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Volumn 50, Issue 1, 2007, Pages 109-118

Regulation of G proteins by human 5-HT1a receptor TM3/i2 and TM5/i3 loop peptides

Author keywords

5HT1a receptor; 35S S GTP; Cyclic AMP; G proteins; Serotonin; Synthetic peptides

Indexed keywords

CYCLIC AMP; FORSKOLIN; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATE; SEROTONIN 1A RECEPTOR; SYNTHETIC PEPTIDE;

EID: 33845297955     PISSN: 01970186     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuint.2006.07.017     Document Type: Article
Times cited : (10)

References (69)
  • 1
    • 0035650717 scopus 로고    scopus 로고
    • Receptor signaling and structure: insights from serotonin-1 receptors
    • Albert P.R., and Tiberi M. Receptor signaling and structure: insights from serotonin-1 receptors. Trends Endocrinol. Metab. 12 10 (2002) 453-460
    • (2002) Trends Endocrinol. Metab. , vol.12 , Issue.10 , pp. 453-460
    • Albert, P.R.1    Tiberi, M.2
  • 2
    • 0028227013 scopus 로고
    • Structure and function of receptors coupled to G proteins
    • Baldwin J.M. Structure and function of receptors coupled to G proteins. Curr. Opin. Cell. Biol. 6 (1994) 180-190
    • (1994) Curr. Opin. Cell. Biol. , vol.6 , pp. 180-190
    • Baldwin, J.M.1
  • 3
    • 0032970989 scopus 로고    scopus 로고
    • A review of central 5-HT receptors and their functions
    • Barnes N.M., and Sharp T. A review of central 5-HT receptors and their functions. Neuropharmacology 38 8 (1999) 1083-1152
    • (1999) Neuropharmacology , vol.38 , Issue.8 , pp. 1083-1152
    • Barnes, N.M.1    Sharp, T.2
  • 4
    • 0032581639 scopus 로고    scopus 로고
    • G-protein coupled receptors: models, mutagenesis, and drug design
    • Bikker J.A., Trumpp-Kallmeyer S., and Humblet C. G-protein coupled receptors: models, mutagenesis, and drug design. J. Med. Chem. 41 (1998) 2911-2927
    • (1998) J. Med. Chem. , vol.41 , pp. 2911-2927
    • Bikker, J.A.1    Trumpp-Kallmeyer, S.2    Humblet, C.3
  • 5
    • 0017184389 scopus 로고
    • A rapid sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0030041761 scopus 로고    scopus 로고
    • Amino acid side chains that define muscarinic receptor/G protein coupling
    • Burstein E.S., Spalding T.A., and Braun M.R. Amino acid side chains that define muscarinic receptor/G protein coupling. J. Biol. Chem. 271 (1996) 2882-2885
    • (1996) J. Biol. Chem. , vol.271 , pp. 2882-2885
    • Burstein, E.S.1    Spalding, T.A.2    Braun, M.R.3
  • 7
    • 20344370764 scopus 로고    scopus 로고
    • Allosteric mechanisms of signal transduction
    • Changeux J.-P., and Edelstein S.J. Allosteric mechanisms of signal transduction. Science 308 (2005) 1424-1428
    • (2005) Science , vol.308 , pp. 1424-1428
    • Changeux, J.-P.1    Edelstein, S.J.2
  • 8
    • 0037133525 scopus 로고    scopus 로고
    • NMR structure of the second intracellular loop of the alpha 2a adrenergic receptor: evidence for a novel cytoplasmic helix
    • Chung D.A., Quiderweg E.R.P., Fowler C.B., Soyer O.S., Mosberg H.I., and Neubig R.R. NMR structure of the second intracellular loop of the alpha 2a adrenergic receptor: evidence for a novel cytoplasmic helix. Biochemistry 41 11 (2002) 3596-3604
    • (2002) Biochemistry , vol.41 , Issue.11 , pp. 3596-3604
