메뉴 건너뛰기




Volumn 1175, Issue , 2014, Pages 121-152

G protein-coupled receptor accessory proteins and signaling: Pharmacogenomic insights

Author keywords

Accessory proteins; Activator of G protein signaling (AGS); G protein coupled receptor; G protein coupled receptor kinases (GRK); Hypertension; Pharmacogenomics; Regulator of G protein signaling (RGS); Signaling

Indexed keywords

ACCESSORY PROTEIN; G PROTEIN COUPLED RECEPTOR; G PROTEIN COUPLED RECEPTOR KINASE 4; GUANINE NUCLEOTIDE BINDING PROTEIN; PROTEIN; RGS PROTEIN; UNCLASSIFIED DRUG; G PROTEIN COUPLED RECEPTOR KINASE;

EID: 84927630842     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4939-0956-8_7     Document Type: Article
Times cited : (17)

References (207)
  • 1
    • 1542358991 scopus 로고    scopus 로고
    • Inherited diseases involving g proteins and G proteincoupled receptors
    • Spiegel AM, Weinstein LS (2004) Inherited diseases involving g proteins and G proteincoupled receptors. Annu Rev Med 55:27-39
    • (2004) Annu Rev Med , vol.55 , pp. 27-39
    • Spiegel, A.M.1    Weinstein, L.S.2
  • 3
    • 84934443716 scopus 로고    scopus 로고
    • The pharmacogenomics of G protein-coupled receptor signaling
    • Thompson MD, Cole DE, Jose P (2008) The pharmacogenomics of G protein-coupled receptor signaling. Methods Mol Biol 448:77-108
    • (2008) Methods Mol Biol , vol.448 , pp. 77-108
    • Thompson, M.D.1    Cole, D.E.2    Jose, P.3
  • 4
  • 6
    • 34250207697 scopus 로고    scopus 로고
    • A functional G300S variant of the cysteinyl leukotriene 1 receptor is associated with atopy in a Tristan da Cunha isolate
    • Thompson MD, Capra V, Takasaki J et al (2007) A functional G300S variant of the cysteinyl leukotriene 1 receptor is associated with atopy in a Tristan da Cunha isolate. Pharmacogenet Genomics 17:539-549
    • (2007) Pharmacogenet Genomics , vol.17 , pp. 539-549
    • Thompson, M.D.1    Capra, V.2    Takasaki, J.3
  • 7
    • 0027434258 scopus 로고
    • Disruption of potential sites for N-linked glycosylation does not impair hormone binding to the lutropin?Choriogonadotropin receptor if Asn-173 is left intact
    • Liu X, Davis D, Segaloff DL (1993) Disruption of potential sites for N-linked glycosylation does not impair hormone binding to the lutropin?choriogonadotropin receptor if Asn-173 is left intact. J Biol Chem 268:1513-1516
    • (1993) J Biol Chem , vol.268 , pp. 1513-1516
    • Liu, X.1    Davis, D.2    Segaloff, D.L.3
  • 8
    • 0032757001 scopus 로고    scopus 로고
    • N-linked glycosylation is required for plasma membrane localization of D5, but not D1, dopamine receptors in transfected mammalian cells
    • Karpa KD, Lidow MS, Pickering MT et al (1999) N-linked glycosylation is required for plasma membrane localization of D5, but not D1, dopamine receptors in transfected mammalian cells. Mol Pharmacol 56:1071-1078
    • (1999) Mol Pharmacol , vol.56 , pp. 1071-1078
    • Karpa, K.D.1    Lidow, M.S.2    Pickering, M.T.3
  • 9
    • 0027465919 scopus 로고
    • Palmitoylation of bovine opsin and its cysteine mutants in COS cells
    • Karnik SS, Ridge KD, Bhattacharya S et al (1993) Palmitoylation of bovine opsin and its cysteine mutants in COS cells. Proc Natl Acad Sci U S A 90:40-44
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 40-44
    • Karnik, S.S.1    Ridge, K.D.2    Bhattacharya, S.3
  • 10
    • 0023859049 scopus 로고
    • Two adjacent cysteine residues in the C-terminal cytoplasmic fragment of bovine rhodopsin are palmitoylated
    • Ovchinnikov Y, Abdulaev N, Bogachuk A (1988) Two adjacent cysteine residues in the C-terminal cytoplasmic fragment of bovine rhodopsin are palmitoylated. FEBS Lett 230:1-5
    • (1988) FEBS Lett , vol.230 , pp. 1-5
    • Ovchinnikov, Y.1    Abdulaev, N.2    Bogachuk, A.3
  • 11
    • 0030775615 scopus 로고    scopus 로고
    • Arrangement of rhodopsin transmembrane alpha-helices
    • Unger VM, Hargrave PA, Baldwin JM et al (1997) Arrangement of rhodopsin transmembrane alpha-helices. Nature 389:203-206
    • (1997) Nature , vol.389 , pp. 203-206
    • Unger, V.M.1    Hargrave, P.A.2    Baldwin, J.M.3
  • 12
    • 0034604451 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: A G proteincoupled receptor
    • Palczewski K, Kumasaka T, Hori T et al (2000) Crystal structure of rhodopsin: a G proteincoupled receptor. Science 289:739-745
    • (2000) Science , vol.289 , pp. 739-745
    • Palczewski, K.1    Kumasaka, T.2    Hori, T.3
  • 13
    • 0025812324 scopus 로고
    • Model systems for the study of seventransmembrane-segment receptors
    • Dohlman HG, Thorner J, Caron MG et al (1991) Model systems for the study of seventransmembrane-segment receptors. Annu Rev Biochem 60:653-688
    • (1991) Annu Rev Biochem , vol.60 , pp. 653-688
    • Dohlman, H.G.1    Thorner, J.2    Caron, M.G.3
  • 15
    • 0028289513 scopus 로고
    • Structure and function of G protein-coupled receptors
    • Strader CD, Fong TM, Tota MR et al (1994) Structure and function of G protein-coupled receptors. Annu Rev Biochem 63:101-132
    • (1994) Annu Rev Biochem , vol.63 , pp. 101-132
    • Strader, C.D.1    Fong, T.M.2    Tota, M.R.3
  • 16
    • 0035040530 scopus 로고    scopus 로고
    • Genetic variations and polymorphisms of G proteincoupled receptors: Functional and therapeutic implications
    • Rana BK, Shiina T, Insel PA (2001) Genetic variations and polymorphisms of G proteincoupled receptors: functional and therapeutic implications. Annu Rev Pharmacol Toxicol 41:593-624
    • (2001) Annu Rev Pharmacol Toxicol , vol.41 , pp. 593-624
    • Rana, B.K.1    Shiina, T.2    Insel, P.A.3
  • 18
    • 0036901518 scopus 로고    scopus 로고
    • Modeling of signaling networks
    • Neves SR, Iyengar R (2002) Modeling of signaling networks. Bioessays 24:1110-1117
    • (2002) Bioessays , vol.24 , pp. 1110-1117
    • Neves, S.R.1    Iyengar, R.2
  • 19
    • 0033600291 scopus 로고    scopus 로고
    • Characterization of the human cysteinyl leukotriene CysLT(1) receptor
    • Lynch KR, O’Neill GP, Liu QY et al (1999) Characterization of the human cysteinyl leukotriene CysLT(1) receptor. Nature 399: 789-793
    • (1999) Nature , vol.399 , pp. 789-793
    • Lynch, K.R.1    O’Neill, G.P.2    Liu, Q.Y.3
  • 20
    • 0034730638 scopus 로고    scopus 로고
    • Characterization of the human cysteinyl leukotriene 2 receptor
    • Heise CE, O’Dowd BF, Figueroa DJ et al (2000) Characterization of the human cysteinyl leukotriene 2 receptor. J Biol Chem 275:30531-30536
    • (2000) J Biol Chem , vol.275 , pp. 30531-30536
    • Heise, C.E.1    O’Dowd, B.F.2    Figueroa, D.J.3
  • 21
    • 0035152877 scopus 로고    scopus 로고
    • Expression of the cysteinyl leukotriene 1 receptor in normal human lung and peripheral blood leukocytes
    • Figueroa DJ, Breyer RM, Defoe SK et al (2001) Expression of the cysteinyl leukotriene 1 receptor in normal human lung and peripheral blood leukocytes. Am J Respir Crit Care Med 163:226-233
    • (2001) Am J Respir Crit Care Med , vol.163 , pp. 226-233
    • Figueroa, D.J.1    Breyer, R.M.2    Defoe, S.K.3
  • 22
    • 0141482048 scopus 로고    scopus 로고
    • Expression of the type 2 receptor for cysteinyl leukotrienes (CysLT2R) by human mast cells: Functional distinction from CysLT1R
    • Mellor EA, Frank N, Soler D et al (2003) Expression of the type 2 receptor for cysteinyl leukotrienes (CysLT2R) by human mast cells: functional distinction from CysLT1R. Proc Natl Acad Sci U S A 100:11589-11593
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 11589-11593
    • Mellor, E.A.1    Frank, N.2    Soler, D.3
  • 23
    • 0346192293 scopus 로고    scopus 로고
    • Dominant expression of the CysLT(2) receptor accounts for calcium signaling by cysteinyl leukotrienes in human umbilical vein endothelial cells
    • Sjostrom M, Johansson AS, Schroder O et al (2003) Dominant expression of the CysLT(2) receptor accounts for calcium signaling by cysteinyl leukotrienes in human umbilical vein endothelial cells. Arterioscler Thromb Vasc Biol 23:E37-E41
    • (2003) Arterioscler Thromb Vasc Biol , vol.23 , pp. E37-E41
    • Sjostrom, M.1    Johansson, A.S.2    Schroder, O.3
  • 24
    • 3042663287 scopus 로고    scopus 로고
    • G protein-coupled receptor dimerization: Function and ligand pharmacology
    • Milligan G (2004) G protein-coupled receptor dimerization: function and ligand pharmacology. Mol Pharmacol 66:1-7
    • (2004) Mol Pharmacol , vol.66 , pp. 1-7
    • Milligan, G.1
  • 25
    • 0034937698 scopus 로고    scopus 로고
    • G protein coupled receptor dimerization: Implications in modulating receptor function
    • Gomes I, Jordan BA, Gupta A et al (2001) G protein coupled receptor dimerization: implications in modulating receptor function. J Mol Med 79:226-242
    • (2001) J Mol Med , vol.79 , pp. 226-242
    • Gomes, I.1    Jordan, B.A.2    Gupta, A.3
  • 26
    • 0034618268 scopus 로고    scopus 로고
    • AT(1)-receptor heterodimers show enhanced G-protein activation and altered receptor sequestration
    • AbdAlla S, Lother H, Quitterer U (2000) AT(1)-receptor heterodimers show enhanced G-protein activation and altered receptor sequestration. Nature 407:94-98
    • (2000) Nature , vol.407 , pp. 94-98
    • Abdalla, S.1    Lother, H.2    Quitterer, U.3
  • 27
    • 7044274535 scopus 로고    scopus 로고
    • Factor XIIIA transglutaminase crosslinks AT(1) receptor dimers of monocytes at the onset of atherosclerosis
    • AbdAlla S, Lother H, Langer A, el Faramawy Y, Quitterer U (2004) Factor XIIIA transglutaminase crosslinks AT(1) receptor dimers of monocytes at the onset of atherosclerosis. Cell 119:343-354
    • (2004) Cell , vol.119 , pp. 343-354
    • Abdalla, S.1    Lother, H.2    Langer, A.3    El Faramawy, Y.4    Quitterer, U.5
  • 28
    • 0033516576 scopus 로고    scopus 로고
    • Identifi cation and molecular characterization of m3 muscarinic receptor dimers
    • Zeng FY, Wess J (1999) Identifi cation and molecular characterization of m3 muscarinic receptor dimers. J Biol Chem 274: 19487-19497
    • (1999) J Biol Chem , vol.274 , pp. 19487-19497
    • Zeng, F.Y.1    Wess, J.2
  • 29
    • 0032515074 scopus 로고    scopus 로고
    • A transmembrane domain-derived peptide inhibits D1 dopamine receptor function without affecting receptor oligomerization
    • George SR, Lee SP, Varghese G et al (1998) A transmembrane domain-derived peptide inhibits D1 dopamine receptor function without affecting receptor oligomerization. J Biol Chem 273:30244-30248
    • (1998) J Biol Chem , vol.273 , pp. 30244-30248
    • George, S.R.1    Lee, S.P.2    Varghese, G.3
  • 30
    • 0141431029 scopus 로고    scopus 로고
    • D2 dopamine receptor homodimerization is mediated by multiple sites of interaction, including an intermolecular interaction involving transmembrane domain 4
    • Lee SP, O’Dowd BF, Rajaram RD et al (2003) D2 dopamine receptor homodimerization is mediated by multiple sites of interaction, including an intermolecular interaction involving transmembrane domain 4. Biochemistry 42:11023-11031
