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Functional significance of oligomerization of G-protein coupled receptors
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Coexpression studies with mutant muscarinic/adrenergic receptors provide evidence for intermolecular 'cross-talk' between G-protein-linked receptors
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A peptide derived from a beta2-adrenergic receptor transmembrane domain inhibits both receptor dimerization and activation
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G protein coupled receptor function as oligomers in vivo
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Overton MC, Blumer KJ. G protein coupled receptor function as oligomers in vivo. Curr Biol. 10:2000;341-344.
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Overton, M.C.1
Blumer, K.J.2
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0034616021
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Receptors for dopamine and somatostatin: Formation of hetero-oligomers with enhanced functional activity
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This paper was the first published example of heterodimerization between two distinct classes of GPCR. The paper uses the powerful technique of photo-bleaching FRET to study the dimerization process
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Rocheville M, Lange DC, Kumar U, Patel SC, Patel RC, Patel YC. Receptors for dopamine and somatostatin: formation of hetero-oligomers with enhanced functional activity. Science. 288:2000;154-157. This paper was the first published example of heterodimerization between two distinct classes of GPCR. The paper uses the powerful technique of photo-bleaching FRET to study the dimerization process.
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Science
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Rocheville, M.1
Lange, D.C.2
Kumar, U.3
Patel, S.C.4
Patel, R.C.5
Patel, Y.C.6
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8
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0034724192
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Detection of beta 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET)
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This paper describes the use of BRET to study receptor dimerization
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Angers S, Salahpour A, Joly E, Hilairet S, Chelsky D, Dennis M, Bouvier M. Detection of beta 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET). Proc Natl Acad Sci USA. 97:2000;3684-3689. This paper describes the use of BRET to study receptor dimerization.
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Proc Natl Acad Sci USA
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Angers, S.1
Salahpour, A.2
Joly, E.3
Hilairet, S.4
Chelsky, D.5
Dennis, M.6
Bouvier, M.7
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0032422771
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Domain swapping in G-protein coupled receptor dimers
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Gouldson PR, Snell CR, Bywater RP, Higgs C, Reynolds CA. Domain swapping in G-protein coupled receptor dimers. Protein Eng. 11:1998;1181-1193.
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Gouldson, P.R.1
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Bywater, R.P.3
Higgs, C.4
Reynolds, C.A.5
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10
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0033806215
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Dimerization and domain swapping in G-protein coupled receptors: A computational study
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This interesting paper discusses a number of potential models including domain swapping to explain the formation of receptor dimers
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Gouldson PR, Higgs C, Smith RE, Dean MK, Gkoutos GV, Reynolds CA. Dimerization and domain swapping in G-protein coupled receptors: a computational study. Neuropsychopharmacology. 23:2000;560-577. This interesting paper discusses a number of potential models including domain swapping to explain the formation of receptor dimers.
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Neuropsychopharmacology
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Gouldson, P.R.1
Higgs, C.2
Smith, R.E.3
Dean, M.K.4
Gkoutos, G.V.5
Reynolds, C.A.6
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11
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0033578005
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G protein coupled receptor heterodimerization modulates receptor function
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This long-awaited paper was the first to show that opioid receptors could indeed form heterodimers and that this might explain some of the mismatch between in vivo pharmacology and cloned receptor pharmacology
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Jordan BA, Devi LA. G protein coupled receptor heterodimerization modulates receptor function. Nature. 399:1999;697-700. This long-awaited paper was the first to show that opioid receptors could indeed form heterodimers and that this might explain some of the mismatch between in vivo pharmacology and cloned receptor pharmacology.
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Nature
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Jordan, B.A.1
Devi, L.A.2
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Mechanism of transdominant inhibition of CCR5-mediated HIV-1 infection by ccr5delta32
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Benkirane, M.1
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Jeang, K.T.5
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0033667466
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A trafficking checkpoint controls GABAB receptor heterodimerization
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B(2) even when it is expressed at the cell surface
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B(2) even when it is expressed at the cell surface.
