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Volumn 51, Issue 4, 2003, Pages 194-214

G protein-regulated signaling dysfunction in human disease

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN RECEPTOR KINASE; UNCLASSIFIED DRUG;

EID: 0038504710     PISSN: 17088267     EISSN: None     Source Type: Journal    
DOI: 10.1136/jim-51-04-21     Document Type: Review
Times cited : (6)

References (215)
  • 1
    • 0001604424 scopus 로고
    • The relation of adenosine-3′,5′-phosphate and phosphorylase to the actions of catecholamines and other hormones
    • Sutherland EW, Rall TW. The relation of adenosine-3′,5′-phosphate and phosphorylase to the actions of catecholamines and other hormones. Pharmacol Rev 1960;12:265-99.
    • (1960) Pharmacol Rev , vol.12 , pp. 265-299
    • Sutherland, E.W.1    Rall, T.W.2
  • 2
    • 0032402450 scopus 로고    scopus 로고
    • Molecular basis of receptor/G-protein-coupling selectivity
    • Wess J. Molecular basis of receptor/G-protein-coupling selectivity. Pharmacol Ther 1998;80:231-64.
    • (1998) Pharmacol Ther , vol.80 , pp. 231-264
    • Wess, J.1
  • 4
    • 0033118334 scopus 로고    scopus 로고
    • Molecular tinkering of G protein-coupled receptors: An evolutionary success
    • Bockaert J, Pin JP. Molecular tinkering of G protein-coupled receptors: an evolutionary success. EMBO J 1999;18:1723-9.
    • (1999) EMBO J , vol.18 , pp. 1723-1729
    • Bockaert, J.1    Pin, J.P.2
  • 5
    • 0037131192 scopus 로고    scopus 로고
    • Regulation of G protein-coupled receptor signaling by scaffold proteins
    • Hall RA, Lefkowitz RJ. Regulation of G protein-coupled receptor signaling by scaffold proteins. Circ Res 2002;91:672-80.
    • (2002) Circ Res , vol.91 , pp. 672-680
    • Hall, R.A.1    Lefkowitz, R.J.2
  • 6
    • 0035336844 scopus 로고    scopus 로고
    • Signaling at zero G: G-protein-independent functions for 7-TM receptors
    • Brzostowski JA, Kimmel AR. Signaling at zero G: G-protein-independent functions for 7-TM receptors, Trends Biochem Sci 2001;26:291-27.
    • (2001) Trends Biochem Sci , vol.26 , pp. 291-327
    • Brzostowski, J.A.1    Kimmel, A.R.2
  • 7
    • 0034307486 scopus 로고    scopus 로고
    • G-protein-independent signaling by G-protein-coupled receptors
    • Heuss C, Gerber U. G-protein-independent signaling by G-protein-coupled receptors. Trends Neurosci 2000;23:469-75.
    • (2000) Trends Neurosci , vol.23 , pp. 469-475
    • Heuss, C.1    Gerber, U.2
  • 9
    • 0029664589 scopus 로고    scopus 로고
    • The 2.0 Å crystal structure of a heterotrimeric G protein
    • Lambright DG, Sondek J, Bohm A, et al. The 2.0 Å crystal structure of a heterotrimeric G protein. Nature 1996;379:311-9.
    • (1996) Nature , vol.379 , pp. 311-319
    • Lambright, D.G.1    Sondek, J.2    Bohm, A.3
  • 11
    • 0035931919 scopus 로고    scopus 로고
    • Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 Å
    • Slep KC, Kercher MA, He W, et al. Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 Å. Nature 2001;409:1071-7.
    • (2001) Nature , vol.409 , pp. 1071-1077
    • Slep, K.C.1    Kercher, M.A.2    He, W.3
  • 13
    • 0033199157 scopus 로고    scopus 로고
    • Emerging roles for RGS proteins in cell signalling
    • Hepler JR. Emerging roles for RGS proteins in cell signalling. Trends Pharmacol Sci 1999;20:376-82.
    • (1999) Trends Pharmacol Sci , vol.20 , pp. 376-382
    • Hepler, J.R.1
  • 15
    • 0033783132 scopus 로고    scopus 로고
    • GTPase-activating proteins for heterotrimeric G proteins: Regulators of G protein signaling (RGS) and RGS-like proteins
    • Ross EM, Wilkie TM. GTPase-activating proteins for heterotrimeric G proteins: regulators of G protein signaling (RGS) and RGS-like proteins. Annu Rev Biochem 2000;69:795-827.
    • (2000) Annu Rev Biochem , vol.69 , pp. 795-827
    • Ross, E.M.1    Wilkie, T.M.2
  • 17
    • 0033605294 scopus 로고    scopus 로고
    • A novel PDZ domain containing guanine nucleotide exchange factor links heterotrimeric G proteins to Rho
    • Fukuhara S, Murga C, Zohar M, et al. A novel PDZ domain containing guanine nucleotide exchange factor links heterotrimeric G proteins to Rho. J Biol Chem 1999;274:5868-79.
    • (1999) J Biol Chem , vol.274 , pp. 5868-5879
    • Fukuhara, S.1    Murga, C.2    Zohar, M.3
  • 18
    • 0035398487 scopus 로고    scopus 로고
    • G-protein-coupled receptors and signaling networks: Emerging paradigms
    • Marinissen MJ, Gutkind JS. G-protein-coupled receptors and signaling networks: emerging paradigms. Trends Pharmacol Sci 2001;22:368-76.
    • (2001) Trends Pharmacol Sci , vol.22 , pp. 368-376
    • Marinissen, M.J.1    Gutkind, J.S.2
  • 21
    • 0033119012 scopus 로고    scopus 로고
    • The expanding spectrum of G protein diseases
    • Farfel Z, Bourne HR, Iiri T. The expanding spectrum of G protein diseases. N Engl J Med 1999;340:1012-20.
    • (1999) N Engl J Med , vol.340 , pp. 1012-1020
    • Farfel, Z.1    Bourne, H.R.2    Iiri, T.3
  • 22
    • 0034718938 scopus 로고    scopus 로고
    • Graves' disease
    • Weetman AP. Graves' disease. N Engl J Med 2000;343:1236-48.
    • (2000) N Engl J Med , vol.343 , pp. 1236-1248
    • Weetman, A.P.1
  • 23
    • 0033012398 scopus 로고    scopus 로고
    • Chemokine receptors as HIV-1 coreceptors: Roles in viral entry, tropism, and disease
    • Berger EA, Murphy PM, Farber JM. Chemokine receptors as HIV-1 coreceptors: roles in viral entry, tropism, and disease. Annu Rev Immunol 1999;17:657-700.
    • (1999) Annu Rev Immunol , vol.17 , pp. 657-700
    • Berger, E.A.1    Murphy, P.M.2    Farber, J.M.3
  • 24
    • 0035259780 scopus 로고    scopus 로고
    • Viral exploitation and subversion of the immune system through chemokine mimicry
    • Murphy PM. Viral exploitation and subversion of the immune system through chemokine mimicry. Nat Immunol 2001;2:116-22.
    • (2001) Nat Immunol , vol.2 , pp. 116-122
    • Murphy, P.M.1
  • 25
    • 0031032769 scopus 로고    scopus 로고
    • Human herpes-virus KSHV encodes a constitutively active G-protein-coupled receptor linked to cell proliferation
    • Arvanitakis L, Geras-Raaka E, Varma A, et al. Human herpes-virus KSHV encodes a constitutively active G-protein-coupled receptor linked to cell proliferation. Nature 1997;385:347-50.
