메뉴 건너뛰기




Volumn 29, Issue 3, 2008, Pages 159-165

Optical techniques to analyze real-time activation and signaling of G-protein-coupled receptors

Author keywords

[No Author keywords available]

Indexed keywords

BETA ARRESTIN; CYAN FLUORESCENT PROTEIN; G PROTEIN COUPLED RECEPTOR; G PROTEIN COUPLED RECEPTOR KINASE; GREEN FLUORESCENT PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; PROTEIN SUBUNIT; YELLOW FLUORESCENT PROTEIN;

EID: 39949085589     PISSN: 01656147     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tips.2007.12.002     Document Type: Review
Times cited : (116)

References (76)
  • 1
    • 0036201254 scopus 로고    scopus 로고
    • G proteins and phototransduction
    • V.Y. Arshavsky G proteins and phototransduction Annu. Rev. Physiol. 64 2002 153 187
    • (2002) Annu. Rev. Physiol. , vol.64 , pp. 153-187
    • Arshavsky, V.Y.1
  • 2
    • 33846014320 scopus 로고    scopus 로고
    • Fluorometric measurements of intermolecular distances between the α- and β-subunits of the Na+/K+-ATPase
    • +-ATPase J. Biol. Chem. 281 2006 36338 36346
    • (2006) J. Biol. Chem. , vol.281 , pp. 36338-36346
    • Dempski, R.E.1
  • 3
    • 34447633368 scopus 로고    scopus 로고
    • Conformational complexity of G-protein-coupled receptors
    • B.K. Kobilka X. Deupi Conformational complexity of G-protein-coupled receptors Trends Pharmacol. Sci. 28 2007 397 406
    • (2007) Trends Pharmacol. Sci. , vol.28 , pp. 397-406
    • Kobilka, B.K.1    Deupi, X.2
  • 4
    • 33645798851 scopus 로고    scopus 로고
    • The fluorescent toolbox for assessing protein location and function
    • B.N. Giepmans The fluorescent toolbox for assessing protein location and function Science 312 2006 217 224
    • (2006) Science , vol.312 , pp. 217-224
    • Giepmans, B.N.1
  • 5
    • 0038487327 scopus 로고    scopus 로고
    • The ins and outs of G protein-coupled receptor trafficking
    • A. Marchese The ins and outs of G protein-coupled receptor trafficking Trends Biochem. Sci. 28 2003 369 376
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 369-376
    • Marchese, A.1
  • 6
    • 13444269196 scopus 로고    scopus 로고
    • Monitoring the formation of dynamic G-protein-coupled receptor–protein complexes in living cells
    • K.D. Pfleger K.A. Eidne Monitoring the formation of dynamic G-protein-coupled receptor–protein complexes in living cells Biochem. J. 385 2005 625 637
    • (2005) Biochem. J. , vol.385 , pp. 625-637
    • Pfleger, K.D.1    Eidne, K.A.2
  • 7
    • 33847419390 scopus 로고    scopus 로고
    • International Union of Basic and Clinical Pharmacology. LXVII. Recommendations for the recognition and nomenclature of G protein-coupled receptor heteromultimers
    • J.P. Pin International Union of Basic and Clinical Pharmacology. LXVII. Recommendations for the recognition and nomenclature of G protein-coupled receptor heteromultimers Pharmacol. Rev. 59 2007 5 13
    • (2007) Pharmacol. Rev. , vol.59 , pp. 5-13
    • Pin, J.P.1
  • 8
    • 34548433883 scopus 로고    scopus 로고
    • Kinetic analysis of G protein-coupled receptor signaling using fluorescence resonance energy transfer in living cells
    • M.J. Lohse Kinetic analysis of G protein-coupled receptor signaling using fluorescence resonance energy transfer in living cells Adv. Protein Chem. 74 2007 167 188
    • (2007) Adv. Protein Chem. , vol.74 , pp. 167-188
    • Lohse, M.J.1
  • 9
    • 35248892144 scopus 로고    scopus 로고
    • Monitoring receptor signaling by intramolecular FRET
