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Volumn 1840, Issue 1, 2014, Pages 16-33

Structural features of the G-protein/GPCR interactions

Author keywords

Coupling determinant; G protein coupled receptor G protein coupling; Oligomerization; Specificity

Indexed keywords

G PROTEIN COUPLED RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN ALPHA SUBUNIT; GUANINE NUCLEOTIDE BINDING PROTEIN GAMMA SUBUNIT; HETEROTRIMERIC GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 84884999937     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2013.08.027     Document Type: Review
Times cited : (99)

References (343)
  • 1
    • 70450171097 scopus 로고    scopus 로고
    • Signaling through G protein coupled receptors
    • N. Tuteja Signaling through G protein coupled receptors Plant Signal. Behav. 4 2009 942 947
    • (2009) Plant Signal. Behav. , vol.4 , pp. 942-947
    • Tuteja, N.1
  • 2
    • 77953384365 scopus 로고    scopus 로고
    • Complexes between photoactivated rhodopsin and transducin: Progress and questions
    • B. Jastrzebska, Y. Tsybovsky, and K. Palczewski Complexes between photoactivated rhodopsin and transducin: progress and questions Biochem. J. 428 2010 1 10
    • (2010) Biochem. J. , vol.428 , pp. 1-10
    • Jastrzebska, B.1    Tsybovsky, Y.2    Palczewski, K.3
  • 3
    • 0031984517 scopus 로고    scopus 로고
    • The many faces of G protein signaling
    • DOI 10.1074/jbc.273.2.669
    • H.E. Hamm The many faces of G protein signaling J. Biol. Chem. 273 1998 669 672 (Pubitemid 28049148)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.2 , pp. 669-672
    • Hamm, H.E.1
  • 5
    • 0033572358 scopus 로고    scopus 로고
    • The G protein subunit gene families
    • DOI 10.1006/geno.1999.5992
    • G.B. Downes, and N. Gautam The G protein subunit gene families Genomics 62 1999 544 552 (Pubitemid 30075189)
    • (1999) Genomics , vol.62 , Issue.3 , pp. 544-552
    • Downes, G.B.1    Gautam, N.2
  • 6
    • 84885369916 scopus 로고    scopus 로고
    • Structures of heterotrimeric G proteins and their complexes
    • S.R. Sprang Structures of heterotrimeric G proteins and their complexes Handb. Cell Signal. 3 2010 11
    • (2010) Handb. Cell Signal. , vol.3 , pp. 11
    • Sprang, S.R.1
  • 8
    • 0028862026 scopus 로고
    • Tertiary and quaternary structural changes in G(Ialpha1) induced by GTP hydrolysis
    • M.B. Mixon, E. Lee, D.E. Coleman, A.M. Berghuis, A.G. Gilman, and S.R. Sprang Tertiary and quaternary structural changes in G(Ialpha1) induced by GTP hydrolysis Science 270 1995 954 960
    • (1995) Science , vol.270 , pp. 954-960
    • Mixon, M.B.1    Lee, E.2    Coleman, D.E.3    Berghuis, A.M.4    Gilman, A.G.5    Sprang, S.R.6
  • 10
    • 0028237708 scopus 로고
    • Structural determinants for activation of the α-subunit of a heterotrimeric G protein
    • DOI 10.1038/369621a0
    • D.G. Lambright, J.P. Noel, H.E. Hamm, and P.B. Sigler Structural determinants for activation of the alpha-subunit of a heterotrimeric G-protein Nature 369 1994 621 628 (Pubitemid 24199466)
    • (1994) Nature , vol.369 , Issue.6482 , pp. 621-628
    • Lambright, D.G.1    Noel, J.P.2    Hamm, H.E.3    Sigler, P.B.4
  • 11
    • 0030589139 scopus 로고    scopus 로고
    • Structure of the GDP-Pi complex of Gly203→Ala G(iα1): A mimic of the ternary product complex of Gα-catalyzed GTP hydrolysis
    • A.M. Berghuis, E. Lee, A.S. Raw, A.G. Gilman, and S.R. Sprang Structure of the GDP-Pi complex of Gly203- > G(i alpha 1): a mimic of the ternary product complex of G alpha-catalyzed GTP hydrolysis Structure 4 1996 1277 1290 (Pubitemid 26420497)
    • (1996) Structure , vol.4 , Issue.11 , pp. 1277-1290
    • Berghuis, A.M.1    Lee, E.2    Raw, A.S.3    Gilman, A.G.4    Sprang, S.R.5
  • 12
    • 0032514722 scopus 로고    scopus 로고
    • 2+: A crystallographic titration experiment
    • DOI 10.1021/bi9810306
    • D.E. Coleman, and S.R. Sprang Crystal structures of the G protein G(i alpha 1) complexed with GDP and Mg2 +: a crystallographic titration experiment Biochemistry 37 1998 14376 14385 (Pubitemid 28489043)
    • (1998) Biochemistry , vol.37 , Issue.41 , pp. 14376-14385
    • Coleman, D.E.1    Sprang, S.R.2
  • 13
    • 70349810683 scopus 로고    scopus 로고
    • Structural evidence for a sequential release mechanism for activation of heterotrimeric G proteins
    • N. Kapoor, S.T. Menon, R. Chauhan, P. Sachdev, and T.P. Sakmar Structural evidence for a sequential release mechanism for activation of heterotrimeric G proteins J. Mol. Biol. 393 2009 882 897
    • (2009) J. Mol. Biol. , vol.393 , pp. 882-897
    • Kapoor, N.1    Menon, S.T.2    Chauhan, R.3    Sachdev, P.4    Sakmar, T.P.5
  • 15
    • 34547571461 scopus 로고    scopus 로고
    • Structure-based Protocol for Identifying Mutations that Enhance Protein-Protein Binding Affinities
    • DOI 10.1016/j.jmb.2007.05.096, PII S0022283607007668
    • D.W. Sammond, Z.M. Eletr, C. Purbeck, R.J. Kimple, D.P. Siderovski, and B. Kuhlman Structure-based protocol for identifying mutations that enhance protein-protein binding affinities J. Mol. Biol. 371 2007 1392 1404 (Pubitemid 47198253)
    • (2007) Journal of Molecular Biology , vol.371 , Issue.5 , pp. 1392-1404
    • Sammond, D.W.1    Eletr, Z.M.2    Purbeck, C.3    Kimple, R.J.4    Siderovski, D.P.5    Kuhlman, B.6
  • 17
    • 79851474025 scopus 로고    scopus 로고
    • The crystal structure of a self-activating G protein alpha subunit reveals its distinct mechanism of signal initiation
    • J.C. Jones, J.W. Duffy, M. Machius, B.R.S. Temple, H.G. Dohlman, and A.M. Jones The crystal structure of a self-activating G protein alpha subunit reveals its distinct mechanism of signal initiation Sci. Signal. 4 2011 ra8
    • (2011) Sci. Signal. , vol.4 , pp. 8
    • Jones, J.C.1    Duffy, J.W.2    Machius, M.3    Temple, B.R.S.4    Dohlman, H.G.5    Jones, A.M.6
  • 18
    • 84860907660 scopus 로고    scopus 로고
    • A P-loop mutation in Gα subunits prevents transition to the active state: Implications for G-protein signaling in fungal pathogenesis
    • D.E. Bosch, F.S. Willard, R. Ramanujam, A.J. Kimple, M.D. Willard, N.I. Naqvi, and D.P. Siderovski A P-loop mutation in Gα subunits prevents transition to the active state: implications for G-protein signaling in fungal pathogenesis PloS Pathog. 8 2012 e1002553
    • (2012) PloS Pathog. , vol.8 , pp. 1002553
    • Bosch, D.E.1    Willard, F.S.2    Ramanujam, R.3    Kimple, A.J.4    Willard, M.D.5    Naqvi, N.I.6    Siderovski, D.P.7
  • 19
    • 85015469735 scopus 로고    scopus 로고
    • Regulators of G-protein signaling accelerate GPCR signaling kinetics and govern sensitivity solely by accelerating GTPase activity
    • Correction for Lambert Regulators of G-protein signaling accelerate GPCR signaling kinetics and govern sensitivity solely by accelerating GTPase activity Proc. Natl. Acad. Sci. 109 2012 2175
    • (2012) Proc. Natl. Acad. Sci. , vol.109 , pp. 2175
    • For Lambert, C.1
  • 20
    • 30144445198 scopus 로고    scopus 로고
    • 12/13 proteins
    • DOI 10.1021/bi051729t
    • B. Kreutz, D.M. Yau, M.R. Nance, S. Tanabe, J.J.G. Tesmer, and T. Kozasa A new approach to producing functional G alpha subunits yields the activated and deactivated structures of G alpha(12/13) proteins Biochemistry 45 2006 167 174 (Pubitemid 43054094)
    • (2006) Biochemistry , vol.45 , Issue.1 , pp. 167-174
    • Kreutz, B.1    Yau, D.M.2    Nance, M.R.3    Tanabe, S.4    Tesmer, J.J.G.5    Kozasa, T.6
  • 22
    • 0037171778 scopus 로고    scopus 로고
    • Structural determinants for GoLoco-induced inhibition of nucleotide release by Gα subunits
    • DOI 10.1038/416878a
    • R.J. Kimple, M.E. Kimple, L. Betts, J. Sondek, and D.P. Siderovski Structural determinants for GoLoco-induced inhibition of nucleotide release by G alpha subunits Nature 416 2002 878 881 (Pubitemid 34453747)
    • (2002) Nature , vol.416 , Issue.6883 , pp. 878-881
    • Kimple, R.J.1    Kimple, M.E.2    Betts, L.3    Sondek, J.4    Siderovski, D.P.5
  • 23
    • 0028027596 scopus 로고
    • Gtpase mechanism of Gproteins from the 1.7 A crystal structure of transducin alpha-center.GDP.ALF4
    • J. Sondek, D.G. Lambright, J.P. Noel, H.E. Hamm, and P.B. Sigler Gtpase mechanism of Gproteins from the 1.7 A crystal structure of transducin alpha-center.GDP.ALF4- Nature 372 1994 276 279
    • (1994) Nature , vol.372 , pp. 276-279
    • Sondek, J.1    Lambright, D.G.2    Noel, J.P.3    Hamm, H.E.4    Sigler, P.B.5
  • 24
    • 0035931919 scopus 로고    scopus 로고
    • Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 Å
    • DOI 10.1038/35059138
    • K.C. Slep, M.A. Kercher, W. He, C.W. Cowan, T.G. Wensel, and P.B. Sigler Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 A Nature 409 2001 1071 1077 (Pubitemid 32204063)
    • (2001) Nature , vol.409 , Issue.6823 , pp. 1071-1077
    • Slep, K.C.1    Kercher, M.A.2    He, W.3    Cowan, C.W.4    Wensel, T.G.5    Sigler, P.B.6
  • 25
    • 0030982264 scopus 로고    scopus 로고
    • --activated G(iα1): Stabilization of the transition state for GTP hydrolysis
    • J.J.G. Tesmer, D.M. Berman, A.G. Gilman, and S.R. Sprang Structure of RGS4 bound to AlF4-activated G(i alpha 1): stabilization of the transition state for GTP hydrolysis Cell 89 1997 251 261 (Pubitemid 27199897)
    • (1997) Cell , vol.89 , Issue.2 , pp. 251-261
    • Tesmer, J.J.G.1    Berman, D.M.2    Gilman, A.G.3    Sprang, S.R.4
  • 29
    • 84874888362 scopus 로고    scopus 로고
    • Structural and functional analysis of the regulator of G protein signaling 2 (RGS2)-Gαq complex
    • M. Nance, B. Kreutz, V. Tesmer, R. Sterne-Marr, T. Kozasa, and J. Tesmer Structural and functional analysis of the regulator of G protein signaling 2 (RGS2)-Gαq complex Structure 21 2013 438 448
    • (2013) Structure , vol.21 , pp. 438-448
    • Nance, M.1    Kreutz, B.2    Tesmer, V.3    Sterne-Marr, R.4    Kozasa, T.5    Tesmer, J.6
  • 31
    • 15544373780 scopus 로고    scopus 로고
    • Structure of the p115RhoGEF rgRGS domain-G alpha 13/i1 chimera complex suggests convergent evolution of a GTPase activator
    • Z. Chen, W.D. Singer, P.C. Sternweis, and S.R. Sprang Structure of the p115RhoGEF rgRGS domain-G alpha 13/i1 chimera complex suggests convergent evolution of a GTPase activator Nat. Struct. Mol. Biol. 12 2005 191 197
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 191-197
    • Chen, Z.1    Singer, W.D.2    Sternweis, P.C.3    Sprang, S.R.4
  • 32
    • 28844463975 scopus 로고    scopus 로고
    • q-GRK2-Gβγ complex
    • DOI 10.1126/science.1118890
    • V.M. Tesmer, T. Kawano, A. Shankaranarayanan, T. Kozasa, and J.J.G. Tesmer Snapshot of activated G proteins at the membrane: the G alpha(q)-GRK2-G beta gamma complex Science 310 2005 1686 1690 (Pubitemid 41780792)
    • (2005) Science , vol.310 , Issue.5754 , pp. 1686-1690
    • Tesmer, V.M.1    Kawano, T.2    Shankaranarayanan, A.3    Kozasa, T.4    Tesmer, J.J.G.5
  • 33
    • 0027132717 scopus 로고
    • The 2.2-A crystal structure of transducin apha complexed with GTP-GAMMA S
    • J.P. Noel, H.E. Hamm, and P.B. Sigler The 2.2-A crystal structure of transducin apha complexed with GTP-GAMMA S Nature 366 1993 654 663
    • (1993) Nature , vol.366 , pp. 654-663
    • Noel, J.P.1    Hamm, H.E.2    Sigler, P.B.3
  • 34
    • 0033546001 scopus 로고    scopus 로고
    • Structure of G(i alpha 1)center dot GppNHp, autoinhibition in a G(alpha) protein-substrate complex
    • D.E. Coleman, and S.R. Sprang Structure of G(i alpha 1)center dot GppNHp, autoinhibition in a G(alpha) protein-substrate complex J. Biol. Chem. 274 1999 16669 16672
    • (1999) J. Biol. Chem. , vol.274 , pp. 16669-16672
    • Coleman, D.E.1    Sprang, S.R.2
  • 35
    • 0027965652 scopus 로고
    • Structures of active conformations of G(ialpha1) and the mechanism of GTP hydrolysis
    • D.E. Coleman, A.M. Berghuis, E. Lee, M.E. Linder, A.G. Gilman, and S.R. Sprang Structures of active conformations of G(ialpha1) and the mechanism of GTP hydrolysis Science 265 1994 1405 1412
    • (1994) Science , vol.265 , pp. 1405-1412
    • Coleman, D.E.1    Berghuis, A.M.2    Lee, E.3    Linder, M.E.4    Gilman, A.G.5    Sprang, S.R.6
  • 36
    • 0031436245 scopus 로고    scopus 로고
    • Crystal structure of the adenylyl cyclase activator G(sα)
    • DOI 10.1126/science.278.5345.1943
    • R.K. Sunahara, J.J.G. Tesmer, A.G. Gilman, and S.R. Sprang Crystal structure of the adenylyl cyclase activator G(S alpha) Science 278 1997 1943 1947 (Pubitemid 28013235)
    • (1997) Science , vol.278 , Issue.5345 , pp. 1943-1947
    • Sunahara, R.K.1    Tesmer, J.J.G.2    Gilman, A.G.3    Sprang, S.R.4
  • 37
    • 2642689663 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domains of adenylyl cyclase in a complex with G(sα).GTPγS
    • DOI 10.1126/science.278.5345.1907
    • J.J.G. Tesmer, R.K. Sunahara, A.G. Gilman, and S.R. Sprang Crystal structure of the catalytic domains of adenylyl cyclase in a complex with G(s alpha).GTP gamma S Science 278 1997 1907 1916 (Pubitemid 28013225)
    • (1997) Science , vol.278 , Issue.5345 , pp. 1907-1916
    • Tesmer, J.J.G.1    Sunahara, R.K.2    Gilman, A.G.3    Sprang, S.R.4
  • 39
    • 0036385914 scopus 로고    scopus 로고
    • Structure and orientation of a G protein fragment in the receptor bound state from residual dipolar couplings
    • B.W. Koenig, G. Kontaxis, D.C. Mitchell, J.M. Louis, B.J. Litman, and A. Bax Structure and orientation of a G protein fragment in the receptor bound state from residual dipolar couplings J. Mol. Biol. 322 2002 441 461
    • (2002) J. Mol. Biol. , vol.322 , pp. 441-461
    • Koenig, B.W.1    Kontaxis, G.2    Mitchell, D.C.3    Louis, J.M.4    Litman, B.J.5    Bax, A.6
  • 40
    • 0037387322 scopus 로고    scopus 로고
    • Rhodopsin controls a conformational switch on the transducin γ subunit
    • DOI 10.1016/S0969-2126(03)00045-5
    • O.G. Kisselev, and M.A. Downs Rhodopsin controls a conformational switch on the transducin gamma subunit Structure 11 2003 367 373 (Pubitemid 36419564)
    • (2003) Structure , vol.11 , Issue.4 , pp. 367-373
    • Kisselev, O.G.1    Downs, M.A.2
  • 41
    • 0030034646 scopus 로고    scopus 로고
    • Crystal structure of a G-protein beta gamma dimer at 2.1A resolution
    • J. Sondek, A. Bohm, D.G. Lambright, H.E. Hamm, and P.B. Sigler Crystal structure of a G-protein beta gamma dimer at 2.1A resolution Nature 379 1996 369 374
    • (1996) Nature , vol.379 , pp. 369-374
    • Sondek, J.1    Bohm, A.2    Lambright, D.G.3    Hamm, H.E.4    Sigler, P.B.5