    • (2003) Biochemistry , vol.42 , pp. 11023-11031
    • Lee, S.P.1    O’Dowd, B.F.2    Rajaram, R.D.3
  • 31
    • 0029903640 scopus 로고    scopus 로고
    • Metabotropic glutamate receptor 5 is a disulfi de-linked dimer
    • Romano C, Yang WL, O’Malley KL (1996) Metabotropic glutamate receptor 5 is a disulfi de-linked dimer. J Biol Chem 271: 28612-28616
    • (1996) J Biol Chem , vol.271 , pp. 28612-28616
    • Romano, C.1    Yang, W.L.2    O’Malley, K.L.3
  • 32
    • 0024110575 scopus 로고
    • Cysteine residues 110 and 187 are essential for the formation of correct structure in bovine rhodopsin
    • Karnik SS, Sakmar TP, Chen HB et al (1988) Cysteine residues 110 and 187 are essential for the formation of correct structure in bovine rhodopsin. Proc Natl Acad Sci U S A 85:8459-8463
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 8459-8463
    • Karnik, S.S.1    Sakmar, T.P.2    Chen, H.B.3
  • 33
    • 0026639831 scopus 로고
    • Site-directed mutagenesis of the rat m1 muscarinic acetylcholine receptor. Role of conserved cysteines in receptor function
    • Savarese TM, Wang CD, Fraser CM (1992) Site-directed mutagenesis of the rat m1 muscarinic acetylcholine receptor. Role of conserved cysteines in receptor function. J Biol Chem 267:11439-11448
    • (1992) J Biol Chem , vol.267 , pp. 11439-11448
    • Savarese, T.M.1    Wang, C.D.2    Fraser, C.M.3
  • 34
    • 0032847878 scopus 로고    scopus 로고
    • Mutation of human mu opioid receptor extracellular “disulfi de cysteine” residues alters ligand binding but does not prevent receptor targeting to the cell plasma membrane
    • Zhang P, Johnson PS, Zollner C et al (1999) Mutation of human mu opioid receptor extracellular “disulfi de cysteine” residues alters ligand binding but does not prevent receptor targeting to the cell plasma membrane. Brain Res Mol Brain Res 72:195-204
    • (1999) Brain Res Mol Brain Res , vol.72 , pp. 195-204
    • Zhang, P.1    Johnson, P.S.2    Zollner, C.3
  • 35
    • 34250852792 scopus 로고    scopus 로고
    • Cysteinyl-leukotrienes and their receptors in health and disease
    • Capra V, Thompson MD, Cole DE et al (2007) Cysteinyl-leukotrienes and their receptors in health and disease. Med Res Rev 27:469-527
    • (2007) Med Res Rev , vol.27 , pp. 469-527
    • Capra, V.1    Thompson, M.D.2    Cole, D.E.3
  • 36
    • 33845513409 scopus 로고    scopus 로고
    • G protein-coupled receptors and asthma endophenotypes: The cysteinyl leukotriene system in perspective
    • Thompson MD, Takasaki J, Capra V et al (2006) G protein-coupled receptors and asthma endophenotypes: the cysteinyl leukotriene system in perspective. Mol Diagn Ther 10:353-366
    • (2006) Mol Diagn Ther , vol.10 , pp. 353-366
    • Thompson, M.D.1    Takasaki, J.2    Capra, V.3
  • 37
    • 3342908589 scopus 로고    scopus 로고
    • Variants of the orexin2/hcrt2 receptor gene identifi ed in patients with excessive daytime sleepiness and patients with Tourette’s syndrome comorbidity
    • Thompson MD, Comings DE, Abu-Ghazalah R et al (2004) Variants of the orexin2/hcrt2 receptor gene identifi ed in patients with excessive daytime sleepiness and patients with Tourette’s syndrome comorbidity. Am J Med Genet B Neuropsychiatr Genet 129B:69-75
    • (2004) Am J Med Genet B Neuropsychiatr Genet , vol.129 , pp. 69-75
    • Thompson, M.D.1    Comings, D.E.2    Abu-Ghazalah, R.3
  • 38
    • 27844543454 scopus 로고    scopus 로고
    • The G protein-coupled receptors: Pharmacogenetics and disease
    • Thompson MD, Burnham WM, Cole DEC (2005) The G protein-coupled receptors: pharmacogenetics and disease. Crit Rev Clin Lab Sci 42:311-392
    • (2005) Crit Rev Clin Lab Sci , vol.42 , pp. 311-392
    • Thompson, M.D.1    Burnham, W.M.2    Cole, D.3
  • 39
    • 1642292051 scopus 로고    scopus 로고
    • Desensitization of G protein-coupled receptors and neuronal functions
    • Gainetdinov RR, Premont RT, Bohn LM et al (2004) Desensitization of G protein-coupled receptors and neuronal functions. Annu Rev Neurosci 27:107-144
    • (2004) Annu Rev Neurosci , vol.27 , pp. 107-144
    • Gainetdinov, R.R.1    Premont, R.T.2    Bohn, L.M.3
  • 40
    • 33646252013 scopus 로고    scopus 로고
    • Genetic diseases associated with heterotrimeric G proteins
    • Weinstein LS, Chen M, Xie T et al (2006) Genetic diseases associated with heterotrimeric G proteins. Trends Pharmacol Sci 27: 260-266
    • (2006) Trends Pharmacol Sci , vol.27 , pp. 260-266
    • Weinstein, L.S.1    Chen, M.2    Xie, T.3
  • 41
    • 34447647848 scopus 로고    scopus 로고
    • P.Gln200Glu, a putative constitutively active mutant of rod alpha-transducin (GNAT1) in autosomal dominant congenital stationary night blindness
    • Szabo V, Kreienkamp HJ, Rosenberg T et al (2007) p.Gln200Glu, a putative constitutively active mutant of rod alpha-transducin (GNAT1) in autosomal dominant congenital stationary night blindness. Hum Mutat 28:741-742
    • (2007) Hum Mutat , vol.28 , pp. 741-742
    • Szabo, V.1    Kreienkamp, H.J.2    Rosenberg, T.3
  • 42
    • 84861133514 scopus 로고    scopus 로고
    • GNAT1 associated with autosomal recessive congenital stationary night blindness
    • Naeem MA, Chavali VR, Ali S et al (2012) GNAT1 associated with autosomal recessive congenital stationary night blindness. Invest Ophthalmol Vis Sci 53:1353-1361
    • (2012) Invest Ophthalmol Vis Sci , vol.53 , pp. 1353-1361
    • Naeem, M.A.1    Chavali, V.R.2    Ali, S.3
  • 43
    • 79251642750 scopus 로고    scopus 로고
    • Clinical and genetic investigation of a large Tunisian family with complete achromatopsia: Identifi cation of a new nonsense mutation in GNAT2 gene
    • Ouechtati F, Merdassi A, Bouyacoub Y et al (2011) Clinical and genetic investigation of a large Tunisian family with complete achromatopsia: identifi cation of a new nonsense mutation in GNAT2 gene. J Hum Genet 56: 22-28
    • (2011) J Hum Genet , vol.56 , pp. 22-28
    • Ouechtati, F.1    Merdassi, A.2    Bouyacoub, Y.3
  • 44
    • 9444251801 scopus 로고    scopus 로고
    • Variant phenotypes of incomplete achromatopsia in two cousins with GNAT2 gene mutations
    • Rosenberg T, Baumann B, Kohl S et al (2004) Variant phenotypes of incomplete achromatopsia in two cousins with GNAT2 gene mutations. Invest Ophthalmol Vis Sci 45: 4256-4262
    • (2004) Invest Ophthalmol Vis Sci , vol.45 , pp. 4256-4262
    • Rosenberg, T.1    Baumann, B.2    Kohl, S.3
  • 45
    • 84883780405 scopus 로고    scopus 로고
    • Mouse model implicates GNB3 duplication in a childhood obesity syndrome
    • Goldlust IS, Hermetz KE, Catalano LM et al (2013) Mouse model implicates GNB3 duplication in a childhood obesity syndrome. Proc Natl Acad Sci U S A 110:14990-14994
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 14990-14994
    • Goldlust, I.S.1    Hermetz, K.E.2    Catalano, L.M.3
  • 46
    • 80051784938 scopus 로고    scopus 로고
    • The GNB3 C825T polymorphism as a pharmacogenetic marker in the treatment of hypertension, obesity, and depression
    • Klenke S, Kussmann M, Siffert W (2011) The GNB3 C825T polymorphism as a pharmacogenetic marker in the treatment of hypertension, obesity, and depression. Pharmacogenet Genomics 21:594-606
    • (2011) Pharmacogenet Genomics , vol.21 , pp. 594-606
    • Klenke, S.1    Kussmann, M.2    Siffert, W.3
  • 47
    • 84892692797 scopus 로고    scopus 로고
    • Genesenvironment interactions in obesity-and diabetes-associated pancreatic cancer: A GWAS data analysis
    • Tang H, Wei P, Duell EJ et al (2014) Genesenvironment interactions in obesity-and diabetes-associated pancreatic cancer: a GWAS data analysis. Cancer Epidemiol Biomarkers Prev 23(1):98-106
    • (2014) Cancer Epidemiol Biomarkers Prev , vol.23 , Issue.1 , pp. 98-106
    • Tang, H.1    Wei, P.2    Duell, E.J.3
  • 48
    • 84873989510 scopus 로고    scopus 로고
    • Pseudohypoparathyroidism type Ia and pseudo-pseudohypoparathyroidism: The growing spectrum of GNAS inactivating mutations
    • Elli FM, deSanctis L, Ceoloni B et al (2013) Pseudohypoparathyroidism type Ia and pseudo-pseudohypoparathyroidism: the growing spectrum of GNAS inactivating mutations. Hum Mutat 34:411-416
    • (2013) Hum Mutat , vol.34 , pp. 411-416
    • Elli, F.M.1    Desanctis, L.2    Ceoloni, B.3
  • 49
    • 0027956207 scopus 로고
    • Rapid GDP release from Gs alpha in patients with gain and loss of endocrine function
    • Iiri T, Herzmark P, Nakamoto JM et al (1994) Rapid GDP release from Gs alpha in patients with gain and loss of endocrine function. Nature 371:164-168
    • (1994) Nature , vol.371 , pp. 164-168
    • Iiri, T.1    Herzmark, P.2    Nakamoto, J.M.3
  • 50
    • 43549102015 scopus 로고    scopus 로고
    • G Protein-coupled receptors disrupted in human genetic disease
    • Thompson MD, Percy ME, Burnham WM et al (2008) G Protein-coupled receptors disrupted in human genetic disease. Methods Mol Biol 448:109-138
    • (2008) Methods Mol Biol , vol.448 , pp. 109-138
    • Thompson, M.D.1    Percy, M.E.2    Burnham, W.M.3
  • 52
    • 0029963793 scopus 로고    scopus 로고
    • Defects in G proteincoupled signal transduction in human disease
    • Spiegel AM (1996) Defects in G proteincoupled signal transduction in human disease. Annu Rev Physiol 58:143-170
    • (1996) Annu Rev Physiol , vol.58 , pp. 143-170
    • Spiegel, A.M.1
  • 53
    • 0029992477 scopus 로고    scopus 로고
    • Complexity and diversity of mammalian adenylyl cyclases
    • Sunahara RK, Dessauer CW et al (1996) Complexity and diversity of mammalian adenylyl cyclases. Annu Rev Pharmacol Toxicol 36:461-480
    • (1996) Annu Rev Pharmacol Toxicol , vol.36 , pp. 461-480
    • Sunahara, R.K.1    Dessauer, C.W.2
  • 54
    • 28844478334 scopus 로고    scopus 로고
    • Genetic variation in G-protein-coupled receptors—consequences for G-protein-coupled receptors as drug targets
    • Tang CM, Insel PA (2005) Genetic variation in G-protein-coupled receptors—consequences for G-protein-coupled receptors as drug targets. Expert Opin Ther Targets 9:1247-1265
    • (2005) Expert Opin Ther Targets , vol.9 , pp. 1247-1265
    • Tang, C.M.1    Insel, P.A.2
  • 55
    • 0038445997 scopus 로고    scopus 로고
    • Protein complexes involved in heptahelical receptormediated signal transduction
    • Rebois RV, Hebert TE (2003) Protein complexes involved in heptahelical receptormediated signal transduction. Receptors Channels 9:169-194
    • (2003) Receptors Channels , vol.9 , pp. 169-194
    • Rebois, R.V.1    Hebert, T.E.2
  • 56
    • 0032030621 scopus 로고    scopus 로고
    • Rethinking receptor-G protein-effector interactions
    • Chidiac P (1998) Rethinking receptor-G protein-effector interactions. Biochem Pharmacol 55:549-556
    • (1998) Biochem Pharmacol , vol.55 , pp. 549-556
    • Chidiac, P.1
  • 57
    • 0023132940 scopus 로고
    • The beta gamma subunits of GTP-binding proteins activate the muscarinic K + channel in heart