    • Chung, D.A.1    Quiderweg, E.R.P.2    Fowler, C.B.3    Soyer, O.S.4    Mosberg, H.I.5    Neubig, R.R.6
  • 9
    • 0033827660 scopus 로고    scopus 로고
    • Psychopharmacology of 5-HT1a receptors
    • Cowen P.J. Psychopharmacology of 5-HT1a receptors. Nucl. Med. Biol. 27 (2000) 437-439
    • (2000) Nucl. Med. Biol. , vol.27 , pp. 437-439
    • Cowen, P.J.1
  • 10
    • 0025817671 scopus 로고
    • Two peptides from the alpha2A-adrenergic receptor alter receptor G protein coupling by distinct mechanisms
    • Dalman H.M., and Neubig R.R. Two peptides from the alpha2A-adrenergic receptor alter receptor G protein coupling by distinct mechanisms. J. Biol. Chem. 266 (1991) 11025-11029
    • (1991) J. Biol. Chem. , vol.266 , pp. 11025-11029
    • Dalman, H.M.1    Neubig, R.R.2
  • 11
  • 12
    • 0033522903 scopus 로고    scopus 로고
    • Role for the third intracellular loop in cell surface stabilization of the alpha2A-adrenergic receptor
    • Edwards S.W., and Limbird L.E. Role for the third intracellular loop in cell surface stabilization of the alpha2A-adrenergic receptor. J. Biol. Chem. 274 (1999) 16331-16336
    • (1999) J. Biol. Chem. , vol.274 , pp. 16331-16336
    • Edwards, S.W.1    Limbird, L.E.2
  • 13
    • 33645751457 scopus 로고    scopus 로고
    • Glucocortocoid receptor-dependent desensitization of 5-HT1A autoreceptors by sleep deprivation: studies in GR-i transgenic mice
    • Evrard A., Barden N., Hamon M., and Adrien J. Glucocortocoid receptor-dependent desensitization of 5-HT1A autoreceptors by sleep deprivation: studies in GR-i transgenic mice. Sleep 29 1 (2006) 31-36
    • (2006) Sleep , vol.29 , Issue.1 , pp. 31-36
    • Evrard, A.1    Barden, N.2    Hamon, M.3    Adrien, J.4
  • 14
    • 0023786564 scopus 로고
    • The genomic clone G-21 which resembles a beta-adrenergic receptor sequence encodes the 5-HT1a receptor
    • Fargin A., Raymond J.R., Lohse M.J., Kobilka B.K., Caron M.G., and Lefkowitz R.J. The genomic clone G-21 which resembles a beta-adrenergic receptor sequence encodes the 5-HT1a receptor. Nature 335 (1988) 358-360
    • (1988) Nature , vol.335 , pp. 358-360
    • Fargin, A.1    Raymond, J.R.2    Lohse, M.J.3    Kobilka, B.K.4    Caron, M.G.5    Lefkowitz, R.J.6
  • 15
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • Farrens D.L., Altenbach C., Yang K., Hubbell W.L., and Khorana H.B. Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science 274 (1996) 768-770
    • (1996) Science , vol.274 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.B.5
  • 16
    • 0029128961 scopus 로고
    • Agonist-induced desensitization and phosphorylation of human 5-HT1a receptor expressed in Sf9 cells
    • Gettys T.W., and Raymond J.R. Agonist-induced desensitization and phosphorylation of human 5-HT1a receptor expressed in Sf9 cells. Biochemistry 34 (1995) 11954-11962
    • (1995) Biochemistry , vol.34 , pp. 11954-11962
    • Gettys, T.W.1    Raymond, J.R.2
  • 17
    • 5644248562 scopus 로고    scopus 로고
    • GABAA-5-HT1A receptor interaction in the mediobasal hypothalamus
    • Guptarak J., Selvamani A., and Uphouse L. GABAA-5-HT1A receptor interaction in the mediobasal hypothalamus. Brain Res. 1027 1-2 (2004) 144-150
    • (2004) Brain Res. , vol.1027 , Issue.1-2 , pp. 144-150