  • 43
    • 0037799206 scopus 로고    scopus 로고
    • Keeping G proteins at bay: A complex between G protein-coupled receptor kinase 2 and Gβγ
    • DOI 10.1126/science.1082348
    • D.T. Lodowski, J.A. Pitcher, W.D. Capel, R.J. Lefkowitz, and J.J.G. Tesmer Keeping G proteins at bay: a complex between G protein-coupled receptor kinase 2 and G beta gamma Science 300 2003 1256 1262 (Pubitemid 36618232)
    • (2003) Science , vol.300 , Issue.5623 , pp. 1256-1262
    • Lodowski, D.T.1    Pitcher, J.A.2    Capel, W.D.3    Lefkowitz, R.J.4    Tesmer, J.J.G.5
  • 44
    • 77649218358 scopus 로고    scopus 로고
    • Structure of human G protein-coupled receptor kinase 2 in complex with the kinase inhibitor balanol
    • J.J.G. Tesmer, V.M. Tesmer, D.T. Lodowski, H. Steinhagen, and J. Huber Structure of human G protein-coupled receptor kinase 2 in complex with the kinase inhibitor balanol J. Med. Chem. 53 2010 1867 1870
    • (2010) J. Med. Chem. , vol.53 , pp. 1867-1870
    • Tesmer, J.J.G.1    Tesmer, V.M.2    Lodowski, D.T.3    Steinhagen, H.4    Huber, J.5
  • 45
    • 79960223285 scopus 로고    scopus 로고
    • Molecular mechanism of selectivity among G protein-coupled receptor kinase 2 inhibitors
    • D.M. Thal, R.Y. Yeow, C. Schoenau, J. Huber, and J.J.G. Tesmer Molecular mechanism of selectivity among G protein-coupled receptor kinase 2 inhibitors Mol. Pharmacol. 80 2011 294 303
    • (2011) Mol. Pharmacol. , vol.80 , pp. 294-303
    • Thal, D.M.1    Yeow, R.Y.2    Schoenau, C.3    Huber, J.4    Tesmer, J.J.G.5
  • 46
    • 0030297912 scopus 로고    scopus 로고
    • Crystal structure at 2.4 Å resolution of the complex of transducin βγ and its regulator, phosducin
    • DOI 10.1016/S0092-8674(00)81376-8
    • R. Gaudet, A. Bohm, and P.B. Sigler Crystal structure at 2.4 angstrom resolution of the complex of transducin beta gamma and its regulator, phosducin Cell 87 1996 577 588 (Pubitemid 26374330)
    • (1996) Cell , vol.87 , Issue.3 , pp. 577-588
    • Gaudet, R.1    Bohm, A.2    Sigler, P.B.3
  • 47
    • 0032528863 scopus 로고    scopus 로고
    • Phosducin induces a structural change in transducin βγ
    • A. Loew, Y.K. Ho, T. Blundell, and B. Bax Phosducin induces a structural change in transducin beta gamma Struct. Fold. Des. 6 1998 1007 1019 (Pubitemid 28397922)
    • (1998) Structure , vol.6 , Issue.8 , pp. 1007-1019
    • Loew, A.1    Ho, Y.-K.2    Blundell, T.3    Bax, B.4
  • 48
    • 0033002698 scopus 로고    scopus 로고
    • A molecular mechanism for the phosphorylation-dependent regulation of heterotrimeric G proteins by phosducin
    • DOI 10.1016/S1097-2765(00)80358-5
    • R. Gaudet, J.R. Savage, J.N. McLaughlin, B.M. Willardson, and P.B. Sigler A molecular mechanism for the phosphorylation-dependent regulation of heterotrimeric G proteins by phosducin Mol. Cell 3 1999 649 660 (Pubitemid 29268448)
    • (1999) Molecular Cell , vol.3 , Issue.5 , pp. 649-660
    • Gaudet, R.1    Savage, J.R.2    McLaughlin, J.N.3    Willardson, B.M.4    Sigler, P.B.5
  • 50
    • 0036020511 scopus 로고    scopus 로고
    • Receptor-mediated adenylyl cyclase activation through XLαs, the extra-large variant of the stimulatory G protein α-subunit
    • DOI 10.1210/me.2002-0054
    • M. Bastepe, Y. Gunes, B. Perez-Villamil, J. Hunzelman, L.S. Weinstein, and H. Juppner Receptor-mediated adenylyl cyclase activation through XL alpha s, the extra-large variant of the stimulatory G protein alpha-subunit Mol. Endocrinol. 16 2002 1912 1919 (Pubitemid 34828097)
    • (2002) Molecular Endocrinology , vol.16 , Issue.8 , pp. 1912-1919
    • Bastepe, M.1    Gunes, Y.2    Perez-Villamil, B.3    Hunzelman, J.4    Weinstein, L.S.5    Juppner, H.6
  • 51
    • 34547157646 scopus 로고    scopus 로고
    • Receptor-mediated activation of heterotrimeric G-proteins: Current structural insights
    • DOI 10.1124/mol.107.034348
    • C.A. Johnston, and D.P. Siderovski Receptor-mediated activation of heterotrimeric G-proteins: current structural insights Mol. Pharmacol. 72 2007 219 230 (Pubitemid 47124101)
    • (2007) Molecular Pharmacology , vol.72 , Issue.2 , pp. 219-230
    • Johnston, C.A.1    Siderovski, D.P.2
  • 52
    • 0026655036 scopus 로고
    • Specificity of G protein beta and gamma subunit interactions
    • C.J. Schmidt, T.C. Thomas, M.A. Levine, and E.J. Neer Specificity of G protein beta and gamma subunit interactions J. Biol. Chem. 267 1992 13807 13810
    • (1992) J. Biol. Chem. , vol.267 , pp. 13807-13810
    • Schmidt, C.J.1    Thomas, T.C.2    Levine, M.A.3    Neer, E.J.4
  • 54
    • 37549016836 scopus 로고    scopus 로고
    • Heterotrimeric G protein activation by G-protein-coupled receptors
    • W.M. Oldham, and H.E. Hamm Heterotrimeric G protein activation by G-protein-coupled receptors Nat. Rev. Mol. Cell Biol. 9 2007 60 71
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 60-71
    • Oldham, W.M.1    Hamm, H.E.2
  • 56
    • 13444261019 scopus 로고    scopus 로고
    • G protein-coupled receptors: A count of 1001 conformations
    • G. Vauquelin, and I.V. Van Liefde G protein-coupled receptors: a count of 1001 conformations Fundam. Clin. Pharmacol. 19 2005 45
    • (2005) Fundam. Clin. Pharmacol. , vol.19 , pp. 45
    • Vauquelin, G.1    Van Liefde, I.V.2
  • 57
    • 33751119043 scopus 로고    scopus 로고
    • The receptor-bound "empty pocket" state of the heterotrimeric G-protein α-subunit is conformationally dynamic
    • DOI 10.1021/bi061088h
    • N.G. Abdulaev, T. Ngo, E. Ramon, D.M. Brabazon, J.P. Marino, and K.D. Ridge The receptor-bound "empty pocket" state of the heterotrimeric G-protein alpha-subunit is conformationally dynamic Biochemistry 45 2006 12986 12997 (Pubitemid 44763421)
    • (2006) Biochemistry , vol.45 , Issue.43 , pp. 12986-12997
    • Abdulaev, N.G.1    Ngo, T.2    Ramon, E.3    Brabazon, D.M.4    Marino, J.P.5    Ridge, K.D.6
  • 58
    • 84874522517 scopus 로고    scopus 로고
    • Towards improved quality of GPCR models by usage of multiple templates and profile-profile comparison
    • 10.1371/journal.pone.0056742
    • D. Latek, P. Pasznik, T. Carlomagno, and S. Filipek Towards improved quality of GPCR models by usage of multiple templates and profile-profile comparison Plos One 8 2013 e56742 10.1371/journal.pone.0056742
    • (2013) Plos One , vol.8 , pp. 56742
    • Latek, D.1    Pasznik, P.2    Carlomagno, T.3    Filipek, S.4
  • 60
    • 0035800032 scopus 로고    scopus 로고
    • Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs)
    • DOI 10.1021/bi0155091
    • D.C. Teller, T. Okada, C.A. Behnke, K. Palczewski, and R.E. Stenkamp Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs) Biochemistry 40 2001 7761 7772 (Pubitemid 32622966)
    • (2001) Biochemistry , vol.40 , Issue.26 , pp. 7761-7772
    • Teller, D.C.1    Okada, T.2    Behnke, C.A.3    Palczewski, K.4    Stenkamp, R.E.5
  • 61
  • 62
    • 4344581120 scopus 로고    scopus 로고
    • The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure
    • DOI 10.1016/j.jmb.2004.07.044, PII S0022283604008733
    • T. Okada, M. Sugihara, A.N. Bondar, M. Elstner, P. Entel, and V. Buss The retinal conformation and its environment in rhodopsin in light of a new 2.2 A crystal structure J. Mol. Biol. 342 2004 571 583 (Pubitemid 39149759)
    • (2004) Journal of Molecular Biology , vol.342 , Issue.2 , pp. 571-583
    • Okada, T.1    Sugihara, M.2    Bondar, A.-N.3    Elstner, M.4    Entel, P.5    Buss, V.6
  • 64
    • 33746321096 scopus 로고    scopus 로고
    • Crystallographic analysis of primary visual photochemistry
    • DOI 10.1002/anie.200600595
    • H. Nakamichi, and T. Okada Crystallographic analysis of primary visual photochemistry Angew. Chem. Int. Ed. 45 2006 4270 4273 (Pubitemid 44105630)
    • (2006) Angewandte Chemie - International Edition , vol.45 , Issue.26 , pp. 4270-4273
    • Nakamichi, H.1    Okada, T.2
  • 67
    • 34250340151 scopus 로고    scopus 로고
    • Photoisomerization mechanism of rhodopsin and 9-cis-rhodopsin revealed by x-ray crystallography
    • H. Nakamichi, V. Buss, and T. Okada Photoisomerization mechanism of rhodopsin and 9-cis-rhodopsin revealed by x-ray crystallography Biophys. J. 92 2007
    • (2007) Biophys. J. , vol.92
    • Nakamichi, H.1    Buss, V.2    Okada, T.3
  • 68
    • 43749109187 scopus 로고    scopus 로고
    • Crystal structure of squid rhodopsin
    • DOI 10.1038/nature06925, PII NATURE06925
    • M. Murakami, and T. Kouyama Crystal structure of squid rhodopsin Nature 453 2008 363 367 (Pubitemid 351693128)
    • (2008) Nature , vol.453 , Issue.7193 , pp. 363-367
    • Murakami, M.1    Kouyama, T.2
  • 70
    • 47749095553 scopus 로고    scopus 로고
    • Alternative models for two crystal structures of bovine rhodopsin
    • DOI 10.1107/S0907444908017162, PII S0907444908017162
    • Stenkamp Alternative models for two crystal structures of bovine rhodopsin Acta Crystallogr. D: Biol. Crystallogr. 64 2008 902 904 (Pubitemid 352032294)
    • (2008) Acta Crystallographica Section D: Biological Crystallography , vol.64 , Issue.8 , pp. 902-904
    • Stenkamp, R.E.1
  • 71
    • 47049130668 scopus 로고    scopus 로고
    • Crystal structure of the ligand-free G-protein-coupled receptor opsin
    • J.H. Park, P. Scheerer, K.P. Hofmann, H.W. Choe, and O.P. Ernst Crystal structure of the ligand-free G-protein-coupled receptor opsin Nature 454 2008 183-U133
    • (2008) Nature , vol.454
    • Park, J.H.1    Scheerer, P.2    Hofmann, K.P.3    Choe, H.W.4    Ernst, O.P.5
  • 77
    • 77955779227 scopus 로고    scopus 로고
    • Conserved binding mode of human beta(2) adrenergic receptor inverse agonists and antagonist revealed by X-ray crystallography
    • D. Wacker, G. Fenalti, M.A. Brown, V. Katritch, R. Abagyan, V. Cherezov, and R.C. Stevens Conserved binding mode of human beta(2) adrenergic receptor inverse agonists and antagonist revealed by X-ray crystallography J. Am. Chem. Soc. 132 2010 11443 11445
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 11443-11445
    • Wacker, D.1    Fenalti, G.2    Brown, M.A.3    Katritch, V.4    Abagyan, R.5    Cherezov, V.6    Stevens, R.C.7
  • 90
    • 79959564813 scopus 로고    scopus 로고
    • Agonist-bound adenosine A2A receptor structures reveal common features of GPCR activation
    • G. Lebon, T. Warne, P.C. Edwards, K. Bennett, C.J. Langmead, A.G.W. Leslie, and C.G. Tate Agonist-bound adenosine A2A receptor structures reveal common features of GPCR activation Nature 474 2011 521 525
    • (2011) Nature , vol.474 , pp. 521-525
    • Lebon, G.1    Warne, T.2    Edwards, P.C.3    Bennett, K.4    Langmead, C.J.5    Leslie, A.G.W.6    Tate, C.G.7
  • 101
    • 77957055780 scopus 로고
    • Integrated methods for the construction of three-dimensional models of structure-function relations in G protein-coupled receptors
    • J. Ballesteros, and H. Weinstein Integrated methods for the construction of three-dimensional models of structure-function relations in G protein-coupled receptors Methods Neurosci. 25 1995 366
    • (1995) Methods Neurosci. , vol.25 , pp. 366
    • Ballesteros, J.1    Weinstein, H.2
  • 103
    • 0037184031 scopus 로고    scopus 로고
    • Conserved helix 7 tyrosine acts as a multistate conformational switch in the 5HT2C receptor - Identification of a novel "locked-on" phenotype and double revertant mutations
    • C. Prioleau, I. Visiers, B.J. Ebersole, H. Weinstein, and S.C. Sealfon Conserved helix 7 tyrosine acts as a multistate conformational switch in the 5HT2C receptor - identification of a novel "locked-on" phenotype and double revertant mutations J. Biol. Chem. 277 2002 36577 36584
    • (2002) J. Biol. Chem. , vol.277 , pp. 36577-36584
    • Prioleau, C.1    Visiers, I.2    Ebersole, B.J.3    Weinstein, H.4    Sealfon, S.C.5
  • 104
    • 66649096395 scopus 로고    scopus 로고
    • Conserved waters mediate structural and functional activation of family A (rhodopsin-like) G protein-coupled receptors
    • T.E. Angel, M.R. Chance, and K. Palczewski Conserved waters mediate structural and functional activation of family A (rhodopsin-like) G protein-coupled receptors Proc. Natl. Acad. Sci. U. S. A. 106 2009 8555 8560
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 8555-8560
    • Angel, T.E.1    Chance, M.R.2    Palczewski, K.3
  • 106
    • 0034787251 scopus 로고    scopus 로고
    • Three-dimensional representations of G protein-coupled receptor structures and mechanisms
    • DOI 10.1016/S0076-6879(02)43145-X
    • I. Visiers, J.A. Ballesteros, and H. Weinstein Three-dimensional Representations of G Protein-Coupled Receptor Structures and Mechanisms G Protein Pathways, Pt A, Receptors 343 2002 329 371 (Pubitemid 32954152)
    • (2001) Methods in Enzymology , vol.343 , pp. 329-371
    • Visiers, I.1    Ballesteros, J.A.2    Weinstein, H.3
  • 107
    • 33747124117 scopus 로고    scopus 로고
    • Hallucinogen actions on 5-HT receptors reveal distinct mechanisms of activation and signaling by G protein-coupled receptors
    • H. Weinstein Hallucinogen actions on 5-HT receptors reveal distinct mechanisms of activation and signaling by G protein-coupled receptors AAPS J. 7 2005 E871 E884
    • (2005) AAPS J. , vol.7
    • Weinstein, H.1
  • 110
    • 0032402450 scopus 로고    scopus 로고
    • Molecular basis of receptor/G-protein-coupling selectivity
    • DOI 10.1016/S0163-7258(98)00030-8, PII S0163725898000308
    • J. Wess Molecular basis of receptor/G-protein-coupling selectivity Pharmacol. Ther. 80 1998 231 264 (Pubitemid 28537822)
    • (1998) Pharmacology and Therapeutics , vol.80 , Issue.3 , pp. 231-264
    • Wess, J.1
  • 111
    • 78650369170 scopus 로고    scopus 로고
    • Probing the structural determinants for the function of intracellular loop 2 in structurally cognate G-protein-coupled receptors
    • J.F. Shan, H. Weinstein, and E.L. Mehler Probing the structural determinants for the function of intracellular loop 2 in structurally cognate G-protein-coupled receptors Biochemistry 49 2010 10691 10701
    • (2010) Biochemistry , vol.49 , pp. 10691-10701
    • Shan, J.F.1    Weinstein, H.2    Mehler, E.L.3
  • 112
    • 3142773613 scopus 로고    scopus 로고
    • Rhodopsin activation exposes a key hydrophobic binding site for the transducin α-subunit C terminus
    • DOI 10.1074/jbc.M402567200
    • J.M. Janz, and D.L. Farrens Rhodopsin activation exposes a key hydrophobic binding site for the transducin alpha-subunit C terminus J. Biol. Chem. 279 2004 29767 29773 (Pubitemid 38915860)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.28 , pp. 29767-29773