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Neuron
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Mitrovic, M.M.1
Jan, Y.N.2
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0005169503
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GABA(B) receptors function as a heteromeric assembly of the subunits GABA(B)R1 and GABA(B)R2
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Jones KA, Borowsky B, Tamm JA, Craig DA, Durkin MM, Dai M, Yao WJ, Johnson M, Gunwaldsen C, Huang LY, et al. GABA(B) receptors function as a heteromeric assembly of the subunits GABA(B)R1 and GABA(B)R2. Nature. 396:1998;674-679.
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Jones, K.A.1
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15
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Heterodimerization is required for the formation of a functional GABA(B) receptor
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White JH, Wise A, Main MJ, Green A, Fraser NJ, Disney GH, Barnes AA, Emson P, Foord SM, Marshall FH. Heterodimerization is required for the formation of a functional GABA(B) receptor. Nature. 396:1998;679-682.
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White, J.H.1
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0032542382
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GABA(B)-receptor subtypes assemble into functional heteromeric complexes
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Kaupmann K, Malitschek B, Schuler V, Heid J, Froestl W, Beck P, Mosbacher J, Bischoff S, Kulik A, Shigemoto R, et al. GABA(B)-receptor subtypes assemble into functional heteromeric complexes. Nature. 396:1998;683-687.
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Kaupmann, K.1
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B receptor activity
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B receptor activity. J Biol Chem. 274:1999;7607-7610.
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Ng, G.Y.1
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Opioids: First lessons from knockout mice
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Kieffer BL. Opioids: first lessons from knockout mice. Trends Pharmacol Sci. 20:1999;19-26.
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Kieffer, B.L.1
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20
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0034714335
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Oligomerization of μ and δ opioid receptors. Generation of novel functional properties
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Another interesting paper on opioid receptor dimerization - this time between μ and δ receptors. Of signficiance is the fact that some endogenous peptides have a higher affinity for the heterodimer than the individual receptors
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George SR, Fan T, Xie Z, Tse R, Tam V, Varghese G, O'Dowd BF. Oligomerization of μ and δ opioid receptors. Generation of novel functional properties. J Biol Chem. 275:2000;26128-26135. Another interesting paper on opioid receptor dimerization - this time between μ and δ receptors. Of signficiance is the fact that some endogenous peptides have a higher affinity for the heterodimer than the individual receptors.
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J Biol Chem
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George, S.R.1
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Xie, Z.3
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Tam, V.5
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O'Dowd, B.F.7
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21
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0032587196
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Serotonin 5-HT1B and 5-HT1D receptors form homodimers when expressed alone and heterodimers when co-expressed
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An interesting example of homo- and heterodimerization between members of the 5-HT receptor family
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Xie Z, Lee SP, O'Dowd BF, George SR. Serotonin 5-HT1B and 5-HT1D receptors form homodimers when expressed alone and heterodimers when co-expressed. FEBS Letters. 456:1999;63-67. An interesting example of homo- and heterodimerization between members of the 5-HT receptor family.
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(1999)
FEBS Letters
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Xie, Z.1
Lee, S.P.2
O'Dowd, B.F.3
George, S.R.4
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22
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0034677745
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Subtypes of the somatostatin receptor assemble as functional homo- And heterodimers
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This paper provides a good example of functional rescue of a mutant receptor through dimerization
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Rocheville M, Lange DC, Kumar U, Sasi R, Patel RC, Patel YC. Subtypes of the somatostatin receptor assemble as functional homo- and heterodimers. J Biol Chem. 275:2000;7862-7869. This paper provides a good example of functional rescue of a mutant receptor through dimerization.
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J Biol Chem
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Rocheville, M.1
Lange, D.C.2
Kumar, U.3
Sasi, R.4
Patel, R.C.5
Patel, Y.C.6
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23
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0034682445
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Dopamine D1 and adenosine A1 receptors form functionally interacting heteromeric complexes
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In this example of heterodimerization an additional layer of complexity is added with the finding that receptors can form co-clusters. This paper is also of interest because the relationship between the receptors in the heterodimer appears to be one of antagonism rather than synergy
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Gines S, Hillion J, Torvinen M, Le Crom S, Casado V, Canela EI, Rondin S, Lew JY, Watson S, Zoli M, et al. Dopamine D1 and adenosine A1 receptors form functionally interacting heteromeric complexes. Proc Natl Acad Sci USA. 97:2000;8606-8611. In this example of heterodimerization an additional layer of complexity is added with the finding that receptors can form co-clusters. This paper is also of interest because the relationship between the receptors in the heterodimer appears to be one of antagonism rather than synergy.