    • (1997) Nature , vol.385 , pp. 347-350
    • Arvanitakis, L.1    Geras-Raaka, E.2    Varma, A.3
  • 26
    • 0034614888 scopus 로고    scopus 로고
    • Transgenic expression of the chemokine receptor encoded by human herpesvirus 8 induces an angioproliferative disease resembling Kaposi's sarcoma
    • Yang TY, Chen SC, Leach MW, et al. Transgenic expression of the chemokine receptor encoded by human herpesvirus 8 induces an angioproliferative disease resembling Kaposi's sarcoma. J Exp Med 2000;191:445-54.
    • (2000) J Exp Med , vol.191 , pp. 445-454
    • Yang, T.Y.1    Chen, S.C.2    Leach, M.W.3
  • 27
    • 0032526065 scopus 로고    scopus 로고
    • Right ventricular outflow tract tachycardia due to a somatic cell mutation in G protein subunitalphai2
    • Lerman BB, Dong B, Stein KM, et al. Right ventricular outflow tract tachycardia due to a somatic cell mutation in G protein subunitalphai2. J Clin Invest 1998;101:2862-8.
    • (1998) J Clin Invest , vol.101 , pp. 2862-2868
    • Lerman, B.B.1    Dong, B.2    Stein, K.M.3
  • 28
    • 0027787680 scopus 로고
    • 2+-sensing receptor gene cause familial hypocalciuric hypercalcemia and neonatal severe hyperparathyroidism
    • 2+-sensing receptor gene cause familial hypocalciuric hypercalcemia and neonatal severe hyperparathyroidism. Cell 1993;75:1297-303.
    • (1993) Cell , vol.75 , pp. 1297-1303
    • Pollak, M.R.1    Brown, E.M.2    Chou, Y.-H.W.3
  • 29
    • 0033820650 scopus 로고    scopus 로고
    • Familial hypocalciuric hypercalcemia and other disorders with resistance to extracellular calcium
    • Brown EM. Familial hypocalciuric hypercalcemia and other disorders with resistance to extracellular calcium. Endocrinol Metab Clin North Am 2000;29:503-22.
    • (2000) Endocrinol Metab Clin North Am , vol.29 , pp. 503-522
    • Brown, E.M.1
  • 30
    • 0025323257 scopus 로고
    • Mutation in the gene encoding the stimulatory G protein of adenylate cyclase in Albright's hereditary osteodystrophy
    • Patten JL, Johns DR, Valle D, et al. Mutation in the gene encoding the stimulatory G protein of adenylate cyclase in Albright's hereditary osteodystrophy. N Engl J Med 1990;322:1412-9.
    • (1990) N Engl J Med , vol.322 , pp. 1412-1419
    • Patten, J.L.1    Johns, D.R.2    Valle, D.3
  • 31
    • 0032981395 scopus 로고    scopus 로고
    • The role of genomic imprinting of G-alpha in the pathogenesis of Albright hereditary osteodystrophy
    • Weinstein LS, Yu S. The role of genomic imprinting of G-alpha in the pathogenesis of Albright hereditary osteodystrophy. Trends Endocrinol Metab 1999;10:81-5.
    • (1999) Trends Endocrinol Metab , vol.10 , pp. 81-85
    • Weinstein, L.S.1    Yu, S.2
  • 32
    • 0034793851 scopus 로고    scopus 로고
    • Endocrine manifestations of stimulatory G protein a-subunit mutations and the role of genomic imprinting
    • Weinstein LS, Yu SH, Warner DR, Liu J. Endocrine manifestations of stimulatory G protein a-subunit mutations and the role of genomic imprinting. Endocr Rev 2001;22:675-705.
    • (2001) Endocr Rev , vol.22 , pp. 675-705
    • Weinstein, L.S.1    Yu, S.H.2    Warner, D.R.3    Liu, J.4
  • 33
    • 0029091772 scopus 로고
    • Osteoblastic cells derived from isolated lesions of fibrous dysplasia contain activating somatic mutations of the Gs alpha gene
    • Shenker A, Chanson P, Weinstein LS, et al. Osteoblastic cells derived from isolated lesions of fibrous dysplasia contain activating somatic mutations of the Gs alpha gene. Hum Mol Genet 1995;4:1675-6.
    • (1995) Hum Mol Genet , vol.4 , pp. 1675-1676
    • Shenker, A.1    Chanson, P.2    Weinstein, L.S.3
  • 34
    • 0030111093 scopus 로고    scopus 로고
    • Activating mutations of Gs protein in monostotic fibrous lesions of bone
    • Alman BA, Greel DA, Wolfe HJ. Activating mutations of Gs protein in monostotic fibrous lesions of bone. J Orthop Res 1996;14:311-35.
    • (1996) J Orthop Res , vol.14 , pp. 311-335
    • Alman, B.A.1    Greel, D.A.2    Wolfe, H.J.3
  • 35
    • 0033971782 scopus 로고    scopus 로고
    • Mutations of the GNAS1 gene, stromal cell dysfunction, and osteomalacic changes in non-McCune-Albright fibrous dysplasia of bone
    • Bianco P, Riminucci M, Majolagbe A, et al. Mutations of the GNAS1 gene, stromal cell dysfunction, and osteomalacic changes in non-McCune-Albright fibrous dysplasia of bone. J Bone Miner Res 2000;15:120-8.
    • (2000) J Bone Miner Res , vol.15 , pp. 120-128
    • Bianco, P.1    Riminucci, M.2    Majolagbe, A.3
  • 36
    • 0033518280 scopus 로고    scopus 로고
    • Leydig-cell tumors caused by an activating mutation of the gene encoding the luteinizing hormone receptor
    • Liu G, Duranteau L, Carel JC, et al. Leydig-cell tumors caused by an activating mutation of the gene encoding the luteinizing hormone receptor. N Engl J Med 1999;341:1731-6.
    • (1999) N Engl J Med , vol.341 , pp. 1731-1736
    • Liu, G.1    Duranteau, L.2    Carel, J.C.3
  • 37
    • 0027372340 scopus 로고
    • A constitutively activating mutation of the luteinizing hormone receptor in familial male precocious puberty
    • Shenker A, Laue L, Kosugi S, et al. A constitutively activating mutation of the luteinizing hormone receptor in familial male precocious puberty. Nature 1993;365:652-64.
    • (1993) Nature , vol.365 , pp. 652-664
    • Shenker, A.1    Laue, L.2    Kosugi, S.3
  • 38
    • 0011488314 scopus 로고    scopus 로고
    • Retinitis pigmentosa and allied diseases
    • Albert DM, Jakobiec FA, Azar DT, Gragoudas ES, editors. Philadelphia: WB Saunders
    • Berson EL. Retinitis pigmentosa and allied diseases. In: Albert DM, Jakobiec FA, Azar DT, Gragoudas ES, editors. Principles and practice of ophthalmology. Philadelphia: WB Saunders;2000. p. 2262-90.
    • (2000) Principles and Practice of Ophthalmology , pp. 2262-2290
    • Berson, E.L.1
  • 39
    • 0025105161 scopus 로고
    • A point mutation of the rhodopsin gene in one form of retinitis pigmentosa
    • Dryja TP, McGee TL, Reichel E, et al. A point mutation of the rhodopsin gene in one form of retinitis pigmentosa. Nature 1990;343:364-6.
    • (1990) Nature , vol.343 , pp. 364-366
    • Dryja, T.P.1    McGee, T.L.2    Reichel, E.3
  • 40
    • 0026463972 scopus 로고
    • Transgenic mice with a rhodopsin mutation (Pro23His): A mouse model of autosomal dominant retinitis pigmentosa
    • Olsson JE, Gordon JW, Pawlyk BS, et al. Transgenic mice with a rhodopsin mutation (Pro23His): a mouse model of autosomal dominant retinitis pigmentosa. Neuron 1992;9:815-30.