    • Janz, J.M.1    Farrens, D.L.2
  • 113
    • 63849294621 scopus 로고    scopus 로고
    • Identification of two distinct inactive conformations of the beta(2)-adrenergic receptor reconciles structural and biochemical observations
    • R.O. Dror, D.H. Arlow, D.W. Borhani, M.O. Jensen, S. Piana, and D.E. Shaw Identification of two distinct inactive conformations of the beta(2)-adrenergic receptor reconciles structural and biochemical observations Proc. Natl. Acad. Sci. U. S. A. 106 2009 4689 4694
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 4689-4694
    • Dror, R.O.1    Arlow, D.H.2    Borhani, D.W.3    Jensen, M.O.4    Piana, S.5    Shaw, D.E.6
  • 115
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • DOI 10.1126/science.274.5288.768
    • D.L. Farrens, C. Altenbach, K. Yang, W.L. Hubbell, and H.G. Khorana Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin Science 274 1996 768 770 (Pubitemid 26398253)
    • (1996) Science , vol.274 , Issue.5288 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.G.5
  • 117
    • 0035800850 scopus 로고    scopus 로고
    • Activation of the beta(2)-adrenergic receptor involves disruption of an ionic lock between the cytoplasmic ends of transmembrane segments 3 and 6
    • J.A. Ballesteros, A.D. Jensen, G. Liapakis, S.G.F. Rasmussen, L. Shi, U. Gether, and J.A. Javitch Activation of the beta(2)-adrenergic receptor involves disruption of an ionic lock between the cytoplasmic ends of transmembrane segments 3 and 6 J. Biol. Chem. 276 2001 29171 29177
    • (2001) J. Biol. Chem. , vol.276 , pp. 29171-29177
    • Ballesteros, J.A.1    Jensen, A.D.2    Liapakis, G.3    Rasmussen, S.G.F.4    Shi, L.5    Gether, U.6    Javitch, J.A.7
  • 119
    • 0033546197 scopus 로고    scopus 로고
    • Similar structures and shared switch mechanisms of the beta(2)-adrenoceptor and the parathyroid hormone receptor - Zn(II) bridges between helices III and VI block activation
    • S.P. Sheikh, J.P. Vilardarga, T.J. Baranski, O. Lichtarge, T. Iiri, E.C. Meng, R.A. Nissenson, and H.R. Bourne Similar structures and shared switch mechanisms of the beta(2)-adrenoceptor and the parathyroid hormone receptor - Zn(II) bridges between helices III and VI block activation J. Biol. Chem. 274 1999 17033 17041
    • (1999) J. Biol. Chem. , vol.274 , pp. 17033-17041
    • Sheikh, S.P.1    Vilardarga, J.P.2    Baranski, T.J.3    Lichtarge, O.4    Iiri, T.5    Meng, E.C.6    Nissenson, R.A.7    Bourne, H.R.8
  • 120
    • 84885386517 scopus 로고    scopus 로고
    • Structural motifs as functional microdomains in signal transduction by G-protein coupled receptors
    • H. Weinstein, and J. Ballesteros Structural motifs as functional microdomains in signal transduction by G-protein coupled receptors Biophys. J. 76 1999 A6-A6
    • (1999) Biophys. J. , vol.76
    • Weinstein, H.1    Ballesteros, J.2
  • 121
    • 0035937786 scopus 로고    scopus 로고
    • Agonist-induced conformational changes at the cytoplasmic side of transmembrane segment 6 in the beta(2) adrenergic receptor mapped by site-selective fluorescent labeling
    • A.D. Jensen, F. Guarnieri, S.G.F. Rasmussen, F. Asmar, J.A. Ballesteros, and U. Gether Agonist-induced conformational changes at the cytoplasmic side of transmembrane segment 6 in the beta(2) adrenergic receptor mapped by site-selective fluorescent labeling J. Biol. Chem. 276 2001 9279 9290
    • (2001) J. Biol. Chem. , vol.276 , pp. 9279-9290
    • Jensen, A.D.1    Guarnieri, F.2    Rasmussen, S.G.F.3    Asmar, F.4    Ballesteros, J.A.5    Gether, U.6
  • 122
    • 14044251558 scopus 로고    scopus 로고
    • Agonist-induced conformational changes in thyrotropin-releasing hormone receptor type I: Disulfide cross-linking and molecular modeling approaches
    • DOI 10.1021/bi048808+
    • W. Huang, R. Osman, and M.C. Gershengorn Agonist-induced conformational changes in thyrotropin-releasing hormone receptor type I: disulfide cross-linking and molecular modeling approaches Biochemistry 44 2005 2419 2431 (Pubitemid 40279546)
    • (2005) Biochemistry , vol.44 , Issue.7 , pp. 2419-2431
    • Huang, W.1    Osman, R.2    Gershengorn, M.C.3
  • 123
    • 31044432667 scopus 로고    scopus 로고
    • 3 muscarinic acetylcholine receptor
    • DOI 10.1021/bi051503q
    • S.D.C. Ward, F.F. Hamdan, L.M. Bloodworth, N.A. Siddiqui, J.H. Li, and J. Wess Use of an in situ disulfide cross-linking strategy to study the dynamic properties of the cytoplasmic end of transmembrane domain VI of the M-3 muscarinic acetylcholine receptor Biochemistry 45 2006 676 685 (Pubitemid 43122233)
    • (2006) Biochemistry , vol.45 , Issue.3 , pp. 676-685
    • Ward, S.D.C.1    Hamdan, F.F.2    Bloodworth, L.M.3    Siddiqui, N.A.4    Li, J.H.5    Wess, J.6
  • 126
    • 74049108724 scopus 로고    scopus 로고
    • Concerted interconversion between ionic lock substates of the beta(2) adrenergic receptor revealed by microsecond timescale molecular dynamics
    • T.D. Romo, A. Grossfield, and M.C. Pitman Concerted interconversion between ionic lock substates of the beta(2) adrenergic receptor revealed by microsecond timescale molecular dynamics Biophys. J. 98 2010 76 84
    • (2010) Biophys. J. , vol.98 , pp. 76-84
    • Romo, T.D.1    Grossfield, A.2    Pitman, M.C.3
  • 127
    • 75749117507 scopus 로고    scopus 로고
    • Visualizing water molecules in transmembrane proteins using radiolytic labeling methods
    • T. Orban, S. Gupta, K. Palczewski, and M.R. Chance Visualizing water molecules in transmembrane proteins using radiolytic labeling methods Biochemistry 49 2010 827 834
    • (2010) Biochemistry , vol.49 , pp. 827-834
    • Orban, T.1    Gupta, S.2    Palczewski, K.3    Chance, M.R.4
  • 129
    • 79953727883 scopus 로고    scopus 로고
    • Role of membrane integrity on G protein-coupled receptors: Rhodospin stability and function
    • B. Jastrzebska, A. Debinski, S. Filipek, and K. Palczewski Role of membrane integrity on G protein-coupled receptors: rhodospin stability and function Prog. Lipid Res. 50 2011 267 277
    • (2011) Prog. Lipid Res. , vol.50 , pp. 267-277
    • Jastrzebska, B.1    Debinski, A.2    Filipek, S.3    Palczewski, K.4
  • 130
    • 0038265194 scopus 로고    scopus 로고
    • Signal transduction in the visual cascade involves specific lipid-protein interactions
    • DOI 10.1074/jbc.M302747200
    • E. Hessel, M. Heck, P. Muller, R. Herrmann, and K.P. Hofmann Signal transduction in the visual cascade involves specific lipid-protein interactions J. Biol. Chem. 289 2003 22853 22860 (Pubitemid 36830348)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.25 , pp. 22853-22860
    • Hessel, E.1    Heck, M.2    Muller, P.3    Herrmann, A.4    Hofmann, K.P.5
  • 131
    • 0035951843 scopus 로고    scopus 로고
    • Light-induced reorganization of phospholipids in rod disc membranes
    • E. Hessel, P. Muller, R. Herrmann, and K.P. Hofmann Light-induced reorganization of phospholipids in rod disc membranes J. Biol. Chem. 276 2001 2538 2543
    • (2001) J. Biol. Chem. , vol.276 , pp. 2538-2543
    • Hessel, E.1    Muller, P.2    Herrmann, R.3    Hofmann, K.P.4
  • 132
    • 0034012727 scopus 로고    scopus 로고
    • The transbilayer distribution of phospholipids in disc membranes is a dynamic equilibrium: Evidence for rapid flip and flop movement
    • DOI 10.1046/j.1432-1327.2000.01147.x
    • E. Hessel, A. Hermann, P. Muller, P.P.M. Schnetkamp, and K.P. Hofmann The transbilayer distribution of phospholipids in disc membranes is a dynamic equilibrium evidence for rapid flip and flop movement Eur. J. Biochem. 267 2000 1473 1483 (Pubitemid 30143287)
    • (2000) European Journal of Biochemistry , vol.267 , Issue.5 , pp. 1473-1483
    • Hessel, E.1    Herrmann, A.2    Muller, P.3    Schnetkamp, P.P.M.4    Hofmann, K.-P.5
  • 134
    • 57649178347 scopus 로고    scopus 로고
    • Eletrostatic and lipid anchor contributions to the interaction of transducin with membranes: Mechanistic implications for activation and translocation
    • M. Kosloff, E. Alexov, V.Y. Arshavsky, and B. Honig Eletrostatic and lipid anchor contributions to the interaction of transducin with membranes: mechanistic implications for activation and translocation J. Biol. Chem. 283 2008 31197 31207
    • (2008) J. Biol. Chem. , vol.283 , pp. 31197-31207
    • Kosloff, M.1    Alexov, E.2    Arshavsky, V.Y.3    Honig, B.4
  • 137
    • 84873306058 scopus 로고    scopus 로고
    • Conformational ensembles in GPCR activation
    • E. Vardy, and Bryan L. Roth Conformational ensembles in GPCR activation Cell 152 2013 385 386
    • (2013) Cell , vol.152 , pp. 385-386
    • Vardy, E.1    Roth, B.L.2
  • 138
    • 84879093879 scopus 로고    scopus 로고
    • Conformational flexibility and structural dynamics in GPCR-mediated g protein activation: A perspective
    • A.M. Preininger, J. Meiler, and H. Hamm Conformational flexibility and structural dynamics in GPCR-mediated g protein activation: a perspective J. Mol. Biol. 425 2013 2288 2298
    • (2013) J. Mol. Biol. , vol.425 , pp. 2288-2298
    • Preininger, A.M.1    Meiler, J.2    Hamm, H.3
  • 139
    • 0023062991 scopus 로고
    • G-proteins - Transducers of receptor-generated signals
    • A.G. Gilman G-proteins - transducers of receptor-generated signals Annu. Rev. Biochem. 56 1987 615 649
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 615-649
    • Gilman, A.G.1
  • 141
    • 21644479599 scopus 로고    scopus 로고
    • i-specific region
    • DOI 10.1074/jbc.M414630200
    • M. Frank, L. Thumer, M.J. Lohse, and M. Bunemann G protein activation without subunit dissociation depends on a G{alpha}i-specific region J. Biol. Chem. 280 2005 24584 24590 (Pubitemid 40934546)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.26 , pp. 24584-24590
    • Frank, M.1    Thumer, L.2    Lohse, M.J.3    Bunemann, M.4
  • 142
    • 18744376919 scopus 로고    scopus 로고
    • Real-time monitoring of receptor and G-protein interactions in living cells
    • DOI 10.1038/nmeth743
    • C. Gales, R.V. Rebois, M. Hogue, P. Trieu, A. Breit, T.E. Hebert, and M. Bouvier Real-time monitoring of receptor and G-protein interactions in living cells Nat. Methods 2 2005 177 184 (Pubitemid 41122124)
    • (2005) Nature Methods , vol.2 , Issue.3 , pp. 177-184
    • Gales, C.1    Rebois, R.V.2    Hogue, M.3    Trieu, P.4    Breit, A.5    Hebert, T.E.6    Bouvier, M.7
  • 143
    • 0026803223 scopus 로고
    • G-protein-coupled mechanism and nervous signaling
    • B. Hille G-protein-coupled mechanism and nervous signaling Neuron 9 1992 187 195
    • (1992) Neuron , vol.9 , pp. 187-195
    • Hille, B.1
  • 144
    • 0038445997 scopus 로고    scopus 로고
    • Protein complexes involved in heptahelical receptor-mediated signal transduction
    • DOI 10.1080/10606820308243
    • R.V. Rebois, and T.E. Hebert Protein complexes involved in heptahelical receptor-mediated signal transduction Receptors Channels 9 2003 169 194 (Pubitemid 36874791)
    • (2003) Receptors and Channels , vol.9 , Issue.3 , pp. 169-194
    • Rebois, R.V.1    Hebert, T.E.2
  • 146
    • 0025924670 scopus 로고
    • The a2 adenosine receptor- guanine nucleotide modulation of agonist binding is enhanced by proteolysis
    • C. Nanoff, K.A. Jacobson, and G.L. Stiles The a2 adenosine receptor- guanine nucleotide modulation of agonist binding is enhanced by proteolysis Mol. Pharmacol. 39 1991 130 135
    • (1991) Mol. Pharmacol. , vol.39 , pp. 130-135
    • Nanoff, C.1    Jacobson, K.A.2    Stiles, G.L.3
  • 147
    • 0027336515 scopus 로고
    • Solubilization and characterization of the a(2)-adenosine receptor
    • C. Nanoff, and G.L. Stiles Solubilization and characterization of the a(2)-adenosine receptor J. Recept. Res. 13 1993 961 973
    • (1993) J. Recept. Res. , vol.13 , pp. 961-973
    • Nanoff, C.1    Stiles, G.L.2
  • 149
    • 0032959367 scopus 로고    scopus 로고
    • 2AR is independent of the state of receptor activation
    • DOI 10.1016/S0898-6568(99)00024-8, PII S0898656899000248
    • M. Lachance, N. Ethier, G. Wolbring, P.P.M. Schnetkamp, and T.E. Hebert Stable association of G proteins with beta(2)AR is independent of the state of receptor activation Cell. Signal. 11 1999 523 533 (Pubitemid 29234122)
    • (1999) Cellular Signalling , vol.11 , Issue.7 , pp. 523-533
    • Lachance, M.1    Ethier, N.2    Wolbring, G.3    Schnetkamp, P.P.M.4    Hebert, T.E.5
  • 151
    • 80052969688 scopus 로고    scopus 로고
    • Inactive-state preassembly of Gq-coupled receptors and Gq heterotrimers
    • K. Qin, C. Dong, G.S. Wu, and N.A. Lambert Inactive-state preassembly of Gq-coupled receptors and Gq heterotrimers Nat. Chem. Biol. 7 2012 740 747
    • (2012) Nat. Chem. Biol. , vol.7 , pp. 740-747
    • Qin, K.1    Dong, C.2    Wu, G.S.3    Lambert, N.A.4
  • 152
    • 0029589916 scopus 로고
    • Identification of a receptor G-protein contact site critical for signaling specifity and G-protein activation
    • J. Liu, B.R. Conklin, N. Blin, J. Yun, and J. Wess Identification of a receptor G-protein contact site critical for signaling specifity and G-protein activation Proc. Natl. Acad. Sci. U. S. A. 92 1995 11642 11646
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 11642-11646
    • Liu, J.1    Conklin, B.R.2    Blin, N.3    Yun, J.4    Wess, J.5
  • 153
    • 33749115868 scopus 로고    scopus 로고
    • Identification of structural elements that determine the G protein coupling selectivity of the V2 vasopressin receptor
    • I. Erlenbach, and J. Wess Identification of structural elements that determine the G protein coupling selectivity of the V2 vasopressin receptor FASEB J. 12 1998 A1458
    • (1998) FASEB J. , vol.12 , pp. 1458
    • Erlenbach, I.1    Wess, J.2
  • 155
    • 0030614427 scopus 로고    scopus 로고
    • Receptor and βγ binding sites in the α subunit of the retinal G protein transducin
    • DOI 10.1126/science.275.5298.381
    • R. Onrust, P. Herzmark, P. Chi, P.D. Garcia, O. Lichtarge, C. Kingsley, and H.R. Bourne Receptor and beta gamma binding sites in the alpha subunit of the retinal G protein transducin Science 275 1997 381 384 (Pubitemid 27051613)
    • (1997) Science , vol.275 , Issue.5298 , pp. 381-384
    • Onrust, R.1    Herzmark, P.2    Chi, P.3    Garcia, P.D.4    Lichtarge, O.5    Kingsley, C.6    Bourne, H.R.7
  • 156
    • 0033591051 scopus 로고    scopus 로고
    • Two amino acids within the alpha 4 helix of G alpha(i1) mediate coupling with 5-hydroxytryptamine(1B) receptors
