메뉴 건너뛰기




Volumn 6, Issue 8, 2010, Pages 587-594

Time-resolved FRET between GPCR ligands reveals oligomers in native tissues

(19)  Albizu, Laura a,b,c,j   Cottet, Martin a,b,c   Kralikova, Michaela d,e,k   Stoev, Stoytcho f   Seyer, René a,b,c   Brabet, Isabelle a,b,c   Roux, Thomas g   Bazin, Hervé g   Bourrier, Emmanuel g   Lamarque, Laurent g   Breton, Christophe h   Rives, Marie Laure d,e   Newman, Amy i   Javitch, Jonathan d,e   Trinquet, Eric g   Manning, Maurice f   Pin, Jean Philippe a,b,c   Mouillac, Bernard a,b,c   Durroux, Thierry a,b,c  


Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN COUPLED RECEPTOR; LIGAND; OLIGOMER; OXYTOCIN RECEPTOR; DOPAMINE 2 RECEPTOR; FLUORESCENT DYE; OLIGOPEPTIDE; VASOPRESSIN RECEPTOR;

EID: 77955874300     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.396     Document Type: Article
Times cited : (296)

References (50)
  • 1
    • 1242276192 scopus 로고    scopus 로고
    • Roles of G-protein-coupled receptor dimerization
    • Terrillon, S. & Bouvier, M. Roles of G-protein-coupled receptor dimerization. EMBO Rep. 5, 30-34 (2004).
    • (2004) EMBO Rep , vol.5 , pp. 30-34
    • Terrillon, S.1    Bouvier, M.2
  • 2
    • 60249098735 scopus 로고    scopus 로고
    • Building a new conceptual framework for receptor heteromers
    • Ferré, S. et al. Building a new conceptual framework for receptor heteromers. Nat. Chem. Biol. 5, 131-134 (2009).
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 131-134
    • Ferré, S.1
  • 3
    • 33645958615 scopus 로고    scopus 로고
    • Structure of the rhodopsin dimer: A working model for G-protein-coupled receptors
    • Fotiadis, D. et al. Structure of the rhodopsin dimer: a working model for G-protein-coupled receptors. Curr. Opin. Struct. Biol. 16, 252-259 (2006).
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 252-259
    • Fotiadis, D.1
  • 4
    • 1842687121 scopus 로고    scopus 로고
    • A role for heterodimerization of mu and delta opiate receptors in enhancing morphine analgesia
    • Gomes, I. et al. A role for heterodimerization of mu and delta opiate receptors in enhancing morphine analgesia. Proc. Natl. Acad. Sci. USA 101, 5135-5139 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 5135-5139
    • Gomes, I.1
  • 5
    • 0029083945 scopus 로고
    • Cooperativity manifest in the binding properties of purified cardiac muscarinic receptors
    • Wreggett, K.A. & Wells, J.W. Cooperativity manifest in the binding properties of purified cardiac muscarinic receptors. J. Biol. Chem. 270, 22488-22499 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 22488-22499
    • Wreggett, K.A.1    Wells, J.W.2
  • 6
    • 0030963248 scopus 로고    scopus 로고
    • Cardiac muscarinic receptors. Cooperativity as the basis for multiple states of affinity
    • DOI 10.1021/bi961939t
    • Chidiac, P., Green, M.A., Pawagi, A.B. & Wells, J.W. Cardiac muscarinic receptors. Cooperativity as the basis for multiple states of affinity. Biochemistry 36, 7361-7379 (1997). (Pubitemid 27262359)
    • (1997) Biochemistry , vol.36 , Issue.24 , pp. 7361-7379
    • Chidiac, P.1    Green, M.A.2    Pawagi, A.B.3    Wells, J.W.4
  • 7
    • 21244460359 scopus 로고    scopus 로고
    • Glycoprotein hormone receptors: Link between receptor homodimerization and negative cooperativity
    • Urizar, E. et al. Glycoprotein hormone receptors: link between receptor homodimerization and negative cooperativity. EMBO J. 24, 1954-1964 (2005).
