메뉴 건너뛰기




Volumn 63, Issue 3, 2011, Pages 728-749

Regulators of G-protein signaling and their Gα substrates: Promises and challenges in their use as drug discovery targets

Author keywords

[No Author keywords available]

Indexed keywords

2 (1,3 BENZOTHIAZOL 2 YL) 3 [9 METHYL 2 (3 METHYLPHENOXY) 4 OXO 4H PYRIDO(1,2 A)PYRIMIDIN 3 YL]PROP 2 ENENITRILE; 2 (1,3 BENZOTHIAZOL 2 YL) 3 [9 METHYL 2 (4 FLUOROLPHENOXY) 4 OXO 4H PYRIDO(1,2 A)PYRIMIDIN 3 YL]PROP 2 ENENITRILE; 4 [(4 FLUOROPHENYL)METHYL] 2 (4 METHYLPHENYL) 1,2,4 THIADIAZOLIDINE 3,5 DIONE; BMS 192364; BMS 195270; CCG 4986; CCG 50014; CCG 63802; CCG 63808; G PROTEIN COUPLED INWARDLY RECTIFYING POTASSIUM CHANNEL; G PROTEIN COUPLED RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN ALPHA SUBUNIT; GUANINE NUCLEOTIDE BINDING PROTEIN BETA SUBUNIT; GUANINE NUCLEOTIDE BINDING PROTEIN GAMMA SUBUNIT; GUANOSINE TRIPHOSPHATASE; PROTEIN INHIBITOR; RGS PROTEIN; RGS4 PROTEIN; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; VEMURAFENIB; YM 254890;

EID: 79960671811     PISSN: 00316997     EISSN: 15210081     Source Type: Journal    
DOI: 10.1124/pr.110.003038     Document Type: Article
Times cited : (205)

References (250)
  • 1
    • 68549106027 scopus 로고    scopus 로고
    • The R7 RGS protein family: Multi-subunit regulators of neuronal G protein signaling
    • Anderson GR, Posokhova E, and Martemyanov KA (2009) The R7 RGS protein family: multi-subunit regulators of neuronal G protein signaling. Cell Biochem Biophys 54: 33-46.
    • (2009) Cell Biochem Biophys , vol.54 , pp. 33-46
    • Anderson, G.R.1    Posokhova, E.2    Martemyanov, K.A.3
  • 2
    • 1042266676 scopus 로고    scopus 로고
    • Differential contribution of GTPase activation and effector antagonism to the inhibitory effect of RGS proteins on Gqmediated signaling in vivo
    • Anger T, Zhang W, and Mende U (2004) Differential contribution of GTPase activation and effector antagonism to the inhibitory effect of RGS proteins on Gqmediated signaling in vivo. J Biol Chem 279: 3906-3915.
    • (2004) J Biol Chem , vol.279 , pp. 3906-3915
    • Anger, T.1    Zhang, W.2    Mende, U.3
  • 3
    • 0032492722 scopus 로고    scopus 로고
    • Sst2 is a GTPaseactivating protein for Gpa1: Purification and characterization of a cognate RGSGalpha protein pair in yeast
    • Apanovitch DM, Slep KC, Sigler PB, and Dohlman HG (1998) Sst2 is a GTPaseactivating protein for Gpa1: purification and characterization of a cognate RGSGalpha protein pair in yeast. Biochemistry 37: 4815-4822.
    • (1998) Biochemistry , vol.37 , pp. 4815-4822
    • Apanovitch, D.M.1    Slep, K.C.2    Sigler, P.B.3    Dohlman, H.G.4
  • 5
    • 77950815005 scopus 로고    scopus 로고
    • Future prospect of RNA interference for cancer therapies
    • Ashihara E, Kawata E, and Maekawa T (2010) Future prospect of RNA interference for cancer therapies. Curr Drug Targets 11: 345-360.
    • (2010) Curr Drug Targets , vol.11 , pp. 345-360
    • Ashihara, E.1    Kawata, E.2    Maekawa, T.3
  • 6
    • 37349103993 scopus 로고    scopus 로고
    • Suppression of immunoglobulin E-mediated allergic responses by regulator of G protein signaling 13
    • Bansal G, Xie Z, Rao S, Nocka KH, and Druey KM (2008) Suppression of immunoglobulin E-mediated allergic responses by regulator of G protein signaling 13. Nat Immunol 9: 73-80.
    • (2008) Nat Immunol , vol.9 , pp. 73-80
    • Bansal, G.1    Xie, Z.2    Rao, S.3    Nocka, K.H.4    Druey, K.M.5
  • 7
    • 14844338481 scopus 로고    scopus 로고
    • Beta-Arrestin 1 and Galphaq/11 coordinately activate RhoA and stress fiber formation following receptor stimulation
    • Barnes WG, Reiter E, Violin JD, Ren XR, Milligan G, and Lefkowitz RJ (2005) beta-Arrestin 1 and Galphaq/11 coordinately activate RhoA and stress fiber formation following receptor stimulation. J Biol Chem 280: 8041-8050.
    • (2005) J Biol Chem , vol.280 , pp. 8041-8050
    • Barnes, W.G.1    Reiter, E.2    Violin, J.D.3    Ren, X.R.4    Milligan, G.5    Lefkowitz, R.J.6
  • 8
    • 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
    • Benians A, Nobles M, Hosny S, and Tinker A (2005) 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: 13383-13394.
    • (2005) J Biol Chem , vol.280 , pp. 13383-13394
    • Benians, A.1    Nobles, M.2    Hosny, S.3    Tinker, A.4
  • 9
    • 12844255716 scopus 로고    scopus 로고
    • Regulator of G-protein signaling-5 induction in pericytes coincides with active vessel remodeling during neovascularization
    • Berger M, Bergers G, Arnold B, Hämmerling GJ, and Ganss R (2005) Regulator of G-protein signaling-5 induction in pericytes coincides with active vessel remodeling during neovascularization. Blood 105: 1094-1101.
    • (2005) Blood , vol.105 , pp. 1094-1101
    • Berger, M.1    Bergers, G.2    Arnold, B.3    Hämmerling, G.J.4    Ganss, R.5
  • 10
    • 0030576518 scopus 로고    scopus 로고
    • GAIP and RGS4 are GTPaseactivating proteins for the Gi subfamily of G protein alpha subunits
    • Berman DM, Wilkie TM, and Gilman AG (1996) GAIP and RGS4 are GTPaseactivating proteins for the Gi subfamily of G protein alpha subunits. Cell 86: 445-452.
    • (1996) Cell , vol.86 , pp. 445-452
    • Berman, D.M.1    Wilkie, T.M.2    Gilman, A.G.3
  • 11
    • 2442717874 scopus 로고    scopus 로고
    • RGS2 binds directly and selectively to the M1 muscarinic acetylcholine receptor third intracellular loop to modulate Gq/11alpha signaling
    • Bernstein LS, Ramineni S, Hague C, Cladman W, Chidiac P, Levey AI, and Hepler JR (2004) RGS2 binds directly and selectively to the M1 muscarinic acetylcholine receptor third intracellular loop to modulate Gq/11alpha signaling. J Biol Chem 279: 21248-21256.
    • (2004) J Biol Chem , vol.279 , pp. 21248-21256
    • Bernstein, L.S.1    Ramineni, S.2    Hague, C.3    Cladman, W.4    Chidiac, P.5    Levey, A.I.6    Hepler, J.R.7
  • 12
    • 67349159879 scopus 로고    scopus 로고
    • Inositol trisphosphate and calcium signalling mechanisms
    • Berridge MJ (2009) Inositol trisphosphate and calcium signalling mechanisms. Biochim Biophys Acta 1793: 933-940.
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 933-940
    • Berridge, M.J.1
  • 13
    • 0026694917 scopus 로고
    • Phospholipase C-beta 1 is a GTPase-activating protein for Gq/11, its physiologic regulator
    • Berstein G, Blank JL, Jhon DY, Exton JH, Rhee SG, and Ross EM (1992) Phospholipase C-beta 1 is a GTPase-activating protein for Gq/11, its physiologic regulator. Cell 70: 411-418.
    • (1992) Cell , vol.70 , pp. 411-418
    • Berstein, G.1    Blank, J.L.2    Jhon, D.Y.3    Exton, J.H.4    Rhee, S.G.5    Ross, E.M.6
  • 15
    • 79953878856 scopus 로고    scopus 로고
    • A nanomolarpotency small molecule inhibitor of regulator of G protein signaling proteins
    • Blazer LL, Zhang H, Casey EM, Husbands SM, and Neubig RR (2011) A nanomolarpotency small molecule inhibitor of regulator of G protein signaling proteins. Biochemistry 50: 3181-3192.
    • (2011) Biochemistry , vol.50 , pp. 3181-3192
    • Blazer, L.L.1    Zhang, H.2    Casey, E.M.3    Husbands, S.M.4    Neubig, R.R.5
  • 16
    • 33947371974 scopus 로고    scopus 로고
    • N-terminal residues control proteasomal degradation of RGS2, RGS4, and RGS5 in human embryonic kidney 293 cells
    • Bodenstein J, Sunahara RK, and Neubig RR (2007) N-terminal residues control proteasomal degradation of RGS2, RGS4, and RGS5 in human embryonic kidney 293 cells. Mol Pharmacol 71: 1040-1050.
    • (2007) Mol Pharmacol , vol.71 , pp. 1040-1050
    • Bodenstein, J.1    Sunahara, R.K.2    Neubig, R.R.3
  • 17
    • 0030835649 scopus 로고    scopus 로고
    • Structural aspects of heterotrimeric G-protein signaling
    • Bohm A, Gaudet R, and Sigler PB (1997) Structural aspects of heterotrimeric G-protein signaling. Curr Opin Biotechnol 8: 480-487.
    • (1997) Curr Opin Biotechnol , vol.8 , pp. 480-487
    • Bohm, A.1    Gaudet, R.2    Sigler, P.B.3
  • 20
    • 0345505671 scopus 로고    scopus 로고
    • Transcription profiling of platelet-derived growth factor-B-deficient mouse embryos identifies RGS5 as a novel marker for pericytes and vascular smooth muscle cells
    • Bondjers C, Kalén M, Hellström M, Scheidl SJ, Abramsson A, Renner O, Lindahl P, Cho H, Kehrl J, and Betsholtz C (2003) Transcription profiling of platelet-derived growth factor-B-deficient mouse embryos identifies RGS5 as a novel marker for pericytes and vascular smooth muscle cells. Am J Pathol 162: 721-729.