    • Guptarak, J.1    Selvamani, A.2    Uphouse, L.3
  • 18
    • 0035942220 scopus 로고    scopus 로고
    • How activated receptors couple to G proteins
    • Hamm H.E. How activated receptors couple to G proteins. Proc. Natl. Acad. Sci. 98 9 (2001) 4819-4821
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , Issue.9 , pp. 4819-4821
    • Hamm, H.E.1
  • 19
    • 0032469383 scopus 로고    scopus 로고
    • A bioactive peptide from the transmembrane 5-intracellular loop 3 region of the human 5HT1a receptor
    • Hayataka K., O'Connor M.F., Kinzler N., Weber J.T., and Parker K.K. A bioactive peptide from the transmembrane 5-intracellular loop 3 region of the human 5HT1a receptor. Biochem. Cell Biol. 76 (1998) 657-660
    • (1998) Biochem. Cell Biol. , vol.76 , pp. 657-660
    • Hayataka, K.1    O'Connor, M.F.2    Kinzler, N.3    Weber, J.T.4    Parker, K.K.5
  • 20
    • 0037469488 scopus 로고    scopus 로고
    • Regulation of 5-HT1a receptor function in brain following agonist or antidepressant administration
    • Hensler J.G. Regulation of 5-HT1a receptor function in brain following agonist or antidepressant administration. Life Sci. 72 15 (2003) 1665-1682
    • (2003) Life Sci. , vol.72 , Issue.15 , pp. 1665-1682
    • Hensler, J.G.1
  • 21
    • 0037418227 scopus 로고    scopus 로고
    • A global representation of the protein fold space
    • Hou J., Sims G.E., Zhang C., and Kim S.-H. A global representation of the protein fold space. Proc. Natl. Acad. Sci. 100 5 (2003) 2386-2390
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , Issue.5 , pp. 2386-2390
    • Hou, J.1    Sims, G.E.2    Zhang, C.3    Kim, S.-H.4
  • 23
    • 3142660328 scopus 로고    scopus 로고
    • In vitro selection of state-specific peptide modulators of G protein signaling using mRNA display
    • Ja W.W., and Roberts R.W. In vitro selection of state-specific peptide modulators of G protein signaling using mRNA display. Biochemistry 43 (2004) 9265-9275
    • (2004) Biochemistry , vol.43 , pp. 9265-9275
    • Ja, W.W.1    Roberts, R.W.2
  • 24
    • 29244489032 scopus 로고    scopus 로고
    • Firing of 5-HT neurons in the dorsal and median raphe nucleus in vitro shows differential alpha1-adrenoceptor and 5-HT1A receptor modulation
    • Judge S.J., and Gartside S.E. Firing of 5-HT neurons in the dorsal and median raphe nucleus in vitro shows differential alpha1-adrenoceptor and 5-HT1A receptor modulation. Neurochem. Int. 48 2 (2006) 100-107
    • (2006) Neurochem. Int. , vol.48 , Issue.2 , pp. 100-107
    • Judge, S.J.1    Gartside, S.E.2
  • 25
    • 0037448057 scopus 로고    scopus 로고
    • Additive neuroprotective effect of Ketanserin and Ipsapirone on the hippocampal damage after transient forebrain ischemia in the Mongolian gerbil
    • Klisch J., Bode-Greuel K.M., Horvath E., Klisch C., and Els T. Additive neuroprotective effect of Ketanserin and Ipsapirone on the hippocampal damage after transient forebrain ischemia in the Mongolian gerbil. Neurosci. Lett. 342 1-2 (2003) 25-28
    • (2003) Neurosci. Lett. , vol.342 , Issue.1-2 , pp. 25-28
    • Klisch, J.1    Bode-Greuel, K.M.2    Horvath, E.3    Klisch, C.4    Els, T.5
  • 26
    • 0023643263 scopus 로고
    • An intronless gene encoding a potential member of the family of receptors coupled to guanine nucleotide regulatory proteins