    • (1992) Neuron , vol.9 , pp. 815-830
    • Olsson, J.E.1    Gordon, J.W.2    Pawlyk, B.S.3
  • 41
    • 0027251934 scopus 로고
    • Simulation of human autosomal dominant retinitis pigmentosa in transgenic mice expressing a mutated murine opsin gene
    • Naash MI, Hollyfield JG, al-Ubaidi MR, Baehr W. Simulation of human autosomal dominant retinitis pigmentosa in transgenic mice expressing a mutated murine opsin gene. Proc Natl Acad Sci U S A 1993;90:5499-503.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 5499-5503
    • Naash, M.I.1    Hollyfield, J.G.2    Al-Ubaidi, M.R.3    Baehr, W.4
  • 42
    • 0037072934 scopus 로고    scopus 로고
    • A rhodopsin mutant linked to autosomal dominant retinitis pigmentosa is prone to aggregate and interacts with the ubiquitin proteasome system
    • Illing ME, Rajan RS, Bence NF, Kopito RR. A rhodopsin mutant linked to autosomal dominant retinitis pigmentosa is prone to aggregate and interacts with the ubiquitin proteasome system. J Biol Chem 2002;277:34150-60.
    • (2002) J Biol Chem , vol.277 , pp. 34150-34160
    • Illing, M.E.1    Rajan, R.S.2    Bence, N.F.3    Kopito, R.R.4
  • 43
    • 0037099080 scopus 로고    scopus 로고
    • The cellular fate of mutant rhodopsin: Quality control, degradation and aggresome formation
    • Saliba RS, Munro PM, Luthert PJ, Cheetham ME. The cellular fate of mutant rhodopsin: quality control, degradation and aggresome formation. J Cell Sci 2002;115:2907-18.
    • (2002) J Cell Sci , vol.115 , pp. 2907-2918
    • Saliba, R.S.1    Munro, P.M.2    Luthert, P.J.3    Cheetham, M.E.4
  • 44
    • 0037154184 scopus 로고    scopus 로고
    • Recent advances in the genetics and pathogenesis of Parkinson disease
    • Mouradian MM. Recent advances in the genetics and pathogenesis of Parkinson disease. Neurology 2002;58:179-85.
    • (2002) Neurology , vol.58 , pp. 179-185
    • Mouradian, M.M.1
  • 45
    • 0025944670 scopus 로고
    • Autosomal dominant retinitis pigmentosa: Four new mutations in rhodopsin, one of them in the retinal attachment site
    • Keen TJ, Inglehearn CF, Lester DH, et al. Autosomal dominant retinitis pigmentosa: four new mutations in rhodopsin, one of them in the retinal attachment site. Genomics 1991;11:199-205.
    • (1991) Genomics , vol.11 , pp. 199-205
    • Keen, T.J.1    Inglehearn, C.F.2    Lester, D.H.3
  • 47
    • 0028947938 scopus 로고
    • Constitutive activation of phototransduction by K296E opsin is not a cause of photoreceptor degeneration
    • Li T, Franson WK, Gordon JW, et al. Constitutive activation of phototransduction by K296E opsin is not a cause of photoreceptor degeneration. Proc Natl Acad Sci U S A 1995;92:3551-5.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 3551-3555
    • Li, T.1    Franson, W.K.2    Gordon, J.W.3
  • 48
    • 0027935666 scopus 로고
    • A rhodopsin gene mutation responsible for autosomal dominant retinitis pigmentosa results in a protein that is defective in localization to the photoreceptor outer segment
    • Sung CH, Makino C, Baylor D, Nathans J. A rhodopsin gene mutation responsible for autosomal dominant retinitis pigmentosa results in a protein that is defective in localization to the photoreceptor outer segment. J Neurosci 1994;14:5818-33.
    • (1994) J Neurosci , vol.14 , pp. 5818-5833
    • Sung, C.H.1    Makino, C.2    Baylor, D.3    Nathans, J.4
  • 49
    • 0030475229 scopus 로고    scopus 로고
    • Transgenic mice carrying the dominant rhodopsin mutation P347S: Evidence for defective vectorial transport of rhodopsin to the outer segments
    • Li T, Snyder WK, Olsson JE, Dryja TP. Transgenic mice carrying the dominant rhodopsin mutation P347S: evidence for defective vectorial transport of rhodopsin to the outer segments. Proc Natl Acad Sci U S A 1996;93:14176-81.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 14176-14181
    • Li, T.1    Snyder, W.K.2    Olsson, J.E.3    Dryja, T.P.4
  • 51
    • 0036725693 scopus 로고    scopus 로고
    • Disease progression in patients with dominant retinitis pigmentosa and rhodopsin mutations
    • Berson EL, Rosner B, Weigel-DiFranco C, et al. Disease progression in patients with dominant retinitis pigmentosa and rhodopsin mutations. Invest Ophthalmol Vis Sci 2002;43:3027-36.
    • (2002) Invest Ophthalmol Vis Sci , vol.43 , pp. 3027-3036
    • Berson, E.L.1    Rosner, B.2    Weigel-DiFranco, C.3
  • 52
    • 0026878962 scopus 로고
    • A null mutation in the rhodopsin gene causes rod photoreceptor dysfunction and autosomal recessive retinitis pigmentosa
    • Rosenfeld PJ, Cowley GS, McGee TL, et al. A null mutation in the rhodopsin gene causes rod photoreceptor dysfunction and autosomal recessive retinitis pigmentosa. Nat Genet 1992;1:209-13.
    • (1992) Nat Genet , vol.1 , pp. 209-213
    • Rosenfeld, P.J.1    Cowley, G.S.2    McGee, T.L.3
  • 53
    • 0028789921 scopus 로고
    • Autosomal recessive retinitis pigmentosa caused by mutations in the alpha subunit of rod cGMP phosphodiesterase
    • Huang SH, Pittler SJ, Huang X, et al. Autosomal recessive retinitis pigmentosa caused by mutations in the alpha subunit of rod cGMP phosphodiesterase. Nat Genet 1995;11:468-71.
    • (1995) Nat Genet , vol.11 , pp. 468-471
    • Huang, S.H.1    Pittler, S.J.2    Huang, X.3
  • 54
    • 0027270053 scopus 로고
    • Recessive mutations in the gene encoding the beta-subunit of rod phosphodiesterase in patients with retinitis pigmentosa
    • McLaughlin ME, Sandberg MA, Berson EL, Dryja TP. Recessive mutations in the gene encoding the beta-subunit of rod phosphodiesterase in patients with retinitis pigmentosa. Nat Genet 1993;4:130-4.
    • (1993) Nat Genet , vol.4 , pp. 130-134
    • McLaughlin, M.E.1    Sandberg, M.A.2    Berson, E.L.3    Dryja, T.P.4
  • 55
    • 0026755953 scopus 로고
    • Human tritanopia associated with a third amino acid substitution in the blue-sensitive visual pigment
    • Weitz CJ, Went LN, Nathans J. Human tritanopia associated with a third amino acid substitution in the blue-sensitive visual pigment. Am J Hum Genet 1992;51:444-6.
    • (1992) Am J Hum Genet , vol.51 , pp. 444-446
    • Weitz, C.J.1    Went, L.N.2    Nathans, J.3
  • 56
    • 0035022297 scopus 로고    scopus 로고
    • Segregation of a mutation in CNGB1 encoding the beta-subunit of the rod cGMP-gated channel in a family with autosomal recessive retinitis pigmentosa
    • Bareil C, Hamel CP, Delague V, et al. Segregation of a mutation in CNGB1 encoding the beta-subunit of the rod cGMP-gated channel in a family with autosomal recessive retinitis pigmentosa. Hum Genet 2001;108:328-34.