    • M.J. Lohse Monitoring receptor signaling by intramolecular FRET Curr. Opin. Pharmacol. 7 2007 547 553
    • (2007) Curr. Opin. Pharmacol. , vol.7 , pp. 547-553
    • Lohse, M.J.1
  • 10
    • 0017795758 scopus 로고
    • Fluorescence energy transfer as a spectroscopic ruler
    • L. Stryer Fluorescence energy transfer as a spectroscopic ruler Annu. Rev. Biochem. 47 1978 819 846
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 819-846
    • Stryer, L.1
  • 11
    • 33646343978 scopus 로고    scopus 로고
    • Illuminating insights into protein–protein interactions using bioluminescence resonance energy transfer (BRET)
    • K.D. Pfleger K.A. Eidne Illuminating insights into protein–protein interactions using bioluminescence resonance energy transfer (BRET) Nat. Methods 3 2006 165 174
    • (2006) Nat. Methods , vol.3 , pp. 165-174
    • Pfleger, K.D.1    Eidne, K.A.2
  • 12
    • 3042798464 scopus 로고    scopus 로고
    • Labeling of fusion proteins with synthetic fluorophores in live cells
    • A. Keppler Labeling of fusion proteins with synthetic fluorophores in live cells Proc. Natl. Acad. Sci. U. S. A. 101 2004 9955 9959
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 9955-9959
    • Keppler, A.1
  • 13
    • 3242754218 scopus 로고    scopus 로고
    • Specific labeling of cell surface proteins with chemically diverse compounds
    • N. George Specific labeling of cell surface proteins with chemically diverse compounds J. Am. Chem. Soc. 126 2004 8896 8897
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 8896-8897
    • George, N.1
  • 14
    • 33846595332 scopus 로고    scopus 로고
    • Tracking of human Y receptors in living cells – a fluorescence approach
    • I. Böhme Tracking of human Y receptors in living cells – a fluorescence approach Peptides 28 2007 226 234
    • (2007) Peptides , vol.28 , pp. 226-234
    • Böhme, I.1
  • 15
    • 33144473025 scopus 로고    scopus 로고
    • FRET imaging reveals that functional neurokinin-1 receptors are monomeric and reside in membrane microdomains of live cells
    • B.H. Meyer FRET imaging reveals that functional neurokinin-1 receptors are monomeric and reside in membrane microdomains of live cells Proc. Natl. Acad. Sci. U. S. A. 103 2006 2138 2143
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 2138-2143
    • Meyer, B.H.1
  • 16
    • 27144448780 scopus 로고    scopus 로고
    • Mammalian cell-based optimization of the biarsenical-binding tetracysteine motif for improved fluorescence and affinity
    • B.R. Martin Mammalian cell-based optimization of the biarsenical-binding tetracysteine motif for improved fluorescence and affinity Nat. Biotechnol. 23 2005 1308 1314
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1308-1314
    • Martin, B.R.1
  • 17
    • 20844434337 scopus 로고    scopus 로고
    • A FLASH-based approach to determine G protein-coupled receptor activation in living cells
    • C. Hoffmann A FLASH-based approach to determine G protein-coupled receptor activation in living cells Nat. Methods 2 2005 171 176
    • (2005) Nat. Methods , vol.2 , pp. 171-176
    • Hoffmann, C.1
  • 18
    • 28644443374 scopus 로고    scopus 로고
    • Dynamics of receptor/G protein coupling in living cells
    • P. Hein Dynamics of receptor/G protein coupling in living cells EMBO J. 24 2005 4106 4114
    • (2005) EMBO J. , vol.24 , pp. 4106-4114
    • Hein, P.1
  • 19
    • 33845942468 scopus 로고    scopus 로고
    • Gs Activation is time-limiting in initiating receptor-mediated signaling