    • (2003) Am J Pathol , vol.162 , pp. 721-729
    • Bondjers, C.1    Kalén, M.2    Hellström, M.3    Scheidl, S.J.4    Abramsson, A.5    Renner, O.6    Lindahl, P.7    Cho, H.8    Kehrl, J.9    Betsholtz, C.10
  • 21
    • 0021993452 scopus 로고
    • GTPase activity of the stimulatory GTP-binding regulatory protein of adenylate cyclase, Gs. Accumulation and turnover of enzymenucleotide intermediates
    • Brandt DR and Ross EM (1985) GTPase activity of the stimulatory GTP-binding regulatory protein of adenylate cyclase, Gs. Accumulation and turnover of enzymenucleotide intermediates. J Biol Chem 260: 266-272.
    • (1985) J Biol Chem , vol.260 , pp. 266-272
    • Brandt, D.R.1    Ross, E.M.2
  • 22
    • 0023940032 scopus 로고
    • + channel activation as revealed by hydrolysis-resistant GTP analogues
    • + channel activation as revealed by hydrolysis-resistant GTP analogues. J Gen Physiol 91: 469-493.
    • (1988) J Gen Physiol , vol.91 , pp. 469-493
    • Breitwieser, G.E.1    Szabo, G.2
  • 23
    • 78049282918 scopus 로고    scopus 로고
    • Regulation of GPCR signaling in hypertension
    • Brinks HL and Eckhart AD (2010) Regulation of GPCR signaling in hypertension. Biochim Biophys Acta 1802: 1268-1275.
    • (2010) Biochim Biophys Acta , vol.1802 , pp. 1268-1275
    • Brinks, H.L.1    Eckhart, A.D.2
  • 25
    • 0021271862 scopus 로고
    • The interleukin-2 T-cell system: A new cell growth model
    • Cantrell DA and Smith KA (1984) The interleukin-2 T-cell system: a new cell growth model. Science 224: 1312-1316.
    • (1984) Science , vol.224 , pp. 1312-1316
    • Cantrell, D.A.1    Smith, K.A.2
  • 27
    • 0018635486 scopus 로고
    • Determination of the turn-off reaction for the hormone-activated adenylate cyclase
    • Cassel D, Eckstein F, Lowe M, and Selinger Z (1979) Determination of the turn-off reaction for the hormone-activated adenylate cyclase. J Biol Chem 254: 9835-9838.
    • (1979) J Biol Chem , vol.254 , pp. 9835-9838
    • Cassel, D.1    Eckstein, F.2    Lowe, M.3    Selinger, Z.4
  • 28
    • 0020040057 scopus 로고
    • Isolation and genetic analysis of Saccharomyces cerevisiae mutants supersensitive to G1 arrest by a factor and alpha factor pheromones
    • Chan RK and Otte CA (1982a) Isolation and genetic analysis of Saccharomyces cerevisiae mutants supersensitive to G1 arrest by a factor and alpha factor pheromones. Mol Cell Biol 2: 11-20.
    • (1982) Mol Cell Biol , vol.2 , pp. 11-20
    • Chan, R.K.1    Otte, C.A.2
  • 29
    • 0020039329 scopus 로고
    • Physiological characterization of Saccharomyces cerevisiae mutants supersensitive to G1 arrest by a factor and alpha factor pheromones
    • Chan RK and Otte CA (1982b) Physiological characterization of Saccharomyces cerevisiae mutants supersensitive to G1 arrest by a factor and alpha factor pheromones. Mol Cell Biol 2: 21-29.
    • (1982) Mol Cell Biol , vol.2 , pp. 21-29
    • Chan, R.K.1    Otte, C.A.2
  • 30
    • 4344596204 scopus 로고    scopus 로고
    • RGS proteins: G protein-coupled receptors meet their match
    • Chasse SA and Dohlman HG (2003) RGS proteins: G protein-coupled receptors meet their match. Assay Drug Dev Technol 1: 357-364.
    • (2003) Assay Drug Dev Technol , vol.1 , pp. 357-364
    • Chasse, S.A.1    Dohlman, H.G.2
  • 31
    • 4344607648 scopus 로고    scopus 로고
    • Endogenous RGS proteins regulate presynaptic and postsynaptic function: Functional expression of RGS-insensitive Galpha subunits in central nervous system neurons
    • Chen H, Clark MA, and Lambert NA (2004) Endogenous RGS proteins regulate presynaptic and postsynaptic function: functional expression of RGS-insensitive Galpha subunits in central nervous system neurons. Methods Enzymol 389: 190-204.
    • (2004) Methods Enzymol , vol.389 , pp. 190-204
    • Chen, H.1    Clark, M.A.2    Lambert, N.A.3
  • 32
    • 15544373780 scopus 로고    scopus 로고
    • Structure of the p115RhoGEF rgRGS domain-Galpha13/i1 chimera complex suggests convergent evolution of a GTPase activator
    • Chen Z, Singer WD, Sternweis PC, and Sprang SR (2005) Structure of the p115RhoGEF rgRGS domain-Galpha13/i1 chimera complex suggests convergent evolution of a GTPase activator. Nat Struct Mol Biol 12: 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
  • 33
    • 3142511068 scopus 로고    scopus 로고
    • Regulators of G protein signaling: Potential drug targets for controlling cardiovascular and immune function
    • Cho H, Harrison K, and Kehrl JH (2004) Regulators of G protein signaling: potential drug targets for controlling cardiovascular and immune function. Curr Drug Targets Immune Endocr Metabol Disord 4: 107-118.
    • (2004) Curr Drug Targets Immune Endocr Metabol Disord , vol.4 , pp. 107-118
    • Cho, H.1    Harrison, K.2    Kehrl, J.H.3
  • 34
    • 0037365902 scopus 로고    scopus 로고
    • Pericyte-specific expression of Rgs5: Implications for PDGF and EDG receptor signaling during vascular maturation
    • Cho H, Kozasa T, Bondjers C, Betsholtz C, and Kehrl JH (2003) Pericyte-specific expression of Rgs5: implications for PDGF and EDG receptor signaling during vascular maturation. FASEB J 17: 440-442.
    • (2003) FASEB J , vol.17 , pp. 440-442
    • Cho, H.1    Kozasa, T.2    Bondjers, C.3    Betsholtz, C.4    Kehrl, J.H.5
  • 38
    • 4344691146 scopus 로고    scopus 로고
    • Assays for G-protein-coupled receptor signaling using RGS-insensitive Galpha subunits
    • Clark MJ and Traynor JR (2004) Assays for G-protein-coupled receptor signaling using RGS-insensitive Galpha subunits. Methods Enzymol 389: 155-169.
    • (2004) Methods Enzymol , vol.389 , pp. 155-169
    • Clark, M.J.1    Traynor, J.R.2
  • 39
    • 0027965652 scopus 로고
    • Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis
    • Coleman DE, Berghuis AM, Lee E, Linder ME, Gilman AG, and Sprang SR (1994) Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis. Science 265: 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
  • 40
    • 0033546001 scopus 로고    scopus 로고
    • Structure of Gialpha1. GppNHp, autoinhibition in a galpha protein-substrate complex
    • Coleman DE and Sprang SR (1999) Structure of Gialpha1. GppNHp, autoinhibition in a galpha protein-substrate complex. J Biol Chem 274: 16669-16672.
    • (1999) J Biol Chem , vol.274 , pp. 16669-16672
    • Coleman, D.E.1    Sprang, S.R.2
  • 41
    • 0038311995 scopus 로고    scopus 로고
    • Ras family signaling: Therapeutic targeting
    • Cox AD and Der CJ (2002) Ras family signaling: therapeutic targeting. Cancer Biol Ther 1: 599-606.
    • (2002) Cancer Biol Ther , vol.1 , pp. 599-606
    • Cox, A.D.1    Der, C.J.2
  • 44
    • 0029559788 scopus 로고
    • GAIP, a protein that specifically interacts with the trimeric G protein G alpha i3, is a member of a protein family with a highly conserved core domain
    • De Vries L, Mousli M, Wurmser A, and Farquhar MG (1995) GAIP, a protein that specifically interacts with the trimeric G protein G alpha i3, is a member of a protein family with a highly conserved core domain. Proc Natl Acad Sci USA 92: 11916-11920.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 11916-11920
    • de Vries, L.1    Mousli, M.2    Wurmser, A.3    Farquhar, M.G.4
  • 45
    • 0029011084 scopus 로고
    • G protein-coupled receptor systems involved in cell growth and oncogenesis
    • Dhanasekaran N, Heasley LE, and Johnson GL (1995) G protein-coupled receptor systems involved in cell growth and oncogenesis. Endocr Rev 16: 259-270.
    • (1995) Endocr Rev , vol.16 , pp. 259-270
    • Dhanasekaran, N.1    Heasley, L.E.2    Johnson, G.L.3
  • 47
    • 0023664976 scopus 로고
    • The yeast SCG1 gene: A G alpha-like protein implicated in the a-and alpha-factor response pathway
    • Dietzel C and Kurjan J (1987) The yeast SCG1 gene: a G alpha-like protein implicated in the a-and alpha-factor response pathway. Cell 50: 1001-1010.
    • (1987) Cell , vol.50 , pp. 1001-1010
    • Dietzel, C.1    Kurjan, J.2
  • 48
    • 0029058433 scopus 로고
    • Inhibition of G-protein signaling by dominant gain-of-function mutations in Sst2p, a pheromone desensitization factor in Saccharomyces cerevisiae
    • Dohlman HG, Apaniesk D, Chen Y, Song J, and Nusskern D (1995) Inhibition of G-protein signaling by dominant gain-of-function mutations in Sst2p, a pheromone desensitization factor in Saccharomyces cerevisiae. Mol Cell Biol 15: 3635-3643.
    • (1995) Mol Cell Biol , vol.15 , pp. 3635-3643
    • Dohlman, H.G.1    Apaniesk, D.2    Chen, Y.3    Song, J.4    Nusskern, D.5
  • 49
    • 33846474121 scopus 로고    scopus 로고
    • G-protein-coupled receptors and cancer
    • Dorsam RT and Gutkind JS (2007) G-protein-coupled receptors and cancer. Nat Rev Cancer 7: 79-94.
    • (2007) Nat Rev Cancer , vol.7 , pp. 79-94
    • Dorsam, R.T.1    Gutkind, J.S.2
  • 51
    • 0030029727 scopus 로고    scopus 로고
    • Inhibition of G-proteinmediated MAP kinase activation by a new mammalian gene family
    • Druey KM, Blumer KJ, Kang VH, and Kehrl JH (1996) Inhibition of G-proteinmediated MAP kinase activation by a new mammalian gene family. Nature 379: 742-746.
    • (1996) Nature , vol.379 , pp. 742-746
    • Druey, K.M.1    Blumer, K.J.2    Kang, V.H.3    Kehrl, J.H.4
  • 52
    • 76349106146 scopus 로고    scopus 로고
    • Mapping cardiac pacemaker circuits: Methodological puzzles of the sinoatrial node optical mapping
    • Efimov IR, Fedorov VV, Joung B, and Lin SF (2010) Mapping cardiac pacemaker circuits: methodological puzzles of the sinoatrial node optical mapping. Circ Res 106: 255-271.