    • (2001) Hum Genet , vol.108 , pp. 328-334
    • Bareil, C.1    Hamel, C.P.2    Delague, V.3
  • 58
    • 0027248024 scopus 로고
    • Heterozygous missense mutation in the rhodopsin gene as a cause of congenital stationary night blindness
    • Dryja TP, Berson EL, Rao VR, Oprian DD. Heterozygous missense mutation in the rhodopsin gene as a cause of congenital stationary night blindness. Nat Genet 1993;4:280-3.
    • (1993) Nat Genet , vol.4 , pp. 280-283
    • Dryja, T.P.1    Berson, E.L.2    Rao, V.R.3    Oprian, D.D.4
  • 59
    • 0028798659 scopus 로고
    • Dark-light: Model for night blindness from the human rhodopsin Gly-90→Asp mutation
    • Sieving PA, Richards JE, Naarendorp F, et al. Dark-light: model for night blindness from the human rhodopsin Gly-90→Asp mutation. Proc Natl Acad Sci U S A 1995;92:880-4.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 880-884
    • Sieving, P.A.1    Richards, J.E.2    Naarendorp, F.3
  • 60
    • 0028125886 scopus 로고
    • Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness
    • Rao VR, Cohen GB, Oprian DD. Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness. Nature 1994;367:639-42.
    • (1994) Nature , vol.367 , pp. 639-642
    • Rao, V.R.1    Cohen, G.B.2    Oprian, D.D.3
  • 61
    • 0035425947 scopus 로고    scopus 로고
    • Constitutive "light" adaptation in rods from G90D rhodopsin: A mechanism for human congenital nightblindness without rod cell loss
    • Sieving PA, Fowler ML, Bush RA, et al. Constitutive "light" adaptation in rods from G90D rhodopsin: a mechanism for human congenital nightblindness without rod cell loss. J Neurosci 2001;21:5449-60.
    • (2001) J Neurosci , vol.21 , pp. 5449-5460
    • Sieving, P.A.1    Fowler, M.L.2    Bush, R.A.3
  • 62
    • 0029902034 scopus 로고    scopus 로고
    • Missense mutation in the gene encoding the alpha subunit of rod transducin in the Nougaret form of congenital stationary night blindness
    • Dryja TP, Hahn LB, Reboul T, Arnaud B. Missense mutation in the gene encoding the alpha subunit of rod transducin in the Nougaret form of congenital stationary night blindness. Nat Genet 1996;13:358-60.
    • (1996) Nat Genet , vol.13 , pp. 358-360
    • Dryja, T.P.1    Hahn, L.B.2    Reboul, T.3    Arnaud, B.4
  • 63
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne HR, Sanders DA, McCormick F. The GTPase superfamily: conserved structure and molecular mechanism. Nature 1991;349:117-27.
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 64
    • 0025193871 scopus 로고
    • Three-dimensional structures of H-ras p21 mutants: Molecular basis for their inability to function as signal switch molecules
    • Krengel U, Schlichting L, Scherer A, et al. Three-dimensional structures of H-ras p21 mutants: molecular basis for their inability to function as signal switch molecules. Cell 1990;62:539-48.
    • (1990) Cell , vol.62 , pp. 539-548
    • Krengel, U.1    Schlichting, L.2    Scherer, A.3
  • 65
    • 0031789648 scopus 로고    scopus 로고
    • Rod and cone function in the Nougaret form of stationary night blindness
    • Sandberg MA, Pawlyk BS, Dan J, et al. Rod and cone function in the Nougaret form of stationary night blindness. Arch Ophthalmol 1998;116:867-72.
    • (1998) Arch Ophthalmol , vol.116 , pp. 867-872
    • Sandberg, M.A.1    Pawlyk, B.S.2    Dan, J.3
  • 66
    • 0034629343 scopus 로고    scopus 로고
    • Loss of the effector function in a transducin-alpha mutant associated with Nougaret night blindness
    • Muradov KG, Artemyev NO. Loss of the effector function in a transducin-alpha mutant associated with Nougaret night blindness. J Biol Chem 2000;275:6969-74.
    • (2000) J Biol Chem , vol.275 , pp. 6969-6974
    • Muradov, K.G.1    Artemyev, N.O.2
  • 67
    • 0028128535 scopus 로고
    • Heterozygous missense mutation in the rod cGMP phosphodiesterase beta-subunit gene in autosomal dominant stationary night blindness
    • Gal A, Orth U, Baehr W, et al. Heterozygous missense mutation in the rod cGMP phosphodiesterase beta-subunit gene in autosomal dominant stationary night blindness. Nat Genet 1994;7:64-8.
    • (1994) Nat Genet , vol.7 , pp. 64-68
    • Gal, A.1    Orth, U.2    Baehr, W.3
  • 68
    • 0027369421 scopus 로고
    • Somatic mutations in the thyrotropin receptor gene cause hyperfunctioning thyroid adenomas
    • Parma J, Duprez L, Van Sande J, et al. Somatic mutations in the thyrotropin receptor gene cause hyperfunctioning thyroid adenomas. Nature 1993;365:649-51.
    • (1993) Nature , vol.365 , pp. 649-651
    • Parma, J.1    Duprez, L.2    Van Sande, J.3
  • 69
    • 0028240982 scopus 로고
    • Germline mutations in the thyrotropin receptor gene cause non-autoimmune autosomal dominant hyperthyroidism
    • Duprez L, Parma J, Van Sande J, et al. Germline mutations in the thyrotropin receptor gene cause non-autoimmune autosomal dominant hyperthyroidism. Nat Genet 1994;7:396-401.
    • (1994) Nat Genet , vol.7 , pp. 396-401
    • Duprez, L.1    Parma, J.2    Van Sande, J.3
  • 71
    • 0030734932 scopus 로고    scopus 로고
    • Identification of a new thyrotropin receptor germline mutation (Leu629Phe) in a family with neonatal onset of autosomal dominant nonautoimmune hyperthyroidism
    • Fuhrer D, Wonerow P, Willgerodt H, Paschke R. Identification of a new thyrotropin receptor germline mutation (Leu629Phe) in a family with neonatal onset of autosomal dominant nonautoimmune hyperthyroidism. J Clin Endocrinol Metab 1997;82:4234-8.
    • (1997) J Clin Endocrinol Metab , vol.82 , pp. 4234-4238
    • Fuhrer, D.1    Wonerow, P.2    Willgerodt, H.3    Paschke, R.4
  • 72
    • 0031406420 scopus 로고    scopus 로고
    • Congenital nonautoimmune hyperthyroidism in a nonidentical twin caused by a sporadic germline mutation in the thyrotropin receptor gene
    • Kopp P, Jameson JL, Roe TF. Congenital nonautoimmune hyperthyroidism in a nonidentical twin caused by a sporadic germline mutation in the thyrotropin receptor gene. Thyroid 1997;7:765-70.
    • (1997) Thyroid , vol.7 , pp. 765-770
    • Kopp, P.1    Jameson, J.L.2    Roe, T.F.3
  • 73
    • 0033312613 scopus 로고    scopus 로고
    • A germline mutation of the thyrotropin receptor gene associated with thyrotoxicosis and mitral valve prolapse in a Chinese family
    • Khoo DH, Parma J, Rajasoorya C, et al. A germline mutation of the thyrotropin receptor gene associated with thyrotoxicosis and mitral valve prolapse in a Chinese family. J Clin Endocrinol Metab 1999;84:1459-62.