    • (2005) EMBO J , vol.24 , pp. 1954-1964
    • Urizar, E.1
  • 8
    • 21144446486 scopus 로고    scopus 로고
    • A heterodimer-selective agonist shows in vivo relevance of G protein-coupled receptor dimmers
    • Waldhoer, M. et al. A heterodimer-selective agonist shows in vivo relevance of G protein-coupled receptor dimers. Proc. Natl. Acad. Sci. USA 102, 9050-9055 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 9050-9055
    • Waldhoer, M.1
  • 9
    • 0034522937 scopus 로고    scopus 로고
    • Luteinizing hormone receptors are self-associated in the plasma membrane
    • Roess, D.A., Horvat, R.D., Munnelly, H. & Barisas, B.G. Luteinizing hormone receptors are self-associated in the plasma membrane. Endocrinology 141, 4518-4523 (2000).
    • (2000) Endocrinology , vol.141 , pp. 4518-4523
    • Roess, D.A.1    Horvat, R.D.2    Munnelly, H.3    Barisas, B.G.4
  • 10
    • 0037022641 scopus 로고    scopus 로고
    • Ligand binding to somatostatin receptors induces receptor-specific oligomer formation in live cells
    • Patel, R.C. et al. Ligand binding to somatostatin receptors induces receptor-specific oligomer formation in live cells. Proc. Natl. Acad. Sci. USA 99, 3294-3299 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 3294-3299
    • Patel, R.C.1
  • 11
    • 0036182267 scopus 로고    scopus 로고
    • Time resolved amplification of cryptate emission: A versatile technology to trace biomolecular interactions
    • Bazin, H., Trinquet, E. & Mathis, G. Time resolved amplification of cryptate emission: a versatile technology to trace biomolecular interactions. J. Biotechnol. 82, 233-250 (2002).
    • (2002) J. Biotechnol. , vol.82 , pp. 233-250
    • Bazin, H.1    Trinquet, E.2    Mathis, G.3
  • 12
    • 0037384043 scopus 로고    scopus 로고
    • Oxytocin and vasopressin V1a and V2 receptors form constitutive homo- and heterodimers during biosynthesis
    • Terrillon, S. et al. Oxytocin and vasopressin V1a and V2 receptors form constitutive homo- and heterodimers during biosynthesis. Mol. Endocrinol. 17, 677-691 (2003).
    • (2003) Mol. Endocrinol. , vol.17 , pp. 677-691
    • Terrillon, S.1
  • 13
    • 0347359063 scopus 로고    scopus 로고
    • Identification of dimeric and oligomeric complexes of the human oxytocin receptor by co-immunoprecipitation and bioluminescence resonance energy transfer
    • Devost, D. & Zingg, H.H. Identification of dimeric and oligomeric complexes of the human oxytocin receptor by co-immunoprecipitation and bioluminescence resonance energy transfer. J. Mol. Endocrinol. 31, 461-471 (2003).
    • (2003) J. Mol. Endocrinol. , vol.31 , pp. 461-471
    • Devost, D.1    Zingg, H.H.2
  • 14
    • 72449173500 scopus 로고    scopus 로고
    • Past, present and future of vasopressin and oxytocin receptor oligomers, prototypical GPCR models to study dimerization processes
    • Cottet, M. et al. Past, present and future of vasopressin and oxytocin receptor oligomers, prototypical GPCR models to study dimerization processes. Curr. Opin. Pharmacol. 1, 59-66 (2009).
    • (2009) Curr. Opin. Pharmacol. , vol.1 , pp. 59-66
    • Cottet, M.1
  • 15
    • 0035933747 scopus 로고    scopus 로고
    • Dopamine D2 receptor dimer formation: Evidence from ligand binding
    • Armstrong, D. & Strange, P.G. Dopamine D2 receptor dimer formation: evidence from ligand binding. J. Biol. Chem. 276, 22621-22629 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 22621-22629
    • Armstrong, D.1    Strange, P.G.2
  • 16
    • 51049112029 scopus 로고    scopus 로고
    • Dopamine D2 receptors form higher-order oligomers at physiological expression levels
    • Guo, W. et al. Dopamine D2 receptors form higher-order oligomers at physiological expression levels. EMBO J. 27, 2293-2304 (2008).