    • Logothetis DE, Kurachi Y, Galper J et al (1987) The beta gamma subunits of GTP-binding proteins activate the muscarinic K + channel in heart. Nature 325:321-326
    • (1987) Nature , vol.325 , pp. 321-326
    • Logothetis, D.E.1    Kurachi, Y.2    Galper, J.3
  • 58
    • 47749117162 scopus 로고    scopus 로고
    • G protein βγsubunits: Central mediators of G protein-coupled receptor signaling
    • Smrcka AV (2008) G protein βγ subunits: central mediators of G protein-coupled receptor signaling. Cell Mol Life Sci 65:2191-2214
    • (2008) Cell Mol Life Sci , vol.65 , pp. 2191-2214
    • Smrcka, A.V.1
  • 59
    • 0038445977 scopus 로고    scopus 로고
    • A novel kind of G protein heterodimer: The G beta5-RGS complex
    • Witherow DS, Slepak VZ (2003) A novel kind of G protein heterodimer: the G beta5-RGS complex. Receptors Channels 9:205-212
    • (2003) Receptors Channels , vol.9 , pp. 205-212
    • Witherow, D.S.1    Slepak, V.Z.2
  • 60
    • 0028920668 scopus 로고
    • Protein kinases that phosphorylate activated G protein-coupled receptors
    • Premont RT, Inglese J, Lefkowitz RJ (1995) Protein kinases that phosphorylate activated G protein-coupled receptors. FASEB J 9:175-182
    • (1995) FASEB J , vol.9 , pp. 175-182
    • Premont, R.T.1    Inglese, J.2    Lefkowitz, R.J.3
  • 61
    • 0029099297 scopus 로고
    • Isolation of cDNA clones encoding eight different human G protein gamma subunits, including three novel forms designated the gamma 4, gamma 10, and gamma 11 subunits
    • Ray K, Kunsch C, Bonner LM et al (1995) Isolation of cDNA clones encoding eight different human G protein gamma subunits, including three novel forms designated the gamma 4, gamma 10, and gamma 11 subunits. J Biol Chem 270:21765-21771
    • (1995) J Biol Chem , vol.270 , pp. 21765-21771
    • Ray, K.1    Kunsch, C.2    Bonner, L.M.3
  • 63
    • 17344366286 scopus 로고    scopus 로고
    • Association of a human G-protein beta3 subunit variant with hypertension
    • Siffert W, Rosskopf D, Siffert G et al (1998) Association of a human G-protein beta3 subunit variant with hypertension. Nat Genet 18:45-48
    • (1998) Nat Genet , vol.18 , pp. 45-48
    • Siffert, W.1    Rosskopf, D.2    Siffert, G.3
  • 64
    • 14944347178 scopus 로고    scopus 로고
    • Quantifi cation of allele-specifi c G-protein beta3 subunit mRNA transcripts in different human cells and tissues by Pyrosequencing
    • Sun A, Ge J, Siffert W, Frey UH (2005) Quantifi cation of allele-specifi c G-protein beta3 subunit mRNA transcripts in different human cells and tissues by Pyrosequencing. Eur J Hum Genet 13:361-369
    • (2005) Eur J Hum Genet , vol.13 , pp. 361-369
    • Sun, A.1    Ge, J.2    Siffert, W.3    Frey, U.H.4
  • 65
    • 0035199506 scopus 로고    scopus 로고
    • Molecular genetics of G proteins and atherosclerosis risk
    • Siffert W (2001) Molecular genetics of G proteins and atherosclerosis risk. Basic Res Cardiol 96:606-611
    • (2001) Basic Res Cardiol , vol.96 , pp. 606-611
    • Siffert, W.1
  • 66
    • 20444440818 scopus 로고    scopus 로고
    • Insulin-mediated venodilation is impaired in young, healthy carriers of the 825T allele of the G-protein beta3 subunit gene (GNB3)
    • Mitchell A, Pace M, Nurnberger J et al (2005) Insulin-mediated venodilation is impaired in young, healthy carriers of the 825T allele of the G-protein beta3 subunit gene (GNB3). Clin Pharmacol Ther 77:495-502
    • (2005) Clin Pharmacol Ther , vol.77 , pp. 495-502
    • Mitchell, A.1    Pace, M.2    Nurnberger, J.3
  • 67
    • 20144389651 scopus 로고    scopus 로고
    • Association of C825T polymorphism of G protein beta3 subunit with the autonomic nervous system in young healthy Japanese individuals
    • Matsunaga T, Nagasumi K, Yamamura T et al (2005) Association of C825T polymorphism of G protein beta3 subunit with the autonomic nervous system in young healthy Japanese individuals. Am J Hypertens 18: 523-529
    • (2005) Am J Hypertens , vol.18 , pp. 523-529
    • Matsunaga, T.1    Nagasumi, K.2    Yamamura, T.3
  • 68
    • 18744382822 scopus 로고    scopus 로고
    • Association of G-protein beta-3 subunit gene (GNB3) T825 allele with type II diabetes
    • Kiani JG, Saeed M, Parvez SH et al (2005) Association of G-protein beta-3 subunit gene (GNB3) T825 allele with type II diabetes. Neuro Endocrinol Lett 26:87-88
    • (2005) Neuro Endocrinol Lett , vol.26 , pp. 87-88
    • Kiani, J.G.1    Saeed, M.2    Parvez, S.H.3
  • 69
    • 0037270351 scopus 로고    scopus 로고
    • G protein beta3 gene variant, vascular function, and insulin sensitivity in type 2 diabetes
    • Fernandez-Real JM, Penarroja G, Richart C et al (2003) G protein beta3 gene variant, vascular function, and insulin sensitivity in type 2 diabetes. Hypertension 41:124-129
    • (2003) Hypertension , vol.41 , pp. 124-129
    • Fernandez-Real, J.M.1    Penarroja, G.2    Richart, C.3
  • 70
    • 21244471908 scopus 로고    scopus 로고
    • Association between beta-adrenergic receptor polymorphisms and their G-protein-coupled receptors with body mass index and obesity in women: A report from the NHLBI-sponsored WISE study
    • Terra SG, McGorray SP, Wu R et al (2005) Association between beta-adrenergic receptor polymorphisms and their G-protein-coupled receptors with body mass index and obesity in women: a report from the NHLBI-sponsored WISE study. Int J Obes (Lond) 29:746-754
    • (2005) Int J Obes (Lond) , vol.29 , pp. 746-754
    • Terra, S.G.1    McGorray, S.P.2    Wu, R.3
  • 71
    • 31444432748 scopus 로고    scopus 로고
    • Studies of the association of the GNB3 825C > T polymorphism with components of the metabolic syndrome in white Danes
    • Andersen G, Overgaard J, Albrechtsen A et al (2006) Studies of the association of the GNB3 825C > T polymorphism with components of the metabolic syndrome in white Danes. Diabetologia 49:75-82
    • (2006) Diabetologia , vol.49 , pp. 75-82
    • Andersen, G.1    Overgaard, J.2    Albrechtsen, A.3
  • 72
    • 26244448109 scopus 로고    scopus 로고
    • Lack of association between certain candidate gene polymorphisms and the metabolic syndrome
    • Meirhaeghe A, Cottel D, Amouyel P et al (2005) Lack of association between certain candidate gene polymorphisms and the metabolic syndrome. Mol Genet Metab 86: 293-299
    • (2005) Mol Genet Metab , vol.86 , pp. 293-299
    • Meirhaeghe, A.1    Cottel, D.2    Amouyel, P.3
  • 73
    • 3042514120 scopus 로고    scopus 로고
    • Polymorphism in genes involved in adrenergic signaling associated with Alzheimer’s
    • Bullido MJ, Ramos MC, Ruiz-Gomez A et al (2004) Polymorphism in genes involved in adrenergic signaling associated with Alzheimer’s. Neurobiol Aging 25:853-859
    • (2004) Neurobiol Aging , vol.25 , pp. 853-859
    • Bullido, M.J.1    Ramos, M.C.2    Ruiz-Gomez, A.3
  • 74
    • 24044497210 scopus 로고    scopus 로고
    • DNA polymorphisms in the tyrosine hydroxylase and GNB3 genes: Association with unexpected death from acute myocardial infarction and increased heart weight
    • Klintschar M, Stiller D, Schwaiger P et al (2005) DNA polymorphisms in the tyrosine hydroxylase and GNB3 genes: association with unexpected death from acute myocardial infarction and increased heart weight. Forensic Sci Int 153:142-146
    • (2005) Forensic Sci Int , vol.153 , pp. 142-146
    • Klintschar, M.1    Stiller, D.2    Schwaiger, P.3
  • 75
    • 28844474867 scopus 로고    scopus 로고
    • Association study of the G-protein beta3 subunit C825T polymorphism with disease progression in patients with bladder cancer
    • Eisenhardt A, Siffert W, Rosskopf D et al (2005) Association study of the G-protein beta3 subunit C825T polymorphism with disease progression in patients with bladder cancer. World J Urol 23:279-286
    • (2005) World J Urol , vol.23 , pp. 279-286
    • Eisenhardt, A.1    Siffert, W.2    Rosskopf, D.3
  • 76
    • 29744467506 scopus 로고    scopus 로고
    • Different genotype distribution of the GNB3 C825T polymorphism of the G protein beta3 subunit in adenomas and differentiated thyroid carcinomas of follicular cell origin
    • Sheu SY, Gorges R, Ensinger C et al (2005) Different genotype distribution of the GNB3 C825T polymorphism of the G protein beta3 subunit in adenomas and differentiated thyroid carcinomas of follicular cell origin. J Pathol 207:430-435
    • (2005) J Pathol , vol.207 , pp. 430-435
    • Sheu, S.Y.1    Gorges, R.2    Ensinger, C.3
  • 77
    • 23444453510 scopus 로고    scopus 로고
    • GNB3 C825T polymorphism and response to interferon-alfa/ribavirin treatment in patients with hepatitis C virus genotype 1 (HCV-1) infection
    • Sarrazin C, Berg T, Weich V et al (2005) GNB3 C825T polymorphism and response to interferon-alfa/ribavirin treatment in patients with hepatitis C virus genotype 1 (HCV-1) infection. J Hepatol 43:388-393
    • (2005) J Hepatol , vol.43 , pp. 388-393
    • Sarrazin, C.1    Berg, T.2    Weich, V.3
  • 78
    • 10744222550 scopus 로고    scopus 로고
    • Association between a G-protein beta 3 subunit gene polymorphism and the symptomatology and treatment responses of major depressive disorders
    • Lee HJ, Cha JH, Ham BJ et al (2004) Association between a G-protein beta 3 subunit gene polymorphism and the symptomatology and treatment responses of major depressive disorders. Pharmacogenomics J 4: 29-33
    • (2004) Pharmacogenomics J , vol.4 , pp. 29-33
    • Lee, H.J.1    Cha, J.H.2    Ham, B.J.3
  • 79
    • 24044544831 scopus 로고    scopus 로고
    • Suggestive association between the C825T polymorphism of the G-protein beta3 subunit gene (GNB3) and clinical improvement with antipsychotics in schizophrenia
    • Muller DJ, De Luca V, Sicard T et al (2005) Suggestive association between the C825T polymorphism of the G-protein beta3 subunit gene (GNB3) and clinical improvement with antipsychotics in schizophrenia. Eur Neuropsychopharmacol 15:525-531
    • (2005) Eur Neuropsychopharmacol , vol.15 , pp. 525-531
    • Muller, D.J.1    De Luca, V.2    Sicard, T.3
  • 80
    • 31044434665 scopus 로고    scopus 로고
    • Interactions between fi ve candidate genes and antihypertensive drug therapy on blood pressure
    • Schelleman H, Stricker BH, Verschuren WM et al (2006) Interactions between fi ve candidate genes and antihypertensive drug therapy on blood pressure. Pharmacogenomics J 6: 22-26
    • (2006) Pharmacogenomics J , vol.6 , pp. 22-26
    • Schelleman, H.1    Stricker, B.H.2    Verschuren, W.M.3
  • 81
    • 0028912416 scopus 로고
    • The role of G-protein beta gamma subunits in signal transduction
    • Muller S, Lohse MJ (1995) The role of G-protein beta gamma subunits in signal transduction. Biochem Soc Trans 23:141-148
    • (1995) Biochem Soc Trans , vol.23 , pp. 141-148
    • Muller, S.1    Lohse, M.J.2
  • 82
    • 0026418426 scopus 로고
    • Type-specifi c regulation of adenylyl cyclase by G protein beta gamma subunits