    • (1999) J Clin Endocrinol Metab , vol.84 , pp. 1459-1462
    • Khoo, D.H.1    Parma, J.2    Rajasoorya, C.3
  • 74
    • 9044240477 scopus 로고    scopus 로고
    • Functional characteristics of three new germline mutations of the thyrotropin receptor gene causing autosomal dominant toxic thyroid hyperplasia
    • Tonacchera M, Van Sande J, Cetani F, et al. Functional characteristics of three new germline mutations of the thyrotropin receptor gene causing autosomal dominant toxic thyroid hyperplasia. J Clin Endocrinol Metab 1996;81:547-54.
    • (1996) J Clin Endocrinol Metab , vol.81 , pp. 547-554
    • Tonacchera, M.1    Van Sande, J.2    Cetani, F.3
  • 75
    • 0034853605 scopus 로고    scopus 로고
    • The first activating TSH receptor mutation in transmembrane domain 1 identified in a family with nonautoimmune hyperthyroidism
    • Biebermann H, Schoneberg T, Hess C, et al. The first activating TSH receptor mutation in transmembrane domain 1 identified in a family with nonautoimmune hyperthyroidism. J Clin Endocrinol Metab 2001;86:4429-33.
    • (2001) J Clin Endocrinol Metab , vol.86 , pp. 4429-4433
    • Biebermann, H.1    Schoneberg, T.2    Hess, C.3
  • 76
    • 0036002619 scopus 로고    scopus 로고
    • An activating mutation of the thyrotropin receptor gene in hereditary non-autoimmune hyperthyroidism
    • Lee YS, Poh L, Loke KY. An activating mutation of the thyrotropin receptor gene in hereditary non-autoimmune hyperthyroidism. J Pediatr Endocrinol Metab 2002;15:211-25.
    • (2002) J Pediatr Endocrinol Metab , vol.15 , pp. 211-225
    • Lee, Y.S.1    Poh, L.2    Loke, K.Y.3
  • 77
    • 0034852079 scopus 로고    scopus 로고
    • A novel germline mutation in the TSH receptor gene causes nonautoimmune autosomal dominant hyperthyroidism
    • Alberti L, Proverbio MC, Costagliola S, et al. A novel germline mutation in the TSH receptor gene causes nonautoimmune autosomal dominant hyperthyroidism. Eur J Endocrinol 2001;145:249-54.
    • (2001) Eur J Endocrinol , vol.145 , pp. 249-254
    • Alberti, L.1    Proverbio, M.C.2    Costagliola, S.3
  • 78
    • 0031470487 scopus 로고    scopus 로고
    • Constitutively active germline mutation of the thyrotropin receptor gene as a cause of congenital hyperthyroidism
    • Schwab KO, Gerlich M, Broecker M, et al. Constitutively active germline mutation of the thyrotropin receptor gene as a cause of congenital hyperthyroidism. J Pediatr 1997;131:899-904.
    • (1997) J Pediatr , vol.131 , pp. 899-904
    • Schwab, K.O.1    Gerlich, M.2    Broecker, M.3
  • 79
    • 0031772403 scopus 로고    scopus 로고
    • Severe congenital hyperthyroidism caused by a germ-line neo mutation in the extracellular portion of the thyrotropin receptor
    • Gruters A, Schoneberg T, Biebermann H, et al. Severe congenital hyperthyroidism caused by a germ-line neo mutation in the extracellular portion of the thyrotropin receptor. J Clin Endocrinol Metab 1998;83:1431-6.
    • (1998) J Clin Endocrinol Metab , vol.83 , pp. 1431-1436
    • Gruters, A.1    Schoneberg, T.2    Biebermann, H.3
  • 80
    • 0033773141 scopus 로고    scopus 로고
    • Sporadic nonautoimmune congenital hyperthyroidism due to a strong activating mutation of the thyrotropin receptor gene
    • Tonacchera M, Agretti P, Rosellini V, et al. Sporadic nonautoimmune congenital hyperthyroidism due to a strong activating mutation of the thyrotropin receptor gene. Thyroid 2000;10:859-63.
    • (2000) Thyroid , vol.10 , pp. 859-863
    • Tonacchera, M.1    Agretti, P.2    Rosellini, V.3
  • 81
    • 0032751937 scopus 로고    scopus 로고
    • A novel thyrotropin receptor mutation in an infant with severe thyrotoxicosis
    • Esapa CT, Duprez L, Ludgate M, et al. A novel thyrotropin receptor mutation in an infant with severe thyrotoxicosis. Thyroid 1999;9:1005-10.
    • (1999) Thyroid , vol.9 , pp. 1005-1010
    • Esapa, C.T.1    Duprez, L.2    Ludgate, M.3
  • 82
    • 0028829472 scopus 로고
    • Clinical review 75: Recent advances in pathogenesis, diagnosis, and management of acromegaly
    • Melmed S, Ho K, Klibanski A, et al. Clinical review 75: recent advances in pathogenesis, diagnosis, and management of acromegaly. J Clin Endocrinol Metab 1995;80:3395-402.
    • (1995) J Clin Endocrinol Metab , vol.80 , pp. 3395-3402
    • Melmed, S.1    Ho, K.2    Klibanski, A.3
  • 83
    • 0031948965 scopus 로고    scopus 로고
    • New options for diagnosing and treating acromegaly
    • Barkan AL. New options for diagnosing and treating acromegaly. Cleve Clin J Med 1998;65:343, 347-9.
    • (1998) Cleve Clin J Med , vol.65 , pp. 343
    • Barkan, A.L.1
  • 85
    • 0023522307 scopus 로고
    • Altered Gs and adenylate cyclase activity in human GH-secreting pituitary adenomas
    • Vallar L, Spada A, Giannattasio G. Altered Gs and adenylate cyclase activity in human GH-secreting pituitary adenomas. Nature 1987;330:566-8.
    • (1987) Nature , vol.330 , pp. 566-568
    • Vallar, L.1    Spada, A.2    Giannattasio, G.3
  • 86
    • 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, et al. GTPase inhibiting mutations activate the alpha chain of Gs and stimulate adenylyl cyclase in human pituitary tumours. Nature 1989;340:692-6.
    • (1989) Nature , vol.340 , pp. 692-696
    • Landis, C.A.1    Masters, S.B.2    Spada, A.3
  • 87
    • 0029882954 scopus 로고    scopus 로고
    • Characteristics of gsp-positive growth hormone-secreting pituitary tumors in Korean acromegalic patients
    • Yang I, Park S, Ryu M, et al. Characteristics of gsp-positive growth hormone-secreting pituitary tumors in Korean acromegalic patients. Eur J Endocrinol 1996;134:720-76.
    • (1996) Eur J Endocrinol , vol.134 , pp. 720-776
    • Yang, I.1    Park, S.2    Ryu, M.3
  • 88
    • 0027325891 scopus 로고
    • Rare mutations of the Gs alpha subunit gene in human endocrine tumors. Mutation detection by polymerase chain reaction-primer-introduced restriction analysis
    • Yoshimoto K, Iwahana H, Fukuda A, et al. Rare mutations of the Gs alpha subunit gene in human endocrine tumors. Mutation detection by polymerase chain reaction-primer-introduced restriction analysis. Cancer 1993;72:1386-193.
    • (1993) Cancer , vol.72 , pp. 1386-2193
    • Yoshimoto, K.1    Iwahana, H.2    Fukuda, A.3
  • 89
    • 0032173907 scopus 로고    scopus 로고
    • Detection of gsp oncogene in growth hormone-secreting pituitary adenomas and the study of clinical characteristics of acromegalic patients with gsp-positive pituitary tumors
    • Shi Y, Tang D, Deng J, Su C. Detection of gsp oncogene in growth hormone-secreting pituitary adenomas and the study of clinical characteristics of acromegalic patients with gsp-positive pituitary tumors. Chin Med J (Engl) 1998;111:891-4.
