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Volumn 8, Issue 13, 2003, Pages 579-585

High-content assays for ligand regulation of G-protein-coupled receptors

Author keywords

Beta arrestins; Biochemistry; Drug Discovery; G protein coupled receptors; Green fluorescent protein; Multiplexed assays; Pharmaceutical Science; Pharmacology; Protein translocation

Indexed keywords

BETA ARRESTIN 1; BETA ARRESTIN 2; G PROTEIN COUPLED RECEPTOR; LIGAND; RETINA S ANTIGEN; UNCLASSIFIED DRUG;

EID: 0038380750     PISSN: 13596446     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-6446(03)02738-7     Document Type: Review
Times cited : (74)

References (60)
  • 1
    • 0035895505 scopus 로고    scopus 로고
    • The sequence of the human genome
    • Venter J.C., et al. The sequence of the human genome. Science. 291:2001;1304-1351.
    • (2001) Science , vol.291 , pp. 1304-1351
    • Venter, J.C.1
  • 2
    • 2042437650 scopus 로고    scopus 로고
    • Initial sequencing and analysis of the human genome
    • Lander E.S., et al. Initial sequencing and analysis of the human genome. Nature. 409:2001;860-921.
    • (2001) Nature , vol.409 , pp. 860-921
    • Lander, E.S.1
  • 3
    • 0037446894 scopus 로고    scopus 로고
    • The G protein-coupled receptor repertoires of human and mouse
    • Vassilatis D.K., et al. The G protein-coupled receptor repertoires of human and mouse. Proc. Natl. Acad. Sci. U. S. A. 100:2003;4903-4908.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 4903-4908
    • Vassilatis, D.K.1
  • 4
    • 0033776857 scopus 로고    scopus 로고
    • Orphan G-protein coupled receptors: Novel drug targets for the pharmaceutical industry
    • Wilson S., Bergsma D. Orphan G-protein coupled receptors: novel drug targets for the pharmaceutical industry. Drug Des. Discov. 17:2000;105-114.
    • (2000) Drug Des. Discov. , vol.17 , pp. 105-114
    • Wilson, S.1    Bergsma, D.2
  • 5
    • 0037082324 scopus 로고    scopus 로고
    • Target validation of G-protein coupled receptors
    • Wise A., et al. Target validation of G-protein coupled receptors. Drug Discov. Today. 7:2002;235-246.
    • (2002) Drug Discov. Today , vol.7 , pp. 235-246
    • Wise, A.1
  • 6
    • 0036669944 scopus 로고    scopus 로고
    • Strategies to identify ligands for orphan G-protein-coupled receptors
    • Milligan G. Strategies to identify ligands for orphan G-protein-coupled receptors. Biochem. Soc. Trans. 30:2002;789-793.
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 789-793
    • Milligan, G.1
  • 7
    • 0036449253 scopus 로고    scopus 로고
    • Functional assays for identifying ligands at orphan G protein-coupled receptors
    • Szekeres P.G. Functional assays for identifying ligands at orphan G protein-coupled receptors. Recept. Channels. 8:2002;297-308.
    • (2002) Recept. Channels , vol.8 , pp. 297-308
    • Szekeres, P.G.1
  • 8
    • 0035028126 scopus 로고    scopus 로고
    • Cell-based versus isolated target screening: How lucky do you feel?
    • Moore K., Rees S. Cell-based versus isolated target screening: how lucky do you feel? J. Biomol. Screen. 6:2001;69-74.
    • (2001) J. Biomol. Screen. , vol.6 , pp. 69-74
    • Moore, K.1    Rees, S.2
  • 9
    • 0036451532 scopus 로고    scopus 로고
    • Aequorin-based functional assays for G-protein-coupled receptors, ion channels and tyrosine kinase receptors
    • Dupriez V.J., et al. Aequorin-based functional assays for G-protein-coupled receptors, ion channels and tyrosine kinase receptors. Recept. Channels. 8:2002;319-330.
    • (2002) Recept. Channels , vol.8 , pp. 319-330
    • Dupriez, V.J.1
  • 10
    • 0035489204 scopus 로고    scopus 로고
    • Reporter-gene systems for the study of G-protein-coupled receptors
    • Hill S.J., et al. Reporter-gene systems for the study of G-protein-coupled receptors. Curr. Opin. Pharmacol. 1:2001;526-532.