    • H. Bae, T.M. Cabrera-Vera, K.M. Depree, S.G. Graber, and H.E. Hamm Two amino acids within the alpha 4 helix of G alpha(i1) mediate coupling with 5-hydroxytryptamine(1B) receptors J. Biol. Chem. 274 1999 14963 14971
    • (1999) J. Biol. Chem. , vol.274 , pp. 14963-14971
    • Bae, H.1    Cabrera-Vera, T.M.2    Depree, K.M.3    Graber, S.G.4    Hamm, H.E.5
  • 157
    • 0029664921 scopus 로고    scopus 로고
    • Evolutionarily conserved G(alpha beta gamma) binding surfaces support a model of the G protein-receptor complex
    • O. Lichtarge, H.R. Bourne, and F.E. Cohen Evolutionarily conserved G(alpha beta gamma) binding surfaces support a model of the G protein-receptor complex Proc. Natl. Acad. Sci. U. S. A. 93 1996 7507 7511
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 7507-7511
    • Lichtarge, O.1    Bourne, H.R.2    Cohen, F.E.3
  • 158
    • 0035942238 scopus 로고    scopus 로고
    • Mapping of contact sites in complex formation between transducin and light-activated rhodopsin by covalent crosslinking: Use of a photoactivatable reagent
    • DOI 10.1073/pnas.051632898
    • K. Cai, Y. Itoh, and H.G. Khorana Mapping of contact sites in complex formation between transducin and light-activated rhodopsin by covalent crosslinking: use of a photoactivatable reagent Proc. Natl. Acad. Sci. U. S. A. 98 2001 4877 4882 (Pubitemid 32397050)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.9 , pp. 4877-4882
    • Cai, K.1    Itoh, Y.2    Khorana, H.G.3
  • 159
    • 0029969175 scopus 로고    scopus 로고
    • Interaction of transducin with light-activated rhodopsin protects it from proteolytic digestion by trypsin
    • DOI 10.1074/jbc.271.47.30034
    • M.R. Mazzoni, and H.E. Hamm Interaction of transducin with light-activated rhodopsin protects it from proteolytic digestion by trypsin J. Biol. Chem. 271 1996 30034 30040 (Pubitemid 26389642)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.47 , pp. 30034-30040
    • Mazzoni, M.R.1    Hamm, H.E.2
  • 160
    • 0031016906 scopus 로고    scopus 로고
    • Molecular basis of receptor/G protein coupling selectivity studied by coexpression of wild type and mutant m2 muscarinic receptors with mutant Gα(q) subunits
    • DOI 10.1021/bi962554d
    • E. Kostenis, B.R. Conklin, and J. Wess Molecular basis of receptor/G protein coupling selectivity studied by coexpression of wild type and mutant m2 muscarinic receptors with mutant G alpha(q) subunits Biochemistry 36 1997 1487 1495 (Pubitemid 27074973)
    • (1997) Biochemistry , vol.36 , Issue.6 , pp. 1487-1495
    • Kostenis, E.1    Conklin, B.R.2    Wess, J.3
  • 161
    • 33750150814 scopus 로고    scopus 로고
    • Importance of the amino terminal extension of G alpha q in receptor/G-protein coupling specificity
    • E. Kostenis, M. Degtyarev, B. Conklin, and J. Wess Importance of the amino terminal extension of G alpha q in receptor/G-protein coupling specificity FASEB J. 11 1997 1137
    • (1997) FASEB J. , vol.11 , pp. 1137
    • Kostenis, E.1    Degtyarev, M.2    Conklin, B.3    Wess, J.4
  • 162
    • 33749104544 scopus 로고    scopus 로고
    • Functional characterization of a series of mutant G protein alphaq subunits displaying promiscuous receptor coupling properties
    • E. Kostenis, F.Y. Zeng, and J. Wess Functional characterization of a series of mutant G protein alphaq subunits displaying promiscuous receptor coupling properties FASEB J. 12 1998 A1368
    • (1998) FASEB J. , vol.12 , pp. 1368
    • Kostenis, E.1    Zeng, F.Y.2    Wess, J.3
  • 163
    • 0034098381 scopus 로고    scopus 로고
    • A surface-exposed region of G(sα) in which substitutions decrease receptor-mediated activation and increase receptor affinity
    • G. Grishina, and C.H. Berlot A surface-exposed region of G(s alpha) in which substitutions decrease receptor-mediated activation and increase receptor affinity Mol. Pharmacol. 57 2000 1081 1092 (Pubitemid 30354380)
    • (2000) Molecular Pharmacology , vol.57 , Issue.6 , pp. 1081-1092
    • Grishina, G.1    Berlot, C.H.2
  • 164
    • 0029106731 scopus 로고
    • Multiple regions of G(alpha16) contribute to the specificity of activation by the C5A receptor
    • C.H. Lee, A. Katz, and M.I. Simon Multiple regions of G(alpha16) contribute to the specificity of activation by the C5A receptor Mol. Pharmacol. 47 1995 218 223
    • (1995) Mol. Pharmacol. , vol.47 , pp. 218-223
    • Lee, C.H.1    Katz, A.2    Simon, M.I.3
  • 165
    • 0032475966 scopus 로고    scopus 로고
    • Extreme C terminus of G protein alpha-subunits contains a site that discriminates between G(i)-coupled metabotropic glutamate receptors
    • J. Blahos, S. Mary, J. Perroy, C. de Colle, I. Brabet, J. Bockaert, and J.P. Pin Extreme C terminus of G protein alpha-subunits contains a site that discriminates between G(i)-coupled metabotropic glutamate receptors J. Biol. Chem. 273 1998 25765 25769
    • (1998) J. Biol. Chem. , vol.273 , pp. 25765-25769
    • Blahos, J.1    Mary, S.2    Perroy, J.3    De Colle, C.4    Brabet, I.5    Bockaert, J.6    Pin, J.P.7
  • 166
    • 34548439826 scopus 로고    scopus 로고
    • How do Receptors Activate G Proteins?
    • DOI 10.1016/S0065-3233(07)74002-0, PII S0065323307740020, Mechanisms and Pathways of Heterotrimeric G Protein Signaling
    • W.M. Oldham, and H.E. Hamm How do receptors activate G proteins? Adv. Protein Chem. 74 2007 67 93 (Pubitemid 47369747)
    • (2007) Advances in Protein Chemistry , vol.74 , pp. 67-93
    • Oldham, W.M.1    Hamm, H.E.2
  • 167
    • 0027245830 scopus 로고
    • Substitution of three amino acids switches receptor specificity of G(q)α to that of G(i)α
    • DOI 10.1038/363274a0
    • B.R. Conklin, Z. Farfel, K.D. Lustig, D. Julius, and H.R. Bourne Substitution of three amino acids switches receptor specificity of Gq[alpha] to that of Gi[alpha] Nature 363 1993 274 276 (Pubitemid 23158533)
    • (1993) Nature , vol.363 , Issue.6426 , pp. 274-276
    • Conklin, B.R.1    Farfel, Z.2    Lustig, K.D.3    Julius, D.4    Bourne, H.R.5
  • 168
    • 0035942229 scopus 로고    scopus 로고
    • Mapping of contact sites in complex formation between light-activated rhodopsin and transducin by covalent crosslinking: Use of a chemically preactivated reagent
    • DOI 10.1073/pnas.051632998
    • Y. Itoh, K. Cai, and H.G. Khorana Mapping of contact sites in complex formation between light-activated rhodopsin and transducin by covalent crosslinking: use of a chemically preactivated reagent Proc. Natl. Acad. Sci. U. S. A. 98 2001 4883 4887 (Pubitemid 32397051)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.9 , pp. 4883-4887
    • Itoh, Y.1    Cai, K.2    Khorana, H.G.3
  • 170
    • 0035942238 scopus 로고    scopus 로고
    • Mapping of contact sites in complex formation between transducin and light-activated rhodopsin by covalent crosslinking: Use of a photoactivatable reagent
    • DOI 10.1073/pnas.051632898
    • K. Cai, Y. Itoh, and F.C. Khorana Mapping of contact sites in complex formation between transducin and light-activated rhodopsin by covalent crosslinking: use of a photoactivatable reagent Proc. Natl. Acad. Sci. U. S. A. 98 2001 4877 4882 (Pubitemid 32397050)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.9 , pp. 4877-4882
    • Cai, K.1    Itoh, Y.2    Khorana, H.G.3
  • 171
    • 0028592603 scopus 로고
    • Peptides as probes for G-protein signal transducin
    • J.M. Taylor, and R.R. Neubig Peptides as probes for G-protein signal transducin Cell. Signal. 6 1994 841 849
    • (1994) Cell. Signal. , vol.6 , pp. 841-849
    • Taylor, J.M.1    Neubig, R.R.2
  • 172
    • 0030064529 scopus 로고    scopus 로고
    • Receptor and membrane interaction sites on G beta - A receptor-derived peptide binds to the carboxyl terminus
    • J.M. Taylor, G.G. JacobMosier, R.G. Lawton, M. VanDort, and R.R. Neubig Receptor and membrane interaction sites on G beta - a receptor-derived peptide binds to the carboxyl terminus J. Biol. Chem. 271 1996 3336 3339
    • (1996) J. Biol. Chem. , vol.271 , pp. 3336-3339
    • Taylor, J.M.1    Jacobmosier, G.G.2    Lawton, R.G.3    Vandort, M.4    Neubig, R.R.5
  • 173
    • 0034056269 scopus 로고    scopus 로고
    • Intrinsic biophysical monitors of transducin activation: Fluorescence, UV-visible spectroscopy, light scattering, and evanescent field techniques
    • O.P. Ernst, C. Bieri, H. Vogel, and K.P. Hofmann Intrinsic Biophysical Monitors of Transducin Activation: Fluorescence, UV-Visible Spectroscopy, Light Scattering, and Evanescent Field Techniques Vertebrate Phototransduction and the Visual Cycle, Part A 315 2000 471 489 (Pubitemid 30123310)
    • (2000) Methods in Enzymology , vol.315 , pp. 471-489
    • Ernst, O.P.1    Bieri, C.2    Vogel, H.3    Hofmann, K.P.4
  • 176
    • 0030975286 scopus 로고    scopus 로고
    • Transducin-α C-terminal peptide binding site consists of C-D and E-F loops of rhodopsin
    • DOI 10.1074/jbc.272.10.6519
    • S. Acharya, Y. Saad, and S.S. Karnik Transducin-alpha C-terminal peptide binding site consists of C-D and E-F loops of rhodopsin J. Biol. Chem. 272 1997 6519 6524 (Pubitemid 27118132)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.10 , pp. 6519-6524
    • Acharya, S.1    Saad, Y.2    Karnik, S.S.3
  • 177
    • 0141733156 scopus 로고    scopus 로고
    • Rhodopsin determinants for transducin activation: A gain-of-function approach
    • DOI 10.1074/jbc.M305136200
    • M. Natochin, K.G. Gasimov, M. Moussaif, and N.O. Artemyev Rhodopsin determinants for transducin activation: a gain-of-function approach J. Biol. Chem. 278 2003 37574 37581 (Pubitemid 37175280)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.39 , pp. 37574-37581
    • Natochin, M.1    Gasimov, K.G.2    Moussaif, M.3    Artemyev, N.O.4
  • 178
    • 0034695476 scopus 로고    scopus 로고
    • The amino terminus of the fourth cytoplasmic loop of rhodopsin modulates rhodopsin-transducin interaction
    • DOI 10.1074/jbc.275.3.1930
    • E.P. Marin, A.G. Krishna, T.A. Zvyaga, J. Isele, F. Siebert, and T.P. Sakmar The amino terminus of the fourth cytoplasmic loop of rhodopsin modulates rhodopsin-transducin interaction J. Biol. Chem. 275 2000 1930 1936 (Pubitemid 30060818)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.3 , pp. 1930-1936
    • Marin, E.P.1    Krishna, A.G.2    Zvyaga, T.A.3    Isele, J.4    Siebert, F.5    Sakmar, T.P.6
  • 179
    • 0034695482 scopus 로고    scopus 로고
    • Mutation of the fourth cytoplasmic loop of rhodopsin affects binding of transducin and peptides derived from the carboxyl-terminal sequences of transducin α and γ subunits
    • DOI 10.1074/jbc.275.3.1937
    • O.P. Ernst, C.K. Meyer, E.P. Marin, P. Henklein, W.Y. Fu, T.P. Sakmar, and K.P. Hofmann Mutation of the fourth cytoplasmic loop of rhodopsin affects binding of transducin and peptides derived from the carboxyl-terminal sequences of transducin alpha and gamma subunits J. Biol. Chem. 275 2000 1937 1943 (Pubitemid 30060819)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.3 , pp. 1937-1943
    • Ernst, O.P.1    Meyer, C.K.2    Marin, E.P.3    Henklein, P.4    Fu, W.-Y.5    Sakmar, T.P.6    Hofmann, K.P.7
  • 180
    • 0028296886 scopus 로고
    • A C-terminal peptide of bovine rhodopsin binds to the transducin α-subunit and facilitates its activation
    • W.J. Phillips, and R.A. Cerione A C-terminal peptide of bovine rhodopsin binds to the transducin alpha subunit and facilitates its activation Biochem. J. 299 1994 351 357 (Pubitemid 24114125)
    • (1994) Biochemical Journal , vol.299 , Issue.2 , pp. 351-357
    • Phillips, W.J.1    Cerione, R.A.2
  • 183
    • 11144225829 scopus 로고    scopus 로고
    • Structural determinants for G protein activation and selectivity in the second intracellular loop of the thyrotropin receptor
    • DOI 10.1210/en.2004-1045
    • S. Neumann, G. Krause, M. Claus, and R. Paschke Structural determinants for G protein activation and selectivity in the second intracellular loop of the thyrotropin receptor Endocrinology 146 2005 477 485 (Pubitemid 40051774)
    • (2005) Endocrinology , vol.146 , Issue.1 , pp. 477-485
    • Neumann, S.1    Krause, G.2    Claus, M.3    Paschke, R.4
  • 184
    • 33750488472 scopus 로고    scopus 로고
    • Structural determinants for G-protein activation and specificity in the third intracellular loop of the thyroid-stimulating hormone receptor
    • DOI 10.1007/s00109-006-0087-8
    • M. Claus, S. Neumann, G. Kleinau, G. Krause, and R. Paschke Structural determinants for G-protein activation and specificity in the third intracellular loop of the thyroid-stimulating hormone receptor J. Mol. Med. 84 2006 943 954 (Pubitemid 44655872)
    • (2006) Journal of Molecular Medicine , vol.84 , Issue.11 , pp. 943-954
    • Claus, M.1    Neumann, S.2    Kleinau, G.3    Krause, G.4    Paschke, R.5
  • 186
    • 38049070335 scopus 로고    scopus 로고
    • Contributions of intracellular loops 2 and 3 of the lutropin receptor in gs coupling
    • K. Angelova, F. Fanelli, and D. Puett Contributions of intracellular loops 2 and 3 of the lutropin receptor in gs coupling Mol. Endocrinol. 22 2008 126 138
    • (2008) Mol. Endocrinol. , vol.22 , pp. 126-138
    • Angelova, K.1    Fanelli, F.2    Puett, D.3
  • 187
    • 0141811657 scopus 로고    scopus 로고
    • 1 angiotensin receptor activation and signaling
    • DOI 10.1210/en.2002-0135
    • Z. Gaborik, G. Jagadeesh, M.J. Zhang, A. Spat, K.J. Catt, and L. Hunyady The role of a conserved region of the second intracellular loop in AT1 angiotensin receptor activation and signaling Endocrinology 144 2003 2220 2228 (Pubitemid 36629870)
    • (2003) Endocrinology , vol.144 , Issue.6 , pp. 2220-2228
    • Gaborik, Z.1    Jagadeesh, G.2    Zhang, M.3    Spat, A.4    Catt, K.J.5    Hunyady, L.6
  • 188
    • 34047246323 scopus 로고    scopus 로고
    • A comprehensive structure-function map of the intracellular surface of the human C5a receptor. I. Identification of critical residues
    • DOI 10.1074/jbc.M607679200
    • M.L. Matsumoto, K. Narzinski, P.D. Kiser, G.V. Nikiforovich, and T.J. Baranski A comprehensive structure-function map of the intracellular surface of the human C5a receptor - I. Identification of critical residues J. Biol. Chem. 282 2007 3105 3121 (Pubitemid 47084352)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.5 , pp. 3105-3121
    • Matsumoto, M.L.1    Narzinski, K.2    Kiser, P.D.3    Nikiforovich, G.V.4    Baranski, T.J.5
  • 189
    • 78649417771 scopus 로고    scopus 로고
    • Structural determinants in the second intracellular loop of the human cannabinoid CB1 receptor mediate selective coupling to Gs and Gi