    • (1998) Chin Med J (Engl) , vol.111 , pp. 891-894
    • Shi, Y.1    Tang, D.2    Deng, J.3    Su, C.4
  • 90
    • 17744393215 scopus 로고    scopus 로고
    • Prevalence of Gs alpha mutations in Korean patients with pituitary adenomas
    • Kim HJ, Kim MS, Park YJ, et al. Prevalence of Gs alpha mutations in Korean patients with pituitary adenomas. J Endocrinol 2001;168:221-6.
    • (2001) J Endocrinol , vol.168 , pp. 221-226
    • Kim, H.J.1    Kim, M.S.2    Park, Y.J.3
  • 91
    • 0027519698 scopus 로고
    • Analysis of the Gs alpha gene in growth hormone-secreting pituitary adenomas by the polymerase chain reaction-direct sequencing method using paraffin-embedded tissues
    • Hosoi E, Yokogoshi Y, Hosoi E, et al. Analysis of the Gs alpha gene in growth hormone-secreting pituitary adenomas by the polymerase chain reaction-direct sequencing method using paraffin-embedded tissues. Acta Endocrinol (Copenh) 1993;129:301-36.
    • (1993) Acta Endocrinol (Copenh) , vol.129 , pp. 301-336
    • Hosoi, E.1    Yokogoshi, Y.2    Hosoi, E.3
  • 93
    • 0025127424 scopus 로고
    • Two G protein oncogenes in human endocrine tumors
    • Lyons J, Landis CA, Harsh G, et al. Two G protein oncogenes in human endocrine tumors. Science 1990;249:655-69.
    • (1990) Science , vol.249 , pp. 655-669
    • Lyons, J.1    Landis, C.A.2    Harsh, G.3
  • 94
    • 0032995963 scopus 로고    scopus 로고
    • Gps mutations in Chilean patients harboring growth hormone-secreting pituitary tumors
    • Johnson MC, Codner E, Eggers M, et al. Gps mutations in Chilean patients harboring growth hormone-secreting pituitary tumors. J Pediatr Endocrinol Metab 1999;12:381-7.
    • (1999) J Pediatr Endocrinol Metab , vol.12 , pp. 381-387
    • Johnson, M.C.1    Codner, E.2    Eggers, M.3
  • 97
    • 0028027596 scopus 로고
    • GTPase mechanism of G proteins from the 1.7-A crystal structure of transducin alpha-GDP-AIF-4
    • Sondek J, Lambright DG, Noel JP, et al. GTPase mechanism of G proteins from the 1.7-A crystal structure of transducin alpha-GDP-AIF-4. Nature 1994;372:276-9.
    • (1994) Nature , vol.372 , pp. 276-279
    • Sondek, J.1    Lambright, D.G.2    Noel, J.P.3
  • 98
    • 0024839696 scopus 로고
    • Hydrolysis of GTP by the alpha-chain of Gs and other GTP binding proteins
    • Bourne HR, Landis CA, Masters SB. Hydrolysis of GTP by the alpha-chain of Gs and other GTP binding proteins. Proteins 1989;6:222-30.
    • (1989) Proteins , vol.6 , pp. 222-230
    • Bourne, H.R.1    Landis, C.A.2    Masters, S.B.3
  • 99
    • 0024854388 scopus 로고
    • Mutations of GS alpha designed to alter the reactivity of the protein with bacterial toxins. Substitutions at ARG187 result in loss of GTPase activity
    • Freissmuth M, Gilman AG. Mutations of GS alpha designed to alter the reactivity of the protein with bacterial toxins. Substitutions at ARG187 result in loss of GTPase activity. J Biol Chem 1989;264:21907-14.
    • (1989) J Biol Chem , vol.264 , pp. 21907-21914
    • Freissmuth, M.1    Gilman, A.G.2
  • 100
    • 0022446058 scopus 로고
    • Dominant inheritance of the complex of myxomas, spotty pigmentation, and endocrine overactivity
    • Carney JA, Hruska LS, Beauchamp GD, Gordon H. Dominant inheritance of the complex of myxomas, spotty pigmentation, and endocrine overactivity. Mayo Clin Proc 1986;61:165-72.
    • (1986) Mayo Clin Proc , vol.61 , pp. 165-172
    • Carney, J.A.1    Hruska, L.S.2    Beauchamp, G.D.3    Gordon, H.4
  • 101
    • 0022397926 scopus 로고
    • The complex of myxomas, spotty pigmentation, and endocrine overactivity
    • Carney JA, Gordon H, Carpenter PC, et al. The complex of myxomas, spotty pigmentation, and endocrine overactivity. Medicine (Baltimore) 1985;64:270-83.
    • (1985) Medicine (Baltimore) , vol.64 , pp. 270-283
    • Carney, J.A.1    Gordon, H.2    Carpenter, P.C.3
  • 102
    • 0035001830 scopus 로고    scopus 로고
    • Clinical genetics of multiple endocrine neoplasias, Carney complex and related syndromes
    • Stratakis CA. Clinical genetics of multiple endocrine neoplasias, Carney complex and related syndromes. J Endocrinol Invest 2001;24:370-83.
    • (2001) J Endocrinol Invest , vol.24 , pp. 370-383
    • Stratakis, C.A.1
  • 103
    • 0034853288 scopus 로고    scopus 로고
    • Clinical and molecular features of the Carney complex: Diagnostic criteria and recommendations for patient evaluation
    • Stratakis CA, Kirschner LS, Carney JA. Clinical and molecular features of the Carney complex: diagnostic criteria and recommendations for patient evaluation. J Clin Endocrinol Metab 2001;86:4041-6.
    • (2001) J Clin Endocrinol Metab , vol.86 , pp. 4041-4046
    • Stratakis, C.A.1    Kirschner, L.S.2    Carney, J.A.3
  • 104
    • 0021929851 scopus 로고
    • Differences between nonfamilial and familial cardiac myxoma
    • Carney JA. Differences between nonfamilial and familial cardiac myxoma. Am J Surg Pathol 1985;9:53-5.
    • (1985) Am J Surg Pathol , vol.9 , pp. 53-55
    • Carney, J.A.1
  • 105
    • 0030049026 scopus 로고    scopus 로고
    • Carney complex, a familial multiple neoplasia and lentiginosis syndrome. Analysis of 11 kindreds and linkage to the short arm of chromosome 2
    • Stratakis CA, Carney JA, Lin JP, et al. Carney complex, a familial multiple neoplasia and lentiginosis syndrome. Analysis of 11 kindreds and linkage to the short arm of chromosome 2. J Clin Invest 1996;97:699-705.
    • (1996) J Clin Invest , vol.97 , pp. 699-705
    • Stratakis, C.A.1    Carney, J.A.2    Lin, J.P.3
  • 106
    • 0032497947 scopus 로고    scopus 로고
    • Identification of a novel genetic locus for familial cardiac myxomas and Carney complex
    • Casey M, Mah C, Merliss AD, et al. Identification of a novel genetic locus for familial cardiac myxomas and Carney complex. Circulation 1998;98:2560-6.
    • (1998) Circulation , vol.98 , pp. 2560-2566
    • Casey, M.1    Mah, C.2    Merliss, A.D.3
  • 107
    • 0033812849 scopus 로고    scopus 로고
    • Mutations of the gene encoding the protein kinase A type I-alpha regulatory subunit in patients with the Carney complex
    • Kirschner LS, Carney JA, Pack SD, et al. Mutations of the gene encoding the protein kinase A type I-alpha regulatory subunit in patients with the Carney complex. Nat Genet 2000;26:89-92.