    • (2010) Circ Res , vol.106 , pp. 255-271
    • Efimov, I.R.1    Fedorov, V.V.2    Joung, B.3    Lin, S.F.4
  • 53
    • 0035968248 scopus 로고    scopus 로고
    • Gbeta gamma isoforms selectively rescue plasma membrane localization and palmitoylation of mutant Galphas and Galphaq
    • Evanko DS, Thiyagarajan MM, Siderovski DP, and Wedegaertner PB (2001) Gbeta gamma isoforms selectively rescue plasma membrane localization and palmitoylation of mutant Galphas and Galphaq. J Biol Chem 276: 23945-23953.
    • (2001) J Biol Chem , vol.276 , pp. 23945-23953
    • Evanko, D.S.1    Thiyagarajan, M.M.2    Siderovski, D.P.3    Wedegaertner, P.B.4
  • 54
    • 0023885845 scopus 로고
    • Relationship among guanine nucleotide exchange, GTP hydrolysis, and transforming potential of mutated ras proteins
    • Feig LA and Cooper GM (1988) Relationship among guanine nucleotide exchange, GTP hydrolysis, and transforming potential of mutated ras proteins. Mol Cell Biol 8: 2472-2478.
    • (1988) Mol Cell Biol , vol.8 , pp. 2472-2478
    • Feig, L.A.1    Cooper, G.M.2
  • 57
    • 0038024615 scopus 로고    scopus 로고
    • The G-proteincoupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints
    • Fredriksson R, Lagerström MC, Lundin LG, and Schiöth HB (2003) The G-proteincoupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints. Mol Pharmacol 63: 1256-1272.
    • (2003) Mol Pharmacol , vol.63 , pp. 1256-1272
    • Fredriksson, R.1    Lagerström, M.C.2    Lundin, L.G.3    Schiöth, H.B.4
  • 58
    • 77249142404 scopus 로고    scopus 로고
    • The art of the chemical probe
    • Frye SV (2010) The art of the chemical probe. Nat Chem Biol 6: 159-161.
    • (2010) Nat Chem Biol , vol.6 , pp. 159-161
    • Frye, S.V.1
  • 59
    • 34250855036 scopus 로고    scopus 로고
    • Endogenous RGS proteins modulate SA and AV nodal functions in isolated heart: Implications for sick sinus syndrome and AV block
    • Fu Y, Huang X, Piao L, Lopatin AN, and Neubig RR (2007) Endogenous RGS proteins modulate SA and AV nodal functions in isolated heart: implications for sick sinus syndrome and AV block. Am J Physiol Heart Circ Physiol 292: H2532-H2539.
    • (2007) Am J Physiol Heart Circ Physiol , vol.292
    • Fu, Y.1    Huang, X.2    Piao, L.3    Lopatin, A.N.4    Neubig, R.R.5
  • 60
    • 33645280654 scopus 로고    scopus 로고
    • Endogenous RGS proteins and Galpha subtypes differentially control muscarinic and adenosine-mediated chronotropic effects
    • Fu Y, Huang X, Zhong H, Mortensen RM, D'Alecy LG, and Neubig RR (2006) Endogenous RGS proteins and Galpha subtypes differentially control muscarinic and adenosine-mediated chronotropic effects. Circ Res 98: 659-666.
    • (2006) Circ Res , vol.98 , pp. 659-666
    • Fu, Y.1    Huang, X.2    Zhong, H.3    Mortensen, R.M.4    D'Alecy, L.G.5    Neubig, R.R.6
  • 62
    • 0035952680 scopus 로고    scopus 로고
    • RGS-containing RhoGEFs: The missing link between transforming G proteins and Rho?
    • Fukuhara S, Chikumi H, and Gutkind JS (2001) RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho? Oncogene 20: 1661-1668.
    • (2001) Oncogene , vol.20 , pp. 1661-1668
    • Fukuhara, S.1    Chikumi, H.2    Gutkind, J.S.3
  • 63
    • 79958287784 scopus 로고    scopus 로고
    • Molecular basis of a novel oncogenic mutation in GNAO1
    • doi:10.1038/onc.2010.645
    • Garcia-Marcos M, Ghosh P, and Farquhar MG (2011) Molecular basis of a novel oncogenic mutation in GNAO1. Oncogene doi:10.1038/onc.2010.645.
    • (2011) Oncogene
    • Garcia-Marcos, M.1    Ghosh, P.2    Farquhar, M.G.3
  • 64
    • 0030297912 scopus 로고    scopus 로고
    • Crystal structure at 2.4 angstroms resolution of the complex of transducin betagamma and its regulator, phosducin
    • Gaudet R, Bohm A, and Sigler PB (1996) Crystal structure at 2.4 angstroms resolution of the complex of transducin betagamma and its regulator, phosducin. Cell 87: 577-588.
    • (1996) Cell , vol.87 , pp. 577-588
    • Gaudet, R.1    Bohm, A.2    Sigler, P.B.3
  • 65
    • 0025967969 scopus 로고
    • A malachite green colorimetric assay for protein phosphatase activity
    • Geladopoulos TP, Sotiroudis TG, and Evangelopoulos AE (1991) A malachite green colorimetric assay for protein phosphatase activity. Anal Biochem 192: 112-116.
    • (1991) Anal Biochem , vol.192 , pp. 112-116
    • Geladopoulos, T.P.1    Sotiroudis, T.G.2    Evangelopoulos, A.E.3
  • 66
    • 61849130484 scopus 로고    scopus 로고
    • The tyrosine kinase network regulating mast cell activation
    • Gilfillan AM and Rivera J (2009) The tyrosine kinase network regulating mast cell activation. Immunol Rev 228: 149-169.
    • (2009) Immunol Rev , vol.228 , pp. 149-169
    • Gilfillan, A.M.1    Rivera, J.2
  • 67
    • 0023062991 scopus 로고
    • G proteins: Transducers of receptor-generated signals
    • Gilman AG (1987) G proteins: transducers of receptor-generated signals. Annu Rev Biochem 56: 615-649.
    • (1987) Annu Rev Biochem , vol.56 , pp. 615-649
    • Gilman, A.G.1
  • 70
    • 41149104014 scopus 로고    scopus 로고
    • The RGS2 gene product from a candidate hypertension allele shows decreased plasma membrane association and inhibition of Gq
    • Gu S, Tirgari S, and Heximer SP (2008) The RGS2 gene product from a candidate hypertension allele shows decreased plasma membrane association and inhibition of Gq. Mol Pharmacol 73: 1037-1043.
    • (2008) Mol Pharmacol , vol.73 , pp. 1037-1043
    • Gu, S.1    Tirgari, S.2    Heximer, S.P.3
  • 73
    • 0026727210 scopus 로고
    • G-protein-regulated phospholipase C. Identification of component proteins
    • Harden TK (1992) G-protein-regulated phospholipase C. Identification of component proteins. Adv Second Messenger Phosphoprotein Res 26: 11-34.
    • (1992) Adv Second Messenger Phosphoprotein Res , vol.26 , pp. 11-34
    • Harden, T.K.1
  • 74
    • 48949087161 scopus 로고    scopus 로고
    • GPCR signalling in hypertension: Role of GRKs
    • (Lond)
    • Harris DM, Cohn HI, Pesant S, and Eckhart AD (2008) GPCR signalling in hypertension: role of GRKs. Clin Sci (Lond) 115: 79-89.
    • (2008) Clin Sci , vol.115 , pp. 79-89
    • Harris, D.M.1    Cohn, H.I.2    Pesant, S.3    Eckhart, A.D.4
  • 75
    • 0018928567 scopus 로고
    • Mutants of Saccharomyces cerevisiae unresponsive to cell division control by polypeptide mating hormone
    • Hartwell LH (1980) Mutants of Saccharomyces cerevisiae unresponsive to cell division control by polypeptide mating hormone. J Cell Biol 85: 811-822.
    • (1980) J Cell Biol , vol.85 , pp. 811-822
    • Hartwell, L.H.1
  • 76
    • 0031936503 scopus 로고    scopus 로고
    • RGS9, a GTPase accelerator for phototransduction
    • He W, Cowan CW, and Wensel TG (1998) RGS9, a GTPase accelerator for phototransduction. Neuron 20: 95-102.
    • (1998) Neuron , vol.20 , pp. 95-102
    • He, W.1    Cowan, C.W.2    Wensel, T.G.3
  • 77
    • 0031017573 scopus 로고    scopus 로고
    • RGS4 and GAIP are GTPase-activating proteins for Gq alpha and block activation of phospholipase C beta by gamma-thio-GTP-Gq alpha
    • Hepler JR, Berman DM, Gilman AG, and Kozasa T (1997) RGS4 and GAIP are GTPase-activating proteins for Gq alpha and block activation of phospholipase C beta by gamma-thio-GTP-Gq alpha. Proc Natl Acad Sci USA 94: 428-432.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 428-432
    • Hepler, J.R.1    Berman, D.M.2    Gilman, A.G.3    Kozasa, T.4
  • 78
    • 0030953246 scopus 로고    scopus 로고
    • Comparison of mRNA expression of two regulators of G-protein signaling, RGS1/BL34/1R20 and RGS2/G0S8, in cultured human blood mononuclear cells
    • Heximer SP, Cristillo AD, and Forsdyke DR (1997a) Comparison of mRNA expression of two regulators of G-protein signaling, RGS1/BL34/1R20 and RGS2/G0S8, in cultured human blood mononuclear cells. DNA Cell Biol 16: 589-598.
    • (1997) DNA Cell Biol , vol.16 , pp. 589-598
    • Heximer, S.P.1    Cristillo, A.D.2    Forsdyke, D.R.3
  • 81
    • 0023164972 scopus 로고
    • Effects of Mg2+ and the beta gamma-subunit complex on the interactions of guanine nucleotides with G proteins
    • Higashijima T, Ferguson KM, Sternweis PC, Smigel MD, and Gilman AG (1987) Effects of Mg2+ and the beta gamma-subunit complex on the interactions of guanine nucleotides with G proteins. J Biol Chem 262: 762-766.
    • (1987) J Biol Chem , vol.262 , pp. 762-766
    • Higashijima, T.1    Ferguson, K.M.2    Sternweis, P.C.3    Smigel, M.D.4    Gilman, A.G.5
  • 83
    • 38449106109 scopus 로고    scopus 로고
    • Resistance to diet-induced obesity and improved insulin sensitivity in mice with a regulator of G protein signaling-insensitive G184S Gnai2 allele
    • Huang X, Charbeneau RA, Fu Y, Kaur K, Gerin I, MacDougald OA, and Neubig RR (2008) Resistance to diet-induced obesity and improved insulin sensitivity in mice with a regulator of G protein signaling-insensitive G184S Gnai2 allele. Diabetes 57: 77-85.