    • P. Hein Gs Activation is time-limiting in initiating receptor-mediated signaling J. Biol. Chem. 281 2006 33345 33351
    • (2006) J. Biol. Chem. , vol.281 , pp. 33345-33351
    • Hein, P.1
  • 20
    • 33747739472 scopus 로고    scopus 로고
    • Molecular basis of partial agonism at the neurotransmitter α2A-adrenergic receptor and Gi-protein heterotrimer
    • i-protein heterotrimer J. Biol. Chem. 281 2006 24506 24511
    • (2006) J. Biol. Chem. , vol.281 , pp. 24506-24511
    • Nikolaev, V.O.1
  • 21
    • 0035860802 scopus 로고    scopus 로고
    • The neurokinin A receptor activates calcium and cAMP responses through distinct conformational states
    • T. Palanche The neurokinin A receptor activates calcium and cAMP responses through distinct conformational states J. Biol. Chem. 276 2001 34853 34861
    • (2001) J. Biol. Chem. , vol.276 , pp. 34853-34861
    • Palanche, T.1
  • 22
    • 27644521278 scopus 로고    scopus 로고
    • Turn-on switch in parathyroid hormone receptor by a two-step PTH binding mechanism
    • M. Castro Turn-on switch in parathyroid hormone receptor by a two-step PTH binding mechanism Proc. Natl. Acad. Sci. U. S. A. 102 2005 16084 16089
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 16084-16089
    • Castro, M.1
  • 23
    • 0038729670 scopus 로고    scopus 로고
    • Measurement of the millisecond activation switch of G-protein-coupled receptors in living cells
    • J.P. Vilardaga Measurement of the millisecond activation switch of G-protein-coupled receptors in living cells Nat. Biotechnol. 21 2003 807 812
    • (2003) Nat. Biotechnol. , vol.21 , pp. 807-812
    • Vilardaga, J.P.1
  • 24
    • 33845973320 scopus 로고    scopus 로고
    • Real-time optical recording of β1-adrenergic receptor activation reveals supersensitivity of the Arg389 variant to carvedilol
    • 1-adrenergic receptor activation reveals supersensitivity of the Arg389 variant to carvedilol J. Clin. Invest. 117 2007 229 235
    • (2007) J. Clin. Invest. , vol.117 , pp. 229-235
    • Rochais, F.1
  • 25
    • 18744376919 scopus 로고    scopus 로고
    • Real-time monitoring of receptor and G-protein interactions in living cells
    • C. Gales Real-time monitoring of receptor and G-protein interactions in living cells Nat. Methods 2 2005 177 184
    • (2005) Nat. Methods , vol.2 , pp. 177-184
    • Gales, C.1
  • 26
    • 33748355624 scopus 로고    scopus 로고
    • Probing the activation-promoted structural rearrangements in preassembled receptor–G protein complexes
    • C. Gales Probing the activation-promoted structural rearrangements in preassembled receptor–G protein complexes Nat. Struct. Mol. Biol. 13 2006 778 786
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 778-786
    • Gales, C.1
  • 27
    • 0035937571 scopus 로고    scopus 로고
    • Receptor-mediated activation of heterotrimeric G-proteins in living cells
    • C. Janetopoulos Receptor-mediated activation of heterotrimeric G-proteins in living cells Science 291 2001 2408 2411
    • (2001) Science , vol.291 , pp. 2408-2411
    • Janetopoulos, C.1
  • 28
    • 0347364629 scopus 로고    scopus 로고
    • Gi protein activation in intact cells involves subunit rearrangement rather than dissociation
    • i protein activation in intact cells involves subunit rearrangement rather than dissociation Proc. Natl. Acad. Sci. U. S. A. 100 2003 16077 16082
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 16077-16082
    • Bünemann, M.1
  • 29
    • 4444377903 scopus 로고    scopus 로고
    • Novel single chain cAMP sensors for receptor-induced signal propagation