    • Kobilka B.K., Frielle T., Collins S., Yang-Feng T., Kobilka T.S., Francke U., Lefkowitz R.J., and Caron M.G. An intronless gene encoding a potential member of the family of receptors coupled to guanine nucleotide regulatory proteins. Nature 329 (1987) 75-79
    • (1987) Nature , vol.329 , pp. 75-79
    • Kobilka, B.K.1    Frielle, T.2    Collins, S.3    Yang-Feng, T.4    Kobilka, T.S.5    Francke, U.6    Lefkowitz, R.J.7    Caron, M.G.8
  • 27
    • 33645831353 scopus 로고    scopus 로고
    • Molecular determinants in the second intracellular loop of the 5-hydroxytryptamine-1A receptor for G-protein coupling
    • Kushwaha N., Harwood S.C., Wilson A.M., Berger M., Tecott L.H., Roth B.L., and Albert P.R. 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
    • Kushwaha, N.1    Harwood, S.C.2    Wilson, A.M.3    Berger, M.4    Tecott, L.H.5    Roth, B.L.6    Albert, P.R.7
  • 28
    • 0030806979 scopus 로고    scopus 로고
    • A conserved threonine residue in the second intracellular loop of the 5-hydroxytryptamine 1A receptor directs signaling specificity
    • Lembo P.M., Ghahremani M.H., Morris S.J., and Albert P.R. A conserved threonine residue in the second intracellular loop of the 5-hydroxytryptamine 1A receptor directs signaling specificity. Mol. Pharmacol. 52 (1997) 164-171
    • (1997) Mol. Pharmacol. , vol.52 , pp. 164-171
    • Lembo, P.M.1    Ghahremani, M.H.2    Morris, S.J.3    Albert, P.R.4
  • 29
    • 0017280145 scopus 로고
    • An agonist-specific effect of guanine nucleotides on binding to the beta adrenergic receptor
    • Maguire M.E., VanArsdale P.M., and Gilman A.G. An agonist-specific effect of guanine nucleotides on binding to the beta adrenergic receptor. Mol. Pharmacol. 12 (1976) 335-339
    • (1976) Mol. Pharmacol. , vol.12 , pp. 335-339
    • Maguire, M.E.1    VanArsdale, P.M.2    Gilman, A.G.3
  • 30
    • 0014897881 scopus 로고
    • Chemical synthesis of peptides and proteins
    • Marglin A., and Merrifield R.B. Chemical synthesis of peptides and proteins. Annu. Rev. Biochem. 39 (1970) 841-866
    • (1970) Annu. Rev. Biochem. , vol.39 , pp. 841-866
    • Marglin, A.1    Merrifield, R.B.2
  • 31
    • 0035398487 scopus 로고    scopus 로고
    • G-protein-coupled receptors and signaling networks: emerging paradigms
    • Marinissen M.J., and Gutkind J.S. G-protein-coupled receptors and signaling networks: emerging paradigms. Trends Pharm. Sci. 22 (2001) 368-376
    • (2001) Trends Pharm. Sci. , vol.22 , pp. 368-376
    • Marinissen, M.J.1    Gutkind, J.S.2
  • 32
    • 0033547819 scopus 로고    scopus 로고
    • Assembly of G protein-coupled receptors from fragments: identification of functional receptors with discontinuities in each of the loops connecting transmembrane segments
    • Martin N.P., Leavitt L.M., Sommers C.M., and Dumont M.E. Assembly of G protein-coupled receptors from fragments: identification of functional receptors with discontinuities in each of the loops connecting transmembrane segments. Biochemistry 38 (1999) 682-695
    • (1999) Biochemistry , vol.38 , pp. 682-695
    • Martin, N.P.1    Leavitt, L.M.2    Sommers, C.M.3    Dumont, M.E.4
  • 34
    • 0035498937 scopus 로고    scopus 로고
    • Receptor activation: what does the rhodopsin structure tell us?