    • (2008) Diabetes , vol.57 , pp. 77-85
    • Huang, X.1    Charbeneau, R.A.2    Fu, Y.3    Kaur, K.4    Gerin, I.5    McDougald, O.A.6    Neubig, R.R.7
  • 85
    • 0029830014 scopus 로고    scopus 로고
    • RGS10 is a selective activator of G alpha i GTPase activity
    • Hunt TW, Fields TA, Casey PJ, and Peralta EG (1996) RGS10 is a selective activator of G alpha i GTPase activity. Nature 383: 175-177.
    • (1996) Nature , vol.383 , pp. 175-177
    • Hunt, T.W.1    Fields, T.A.2    Casey, P.J.3    Peralta, E.G.4
  • 86
    • 70349473057 scopus 로고    scopus 로고
    • Regulator of G-protein signaling (RGS) proteins in cancer biology
    • Hurst JH and Hooks SB (2009) Regulator of G-protein signaling (RGS) proteins in cancer biology. Biochem Pharmacol 78: 1289-1297.
    • (2009) Biochem Pharmacol , vol.78 , pp. 1289-1297
    • Hurst, J.H.1    Hooks, S.B.2
  • 87
    • 34249886323 scopus 로고    scopus 로고
    • Development of a Transcreener kinase assay for protein kinase A and demonstration of concordance of data with a filter-binding assay format
    • Huss KL, Blonigen PE, and Campbell RM (2007) Development of a Transcreener kinase assay for protein kinase A and demonstration of concordance of data with a filter-binding assay format. J Biomol Screen 12: 578-584.
    • (2007) J Biomol Screen , vol.12 , pp. 578-584
    • Huss, K.L.1    Blonigen, P.E.2    Campbell, R.M.3
  • 88
    • 70350736250 scopus 로고    scopus 로고
    • Isofluraneinduced changes in righting response and breathing are modulated by RGS proteins
    • Icaza EE, Huang X, Fu Y, Neubig RR, Baghdoyan HA, and Lydic R (2009) Isofluraneinduced changes in righting response and breathing are modulated by RGS proteins. Anesth Analg 109: 1500-1505.
    • (2009) Anesth Analg , vol.109 , pp. 1500-1505
    • Icaza, E.E.1    Huang, X.2    Fu, Y.3    Neubig, R.R.4    Baghdoyan, H.A.5    Lydic, R.6
  • 89
    • 4344653893 scopus 로고    scopus 로고
    • Use of RGS-insensitive Galpha subunits to study endogenous RGS protein action on G-protein modulation of N-type calcium channels in sympathetic neurons
    • Ikeda SR and Jeong SW (2004) Use of RGS-insensitive Galpha subunits to study endogenous RGS protein action on G-protein modulation of N-type calcium channels in sympathetic neurons. Methods Enzymol 389: 170-189.
    • (2004) Methods Enzymol , vol.389 , pp. 170-189
    • Ikeda, S.R.1    Jeong, S.W.2
  • 90
    • 12744274775 scopus 로고    scopus 로고
    • 2+/calmodulin competitively bind to the regulators of G-protein-signalling (RGS) domain of RGS4 and reciprocally regulate its action
    • 2+/calmodulin competitively bind to the regulators of G-protein-signalling (RGS) domain of RGS4 and reciprocally regulate its action. Biochem J 385: 65-73.
    • (2005) Biochem J , vol.385 , pp. 65-73
    • Ishii, M.1    Fujita, S.2    Yamada, M.3    Hosaka, Y.4    Kurachi, Y.5
  • 91
    • 0035941424 scopus 로고    scopus 로고
    • Ca(2+) elevation evoked by membrane depolarization regulates G protein cycle via RGS proteins in the heart
    • Ishii M, Inanobe A, Fujita S, Makino Y, Hosoya Y, and Kurachi Y (2001) Ca(2+) elevation evoked by membrane depolarization regulates G protein cycle via RGS proteins in the heart. Circ Res 89: 1045-1050.
    • (2001) Circ Res , vol.89 , pp. 1045-1050
    • Ishii, M.1    Inanobe, A.2    Fujita, S.3    Makino, Y.4    Hosoya, Y.5    Kurachi, Y.6
  • 93
    • 0242384221 scopus 로고    scopus 로고
    • Physiological actions of regulators of G-protein signaling (RGS) proteins
    • Ishii M and Kurachi Y (2003) Physiological actions of regulators of G-protein signaling (RGS) proteins. Life Sci 74: 163-171.
    • (2003) Life Sci , vol.74 , pp. 163-171
    • Ishii, M.1    Kurachi, Y.2
  • 94
    • 4344561709 scopus 로고    scopus 로고
    • Assays of RGS protein modulation by phosphatidylinositides and calmodulin
    • Ishii M and Kurachi Y (2004) Assays of RGS protein modulation by phosphatidylinositides and calmodulin. Methods Enzymol 389: 105-118.
    • (2004) Methods Enzymol , vol.389 , pp. 105-118
    • Ishii, M.1    Kurachi, Y.2
  • 98
    • 34547157646 scopus 로고    scopus 로고
    • Receptor-mediated activation of heterotrimeric G-proteins: Current structural insights
    • Johnston CA and Siderovski DP (2007) Receptor-mediated activation of heterotrimeric G-proteins: current structural insights. Mol Pharmacol 72: 219-230.
    • (2007) Mol Pharmacol , vol.72 , pp. 219-230
    • Johnston, C.A.1    Siderovski, D.P.2
  • 99
  • 100
    • 0034255279 scopus 로고    scopus 로고
    • A voltage-independent calcium current inhibitory pathway activated by muscarinic agonists in rat sympathetic neurons requires both Galpha q/11 and Gbeta gamma
    • Kammermeier PJ, Ruiz-Velasco V, and Ikeda SR (2000) A voltage-independent calcium current inhibitory pathway activated by muscarinic agonists in rat sympathetic neurons requires both Galpha q/11 and Gbeta gamma. J Neurosci 20: 5623-5629.
    • (2000) J Neurosci , vol.20 , pp. 5623-5629
    • Kammermeier, P.J.1    Ruiz-Velasco, V.2    Ikeda, S.R.3
  • 102
    • 0036015208 scopus 로고    scopus 로고
    • Additional 5′ exons in the RGS3 locus generate multiple mRNA transcripts, one of which accounts for the origin of human PDZ-RGS3
    • Kehrl JH, Srikumar D, Harrison K, Wilson GL, and Shi CS (2002) Additional 5′ exons in the RGS3 locus generate multiple mRNA transcripts, one of which accounts for the origin of human PDZ-RGS3. Genomics 79: 860-868.
    • (2002) Genomics , vol.79 , pp. 860-868
    • Kehrl, J.H.1    Srikumar, D.2    Harrison, K.3    Wilson, G.L.4    Shi, C.S.5
  • 106
    • 0035800830 scopus 로고    scopus 로고
    • RGS12 and RGS14 GoLoco motifs are G alpha(i) interaction sites with guanine nucleotide dissociation inhibitor Activity
    • Kimple RJ, De Vries L, Tronchère H, Behe CI, Morris RA, Gist Farquhar M, and Siderovski DP (2001) RGS12 and RGS14 GoLoco motifs are G alpha(i) interaction sites with guanine nucleotide dissociation inhibitor Activity. J Biol Chem 276: 29275-29281.
    • (2001) J Biol Chem , vol.276 , pp. 29275-29281
    • Kimple, R.J.1    de Vries, L.2    Tronchère, H.3    Behe, C.I.4    Morris, R.A.5    Gist Farquhar, M.6    Siderovski, D.P.7
  • 107
    • 0032970154 scopus 로고    scopus 로고
    • The high-affinity IgE receptor (Fc epsilon RI): From physiology to pathology
    • Kinet JP (1999) The high-affinity IgE receptor (Fc epsilon RI): from physiology to pathology. Annu Rev Immunol 17: 931-972.
    • (1999) Annu Rev Immunol , vol.17 , pp. 931-972
    • Kinet, J.P.1
  • 111
    • 0030032001 scopus 로고    scopus 로고
    • EGL-10 regulates G protein signaling in the C. elegans nervous system and shares a conserved domain with many mammalian proteins
    • Koelle MR and Horvitz HR (1996) EGL-10 regulates G protein signaling in the C. elegans nervous system and shares a conserved domain with many mammalian proteins. Cell 84: 115-125.
    • (1996) Cell , vol.84 , pp. 115-125
    • Koelle, M.R.1    Horvitz, H.R.2
  • 114
    • 42149181885 scopus 로고    scopus 로고
    • Structural diversity of G protein-coupled receptors and significance for drug discovery
    • Lagerström MC and Schiöth HB (2008) Structural diversity of G protein-coupled receptors and significance for drug discovery. Nat Rev Drug Discov 7: 339-357.
    • (2008) Nat Rev Drug Discov , vol.7 , pp. 339-357
    • Lagerström, M.C.1    Schiöth, H.B.2
  • 115
  • 116
    • 0028237708 scopus 로고
    • Structural determinants for activation of the alpha-subunit of a heterotrimeric G protein
    • Lambright DG, Noel JP, Hamm HE, and Sigler PB (1994) Structural determinants for activation of the alpha-subunit of a heterotrimeric G protein. Nature 369: 621-628.
    • (1994) Nature , vol.369 , pp. 621-628
    • Lambright, D.G.1    Noel, J.P.2    Hamm, H.E.3    Sigler, P.B.4
  • 117
  • 118
    • 0024404145 scopus 로고
    • GTPase inhibiting mutations activate the alpha chain of Gs and stimulate adenylyl cyclase in human pituitary tumours
    • Landis CA, Masters SB, Spada A, Pace AM, Bourne HR, and Vallar L (1989) GTPase inhibiting mutations activate the alpha chain of Gs and stimulate adenylyl cyclase in human pituitary tumours. Nature 340: 692-696.
    • (1989) Nature , vol.340 , pp. 692-696
    • Landis, C.A.1    Masters, S.B.2    Spada, A.3    Pace, A.M.4    Bourne, H.R.5    Vallar, L.6
  • 119
    • 3042523825 scopus 로고    scopus 로고
    • AGS proteins, GPR motifs and the signals processed by heterotrimeric G proteins
    • Lanier SM (2004) AGS proteins, GPR motifs and the signals processed by heterotrimeric G proteins. Biol Cell 96: 369-372.
    • (2004) Biol Cell , vol.96 , pp. 369-372
    • Lanier, S.M.1
  • 120
    • 77956609549 scopus 로고    scopus 로고
    • RNA interference screen for RGS protein specificity at muscarinic and protease-activated receptors reveals bidirectional modulation of signaling
    • Laroche G, Giguère PM, Roth BL, Trejo J, and Siderovski DP (2010) RNA interference screen for RGS protein specificity at muscarinic and protease-activated receptors reveals bidirectional modulation of signaling. Am J Physiol Cell Physiol 299: C654-C664.