    • V.O. Nikolaev Novel single chain cAMP sensors for receptor-induced signal propagation J. Biol. Chem. 279 2004 37215 37218
    • (2004) J. Biol. Chem. , vol.279 , pp. 37215-37218
    • Nikolaev, V.O.1
  • 30
    • 9344220483 scopus 로고    scopus 로고
    • Fluorescent indicators of cAMP and Epac activation reveal differential dynamics of cAMP signaling within discrete subcellular compartments
    • L.M. DiPilato Fluorescent indicators of cAMP and Epac activation reveal differential dynamics of cAMP signaling within discrete subcellular compartments Proc. Natl. Acad. Sci. U. S. A. 101 2004 16513 16518
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 16513-16518
    • DiPilato, L.M.1
  • 31
    • 12144282761 scopus 로고    scopus 로고
    • Detecting cAMP-induced Epac activation by fluorescence resonance energy transfer: Epac as a novel cAMP indicator
    • B. Ponsioen Detecting cAMP-induced Epac activation by fluorescence resonance energy transfer: Epac as a novel cAMP indicator EMBO Rep. 5 2004 1176 1180
    • (2004) EMBO Rep. , vol.5 , pp. 1176-1180
    • Ponsioen, B.1
  • 32
    • 0035861758 scopus 로고    scopus 로고
    • Activation and deactivation kinetics of α2A- and α2C-adrenergic receptor-activated G protein-activated inwardly rectifying K+-channel currents
    • +-channel currents J. Biol. Chem. 276 2001 47512 47517
    • (2001) J. Biol. Chem. , vol.276 , pp. 47512-47517
    • Bünemann, M.1
  • 33
    • 0025788724 scopus 로고
    • Comparative rates of desensitization of β-adrenergic receptors by the β-adrenergic receptor kinase and the cyclic AMP-dependent protein kinase
    • N.S. Roth Comparative rates of desensitization of β-adrenergic receptors by the β-adrenergic receptor kinase and the cyclic AMP-dependent protein kinase Proc. Natl. Acad. Sci. U. S. A. 88 1991 6201 6204
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 6201-6204
    • Roth, N.S.1
  • 34
    • 15744379282 scopus 로고    scopus 로고
    • β-Arrestin binding to the β2-adrenergic receptor requires both receptor phosphorylation and receptor activation
    • 2-adrenergic receptor requires both receptor phosphorylation and receptor activation J. Biol. Chem. 280 2005 9528 9535
    • (2005) J. Biol. Chem. , vol.280 , pp. 9528-9535
    • Krasel, C.1
  • 35
    • 33746012381 scopus 로고    scopus 로고
    • G-protein-coupled receptor kinase specificity for β-arrestin recruitment to the β2-adrenergic receptor revealed by fluorescence resonance energy transfer
    • 2-adrenergic receptor revealed by fluorescence resonance energy transfer J. Biol. Chem. 281 2006 20577 20588
    • (2006) J. Biol. Chem. , vol.281 , pp. 20577-20588
    • Violin, J.D.1
  • 36
    • 17644391412 scopus 로고    scopus 로고
    • Monitoring agonist-promoted conformational changes of beta-arrestin in living cells by intramolecular BRET
    • P.G. Charest Monitoring agonist-promoted conformational changes of beta-arrestin in living cells by intramolecular BRET EMBO Rep. 6 2005 334 340
    • (2005) EMBO Rep. , vol.6 , pp. 334-340
    • Charest, P.G.1
  • 37
    • 12544251544 scopus 로고    scopus 로고
    • Real-time monitoring of the PDE2 activity of live cells: hormone-stimulated cAMP hydrolysis is faster than hormone-stimulated cAMP synthesis
    • V.O. Nikolaev Real-time monitoring of the PDE2 activity of live cells: hormone-stimulated cAMP hydrolysis is faster than hormone-stimulated cAMP synthesis J. Biol. Chem. 280 2005 1716 1719
    • (2005) J. Biol. Chem. , vol.280 , pp. 1716-1719
    • Nikolaev, V.O.1
  • 38