    • Meng E.C., and Bourne H.R. Receptor activation: what does the rhodopsin structure tell us?. Trends Pharm. Sci. 22 11 (2001) 587-593
    • (2001) Trends Pharm. Sci. , vol.22 , Issue.11 , pp. 587-593
    • Meng, E.C.1    Bourne, H.R.2
  • 35
    • 0029955446 scopus 로고    scopus 로고
    • Identification of the critical domains of the sigma-opioid receptor involved in G protein coupling using site-specific synthetic peptides
    • Merkouris M., Dragatsis I., Megaritis G., Konidakis G., Zioudrou C., Milligan G., and Georgoussi Z. Identification of the critical domains of the sigma-opioid receptor involved in G protein coupling using site-specific synthetic peptides. Mol. Pharmacol. 50 (1996) 985-993
    • (1996) Mol. Pharmacol. , vol.50 , pp. 985-993
    • Merkouris, M.1    Dragatsis, I.2    Megaritis, G.3    Konidakis, G.4    Zioudrou, C.5    Milligan, G.6    Georgoussi, Z.7
  • 36
    • 0025882303 scopus 로고
    • Multisite contacts involved in coupling of the beta-adrenergic receptor with the stimulatory guanine-nucleotide-binding protein
    • Munch G., Dees C., Hekman M., and Palm D. Multisite contacts involved in coupling of the beta-adrenergic receptor with the stimulatory guanine-nucleotide-binding protein. Eur. J. Biochem. 198 (1991) 357-364
    • (1991) Eur. J. Biochem. , vol.198 , pp. 357-364
    • Munch, G.1    Dees, C.2    Hekman, M.3    Palm, D.4
  • 38
    • 0023667072 scopus 로고
    • [3H]Spiroxatrine labels a serotonin1a-like site in the rat hippocampus
    • Nelson D.L., Monroe P.J., Lambert G., and Yamamura H.I. [3H]Spiroxatrine labels a serotonin1a-like site in the rat hippocampus. Life Sci. 41 (1987) 1567-1576
    • (1987) Life Sci. , vol.41 , pp. 1567-1576
    • Nelson, D.L.1    Monroe, P.J.2    Lambert, G.3    Yamamura, H.I.4
  • 39
    • 0028947674 scopus 로고
    • The third intracellular loop of the 5-hydroxytryptamine2a receptor determines effector coupling specificity
    • Oksenberg G., Havlik S., Peroutka S.J., and Ashkenazi A. The third intracellular loop of the 5-hydroxytryptamine2a receptor determines effector coupling specificity. J. Neurochem. 64 (1995) 1440-1447
    • (1995) J. Neurochem. , vol.64 , pp. 1440-1447
    • Oksenberg, G.1    Havlik, S.2    Peroutka, S.J.3    Ashkenazi, A.4
  • 40
    • 0030614427 scopus 로고    scopus 로고
    • Receptor and betagamma binding sites in the alpha subunit of the retinal G protein transducin
    • Onrust R., Herzmark P., Chi P., Garcia P.D., Lichtarge O., Kingsley C., and Bourne H.R. Receptor and betagamma binding sites in the alpha subunit of the retinal G protein transducin. Science 275 (1997) 381-384
    • (1997) Science , vol.275 , 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
  • 41
    • 33845302681 scopus 로고    scopus 로고
    • Coupling and G protein activating characteristics of a human 5HT1a receptor i2 loop peptide
    • Ortiz T.C., Devereaux M.C., and Parker K.K. Coupling and G protein activating characteristics of a human 5HT1a receptor i2 loop peptide. Soc. Neurosci. Abstr. 25 (1999) 1466
    • (1999) Soc. Neurosci. Abstr. , vol.25 , pp. 1466
    • Ortiz, T.C.1    Devereaux, M.C.2    Parker, K.K.3
  • 42
    • 0034109965 scopus 로고    scopus 로고
    • Structural variants of a human 5-HT1a receptor intracellular loop 3 peptide
    • Ortiz T.C., Devereaux M.C., and Parker K.K. Structural variants of a human 5-HT1a receptor intracellular loop 3 peptide. Pharmacology 60 (2000) 195-202
    • (2000) Pharmacology , vol.60 , pp. 195-202
    • Ortiz, T.C.1    Devereaux, M.C.2    Parker, K.K.3