    • (2010) Am J Physiol Cell Physiol , vol.299
    • Laroche, G.1    Giguère, P.M.2    Roth, B.L.3    Trejo, J.4    Siderovski, D.P.5
  • 121
    • 58149194624 scopus 로고    scopus 로고
    • SMART 6: Recent updates and new developments
    • Letunic I, Doerks T, and Bork P (2009) SMART 6: recent updates and new developments. Nucleic Acids Res 37: D229-232.
    • (2009) Nucleic Acids Res , vol.37
    • Letunic, I.1    Doerks, T.2    Bork, P.3
  • 123
    • 2442474029 scopus 로고    scopus 로고
    • G protein-coupled receptors and their signaling pathways: Classical therapeutical targets susceptible to novel therapeutic concepts
    • Liebmann C (2004) G protein-coupled receptors and their signaling pathways: classical therapeutical targets susceptible to novel therapeutic concepts. Curr Pharm Des 10: 1937-1958.
    • (2004) Curr Pharm Des , vol.10 , pp. 1937-1958
    • Liebmann, C.1
  • 124
    • 34247589126 scopus 로고    scopus 로고
    • Discovery of acetyl-coenzyme A carboxylase 2 inhibitors: Comparison of a fluorescence intensity-based phosphate assay and a fluorescence polarization-based ADP Assay for high-throughput screening
    • Liu Y, Zalameda L, Kim KW, Wang M, and McCarter JD (2007) Discovery of acetyl-coenzyme A carboxylase 2 inhibitors: comparison of a fluorescence intensity-based phosphate assay and a fluorescence polarization-based ADP Assay for high-throughput screening. Assay Drug Dev Technol 5: 225-235.
    • (2007) Assay Drug Dev Technol , vol.5 , pp. 225-235
    • Liu, Y.1    Zalameda, L.2    Kim, K.W.3    Wang, M.4    McCarter, J.D.5
  • 125
    • 0037799206 scopus 로고    scopus 로고
    • Keeping G proteins at bay: A complex between G protein-coupled receptor kinase 2 and Gbetagamma
    • Lodowski DT, Pitcher JA, Capel WD, Lefkowitz RJ, and Tesmer JJ (2003) Keeping G proteins at bay: a complex between G protein-coupled receptor kinase 2 and Gbetagamma. Science 300: 1256-1262.
    • (2003) Science , vol.300 , pp. 1256-1262
    • Lodowski, D.T.1    Pitcher, J.A.2    Capel, W.D.3    Lefkowitz, R.J.4    Tesmer, J.J.5
  • 129
    • 0033515040 scopus 로고    scopus 로고
    • The GTPase activating factor for transducin in rod photoreceptors is the complex between RGS9 and type 5 G protein beta subunit
    • Makino ER, Handy JW, Li T, and Arshavsky VY (1999) The GTPase activating factor for transducin in rod photoreceptors is the complex between RGS9 and type 5 G protein beta subunit. Proc Natl Acad Sci USA 96: 1947-1952.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 1947-1952
    • Makino, E.R.1    Handy, J.W.2    Li, T.3    Arshavsky, V.Y.4
  • 130
    • 65649110132 scopus 로고    scopus 로고
    • Regulator of G protein signaling 5: A new player in vascular remodeling
    • Manzur M and Ganss R (2009) Regulator of G protein signaling 5: a new player in vascular remodeling. Trends Cardiovasc Med 19: 26-30.
    • (2009) Trends Cardiovasc Med , vol.19 , pp. 26-30
    • Manzur, M.1    Ganss, R.2
  • 131
    • 0346755948 scopus 로고    scopus 로고
    • Rapid activation of transducin by mutations distant from the nucleotide-binding site: Evidence for a mechanistic model of receptor-catalyzed nucleotide exchange by G proteins
    • Marin EP, Krishna AG, and Sakmar TP (2001) Rapid activation of transducin by mutations distant from the nucleotide-binding site: evidence for a mechanistic model of receptor-catalyzed nucleotide exchange by G proteins. J Biol Chem 276: 27400-27405.
    • (2001) J Biol Chem , vol.276 , pp. 27400-27405
    • Marin, E.P.1    Krishna, A.G.2    Sakmar, T.P.3
  • 133
    • 34247481344 scopus 로고    scopus 로고
    • Mast cells-key effector cells in immune responses
    • Metz M and Maurer M (2007) Mast cells-key effector cells in immune responses. Trends Immunol 28: 234-241.
    • (2007) Trends Immunol , vol.28 , pp. 234-241
    • Metz, M.1    Maurer, M.2
  • 134
    • 0035061298 scopus 로고    scopus 로고
    • Diseasespecific changes in regulator of G-protein signaling 4 (RGS4) expression in schizophrenia
    • Mirnics K, Middleton FA, Stanwood GD, Lewis DA, and Levitt P (2001) Diseasespecific changes in regulator of G-protein signaling 4 (RGS4) expression in schizophrenia. Mol Psychiatry 6: 293-301.
    • (2001) Mol Psychiatry , vol.6 , pp. 293-301
    • Mirnics, K.1    Middleton, F.A.2    Stanwood, G.D.3    Lewis, D.A.4    Levitt, P.5
  • 135
    • 33144486942 scopus 로고    scopus 로고
    • Biochemical characterization of RGS14: RGS14 activity towards G-protein alpha subunits is independent of its binding to Rap2A
    • Mittal V and Linder ME (2006) Biochemical characterization of RGS14: RGS14 activity towards G-protein alpha subunits is independent of its binding to Rap2A. Biochem J 394: 309-315.
    • (2006) Biochem J , vol.394 , pp. 309-315
    • Mittal, V.1    Linder, M.E.2
  • 136
    • 0023665139 scopus 로고
    • GPA1, a haploid-specific essential gene, encodes a yeast homolog of mammalian G protein which may be involved in mating factor signal transduction
    • Miyajima I, Nakafuku M, Nakayama N, Brenner C, Miyajima A, Kaibuchi K, Arai K, Kaziro Y, and Matsumoto K (1987) GPA1, a haploid-specific essential gene, encodes a yeast homolog of mammalian G protein which may be involved in mating factor signal transduction. Cell 50: 1011-1019.
    • (1987) Cell , vol.50 , pp. 1011-1019
    • Miyajima, I.1    Nakafuku, M.2    Nakayama, N.3    Brenner, C.4    Miyajima, A.5    Kaibuchi, K.6    Arai, K.7    Kaziro, Y.8    Matsumoto, K.9
  • 137
    • 2942753952 scopus 로고    scopus 로고
    • Abnormal B-cell responses to chemokines, disturbed plasma cell localization, and distorted immune tissue architecture in Rgs1-/-mice
    • Moratz C, Hayman JR, Gu H, and Kehrl JH (2004) Abnormal B-cell responses to chemokines, disturbed plasma cell localization, and distorted immune tissue architecture in Rgs1-/-mice. Mol Cell Biol 24: 5767-5775.
    • (2004) Mol Cell Biol , vol.24 , pp. 5767-5775
    • Moratz, C.1    Hayman, J.R.2    Gu, H.3    Kehrl, J.H.4
  • 138
    • 0348047597 scopus 로고    scopus 로고
    • Crystal structure of ARF1*Sec7 complexed with Brefeldin A and its implications for the guanine nucleotide exchange mechanism
    • Mossessova E, Corpina RA, and Goldberg J (2003) Crystal structure of ARF1*Sec7 complexed with Brefeldin A and its implications for the guanine nucleotide exchange mechanism. Mol Cell 12: 1403-1411.
    • (2003) Mol Cell , vol.12 , pp. 1403-1411
    • Mossessova, E.1    Corpina, R.A.2    Goldberg, J.3
  • 140
    • 0023729456 scopus 로고
    • Role of STE genes in the mating factor signaling pathway mediated by GPA1 in Saccharomyces cerevisiae
    • Nakayama N, Kaziro Y, Arai K, and Matsumoto K (1988) Role of STE genes in the mating factor signaling pathway mediated by GPA1 in Saccharomyces cerevisiae. Mol Cell Biol 8: 3777-3783.
    • (1988) Mol Cell Biol , vol.8 , pp. 3777-3783
    • Nakayama, N.1    Kaziro, Y.2    Arai, K.3    Matsumoto, K.4
  • 141
    • 0036490096 scopus 로고    scopus 로고
    • Regulators of G-protein signalling as new central nervous system drug targets
    • Neubig RR and Siderovski DP (2002) Regulators of G-protein signalling as new central nervous system drug targets. Nat Rev Drug Discov 1: 187-197.
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 187-197
    • Neubig, R.R.1    Siderovski, D.P.2
  • 142
  • 144
    • 0028883514 scopus 로고
    • Significance of Thr182 in the nucleotide-exchange and GTPhydrolysis reactions of the alpha subunit of GTP-binding protein Gi2
    • Nishina H, Nimota K, Kukimoto I, Maehama T, Takahashi K, Hoshino S, Kanaho Y, and Katada T (1995) Significance of Thr182 in the nucleotide-exchange and GTPhydrolysis reactions of the alpha subunit of GTP-binding protein Gi2. J Biochem 118: 1083-1089.
    • (1995) J Biochem , vol.118 , pp. 1083-1089
    • Nishina, H.1    Nimota, K.2    Kukimoto, I.3    Maehama, T.4    Takahashi, K.5    Hoshino, S.6    Kanaho, Y.7    Katada, T.8
  • 145
    • 37549016836 scopus 로고    scopus 로고
    • Heterotrimeric G protein activation by G-protein-coupled receptors
    • Oldham WM and Hamm HE (2008) Heterotrimeric G protein activation by G-protein-coupled receptors. Nat Rev Mol Cell Biol 9: 60-71.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 60-71
    • Oldham, W.M.1    Hamm, H.E.2
  • 149
    • 0030203863 scopus 로고    scopus 로고
    • TreeView: An application to display phylogenetic trees on personal computers
    • Page RD (1996) TreeView: an application to display phylogenetic trees on personal computers. Comput Appl Biosci 12: 357-358.
    • (1996) Comput Appl Biosci , vol.12 , pp. 357-358
    • Page, R.D.1
  • 150
    • 0038102324 scopus 로고    scopus 로고
    • The evolutionarily triumphant G-protein-coupled receptor
    • Perez DM (2003) The evolutionarily triumphant G-protein-coupled receptor. Mol Pharmacol 63: 1202-1205.
    • (2003) Mol Pharmacol , vol.63 , pp. 1202-1205
    • Perez, D.M.1
  • 151
    • 0032751298 scopus 로고    scopus 로고
    • Raf-like Ras/Rap-binding domains in RGS12-and still-life-like signalling proteins
    • Ponting CP (1999) Raf-like Ras/Rap-binding domains in RGS12-and still-life-like signalling proteins. J Mol Med 77: 695-698.