    • 29444444012 scopus 로고    scopus 로고
    • Molecular basis of inverse agonism in a G protein-coupled receptor
    • J.P. Vilardaga Molecular basis of inverse agonism in a G protein-coupled receptor Nat. Chem. Biol. 1 2005 25 28
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 25-28
    • Vilardaga, J.P.1
  • 39
    • 34848863094 scopus 로고    scopus 로고
    • Live-cell monitoring of μ-opioid receptor mediated G-protein activation reveals strong biological activity of close morphine biosynthetic precursors
    • V.O. Nikolaev Live-cell monitoring of μ-opioid receptor mediated G-protein activation reveals strong biological activity of close morphine biosynthetic precursors J. Biol. Chem. 282 2007 27126 27132
    • (2007) J. Biol. Chem. , vol.282 , pp. 27126-27132
    • Nikolaev, V.O.1
  • 40
    • 0035971240 scopus 로고    scopus 로고
    • Maximal rate and nucleotide dependence of rhodopsin-catalyzed transducin activation: initial rate analysis based on a double displacement mechanism
    • M. Heck K.P. Hofmann Maximal rate and nucleotide dependence of rhodopsin-catalyzed transducin activation: initial rate analysis based on a double displacement mechanism J. Biol. Chem. 276 2001 10000 10009
    • (2001) J. Biol. Chem. , vol.276 , pp. 10000-10009
    • Heck, M.1    Hofmann, K.P.2
  • 41
    • 0018125541 scopus 로고
    • Mode of coupling between the β-adrenergic receptor and adenylate cyclase in turkey erythrocytes
    • A.M. Tolkovsky A. Levitzki Mode of coupling between the β-adrenergic receptor and adenylate cyclase in turkey erythrocytes Biochemistry 17 1978 3795 3810
    • (1978) Biochemistry , vol.17 , pp. 3795-3810
    • Tolkovsky, A.M.1    Levitzki, A.2
  • 42
    • 0018126502 scopus 로고
    • Coupling of a single adenylate cyclase to two receptors: adenosine and catecholamine
    • A.M. Tolkovsky A. Levitzki Coupling of a single adenylate cyclase to two receptors: adenosine and catecholamine Biochemistry 17 1978 3811 3817
    • (1978) Biochemistry , vol.17 , pp. 3811-3817
    • Tolkovsky, A.M.1    Levitzki, A.2
  • 43
    • 0021697164 scopus 로고
    • The ternary complex model. Its properties and application to ligand interactions with the D2-dopamine receptor of the anterior pituitary gland
    • K.A. Wreggett A. De Lean The ternary complex model. Its properties and application to ligand interactions with the D2-dopamine receptor of the anterior pituitary gland Mol. Pharmacol. 26 1984 214 227
    • (1984) Mol. Pharmacol. , vol.26 , pp. 214-227
    • Wreggett, K.A.1    De Lean, A.2
  • 44
    • 0021287011 scopus 로고
    • Two affinity states of Ri adenosine receptors in brain membranes: analysis of guanine nucleotide and temperature effects on radioligand binding
    • i adenosine receptors in brain membranes: analysis of guanine nucleotide and temperature effects on radioligand binding Mol. Pharmacol. 26 1984 1 9
    • (1984) Mol. Pharmacol. , vol.26 , pp. 1-9
    • Lohse, M.J.1
  • 45
    • 29444446964 scopus 로고    scopus 로고
    • Heterotrimeric G proteins pre-couple with G protein-coupled receptors in living cells
    • M. Nobles Heterotrimeric G proteins pre-couple with G protein-coupled receptors in living cells Proc. Natl. Acad. Sci. U. S. A. 102 2005 18706 18711
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 18706-18711
    • Nobles, M.1
  • 46
    • 34547124343 scopus 로고    scopus 로고
    • Signaling through a G protein-coupled receptor and its corresponding G protein follows a stoichiometrically limited model