  • 44
    • 0008510614 scopus 로고
    • Mapping G protein coupling domains by site-specific peptides
    • Palm D., Munch G., and Malek D. Mapping G protein coupling domains by site-specific peptides. Meth. Neurosci. 25 (1995) 302-321
    • (1995) Meth. Neurosci. , vol.25 , pp. 302-321
    • Palm, D.1    Munch, G.2    Malek, D.3
  • 45
    • 0034672622 scopus 로고    scopus 로고
    • Diverse signaling by 5-hydroxytryptamine (5HT) receptors
    • Pauwels P.J. Diverse signaling by 5-hydroxytryptamine (5HT) receptors. Biochem. Pharmacol. 60 (2000) 1743-1750
    • (2000) Biochem. Pharmacol. , vol.60 , pp. 1743-1750
    • Pauwels, P.J.1
  • 46
    • 0018583162 scopus 로고
    • Serotonin receptor binding sites affected differentially by guanine nucleotides
    • Peroutka S.J., Lebovitz R.M., and Snyder S.H. Serotonin receptor binding sites affected differentially by guanine nucleotides. Mol. Pharmacol. 16 (1979) 700-708
    • (1979) Mol. Pharmacol. , vol.16 , pp. 700-708
    • Peroutka, S.J.1    Lebovitz, R.M.2    Snyder, S.H.3
  • 47
    • 9644289344 scopus 로고    scopus 로고
    • The 5HT1a receptor agonist, 8-OH-DPAT, protects neurons and reduces astroglial reaction after ischemic damage caused by cortical devascularization
    • Ramos A.J., Rubio M.D., Defagot C., Hirschberg L., Villar M.J., and Brusco A. The 5HT1a receptor agonist, 8-OH-DPAT, protects neurons and reduces astroglial reaction after ischemic damage caused by cortical devascularization. Brain Res. 1030 (2004) 201-220
    • (2004) Brain Res. , vol.1030 , pp. 201-220
    • Ramos, A.J.1    Rubio, M.D.2    Defagot, C.3    Hirschberg, L.4    Villar, M.J.5    Brusco, A.6
  • 49
    • 0032588147 scopus 로고    scopus 로고
    • The recombinant 5-HT1a receptor: G protein coupling and signaling pathways
    • Raymond J.R., Mukhin Y.V., Gettys T.W., and Garnovskaya M.N. The recombinant 5-HT1a receptor: G protein coupling and signaling pathways. Br. J. Pharmacol. 127 (1999) 1751-1764
    • (1999) Br. J. Pharmacol. , vol.127 , pp. 1751-1764
    • Raymond, J.R.1    Mukhin, Y.V.2    Gettys, T.W.3    Garnovskaya, M.N.4
  • 50
    • 0027522086 scopus 로고
    • Cell-specific physical and functional coupling of human 5-HT1a receptors to inhibitory G protein alpha-subunits and lack of coupling to Gsalpha
    • Raymond J.R., Olsen C.L., and Gettys T.W. Cell-specific physical and functional coupling of human 5-HT1a receptors to inhibitory G protein alpha-subunits and lack of coupling to Gsalpha. Biochemistry 32 (1993) 11064-11073
    • (1993) Biochemistry , vol.32 , pp. 11064-11073
    • Raymond, J.R.1    Olsen, C.L.2    Gettys, T.W.3
  • 51
    • 0028018966 scopus 로고
    • Cloning and characterization of a mammalian melatonin receptor that mediates reproduction and circadian responses
    • Reppert S.M., Weaver D.R., and Ebisawa T. Cloning and characterization of a mammalian melatonin receptor that mediates reproduction and circadian responses. Neuron 13 (1994) 1177-1185
    • (1994) Neuron , vol.13 , pp. 1177-1185
    • Reppert, S.M.1    Weaver, D.R.2    Ebisawa, T.3
  • 52
    • 0036532207 scopus 로고    scopus 로고
    • Structure of rhodopsin and the super family of seven-helical receptors: the same and not the same
    • Sakmar T.P. Structure of rhodopsin and the super family of seven-helical receptors: the same and not the same. Curr. Opin. Cell Biol. 14 (2002) 189-195
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 189-195
    • Sakmar, T.P.1
  • 53
    • 0026548156 scopus 로고