    • (2008) EMBO J , vol.27 , pp. 2293-2304
    • Guo, W.1
  • 17
    • 6944237210 scopus 로고    scopus 로고
    • The ants go marching two by two: Oligomeric structure of G-protein-coupled receptors
    • Javitch, J.A. The ants go marching two by two: oligomeric structure of G-protein-coupled receptors. Mol. Pharmacol. 66, 1077-1082 (2004).
    • (2004) Mol. Pharmacol. , vol.66 , pp. 1077-1082
    • Javitch, J.A.1
  • 18
    • 30044435477 scopus 로고    scopus 로고
    • Investigation of cooperativity in the binding of ligands to the D(2) dopamine receptor
    • Vivo, M., Lin, H. & Strange, P.G. Investigation of cooperativity in the binding of ligands to the D(2) dopamine receptor. Mol. Pharmacol. 69, 226-235 (2006).
    • (2006) Mol. Pharmacol. , vol.69 , pp. 226-235
    • Vivo, M.1    Lin, H.2    Strange, P.G.3
  • 19
    • 33751195311 scopus 로고    scopus 로고
    • Probing the existence of G protein-coupled receptor dimers by positive and negative ligand-dependent cooperative binding
    • Albizu, L. et al. Probing the existence of G protein-coupled receptor dimers by positive and negative ligand-dependent cooperative binding. Mol. Pharmacol. 70, 1783-1791 (2006).
    • (2006) Mol. Pharmacol. , vol.70 , pp. 1783-1791
    • Albizu, L.1
  • 20
    • 34948854685 scopus 로고    scopus 로고
    • Towards efficient drug screening by homogeneous assays based on the development of new fluorescent vasopressin and oxytocin receptor ligands
    • Albizu, L. et al. Towards efficient drug screening by homogeneous assays based on the development of new fluorescent vasopressin and oxytocin receptor ligands. J. Med. Chem. 50, 4976-4985 (2007).
    • (2007) J. Med. Chem. , vol.50 , pp. 4976-4985
    • Albizu, L.1
  • 21
    • 0033535519 scopus 로고    scopus 로고
    • Fluorescent pseudo-peptide linear vasopressin antagonists: Design, synthesis, and applications
    • Durroux, T. et al. Fluorescent pseudo-peptide linear vasopressin antagonists: design, synthesis, and applications. J. Med. Chem. 42, 1312-1319 (1999).
    • (1999) J. Med. Chem. , vol.42 , pp. 1312-1319
    • Durroux, T.1
  • 22
    • 0029134581 scopus 로고
    • Probing molecular interactions with homogeneous techniques based on rare earth cryptates and fluorescence energy transfer
    • Mathis, G. Probing molecular interactions with homogeneous techniques based on rare earth cryptates and fluorescence energy transfer. Clin. Chem. 41, 1391-1397 (1995).
    • (1995) Clin. Chem. , vol.41 , pp. 1391-1397
    • Mathis, G.1
  • 23
    • 0028077111 scopus 로고
    • Luminescence energy transfer using a terbium chelate: Improvements on fluorescence energy transfer
    • Selvin, P.R. & Hearst, J.E. Luminescence energy transfer using a terbium chelate: improvements on fluorescence energy transfer. Proc. Natl. Acad. Sci. USA 91, 10024-10028 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10024-10028
    • Selvin, P.R.1    Hearst, J.E.2
  • 24
    • 56049122715 scopus 로고    scopus 로고
    • Fluorescent agonists and antagonists for vasopressin/oxytocin G protein-coupled receptors: Usefulness in ligand screening assays and receptor studies
    • Mouillac, B., Manning, M. & Durroux, T. Fluorescent agonists and antagonists for vasopressin/oxytocin G protein-coupled receptors: usefulness in ligand screening assays and receptor studies. Mini Rev. Med. Chem. 8, 996-1005 (2008).