    • F. Philip Signaling through a G protein-coupled receptor and its corresponding G protein follows a stoichiometrically limited model J. Biol. Chem. 282 2007 19203 19216
    • (2007) J. Biol. Chem. , vol.282 , pp. 19203-19216
    • Philip, F.1
  • 47
    • 34247511554 scopus 로고    scopus 로고
    • Real-time analysis of agonist-induced activation of protease-activated receptor 1/Gαi1 protein complex measured by bioluminescence resonance energy transfer in living cells
    • i1 protein complex measured by bioluminescence resonance energy transfer in living cells Mol. Pharmacol. 71 2007 1329 1340
    • (2007) Mol. Pharmacol. , vol.71 , pp. 1329-1340
    • Ayoub, M.A.1
  • 48
    • 3042549102 scopus 로고    scopus 로고
    • A fluorescence resonance energy transfer-based sensor indicates that receptor access to a G protein is unrestricted in a living mammalian cell
    • I. Azpiazu N. Gautam A fluorescence resonance energy transfer-based sensor indicates that receptor access to a G protein is unrestricted in a living mammalian cell J. Biol. Chem. 279 2004 27709 27718
    • (2004) J. Biol. Chem. , vol.279 , pp. 27709-27718
    • Azpiazu, I.1    Gautam, N.2
  • 49
    • 34447645129 scopus 로고    scopus 로고
    • Resonance energy transfer approaches in molecular pharmacology and beyond
    • S. Marullo M. Bouvier Resonance energy transfer approaches in molecular pharmacology and beyond Trends Pharmacol. Sci. 28 2007 362 365
    • (2007) Trends Pharmacol. Sci. , vol.28 , pp. 362-365
    • Marullo, S.1    Bouvier, M.2
  • 50
    • 33947362780 scopus 로고    scopus 로고
    • The α1b-adrenoceptor exists as a higher-order oligomer: effective oligomerization is required for receptor maturation, surface delivery, and function
    • 1b-adrenoceptor exists as a higher-order oligomer: effective oligomerization is required for receptor maturation, surface delivery, and function Mol. Pharmacol. 71 2007 1015 1029
    • (2007) Mol. Pharmacol. , vol.71 , pp. 1015-1029
    • Lopez-Gimenez, J.F.1
  • 51
    • 33751215258 scopus 로고    scopus 로고
    • A rigorous experimental framework for detecting protein oligomerization using bioluminescence resonance energy transfer
    • J.R. James A rigorous experimental framework for detecting protein oligomerization using bioluminescence resonance energy transfer Nat. Methods 3 2006 1001 1006
    • (2006) Nat. Methods , vol.3 , pp. 1001-1006
    • James, J.R.1
  • 52
    • 33751237718 scopus 로고    scopus 로고
    • G protein-coupled receptors: too many dimers?
    • M.J. Lohse G protein-coupled receptors: too many dimers? Nat. Methods 3 2006 972 973
    • (2006) Nat. Methods , vol.3 , pp. 972-973
    • Lohse, M.J.1
  • 53
    • 33845923854 scopus 로고    scopus 로고
    • BRET analysis of GPCR oligomerization: newer does not mean better
    • M. Bouvier BRET analysis of GPCR oligomerization: newer does not mean better Nat. Methods 4 2007 3 4
    • (2007) Nat. Methods , vol.4 , pp. 3-4
    • Bouvier, M.1
  • 54
    • 21344446100 scopus 로고    scopus 로고
    • Allosteric functioning of dimeric class C G-protein-coupled receptors
    • J.P. Pin Allosteric functioning of dimeric class C G-protein-coupled receptors FEBS J. 272 2005 2947 2955
    • (2005) FEBS J. , vol.272 , pp. 2947-2955
    • Pin, J.P.1
  • 55
    • 34547434085 scopus 로고    scopus 로고
    • Monomeric G protein-coupled receptor rhodopsin in solution activates its G protein transducin at the diffusion limit
    • O.P. Ernst Monomeric G protein-coupled receptor rhodopsin in solution activates its G protein transducin at the diffusion limit Proc. Natl. Acad. Sci. U. S. A. 104 2007 10859 10864