    • (2001) Curr. Opin. Pharmacol. , vol.1 , pp. 526-532
    • Hill, S.J.1
  • 11
    • 0036449330 scopus 로고    scopus 로고
    • The use of biosensors to study GPCR function: Applications for high content screening
    • Conway B.R., Demarest K.T. The use of biosensors to study GPCR function: Applications for high content screening. Recept. Channels. 8:2002;331-341.
    • (2002) Recept. Channels , vol.8 , pp. 331-341
    • Conway, B.R.1    Demarest, K.T.2
  • 12
    • 0036902813 scopus 로고    scopus 로고
    • Creating new fluorescent probes for cell biology
    • Zhang J., et al. Creating new fluorescent probes for cell biology. Nat. Rev. Mol. Cell Biol. 3:2002;906-918.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 906-918
    • Zhang, J.1
  • 13
    • 0034581533 scopus 로고    scopus 로고
    • Studies of signal transduction events using chimeras to green fluorescent protein
    • Meyer T., Oancea E. Studies of signal transduction events using chimeras to green fluorescent protein. Methods Enzymol. 327:2000;500-513.
    • (2000) Methods Enzymol. , vol.327 , pp. 500-513
    • Meyer, T.1    Oancea, E.2
  • 14
    • 0036341207 scopus 로고    scopus 로고
    • Signal transduction and endocytosis: Close encounters of many kinds
    • Sorkin A., Von Zastrow M. Signal transduction and endocytosis: close encounters of many kinds. Nat. Rev. Mol. Cell Biol. 3:2002;600-614.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 600-614
    • Sorkin, A.1    Von Zastrow, M.2
  • 15
    • 0035055204 scopus 로고    scopus 로고
    • Diversity and specificity in the regulated endocytic membrane trafficking of G-protein-coupled receptors
    • Tsao P.I., von Zastrow M. Diversity and specificity in the regulated endocytic membrane trafficking of G-protein-coupled receptors. Pharmacol. Ther. 89:2001;139-147.
    • (2001) Pharmacol. Ther. , vol.89 , pp. 139-147
    • Tsao, P.I.1    Von Zastrow, M.2
  • 16
    • 0031025764 scopus 로고    scopus 로고
    • Internal trafficking and surface mobility of a functionally intact β2-adrenergic receptor-green fluorescent protein conjugate
    • Barak L.S., et al. Internal trafficking and surface mobility of a functionally intact β2-adrenergic receptor-green fluorescent protein conjugate. Mol. Pharmacol. 51:1997;177-184.
    • (1997) Mol. Pharmacol. , vol.51 , pp. 177-184
    • Barak, L.S.1
  • 17
    • 0034193130 scopus 로고    scopus 로고
    • Using green fluorescent proteins to study G-protein-coupled receptor localization and trafficking
    • Kallal L., Benovic J.L. Using green fluorescent proteins to study G-protein-coupled receptor localization and trafficking. Trends Pharmacol. Sci. 21:2000;175-180.
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 175-180
    • Kallal, L.1    Benovic, J.L.2
  • 18
    • 0032699862 scopus 로고    scopus 로고
    • Exploring the dynamics of regulation of G protein-coupled receptors using green fluorescent protein
    • Milligan G. Exploring the dynamics of regulation of G protein-coupled receptors using green fluorescent protein. Br. J. Pharmacol. 128:1999;501-510.
    • (1999) Br. J. Pharmacol. , vol.128 , pp. 501-510
    • Milligan, G.1
  • 19
    • 0030993594 scopus 로고    scopus 로고
    • Antagonist-stimulated internalization of the G protein-coupled cholecystokinin receptor
    • Roettger B.F., et al. Antagonist-stimulated internalization of the G protein-coupled cholecystokinin receptor. Mol. Pharmacol. 51:1997;357-362.
    • (1997) Mol. Pharmacol. , vol.51 , pp. 357-362
    • Roettger, B.F.1
  • 20
    • 0035830863 scopus 로고    scopus 로고
    • Newly synthesized human δ opioid receptors retained in the endoplasmic reticulum are retrotranslocated to the cytosol, deglycosylated, ubiquitinated, and degraded by the proteasome
    • Petaja-Repo U.E., et al. Newly synthesized human δ opioid receptors retained in the endoplasmic reticulum are retrotranslocated to the cytosol, deglycosylated, ubiquitinated, and degraded by the proteasome. J. Biol. Chem. 276:2001;4416-4423.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4416-4423
    • Petaja-Repo, U.E.1
  • 21
    • 0035164176 scopus 로고    scopus 로고
    • Quantitative analysis of agonist-dependent parathyroid hormone receptor trafficking in whole cells using a functional green fluorescent protein conjugate
    • Conway B.R., et al. Quantitative analysis of agonist-dependent parathyroid hormone receptor trafficking in whole cells using a functional green fluorescent protein conjugate. J. Cell. Physiol. 189:2001;341-355.