    • Tang WJ, Gilman AG (1991) Type-specifi c regulation of adenylyl cyclase by G protein beta gamma subunits. Science 254: 1500-1503
    • (1991) Science , vol.254 , pp. 1500-1503
    • Tang, W.J.1    Gilman, A.G.2
  • 83
    • 0028169730 scopus 로고
    • G protein beta gamma subunits. Simplifi ed purifi cation and properties of novel isoforms
    • Ueda N, Iniguez-Lluhi JA, Lee E et al (1994) G protein beta gamma subunits. Simplifi ed purifi cation and properties of novel isoforms. J Biol Chem 269:4388-4395
    • (1994) J Biol Chem , vol.269 , pp. 4388-4395
    • Ueda, N.1    Iniguez-Lluhi, J.A.2    Lee, E.3
  • 84
    • 0027981982 scopus 로고
    • Selective activation of phospholipase C by recombinant G-protein alpha-and beta gamma-subunits
    • Boyer JL, Graber SG, Waldo GL et al (1994) Selective activation of phospholipase C by recombinant G-protein alpha-and beta gamma-subunits. J Biol Chem 269: 2814-2819
    • (1994) J Biol Chem , vol.269 , pp. 2814-2819
    • Boyer, J.L.1    Graber, S.G.2    Waldo, G.L.3
  • 85
    • 0025256090 scopus 로고
    • Distinct guanine nucleotide binding and release properties of the three Gi proteins
    • Carty DJ, Padrell E, Codina J et al (1990) Distinct guanine nucleotide binding and release properties of the three Gi proteins. J Biol Chem 265:6268-6273
    • (1990) J Biol Chem , vol.265 , pp. 6268-6273
    • Carty, D.J.1    Padrell, E.2    Codina, J.3
  • 86
    • 0027118914 scopus 로고
    • G proteins. The target sets the tempo
    • Bourne HR, Stryer L (1992) G proteins. The target sets the tempo. Nature 358:541-543
    • (1992) Nature , vol.358 , pp. 541-543
    • Bourne, H.R.1    Stryer, L.2
  • 87
    • 30944451158 scopus 로고    scopus 로고
    • RGS proteins have a signalling complex: Interactions between RGS proteins and GPCRs, effectors, and auxiliary proteins
    • Abramow-Newerly M, Roy AA, Nunn C et al (2006) RGS proteins have a signalling complex: interactions between RGS proteins and GPCRs, effectors, and auxiliary proteins. Cell Signal 18:579-591
    • (2006) Cell Signal , vol.18 , pp. 579-591
    • Abramow-Newerly, M.1    Roy, A.A.2    Nunn, C.3
  • 88
    • 27444440633 scopus 로고    scopus 로고
    • Cell signalling diversity of the Gqαfamily of heterotrimeric G proteins
    • Hubbard KB, Hepler JR (2006) Cell signalling diversity of the Gqα family of heterotrimeric G proteins. Cell Signal 18:135-150
    • (2006) Cell Signal , vol.18 , pp. 135-150
    • Hubbard, K.B.1    Hepler, J.R.2
  • 89
    • 53149135853 scopus 로고    scopus 로고
    • Regulation of cAMP responses by the G12/13 pathway converges on adenylyl cyclase VII
    • Jiang LI, Collins J, Davis R et al (2008) Regulation of cAMP responses by the G12/13 pathway converges on adenylyl cyclase VII. J Biol Chem 283:23429-23439
    • (2008) J Biol Chem , vol.283 , pp. 23429-23439
    • Jiang, L.I.1    Collins, J.2    Davis, R.3
  • 90
    • 5644249233 scopus 로고    scopus 로고
    • Regulation of RGS-RhoGEFs by G alpha 12 and G alpha 13 proteins
    • Tanabe S, Kreutz B, Suzuki N et al (2004) Regulation of RGS-RhoGEFs by G alpha 12 and G alpha 13 proteins. Methods Enzymol 390:285-294
    • (2004) Methods Enzymol , vol.390 , pp. 285-294
    • Tanabe, S.1    Kreutz, B.2    Suzuki, N.3
  • 91
    • 30444435782 scopus 로고    scopus 로고
    • Heterotrimeric G-proteins: A short history
    • Milligan G, Kostenis E (2006) Heterotrimeric G-proteins: a short history. Br J Pharmacol 147:S46-S55
    • (2006) Br J Pharmacol , vol.147 , pp. S46-S55
    • Milligan, G.1    Kostenis, E.2
  • 92
    • 74249123592 scopus 로고    scopus 로고
    • The role of GNAS and other imprinted genes in the development of obesity
    • Weinstein LS, Xie T, Qasem A et al (2010) The role of GNAS and other imprinted genes in the development of obesity. Int J Obes (Lond) 34:6-17
    • (2010) Int J Obes (Lond) , vol.34 , pp. 6-17
    • Weinstein, L.S.1    Xie, T.2    Qasem, A.3
  • 93
    • 0028169341 scopus 로고
    • An activating Gs alpha mutation is present in fi brous dysplasia of bone in the McCune-Albright syndrome
    • Shenker A, Weinstein LS, Sweet DE et al (1994) An activating Gs alpha mutation is present in fi brous dysplasia of bone in the McCune-Albright syndrome. J Clin Endocrinol Metab 79:750-755
    • (1994) J Clin Endocrinol Metab , vol.79 , pp. 750-755
    • Shenker, A.1    Weinstein, L.S.2    Sweet, D.E.3
  • 94
    • 0038030796 scopus 로고    scopus 로고
    • Cushing’s syndrome secondary to adrenocorticotropin-independent macronodular adrenocortical hyperplasia due to activating mutations of GNAS1 gene
    • Fragoso MC, Domenice S, Latronico AC et al (2003) Cushing’s syndrome secondary to adrenocorticotropin-independent macronodular adrenocortical hyperplasia due to activating mutations of GNAS1 gene. J Clin Endocrinol Metab 88:2147-2151
    • (2003) J Clin Endocrinol Metab , vol.88 , pp. 2147-2151
    • Fragoso, M.C.1    Domenice, S.2    Latronico, A.C.3
  • 95
    • 3342886382 scopus 로고    scopus 로고
    • Activating GNAS1 gene mutations in patients with premature thelarche
    • Roman R, Johnson MC, Codner E et al (2004) Activating GNAS1 gene mutations in patients with premature thelarche. J Pediatr 145:218-222
    • (2004) J Pediatr , vol.145 , pp. 218-222
    • Roman, R.1    Johnson, M.C.2    Codner, E.3
  • 96
    • 0025326074 scopus 로고
    • Albright’s hereditary osteodystrophy and defective G proteins
    • Spiegel AM (1990) Albright’s hereditary osteodystrophy and defective G proteins. N Engl J Med 322:1461-1462
    • (1990) N Engl J Med , vol.322 , pp. 1461-1462
    • Spiegel, A.M.1
  • 97
    • 0034793851 scopus 로고    scopus 로고
    • Endocrine manifestations of stimulatory G protein alpha-subunit mutations and the role of genomic imprinting
    • Weinstein LS, Yu S, Warner DR et al (2001) Endocrine manifestations of stimulatory G protein alpha-subunit mutations and the role of genomic imprinting. Endocr Rev 22:675-705
    • (2001) Endocr Rev , vol.22 , pp. 675-705
    • Weinstein, L.S.1    Yu, S.2    Warner, D.R.3
  • 98
    • 6944221426 scopus 로고    scopus 로고
    • Stimulatory G protein directly regulates hypertrophic differentiation of growth plate cartilage in vivo
    • Bastepe M, Weinstein LS, Ogata N et al (2004) Stimulatory G protein directly regulates hypertrophic differentiation of growth plate cartilage in vivo . Proc Natl Acad Sci U S A 101:14794-14799
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 14794-14799
    • Bastepe, M.1    Weinstein, L.S.2    Ogata, N.3
  • 99
    • 15344349695 scopus 로고    scopus 로고
    • Chondrocyte-specifi c knockout of the G protein G(S)alpha leads to epiphyseal and growth plate abnormalities and ectopic chondrocyte formation
    • Sakamoto A, Chen M, Kobayashi T et al (2005) Chondrocyte-specifi c knockout of the G protein G(s)alpha leads to epiphyseal and growth plate abnormalities and ectopic chondrocyte formation. J Bone Miner Res 20:663-671
    • (2005) J Bone Miner Res , vol.20 , pp. 663-671
    • Sakamoto, A.1    Chen, M.2    Kobayashi, T.3
  • 100
    • 0141606268 scopus 로고    scopus 로고
    • Growth hormone defi ciency in pseudohypoparathyroidism type 1a: Another manifestation of multihormone resistance
    • Germain-Lee EL, Groman J, Crane JL, Jan de Beur SM, Levine MA (2003) Growth hormone defi ciency in pseudohypoparathyroidism type 1a: another manifestation of multihormone resistance. J Clin Endocrinol Metab 88:4059-4069
    • (2003) J Clin Endocrinol Metab , vol.88 , pp. 4059-4069
    • Germain-Lee, E.L.1    Groman, J.2    Crane, J.L.3    De Jan Beur, S.M.4    Levine, M.A.5
  • 101
    • 0141857716 scopus 로고    scopus 로고
    • Growth hormone-releasing hormone resistance in pseudohypoparathyroidism type Ia: New evidence for imprinting of the Gs alpha gene
    • Mantovani G, Maghnie M, Weber G et al (2003) Growth hormone-releasing hormone resistance in pseudohypoparathyroidism type Ia: new evidence for imprinting of the Gs alpha gene. J Clin Endocrinol Metab 88:4070-4074
    • (2003) J Clin Endocrinol Metab , vol.88 , pp. 4070-4074
    • Mantovani, G.1    Maghnie, M.2    Weber, G.3
  • 102
    • 0032555241 scopus 로고    scopus 로고
    • Variable and tissue-specifi c hormone resistance in heterotrimeric Gs protein alpha-subunit (Gsalpha) knockout mice is due to tissue-specifi c imprinting of the gsalpha gene
    • Yu S, Yu D, Lee E et al (1998) Variable and tissue-specifi c hormone resistance in heterotrimeric Gs protein alpha-subunit (Gsalpha) knockout mice is due to tissue-specifi c imprinting of the gsalpha gene. Proc Natl Acad Sci U S A 95:8715-8720
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 8715-8720
    • Yu, S.1    Yu, D.2    Lee, E.3
  • 103
    • 0035106246 scopus 로고    scopus 로고
    • Imprinting of the G(S)alpha gene GNAS1 in the pathogenesis of acromegaly
    • Hayward BE, Barlier A, Korbonits M et al (2001) Imprinting of the G(s)alpha gene GNAS1 in the pathogenesis of acromegaly. J Clin Invest 107:R31-R36
    • (2001) J Clin Invest , vol.107 , pp. R31-R36
    • Hayward, B.E.1    Barlier, A.2    Korbonits, M.3
  • 104
    • 0036771614 scopus 로고    scopus 로고
    • The gsalpha gene: Predominant maternal origin of transcription in human thyroid gland and gonads
    • Mantovani G, Ballare E, Giammona E et al (2002) The gsalpha gene: predominant maternal origin of transcription in human thyroid gland and gonads. J Clin Endocrinol Metab 87:4736-4740
    • (2002) J Clin Endocrinol Metab , vol.87 , pp. 4736-4740
    • Mantovani, G.1    Ballare, E.2    Giammona, E.3
  • 105
    • 0035982094 scopus 로고    scopus 로고
    • Paternal imprinting of Galpha(S) in the human thyroid as the basis of TSH resistance in pseudohypoparathyroidism type 1a
    • Germain-Lee EL, Ding CL, Deng Z et al (2002) Paternal imprinting of Galpha(s) in the human thyroid as the basis of TSH resistance in pseudohypoparathyroidism type 1a. Biochem Biophys Res Commun 296:67-72
    • (2002) Biochem Biophys Res Commun , vol.296 , pp. 67-72
    • Germain-Lee, E.L.1    Ding, C.L.2    Deng, Z.3
  • 106
    • 0141857714 scopus 로고    scopus 로고
    • The stimulatory G protein alpha-subunit Gs alpha is imprinted in human thyroid glands: Implications for thyroid function in pseudohypoparathyroidism types 1A and 1B
    • Liu J, Erlichman B, Weinstein LS (2003) The stimulatory G protein alpha-subunit Gs alpha is imprinted in human thyroid glands: implications for thyroid function in pseudohypoparathyroidism types 1A and 1B. J Clin Endocrinol Metab 88:4336-4341
    • (2003) J Clin Endocrinol Metab , vol.88 , pp. 4336-4341
    • Liu, J.1    Erlichman, B.2    Weinstein, L.S.3
  • 107
    • 11244353640 scopus 로고    scopus 로고
    • Deletion of the NESP55 differentially methylated region causes loss of maternal GNAS imprints and pseudohypoparathyroidism type Ib
    • Bastepe M, Frohlich LF, Linglart A et al (2005) Deletion of the NESP55 differentially methylated region causes loss of maternal GNAS imprints and pseudohypoparathyroidism type Ib. Nat Genet 37:25-27