    • X. Chen, W. Yang, Y. Fab, J.S. Luo, K. Hong, Z. Wang, J.F. Yan, X. Chen, J.X. Lu, J.L. Benovic, and N.M. Zhou Structural determinants in the second intracellular loop of the human cannabinoid CB1 receptor mediate selective coupling to Gs and Gi Br. J. Pharmacol. 161 2010 1817 1834
    • (2010) Br. J. Pharmacol. , vol.161 , pp. 1817-1834
    • Chen, X.1    Yang, W.2    Fab, Y.3    Luo, J.S.4    Hong, K.5    Wang, Z.6    Yan, J.F.7    Chen, X.8    Lu, J.X.9    Benovic, J.L.10    Zhou, N.M.11
  • 191
    • 0029966772 scopus 로고    scopus 로고
    • Identification of G-protein binding sites of the human interleukin-8 receptors by functional mapping of the intracellular loops
    • B.B. Damaj, S.R. McColl, K. Neote, N. Songqing, K.T. Ogborn, C.A. Hebert, and P.H. Naccache Identification of G-protein binding sites of the human interleukin-8 receptors by functional mapping of the intracellular loops FASEB J. 10 1996 1426 1434 (Pubitemid 26347877)
    • (1996) FASEB Journal , vol.10 , Issue.12 , pp. 1426-1434
    • Damaj, B.B.1    McColl, S.R.2    Neote, K.3    Songqing, N.A.4    Ogborn, K.T.5    Hebert, C.A.6    Naccache, P.H.7
  • 192
    • 0032960146 scopus 로고    scopus 로고
    • Single amino acid substitution of Serine82 to Asparagine in first intracellular loop of human cholecystokinin (CCK)-B receptor confers full cyclic AMP responses to CCK and gastrin
    • S.V. Wu, M. Yang, D. Avedian, M. Birnbaumer, and J.H. Walsh Single amino acid substitution of serine82 to asparagine in first intracellular loop of human cholecystokinin (CCK)-B receptor confers full cyclic AMP responses to CCK and gastrin Mol. Pharmacol. 55 1999 795 803 (Pubitemid 29214598)
    • (1999) Molecular Pharmacology , vol.55 , Issue.5 , pp. 795-803
    • Wu, S.V.1    Yang, M.2    Avedian, D.3    Birnbaumer, M.4    Walsh, J.H.5
  • 193
    • 0030943262 scopus 로고    scopus 로고
    • Basic amino acids at the C-terminus of the third intracellular loop are required for the activation of phospholipase C by cholecystokinin-B receptors
    • H.L. Wang Basic amino acids at the C-terminus of the third intracellular loop are required for the activation of phospholipase C by cholecystokinin-B receptors J. Neurochem. 68 1997 1728 1735
    • (1997) J. Neurochem. , vol.68 , pp. 1728-1735
    • Wang, H.L.1
  • 194
    • 0032475883 scopus 로고    scopus 로고
    • Mediation of cyclic AMP signaling by the first intracellular loop of the gonadotropin-releasing hormone receptor
    • DOI 10.1074/jbc.273.40.25581
    • K.K. Arora, L.Z. Krsmanovic, N. Mores, H. O'Farrell, and K.J. Catt Mediation of cyclic AMP signaling by the first intracellular loop of the gonadotropin-releasing hormone receptor J. Biol. Chem. 273 1998 25581 25586 (Pubitemid 28475777)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.40 , pp. 25581-25586
    • Arora, K.K.1    Krsmanovic, L.Z.2    Mores, N.3    O'Farrell, H.4    Catt, K.J.5
  • 196
    • 0033544868 scopus 로고    scopus 로고
    • Expression and function of the gonadotropin-releasing hormone receptor are dependent on a conserved apolar amino acid in the third intracellular loop
    • H. Chung, Q. Yang, C.K. J., and K.K. Arora Expression and function of the gonadotropin-releasing hormone receptor are dependent on a conserved apolar amino acid in the third intracellular loop J. Biol. Chem. 274 1999 35756 35762 (Pubitemid 129512878)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.50 , pp. 35756-35762
    • Chung, H.-O.1    Yang, Q.2    Catt, K.J.3    Arora, K.K.4
  • 197
    • 0032079392 scopus 로고    scopus 로고
    • Alanine-261 in intracellular loop III of the human gonadotropin-releasing hormone receptor is crucial for G-protein coupling and receptor internalization
    • D.B. Myburgh, R.P. Millar, and J.P. Hapgood Alanine-261 in intracellular loop III of the human gonadotropin-releasing hormone receptor is crucial for G-protein coupling and receptor internalization Biochem. J. 331 1998 893 896 (Pubitemid 28211914)
    • (1998) Biochemical Journal , vol.331 , Issue.3 , pp. 893-896
    • Myburgh, D.B.1    Millar, R.P.2    Hapgood, J.P.3
  • 198
    • 0033048623 scopus 로고    scopus 로고
    • A conserved arginine in the distal third intracellular loop of the mu-opioid receptor is required for G protein activation
    • H.L. Wang A conserved arginine in the distal third intracellular loop of the mu-opioid receptor is required for G protein activation J. Neurochem. 72 1999 1307 1314
    • (1999) J. Neurochem. , vol.72 , pp. 1307-1314
    • Wang, H.L.1
  • 199
    • 0035800798 scopus 로고    scopus 로고
    • Single amino acid substitutions and deletions that alter the G protein coupling properties of the V2 vasopressin receptor identified in yeast by receptor random mutagenesis
    • I. Erlenbach, E. Kostenis, C. Schmidt, C. Serradeil-Le Gal, D. Raufaste, M.E. Dumont, M.H. Pausch, and J. Wess Single amino acid substitutions and deletions that alter the G protein coupling properties of the V2 vasopressin receptor identified in yeast by receptor random mutagenesis J. Biol. Chem. 276 2001 29382 29392
    • (2001) J. Biol. Chem. , vol.276 , pp. 29382-29392
    • Erlenbach, I.1    Kostenis, E.2    Schmidt, C.3    Serradeil-Le Gal, C.4    Raufaste, D.5    Dumont, M.E.6    Pausch, M.H.7    Wess, J.8
  • 200
    • 0032500569 scopus 로고    scopus 로고
    • Molecular basis of V2 vasopressin receptor/G(s) coupling selectivity
    • DOI 10.1074/jbc.273.41.26549
    • I. Erlenbach, and J. Wess Molecular basis of V2 vasopressin receptor/Gs coupling selectivity J. Biol. Chem. 273 1998 26549 26558 (Pubitemid 28471665)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.41 , pp. 26549-26558
    • Erlenbach, I.1    Wess, J.2
  • 201
    • 0029953103 scopus 로고    scopus 로고
    • Alanine scanning mutagenesis of conserved arginine/lysine- arginine/lysine-X-X-arginine/lysine G protein-activating motifs on m1 muscarinic acetylcholine receptors
    • N.H. Lee, N.S.M. Geoghagen, E. Cheng, R.T. Cline, and C.M. Fraser Alanine scanning mutagenesis of conserved arginine/lysine-arginine/lysine-X-X-arginine/ lysine G protein-activating motifs on m1 muscarinic acetylcholine receptors Mol. Pharmacol. 50 1996 140 148 (Pubitemid 26250085)
    • (1996) Molecular Pharmacology , vol.50 , Issue.1 , pp. 140-148
    • Lee, N.H.1    Geoghagen, N.S.M.2    Cheng, E.3    Cline, R.T.4    Fraser, C.M.5
  • 202
    • 79953016938 scopus 로고    scopus 로고
    • Helix 8 of the M1 muscarinic acetylcholine receptor: Scanning mutagenesis delineates a G protein recognition site
    • R.G. Kaye, J.W. Saldanha, Z.L. Lu, and E.C. Hulme Helix 8 of the M1 muscarinic acetylcholine receptor: scanning mutagenesis delineates a G protein recognition site Mol. Pharmacol. 79 2011 701 709
    • (2011) Mol. Pharmacol. , vol.79 , pp. 701-709
    • Kaye, R.G.1    Saldanha, J.W.2    Lu, Z.L.3    Hulme, E.C.4
  • 203
    • 0029059732 scopus 로고
    • Mapping of single amino-acid residues required for selective activation of G(q/11) by the M3 muscarinic acetylcholine receptor
    • N. Blin, J. Yun, and J. Wess Mapping of single amino-acid residues required for selective activation of G(q/11) by the M3 muscarinic acetylcholine receptor J. Biol. Chem. 270 1995 17741 17748
    • (1995) J. Biol. Chem. , vol.270 , pp. 17741-17748
    • Blin, N.1    Yun, J.2    Wess, J.3
  • 204
    • 0028814543 scopus 로고
    • Structure function of muscarinic receptor coupling to G-proteins- random saturation mutagenesis identifies a critical determinant of receptor affinity for G-proteins
    • E.S. Burstein, T.A. Spalding, D. Hilleubanks, and M.R. Brann Structure function of muscarinic receptor coupling to G-proteins- random saturation mutagenesis identifies a critical determinant of receptor affinity for G-proteins J. Biol. Chem. 270 1995 3141 3146
    • (1995) J. Biol. Chem. , vol.270 , pp. 3141-3146
    • Burstein, E.S.1    Spalding, T.A.2    Hilleubanks, D.3    Brann, M.R.4
  • 205
    • 0030041761 scopus 로고    scopus 로고
    • Amino acid side chains that define muscarinic receptor/G-protein coupling: Studies of the third intracellular loop
    • DOI 10.1074/jbc.271.6.2882
    • E.S. Burstein, T.A. Spalding, and M.R. Brann Amino acid side chains that define muscarinic receptor G-protein coupling - studies of the third intracellular loop J. Biol. Chem. 271 1996 2882 2885 (Pubitemid 26055585)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.6 , pp. 2882-2885
    • Burstein, E.S.1    Spalding, T.A.2    Brann, M.R.3
  • 206
    • 0001107340 scopus 로고    scopus 로고
    • Structure/function relationships of a G-protein coupling pocket formed by third intracellular loop of the m5 muscarinic receptor
    • DOI 10.1021/bi972132j
    • E.S. Burstein, T.A. Spalding, and M.R. Brann Structure/function relationships of a G-protein coupling pocket formed by the third intracellular loop of the m5 muscarinic receptor Biochemistry 37 1998 4052 4058 (Pubitemid 28166426)
    • (1998) Biochemistry , vol.37 , Issue.12 , pp. 4052-4058
    • Burstein, E.S.1    Spalding, T.A.2    Brann, M.R.3
  • 207
    • 0035824582 scopus 로고    scopus 로고
    • Mutational and computational analysis of the alpha(1b)-adrenergic receptor. Involvement of basic and hydrophobic residues in receptor activation and G protein coupling
    • P.J. Greasley, F. Fanelli, A. Scheer, L. Abuin, M. Nenniger-Tosato, P.G. DeBenedetti, and S. Cotecchia Mutational and computational analysis of the alpha(1b)-adrenergic receptor. Involvement of basic and hydrophobic residues in receptor activation and G protein coupling J. Biol. Chem. 276 2001 46485 46494
    • (2001) J. Biol. Chem. , vol.276 , pp. 46485-46494
    • Greasley, P.J.1    Fanelli, F.2    Scheer, A.3    Abuin, L.4    Nenniger-Tosato, M.5    Debenedetti, P.G.6    Cotecchia, S.7
  • 208
    • 0027379660 scopus 로고
    • Hydrophobic amino acid in the i2 loop plays a key role in receptor-G protein coupling
    • O. Moro, J. Lameh, P. Hogger, and W. Sadee Hydrophobic amino-acid in the IL2-loop plays a key role in receptor G-protein coupling J. Biol. Chem. 268 1993 22273 22276 (Pubitemid 23318268)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.30 , pp. 22273-22276
    • Moro, O.1    Lameh, J.2    Hogger, P.3    Sadee, W.4
  • 210
    • 33645831353 scopus 로고    scopus 로고
    • Molecular determinants in the second intracellular loop of the 5-hydroxytryptamine-1A receptor for g-protein coupling
    • N. Kushwaka, S.C. Harwood, A.M. Wilson, M.S. Berger, L.H. Tecott, B.L. Roth, and P.R. Albert Molecular determinants in the second intracellular loop of the 5-hydroxytryptamine-1A receptor for g-protein coupling Mol. Pharmacol. 69 2006 1518 1526
    • (2006) Mol. Pharmacol. , vol.69 , pp. 1518-1526
    • Kushwaka, N.1    Harwood, S.C.2    Wilson, A.M.3    Berger, M.S.4    Tecott, L.H.5    Roth, B.L.6    Albert, P.R.7
  • 211
    • 0028973233 scopus 로고
    • Identification of a Gs coupling domain in the amino terminus of the third intracellular loop of the a2A-adrenergic receptor
    • M.G. Eason, and S.B. Ligget Identification of a Gs coupling domain in the amino terminus of the third intracellular loop of the a2A-adrenergic receptor J. Biol. Chem. 270 1995 24753 24760
    • (1995) J. Biol. Chem. , vol.270 , pp. 24753-24760
    • Eason, M.G.1    Ligget, S.B.2
  • 212
    • 0029993438 scopus 로고    scopus 로고
    • Mutation of an aspartate at position 63 in the human platelet-activating factor receptor augments binding affinity but abolishes G-protein-coupling and inositol phosphate production
    • DOI 10.1006/bbrc.1996.0341
    • J.L. Parent, C. LeGouill, M. RolaPleszczynski, and J. Stankova Mutation of an aspartate at position 63 in the human platelet-activating factor receptor augments binding affinity but abolishes G-protein-coupling and inositol phosphate production Biochem. Biophys. Res. Commun. 219 1996 968 975 (Pubitemid 26106787)
    • (1996) Biochemical and Biophysical Research Communications , vol.219 , Issue.3 , pp. 968-975
    • Parent, J.-L.1    Le Gouill, C.2    Rola-Pleszczynski, M.3    Stankova, J.4
  • 213
    • 84859103411 scopus 로고    scopus 로고
    • Protease-activated receptor 1 (PAR1) coupling to Gq/11 but not to Gi/o or G12/13 is mediated by discrete amino acids within the receptor second intracellular loop
    • K.L. McCoy, S. Gyoneva, C.P. Vellano, A.V. Smrcka, S.F. Traynelis, and J.R. Hepler Protease-activated receptor 1 (PAR1) coupling to Gq/11 but not to Gi/o or G12/13 is mediated by discrete amino acids within the receptor second intracellular loop Cell. Signal. 24 2012 9
    • (2012) Cell. Signal. , vol.24 , pp. 9
    • McCoy, K.L.1    Gyoneva, S.2    Vellano, C.P.3    Smrcka, A.V.4    Traynelis, S.F.5    Hepler, J.R.6
  • 214
    • 23944506541 scopus 로고    scopus 로고
    • A profile of the residues in the first intracellular loop critical for Gs-mediated signaling of human prostacyclin receptor characterized by an integrative approach of NMR-experiment and mutagenesis
    • DOI 10.1021/bi050483p
    • L. Zhang, G. Huang, J. Wu, and H.H. Ruan A profile of the residues in the first intracellular loop critical for Gs-mediated signaling of human prostacyclin receptor characterized by an integrative approach of NMR - experiment and mutagenesis Biochemistry 44 2005 11389 11401 (Pubitemid 41209075)
    • (2005) Biochemistry , vol.44 , Issue.34 , pp. 11389-11401
    • Zhang, L.1    Huang, G.2    Wu, J.3    Ruan, K.-H.4
  • 215
    • 0348010316 scopus 로고    scopus 로고
    • Closely Related G-protein-coupled Receptors Use Multiple and Distinct Domains on G-protein α-Subunits for Selective Coupling
    • DOI 10.1074/jbc.M304417200
    • J.E. Slessareva, H.Z. Ma, K.M. Depree, L.A. Flood, H.S. Bae, T.M. Cabrera-Vera, H.E. Hamm, and S.G. Graber Closely related G-protein-coupled receptors use multiple and distinct domains on G-protein alpha-subunits for selective coupling J. Biol. Chem. 278 2003 50530 50536 (Pubitemid 37548899)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.50 , pp. 50530-50536
    • Slessareva, J.E.1    Ma, H.2    Depree, K.M.3    Flood, L.A.4    Bae, H.5    Cabrera-Vera, T.M.6    Hamm, H.E.7    Graber, S.G.8
  • 216
    • 0032562289 scopus 로고    scopus 로고
    • Targeting the receptor-G(q) interface to inhibit in vivo pressure overload myocardial hypertrophy
    • DOI 10.1126/science.280.5363.574
    • S.A. Akhter, L.M. Luttrell, H.A. Rockman, G. Iaccarino, R.J. Lefkowitz, and W.J. Koch Targeting the receptor-G(q) interface to inhibit in vivo pressure overload myocardial hypertrophy Science 280 1998 574 577 (Pubitemid 28227758)