    • In vitro mutagenesis and the search for structure-function relationships among G protein-coupled receptors
    • Savarese T.M., and Fraser C.M. In vitro mutagenesis and the search for structure-function relationships among G protein-coupled receptors. Biochem. J. 283 (1992) 1-19
    • (1992) Biochem. J. , vol.283 , pp. 1-19
    • Savarese, T.M.1    Fraser, C.M.2
  • 54
    • 3142585284 scopus 로고    scopus 로고
    • Controlling the location and activation of Rab GTPases
    • Seabra M.C., and Wasmeier C. Controlling the location and activation of Rab GTPases. Curr. Opin. Cell Biol. 16 (2004) 451-457
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 451-457
    • Seabra, M.C.1    Wasmeier, C.2
  • 55
    • 0141890725 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the ligand-induced chemical information transfer in the 5-HT1A receptor
    • Seeber M., De Benedetti P.G., and Fanelli F. Molecular dynamics simulations of the ligand-induced chemical information transfer in the 5-HT1A receptor. J. Chem. Inf. Comput. Sci. 43 (2003) 1520-1531
    • (2003) J. Chem. Inf. Comput. Sci. , vol.43 , pp. 1520-1531
    • Seeber, M.1    De Benedetti, P.G.2    Fanelli, F.3
  • 56
    • 0037192858 scopus 로고    scopus 로고
    • Evidence for a model of agonist-induced activation of 5-hydroxytryptamine 2a serotonin receptors that involves the disruption of a strong ionic interaction between helices 3 and 6
    • Shapiro D.A., Kristiansen K., Weiner D.M., Kroeze W.K., and Roth B.L. Evidence for a model of agonist-induced activation of 5-hydroxytryptamine 2a serotonin receptors that involves the disruption of a strong ionic interaction between helices 3 and 6. J. Biol. Chem. 277 13 (2002) 11441-11449
    • (2002) J. Biol. Chem. , vol.277 , Issue.13 , pp. 11441-11449
    • Shapiro, D.A.1    Kristiansen, K.2    Weiner, D.M.3    Kroeze, W.K.4    Roth, B.L.5
  • 58
    • 0035800032 scopus 로고    scopus 로고
    • Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCR's)
    • Teller D.C., Okada T., Behnke C.A., Palczewski K., and Stenkamp R.E. Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCR's). Biochemistry 40 26 (2001) 7761-7772
    • (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
  • 59
    • 28844463975 scopus 로고    scopus 로고
    • Snapshot of activated G proteins at the membrane: the Galphaq-GRK2-Gbetagamma complex
    • Tesmer V.M., Kawano T., Shankaranarayanan A., Kozasa T., and Tesmer J.J.G. Snapshot of activated G proteins at the membrane: the Galphaq-GRK2-Gbetagamma complex. Science 310 (2005) 1686-1690
    • (2005) Science , vol.310 , pp. 1686-1690
    • Tesmer, V.M.1    Kawano, T.2    Shankaranarayanan, A.3    Kozasa, T.4    Tesmer, J.J.G.5
  • 60
    • 0037187331 scopus 로고    scopus 로고
    • Structural determinants in the second intracellular loop of the human follicle-stimulating hormone receptor are involved in G (s) protein activation
    • Timossi C., Maldonado D., Vizcaino A., Lindau-Shepard B., Conn P.M., and Ulloa-Aguirre A. Structural determinants in the second intracellular loop of the human follicle-stimulating hormone receptor are involved in G (s) protein activation. Mol. Cell. Endocrinol. 189 1-2 (2002) 157-168
    • (2002) Mol. Cell. Endocrinol. , vol.189 , Issue.1-2 , pp. 157-168
    • Timossi, C.1    Maldonado, D.2    Vizcaino, A.3    Lindau-Shepard, B.4    Conn, P.M.5    Ulloa-Aguirre, A.6
  • 62
    • 33044502647 scopus 로고    scopus 로고
    • G protein coupling and activation characteristics of intracellular loops 2 and 3 of the 5HT1a receptor