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 10859-10864
    • Ernst, O.P.1
  • 56
    • 34250666273 scopus 로고    scopus 로고
    • A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein
    • M.R. Whorton A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein Proc. Natl. Acad. Sci. U. S. A. 104 2007 7682 7687
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 7682-7687
    • Whorton, M.R.1
  • 57
    • 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
  • 58
    • 0028912416 scopus 로고
    • The role of G-protein βγ subunits in signal transduction
    • S. Müller M.J. Lohse The role of G-protein βγ subunits in signal transduction Biochem. Soc. Trans. 23 1995 141 148
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 141-148
    • Müller, S.1    Lohse, M.J.2
  • 59
    • 0032588307 scopus 로고    scopus 로고
    • Crosstalk between Gαi- and Gαq-coupled receptors is mediated via Gβγ exchange
    • q-coupled receptors is mediated via Gβγ exchange Proc. Natl. Acad. Sci. U. S. A. 96 1999 10626 10631
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 10626-10631
    • Quitterer, U.1    Lohse, M.J.2
  • 60
    • 0034724206 scopus 로고    scopus 로고
    • Signal transduction by a nondissociable heterotrimeric yeast G protein
    • S. Klein Signal transduction by a nondissociable heterotrimeric yeast G protein Proc. Natl. Acad. Sci. U. S. A. 97 2000 3219 3223
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 3219-3223
    • Klein, S.1
  • 61
    • 21644479599 scopus 로고    scopus 로고
    • G-protein activation without subunit dissociation depends on a Gαi-specific region
    • i-specific region J. Biol. Chem. 280 2005 24584 24590
    • (2005) J. Biol. Chem. , vol.280 , pp. 24584-24590
    • Frank, M.1
  • 63
    • 33845219419 scopus 로고    scopus 로고
    • Some G protein heterotrimers physically dissociate in living cells
    • G.J. Digby Some G protein heterotrimers physically dissociate in living cells Proc. Natl. Acad. Sci. U. S. A. 103 2006 17789 17794
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 17789-17794
    • Digby, G.J.1
  • 64
    • 34249011789 scopus 로고    scopus 로고
    • Subunit dissociation and diffusion determine the subcellular localization of rod and cone transducins
    • D.H. Rosenzweig Subunit dissociation and diffusion determine the subcellular localization of rod and cone transducins J. Neurosci. 27 2007 5484 5494
    • (2007) J. Neurosci. , vol.27 , pp. 5484-5494
    • Rosenzweig, D.H.1
  • 65
    • 34547129113 scopus 로고    scopus 로고
    • Signaling by a non-dissociated complex of G protein βγ and α subunits stimulated by a receptor-independent activator of G protein signaling, AGS8
    • C. Yuan Signaling by a non-dissociated complex of G protein βγ and α subunits stimulated by a receptor-independent activator of G protein signaling, AGS8 J. Biol. Chem. 282 2007 19938 19947
    • (2007) J. Biol. Chem. , vol.282 , pp. 19938-19947
    • Yuan, C.1
  • 66
    • 34548379040 scopus 로고    scopus 로고
    • Some mechanistic insights into GPCR activation from detergent-solubilized ternary complexes on beads
    • T. Buranda Some mechanistic insights into GPCR activation from detergent-solubilized ternary complexes on beads Adv. Protein Chem. 74 2007 95 135
    • (2007) Adv. Protein Chem. , vol.74 , pp. 95-135
    • Buranda, T.1
  • 67
    • 24744455039 scopus 로고    scopus 로고
    • Interplay of Ca2+ and cAMP signaling in the insulin-secreting MIN6 β-cell line