    • (1998) Science , vol.280 , Issue.5363 , pp. 574-577
    • Akhter, S.A.1    Luttrell, L.M.2    Rockman, H.A.3    Iaccarino, G.4    Lefkowitz, R.J.5    Koch, W.J.6
  • 217
    • 0030851384 scopus 로고    scopus 로고
    • The N-terminal extension of Gα(q) is critical for constraining the selectivity of receptor coupling
    • DOI 10.1074/jbc.272.31.19107
    • E. Kostenis, M. Degtyarev, B. Conklin, and J. Wess The N-terminal extension of Gaq is critical for constraining the selectivity of receptor coupling J. Biol. Chem. 272 1997 19107 19110 (Pubitemid 27337695)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.31 , pp. 19107-19110
    • Kostenis, E.1    Degtyarev, M.Y.2    Conklin, B.R.3    Wess, J.4
  • 218
    • 36849073830 scopus 로고    scopus 로고
    • Mechanisms of dominant negative G-protein α subunits
    • DOI 10.1002/jnr.21414
    • B. Barren, and N.O. Artemyev Mechanisms of dominant negative G-protein alpha subunits J. Neurosci. Res. 85 2007 3505 3514 (Pubitemid 350228695)
    • (2007) Journal of Neuroscience Research , vol.85 , Issue.16 , pp. 3505-3514
    • Barren, B.1    Artemyev, N.O.2
  • 219
    • 0344609797 scopus 로고    scopus 로고
    • A dominant-negative strategy for studying roles of G proteins in vivo
    • DOI 10.1074/jbc.274.10.6610
    • A. Gilchrist, M. Bunemann, A. Li, M.M. Hosey, and H.E. Hamm A dominant-negative strategy for studying roles of G proteins in vivo J. Biol. Chem. 274 1999 6610 6616 (Pubitemid 29111079)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.10 , pp. 6610-6616
    • Gilchrist, A.1    Bunemann, M.2    Li, A.3    Hosey, M.M.4    Hamm, H.E.5
  • 220
    • 33751248238 scopus 로고    scopus 로고
    • Unravelling hot spots: A comprehensive computational mutagenesis study
    • DOI 10.1007/s00214-006-0151-z
    • I.S. Moreira, P.A. Fernandes, and M.J. Ramos Unravelling hot spots: a comprehensive computational mutagenesis study Theor. Chem. Acc. 117 2007 99 113 (Pubitemid 44791243)
    • (2007) Theoretical Chemistry Accounts , vol.117 , Issue.1 , pp. 99-113
    • Moreira, I.S.1    Fernandes, P.A.2    Ramos, M.J.3
  • 221
    • 33847650393 scopus 로고    scopus 로고
    • Computational alanine scanning mutagenesis - An improved methodological approach
    • DOI 10.1002/jcc.20566
    • I.S. Moreira, P.A. Fernandes, and M.J. Ramos Computational alanine scanning mutagenesis - an improved methodological approach J. Comput. Chem. 28 2007 644 654 (Pubitemid 46353600)
    • (2007) Journal of Computational Chemistry , vol.28 , Issue.3 , pp. 644-654
    • Moreira, I.S.1    Fernandes, P.A.2    Ramos, M.J.3
  • 222
    • 34548779127 scopus 로고    scopus 로고
    • Hot spots - A review of the protein-protein interface determinant amino-acid residues
    • DOI 10.1002/prot.21396
    • I.S. Moreira, P.A. Fernandes, and M.J. Ramos Hot spots - a review of the protein-protein interface determinant amino-acid residues Proteins 68 2007 803 812 (Pubitemid 47434705)
    • (2007) Proteins: Structure, Function and Genetics , vol.68 , Issue.4 , pp. 803-812
    • Moreira, I.S.1    Fernandes, P.A.2    Ramos, M.J.3
  • 224
    • 0030987069 scopus 로고    scopus 로고
    • How receptors talk to trimeric G proteins
    • DOI 10.1016/S0955-0674(97)80054-3
    • H.R. Bourne How receptors talk to trimeric G proteins Curr. Opin. Cell Biol. 9 1997 134 142 (Pubitemid 27135978)
    • (1997) Current Opinion in Cell Biology , vol.9 , Issue.2 , pp. 134-142
    • Bourne, H.R.1
  • 226
    • 77953252509 scopus 로고    scopus 로고
    • The quest to understand heterotrimeric G protein signaling
    • J.J.G. Tesmer The quest to understand heterotrimeric G protein signaling Nat. Struct. Mol. Biol. 17 2010 650 652
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 650-652
    • Tesmer, J.J.G.1
  • 228
    • 33750702165 scopus 로고    scopus 로고
    • Structural basis of function in heterotrimeric G proteins
    • W.M. Oldham, and H.E. Hamm Structural basis of function in heterotrimeric G proteins Q. Rev. Biophys. 2006 1 50
    • (2006) Q. Rev. Biophys. , pp. 1-50
    • Oldham, W.M.1    Hamm, H.E.2
  • 230
    • 77956638608 scopus 로고    scopus 로고
    • Putative active states of a prototypic G-protein-coupled receptor from biased molecular dynamics
    • D. Provasi, and M. Filizola Putative active states of a prototypic G-protein-coupled receptor from biased molecular dynamics Biophys. J. 98 2010 2347 2355
    • (2010) Biophys. J. , vol.98 , pp. 2347-2355
    • Provasi, D.1    Filizola, M.2
  • 235
    • 84864622261 scopus 로고    scopus 로고
    • GDP release preferentially occurs on the phosphate side in heterotrimeric G-proteins
    • M. Louet, J. Martinez, and N. Floquet GDP release preferentially occurs on the phosphate side in heterotrimeric G-proteins PLoS Comput. Biol. 8 2012 e1002595
    • (2012) PLoS Comput. Biol. , vol.8 , pp. 1002595
    • Louet, M.1    Martinez, J.2    Floquet, N.3
  • 236
    • 0028172426 scopus 로고
    • Binding of an alpha2 adrenergic receptor third intracellular loop peptide to Gbeta and the amino terminus of Galpha
    • J.M. Taylor, G.G. Jacobmosier, R.G. Lawton, A.E. Remmers, and R.R. Neubig Binding of an alpha(2) adrenergic-receptor 3rd intracellular loop peptide to g-beta and the amino-terminus of g-alpha J. Biol. Chem. 269 1994 27618 27624 (Pubitemid 2158570)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.44 , pp. 27618-27624
    • Taylor, J.M.1    Jacob-Mosier, G.G.2    Lawton, R.G.3    Remmers, A.E.4    Neubig, R.R.5
  • 237
    • 0026786080 scopus 로고
    • Rhodopsin transducin interactions. Characterization of the binding of the transducin beta gamma subunit complex to rhodopsin using florescence spectroscopy
    • W.J. Phillips, and R.A. Cerione Rhodopsin transducin interactions. Characterization of the binding of the transducin beta gamma subunit complex to rhodopsin using florescence spectroscopy J. Biol. Chem. 267 1992 17032 17039
    • (1992) J. Biol. Chem. , vol.267 , pp. 17032-17039
    • Phillips, W.J.1    Cerione, R.A.2
  • 238
    • 0029026880 scopus 로고
    • Receptor G-protein coupling is established by a potential conformational switch in the beta-gamma complex
    • O. Kisselev, A. Pronin, M. Ermolaeva, and N. Gautam Receptor G-protein coupling is established by a potential conformational switch in the beta-gamma complex Proc. Natl. Acad. Sci. U. S. A. 92 1995 9102 9106
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 9102-9106
    • Kisselev, O.1    Pronin, A.2    Ermolaeva, M.3    Gautam, N.4
  • 239
    • 47749117162 scopus 로고    scopus 로고
    • G protein beta gamma subunits: Central mediators of G protein-coupled receptor signaling
    • A.V. Smrcka G protein beta gamma subunits: central mediators of G protein-coupled receptor signaling Cell Mol. Life Sci. 65 2008 2191 2214
    • (2008) Cell Mol. Life Sci. , vol.65 , pp. 2191-2214
    • Smrcka, A.V.1
  • 240
    • 0025904873 scopus 로고
    • S: Requirement for multiple cytoplasmic domains in the coupling process
    • S.B. Liggett, M.G. Caron, R.J. Lefkowitz, and M. Hnatowich Coupling of a mutated form of the human beta-2-adrenergic receptor to Gi and Gs-requirement for multiple cytoplasmatic domains in the coupling process J. Biol. Chem. 266 1991 4816 4821 (Pubitemid 21909428)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.8 , pp. 4816-4821
    • Liggett, S.B.1    Caron, M.G.2    Lefkowitz, R.J.3    Hnatowich, M.4
  • 241
    • 0028326850 scopus 로고
    • The middle portion in the second cytoplasmic loop of the thyrotropin receptor plays a crucial role in adenylate cyclase activation
    • DOI 10.1210/me.8.4.498
    • S. Kosugi, L.D. Kohn, T. Akamizu, and T. Mori The middle portion in the 2Nd cytoplasmic loop of the thyrotropin receptor plays a crucial role in adenylate-cyclase activation Mol. Endocrinol. 8 1994 498 509 (Pubitemid 24114740)
    • (1994) Molecular Endocrinology , vol.8 , Issue.4 , pp. 498-509
    • Kosugi, S.1    Kohn, L.D.2    Akamizu, T.3    Mori, T.4
  • 242
    • 0031002654 scopus 로고    scopus 로고
    • The thrombin receptor second cytoplasmic loop confers coupling to G(q)- like G proteins in chimeric receptors: Additional evidence for a common transmembrane signaling and G protein coupling mechanism in G protein- coupled receptors
    • DOI 10.1074/jbc.272.11.6898
    • S. Verrall, M. Ishii, M. Chen, L. Wang, T. Tram, and S.R. Coughlin The thrombin receptor second cytoplasmic loop confers coupling to G(q)-like G proteins in chimeric receptors - additional evidence for a common transmembrane signaling and G protein coupling mechanism in G protein-coupled receptors J. Biol. Chem. 272 1997 6898 6902 (Pubitemid 27166387)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.11 , pp. 6898-6902
    • Verrall, S.1    Ishii, M.2    Chen, M.3    Wang, L.4    Tram, T.5    Coughlin, S.R.6
  • 243
    • 3042798261 scopus 로고    scopus 로고
    • Molecular mechanisms of ligand binding, signaling, and regulation within the superfamily of G-protein-coupled receptors: Molecular modeling and mutagenesis approaches to receptor structure and function
    • DOI 10.1016/j.pharmthera.2004.05.002, PII S0163725804000695
    • K. Kristiansen Molecular mechanisms of ligand binding, signaling, and regulation within the superfamily of G-protein-coupled receptors: molecular modeling and mutagenesis approaches to receptor structure and function Pharmacol. Ther. 103 2004 21 80 (Pubitemid 38891912)
    • (2004) Pharmacology and Therapeutics , vol.103 , Issue.1 , pp. 21-80
    • Kristiansen, K.1
  • 244
    • 0034948696 scopus 로고    scopus 로고
    • Structural mimicry in G-protein-coupled receptors: Implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors
    • J.A. Ballesteros, L. Shi, and J.A. Javitch Structural mimicry in G-protein-coupled receptors: implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors Mol. Pharmacol. 60 2001 1
    • (2001) Mol. Pharmacol. , vol.60 , pp. 1
    • Ballesteros, J.A.1    Shi, L.2    Javitch, J.A.3
  • 245
    • 33845959757 scopus 로고    scopus 로고
    • Accessibility of cysteine residues substituted into the cytoplasmic regions of the α-factor receptor identifies the intracellular residues that are available for G protein interaction
    • DOI 10.1021/bi0614939
    • Y. Choi, and J.B. Konopka Accessibility of cysteine residues substituted into the cytoplasmic regions of the alpha-factor receptor identifies the intracellular residues that are available for G protein interaction Biochemistry 45 2006 15310 15317 (Pubitemid 46032457)
    • (2006) Biochemistry , vol.45 , Issue.51 , pp. 15310-15317
    • Choi, Y.1    Konopka, J.B.2
  • 246
    • 69249158290 scopus 로고    scopus 로고
    • Allosteric communication between protomers of dopamine class A GPCR dimers modulates activation
    • Y. Han, I.S. Moreira, E. Urizar, H. Weinstein, and J.A. Javitch Allosteric communication between protomers of dopamine class A GPCR dimers modulates activation Nat. Chem. Biol. 5 2009 688 695
    • (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
  • 247
    • 0032544633 scopus 로고    scopus 로고
    • The second intracellular loop of the m5 muscarinic receptor is the switch which enables G-protein coupling
    • DOI 10.1074/jbc.273.38.24322
    • E.S. Burstein, T.A. Spalding, and M.R. Brann The second intracellular loop of the m5 muscarinic receptor is the switch which enables G-protein coupling J. Biol. Chem. 273 1998 24322 24327 (Pubitemid 28454919)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.38 , pp. 24322-24327
    • Burstein, E.S.1    Spalding, T.A.2    Brann, M.R.3
  • 248
    • 0036073523 scopus 로고    scopus 로고
    • The intracellular loops of the GB2 subunit are crucial for G-protein coupling of the heteromeric γ-aminobutyrate B receptor
    • DOI 10.1124/mol.62.2.343
    • M. Havlickova The intracellular loops of the GB2 subunit are crucial for G-protein coupling of the heteromeric [gamma]-aminobutyrate B receptor Mol. Pharmacol. 62 2002 343 350 (Pubitemid 34804115)
    • (2002) Molecular Pharmacology , vol.62 , Issue.2 , pp. 343-350
    • Havlickova, M.1    Prezeau, L.2    Duthey, B.3    Bettler, B.4    Pin, J.-P.5    Blahos, J.6
  • 249
    • 0030928868 scopus 로고    scopus 로고
    • Evidence for an important functional role of intracellular loop II of the lutropin receptor
    • DOI 10.1016/S0303-7207(97)04035-5, PII S0303720797040355
    • L.M. Fernandez, and D. Puett Evidence for an important functional role of intracellular loop II of the lutropin receptor Mol. Cell. Endocrinol. 128 1997 161 169 (Pubitemid 27158142)
    • (1997) Molecular and Cellular Endocrinology , vol.128 , Issue.1-2 , pp. 161-169
    • Fernandez, L.M.1    Puett, D.2
  • 250
    • 0025817671 scopus 로고
    • 2a-adrenergic receptor alter receptor G protein coupling by distinct mechanisms
    • H.M. Dalman, and R.R. Neubig 2 Peptides from the alpha 2 adrenergic receptor alter receptor G Protein coupling by distinct mechanisms J. Biol. Chem. 266 1991 11025 11029 (Pubitemid 21906906)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.17 , pp. 11025-11029
    • Dalman, H.M.1    Neubig, R.R.2
  • 251
    • 0029841941 scopus 로고    scopus 로고
    • 2-adrenergic receptor i3c region
    • S.M. Wade, M.K. Scribner, H.M. Dalman, J.M. Taylor, and R.R. Neubig Structural requirements for G(0) activation by receptor-derived peptides: activation and modulation domains of the alpha(2)-adrenergic receptor i3c region Mol. Pharmacol. 50 1996 351 358 (Pubitemid 26265140)
    • (1996) Molecular Pharmacology , vol.50 , Issue.2 , pp. 351-358
    • Wade, S.M.1    Scribner, M.K.2    Dalman, H.M.3    Taylor, J.M.4    Neubig, R.R.5
  • 253
    • 0025605345 scopus 로고
    • Cloning and expression of a cDNA encoding an endothelin receptor
    • H. Arai, S. Hori, I. Aramori, H. Ohkubo, and S. Nakanishi Cloning and expression of a cDNA encoding an endothelial receptor Nature 348 1990 730 732 (Pubitemid 120015147)
    • (1990) Nature , vol.348 , Issue.6303 , pp. 730-732
    • Arai, H.1    Hori, S.2    Aramori, I.3    Ohkubo, H.4    Nakanishi, S.5
  • 255
    • 0026672627 scopus 로고
    • Brain and gastrointestinal cholecystokinin receptor family - Structure and functional expression
    • S.A. Wank, J.R. Pisegna, and A. Deweerth Brain and gastrointestinal cholecystokinin receptor family - structure and functional expression Proc. Natl. Acad. Sci. U. S. A. 89 1992 8691 8695
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 8691-8695
    • Wank, S.A.1    Pisegna, J.R.2    Deweerth, A.3
  • 256
    • 0027328071 scopus 로고