    • (1999) J Mol Med , vol.77 , pp. 695-698
    • Ponting, C.P.1
  • 152
    • 0030738476 scopus 로고    scopus 로고
    • The regulators of G protein signaling (RGS) domains of RGS4, RGS10, and GAIP retain GTPase activating protein activity in vitro
    • Popov S, Yu K, Kozasa T, and Wilkie TM (1997) The regulators of G protein signaling (RGS) domains of RGS4, RGS10, and GAIP retain GTPase activating protein activity in vitro. Proc Natl Acad Sci USA 94: 7216-7220.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 7216-7220
    • Popov, S.1    Yu, K.2    Kozasa, T.3    Wilkie, T.M.4
  • 153
    • 0034705237 scopus 로고    scopus 로고
    • 2+/Calmodulin reverses phosphatidylinositol 3,4,5-trisphosphate-dependent inhibition of regulators of G protein-signaling GTPase-activating protein activity
    • 2+/Calmodulin reverses phosphatidylinositol 3,4,5-trisphosphate-dependent inhibition of regulators of G protein-signaling GTPase-activating protein activity. J Biol Chem 275: 18962-18968.
    • (2000) J Biol Chem , vol.275 , pp. 18962-18968
    • Popov, S.G.1    Krishna, U.M.2    Falck, J.R.3    Wilkie, T.M.4
  • 154
    • 0032695796 scopus 로고    scopus 로고
    • Regulators of G protein signaling 6 and 7. Purification of complexes with gbeta5 and assessment of their effects on g protein-mediated signaling pathways
    • Posner BA, Gilman AG, and Harris BA (1999) Regulators of G protein signaling 6 and 7. Purification of complexes with gbeta5 and assessment of their effects on g protein-mediated signaling pathways. J Biol Chem 274: 31087-31093.
    • (1999) J Biol Chem , vol.274 , pp. 31087-31093
    • Posner, B.A.1    Gilman, A.G.2    Harris, B.A.3
  • 155
    • 0032555296 scopus 로고    scopus 로고
    • The A326S mutant of Gialpha1 as an approximation of the receptor-bound state
    • Posner BA, Mixon MB, Wall MA, Sprang SR, and Gilman AG (1998) The A326S mutant of Gialpha1 as an approximation of the receptor-bound state. J Biol Chem 273: 21752-21758.
    • (1998) J Biol Chem , vol.273 , pp. 21752-21758
    • Posner, B.A.1    Mixon, M.B.2    Wall, M.A.3    Sprang, S.R.4    Gilman, A.G.5
  • 156
    • 78650414238 scopus 로고    scopus 로고
    • RGS6/G → 5 complex accelerates IKACh gating kinetics in atrial myocytes and modulates parasympathetic regulation of heart rate
    • Posokhova E, Wydeven N, Allen KL, Wickman K, and Martemyanov KA (2010) RGS6/G → 5 complex accelerates IKACh gating kinetics in atrial myocytes and modulates parasympathetic regulation of heart rate. Circ Res 107: 1350-1354.
    • (2010) Circ Res , vol.107 , pp. 1350-1354
    • Posokhova, E.1    Wydeven, N.2    Allen, K.L.3    Wickman, K.4    Martemyanov, K.A.5
  • 157
    • 0031471341 scopus 로고    scopus 로고
    • Structural and biochemical characterization of the GTPgammaS-, GDP. Pi-, and GDP-bound forms of a GTPase-deficient Gly423Val mutant of Gialpha1
    • Raw AS, Coleman DE, Gilman AG, and Sprang SR (1997) Structural and biochemical characterization of the GTPgammaS-, GDP. Pi-, and GDP-bound forms of a GTPase-deficient Gly423Val mutant of Gialpha1. Biochemistry 36: 15660-15669.
    • (1997) Biochemistry , vol.36 , pp. 15660-15669
    • Raw, A.S.1    Coleman, D.E.2    Gilman, A.G.3    Sprang, S.R.4
  • 158
    • 0344995242 scopus 로고    scopus 로고
    • Interdomain interactions regulate GDP release from heterotrimeric G proteins
    • Remmers AE, Engel C, Liu M, and Neubig RR (1999) Interdomain interactions regulate GDP release from heterotrimeric G proteins. Biochemistry 38: 13795-13800.
    • (1999) Biochemistry , vol.38 , pp. 13795-13800
    • Remmers, A.E.1    Engel, C.2    Liu, M.3    Neubig, R.R.4
  • 159
    • 0034927336 scopus 로고    scopus 로고
    • Regulation of phosphoinositide-specific phospholipase C
    • Rhee SG (2001) Regulation of phosphoinositide-specific phospholipase C. Annu Rev Biochem 70: 281-312.
    • (2001) Annu Rev Biochem , vol.70 , pp. 281-312
    • Rhee, S.G.1
  • 160
    • 14844343100 scopus 로고    scopus 로고
    • Multi-tasking RGS proteins in the heart: The next therapeutic target?
    • Riddle EL, Schwartzman RA, Bond M, and Insel PA (2005) Multi-tasking RGS proteins in the heart: the next therapeutic target? Circ Res 96: 401-411.
    • (2005) Circ Res , vol.96 , pp. 401-411
    • Riddle, E.L.1    Schwartzman, R.A.2    Bond, M.3    Insel, P.A.4
  • 161
    • 33646933031 scopus 로고    scopus 로고
    • Molecular regulation of mast cell activation
    • quiz 1226
    • Rivera J and Gilfillan AM (2006) Molecular regulation of mast cell activation. J Allergy Clin Immunol 117: 1214-1225; quiz 1226.
    • (2006) J Allergy Clin Immunol , vol.117 , pp. 1214-1225
    • Rivera, J.1    Gilfillan, A.M.2
  • 162
    • 0033626331 scopus 로고    scopus 로고
    • Gbetagamma subunit combinations differentially modulate receptor and effector coupling in vivo
    • Robillard L, Ethier N, Lachance M, and Hébert TE (2000) Gbetagamma subunit combinations differentially modulate receptor and effector coupling in vivo. Cell Signal 12: 673-682.
    • (2000) Cell Signal , vol.12 , pp. 673-682
    • Robillard, L.1    Ethier, N.2    Lachance, M.3    Hébert, T.E.4
  • 163
    • 77956254989 scopus 로고    scopus 로고
    • Allosteric inhibition of the regulator of G protein signaling-Galpha protein-protein interaction by CCG-4986
    • Roman DL, Blazer LL, Monroy CA, and Neubig RR (2010) Allosteric inhibition of the regulator of G protein signaling-Galpha protein-protein interaction by CCG-4986. Mol Pharmacol 78: 360-365.
    • (2010) Mol Pharmacol , vol.78 , pp. 360-365
    • Roman, D.L.1    Blazer, L.L.2    Monroy, C.A.3    Neubig, R.R.4
  • 164
    • 67651070993 scopus 로고    scopus 로고
    • Polyplexed flow cytometry protein interaction assay: A novel high-throughput screening paradigm for RGS protein inhibitors
    • Roman DL, Ota S, and Neubig RR (2009) Polyplexed flow cytometry protein interaction assay: a novel high-throughput screening paradigm for RGS protein inhibitors. J Biomol Screen 14: 610-619.
    • (2009) J Biomol Screen , vol.14 , pp. 610-619
    • Roman, D.L.1    Ota, S.2    Neubig, R.R.3
  • 165
    • 33845301393 scopus 로고    scopus 로고
    • Identification of small-molecule inhibitors of RGS4 using a high-throughput flow cytometry protein interaction assay
    • Roman DL, Talbot JN, Roof RA, Sunahara RK, Traynor JR, and Neubig RR (2007) Identification of small-molecule inhibitors of RGS4 using a high-throughput flow cytometry protein interaction assay. Mol Pharmacol 71: 169-175.
    • (2007) Mol Pharmacol , vol.71 , pp. 169-175
    • Roman, D.L.1    Talbot, J.N.2    Roof, R.A.3    Sunahara, R.K.4    Traynor, J.R.5    Neubig, R.R.6
  • 166
    • 0035719046 scopus 로고    scopus 로고
    • Quantitative assays for GTPase-activating proteins
    • Ross EM (2002) Quantitative assays for GTPase-activating proteins. Methods Enzymol 344: 601-617.
    • (2002) Methods Enzymol , vol.344 , pp. 601-617
    • Ross, E.M.1
  • 168
    • 0037138426 scopus 로고    scopus 로고
    • Transformation of the microvascular system during multistage tumorigenesis
    • Ryschich E, Schmidt J, Hämmerling GJ, Klar E, and Ganss R (2002) Transformation of the microvascular system during multistage tumorigenesis. Int J Cancer 97: 719-725.
    • (2002) Int J Cancer , vol.97 , pp. 719-725
    • Ryschich, E.1    Schmidt, J.2    Hämmerling, G.J.3    Klar, E.4    Ganss, R.5
  • 170
    • 0034111099 scopus 로고    scopus 로고
    • Selective regulation of Gq signaling by G protein-coupled receptor kinase 2: Direct interaction of kinase N terminus with activated Galphaq
    • Sallese M, Mariggiò S, D'Urbano E, Iacovelli L, and De Blasi A (2000) Selective regulation of Gq signaling by G protein-coupled receptor kinase 2: direct interaction of kinase N terminus with activated Galphaq. Mol Pharmacol 57: 826-831.
    • (2000) Mol Pharmacol , vol.57 , pp. 826-831
    • Sallese, M.1    Mariggiò, S.2    D'Urbano, E.3    Iacovelli, L.4    de Blasi, A.5
  • 171
    • 77952391404 scopus 로고    scopus 로고
    • Locoregional management of hepatic metastasis from primary uveal melanoma
    • Sato T (2010) Locoregional management of hepatic metastasis from primary uveal melanoma. Semin Oncol 37: 127-138.
    • (2010) Semin Oncol , vol.37 , pp. 127-138
    • Sato, T.1
  • 173
    • 0035865394 scopus 로고    scopus 로고
    • Evidence that a protein-protein interaction 'hot spot' on heterotrimeric G protein betagamma subunits is used for recognition of a subclass of effectors
    • Scott JK, Huang SF, Gangadhar BP, Samoriski GM, Clapp P, Gross RA, Taussig R, and Smrcka AV (2001) Evidence that a protein-protein interaction 'hot spot' on heterotrimeric G protein betagamma subunits is used for recognition of a subclass of effectors. EMBO J 20: 767-776.
    • (2001) EMBO J , vol.20 , pp. 767-776
    • Scott, J.K.1    Huang, S.F.2    Gangadhar, B.P.3    Samoriski, G.M.4    Clapp, P.5    Gross, R.A.6    Taussig, R.7    Smrcka, A.V.8
  • 175
    • 71349084088 scopus 로고    scopus 로고
    • RGS14 is a multifunctional scaffold that integrates G protein and Ras/Raf MAPkinase signalling pathways
    • Shu FJ, Ramineni S, and Hepler JR (2010) RGS14 is a multifunctional scaffold that integrates G protein and Ras/Raf MAPkinase signalling pathways. Cell Signal 22: 366-376.