    • (2005) Nat Genet , vol.37 , pp. 25-27
    • Bastepe, M.1    Frohlich, L.F.2    Linglart, A.3
  • 108
    • 0035013623 scopus 로고    scopus 로고
    • Paternal uniparental isodisomy of chromosome 20q—and the resulting changes in GNAS1 methylation—as a plausible cause of pseudohypoparathyroidism
    • Bastepe M, Lane AH, Juppner H (2001) Paternal uniparental isodisomy of chromosome 20q—and the resulting changes in GNAS1 methylation—as a plausible cause of pseudohypoparathyroidism. Am J Hum Genet 68:1283-1289
    • (2001) Am J Hum Genet , vol.68 , pp. 1283-1289
    • Bastepe, M.1    Lane, A.H.2    Juppner, H.3
  • 109
    • 0035808314 scopus 로고    scopus 로고
    • Selective resistance to parathyroid hormone caused by a novel uncoupling mutation in the carboxyl terminus of G alpha(S). A cause of pseudohypoparathyroidism type Ib
    • Wu WI, Schwindinger WF, Aparicio LF et al (2001) Selective resistance to parathyroid hormone caused by a novel uncoupling mutation in the carboxyl terminus of G alpha(s). A cause of pseudohypoparathyroidism type Ib. J Biol Chem 276:165-171
    • (2001) J Biol Chem , vol.276 , pp. 165-171
    • Wu, W.I.1    Schwindinger, W.F.2    Aparicio, L.F.3
  • 110
    • 33745972929 scopus 로고    scopus 로고
    • Non-receptor activators of heterotrimeric G-protein signaling (AGS proteins)
    • Cismowski MJ (2006) Non-receptor activators of heterotrimeric G-protein signaling (AGS proteins). Semin Cell Dev Biol 17:334-344
    • (2006) Semin Cell Dev Biol , vol.17 , pp. 334-344
    • Cismowski, M.J.1
  • 111
    • 31444453235 scopus 로고    scopus 로고
    • Identifi cation of a receptor-independent activator of G protein signaling (AGS8) in ischemic heart and its interaction with Gbetagamma
    • Sato M, Cismowski MJ, Toyota E et al (2006) Identifi cation of a receptor-independent activator of G protein signaling (AGS8) in ischemic heart and its interaction with Gbetagamma. Proc Natl Acad Sci U S A 103:797-802
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 797-802
    • Sato, M.1    Cismowski, M.J.2    Toyota, E.3
  • 113
    • 0041353628 scopus 로고    scopus 로고
    • RGS protein and G protein interactions: A little help from their friends
    • Hepler JR (2003) RGS protein and G protein interactions: a little help from their friends. Mol Pharmacol 64:547-549
    • (2003) Mol Pharmacol , vol.64 , pp. 547-549
    • Hepler, J.R.1
  • 114
    • 0041854353 scopus 로고    scopus 로고
    • Recruitment of RGS2 and RGS4 to the plasma membrane by G proteins and receptors refl ects functional interactions
    • Roy AA, Lemberg KE, Chidiac P (2003) Recruitment of RGS2 and RGS4 to the plasma membrane by G proteins and receptors refl ects functional interactions. Mol Pharmacol 64:587-593
    • (2003) Mol Pharmacol , vol.64 , pp. 587-593
    • Roy, A.A.1    Lemberg, K.E.2    Chidiac, P.3
  • 115
    • 33644972273 scopus 로고    scopus 로고
    • Polymorphisms and haplotypes of the regulator of G protein signaling-2 gene in normotensives and hypertensives
    • Riddle EL, Rana BK, Murthy KK et al (2006) Polymorphisms and haplotypes of the regulator of G protein signaling-2 gene in normotensives and hypertensives. Hypertension 47:415-420
    • (2006) Hypertension , vol.47 , pp. 415-420
    • Riddle, E.L.1    Rana, B.K.2    Murthy, K.K.3
  • 116
    • 0038446043 scopus 로고    scopus 로고
    • Activity, regulation, and intracellular localization of RGS proteins
    • Chidiac P, Roy AA (2003) Activity, regulation, and intracellular localization of RGS proteins. Receptors Channels 9:135-147
    • (2003) Receptors Channels , vol.9 , pp. 135-147
    • Chidiac, P.1    Roy, A.A.2
  • 117
    • 2442717874 scopus 로고    scopus 로고
    • RGS2 binds directly and selectively to the M1 muscarinic acetylcholine receptor third intracellular loop to modulate G(Q/11 alpha) signaling
    • Bernstein LS, Ramineni S, Hague C et al (2004) RGS2 binds directly and selectively to the M1 muscarinic acetylcholine receptor third intracellular loop to modulate G(q/11 alpha) 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
  • 118
    • 33847781275 scopus 로고    scopus 로고
    • Mechanistic pathways and biological roles for receptor-independent activators of G-protein signaling
    • Blumer JB, Smrcka AV, Lanier SM (2007) Mechanistic pathways and biological roles for receptor-independent activators of G-protein signaling. Pharmacol Ther 113:488-506
    • (2007) Pharmacol Ther , vol.113 , pp. 488-506
    • Blumer, J.B.1    Smrcka, A.V.2    Lanier, S.M.3
  • 119
    • 84873929438 scopus 로고    scopus 로고
    • Fine-tuning of GPCR signals by intracellular G protein modulators
    • Zhao P, Cladman W, Van Tol HH et al (2013) Fine-tuning of GPCR signals by intracellular G protein modulators. Prog Mol Biol Transl Sci 115:421-453
    • (2013) Prog Mol Biol Transl Sci , vol.115 , pp. 421-453
    • Zhao, P.1    Cladman, W.2    Van Tol, H.H.3
  • 120
    • 84455173156 scopus 로고    scopus 로고
    • Identifi cation of a cAMP-response element in the regulator of G-protein signaling-2 (RGS2) promoter as a key cis-regulatory element for RGS2 transcriptional regulation by angiotensin II in cultured vascular smooth muscles
    • Xie Z, Liu D, Liu S et al (2011) Identifi cation of a cAMP-response element in the regulator of G-protein signaling-2 (RGS2) promoter as a key cis-regulatory element for RGS2 transcriptional regulation by angiotensin II in cultured vascular smooth muscles. J Biol Chem 286:44646-44658
    • (2011) J Biol Chem , vol.286 , pp. 44646-44658
    • Xie, Z.1    Liu, D.2    Liu, S.3
  • 121
    • 0033538337 scopus 로고    scopus 로고
    • Phospholipase C-beta1 directly accelerates GTP hydrolysis by Galphaq and acceleration is inhibited by Gbeta gamma subunits
    • Chidiac P, Ross EM (1999) Phospholipase C-beta1 directly accelerates GTP hydrolysis by Galphaq and acceleration is inhibited by Gbeta gamma subunits. J Biol Chem 274:19639-19643
    • (1999) J Biol Chem , vol.274 , pp. 19639-19643
    • Chidiac, P.1    Ross, E.M.2
  • 122
    • 69249208550 scopus 로고    scopus 로고
    • Regulation of RhoGEF proteins by G12/13-coupled receptors
    • Siehler S (2009) Regulation of RhoGEF proteins by G12/13-coupled receptors. Br J Pharmacol 158:41-49
    • (2009) Br J Pharmacol , vol.158 , pp. 41-49
    • Siehler, S.1
  • 123
    • 0031916822 scopus 로고    scopus 로고
    • Mammalian RGS proteins: Barbarians at the gate
    • Berman DM, Gilman AG (1998) Mammalian RGS proteins: barbarians at the gate. J Biol Chem 273:1269-1272
    • (1998) J Biol Chem , vol.273 , pp. 1269-1272
    • Berman, D.M.1    Gilman, A.G.2
  • 124
    • 77957293797 scopus 로고    scopus 로고
    • Deregulation of RGS2 in cardiovascular diseases
    • Tsang S, Woo AY, Zhu W et al (2010) Deregulation of RGS2 in cardiovascular diseases. Front Biosci (Schol Ed) 2:547-557
    • (2010) Front Biosci (Schol Ed) , vol.2 , pp. 547-557
    • Tsang, S.1    Woo, A.Y.2    Zhu, W.3
  • 125
    • 65649110132 scopus 로고    scopus 로고
    • Regulator of G protein signaling 5: A new player in vascular remodeling
    • Manzur M, 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
  • 126
    • 63449118167 scopus 로고    scopus 로고
    • RGS proteins: Identifying new GAPs in the understanding of blood pressure regulation and cardiovascular function
    • Gu S, Cifelli C, Wang S et al (2009) RGS proteins: identifying new GAPs in the understanding of blood pressure regulation and cardiovascular function. Clin Sci (Lond) 116:391-399
    • (2009) Clin Sci (Lond) , vol.116 , pp. 391-399
    • Gu, S.1    Cifelli, C.2    Wang, S.3
  • 127
    • 4344575064 scopus 로고    scopus 로고
    • Is RGS-2 a new drug development target in cardiovascular disease?
    • Doggrell SA (2004) Is RGS-2 a new drug development target in cardiovascular disease? Expert Opin Ther Targets 8:355-358
    • (2004) Expert Opin Ther Targets , vol.8 , pp. 355-358
    • Doggrell, S.A.1
  • 128
    • 0347706930 scopus 로고    scopus 로고
    • Hypertension and prolonged vasoconstrictor signaling in RGS2-defi cient mice
    • Heximer SP, Knutsen RH, Sun X et al (2003) Hypertension and prolonged vasoconstrictor signaling in RGS2-defi cient mice. J Clin Invest 111:1259
    • (2003) J Clin Invest , vol.111 , pp. 1259
    • Heximer, S.P.1    Knutsen, R.H.2    Sun, X.3
  • 129
    • 14944383669 scopus 로고    scopus 로고
    • RGS2 is a mediator of nitric oxide action on blood pressure and vasoconstrictor signaling
    • Sun X, Kaltenbronn KM, Steinberg TH et al (2005) RGS2 is a mediator of nitric oxide action on blood pressure and vasoconstrictor signaling. Mol Pharmacol 67:631-639
    • (2005) Mol Pharmacol , vol.67 , pp. 631-639
    • Sun, X.1    Kaltenbronn, K.M.2    Steinberg, T.H.3
  • 130
    • 0027968353 scopus 로고
    • Synergistic effects of angiotensinconverting enzyme and angiotensin-II type-1 receptor gene polymorphisms on risk of myocardial-infarction
    • Tiret L, Bonnardeaux A, Poirier O et al (1994) Synergistic effects of angiotensinconverting enzyme and angiotensin-II type-1 receptor gene polymorphisms on risk of myocardial-infarction. Lancet 344:910-913
    • (1994) Lancet , vol.344 , pp. 910-913
    • Tiret, L.1    Bonnardeaux, A.2    Poirier, O.3
  • 131
    • 0031955106 scopus 로고    scopus 로고
    • Angiotensin II type 1 receptor gene polymorphism is associated with increase of left ventricular mass but not with hypertension
    • Takami S, Katsuya T, Rakugi H et al (1998) Angiotensin II type 1 receptor gene polymorphism is associated with increase of left ventricular mass but not with hypertension. Am J Hypertens 11:316-321
    • (1998) Am J Hypertens , vol.11 , pp. 316-321
    • Takami, S.1    Katsuya, T.2    Rakugi, H.3
  • 132
    • 4043103612 scopus 로고    scopus 로고
    • Increased expression of regulator of G protein signaling-2 (RGS-2) in Bartter’s/Gitelman’s syndrome. A role in the control of vascular tone and implication for hypertension
    • Calo LA, Pagnin E, Davis PA et al (2004) Increased expression of regulator of G protein signaling-2 (RGS-2) in Bartter’s/Gitelman’s syndrome. A role in the control of vascular tone and implication for hypertension. J Clin Endocrinol Metab 89:4153-4157
    • (2004) J Clin Endocrinol Metab , vol.89 , pp. 4153-4157
    • Calo, L.A.1    Pagnin, E.2    Davis, P.A.3
  • 133
    • 33847713292 scopus 로고    scopus 로고
    • Role of Rho kinases in PKG-mediated relaxation of pulmonary arteries of fetal lambs exposed to chronic high altitude hypoxia
    • Gao Y, Portugal AD, Negash S et al (2007) Role of Rho kinases in PKG-mediated relaxation of pulmonary arteries of fetal lambs exposed to chronic high altitude hypoxia. Am J Physiol Lung Cell Mol Physiol 292:L678-L684
    • (2007) Am J Physiol Lung Cell Mol Physiol , vol.292 , pp. L678-L684
    • Gao, Y.1    Portugal, A.D.2    Negash, S.3
  • 134
    • 14844343100 scopus 로고    scopus 로고
    • Multi-tasking RGS proteins in the heart: The next therapeutic target?