    • (2000) Nat Genet , vol.26 , pp. 89-92
    • Kirschner, L.S.1    Carney, J.A.2    Pack, S.D.3
  • 108
    • 0034642302 scopus 로고    scopus 로고
    • Genetic heterogeneity and spectrum of mutations of the PRKAR1A gene in patients with the Carney complex
    • Kirschner LS, Sandrini F, Monbo J, et al. Genetic heterogeneity and spectrum of mutations of the PRKAR1A gene in patients with the Carney complex. Hum Mol Genet 2000;9:3037-46.
    • (2000) Hum Mol Genet , vol.9 , pp. 3037-3046
    • Kirschner, L.S.1    Sandrini, F.2    Monbo, J.3
  • 109
    • 18544406892 scopus 로고    scopus 로고
    • Mutations in the protein kinase A R1alpha regulatory subunit cause familial cardiac myxomas and Carney complex
    • Casey M, Vaughan CJ, He J, et al. Mutations in the protein kinase A R1alpha regulatory subunit cause familial cardiac myxomas and Carney complex. J Clin Invest 2000;106:R31-8.
    • (2000) J Clin Invest , vol.106
    • Casey, M.1    Vaughan, C.J.2    He, J.3
  • 112
    • 0030930754 scopus 로고    scopus 로고
    • Type II regulatory subunits are not required for the anchoring-dependent modulation of Ca2+ channel activity by cAMP-dependent protein kinase
    • Burton KA, Johnson BD, Hausken ZE, et al. Type II regulatory subunits are not required for the anchoring-dependent modulation of Ca2+ channel activity by cAMP-dependent protein kinase. Proc Natl Acad Sci U S A 1997;94:11067-72.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 11067-11072
    • Burton, K.A.1    Johnson, B.D.2    Hausken, Z.E.3
  • 113
    • 0030614908 scopus 로고    scopus 로고
    • Compensatory regulation of RIalpha protein levels in protein kinase A mutant mice
    • Amieux PS, Cummings DE, Motamed K, et al. Compensatory regulation of RIalpha protein levels in protein kinase A mutant mice. J Biol Chem 1997;272:3993-8.
    • (1997) J Biol Chem , vol.272 , pp. 3993-3998
    • Amieux, P.S.1    Cummings, D.E.2    Motamed, K.3
  • 114
    • 0037133693 scopus 로고    scopus 로고
    • G protein-coupled receptor kinase 4 gene variants in human essential hypertension
    • Felder RA, Sanada H, Xu J, et al. G protein-coupled receptor kinase 4 gene variants in human essential hypertension. Proc Natl Acad Sci U S A 2002;99:3872-7.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 3872-3877
    • Felder, R.A.1    Sanada, H.2    Xu, J.3
  • 115
    • 0029067542 scopus 로고
    • A homozygous 1-base pair deletion in the arrestin gene is a frequent cause of Oguchi disease in Japanese
    • Fuchs S, Nakazawa M, Maw M, et al. A homozygous 1-base pair deletion in the arrestin gene is a frequent cause of Oguchi disease in Japanese. Nat Genet 1995;10:360-2.
    • (1995) Nat Genet , vol.10 , pp. 360-362
    • Fuchs, S.1    Nakazawa, M.2    Maw, M.3
  • 116
    • 0031038950 scopus 로고    scopus 로고
    • Defects in the rhodopsin kinase gene in the Oguchi form of stationary night blindness
    • Yamamoto S, Sippel KC, Berson EL, Dryja TP. Defects in the rhodopsin kinase gene in the Oguchi form of stationary night blindness. Nat Genet 1997;15:175-8.
    • (1997) Nat Genet , vol.15 , pp. 175-178
    • Yamamoto, S.1    Sippel, K.C.2    Berson, E.L.3    Dryja, T.P.4
  • 117
    • 0031006407 scopus 로고    scopus 로고
    • Six novel mutations in the vasopressin V2 receptor gene causing nephrogenic diabetes insipidus
    • Cheong HI, Park HW, Ha IS, et al. Six novel mutations in the vasopressin V2 receptor gene causing nephrogenic diabetes insipidus. Nephron 1997;75:431-47.
    • (1997) Nephron , vol.75 , pp. 431-447
    • Cheong, H.I.1    Park, H.W.2    Ha, I.S.3
  • 118
    • 0032862476 scopus 로고    scopus 로고
    • Successful pregnancy outcome in a woman with a gain-of-function mutation of the calcium-sensing receptor. A case report
    • Gherman RB, Bowen E, Eggleston MK, et al. Successful pregnancy outcome in a woman with a gain-of-function mutation of the calcium-sensing receptor. A case report. J Reprod Med 1999;44:745-77.
    • (1999) J Reprod Med , vol.44 , pp. 745-777
    • Gherman, R.B.1    Bowen, E.2    Eggleston, M.K.3
  • 119
    • 0031565726 scopus 로고    scopus 로고
    • An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors
    • Baldwin JM, Schertler GF, Unger VM. An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors. J Mol Biol 1997;272:144-64.
    • (1997) J Mol Biol , vol.272 , pp. 144-164
    • Baldwin, J.M.1    Schertler, G.F.2    Unger, V.M.3
  • 120
    • 0034604451 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: A G protein-coupled receptor
    • Palczewski K, Kumasaka T, Hori T, et al. Crystal structure of rhodopsin: a G protein-coupled receptor. Science 2000;289:739-45.
    • (2000) Science , vol.289 , pp. 739-745
    • Palczewski, K.1    Kumasaka, T.2    Hori, T.3
  • 121
    • 0033843626 scopus 로고    scopus 로고
    • Towards 3D structures of G protein-coupled receptors: A multidisciplinary approach
    • Muller G. Towards 3D structures of G protein-coupled receptors: a multidisciplinary approach. Curr Med Chem 2000;7:861-88.
    • (2000) Curr Med Chem , vol.7 , pp. 861-888
    • Muller, G.1
  • 122
    • 0001169515 scopus 로고
    • Antagonists with negative intrinsic activity at delta opioid receptors coupled to GTP-binding proteins
    • Costa T, Herz A. Antagonists with negative intrinsic activity at delta opioid receptors coupled to GTP-binding proteins. Proc Natl Acad Sci U S A 1989;86:7321-5.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 7321-7325
    • Costa, T.1    Herz, A.2
  • 123
    • 0034741106 scopus 로고    scopus 로고
    • 5-Hydroxytryptamine2A receptor inverse agonists as antipsychotics
    • Weiner DM, Burstein ES, Nash N, et al. 5-hydroxytryptamine2A receptor inverse agonists as antipsychotics. J Pharmacol Exp Ther 2001;299:268-76.
    • (2001) J Pharmacol Exp Ther , vol.299 , pp. 268-276
    • Weiner, D.M.1    Burstein, E.S.2    Nash, N.3
  • 124
    • 0033976851 scopus 로고    scopus 로고
    • Use of constitutive G protein-coupled receptor activity for drug discovery
    • Chen G, Way J, Armour S, et al. Use of constitutive G protein-coupled receptor activity for drug discovery. Mol Pharmacol 2000;57:125-34.
    • (2000) Mol Pharmacol , vol.57 , pp. 125-134
    • Chen, G.1    Way, J.2    Armour, S.3
  • 125
    • 0031543433 scopus 로고    scopus 로고
    • G-protein-coupled receptors in Saccharomyces cerevisiae: High-throughput screening assays for drug discovery
    • Pausch MH. G-protein-coupled receptors in Saccharomyces cerevisiae: high-throughput screening assays for drug discovery. Trends Biotechnol 1997;15:487-94.