    • Thiagaraj H.V., Ortiz T.C., Burnett A., and Parker K.K. G protein coupling and activation characteristics of intracellular loops 2 and 3 of the 5HT1a receptor. Trends Comp. Biochem. Physiol. 9 (2002) 117-129
    • (2002) Trends Comp. Biochem. Physiol. , vol.9 , pp. 117-129
    • Thiagaraj, H.V.1    Ortiz, T.C.2    Burnett, A.3    Parker, K.K.4
  • 63
    • 0031978266 scopus 로고    scopus 로고
    • Cotransfection of second and third intracellular loop fragments inhibit angiotensin AT1a receptor activation of phospholipase C in HEK-293 cells
    • Thompson J.B., Wade S.M., Harrison J.K., Salafranca M.N., and Neubig R.R. Cotransfection of second and third intracellular loop fragments inhibit angiotensin AT1a receptor activation of phospholipase C in HEK-293 cells. J. Pharm. Exp. Ther. 285 (1998) 216-222
    • (1998) J. Pharm. Exp. Ther. , vol.285 , pp. 216-222
    • Thompson, J.B.1    Wade, S.M.2    Harrison, J.K.3    Salafranca, M.N.4    Neubig, R.R.5
  • 64
    • 2342425115 scopus 로고    scopus 로고
    • Calmodulin interacts with the third intracellular loop of the serotonin 5-hydroxytryptamine1A receptor at two distinct sites: putative role in receptor phosphorylation by protein kinase C
    • Turner J.H., Gelasco A.K., and Raymond J.R. Calmodulin interacts with the third intracellular loop of the serotonin 5-hydroxytryptamine1A receptor at two distinct sites: putative role in receptor phosphorylation by protein kinase C. J. Biol. Chem. 279 17 (2004) 17027-17037
    • (2004) J. Biol. Chem. , vol.279 , Issue.17 , pp. 17027-17037
    • Turner, J.H.1    Gelasco, A.K.2    Raymond, J.R.3
  • 65
    • 0028775602 scopus 로고
    • 5-Hydroxytryptamine1a receptor synthetic peptides: mechanisms of adenylyl cyclase inhibition
    • Varrault A., Nguyen D.L., Mcclue S., Harris B., Jouin P., and Bockaert J. 5-Hydroxytryptamine1a receptor synthetic peptides: mechanisms of adenylyl cyclase inhibition. J. Biol. Chem. 269 (1994) 16720-16725
    • (1994) J. Biol. Chem. , vol.269 , pp. 16720-16725
    • Varrault, A.1    Nguyen, D.L.2    Mcclue, S.3    Harris, B.4    Jouin, P.5    Bockaert, J.6
  • 66
    • 0034787251 scopus 로고    scopus 로고
    • Three-dimensional representations of G protein-coupled receptor structures and mechanisms
    • Visiers I., Balleteros J.A., and Weinstein H. Three-dimensional representations of G protein-coupled receptor structures and mechanisms. Meth. Enzymol. 343 (2002) 329-371
    • (2002) Meth. Enzymol. , vol.343 , pp. 329-371
    • Visiers, I.1    Balleteros, J.A.2    Weinstein, H.3
  • 67
    • 27844511015 scopus 로고    scopus 로고
    • A key serine for the GTPase-activating protein function of regulator of G protein signaling proteins is not a general target for 14-3-3 interactions
    • Ward R.J., and Milligan G. A key serine for the GTPase-activating protein function of regulator of G protein signaling proteins is not a general target for 14-3-3 interactions. Mol. Pharmacol. 68 (2005) 1821-1830
    • (2005) Mol. Pharmacol. , vol.68 , pp. 1821-1830
    • Ward, R.J.1    Milligan, G.2
  • 69
    • 0028314995 scopus 로고
    • Measurement of receptor-stimulated guanosine S′-O-(gamma-thiophosphate) binding by G protein
    • Wieland T., and Jacobs K.H. Measurement of receptor-stimulated guanosine S′-O-(gamma-thiophosphate) binding by G protein. Meth. Enzymol. 217 (1994) 3-27
    • (1994) Meth. Enzymol. , vol.217 , pp. 3-27
    • Wieland, T.1    Jacobs, K.H.2


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