    • (2008) Mini Rev. Med. Chem. , vol.8 , pp. 996-1005
    • Mouillac, B.1    Manning, M.2    Durroux, T.3
  • 25
    • 0030592691 scopus 로고    scopus 로고
    • Two aromatic residues regulate the response of the human oxytocin receptor to the partial agonist arginine vasopressin
    • Chini, B. et al. Two aromatic residues regulate the response of the human oxytocin receptor to the partial agonist arginine vasopressin. FEBS Lett. 397, 201-206 (1996).
    • (1996) FEBS Lett , vol.397 , pp. 201-206
    • Chini, B.1
  • 26
    • 0033802337 scopus 로고    scopus 로고
    • Binding properties of a selective tritiated vasopressin V2 receptor antagonist [H]-SR 121463
    • Serradeil-Le Gal, C. et al. Binding properties of a selective tritiated vasopressin V2 receptor antagonist, [H]-SR 121463. Kidney Int. 58, 1613-1622 (2000).
    • (2000) Kidney Int , vol.58 , pp. 1613-1622
    • Serradeil-Le Gal, C.1
  • 27
    • 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. et al. Cell-surface protein-protein interaction analysis with time-resolved FRET and snap-tag technologies: application to GPCR oligomerization. Nat. Methods 5, 561-567 (2008).
    • (2008) Nat. Methods , vol.5 , pp. 561-567
    • Maurel, D.1
  • 28
    • 0036258990 scopus 로고    scopus 로고
    • G protein-coupled receptor allosterism and complexing
    • Christopoulos, A. & Kenakin, T. G protein-coupled receptor allosterism and complexing. Pharmacol. Rev. 54, 323-374 (2002).
    • (2002) Pharmacol. Rev. , vol.54 , pp. 323-374
    • Christopoulos, A.1    Kenakin, T.2
  • 29
    • 20544449873 scopus 로고    scopus 로고
    • Principles: A model for the allosteric interactions between ligand binding sites within a dimeric GPCR
    • Durroux, T. Principles: a model for the allosteric interactions between ligand binding sites within a dimeric GPCR. Trends Pharmacol. Sci. 26, 376-384 (2005).
    • (2005) Trends Pharmacol. Sci. , vol.26 , pp. 376-384
    • Durroux, T.1
  • 30
    • 0030944020 scopus 로고    scopus 로고
    • Kinetic studies of co-operativity at atrial muscarinic M2 receptors with an "infinite dilution" procedure
    • Christopoulos, A., Lanzafame, A., Ziegler, A. & Mitchelson, F. Kinetic studies of co-operativity at atrial muscarinic M2 receptors with an "infinite dilution" procedure. Biochem. Pharmacol. 53, 795-800 (1997).
    • (1997) Biochem. Pharmacol. , vol.53 , pp. 795-800
    • Christopoulos, A.1    Lanzafame, A.2    Ziegler, A.3    Mitchelson, F.4
  • 31
    • 0035920099 scopus 로고    scopus 로고
    • Direct identification of human oxytocin receptor-binding domains using a photoactivatable cyclic peptide antagonist: Comparison with the human V1a vasopressin receptor
    • Breton, C. et al. Direct identification of human oxytocin receptor-binding domains using a photoactivatable cyclic peptide antagonist: comparison with the human V1a vasopressin receptor. J. Biol. Chem. 276, 26931-26941 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 26931-26941
    • Breton, C.1
  • 32
    • 0032491601 scopus 로고    scopus 로고
    • Identification of residues responsible for the selective binding of peptide antagonists and agonists in the V2 vasopressin receptor
    • Cotte, N. et al. Identification of residues responsible for the selective binding of peptide antagonists and agonists in the V2 vasopressin receptor. J. Biol. Chem. 273, 29462-29468 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 29462-29468
    • Cotte, N.1
  • 33
    • 0031678376 scopus 로고    scopus 로고
    • Mapping peptide antagonist binding sites of the human V1a and V2 vasopressin receptors
    • Mouillac, B. et al. Mapping peptide antagonist binding sites of the human V1a and V2 vasopressin receptors. Adv. Exp. Med. Biol. 449, 359-361 (1998).