    • (2010) Cell Signal , vol.22 , pp. 366-376
    • Shu, F.J.1    Ramineni, S.2    Hepler, J.R.3
  • 176
    • 27744509899 scopus 로고    scopus 로고
    • Real-time in vitro measurement of GTP hydrolysis
    • Shutes A and Der CJ (2005) Real-time in vitro measurement of GTP hydrolysis. Methods 37: 183-189.
    • (2005) Methods , vol.37 , pp. 183-189
    • Shutes, A.1    Der, C.J.2
  • 177
    • 0025155076 scopus 로고
    • A set of human putative lymphocyte G0/G1 switch genes includes genes homologous to rodent cytokine and zinc finger protein-encoding genes
    • Siderovski DP, Blum S, Forsdyke RE, and Forsdyke DR (1990) A set of human putative lymphocyte G0/G1 switch genes includes genes homologous to rodent cytokine and zinc finger protein-encoding genes. DNA Cell Biol 9: 579-587.
    • (1990) DNA Cell Biol , vol.9 , pp. 579-587
    • Siderovski, D.P.1    Blum, S.2    Forsdyke, R.E.3    Forsdyke, D.R.4
  • 178
  • 179
    • 0028109139 scopus 로고
    • A human gene encoding a putative basic helix-loop-helix phosphoprotein whose mRNA increases rapidly in cycloheximide-treated blood mononuclear cells
    • Siderovski DP, Heximer SP, and Forsdyke DR (1994) A human gene encoding a putative basic helix-loop-helix phosphoprotein whose mRNA increases rapidly in cycloheximide-treated blood mononuclear cells. DNA Cell Biol 13: 125-147.
    • (1994) DNA Cell Biol , vol.13 , pp. 125-147
    • Siderovski, D.P.1    Heximer, S.P.2    Forsdyke, D.R.3
  • 182
    • 0033082655 scopus 로고    scopus 로고
    • G protein regulation of adenylate cyclase
    • Simonds WF (1999) G protein regulation of adenylate cyclase. Trends Pharmacol Sci 20: 66-73.
    • (1999) Trends Pharmacol Sci , vol.20 , pp. 66-73
    • Simonds, W.F.1
  • 183
    • 77957240736 scopus 로고    scopus 로고
    • Regulators of G protein signaling proteins as targets for drug discovery
    • Sjögren B, Blazer LL, and Neubig RR (2010) Regulators of G protein signaling proteins as targets for drug discovery. Prog Mol Biol Transl Sci 91: 81-119.
    • (2010) Prog Mol Biol Transl Sci , vol.91 , pp. 81-119
    • Sjögren, B.1    Blazer, L.L.2    Neubig, R.R.3
  • 184
    • 77957235831 scopus 로고    scopus 로고
    • Thinking outside of the "RGS box": New approaches to therapeutic targeting of regulators of G protein signaling
    • Sjögren B and Neubig RR (2010) Thinking outside of the "RGS box": new approaches to therapeutic targeting of regulators of G protein signaling. Mol Pharmacol 78: 550-557.
    • (2010) Mol Pharmacol , vol.78 , pp. 550-557
    • Sjögren, B.1    Neubig, R.R.2
  • 185
    • 0035931919 scopus 로고    scopus 로고
    • Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 A
    • Slep KC, Kercher MA, He W, Cowan CW, Wensel TG, and Sigler PB (2001) Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 A. Nature 409: 1071-1077.
    • (2001) Nature , vol.409 , 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
  • 187
    • 78650301416 scopus 로고    scopus 로고
    • When simple agonism is not enough: Emerging modalities of GPCR ligands
    • Smith NJ, Bennett KA, and Milligan G (2011) When simple agonism is not enough: emerging modalities of GPCR ligands. Mol Cell Endocrinol 331: 241-247.
    • (2011) Mol Cell Endocrinol , vol.331 , pp. 241-247
    • Smith, N.J.1    Bennett, K.A.2    Milligan, G.3
  • 188
    • 0033038913 scopus 로고    scopus 로고
    • Fidelity of G protein beta-subunit association by the G protein gamma-subunit-like domains of RGS6, RGS7, and RGS11
    • Snow BE, Betts L, Mangion J, Sondek J, and Siderovski DP (1999) Fidelity of G protein beta-subunit association by the G protein gamma-subunit-like domains of RGS6, RGS7, and RGS11. Proc Natl Acad Sci USA 96: 6489-6494.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6489-6494
    • Snow, B.E.1    Betts, L.2    Mangion, J.3    Sondek, J.4    Siderovski, D.P.5
  • 191
    • 10044254636 scopus 로고    scopus 로고
    • Viral hijacking of G-protein-coupledreceptor signalling networks
    • Sodhi A, Montaner S, and Gutkind JS (2004) Viral hijacking of G-protein-coupledreceptor signalling networks. Nat Rev Mol Cell Biol 5: 998-1012.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 998-1012
    • Sodhi, A.1    Montaner, S.2    Gutkind, J.S.3
  • 192
    • 0030034646 scopus 로고    scopus 로고
    • Crystal structure of a G-protein beta gamma dimer at 2.1A resolution
    • Sondek J, Bohm A, Lambright DG, Hamm HE, and Sigler PB (1996) Crystal structure of a G-protein beta gamma dimer at 2.1A resolution. Nature 379: 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
  • 193
    • 0028027596 scopus 로고
    • GTPase mechanism of Gproteins from the 1.7-A crystal structure of transducin alpha-GDP-AIF-4
    • Sondek J, Lambright DG, Noel JP, Hamm HE, and Sigler PB (1994) GTPase mechanism of Gproteins from the 1.7-A crystal structure of transducin alpha-GDP-AIF-4. Nature 372: 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
  • 195
    • 0034652331 scopus 로고    scopus 로고
    • A regulator of G protein signaling interaction surface linked to effector specificity
    • Sowa ME, He W, Wensel TG, and Lichtarge O (2000) A regulator of G protein signaling interaction surface linked to effector specificity. Proc Natl Acad Sci USA 97: 1483-1488.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 1483-1488
    • Sowa, M.E.1    He, W.2    Wensel, T.G.3    Lichtarge, O.4
  • 196
    • 1542358991 scopus 로고    scopus 로고
    • Inherited diseases involving g proteins and g protein-coupled receptors
    • Spiegel AM and Weinstein LS (2004) Inherited diseases involving g proteins and g protein-coupled receptors. Annu Rev Med 55: 27-39.
    • (2004) Annu Rev Med , vol.55 , pp. 27-39
    • Spiegel, A.M.1    Weinstein, L.S.2
  • 197
    • 33846196309 scopus 로고    scopus 로고
    • Roles of G-protein-coupled receptor signaling in cancer biology and gene transcription
    • Spiegelberg BD and Hamm HE (2007) Roles of G-protein-coupled receptor signaling in cancer biology and gene transcription. Curr Opin Genet Dev 17: 40-44.
    • (2007) Curr Opin Genet Dev , vol.17 , pp. 40-44
    • Spiegelberg, B.D.1    Hamm, H.E.2
  • 198
    • 0031939692 scopus 로고    scopus 로고
    • Mechanism of RGS4, a GTPase-activating protein for G protein alpha subunits
    • Srinivasa SP, Watson N, Overton MC, and Blumer KJ (1998) Mechanism of RGS4, a GTPase-activating protein for G protein alpha subunits. J Biol Chem 273: 1529-1533.
    • (1998) J Biol Chem , vol.273 , pp. 1529-1533
    • Srinivasa, S.P.1    Watson, N.2    Overton, M.C.3    Blumer, K.J.4
  • 199
    • 79960668514 scopus 로고    scopus 로고
    • Promoter polymorphism of RGS2 gene is associated with change of blood pressure in subjects with antihypertensive treatment: The azelnidipine and temocapril in hypertensive patients with type 2 diabetes study
    • Sugimoto K, Katsuya T, Kamide K, Fujisawa T, Shimaoka I, Ohishi M, Morishita R, Ogihara T, and Rakugi H (2010) Promoter polymorphism of RGS2 gene is associated with change of blood pressure in subjects with antihypertensive treatment: the azelnidipine and temocapril in hypertensive patients with type 2 diabetes study. Int J Hypertens 2010: 196307.
    • (2010) Int J Hypertens , vol.2010 , pp. 196307
    • Sugimoto, K.1    Katsuya, T.2    Kamide, K.3    Fujisawa, T.4    Shimaoka, I.5    Ohishi, M.6    Morishita, R.7    Ogihara, T.8    Rakugi, H.9
  • 201
    • 0037024360 scopus 로고    scopus 로고
    • Identification of G protein-coupled receptor genes from the human genome sequence
    • Takeda S, Kadowaki S, Haga T, Takaesu H, and Mitaku S (2002) Identification of G protein-coupled receptor genes from the human genome sequence. FEBS Lett 520: 97-101.
    • (2002) FEBS Lett , vol.520 , pp. 97-101
    • Takeda, S.1    Kadowaki, S.2    Haga, T.3    Takaesu, H.4    Mitaku, S.5
  • 206
    • 0030982264 scopus 로고    scopus 로고
    • 4+ activated G(i alpha1): Stabilization of the transition state for GTP hydrolysis
    • 4+ activated G(i alpha1): stabilization of the transition state for GTP hydrolysis. Cell 89: 251-261.
    • (1997) Cell , vol.89 , pp. 251-261
    • Tesmer, J.J.1    Berman, D.M.2    Gilman, A.G.3    Sprang, S.R.4
  • 207
    • 2642689663 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha. GTPgammaS
    • Tesmer JJ, Sunahara RK, Gilman AG, and Sprang SR (1997b) Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha. GTPgammaS. Science 278: 1907-1916.
    • (1997) Science , vol.278 , pp. 1907-1916
    • Tesmer, J.J.1    Sunahara, R.K.2    Gilman, A.G.3    Sprang, S.R.4
  • 208
    • 28844463975 scopus 로고    scopus 로고
    • Snapshot of activated G proteins at the membrane: The Galphaq-GRK2-Gbetagamma complex
    • Tesmer VM, Kawano T, Shankaranarayanan A, Kozasa T, and Tesmer JJ (2005) Snapshot of activated G proteins at the membrane: the Galphaq-GRK2-Gbetagamma complex. Science 310: 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.5
  • 209
    • 2442676591 scopus 로고    scopus 로고
    • Uncoupling conformational change from GTP hydrolysis in a heterotrimeric G protein alphasubunit
    • Thomas CJ, Du X, Li P, Wang Y, Ross EM, and Sprang SR (2004) Uncoupling conformational change from GTP hydrolysis in a heterotrimeric G protein alphasubunit. Proc Natl Acad Sci USA 101: 7560-7565.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7560-7565
    • Thomas, C.J.1    Du, X.2    Li, P.3    Wang, Y.4    Ross, E.M.5    Sprang, S.R.6
  • 210
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, and Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 211
    • 77952043572 scopus 로고    scopus 로고
    • RNAi-based therapeutics-current status, challenges and prospects
    • Tiemann K and Rossi JJ (2009) RNAi-based therapeutics-current status, challenges and prospects. EMBO Mol Med 1: 142-151.