    • (2001) J. Cell. Physiol. , vol.189 , pp. 341-355
    • Conway, B.R.1
  • 22
    • 0035101820 scopus 로고    scopus 로고
    • Evolving concepts in G protein-coupled receptor endocytosis: The role in receptor desensitization and signaling
    • Ferguson S.S. Evolving concepts in G protein-coupled receptor endocytosis: the role in receptor desensitization and signaling. Pharmacol. Rev. 53:2001;1-24.
    • (2001) Pharmacol. Rev. , vol.53 , pp. 1-24
    • Ferguson, S.S.1
  • 23
    • 0030736417 scopus 로고    scopus 로고
    • A β-arrestin/green fluorescent protein biosensor for detecting G protein-coupled receptor activation
    • Barak L.S., et al. A β-arrestin/green fluorescent protein biosensor for detecting G protein-coupled receptor activation. J. Biol. Chem. 272:1997;27497-27500.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27497-27500
    • Barak, L.S.1
  • 24
    • 0034595860 scopus 로고    scopus 로고
    • Differential affinities of visual arrestin, β arrestin1, and β arrestin2 for G protein-coupled receptors delineate two major classes of receptors
    • Oakley R.H., et al. Differential affinities of visual arrestin, β arrestin1, and β arrestin2 for G protein-coupled receptors delineate two major classes of receptors. J. Biol. Chem. 275:2000;17201-17210.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17201-17210
    • Oakley, R.H.1
  • 25
    • 0012132962 scopus 로고    scopus 로고
    • The cellular distribution of fluorescently labelled arrestins provides a robust, sensitive and universal assay for screening G protein-coupled receptors
    • Oakley R.H., et al. The cellular distribution of fluorescently labelled arrestins provides a robust, sensitive and universal assay for screening G protein-coupled receptors. Assays Drug Develop. Tech. 1:2002;21-30.
    • (2002) Assays Drug Develop. Tech. , vol.1 , pp. 21-30
    • Oakley, R.H.1
  • 26
    • 0036973242 scopus 로고    scopus 로고
    • The BRET2/arrestin assay in stable recombinant cells: A platform to screen for compounds that interact with G protein-coupled receptors (GPCRS)
    • Bertrand L., et al. The BRET2/arrestin assay in stable recombinant cells: a platform to screen for compounds that interact with G protein-coupled receptors (GPCRS). J. Recept. Signal Transduct. Res. 22:2002;533-541.
    • (2002) J. Recept. Signal Transduct. Res. , vol.22 , pp. 533-541
    • Bertrand, L.1
  • 27
    • 0038341013 scopus 로고    scopus 로고
    • The use of bioluminescence resonance energy transfer (BRET2) to study neuropeptide Y receptor agonist induced {β}-arrestin 2 interaction
    • in press
    • Berglund, M.M. et al. The use of bioluminescence resonance energy transfer (BRET2) to study neuropeptide Y receptor agonist induced {β}-arrestin 2 interaction. J. Pharmacol. Exp. Ther. (in press).
    • J. Pharmacol. Exp. Ther.
    • Berglund, M.M.1
  • 28
    • 0034234718 scopus 로고    scopus 로고
    • How accurately can we image inositol lipids in living cells?
    • Balla T., et al. How accurately can we image inositol lipids in living cells? Trends Pharmacol. Sci. 21:2000;238-241.
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 238-241
    • Balla, T.1
  • 29
    • 0037184051 scopus 로고    scopus 로고
    • 2+ and inositol 1,4,5-trisphosphate oscillation frequency. Receptor density versus agonist concentration
    • 2+ and inositol 1,4,5-trisphosphate oscillation frequency. Receptor density versus agonist concentration. J. Biol. Chem. 277:2002;35947-35960.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35947-35960
    • Nash, M.S.1
  • 30
    • 0036688175 scopus 로고    scopus 로고
    • The use of constitutively active GPCRs in drug discovery and functional genomics
    • Chalmers D.T., Behan D.P. The use of constitutively active GPCRs in drug discovery and functional genomics. Nat. Rev. Drug Discov. 1:2002;599-608.