    • Charged amino acids required for signal transduction by the m3 muscarinic acetylcholine receptor
    • M.T. Kunkel, and E.G. Peralta Charged amino acid required for signal transduction by the m3 muscarinic acetylcholine receptor EMBO J. 12 1993 3809 3815 (Pubitemid 23282757)
    • (1993) EMBO Journal , vol.12 , Issue.10 , pp. 3809-3815
    • Kunkel, M.T.1    Peralta, E.G.2
  • 257
    • 0030060858 scopus 로고    scopus 로고
    • Constitutive activation of chimeric m2/m5 muscarinic receptors and delineation of G-protein coupling selectivity domains
    • DOI 10.1016/0006-2952(95)02234-1
    • E.S. Burstein, T.A. Spalding, and M.R. Brann Constitutive activation of chimeric m2/m5 muscarinic receptors and delineation of G-protein coupling selectivity domains Biochem. Pharmacol. 51 1996 539 544 (Pubitemid 26069856)
    • (1996) Biochemical Pharmacology , vol.51 , Issue.4 , pp. 539-544
    • Burstein, E.S.1    Spalding, T.A.2    Brann, M.R.3
  • 258
    • 0031037633 scopus 로고    scopus 로고
    • Pharmacology of muscarinic receptor subtypes constitutively activated by G proteins
    • E.S. Burstein, T.A. Spalding, and M.R. Brann Pharmacology of muscarinic receptor subtypes constitutively activated by G proteins Mol. Pharmacol. 51 1997 312 319 (Pubitemid 27074153)
    • (1997) Molecular Pharmacology , vol.51 , Issue.2 , pp. 312-319
    • Burstein, E.S.1    Spalding, T.A.2    Brann, M.R.3
  • 259
  • 260
    • 0027422737 scopus 로고
    • Specificity of receptor-G protein interactions: Searching for the structure behind the signal
    • DOI 10.1016/0898-6568(93)90046-O
    • K.E. Hedin, K. Duerson, and D.E. Clapham Specificity of receptor G-protein interactions-searching for the structure behind the signal Cell. Signal. 5 1993 505 518 (Pubitemid 23343362)
    • (1993) Cellular Signalling , vol.5 , Issue.5 , pp. 505-518
    • Hedin, K.E.1    Duerson, K.2    Clapham, D.E.3
  • 263
    • 0025193034 scopus 로고
    • Regulation of Gi and Go by mastoparan, related amphilic peptides and hydrophobic amines - Mechanism and structural determinants of activity
    • T. Higashijima, J. Burnier, and E.M. Ross Regulation of Gi and Go by mastoparan, related amphilic peptides and hydrophobic amines - mechanism and structural determinants of activity J. Biol. Chem. 265 1990 14176 14186
    • (1990) J. Biol. Chem. , vol.265 , pp. 14176-14186
    • Higashijima, T.1    Burnier, J.2    Ross, E.M.3
  • 264
    • 0026787417 scopus 로고
    • G-protein bound conformation of a mastoparan-x a receptor mimetic peptide
    • M. Sukumar, and T. Higashijima G-protein bound conformation of a mastoparan-x a receptor mimetic peptide J. Biol. Chem. 267 1992 21421 21424
    • (1992) J. Biol. Chem. , vol.267 , pp. 21421-21424
    • Sukumar, M.1    Higashijima, T.2
  • 265
    • 0030610242 scopus 로고    scopus 로고
    • A G(s)-selective analog of the receptor-mimetic peptide mastoparan binds to G(s)α in a kinked helical conformation
    • DOI 10.1021/bi962356m
    • M. Sukumar, E.M. Ross, and T. Higashijima A G(s)-selective analog of the receptor-mimetic peptide mastoparan binds to G(s)alpha in a kinked helical conformation Biochemistry 36 1997 3632 3639 (Pubitemid 27143518)
    • (1997) Biochemistry , vol.36 , Issue.12 , pp. 3632-3639
    • Sukumar, M.1    Ross, E.M.2    Higashijima, T.3
  • 266
    • 29344473088 scopus 로고    scopus 로고
    • 2 subtype
    • DOI 10.1016/j.febslet.2005.11.042, PII S0014579305014110
    • S. Ichiyama, Y. Oka, K. Haga, S. Kojima, Y. Tateishi, M. Shirakawa, and T. Haga The structure of the third intracellular loop of the muscarinic acetylcholine receptor M2 subtype FEBS Lett. 580 2006 23 26 (Pubitemid 43005306)
    • (2006) FEBS Letters , vol.580 , Issue.1 , pp. 23-26
    • Ichiyama, S.1    Oka, Y.2    Haga, K.3    Kojima, S.4    Tateishi, Y.5    Shirakawa, M.6    Haga, T.7
  • 267
    • 0037452913 scopus 로고    scopus 로고
    • Sequences in the intracellular loops of the yeast pheromone receptor ste2p required for G protein activation
    • DOI 10.1021/bi0269308
    • A. Celic, N.P. Martin, C.D. Son, J.M. Becker, F. Naider, and M.E. Dumont Sequences in the intracellular loops of the yeast pheromone receptor Ste2p required for G protein activation Biochemistry 42 2003 3004 3017 (Pubitemid 36331544)
    • (2003) Biochemistry , vol.42 , Issue.10 , pp. 3004-3017
    • Celic, A.1    Martin, N.P.2    Son, C.D.3    Becker, J.M.4    Naider, F.5    Dumont, M.E.6
  • 268
    • 33646531437 scopus 로고    scopus 로고
    • G proteins in drug screening: From analysis of receptor-G protein specificity to manipulation of GPCR-mediated signalling pathways
    • E. Kostenis G proteins in drug screening: from analysis of receptor-G protein specificity to manipulation of GPCR-mediated signalling pathways Curr. Pharm. Des. 12 2006 1703 1715
    • (2006) Curr. Pharm. Des. , vol.12 , pp. 1703-1715
    • Kostenis, E.1
  • 269
    • 3342875499 scopus 로고    scopus 로고
    • Identification of a novel site within G protein α subunits important for specificity of receptor-G protein interaction
    • DOI 10.1124/mol.66.2.250
    • A. Heydorn, R. Ward, R. Jorgensen, M. Rosenkilde, T. Frimurer, G. Milligan, and E. Kostenis Identification of a novel site within G protein alpha subunits important for specificity of receptor-G protein interaction Mol. Pharmacol. 66 2004 250 259 (Pubitemid 38989481)
    • (2004) Molecular Pharmacology , vol.66 , Issue.2 , pp. 250-259
    • Heydorn, A.1    Ward, R.J.2    Jorgensen, R.3    Rosenkilde, M.M.4    Frimurer, T.M.5    Milligan, G.6    Kostenis, E.7
  • 270
    • 0025212680 scopus 로고
    • Regions of the alpha 1-adrenergic receptor involved in coupling to phosphatidylinositol hydrolysis and enhanced sensitivity of biological function
    • S. Cotecchia, S. Exum, M.G. Caron, and R.J. Lefkowitz Regions of the alpha 1-adrenergic receptor involved in coupling to phosphatidylinositol hydrolysis and enhanced sensitivity of biological function Proc. Natl. Acad. Sci. U. S. A. 87 1990 2896 2900
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 2896-2900
    • Cotecchia, S.1    Exum, S.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 271
    • 0032705301 scopus 로고    scopus 로고
    • Gi activator region of alpha 2A-adrenergic receptors: Distinct basic residues mediate Gi versus Gs activation
    • S. Wade, W. Lim, K.-L. Lan, D. Chung, M. Nanamori, and R. Neubig Gi activator region of alpha 2A-adrenergic receptors: distinct basic residues mediate Gi versus Gs activation Mol. Pharmacol. 56 1999 1005 1013
    • (1999) Mol. Pharmacol. , vol.56 , pp. 1005-1013
    • Wade, S.1    Lim, W.2    Lan, K.-L.3    Chung, D.4    Nanamori, M.5    Neubig, R.6
  • 272
    • 0033978672 scopus 로고    scopus 로고
    • A cluster of Ser/Thr residues at the C-terminus of μ-opioid receptor is required for G protein-coupled receptor kinase 2-mediated desensitization
    • DOI 10.1016/S0028-3908(99)00174-4, PII S0028390899001744
    • H.L. Wang A cluster of Ser/Thr residues at the C-terminus of mu-opioid receptor is required for G protein-coupled receptor kinase 2-mediated desensitization Neuropharmacology 39 2000 353 363 (Pubitemid 30052924)
    • (2000) Neuropharmacology , vol.39 , Issue.3 , pp. 353-363
    • Wang, H.L.1
  • 274
    • 77951844975 scopus 로고    scopus 로고
    • Teaching old receptors new tricks: Biasing seven-transmembrane receptors
    • S. Rajagopal, K. Rajagopal, and R.J. Lefkowitz Teaching old receptors new tricks: biasing seven-transmembrane receptors Nat. Rev. Drug Discov. 9 2010 373 386
    • (2010) Nat. Rev. Drug Discov. , vol.9 , pp. 373-386
    • Rajagopal, S.1    Rajagopal, K.2    Lefkowitz, R.J.3
  • 276
    • 0031815337 scopus 로고    scopus 로고
    • Effector pathway-dependent relative efficacy at serotonin type 2A and 2C receptors: Evidence for agonist-directed trafficking of receptor stimulus
    • K.A. Berg, S. Maayani, J. Goldfarb, C. Scaramellini, P. Leff, and W.P. Clarke Effector pathway-dependent relative efficacy at serotonin type 2A and 2C receptors: evidence for agonist-directed trafficking of receptor stimulus Mol. Pharmacol. 54 1998 94
    • (1998) Mol. Pharmacol. , vol.54 , pp. 94
    • Berg, K.A.1    Maayani, S.2    Goldfarb, J.3    Scaramellini, C.4    Leff, P.5    Clarke, W.P.6
  • 277
    • 0029054965 scopus 로고
    • Agonist-receptor efficacy.2. Agonist trafficking of receptor signals
    • T. Kenakin Agonist-receptor efficacy.2. Agonist trafficking of receptor signals Trends Pharmacol. Sci. 16 1995 232 238
    • (1995) Trends Pharmacol. Sci. , vol.16 , pp. 232-238
    • Kenakin, T.1
  • 278
    • 73549104285 scopus 로고    scopus 로고
    • The year in G protein-coupled receptor research
    • R.P. Millar, and C.L. Newton The year in G protein-coupled receptor research Mol. Endocrinol. 24 2010 261 274
    • (2010) Mol. Endocrinol. , vol.24 , pp. 261-274
    • Millar, R.P.1    Newton, C.L.2
  • 279
    • 0030938936 scopus 로고    scopus 로고
    • G-protein-coupled receptors: Molecular mechanisms involved in receptor activation and selectivity of G-protein recognition
    • J. Wess G-protein-coupled receptors: molecular mechanisms involved in receptor activation and selectivity of G-protein recognition FASEB J. 11 1997 346 354 (Pubitemid 27193939)
    • (1997) FASEB Journal , vol.11 , Issue.5 , pp. 346-354
    • Wess, J.1
  • 280
    • 0037762755 scopus 로고    scopus 로고
    • G protein selectivity is regulated by multiple intracellular regions of GPCRs
    • S.K.F. Wong G protein selectivity is regulated by multiple intracellular regions of GPCRs Neurosignals 12 2003 1 12
    • (2003) Neurosignals , vol.12 , pp. 1-12
    • Wong, S.K.F.1
  • 281
    • 0034671531 scopus 로고    scopus 로고
    • Selective role of G protein γ subunits in receptor interaction
    • DOI 10.1074/jbc.C000604200
    • Y.M. Hou, I. Azpiazu, A. Smrcka, and N. Gautam Selective role of G protein gamma subunits in receptor interaction J. Biol. Chem. 275 2000 38961 38964 (Pubitemid 32058906)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.50 , pp. 38961-38964
    • Hou, Y.1    Azpiazu, I.2    Smrcka, A.3    Gautam, N.4
  • 282
    • 33644835080 scopus 로고    scopus 로고
    • Regions in the G protein γ subunit important for interaction with receptors and effectors
    • DOI 10.1124/mol.105.018994
    • C.S. Myung, W.K. Lim, J.M. DeFilippo, H. Yasuda, R.R. Neubig, and J.C. Garrison Regions in the G protein gamma subunit important for interaction with receptors and effectors Mol. Pharmacol. 69 2006 877 887 (Pubitemid 43363862)
    • (2006) Molecular Pharmacology , vol.69 , Issue.3 , pp. 877-887
    • Myung, C.-S.1    Lim, W.K.2    DeFilippo, J.M.3    Yasuda, H.4    Neubig, R.R.5    Garrison, J.C.6
  • 283
    • 0029784196 scopus 로고    scopus 로고
    • The luteinizing hormone/chorionic gonadotropin receptor has distinct transmembrane conductors for cAMP and inositol phosphate signals
    • DOI 10.1074/jbc.271.32.19283
    • R.L. Gilchrist, K.S. Ryu, I.H. Ji, and T.H. Ji The luteinizing hormone chorionic gonadotropin receptor has distinct transmembrane conductors for cAMP and inositol phosphate signals J. Biol. Chem. 271 1996 19283 19287 (Pubitemid 26271596)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.32 , pp. 19283-19287
    • Gilchrist, R.L.1    Ryu, K.-S.2    Ji, I.3    Ji, T.H.4
  • 284
    • 0030049488 scopus 로고    scopus 로고
    • Constitutive activation of a single effector pathway: Evidence for multiple activation states of a G protein-coupled receptor
    • D.M. Perez, J. Hwa, R. Gaivin, M. Mathur, F. Brown, and R.M. Graham Constitutive activation of a single effector pathway: evidence for multiple activation states of a G protein-coupled receptor Mol. Pharmacol. 49 1996 112 122 (Pubitemid 26037325)
    • (1996) Molecular Pharmacology , vol.49 , Issue.1 , pp. 112-122
    • Perez, D.M.1    Hwa, J.2    Gaivin, R.3    Mathur, M.4    Brown, F.5    Graham, R.M.6
  • 285
    • 0026706979 scopus 로고
    • A point mutation of the alpha-2-adrenoceptor that blocks coupling to potassium but not calcium currents
    • A. Surprenant, D.A. Horstman, H. Akbarali, and L.E. Limbird A point mutation of the alpha-2-adrenoceptor that blocks coupling to potassium but not calcium currents Science 257 1992 977 980
    • (1992) Science , vol.257 , pp. 977-980
    • Surprenant, A.1    Horstman, D.A.2    Akbarali, H.3    Limbird, L.E.4
  • 286
    • 0035577682 scopus 로고    scopus 로고
    • s-protein coupling and effector response
    • DOI 10.1016/S0165-6147(00)01864-2, PII S0165614700018642
    • J.P. Kukkonen, J. Näsman, and K.E.O. Åkerman Modelling of promiscuous receptor Gi/Gs-protein coupling and effector response Trends Pharmacol. Sci. 22 2001 616 622 (Pubitemid 33135522)
    • (2001) Trends in Pharmacological Sciences , vol.22 , Issue.12 , pp. 616-622
    • Kukkonen, J.P.1    Nasman, J.2    Akerman, K.E.O.3
  • 287
    • 33646526069 scopus 로고    scopus 로고
    • G-protein-coupled receptor heterodimers: Pharmacology, function and relevance to drug discovery
    • G. Milligan G-protein-coupled receptor heterodimers: pharmacology, function and relevance to drug discovery Drug Discov. Today 11 2006 541 549
    • (2006) Drug Discov. Today , vol.11 , pp. 541-549
    • Milligan, G.1
  • 288
    • 84885385088 scopus 로고    scopus 로고
    • GPCR dimerisation: Molecular basis and relevance for function and pharmacology
    • G. Milligan GPCR dimerisation: molecular basis and relevance for function and pharmacology Fundam. Clin. Pharmacol. 22 2008 18-18
    • (2008) Fundam. Clin. Pharmacol. , vol.22 , pp. 18-18
    • Milligan, G.1
  • 290
    • 73049085563 scopus 로고    scopus 로고
    • The asymmetric/symmetric activation of GPCR dimers as a possible mechanistic rationale for multiple signalling pathways
    • X. Rovira, J.P. Pin, and J. Giraldo The asymmetric/symmetric activation of GPCR dimers as a possible mechanistic rationale for multiple signalling pathways Trends Pharmacol. Sci. 31 2010 15 21
    • (2010) Trends Pharmacol. Sci. , vol.31 , pp. 15-21
    • Rovira, X.1    Pin, J.P.2    Giraldo, J.3
  • 291
    • 65549121608 scopus 로고    scopus 로고
    • Modelling the interdependence between the stoichiometry of receptor oligomerization and ligand binding for a coexisting dimer/tetramer receptor system
    • X. Rovira, M. Vivo, J. Serra, D. Roche, P.G. Strange, and J. Giraldo Modelling the interdependence between the stoichiometry of receptor oligomerization and ligand binding for a coexisting dimer/tetramer receptor system Br. J. Pharmacol. 156 2009 28 35
    • (2009) Br. J. Pharmacol. , vol.156 , pp. 28-35