    • (2009) EMBO Mol Med , vol.1 , pp. 142-151
    • Tiemann, K.1    Rossi, J.J.2
  • 212
    • 0023619575 scopus 로고
    • A cytoplasmic protein stimulates normal N-ras p21 GTPase, but does not affect oncogenic mutants
    • Trahey M and McCormick F (1987) A cytoplasmic protein stimulates normal N-ras p21 GTPase, but does not affect oncogenic mutants. Science 238: 542-545.
    • (1987) Science , vol.238 , pp. 542-545
    • Trahey, M.1    McCormick, F.2
  • 214
    • 77949286973 scopus 로고    scopus 로고
    • Regulator of G protein-signaling proteins and addictive drugs
    • Traynor J (2010) Regulator of G protein-signaling proteins and addictive drugs. Ann NY Acad Sci 1187: 341-352.
    • (2010) Ann NY Acad Sci , vol.1187 , pp. 341-352
    • Traynor, J.1
  • 215
    • 4344600505 scopus 로고    scopus 로고
    • Allosteric regulation of GAP activity by phospholipids in regulators of G-protein signaling
    • Tu Y and Wilkie TM (2004) Allosteric regulation of GAP activity by phospholipids in regulators of G-protein signaling. Methods Enzymol 389: 89-105.
    • (2004) Methods Enzymol , vol.389 , pp. 89-105
    • Tu, Y.1    Wilkie, T.M.2
  • 216
    • 50849086372 scopus 로고    scopus 로고
    • Coordinate regulation of G protein signaling via dynamic interactions of receptor and GAP
    • Turcotte M, Tang W, and Ross EM (2008) Coordinate regulation of G protein signaling via dynamic interactions of receptor and GAP. PLoS Comput Biol 4: e1000148.
    • (2008) PLoS Comput Biol , vol.4
    • Turcotte, M.1    Tang, W.2    Ross, E.M.3
  • 218
    • 60149087726 scopus 로고    scopus 로고
    • Treatment of melanoma metastases confined to the liver and future perspectives
    • Vahrmeijer AL, van de Velde CJ, Hartgrink HH, and Tollenaar RA (2008) Treatment of melanoma metastases confined to the liver and future perspectives. Dig Surg 25: 467-472.
    • (2008) Dig Surg , vol.25 , pp. 467-472
    • Vahrmeijer, A.L.1    van de Velde, C.J.2    Hartgrink, H.H.3    Tollenaar, R.A.4
  • 221
    • 0023158563 scopus 로고
    • Inorganic and organic phosphate measurements in the nanomolar range
    • Van Veldhoven PP and Mannaerts GP (1987) Inorganic and organic phosphate measurements in the nanomolar range. Anal Biochem 161: 45-48.
    • (1987) Anal Biochem , vol.161 , pp. 45-48
    • van Veldhoven, P.P.1    Mannaerts, G.P.2
  • 223
    • 0035834388 scopus 로고    scopus 로고
    • The guanine nucleotide-binding switch in three dimensions
    • Vetter IR and Wittinghofer A (2001) The guanine nucleotide-binding switch in three dimensions. Science 294: 1299-1304.
    • (2001) Science , vol.294 , pp. 1299-1304
    • Vetter, I.R.1    Wittinghofer, A.2
  • 224
    • 78649743311 scopus 로고    scopus 로고
    • Alterations in metabotropic glutamate receptor 1alpha and regulator of G protein signaling 4 in the prefrontal cortex in schizophrenia
    • Volk DW, Eggan SM, and Lewis DA (2010) Alterations in metabotropic glutamate receptor 1alpha and regulator of G protein signaling 4 in the prefrontal cortex in schizophrenia. Am J Psychiatry 167: 1489-1498.
    • (2010) Am J Psychiatry , vol.167 , pp. 1489-1498
    • Volk, D.W.1    Eggan, S.M.2    Lewis, D.A.3
  • 225
    • 0025938677 scopus 로고
    • Deactivation kinetics of the transduction cascade of vision
    • Vuong TM and Chabre M (1991) Deactivation kinetics of the transduction cascade of vision. Proc Natl Acad Sci USA 88: 9813-9817.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 9813-9817
    • Vuong, T.M.1    Chabre, M.2
  • 228
    • 0032530652 scopus 로고    scopus 로고
    • Structural basis of activity and subunit recognition in G protein heterotrimers
    • Wall MA, Posner BA, and Sprang SR (1998) Structural basis of activity and subunit recognition in G protein heterotrimers. Structure 6: 1169-1183.
    • (1998) Structure , vol.6 , pp. 1169-1183
    • Wall, M.A.1    Posner, B.A.2    Sprang, S.R.3
  • 229
    • 67650563911 scopus 로고    scopus 로고
    • Differential modulation of mu-and delta-opioid receptor agonists by endogenous RGS4 protein in SH-SY5Y cells
    • Wang Q, Liu-Chen LY, and Traynor JR (2009) Differential modulation of mu-and delta-opioid receptor agonists by endogenous RGS4 protein in SH-SY5Y cells. J Biol Chem 284: 18357-18367.
    • (2009) J Biol Chem , vol.284 , pp. 18357-18367
    • Wang, Q.1    Liu-Chen, L.Y.2    Traynor, J.R.3
  • 231
    • 5644247331 scopus 로고    scopus 로고
    • Analysis of RGSZ1 protein interaction with Galphai subunits
    • Wang Y and Young KH (2004) Analysis of RGSZ1 protein interaction with Galphai subunits. Methods Enzymol 390: 31-52.
    • (2004) Methods Enzymol , vol.390 , pp. 31-52
    • Wang, Y.1    Young, K.H.2
  • 232
    • 0029808079 scopus 로고    scopus 로고
    • RGS family members: GTPase-activating proteins for heterotrimeric G-protein alphasubunits
    • Watson N, Linder ME, Druey KM, Kehrl JH, and Blumer KJ (1996) RGS family members: GTPase-activating proteins for heterotrimeric G-protein alphasubunits. Nature 383: 172-175.
    • (1996) Nature , vol.383 , pp. 172-175
    • Watson, N.1    Linder, M.E.2    Druey, K.M.3    Kehrl, J.H.4    Blumer, K.J.5
  • 234
    • 0034666426 scopus 로고    scopus 로고
    • Polarity exchange at the interface of regulators of G protein signaling with G protein alpha-subunits
    • Wieland T, Bahtijari N, Zhou XB, Kleuss C, and Simon MI (2000) Polarity exchange at the interface of regulators of G protein signaling with G protein alpha-subunits. J Biol Chem 275: 28500-28506.
    • (2000) J Biol Chem , vol.275 , pp. 28500-28506
    • Wieland, T.1    Bahtijari, N.2    Zhou, X.B.3    Kleuss, C.4    Simon, M.I.5
  • 235
    • 17444404203 scopus 로고    scopus 로고
    • A direct fluorescence-based assay for RGS domain GTPase accelerating activity
    • Willard FS, Kimple AJ, Johnston CA, and Siderovski DP (2005) A direct fluorescence-based assay for RGS domain GTPase accelerating activity. Anal Biochem 340: 341-351.
    • (2005) Anal Biochem , vol.340 , pp. 341-351
    • Willard, F.S.1    Kimple, A.J.2    Johnston, C.A.3    Siderovski, D.P.4
  • 237
  • 238
    • 4344670030 scopus 로고    scopus 로고
    • Purification and in vitro functional analysis of the Arabidopsis thaliana regulator of G-protein signaling-1
    • Willard FS and Siderovski DP (2004) Purification and in vitro functional analysis of the Arabidopsis thaliana regulator of G-protein signaling-1. Methods Enzymol 389: 320-338.
    • (2004) Methods Enzymol , vol.389 , pp. 320-338
    • Willard, F.S.1    Siderovski, D.P.2
  • 240
    • 34247274512 scopus 로고    scopus 로고
    • Selective role for RGS12 as a Ras/Raf/MEK scaffold in nerve growth factormediated differentiation
    • Willard MD, Willard FS, Li X, Cappell SD, Snider WD, and Siderovski DP (2007) Selective role for RGS12 as a Ras/Raf/MEK scaffold in nerve growth factormediated differentiation. EMBO J 26: 2029-2040.
    • (2007) EMBO J , vol.26 , pp. 2029-2040
    • Willard, M.D.1    Willard, F.S.2    Li, X.3    Cappell, S.D.4    Snider, W.D.5    Siderovski, D.P.6
  • 247
    • 0032560061 scopus 로고    scopus 로고
    • G-protein signaling: Fine-tuning signaling kinetics
    • Zerangue N and Jan LY (1998) G-protein signaling: fine-tuning signaling kinetics. Curr Biol 8: R313-316.
    • (1998) Curr Biol , vol.8
    • Zerangue, N.1    Jan, L.Y.2
  • 248
    • 0034138114 scopus 로고    scopus 로고
    • Copurification of brain G-protein beta5 with RGS6 and RGS7
    • Zhang JH and Simonds WF (2000) Copurification of brain G-protein beta5 with RGS6 and RGS7. J Neurosci 20: RC59.
    • (2000) J Neurosci , vol.20
    • Zhang, J.H.1    Simonds, W.F.2
  • 249
    • 0037470041 scopus 로고    scopus 로고
    • A spatial focusing model for G protein signals. Regulator of G protein signaling (RGS) protein-mediated kinetic scaffolding
    • Zhong H, Wade SM, Woolf PJ, Linderman JJ, Traynor JR, and Neubig RR (2003) A spatial focusing model for G protein signals. Regulator of G protein signaling (RGS) protein-mediated kinetic scaffolding. J Biol Chem 278: 7278-7284.
    • (2003) J Biol Chem , vol.278 , pp. 7278-7284
    • Zhong, H.1    Wade, S.M.2    Woolf, P.J.3    Linderman, J.J.4    Traynor, J.R.5    Neubig, R.R.6
  • 250
    • 71949127119 scopus 로고    scopus 로고
    • Two Galpha(i1) rate-modifying mutations act in concert to allow receptorindependent, steady-state measurements of RGS protein activity
    • Zielinski T, Kimple AJ, Hutsell SQ, Koeff MD, Siderovski DP, and Lowery RG (2009) Two Galpha(i1) rate-modifying mutations act in concert to allow receptorindependent, steady-state measurements of RGS protein activity. J Biomol Screen 14: 1195-1206.
    • (2009) J Biomol Screen , vol.14 , pp. 1195-1206
    • Zielinski, T.1    Kimple, A.J.2    Hutsell, S.Q.3    Koeff, M.D.4    Siderovski, D.P.5    Lowery, R.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.