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 599-608
    • Chalmers, D.T.1    Behan, D.P.2
  • 31
    • 0031018485 scopus 로고    scopus 로고
    • Structural instability of a constitutively active G protein-coupled receptor. Agonist-independent activation due to conformational flexibility
    • Gether U., et al. Structural instability of a constitutively active G protein-coupled receptor. Agonist-independent activation due to conformational flexibility. J. Biol. Chem. 272:1997;2587-2590.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2587-2590
    • Gether, U.1
  • 32
    • 0030752182 scopus 로고    scopus 로고
    • Up-regulation of the levels of expression and function of a constitutively active mutant of the hamster α1B-adrenoceptor by ligands that act as inverse agonists
    • Lee T.W., et al. Up-regulation of the levels of expression and function of a constitutively active mutant of the hamster α1B-adrenoceptor by ligands that act as inverse agonists. Biochem. J. 325:1997;733-739.
    • (1997) Biochem. J. , vol.325 , pp. 733-739
    • Lee, T.W.1
  • 33
    • 0030473469 scopus 로고    scopus 로고
    • Inverse agonist-induced up-regulation of the human β2-adrenoceptor in transfected neuroblastoma X glioma hybrid cells
    • MacEwan D.J., Milligan G. Inverse agonist-induced up-regulation of the human β2-adrenoceptor in transfected neuroblastoma X glioma hybrid cells. Mol. Pharmacol. 50:1996;1479-1486.
    • (1996) Mol. Pharmacol. , vol.50 , pp. 1479-1486
    • MacEwan, D.J.1    Milligan, G.2
  • 34
    • 0034763966 scopus 로고    scopus 로고
    • Inverse agonist upregulates the constitutively active D3.49(164)Q mutant of the rat μ-opioid receptor by stabilizing the structure and blocking constitutive internalization and down-regulation
    • Li J., et al. Inverse agonist upregulates the constitutively active D3.49(164)Q mutant of the rat μ-opioid receptor by stabilizing the structure and blocking constitutive internalization and down-regulation. Mol. Pharmacol. 60:2001;1064-1075.
    • (2001) Mol. Pharmacol. , vol.60 , pp. 1064-1075
    • Li, J.1
  • 35
    • 0036366653 scopus 로고    scopus 로고
    • Ligand rescue of constitutively active mutant receptors
    • Milligan G., et al. Ligand rescue of constitutively active mutant receptors. Neurosignals. 11:2002;29-33.
    • (2002) Neurosignals , vol.11 , pp. 29-33
    • Milligan, G.1
  • 36
    • 0031465316 scopus 로고    scopus 로고
    • Inverse agonism and the regulation of receptor number
    • Milligan G., Bond R.A. Inverse agonism and the regulation of receptor number. Trends Pharmacol. Sci. 18:1997;468-474.
    • (1997) Trends Pharmacol. Sci. , vol.18 , pp. 468-474
    • Milligan, G.1    Bond, R.A.2
  • 37
    • 0032730974 scopus 로고    scopus 로고
    • Visualizing differences in ligand regulation of wild-type and constitutively active mutant β(2)-green fluorescent protein fusion proteins
    • McLean A.J., et al. Visualizing differences in ligand regulation of wild-type and constitutively active mutant β(2)-green fluorescent protein fusion proteins. Mol. Pharmacol. 56:1999;1182-1191.
    • (1999) Mol. Pharmacol. , vol.56 , pp. 1182-1191
    • McLean, A.J.1
  • 39
    • 0034986205 scopus 로고    scopus 로고
    • Detection of receptor ligands by monitoring selective stabilization of a Renilla luciferase-tagged, constitutively active mutant, G protein-coupled receptor
    • Ramsay D., et al. Detection of receptor ligands by monitoring selective stabilization of a Renilla luciferase-tagged, constitutively active mutant, G protein-coupled receptor. Br. J. Pharmacol. 133:2001;315-323.
    • (2001) Br. J. Pharmacol. , vol.133 , pp. 315-323
    • Ramsay, D.1
  • 41
    • 0036780743 scopus 로고    scopus 로고
    • G-protein-coupled receptor oligomerization and its potential for drug discovery
    • George S.R., et al. G-protein-coupled receptor oligomerization and its potential for drug discovery. Nat. Rev. Drug Discov. 1:2002;808-820.