    • Riddle EL, Schwartzman RA, Bond M et al (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
  • 135
    • 33646852581 scopus 로고    scopus 로고
    • Reduced expression of regulator of G-protein signaling 2 (RGS2) in hypertensive patients increases calcium mobilization and ERK1/2 phosphorylation induced by angiotensin II
    • Semplicini A, Lenzini L, Sartori M et al (2006) Reduced expression of regulator of G-protein signaling 2 (RGS2) in hypertensive patients increases calcium mobilization and ERK1/2 phosphorylation induced by angiotensin II. J Hypertens 24:1115-1124
    • (2006) J Hypertens , vol.24 , pp. 1115-1124
    • Semplicini, A.1    Lenzini, L.2    Sartori, M.3
  • 136
    • 0016374975 scopus 로고
    • A highly sensitive adenylate cyclase assay
    • Salomon Y, Londos C, Rodbell M (1974) A highly sensitive adenylate cyclase assay. Anal Biochem 58:541-548
    • (1974) Anal Biochem , vol.58 , pp. 541-548
    • Salomon, Y.1    Londos, C.2    Rodbell, M.3
  • 137
    • 0037088586 scopus 로고    scopus 로고
    • Distinct residues in the carboxyl tail mediate agonist-induced desensitization and internalization of the human dopamine D-1 receptor
    • Lamey M, Thompson M, Varghese G et al (2002) Distinct residues in the carboxyl tail mediate agonist-induced desensitization and internalization of the human dopamine D-1 receptor. J Biol Chem 277:9415-9421
    • (2002) J Biol Chem , vol.277 , pp. 9415-9421
    • Lamey, M.1    Thompson, M.2    Varghese, G.3
  • 138
    • 0031747997 scopus 로고    scopus 로고
    • The role of receptor kinases and arrestins in G proteincoupled receptor regulation
    • Krupnick JG, Benovic JL (1998) The role of receptor kinases and arrestins in G proteincoupled receptor regulation. Annu Rev Pharmacol Toxicol 38:289-319
    • (1998) Annu Rev Pharmacol Toxicol , vol.38 , pp. 289-319
    • Krupnick, J.G.1    Benovic, J.L.2
  • 139
    • 0029122154 scopus 로고
    • Mechanism of rhodopsin phosphorylation
    • Zhao X, Palczewski K, Ohguro H (1995) Mechanism of rhodopsin phosphorylation. Biophys Chem 56:183-188
    • (1995) Biophys Chem , vol.56 , pp. 183-188
    • Zhao, X.1    Palczewski, K.2    Ohguro, H.3
  • 140
    • 0032851118 scopus 로고    scopus 로고
    • Regulation of D(1) dopamine receptors with mutations of protein kinase phosphorylation sites: Attenuation of the rate of agonist-induced desensitization
    • Jiang D, Sibley DR (1999) Regulation of D(1) dopamine receptors with mutations of protein kinase phosphorylation sites: attenuation of the rate of agonist-induced desensitization. Mol Pharmacol 56:675-683
    • (1999) Mol Pharmacol , vol.56 , pp. 675-683
    • Jiang, D.1    Sibley, D.R.2
  • 141
    • 0024397065 scopus 로고
    • Phosphorylation sites on two domains of the beta 2-adrenergic receptor are involved in distinct pathways of receptor desensitization
    • Hausdorff WP, Bouvier M, O’Dowd BF et al (1989) Phosphorylation sites on two domains of the beta 2-adrenergic receptor are involved in distinct pathways of receptor desensitization. J Biol Chem 264:12657-12665
    • (1989) J Biol Chem , vol.264 , pp. 12657-12665
    • Hausdorff, W.P.1    Bouvier, M.2    O’Dowd, B.F.3
  • 142
    • 0025250147 scopus 로고
    • Multiple pathways of rapid beta 2-adrenergic receptor desensitization. Delineation with specifi c inhibitors
    • Lohse MJ, Benovic JL, Caron MG et al (1990) Multiple pathways of rapid beta 2-adrenergic receptor desensitization. Delineation with specifi c inhibitors. J Biol Chem 265:3202-3211
    • (1990) J Biol Chem , vol.265 , pp. 3202-3211
    • Lohse, M.J.1    Benovic, J.L.2    Caron, M.G.3
  • 143
    • 0027375964 scopus 로고
    • Molecular mechanisms of membrane receptor desensitization
    • Lohse MJ (1993) Molecular mechanisms of membrane receptor desensitization. Biochim Biophys Acta 1179:171-188
    • (1993) Biochim Biophys Acta , vol.1179 , pp. 171-188
    • Lohse, M.J.1
  • 144
    • 0031597626 scopus 로고    scopus 로고
    • Homologous desensitization of the D1A dopamine receptor: Effi cacy in causing desensitization dissociates from both receptor occupancy and functional potency
    • Lewis MM, Watts VJ, Lawler CP et al (1998) Homologous desensitization of the D1A dopamine receptor: effi cacy in causing desensitization dissociates from both receptor occupancy and functional potency. J Pharmacol Exp Ther 286:345-353
    • (1998) J Pharmacol Exp Ther , vol.286 , pp. 345-353
    • Lewis, M.M.1    Watts, V.J.2    Lawler, C.P.3
  • 145
    • 0028053755 scopus 로고
    • Oligodeoxynucleotides antisense to mRNA encoding protein kinase A, protein kinase C, and beta-adrenergic receptor kinase reveal distinctive cell-type-specifi c roles in agonistinduced desensitization
    • Shih M, Malbon CC (1994) Oligodeoxynucleotides antisense to mRNA encoding protein kinase A, protein kinase C, and beta-adrenergic receptor kinase reveal distinctive cell-type-specifi c roles in agonistinduced desensitization. Proc Natl Acad Sci U S A 91:12193-12197
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 12193-12197
    • Shih, M.1    Malbon, C.C.2
  • 146
    • 0025788724 scopus 로고
    • Comparative rates of desensitization of beta-adrenergic receptors by the betaadrenergic receptor kinase and the cyclic AMP-dependent protein kinase
    • Roth NS, Campbell PT, Caron MG et al (1991) Comparative rates of desensitization of beta-adrenergic receptors by the betaadrenergic receptor kinase and the cyclic AMP-dependent protein kinase. Proc Natl Acad Sci U S A 88:6201-6204
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 6201-6204
    • Roth, N.S.1    Campbell, P.T.2    Caron, M.G.3
  • 147
    • 0028916344 scopus 로고
    • Four consecutive serines in the third intracellular loop are the sites for beta-adrenergic receptor kinase-mediated phosphorylation and desensitization of the alpha 2A-adrenergic receptor
    • Eason MG, Moreira SP, Liggett SB (1995) Four consecutive serines in the third intracellular loop are the sites for beta-adrenergic receptor kinase-mediated phosphorylation and desensitization of the alpha 2A-adrenergic receptor. J Biol Chem 270:4681-4688
    • (1995) J Biol Chem , vol.270 , pp. 4681-4688
    • Eason, M.G.1    Moreira, S.P.2    Liggett, S.B.3
  • 148
    • 0030699386 scopus 로고    scopus 로고
    • Characterization of the phosphorylation sites involved in G protein-coupled receptor kinase and protein kinase C-mediated desensitization of the alpha1B-adrenergic receptor
    • Diviani D, Lattion AL, Cotecchia S (1997) Characterization of the phosphorylation sites involved in G protein-coupled receptor kinase and protein kinase C-mediated desensitization of the alpha1B-adrenergic receptor. J Biol Chem 272:28712-28719
    • (1997) J Biol Chem , vol.272 , pp. 28712-28719
    • Diviani, D.1    Lattion, A.L.2    Cotecchia, S.3
  • 149
    • 0033569754 scopus 로고    scopus 로고
    • Differential phosphorylation paradigms dictate desensitization and internalization of the N-formyl peptide receptor
    • Maestes DC, Potter RM, Prossnitz ER (1999) Differential phosphorylation paradigms dictate desensitization and internalization of the N-formyl peptide receptor. J Biol Chem 274:29791-29795
    • (1999) J Biol Chem , vol.274 , pp. 29791-29795
    • Maestes, D.C.1    Potter, R.M.2    Prossnitz, E.R.3
  • 150
    • 0032570554 scopus 로고    scopus 로고
    • Internalization and down-regulation of human muscarinic acetylcholine receptor m2 subtypes. Role of third intracellular m2 loop and G protein-coupled receptor kinase 2
    • Tsuga H, Kameyama K, Haga T et al (1998) Internalization and down-regulation of human muscarinic acetylcholine receptor m2 subtypes. Role of third intracellular m2 loop and G protein-coupled receptor kinase 2. J Biol Chem 273:5323-5330
    • (1998) J Biol Chem , vol.273 , pp. 5323-5330
    • Tsuga, H.1    Kameyama, K.2    Haga, T.3
  • 151
    • 0031009124 scopus 로고    scopus 로고
    • Two homologous phosphorylation domains differentially contribute to desensitization and internalization of the m2 muscarinic acetyl-choline receptor
    • Pals-Rylaarsdam R, Hosey MM (1997) Two homologous phosphorylation domains differentially contribute to desensitization and internalization of the m2 muscarinic acetyl-choline receptor. J Biol Chem 272:14152-14158
    • (1997) J Biol Chem , vol.272 , pp. 14152-14158
    • Pals-Rylaarsdam, R.1    Hosey, M.M.2
  • 152
    • 0030020424 scopus 로고    scopus 로고
    • Differential regulation of dopamine D1 receptor responsiveness by various G proteincoupled receptor kinases
    • Tiberi M, Nash SR, Bertrand L et al (1996) Differential regulation of dopamine D1 receptor responsiveness by various G proteincoupled receptor kinases. J Biol Chem 271:3771-3778
    • (1996) J Biol Chem , vol.271 , pp. 3771-3778
    • Tiberi, M.1    Nash, S.R.2    Bertrand, L.3
  • 153
    • 0023897940 scopus 로고
    • Removal of phosphorylation sites from the beta 2-adrenergic receptor delays onset of agonist-promoted desensitization
    • Bouvier M, Hausdorff WP, de Blasi A et al (1988) Removal of phosphorylation sites from the beta 2-adrenergic receptor delays onset of agonist-promoted desensitization. Nature 333:370-373
    • (1988) Nature , vol.333 , pp. 370-373
    • Bouvier, M.1    Hausdorff, W.P.2    De Blasi, A.3
  • 154
    • 0026356171 scopus 로고
    • A small region of the betaadrenergic receptor is selectively involved in its rapid regulation
    • Hausdorff WP, Campbell PT, Ostrowski J et al (1991) A small region of the betaadrenergic receptor is selectively involved in its rapid regulation. Proc Natl Acad Sci U S A 88:2979-2983
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 2979-2983
    • Hausdorff, W.P.1    Campbell, P.T.2    Ostrowski, J.3
  • 155
    • 0029884416 scopus 로고    scopus 로고
    • Identifi cation of the G proteincoupled receptor kinase phosphorylation sites in the human beta2-adrenergic receptor
    • Fredericks ZL, Pitcher JA, Lefkowitz RJ (1996) Identifi cation of the G proteincoupled receptor kinase phosphorylation sites in the human beta2-adrenergic receptor. J Biol Chem 271:13796-13803
    • (1996) J Biol Chem , vol.271 , pp. 13796-13803
    • Fredericks, Z.L.1    Pitcher, J.A.2    Lefkowitz, R.J.3
  • 156
    • 0032571003 scopus 로고    scopus 로고
    • Desensitization of beta2-adrenergic receptors with mutations of the proposed G protein-coupled receptor kinase phosphorylation sites
    • Seibold A, January BG, Friedman J et al (1998) Desensitization of beta2-adrenergic receptors with mutations of the proposed G protein-coupled receptor kinase phosphorylation sites. J Biol Chem 273:7637-7642
    • (1998) J Biol Chem , vol.273 , pp. 7637-7642
    • Seibold, A.1    January, B.G.2    Friedman, J.3
  • 157
    • 0030875721 scopus 로고    scopus 로고
    • Agonist-induced desensitization of the mu opioid receptor is determined by threonine 394 preceded by acidic amino acids in the COOH-terminal tail