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(2000)
Proc Natl Acad Sci USA
, vol.97
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Gines, S.1
Hillion, J.2
Torvinen, M.3
Le Crom, S.4
Casado, V.5
Canela, E.I.6
Rondin, S.7
Lew, J.Y.8
Watson, S.9
Zoli, M.10
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24
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0034618268
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AT-receptor heterodimers show enhanced G-protein activation and altered receptor sequestration
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Heterodimers between angiotensin and bradykinin receptor in smooth muscle lead to enhanced signalling through G proteins by angiotensin
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Abdalla S, Lother H, Quitterer U. AT-receptor heterodimers show enhanced G-protein activation and altered receptor sequestration. Nature. 407:2000;94-98. Heterodimers between angiotensin and bradykinin receptor in smooth muscle lead to enhanced signalling through G proteins by angiotensin.
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Nature
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Abdalla, S.1
Lother, H.2
Quitterer, U.3
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25
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0034611727
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PAR3 is a cofactor for PAR4 activation by thrombin
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Nakanishi-Matsui M, Zheng YW, Sulciner DJ, Weiss EJ, Ludeman MJ, Coughlin SR. PAR3 is a cofactor for PAR4 activation by thrombin. Nature. 404:2000;609-613.
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Nature
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Nakanishi-Matsui, M.1
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Ludeman, M.J.5
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26
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0032574982
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RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor
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McLatchie, L.M.1
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Multiple amylin receptors arise from receptor activity-modifying protein interaction with the calcitonin receptor gene product
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Christopoulos G, Perry KJ, Morfis M, Tilakaratne N, Gao Y, Fraser NJ, Main MJ, Foord SM, Sexton PM. Multiple amylin receptors arise from receptor activity-modifying protein interaction with the calcitonin receptor gene product. Mol Pharmacol. 56:1999;235-242.
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Mol Pharmacol
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Christopoulos, G.1
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0034048720
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Dual signaling regulated by calcyon, a D1 dopamine receptor interacting protein
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Lezcano N, Mrzljak L, Eubanks S, Levenson R, Goldman-Rakic P, Bergson C. Dual signaling regulated by calcyon, a D1 dopamine receptor interacting protein. Science. 287:2000;1660-1664.
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Science
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Lezcano, N.1
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Bergson, C.6
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29
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0034688225
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Direct protein-protein coupling enables cross-talk between dopamine D5 and gamma-aminobutyric acid A receptors
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This fascinating paper took the heterodimerization of GPCRs one step further by showing interactions with receptors from a completely different class - ligand-gated ion channels
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Liu F, Wan Q, Pristupa ZB, Yu XM, Wang YT, Niznik HB. Direct protein-protein coupling enables cross-talk between dopamine D5 and gamma-aminobutyric acid A receptors. Nature. 403:2000;274-280. This fascinating paper took the heterodimerization of GPCRs one step further by showing interactions with receptors from a completely different class - ligand-gated ion channels.
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(2000)
Nature
, vol.403
, pp. 274-280
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Liu, F.1
Wan, Q.2
Pristupa, Z.B.3
Yu, X.M.4
Wang, Y.T.5
Niznik, H.B.6
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30
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0034737483
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The beta(2)-adrenergic receptor mediates extracellular signal-regulated kinase activation via assembly of a multi-receptor complex with the epidermal growth factor receptor
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Maudsley S, Pierce KL, Zamah AM, Miller WE, Ahn S, Daaka Y, Lefkowitz RJ, Luttrell LM. The beta(2)-adrenergic receptor mediates extracellular signal-regulated kinase activation via assembly of a multi-receptor complex with the epidermal growth factor receptor. J Biol Chem. 275:2000;9572-9580.
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J Biol Chem
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Maudsley, S.1
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Miller, W.E.4
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Daaka, Y.6
Lefkowitz, R.J.7
Luttrell, L.M.8
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