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 808-820
    • George, S.R.1
  • 42
    • 0036174608 scopus 로고    scopus 로고
    • Dimerization: An emerging concept for G protein-coupled receptor ontogeny and function
    • Angers S., et al. Dimerization: an emerging concept for G protein-coupled receptor ontogeny and function. Annu. Rev. Pharmacol. Toxicol. 42:2002;409-435.
    • (2002) Annu. Rev. Pharmacol. Toxicol. , vol.42 , pp. 409-435
    • Angers, S.1
  • 43
    • 0005604872 scopus 로고    scopus 로고
    • Receptor dimerization: A key step in chemokine signaling
    • Mellado M., et al. Receptor dimerization: a key step in chemokine signaling. Cell. Mol. Biol. 47:2001;575-582.
    • (2001) Cell. Mol. Biol. , vol.47 , pp. 575-582
    • Mellado, M.1
  • 44
    • 0038170289 scopus 로고    scopus 로고
    • Applications of novel resonance energy transfer techniques to study dynamic hormone receptor interactions in living cells
    • Eidne K.A., et al. Applications of novel resonance energy transfer techniques to study dynamic hormone receptor interactions in living cells. Trends Endocrinol. and Metabol. 13:2002;415-421.
    • (2002) Trends Endocrinol. and Metabol. , vol.13 , pp. 415-421
    • Eidne, K.A.1
  • 45
    • 0035918215 scopus 로고    scopus 로고
    • Constitutive and agonist-dependent homo-oligomerization of the thyrotropin-releasing hormone receptor. Detection in living cells using bioluminescence resonance energy transfer
    • Kroeger K.M., et al. Constitutive and agonist-dependent homo-oligomerization of the thyrotropin-releasing hormone receptor. Detection in living cells using bioluminescence resonance energy transfer. J. Biol. Chem. 276:2001;12736-12743.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12736-12743
    • Kroeger, K.M.1
  • 46
    • 0035930602 scopus 로고    scopus 로고
    • Agonist-dependent dissociation of oligomeric complexes of G protein-coupled cholecystokinin receptors demonstrated in living cells using bioluminescence resonance energy transfer
    • Cheng Z.J., Miller L.J. Agonist-dependent dissociation of oligomeric complexes of G protein-coupled cholecystokinin receptors demonstrated in living cells using bioluminescence resonance energy transfer. J. Biol. Chem. 276:2001;48040-48047.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48040-48047
    • Cheng, Z.J.1    Miller, L.J.2
  • 47
    • 0037160035 scopus 로고    scopus 로고
    • Ligand-dependent inhibition of oligomerization at the human thyrotropin receptor
    • Latif R., et al. Ligand-dependent inhibition of oligomerization at the human thyrotropin receptor. J. Biol. Chem. 277:2001;45059-45067.
    • (2001) J. Biol. Chem. , vol.277 , pp. 45059-45067
    • Latif, R.1
  • 48
    • 0035958023 scopus 로고    scopus 로고
    • Monitoring receptor oligomerization using time-resolved fluorescence resonance energy transfer and bioluminescence resonance energy transfer. The human δ-opioid receptor displays constitutive oligomerization at the cell surface, which is not regulated by receptor occupancy
    • McVey M., et al. Monitoring receptor oligomerization using time-resolved fluorescence resonance energy transfer and bioluminescence resonance energy transfer. The human δ-opioid receptor displays constitutive oligomerization at the cell surface, which is not regulated by receptor occupancy. J. Biol. Chem. 276:2001;14092-14099.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14092-14099
    • McVey, M.1
  • 49
    • 0037077208 scopus 로고    scopus 로고
    • Monitoring of ligand-independent dimerization and ligand-induced conformational changes of melatonin receptors in living cells by bioluminescence resonance energy transfer
    • Ayoub M.A., et al. Monitoring of ligand-independent dimerization and ligand-induced conformational changes of melatonin receptors in living cells by bioluminescence resonance energy transfer. J. Biol. Chem. 277:2002;21522-21528.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21522-21528
    • Ayoub, M.A.1
  • 50
    • 0037474238 scopus 로고    scopus 로고
    • Ligand-independent dimerization of CXCR4, a principal HIV-1 coreceptor
    • Babcock G.J., et al. Ligand-independent dimerization of CXCR4, a principal HIV-1 coreceptor. J. Biol. Chem. 278:2003;3378-3385.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3378-3385
    • Babcock, G.J.1
  • 51
    • 0035937571 scopus 로고    scopus 로고
    • Receptor-mediated activation of heterotrimeric G-proteins in living cells
    • Janetopoulos C., et al. 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
  • 52
    • 0036382757 scopus 로고    scopus 로고
    • Monitoring receptor-mediated activation of heterotrimeric G-proteins by fluorescence resonance energy transfer
    • Janetopoulos C., Devreotes P. Monitoring receptor-mediated activation of heterotrimeric G-proteins by fluorescence resonance energy transfer. Methods. 27:2002;366-373.