    • Pak Y, O’Dowd BF, George SR (1997) Agonist-induced desensitization of the mu opioid receptor is determined by threonine 394 preceded by acidic amino acids in the COOH-terminal tail. J Biol Chem 272:24961-24965
    • (1997) J Biol Chem , vol.272 , pp. 24961-24965
    • Pak, Y.1    O’Dowd, B.F.2    George, S.R.3
  • 158
    • 0033789012 scopus 로고    scopus 로고
    • Identifi cation of G protein-coupled receptor kinase 2 phosphorylation sites responsible for agonist-stimulated delta-opioid receptor phosphorylation
    • Guo J, Wu Y, Zhang W et al (2000) Identifi cation of G protein-coupled receptor kinase 2 phosphorylation sites responsible for agonist-stimulated delta-opioid receptor phosphorylation. Mol Pharmacol 58:1050-1056
    • (2000) Mol Pharmacol , vol.58 , pp. 1050-1056
    • Guo, J.1    Wu, Y.2    Zhang, W.3
  • 159
    • 0028818439 scopus 로고
    • Agonist-dependent phosphorylation and desensitization of the rat A3 adenosine receptor. Evidence for a G-protein-coupled receptor kinase-mediated mechanism
    • Palmer TM, Benovic JL, Stiles GL (1995) Agonist-dependent phosphorylation and desensitization of the rat A3 adenosine receptor. Evidence for a G-protein-coupled receptor kinase-mediated mechanism. J Biol Chem 270:29607-29613
    • (1995) J Biol Chem , vol.270 , pp. 29607-29613
    • Palmer, T.M.1    Benovic, J.L.2    Stiles, G.L.3
  • 160
    • 0030614357 scopus 로고    scopus 로고
    • Identifi cation of an A2a adenosine receptor domain specifi-cally responsible for mediating short-term desensitization
    • Palmer TM, Stiles GL (1997) Identifi cation of an A2a adenosine receptor domain specifi-cally responsible for mediating short-term desensitization. Biochemistry 36:832-838
    • (1997) Biochemistry , vol.36 , pp. 832-838
    • Palmer, T.M.1    Stiles, G.L.2
  • 161
    • 0034006037 scopus 로고    scopus 로고
    • Identifi cation of threonine residues controlling the agonistdependent phosphorylation and desensitization of the rat A(3) adenosine receptor
    • Palmer TM, Stiles GL (2000) Identifi cation of threonine residues controlling the agonistdependent phosphorylation and desensitization of the rat A(3) adenosine receptor. Mol Pharmacol 57:539-545
    • (2000) Mol Pharmacol , vol.57 , pp. 539-545
    • Palmer, T.M.1    Stiles, G.L.2
  • 162
    • 4444323793 scopus 로고    scopus 로고
    • Identifi cation of a novel endocytic recycling signal in the D1 dopamine receptor
    • Vargas GA, von Zastrow M (2004) Identifi cation of a novel endocytic recycling signal in the D1 dopamine receptor. J Biol Chem 279:37461-37469
    • (2004) J Biol Chem , vol.279 , pp. 37461-37469
    • Vargas, G.A.1    Von Zastrow, M.2
  • 163
    • 0029066872 scopus 로고
    • Rhodopsin phosphorylation and dephosphorylation in vivo
    • Ohguro H, Van Hooser JP, Milam AH et al (1995) Rhodopsin phosphorylation and dephosphorylation in vivo. J Biol Chem 270:14259-14262
    • (1995) J Biol Chem , vol.270 , pp. 14259-14262
    • Ohguro, H.1    Van Hooser, J.P.2    Milam, A.H.3
  • 164
    • 80051646969 scopus 로고    scopus 로고
    • Phosphorylation barcoding as a mechanism of directing GPCR signaling
    • Liggett SB (2011) Phosphorylation barcoding as a mechanism of directing GPCR signaling. Sci Signal 4(185):pe36. doi: 10.1126?scisignal.2002331
    • (2011) Sci Signal , vol.4 , Issue.185
    • Liggett, S.B.1
  • 165
    • 1542349921 scopus 로고    scopus 로고
    • The role of phosphorylation in D1 Dopamine receptor desensitization: Evidence for a novel mechanism of arrestin association
    • Kim OJ, Gardner BR, Williams DB et al (2004) The role of phosphorylation in D1 Dopamine receptor desensitization: evidence for a novel mechanism of arrestin association. J Biol Chem 279:7999-8010
    • (2004) J Biol Chem , vol.279 , pp. 7999-8010
    • Kim, O.J.1    Gardner, B.R.2    Williams, D.B.3
  • 166
    • 0030460743 scopus 로고    scopus 로고
    • G-protein-coupled receptor regulation: Role of G-protein-coupled receptor kinases and arrestins
    • Ferguson SS, Barak LS, Zhang J et al (1996) G-protein-coupled receptor regulation: role of G-protein-coupled receptor kinases and arrestins. Can J Physiol Pharmacol 74:1095-1110
    • (1996) Can J Physiol Pharmacol , vol.74 , pp. 1095-1110
    • Ferguson, S.S.1    Barak, L.S.2    Zhang, J.3
  • 167
    • 0030593035 scopus 로고    scopus 로고
    • Role of beta-arrestin in mediating agonist-promoted G protein-coupled receptor internalization
    • Ferguson SS, Downey WE, Colapietro AM et al (1996) Role of beta-arrestin in mediating agonist-promoted G protein-coupled receptor internalization. Science 271:363-366
    • (1996) Science , vol.271 , pp. 363-366
    • Ferguson, S.S.1    Downey, W.E.2    Colapietro, A.M.3
  • 168
    • 0032579389 scopus 로고    scopus 로고
    • Infl uence of the cytosolic carboxyl termini of human B1 and B2 kinin receptors on receptor sequestration, ligand internalization, and signal transduction
    • Faussner A, Proud D, Towns M et al (1998) Infl uence of the cytosolic carboxyl termini of human B1 and B2 kinin receptors on receptor sequestration, ligand internalization, and signal transduction. J Biol Chem 273:2617-2623
    • (1998) J Biol Chem , vol.273 , pp. 2617-2623
    • Faussner, A.1    Proud, D.2    Towns, M.3
  • 170
    • 0028829471 scopus 로고
    • Desensitization and internalization of the m2 muscarinic acetylcholine receptor are directed by independent mechanisms
    • Pals-Rylaarsdam R, Xu Y, Witt-Enderby P et al (1995) Desensitization and internalization of the m2 muscarinic acetylcholine receptor are directed by independent mechanisms. J Biol Chem 270:29004-29011
    • (1995) J Biol Chem , vol.270 , pp. 29004-29011
    • Pals-Rylaarsdam, R.1    Xu, Y.2    Witt-Enderby, P.3
  • 171
    • 0033789017 scopus 로고    scopus 로고
    • Localization of the sites mediating desensitization of the beta(2)-adrenergic receptor by the GRK pathway
    • Seibold A, Williams B, Huang ZF et al (2000) Localization of the sites mediating desensitization of the beta(2)-adrenergic receptor by the GRK pathway. Mol Pharmacol 58:1162-1173
    • (2000) Mol Pharmacol , vol.58 , pp. 1162-1173
    • Seibold, A.1    Williams, B.2    Huang, Z.F.3
  • 172
    • 0033600736 scopus 로고    scopus 로고
    • Agonist-induced G protein-dependent and-independent down-regulation of the mu opioid receptor. The receptor is a direct substrate for protein-tyrosine kinase
    • Pak Y, O’Dowd BF, Wang JB et al (1999) Agonist-induced G protein-dependent and-independent down-regulation of the mu opioid receptor. The receptor is a direct substrate for protein-tyrosine kinase. J Biol Chem 274:27610-27616
    • (1999) J Biol Chem , vol.274 , pp. 27610-27616
    • Pak, Y.1    O’Dowd, B.F.2    Wang, J.B.3
  • 173
    • 0034028438 scopus 로고    scopus 로고
    • Internalization and recycling of delta-opioid receptor are dependent on a phosphorylationdephosphorylation mechanism
    • Hasbi A, Allouche S, Sichel F et al (2000) Internalization and recycling of delta-opioid receptor are dependent on a phosphorylationdephosphorylation mechanism. J Biol Chem 293:237-247
    • (2000) J Biol Chem , vol.293 , pp. 237-247
    • Hasbi, A.1    Allouche, S.2    Sichel, F.3
  • 174
    • 0035839489 scopus 로고    scopus 로고
    • Rapid agonist-induced desensitization and internalization of the a2b adenosine receptor is mediated by a serine residue close to the COOH terminus
    • Mathuru AL, Mundell SL, Benovic JL et al (2001) Rapid agonist-induced desensitization and internalization of the a2b adenosine receptor is mediated by a serine residue close to the COOH terminus. J Biochem 276:30199-30207
    • (2001) J Biochem , vol.276 , pp. 30199-30207
    • Mathuru, A.L.1    Mundell, S.L.2    Benovic, J.L.3
  • 175
    • 0029790078 scopus 로고    scopus 로고
    • Role of receptor phosphorylation in desensitization and internalization of the secretin receptor
    • Holtmann MH, Roettger BF, Pinon DI et al (1996) Role of receptor phosphorylation in desensitization and internalization of the secretin receptor. J Biol Chem 271:23566-23571
    • (1996) J Biol Chem , vol.271 , pp. 23566-23571
    • Holtmann, M.H.1    Roettger, B.F.2    Pinon, D.I.3
  • 176
    • 0035163581 scopus 로고    scopus 로고
    • The palmitoylation state of the beta2-adrenergic receptor regulates the synergistic action of cyclic AMP-dependent protein kinase and beta2-adrenergic receptor kinase involved in its phosphorylation and desensitization
    • Moffett S, Rousseau G, Lagace M et al (2001) The palmitoylation state of the beta2-adrenergic receptor regulates the synergistic action of cyclic AMP-dependent protein kinase and beta2-adrenergic receptor kinase involved in its phosphorylation and desensitization. J Neurochem 76:269-279
    • (2001) J Neurochem , vol.76 , pp. 269-279
    • Moffett, S.1    Rousseau, G.2    Lagace, M.3
  • 177
    • 0034737475 scopus 로고    scopus 로고
    • Arrestin binding to the M(2) muscarinic acetylcholine receptor is precluded by an inhibitory element in the third intracellular loop of the receptor
    • Lee KB, Ptasienski JA, Pals-Rylaarsdam R et al (2000) Arrestin binding to the M(2) muscarinic acetylcholine receptor is precluded by an inhibitory element in the third intracellular loop of the receptor. J Biol Chem 275:9284-9289
    • (2000) J Biol Chem , vol.275 , pp. 9284-9289
    • Lee, K.B.1    Ptasienski, J.A.2    Pals-Rylaarsdam, R.3
  • 178
    • 0029770657 scopus 로고    scopus 로고
    • Beta-arrestin acts as a clathrin adaptor in endocytosis of the beta2-adrenergic receptor
    • Goodman OB Jr, Krupnick JG, Santini F et al (1996) Beta-arrestin acts as a clathrin adaptor in endocytosis of the beta2-adrenergic receptor. Nature 383:447-450
    • (1996) Nature , vol.383 , pp. 447-450
    • Goodman, O.B.1    Krupnick, J.G.2    Santini, F.3
  • 179
    • 0028898261 scopus 로고
    • Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding
    • Hinshaw JE, Schmid SL (1995) Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding. Nature 374:190-192
    • (1995) Nature , vol.374 , pp. 190-192
    • Hinshaw, J.E.1    Schmid, S.L.2
  • 180
    • 0028923349 scopus 로고
    • Tubular membrane invaginations coated by dynamin rings are induced by GTPgamma S in nerve terminals
    • Takei K, McPherson PS, Schmid SL et al (1995) Tubular membrane invaginations coated by dynamin rings are induced by GTPgamma S in nerve terminals. Nature 374: 186-190
    • (1995) Nature , vol.374 , pp. 186-190
    • Takei, K.1    McPherson, P.S.2    Schmid, S.L.3
  • 181
    • 0026928718 scopus 로고
    • The mechanism of receptor-mediated endocytosis—more questions than answers
    • Schmid SL (1992) The mechanism of receptor-mediated endocytosis—more questions than answers. Bioessays 14:589-596
    • (1992) Bioessays , vol.14 , pp. 589-596
    • Schmid, S.L.1
  • 182
    • 0032563291 scopus 로고    scopus 로고
    • G protein-coupled receptors. III. New roles for receptor kinases and beta-arrestins in receptor signaling and desensitization