    • (1998) Adv. Exp. Med. Biol. , vol.449 , pp. 359-361
    • Mouillac, B.1
  • 34
    • 0031576219 scopus 로고    scopus 로고
    • Mapping peptide-binding domains of the human V1a vasopressin receptor with a photoactivatable linear peptide antagonist
    • Phalipou, S. et al. Mapping peptide-binding domains of the human V1a vasopressin receptor with a photoactivatable linear peptide antagonist. J. Biol. Chem. 272, 26536-26544 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 26536-26544
    • Phalipou, S.1
  • 35
    • 0037030691 scopus 로고    scopus 로고
    • Synthesis and characterization of fluorescent antagonists and agonists for human oxytocin and vasopressin V(1)(a) receptors
    • Terrillon, S. et al. Synthesis and characterization of fluorescent antagonists and agonists for human oxytocin and vasopressin V(1)(a) receptors. J. Med. Chem. 45, 2579-2588 (2002).
    • (2002) J. Med. Chem. , vol.45 , pp. 2579-2588
    • Terrillon, S.1
  • 36
    • 69249158290 scopus 로고    scopus 로고
    • Allosteric communication between protomers of dopamine class A GPCR dimers modulates activation
    • Han, Y., Moreira, I.S., Urizar, E., Weinstein, H. & Javitch, J.A. Allosteric communication between protomers of dopamine class A GPCR dimers modulates activation. Nat. Chem. Biol. 5, 688-695 (2009).
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 688-695
    • Han, Y.1    Moreira, I.S.2    Urizar, E.3    Weinstein, H.4    Javitch, J.A.5
  • 37
    • 0141841603 scopus 로고    scopus 로고
    • Dual inhibition of beta-adrenergic and angiotensin II receptors by a single antagonist: A functional role for receptor-receptor interaction in vivo
    • Barki-Harrington, L., Luttrell, L.M. & Rockman, H.A. Dual inhibition of beta-adrenergic and angiotensin II receptors by a single antagonist: a functional role for receptor-receptor interaction in vivo. Circulation 108, 1611-1618 (2003).
    • (2003) Circulation , vol.108 , pp. 1611-1618
    • Barki-Harrington, L.1    Luttrell, L.M.2    Rockman, H.A.3
  • 38
    • 33845720603 scopus 로고    scopus 로고
    • Asymmetric conformational changes in a GPCR dimer controlled by G-proteins
    • Damian, M., Martin, A., Mesnier, D., Pin, J.P. & Baneres, J.L. Asymmetric conformational changes in a GPCR dimer controlled by G-proteins. EMBO J. 25, 5693-5702 (2006).
    • (2006) EMBO J , vol.25 , pp. 5693-5702
    • Damian, M.1    Martin, A.2    Mesnier, D.3    Pin, J.P.4    Baneres, J.L.5
  • 39
    • 0038576278 scopus 로고    scopus 로고
    • The fourth transmembrane segment forms the interface of the dopamine D2 receptor homodimer
    • Guo, W., Shi, L. & Javitch, J.A. The fourth transmembrane segment forms the interface of the dopamine D2 receptor homodimer. J. Biol. Chem. 278, 4385-4388 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 4385-4388
    • Guo, W.1    Shi, L.2    Javitch, J.A.3
  • 40
    • 38349054282 scopus 로고    scopus 로고
    • Conformational cross-talk between alpha2A-adrenergic and mu-opioid receptors controls cell signaling
    • Vilardaga, J.P. et al. Conformational cross-talk between alpha2A-adrenergic and mu-opioid receptors controls cell signaling. Nat. Chem. Biol. 4, 126-131 (2008).
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 126-131
    • Vilardaga, J.P.1
  • 41
    • 33645802812 scopus 로고    scopus 로고
    • Allosteric modulation of binding properties between units of chemokine receptor homo- and hetero-oligomers
    • Springael, J.Y. et al. Allosteric modulation of binding properties between units of chemokine receptor homo- and hetero-oligomers. Mol. Pharmacol. 69, 1652-1661 (2006).