    • (2002) Methods , vol.27 , pp. 366-373
    • Janetopoulos, C.1    Devreotes, P.2
  • 53
    • 0035830890 scopus 로고    scopus 로고
    • Visualization of a functional Gα q-green fluorescent protein fusion in living cells. Association with the plasma membrane is disrupted by mutational activation and by elimination of palmitoylation sites, but not by activation mediated by receptors or AlF4
    • Hughes T.E., et al. Visualization of a functional Gα q-green fluorescent protein fusion in living cells. Association with the plasma membrane is disrupted by mutational activation and by elimination of palmitoylation sites, but not by activation mediated by receptors or AlF4. J. Biol. Chem. 276:2001;4227-4235.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4227-4235
    • Hughes, T.E.1
  • 54
    • 0037047366 scopus 로고    scopus 로고
    • A novel strategy to engineer functional fluorescent inhibitory G-protein α subunits
    • Leaney J.L., et al. A novel strategy to engineer functional fluorescent inhibitory G-protein α subunits. J. Biol. Chem. 277:2002;28803-28809.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28803-28809
    • Leaney, J.L.1
  • 55
    • 0036151483 scopus 로고    scopus 로고
    • Real-time visualization of a fluorescent G(α)(s): Dissociation of the activated G protein from plasma membrane
    • Yu J.Z., Rasenick M.M. Real-time visualization of a fluorescent G(α)(s): dissociation of the activated G protein from plasma membrane. Mol. Pharmacol. 61:2002;352-359.
    • (2002) Mol. Pharmacol. , vol.61 , pp. 352-359
    • Yu, J.Z.1    Rasenick, M.M.2
  • 56
    • 0036841022 scopus 로고    scopus 로고
    • A pH-sensitive fluor, CypHer 5, used to monitor agonist-induced G protein-coupled receptor internalization in live cells
    • Adie E.J., et al. A pH-sensitive fluor, CypHer 5, used to monitor agonist-induced G protein-coupled receptor internalization in live cells. BioTechniques. 33:2002;1152-1157.
    • (2002) BioTechniques , vol.33 , pp. 1152-1157
    • Adie, E.J.1
  • 57
    • 0038559375 scopus 로고    scopus 로고
    • CypHer 5 - A generic approach for measuring the activation and trafficking of G-protein-coupled receptors in live cells
    • in press
    • Adie, E.J. et al. CypHer 5 - a generic approach for measuring the activation and trafficking of G-protein-coupled receptors in live cells. Assays Drug Develop. Tech. (in press).
    • Assays Drug Develop. Tech.
    • Adie, E.J.1
  • 58
    • 0037452949 scopus 로고    scopus 로고
    • Regulation of epidermal growth factor receptor internalization by G protein-coupled receptors
    • Kim J., et al. Regulation of epidermal growth factor receptor internalization by G protein-coupled receptors. Biochemistry. 42:2003;2887-2894.
    • (2003) Biochemistry , vol.42 , pp. 2887-2894
    • Kim, J.1
  • 59
    • 0034737483 scopus 로고    scopus 로고
    • The β(2)-adrenergic receptor mediates extracellular signal-regulated kinase activation via assembly of a multi-receptor complex with the epidermal growth factor receptor
    • Maudsley S., et al. The β(2)-adrenergic receptor mediates extracellular signal-regulated kinase activation via assembly of a multi-receptor complex with the epidermal growth factor receptor. J. Biol. Chem. 275:2000;9572-9580.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9572-9580
    • Maudsley, S.1
  • 60
    • 0030683639 scopus 로고    scopus 로고
    • Signal characteristics of G protein-transactivated EGF receptor
    • Daub H., et al. Signal characteristics of G protein-transactivated EGF receptor. EMBO J. 16:1997;7032-7044.
    • (1997) EMBO J. , vol.16 , pp. 7032-7044
    • Daub, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.