    • 2+ and cAMP signaling in the insulin-secreting MIN6 β-cell line J. Biol. Chem. 280 2005 31294 31302
    • (2005) J. Biol. Chem. , vol.280 , pp. 31294-31302
    • Landa, L.R.1
  • 68
    • 33645222621 scopus 로고    scopus 로고
    • Ca2+ stimulation of adenylyl cyclase generates dynamic oscillations in cyclic AMP
    • 2+ stimulation of adenylyl cyclase generates dynamic oscillations in cyclic AMP J. Cell Sci. 119 2006 828 836
    • (2006) J. Cell Sci. , vol.119 , pp. 828-836
    • Willoughby, D.1    Cooper, D.M.2
  • 69
    • 33845422428 scopus 로고    scopus 로고
    • Imaging of cAMP levels and protein kinase A activity reveals that retinal waves drive oscillations in second-messenger cascades
    • T.A. Dunn Imaging of cAMP levels and protein kinase A activity reveals that retinal waves drive oscillations in second-messenger cascades J. Neurosci. 26 2006 12807 12815
    • (2006) J. Neurosci. , vol.26 , pp. 12807-12815
    • Dunn, T.A.1
  • 70
    • 0027246341 scopus 로고
    • Spatially resolved dynamics of cAMP and protein kinase A subunits in Aplysia sensory neurons
    • B.J. Bacskai Spatially resolved dynamics of cAMP and protein kinase A subunits in Aplysia sensory neurons Science 260 1993 222 226
    • (1993) Science , vol.260 , pp. 222-226
    • Bacskai, B.J.1
  • 71
    • 0029951674 scopus 로고    scopus 로고
    • Spatio-temporal dynamics of cyclic AMP signals in an intact neural circuit
    • C.M. Hempel Spatio-temporal dynamics of cyclic AMP signals in an intact neural circuit Nature 384 1996 166 169
    • (1996) Nature , vol.384 , pp. 166-169
    • Hempel, C.M.1
  • 72
    • 33749665081 scopus 로고    scopus 로고
    • Compartmentation of cyclic nucleotide signaling in the heart: the role of cyclic nucleotide phosphodiesterases
    • R. Fischmeister Compartmentation of cyclic nucleotide signaling in the heart: the role of cyclic nucleotide phosphodiesterases Circ. Res. 99 2006 816 828
    • (2006) Circ. Res. , vol.99 , pp. 816-828
    • Fischmeister, R.1
  • 73
    • 0036500494 scopus 로고    scopus 로고
    • Discrete microdomains with high concentration of cAMP in stimulated rat neonatal cardiac myocytes
    • M. Zaccolo T. Pozzan Discrete microdomains with high concentration of cAMP in stimulated rat neonatal cardiac myocytes Science 295 2002 1711 1715
    • (2002) Science , vol.295 , pp. 1711-1715
    • Zaccolo, M.1    Pozzan, T.2
  • 74
    • 3142723295 scopus 로고    scopus 로고
    • FRET-based analysis of cAMP dynamics in live cells reveals distinct functions of compartmentalized phosphodiesterases in cardiac myocytes
    • M. Mongillo FRET-based analysis of cAMP dynamics in live cells reveals distinct functions of compartmentalized phosphodiesterases in cardiac myocytes Circ. Res. 95 2004 67 75
    • (2004) Circ. Res. , vol.95 , pp. 67-75
    • Mongillo, M.1
  • 75
    • 33750910207 scopus 로고    scopus 로고
    • Cyclic AMP imaging in adult cardiac myocytes reveals far-reaching β1-adrenergic but locally confined β2-adrenergic receptor-mediated signaling
    • 2-adrenergic receptor-mediated signaling Circ. Res. 99 2006 1084 1091
    • (2006) Circ. Res. , vol.99 , pp. 1084-1091
    • Nikolaev, V.O.1
  • 76
    • 34249863122 scopus 로고    scopus 로고
    • cAMP microdomains and L-type Ca2+ channel regulation in guinea-pig ventricular myocytes
    • 2+ channel regulation in guinea-pig ventricular myocytes J. Physiol. 580 2007 765 776
    • (2007) J. Physiol. , vol.580 , pp. 765-776
    • Warrier, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.