    • (2006) Mol. Pharmacol. , vol.69 , pp. 1652-1661
    • Springael, J.Y.1
  • 42
    • 21644435532 scopus 로고    scopus 로고
    • Asymmetric functioning of dimeric metabotropic glutamate receptors disclosed by positive allosteric modulators
    • Goudet, C. et al. Asymmetric functioning of dimeric metabotropic glutamate receptors disclosed by positive allosteric modulators. J. Biol. Chem. 280, 24380-24385 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 24380-24385
    • Goudet, C.1
  • 43
    • 20044364938 scopus 로고    scopus 로고
    • Evidence for a single heptahelical domain being turned on upon activation of a dimeric GPCR
    • Hlavackova, V. et al. Evidence for a single heptahelical domain being turned on upon activation of a dimeric GPCR. EMBO J. 24, 499-509 (2005).
    • (2005) EMBO J , vol.24 , pp. 499-509
    • Hlavackova, V.1
  • 44
    • 27144548417 scopus 로고    scopus 로고
    • Dimerization of chemokine receptors and its functional consequences
    • Springael, J.Y., Urizar, E. & Parmentier, M. Dimerization of chemokine receptors and its functional consequences. Cytokine Growth Factor Rev. 16, 611-623 (2005).
    • (2005) Cytokine Growth Factor Rev , vol.16 , pp. 611-623
    • Springael, J.Y.1    Urizar, E.2    Parmentier, M.3
  • 45
    • 0242460494 scopus 로고    scopus 로고
    • Metabotropic glutamate 1alpha and adenosine A1 receptors assemble into functionally interacting complexes
    • Ciruela, F. et al. Metabotropic glutamate 1alpha and adenosine A1 receptors assemble into functionally interacting complexes. J. Biol. Chem. 276, 18345-18351 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 18345-18351
    • Ciruela, F.1
  • 46
    • 71449122467 scopus 로고    scopus 로고
    • Hetero-oligomerization of CCR2 CCR5 and CXCR4 and the protean effects of "selective" antagonists
    • Sohy, D. et al. Hetero-oligomerization of CCR2, CCR5, and CXCR4 and the protean effects of "selective" antagonists. J. Biol. Chem. 284, 31270-31279 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 31270-31279
    • Sohy, D.1
  • 47
    • 30044442319 scopus 로고    scopus 로고
    • Opioid-induced tolerance and dependence in mice is modulated by the distance between pharmacophores in a bivalent ligand series
    • Daniels, D.J. et al. Opioid-induced tolerance and dependence in mice is modulated by the distance between pharmacophores in a bivalent ligand series. Proc. Natl. Acad. Sci. USA 102, 19208-19213 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 19208-19213
    • Daniels, D.J.1
  • 48
    • 2442597256 scopus 로고    scopus 로고
    • Cell surface expression of alpha1D-adrenergic receptors is controlled by heterodimerization with alpha1B-adrenergic receptors
    • Hague, C., Uberti, M.A., Chen, Z., Hall, R.A. & Minneman, K.P. Cell surface expression of alpha1D-adrenergic receptors is controlled by heterodimerization with alpha1B-adrenergic receptors. J. Biol. Chem. 279, 15541-15549 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 15541-15549
    • Hague, C.1    Uberti, M.A.2    Chen, Z.3    Hall, R.A.4    Minneman, K.P.5
  • 49
    • 62949087122 scopus 로고    scopus 로고
    • The apparent cooperativity of some GPCRs does not necessarily imply dimerization
    • Chabre, M., Deterre, P. & Antonny, B. The apparent cooperativity of some GPCRs does not necessarily imply dimerization. Trends Pharmacol. Sci. 30, 182-187 (2009).
    • (2009) Trends Pharmacol. Sci. , vol.30 , pp. 182-187
    • Chabre, M.1    Deterre, P.2    Antonny, B.3
  • 50
    • 68249159980 scopus 로고    scopus 로고
    • Crosstalk between GABA(B) and mGlu1a receptors reveals new insight into GPCR signal integration
    • Rives, M.L. et al. Crosstalk between GABA(B) and mGlu1a receptors reveals new insight into GPCR signal integration. EMBO J. 28, 2195-2208 (2009).
    • (2009) EMBO J , vol.28 , pp. 2195-2208
    • Rives, M.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.