    • Rovira, X.1    Vivo, M.2    Serra, J.3    Roche, D.4    Strange, P.G.5    Giraldo, J.6
  • 292
    • 84885373526 scopus 로고    scopus 로고
    • Dimerization in G-protein coupled receptors: Correlation analysis and electron density maps of rhodopsin from different species suggest subtype-specific interfaces
    • M. Filizola, W. Guo, J.A. Javitch, and H. Weinstein Dimerization in G-protein coupled receptors: correlation analysis and electron density maps of rhodopsin from different species suggest subtype-specific interfaces Biophys. J. 84 2003 269A 270A
    • (2003) Biophys. J. , vol.84
    • Filizola, M.1    Guo, W.2    Javitch, J.A.3    Weinstein, H.4
  • 293
    • 0346193226 scopus 로고    scopus 로고
    • Using correlated mutation analysis to predict the heterodimerization interface of GPCRs
    • M. Filizola, O. Olmea, and H. Weinstein Using correlated mutation analysis to predict the heterodimerization interface of GPCRs Biophys. J. 82 2002 2307
    • (2002) Biophys. J. , vol.82 , pp. 2307
    • Filizola, M.1    Olmea, O.2    Weinstein, H.3
  • 295
    • 33845720603 scopus 로고    scopus 로고
    • Asymmetric conformational changes in a GPCR dimer controlled by G-proteins
    • DOI 10.1038/sj.emboj.7601449, PII 7601449
    • M. Damian, A. Martin, D. Mesnier, J.P. Pin, and J.L. Baneres Asymmetric conformational changes in a GPCR dimer controlled by G-proteins EMBO J. 25 2006
    • (2006) EMBO Journal , vol.25 , Issue.24 , pp. 5693-5702
    • Damian, M.1    Martin, A.2    Mesnier, D.3    Pin, J.-P.4    Baneres, J.-L.5
  • 297
    • 34447509986 scopus 로고    scopus 로고
    • Transducin activation by nanoscale lipid bilayers containing one and two rhodopsins
    • DOI 10.1074/jbc.M701433200
    • T.H. Bayburt, A.J. Leitz, G.F. Xie, D.D. Oprian, and S.G. Sligar Transducin activation by nanoscale lipid bilayers containing one and two rhodopsins J. Biol. Chem. 282 2007 14875 14881 (Pubitemid 47093370)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.20 , pp. 14875-14881
    • Bayburt, T.H.1    Leitz, A.J.2    Xie, G.3    Oprian, D.D.4    Sligar, S.G.5
  • 301
    • 0037648337 scopus 로고    scopus 로고
    • 4 binding to recombinant BLT1
    • DOI 10.1016/S0022-2836(03)00438-8
    • J.L. Baneres, A. Martin, P. Hullot, J.P. Girard, J.C. Rossi, and J. Parello Structure-based analysis of GPCR function: conformational adaptation of both agonist and receptor upon leukotriene B-4 binding to recombinant BLT1 J. Mol. Biol. 329 2003 801 814 (Pubitemid 36629372)
    • (2003) Journal of Molecular Biology , vol.329 , Issue.4 , pp. 801-814
    • Baneres, J.-L.1    Martin, A.2    Hullot, P.3    Girard, J.-P.4    Rossi, J.-C.5    Parello, J.6
  • 303
    • 0038392702 scopus 로고    scopus 로고
    • 4 receptor BLT1 and the G-protein
    • DOI 10.1016/S0022-2836(03)00439-X
    • J.L. Baneres, and J. Parello Structure-based analysis of GPCR function: evidence for a novel pentameric assembly between the dimeric leukotriene B-4 receptor BLT1 and the G-protein J. Mol. Biol. 329 2003 815 829 (Pubitemid 36629373)
    • (2003) Journal of Molecular Biology , vol.329 , Issue.4 , pp. 815-829
    • Baneres, J.-L.1    Parello, J.2
  • 309
    • 0037426865 scopus 로고    scopus 로고
    • Rhodopsin dimers in native disc membranes
    • DOI 10.1038/421127a
    • D. Fotiadis, Y. Liang, S. Filipek, D.A. Saperstein, A. Engel, and K. Palczewski Atomic-force microscopy: rhodopsin dimers in native disc membranes Nature 421 2003 127 128 (Pubitemid 36090969)
    • (2003) Nature , vol.421 , Issue.6919 , pp. 127-128
    • Fotiadis, D.1    Liang, Y.2    Filipek, S.3    Saperstein, D.A.4    Engel, A.5    Palczewski, K.6
  • 310
    • 1942468189 scopus 로고    scopus 로고
    • The G protein-coupled receptor rhodopsin in the native membrane
    • DOI 10.1016/S0014-5793(04)00194-2, PII S0014579304001942
    • D. Fotiadis, Y. Liang, S. Filipek, D.A. Saperstein, A. Engel, and K. Palczewski The G protein-coupled receptor rhodopsin in the native membrane FEBS Lett. 564 2004 281 288 (Pubitemid 38520934)
    • (2004) FEBS Letters , vol.564 , Issue.3 , pp. 281-288
    • Fotiadis, D.1    Liang, Y.2    Filipek, S.3    Saperstein, D.A.4    Engel, A.5    Palczewski, K.6
  • 313
    • 11144301981 scopus 로고    scopus 로고
    • The supramolecular structure of the GPCR rhodopsin in solution and native disc membranes
    • DOI 10.1080/09687860400020291
    • K. Suda, S. Filipek, K. Palczewski, A. Engel, and D. Fotiadis The supramolecular structure of the GPCR rhodopsin in solution and native disc membranes Mol. Membr. Biol. 21 2004 435 446 (Pubitemid 40030219)
    • (2004) Molecular Membrane Biology , vol.21 , Issue.6 , pp. 435-446
    • Suda, K.1    Filipek, S.2    Palczewski, K.3    Engel, A.4    Fotiadis, D.5
  • 314
    • 25444444202 scopus 로고    scopus 로고
    • Computational modeling approaches to structure-function analysis of G protein-coupled receptors
    • DOI 10.1021/cr000095n
    • F. Fanelli, and P.G. De Benedetti Computational modeling approaches to structure-function analysis of G protein-coupled receptors Chem. Rev. 105 2005 3297 3351 (Pubitemid 41430812)
    • (2005) Chemical Reviews , vol.105 , Issue.9 , pp. 3297-3351
    • Fanelli, F.1    De Benedetti, P.G.2
  • 315
    • 27744531868 scopus 로고    scopus 로고
    • Rhodopsin activation follows precoupling with transducin: Inferences from computational analysis
    • DOI 10.1021/bi051537y
    • F. Fanelli, and D. Dell'Orco Rhodopsin activation follows precoupling with transducin: inferences from computational analysis Biochemistry 44 2005 14695 14700 (Pubitemid 41612248)
    • (2005) Biochemistry , vol.44 , Issue.45 , pp. 14695-14700
    • Fanelli, F.1    Dell'Orco, D.2
  • 317
    • 69949119573 scopus 로고    scopus 로고
    • Lateral diffusion of rhodopsin in photoreceptor membrane: A reappraisal
    • V.I. Govardovskii, D.A. Korenyak, S.A. Shukolyukov, and L.V. Zueva Lateral diffusion of rhodopsin in photoreceptor membrane: a reappraisal Mol. Vis. 15 2009 1717 1729
    • (2009) Mol. Vis. , vol.15 , pp. 1717-1729
    • Govardovskii, V.I.1    Korenyak, D.A.2    Shukolyukov, S.A.3    Zueva, L.V.4
  • 320
    • 0036878162 scopus 로고    scopus 로고
    • Prediction of heterodimerization interfaces of G-protein coupled receptors with a new subtractive correlated mutation method
    • M. Filizola, O. Olmea, and H. Weinstein Prediction of heterodimerization interfaces of G-protein coupled receptors with a new subtractive correlated mutation method Protein Eng. 15 2002 881 885 (Pubitemid 36172725)
    • (2002) Protein Engineering , vol.15 , Issue.11 , pp. 881-885
    • Filizola, M.1    Olmea, O.2    Weinstein, H.3
  • 321
    • 24044480644 scopus 로고    scopus 로고
    • The structure and dynamics of GPCR oligomers: A new focus in models of cell-signaling mechanisms and drug design
    • M. Filizola, and H. Weinstein The structure and dynamics of GPCR oligomers: a new focus in models of cell-signaling mechanisms and drug design Curr. Opin. Drug Discov. Dev. 8 2005 577 584 (Pubitemid 41224120)
    • (2005) Current Opinion in Drug Discovery and Development , vol.8 , Issue.5 , pp. 577-584
    • Filizola, M.1    Weinstein, H.2
  • 322
    • 21344467203 scopus 로고    scopus 로고
    • The study of G-protein coupled receptor oligomerization with computational modeling and bioinformatics
    • DOI 10.1111/j.1742-4658.2005.04730.x
    • M. Filizola, and H. Weinstein The study of G-protein coupled receptor oligomerization with computational modeling and bioinformatics FEBS J. 272 2005 2926 2938 (Pubitemid 40904681)
    • (2005) FEBS Journal , vol.272 , Issue.12 , pp. 2926-2938
    • Filizola, M.1    Weinstein, H.2
  • 323
    • 41149141017 scopus 로고    scopus 로고
    • Influence of oligomerization on the dynamics of G-protein coupled receptors as assessed by normal mode analysis
    • M.F. Masha, and Y. Niv Influence of oligomerization on the dynamics of G-protein coupled receptors as assessed by normal mode analysis Proteins Struct. Funct. Bioinform. 71 2008 575 586
    • (2008) Proteins Struct. Funct. Bioinform. , vol.71 , pp. 575-586
    • Masha, M.F.1    Niv, Y.2
  • 324
    • 84885390005 scopus 로고    scopus 로고
    • Rhodopsin dimers: Molecular dynamics simulations using discrete representations of the membrane and water environment
    • X.S. Wang, M. Filizola, M. Ceruso, and H. Weinstein Rhodopsin dimers: molecular dynamics simulations using discrete representations of the membrane and water environment Biophys. J. 88 2005 81A-81A
    • (2005) Biophys. J. , vol.88
    • Wang, X.S.1    Filizola, M.2    Ceruso, M.3    Weinstein, H.4
  • 325
    • 34347370129 scopus 로고    scopus 로고
    • Dynamic models of G-protein coupled receptor dimers: Indications of asymmetry in the rhodopsin dimer from molecular dynamics simulations in a POPC bilayer
    • DOI 10.1007/s10822-006-9053-3
    • M. Filizola, S.X. Wang, and H. Weinstein Dynamic models of G-protein coupled receptor dimers: indications of asymmetry in the rhodopsin dimer from molecular dynamics simulations in a POPC bilayer J. Comput. Aided Mol. Des. 20 2006 405 416 (Pubitemid 44823879)
    • (2006) Journal of Computer-Aided Molecular Design , vol.20 , Issue.7-8 , pp. 405-416
    • Filizola, M.1    Wang, S.X.2    Weinstein, H.3
  • 326
    • 0036997276 scopus 로고    scopus 로고
    • Structural models for dimerization of G-protein coupled receptors: The opioid receptor homodimers
    • DOI 10.1002/bip.10311
    • M. Filizola, and H. Weinstein Structural models for dimerization of G-protein coupled receptors: the opioid receptor homodimers Biopolymers 66 2002 317 325 (Pubitemid 36222409)
    • (2002) Biopolymers - Peptide Science Section , vol.66 , Issue.5 , pp. 317-325
    • Filizola, M.1    Weinstein, H.2
  • 331
    • 80052027428 scopus 로고    scopus 로고
    • Asymmetry of GPCR oligomers supports their functional relevance
    • P. Maurice, M. Kamal, and R. Jockers Asymmetry of GPCR oligomers supports their functional relevance Trends Pharmacol. Sci. 32 2011 514 520
    • (2011) Trends Pharmacol. Sci. , vol.32 , pp. 514-520
    • Maurice, P.1    Kamal, M.2    Jockers, R.3
  • 332
    • 51049110332 scopus 로고    scopus 로고
    • G protein activation by the leukotriene B-4 receptor dimer - Evidence for an absence of trans-activation
    • M. Damian, S. Mary, A. Martin, J.P. Pin, and J.L. Baneres G protein activation by the leukotriene B-4 receptor dimer - evidence for an absence of trans-activation J. Biol. Chem. 283 2008 21084 21092
    • (2008) J. Biol. Chem. , vol.283 , pp. 21084-21092
    • Damian, M.1    Mary, S.2    Martin, A.3    Pin, J.P.4    Baneres, J.L.5
  • 334
    • 0037013328 scopus 로고    scopus 로고
    • Two defective heterozygous luteinizing hormone receptors can rescue hormone action
    • DOI 10.1074/jbc.M111818200
    • C. Lee, I. Ji, K. Ryu, Y. Song, P.M. Conn, and T.H. Ji Two defective heterozygous luteinizing hormone receptors can rescue hormone action J. Biol. Chem. 277 2002 15795 15800 (Pubitemid 34967856)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.18 , pp. 15795-15800
    • Lee, C.1    Ji, I.2    Ryu, K.3    Song, Y.4    Michael Conn, P.5    Ji, T.H.6
  • 335
  • 336
    • 84861165939 scopus 로고    scopus 로고
    • Ligand-dependent conformations and dynamics of the serotonin 5-HT2A receptor determine its activation and membrane-driven oligomerization properties
    • J. Shan, G. Khelashvili, S. Mondal, E.L. Mehler, and H. Weinstein Ligand-dependent conformations and dynamics of the serotonin 5-HT2A receptor determine its activation and membrane-driven oligomerization properties PLoS Comput. Biol. 8 2012 e1002473
    • (2012) PLoS Comput. Biol. , vol.8 , pp. 1002473
    • Shan, J.1    Khelashvili, G.2    Mondal, S.3    Mehler, E.L.4    Weinstein, H.5
  • 337
    • 77957240736 scopus 로고    scopus 로고
    • Regulators of g protein signaling proteins as targets for drug discovery
    • B. Sjogren, L.L. Blazer, and R.R. Neubig Regulators of g protein signaling proteins as targets for drug discovery Prog. Mol. Biol. Transl. Sci. 91 2010 81 119
    • (2010) Prog. Mol. Biol. Transl. Sci. , vol.91 , pp. 81-119
    • Sjogren, B.1    Blazer, L.L.2    Neubig, R.R.3
  • 339
    • 17144381258 scopus 로고    scopus 로고
    • Regulators of G-protein signaling form a quaternary complex with the agonist, receptor, and G-protein: A novel explanation for the acceleration of signaling activation kinetics
    • DOI 10.1074/jbc.M410163200
    • A. Benians, M. Nobles, S. Hosny, and A. Tinker Regulators of G-protein signaling form a quaternary complex with the agonist, receptor, and G-protein: a novel explanation for the acceleration of signaling activation kinetics J. Biol. Chem. 280 2005 13383 13394 (Pubitemid 40517225)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.14 , pp. 13383-13394
    • Benians, A.1    Nobles, M.2    Hosny, S.3    Tinker, A.4
  • 340
    • 22844433094 scopus 로고    scopus 로고
    • 1A-adrenergic receptor signaling by RGS2 association with the receptor third intracellular loop
    • DOI 10.1074/jbc.M502365200
    • C. Hague, L.S. Bernstein, S. Ramineni, Z. Chen, K.P. Minneman, and J.R. Hepler Selective inhibition of α1A-adrenergic receptor signaling by RGS2 association with the receptor third intracellular loop J. Biol. Chem. 280 2005 27289 27295 (Pubitemid 41040769)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.29 , pp. 27289-27295
    • Hague, C.1    Bernstein, L.S.2    Ramineni, S.3    Chen, Z.4    Minneman, K.P.5    Hepler, J.R.6
  • 341
    • 30944451158 scopus 로고    scopus 로고
    • RGS proteins have a signalling complex: Interactions between RGS proteins and GPCRs, effectors, and auxiliary proteins
    • DOI 10.1016/j.cellsig.2005.08.010, PII S0898656805002305
    • M. Abramow-Newerly, A.A. Roy, C. Nunn, and P. Chidiac RGS proteins have a signalling complex: interactions between RGS proteins and GPCRs, effectors, and auxiliary proteins Cell. Signal. 18 2006 579 591 (Pubitemid 43113289)
    • (2006) Cellular Signalling , vol.18 , Issue.5 , pp. 579-591
    • Abramow-Newerly, M.1    Roy, A.A.2    Nunn, C.3    Chidiac, P.4
  • 343
    • 33747124339 scopus 로고    scopus 로고
    • Rhodopsin-interacting surface of the transducin γ subunit
    • DOI 10.1021/bi060806x
    • O.G. Kisselev, and M.A. Downs Rhodopsin-interacting surface of the transducin gamma subunit Biochemistry 45 2006 9386 9392 (Pubitemid 44223243)
    • (2006) Biochemistry , vol.45 , Issue.31 , pp. 9386-9392
    • Kisselev, O.G.1    Downs, M.A.2


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