaussia luciferase. Nat Methods 3 : 977 979.
    • (2006) Nat Methods , vol.3 , pp. 977-979
    • Remy, I.1    Michnick, S.W.2
  • 56
    • 2342647439 scopus 로고    scopus 로고
    • PKB/Akt modulates TGF-beta signalling through a direct interaction with Smad3
    • Remy I, Montmarquette A, Michnick SW (2004). PKB/Akt modulates TGF-beta signalling through a direct interaction with Smad3. Nat Cell Biol 6 : 358 365.
    • (2004) Nat Cell Biol , vol.6 , pp. 358-365
    • Remy, I.1    Montmarquette, A.2    Michnick, S.W.3
  • 57
    • 0033548048 scopus 로고    scopus 로고
    • Erythropoietin receptor activation by a ligand-induced conformation change
    • Remy I, Wilson IA, Michnick SW (1999). Erythropoietin receptor activation by a ligand-induced conformation change. Science 283 : 990 993.
    • (1999) Science , vol.283 , pp. 990-993
    • Remy, I.1    Wilson, I.A.2    Michnick, S.W.3
  • 58
    • 0035801541 scopus 로고    scopus 로고
    • Beat-to-beat oscillations of mitochondrial ca2+ in cardiac cells
    • Robert V, Gurlini P, Tosello V, Nagai T, Miyawaki A, Di Lisa F et al. (2001). Beat-to-beat oscillations of mitochondrial Ca2+ in cardiac cells. EMBO J 20 : 4998 5007.
    • (2001) EMBO J , vol.20 , pp. 4998-5007
    • Robert, V.1    Gurlini, P.2    Tosello, V.3    Nagai, T.4    Miyawaki, A.5    Di Lisa, F.6
  • 59
    • 84859008945 scopus 로고    scopus 로고
    • The effect of agonist activation and homodimerisation on the membrane diffusion of the human histamine H1 receptor
    • Available at. (accessed 1 September 2009).
    • Rose R, Briddon SJ, Hill SJ (2008). The effect of agonist activation and homodimerisation on the membrane diffusion of the human histamine H1 receptor. Proc Br Pharmacol Soc. Available at http://www.pa2online.org/abstracts/ Vol6Issue4abst002P.pdf (accessed 1 September 2009).
    • (2008) Proc Br Pharmacol Soc.
    • Rose, R.1    Briddon, S.J.2    Hill, S.J.3
  • 60
    • 0030738524 scopus 로고    scopus 로고
    • Monitoring protein-protein interactions in intact eukaryotic cells by -galactosidase complementation
    • Rossi F, Charlton CA, Blau HM (1997). Monitoring protein-protein interactions in intact eukaryotic cells by -galactosidase complementation. Proc Natl Acad Sci USA 94 : 8405 8410.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 8405-8410
    • Rossi, F.1    Charlton, C.A.2    Blau, H.M.3
  • 61
    • 53949107378 scopus 로고    scopus 로고
    • Fluorescence complementation: An emerging tool for biological research
    • Shyu YJ, Hu CD (2008). Fluorescence complementation: an emerging tool for biological research. Trends Biotechnol 26 : 622 630.
    • (2008) Trends Biotechnol , vol.26 , pp. 622-630
    • Shyu, Y.J.1    Hu, C.D.2
  • 62
    • 50449091328 scopus 로고    scopus 로고
    • Ligand-dependent oligomerization of dopamine D(2) and adenosine A(2A) receptors in living neuronal cells
    • Vidi PA, Chemel BR, Hu CD, Watts VJ (2008a). Ligand-dependent oligomerization of dopamine D(2) and adenosine A(2A) receptors in living neuronal cells. Mol Pharmacol 74 : 544 551.
    • (2008) Mol Pharmacol , vol.74 , pp. 544-551
    • Vidi, P.A.1    Chemel, B.R.2    Hu, C.D.3    Watts, V.J.4
  • 63
    • 56649106450 scopus 로고    scopus 로고
    • Adenosine A(2A) receptors assemble into higher-order oligomers at the plasma membrane
    • Vidi PA, Chen J, Irudayaraj JM, Watts VJ (2008b). Adenosine A(2A) receptors assemble into higher-order oligomers at the plasma membrane. FEBS Lett 582 : 3985 3990.
    • (2008) FEBS Lett , vol.582 , pp. 3985-3990
    • Vidi, P.A.1    Chen, J.2    Irudayaraj, J.M.3    Watts, V.J.4
  • 64
    • 63849341905 scopus 로고    scopus 로고
    • Fluorescent and bioluminescent protein-fragment complementation assays in the study of G protein-coupled receptor oligomerization and signaling
    • Vidi PA, Watts VJ (2009). Fluorescent and bioluminescent protein-fragment complementation assays in the study of G protein-coupled receptor oligomerization and signaling. Mol Pharmacol 75 : 733 739.
    • (2009) Mol Pharmacol , vol.75 , pp. 733-739
    • Vidi, P.A.1    Watts, V.J.2
  • 65
    • 35348813658 scopus 로고    scopus 로고
    • Current state of imaging protein-protein interactions in vivo with genetically encoded reporters
    • Villalobos V, Naik S, Piwnica-Worms D (2007). Current state of imaging protein-protein interactions in vivo with genetically encoded reporters. Annu Rev Biomed Eng 9 : 321 349.
    • (2007) Annu Rev Biomed Eng , vol.9 , pp. 321-349
    • Villalobos, V.1    Naik, S.2    Piwnica-Worms, D.3
  • 66
    • 55949121452 scopus 로고    scopus 로고
    • Different polycomb group CBX family proteins associate with distinct regions of chromatin using nonhomologous protein sequences
    • Vincenz C, Kerppola TK (2008). Different polycomb group CBX family proteins associate with distinct regions of chromatin using nonhomologous protein sequences. Proc Natl Acad Sci USA 105 : 16572 16577.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 16572-16577
    • Vincenz, C.1    Kerppola, T.K.2
  • 67
    • 34250666273 scopus 로고    scopus 로고
    • A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein
    • Whorton MR, Bokoch MP, Rasmussen SG, Huang B, Zare RN, 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 USA 104 : 7682 7687.
    • (2007) Proc Natl Acad Sci USA , 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
  • 68
    • 34748916964 scopus 로고    scopus 로고
    • Live cell analysis of G protein 5 complex formation, function, and targeting
    • Yost EA, Mervine SM, Sabo JL, Hynes TR, Berlot CH (2007). Live cell analysis of G protein 5 complex formation, function, and targeting. Mol Pharmacol 72 : 812 825.
    • (2007) Mol Pharmacol , vol.72 , pp. 812-825
    • Yost, E.A.1    Mervine, S.M.2    Sabo, J.L.3    Hynes, T.R.4    Berlot, C.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.