    • Lefkowitz RJ (1998) G protein-coupled receptors. III. New roles for receptor kinases and beta-arrestins in receptor signaling and desensitization. J Biol Chem 273: 18677-18680
    • (1998) J Biol Chem , vol.273 , pp. 18677-18680
    • Lefkowitz, R.J.1
  • 183
    • 0029719789 scopus 로고    scopus 로고
    • Desensitization of G protein-coupled receptors
    • Freedman NJ, Lefkowitz RJ (1996) Desensitization of G protein-coupled receptors. Recent Prog Horm Res 51:319-351
    • (1996) Recent Prog Horm Res , vol.51 , pp. 319-351
    • Freedman, N.J.1    Lefkowitz, R.J.2
  • 185
    • 0031036520 scopus 로고    scopus 로고
    • The role of sequestration in G proteincoupled receptor resensitization. Regulation of beta2-adrenergic receptor dephosphorylation by vesicular acidifi cation
    • Krueger KM, Daaka Y, Pitcher JA et al (1997) The role of sequestration in G proteincoupled receptor resensitization. Regulation of beta2-adrenergic receptor dephosphorylation by vesicular acidifi cation. J Biol Chem 272:5-8
    • (1997) J Biol Chem , vol.272 , pp. 5-8
    • Krueger, K.M.1    Daaka, Y.2    Pitcher, J.A.3
  • 186
    • 0028986859 scopus 로고
    • Sequestration and recycling of beta 2-adrenergic receptors permit receptor resensitization
    • Pippig S, Andexinger S, Lohse MJ (1995) Sequestration and recycling of beta 2-adrenergic receptors permit receptor resensitization. Mol Pharmacol 47:666-676
    • (1995) Mol Pharmacol , vol.47 , pp. 666-676
    • Pippig, S.1    Exinger, S.2    Lohse, M.J.3
  • 187
    • 0030756892 scopus 로고    scopus 로고
    • Endocytosis and recycling of G proteincoupled receptors
    • Koenig JA, Edwardson JM (1997) Endocytosis and recycling of G proteincoupled receptors. Trends Pharmacol Sci 18:276-287
    • (1997) Trends Pharmacol Sci , vol.18 , pp. 276-287
    • Koenig, J.A.1    Edwardson, J.M.2
  • 188
    • 0028000662 scopus 로고
    • A highly conserved tyrosine residue in G protein-coupled receptors is required for agonist-mediated beta 2-adrenergic receptor sequestration
    • Barak LS, Tiberi M, Freedman NJ et al (1994) A highly conserved tyrosine residue in G protein-coupled receptors is required for agonist-mediated beta 2-adrenergic receptor sequestration. J Biol Chem 269:2790-2795
    • (1994) J Biol Chem , vol.269 , pp. 2790-2795
    • Barak, L.S.1    Tiberi, M.2    Freedman, N.J.3
  • 189
    • 0030812586 scopus 로고    scopus 로고
    • A dileucine motif in the C terminus of the beta2-adrenergic receptor is involved in receptor internalization
    • Gabilondo AM, Hegler J, Krasel C et al (1997) A dileucine motif in the C terminus of the beta2-adrenergic receptor is involved in receptor internalization. Proc Natl Acad Sci U S A 94:12285-12290
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 12285-12290
    • Gabilondo, A.M.1    Hegler, J.2    Krasel, C.3
  • 190
    • 0032742961 scopus 로고    scopus 로고
    • Role of the carboxyl-terminal region, di-leucine motif and cysteine residues in signalling and internalization of vasopressin V1a receptor
    • Preisser L, Ancellin N, Michaelis L et al (1999) Role of the carboxyl-terminal region, di-leucine motif and cysteine residues in signalling and internalization of vasopressin V1a receptor. FEBS Lett 460:303-308
    • (1999) FEBS Lett , vol.460 , pp. 303-308
    • Preisser, L.1    Ancellin, N.2    Michaelis, L.3
  • 191
    • 0027239858 scopus 로고
    • Serines and threonines in the gastrin-releasing peptide receptor carboxyl terminus mediate internalization
    • Benya RV, Fathi Z, Battey JF et al (1993) Serines and threonines in the gastrin-releasing peptide receptor carboxyl terminus mediate internalization. J Biol Chem 268: 20285-20290
    • (1993) J Biol Chem , vol.268 , pp. 20285-20290
    • Benya, R.V.1    Fathi, Z.2    Battey, J.F.3
  • 192
    • 0030816392 scopus 로고    scopus 로고
    • Phosphorylation of four amino acid residues in the carboxyl terminus of the rat somatostatin receptor subtype 3 is crucial for its desensitization and internalization
    • Roth A, Kreienkamp HJ, Meyerhof W et al (1997) Phosphorylation of four amino acid residues in the carboxyl terminus of the rat somatostatin receptor subtype 3 is crucial for its desensitization and internalization. J Biol Chem 272:23769-23774
    • (1997) J Biol Chem , vol.272 , pp. 23769-23774
    • Roth, A.1    Kreienkamp, H.J.2    Meyerhof, W.3
  • 193
    • 0033617468 scopus 로고    scopus 로고
    • Bradykinin-induced internalization of the human B2 receptor requires phosphorylation of three serine and two threonine residues at its carboxyl tail
    • Pizard A, Blaukat A, Muller-Esterl W et al (1999) Bradykinin-induced internalization of the human B2 receptor requires phosphorylation of three serine and two threonine residues at its carboxyl tail. J Biol Chem 274:12738-12747
    • (1999) J Biol Chem , vol.274 , pp. 12738-12747
    • Pizard, A.1    Blaukat, A.2    Muller-Esterl, W.3
  • 194
    • 0026040191 scopus 로고
    • Consensus sequences as substrate specifi city determinants for protein kinases and protein phosphatases
    • Kennelly PJ, Krebs EG (1991) Consensus sequences as substrate specifi city determinants for protein kinases and protein phosphatases. J Biol Chem 266:15555-15558
    • (1991) J Biol Chem , vol.266 , pp. 15555-15558
    • Kennelly, P.J.1    Krebs, E.G.2
  • 195
    • 0025742855 scopus 로고
    • Role of acidic amino acids in peptide substrates of the beta-adrenergic receptor kinase and rhodopsin kinase
    • Onorato JJ, Palczewski K, Regan JW et al (1991) Role of acidic amino acids in peptide substrates of the beta-adrenergic receptor kinase and rhodopsin kinase. Biochemistry 30:5118-5125
    • (1991) Biochemistry , vol.30 , pp. 5118-5125
    • Onorato, J.J.1    Palczewski, K.2    Regan, J.W.3
  • 196
    • 0027368165 scopus 로고
    • Structure and mechanism of the G proteincoupled receptor kinases
    • Inglese J, Freedman NJ, Koch WJ et al (1993) Structure and mechanism of the G proteincoupled receptor kinases. J Biol Chem 268:23735-23738
    • (1993) J Biol Chem , vol.268 , pp. 23735-23738
    • Inglese, J.1    Freedman, N.J.2    Koch, W.J.3
  • 197
    • 0029823556 scopus 로고    scopus 로고
    • Monoclonal antibodies reveal receptor specifi city among G-proteincoupled receptor kinases
    • Oppermann M, Diverse-Pierluissi M, Drazner MH et al (1996) Monoclonal antibodies reveal receptor specifi city among G-proteincoupled receptor kinases. Proc Natl Acad Sci U S A 93:7649-7654
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 7649-7654
    • Oppermann, M.1    Diverse-Pierluissi, M.2    Drazner, M.H.3
  • 198
    • 0035789765 scopus 로고    scopus 로고
    • Characterization of human GRK7 as a potential cone opsin kinase
    • Chen CK, Zhang K, Church-Kopish J et al (2001) Characterization of human GRK7 as a potential cone opsin kinase. Mol Vis 7:305-313
    • (2001) Mol Vis , vol.7 , pp. 305-313
    • Chen, C.K.1    Zhang, K.2    Church-Kopish, J.3
  • 199
    • 0033645593 scopus 로고    scopus 로고
    • Effect of activating and inactivating mutations on the phosphorylation and traffi cking of the human lutropin?Choriogonadotropin receptor
    • Min L, Ascoli M (2000) Effect of activating and inactivating mutations on the phosphorylation and traffi cking of the human lutropin?choriogonadotropin receptor. Mol Endocrinol 14:1797-1810
    • (2000) Mol Endocrinol , vol.14 , pp. 1797-1810
    • Min, L.1    Ascoli, M.2
  • 200
    • 0027992129 scopus 로고
    • Expression, purifi cation, and characterization of the G protein-coupled receptor kinase GRK6
    • Loudon RP, Benovic JL (1994) Expression, purifi cation, and characterization of the G protein-coupled receptor kinase GRK6. J Biol Chem 269:22691-22697
    • (1994) J Biol Chem , vol.269 , pp. 22691-22697
    • Loudon, R.P.1    Benovic, J.L.2
  • 201
    • 33644841768 scopus 로고    scopus 로고
    • The D1 dopamine receptor is constitutively phosphorylated by G protein-coupled receptor kinase 4
    • Rankin ML, Marinec PS, Cabrera DM et al (2006) The D1 dopamine receptor is constitutively phosphorylated by G protein-coupled receptor kinase 4. Mol Pharmacol 69: 759-769
    • (2006) Mol Pharmacol , vol.69 , pp. 759-769
    • Rankin, M.L.1    Marinec, P.S.2    Cabrera, D.M.3
  • 202
    • 33748430810 scopus 로고    scopus 로고
    • D1 Dopamine receptor hyperphosphorylation in renal proximal tubules in hypertension
    • Yu P, Asico LD, Luo Y et al (2006) D1 Dopamine receptor hyperphosphorylation in renal proximal tubules in hypertension. Kidney Int 70:1072-1079
    • (2006) Kidney Int , vol.70 , pp. 1072-1079
    • Yu, P.1    Asico, L.D.2    Luo, Y.3
  • 203
    • 33750431036 scopus 로고    scopus 로고
    • Mechanisms of disease: The role of GRK4 in the etiology of essential hypertension and salt sensitivity
    • Felder RA, Jose PA (2006) Mechanisms of disease: the role of GRK4 in the etiology of essential hypertension and salt sensitivity. Nat Clin Pract Nephrol 2:637-650
    • (2006) Nat Clin Pract Nephrol , vol.2 , pp. 637-650
    • Felder, R.A.1    Jose, P.A.2
  • 204
    • 0033744611 scopus 로고    scopus 로고
    • Molecular genetics of Oguchi disease, fundus albipunctatus, and other forms of stationary night blindness: LVII Edward Jackson Memorial Lecture
    • Dryja TP (2000) Molecular genetics of Oguchi disease, fundus albipunctatus, and other forms of stationary night blindness: LVII Edward Jackson Memorial Lecture. Am J Ophthalmol 130:547-563
    • (2000) Am J Ophthalmol , vol.130 , pp. 547-563
    • Dryja, T.P.1
  • 205
    • 0029741177 scopus 로고    scopus 로고
    • The relationship between visual fi eld size and electroretinogram amplitude in retinitis pigmentosa
    • Sandberg MA, Weigel-DiFranco C, Rosner B et al (1996) The relationship between visual fi eld size and electroretinogram amplitude in retinitis pigmentosa. Invest Ophthalmol Vis Sci 37:1693-1698
    • (1996) Invest Ophthalmol Vis Sci , vol.37 , pp. 1693-1698
    • Sandberg, M.A.1    Weigel-Difranco, C.2    Rosner, B.3
  • 206
    • 0031892644 scopus 로고    scopus 로고
    • Null mutation in the rhodopsin kinase gene slows recovery kinetics of rod and cone phototransduction in man
    • Cideciyan AV, Zhao X, Nielsen L et al (1998) Null mutation in the rhodopsin kinase gene slows recovery kinetics of rod and cone phototransduction in man. Proc Natl Acad Sci U S A 95:328-333
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 328-333
    • Cideciyan, A.V.1    Zhao, X.2    Nielsen, L.3
  • 207
    • 0029093559 scopus 로고
    • G protein-coupled receptor structure and function: The impact of disease-causing mutations
    • Shenker A (1995) G protein-coupled receptor structure and function: the impact of disease-causing mutations. Baillieres Clin Endocrinol Metab 9:427-451
    • (1995) Baillieres Clin Endocrinol Metab , vol.9 , pp. 427-451
    • Shenker, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.