    • (1997) Trends Biotechnol , vol.15 , pp. 487-494
    • Pausch, M.H.1
  • 126
    • 85084247357 scopus 로고    scopus 로고
    • High-throughput screening for drug discovery
    • Broach JR, Thorner J. High-throughput screening for drug discovery. Nature 1996;384:14-6.
    • (1996) Nature , vol.384 , pp. 14-16
    • Broach, J.R.1    Thorner, J.2
  • 127
    • 0038540424 scopus 로고    scopus 로고
    • Validation of genomics-derived drug targets using yeast
    • Klein I. Validation of genomics-derived drug targets using yeast. Drug Discov Today 2000;5:37-8.
    • (2000) Drug Discov Today , vol.5 , pp. 37-38
    • Klein, I.1
  • 128
    • 0035271616 scopus 로고    scopus 로고
    • Allosteric modulation of G protein-coupled receptors
    • Ijzerman A, Kourounakis A, van der Klein P. Allosteric modulation of G protein-coupled receptors. Farmaco 2001;56:67-70.
    • (2001) Farmaco , vol.56 , pp. 67-70
    • Ijzerman, A.1    Kourounakis, A.2    Van der Klein, P.3
  • 129
    • 0033029793 scopus 로고    scopus 로고
    • Calcimimetic compounds: A direct approach to controlling plasma levels of parathyroid hormone in hyperparathyroidism
    • Nemeth EF, Fox J. Calcimimetic compounds: a direct approach to controlling plasma levels of parathyroid hormone in hyperparathyroidism. Trends Endocrinol Metab 1999;10:66-71.
    • (1999) Trends Endocrinol Metab , vol.10 , pp. 66-71
    • Nemeth, E.F.1    Fox, J.2
  • 130
    • 0031763613 scopus 로고    scopus 로고
    • Treatment of hypercalcemia secondary to parathyroid carcinoma with a novel calcimimetic agent
    • Collins MT, Skarulis MC, Bilezikian JP, et al. Treatment of hypercalcemia secondary to parathyroid carcinoma with a novel calcimimetic agent. J Clin Endocrinol Metab 1998;83:1083-8.
    • (1998) J Clin Endocrinol Metab , vol.83 , pp. 1083-1088
    • Collins, M.T.1    Skarulis, M.C.2    Bilezikian, J.P.3
  • 131
    • 0035818605 scopus 로고    scopus 로고
    • Positive allosteric modulators of metabotropic glutamate 1 receptor: Characterization, mechanism of action, and binding site
    • Knoflach F, Mutel V, Jolidon S, et al. Positive allosteric modulators of metabotropic glutamate 1 receptor: characterization, mechanism of action, and binding site. Proc Natl Acad Sci U S A 2001;98:13402-7.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 13402-13407
    • Knoflach, F.1    Mutel, V.2    Jolidon, S.3
  • 132
    • 0032590063 scopus 로고    scopus 로고
    • Adenosine A1 receptor-dependent and -independent effects of the allosteric enhancer PD 81,723
    • Musser B, Mudumbi RV, Liu J, et al. Adenosine A1 receptor-dependent and -independent effects of the allosteric enhancer PD 81,723. J Pharmacol Exp Ther 1999;288:446-54.
    • (1999) J Pharmacol Exp Ther , vol.288 , pp. 446-454
    • Musser, B.1    Mudumbi, R.V.2    Liu, J.3
  • 134
    • 0035170060 scopus 로고    scopus 로고
    • SCH-202676: An allosteric modulator of both agonist and antagonist binding to G protein-coupled receptors
    • Fawzi AB, Macdonald D, Benbow LL, et al. SCH-202676: an allosteric modulator of both agonist and antagonist binding to G protein-coupled receptors. Mol Pharmacol 2001;59:30-7.
    • (2001) Mol Pharmacol , vol.59 , pp. 30-37
    • Fawzi, A.B.1    Macdonald, D.2    Benbow, L.L.3
  • 135
    • 0036174608 scopus 로고    scopus 로고
    • Dimerization: An emerging concept for G protein-coupled receptor ontogeny and function
    • Angers S, Salahpour A, Bouvier M. Dimerization: an emerging concept for G protein-coupled receptor ontogeny and function. Annu Rev Pharmacol Toxicol 2002;42:409-35.
    • (2002) Annu Rev Pharmacol Toxicol , vol.42 , pp. 409-435
    • Angers, S.1    Salahpour, A.2    Bouvier, M.3
  • 136
    • 0032574982 scopus 로고    scopus 로고
    • RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor
    • McLatchie LM, Fraser NJ, Main MJ, et al. RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor. Nature 1998;393:333-9.
    • (1998) Nature , vol.393 , pp. 333-339
    • McLatchie, L.M.1    Fraser, N.J.2    Main, M.J.3
  • 137
    • 0034646972 scopus 로고    scopus 로고
    • Mammalian calcitonin receptor-like receptor/receptor activity modifying protein complexes define calcitonin gene-related peptide and adrenomedullin receptors in Drosophila Schneider 2 cells
    • Aldecoa A, Gujer R, Fischer JA, Born W. Mammalian calcitonin receptor-like receptor/receptor activity modifying protein complexes define calcitonin gene-related peptide and adrenomedullin receptors in Drosophila Schneider 2 cells. FEBS Lett 2000;471:156-60.
    • (2000) FEBS Lett , vol.471 , pp. 156-160
    • Aldecoa, A.1    Gujer, R.2    Fischer, J.A.3    Born, W.4
  • 138
    • 0035800877 scopus 로고    scopus 로고
    • Protein-protein interaction and not glycosylation determines the binding selectivity of heterodimers between the calcitonin receptor-like receptor and the receptor activity-modifying proteins
    • Hilairet S, Foord SM, Marshall FH, Bouvier M. Protein-protein interaction and not glycosylation determines the binding selectivity of heterodimers between the calcitonin receptor-like receptor and the receptor activity-modifying proteins. J Biol Chem 2001;276:29575-81.
    • (2001) J Biol Chem , vol.276 , pp. 29575-29581
    • Hilairet, S.1    Foord, S.M.2    Marshall, F.H.3    Bouvier, M.4
  • 139
    • 0030970135 scopus 로고    scopus 로고
    • Homer: A protein that selectively binds metabotropic glutamate receptors
    • Brakeman PR, Lanahan AA, O'Brien R, et al. Homer: a protein that selectively binds metabotropic glutamate receptors. Nature 1997;386:284-8.
    • (1997) Nature , vol.386 , pp. 284-288
    • Brakeman, P.R.1    Lanahan, A.A.2    O'Brien, R.3
  • 140
    • 0033679292 scopus 로고    scopus 로고
    • Structure of the Homer EVH1 domain-peptide complex reveals a new twist in polyproline recognition
    • Beneken J, Tu IC, Xiao B, et al. Structure of the Homer EVH1 domain-peptide complex reveals a new twist in polyproline recognition. Neuron 2000;26:143-54.
    • (2000) Neuron , vol.26 , pp. 143-154
    • Beneken, J.1    Tu, I.C.2    Xiao, B.3
  • 141
    • 0033598771 scopus 로고    scopus 로고
    • Involvement of unique leucine-zipper motif of PSD-Zip45 (Homer 1c/vesl-1L) in group 1 metabotropic glutamate receptor clustering
    • Tadokoro S, Tachibana T, Imanaka T, et al. Involvement of unique leucine-zipper motif of PSD-Zip45 (Homer 1c/vesl-1L) in group 1 metabotropic glutamate receptor clustering. Proc Natl Acad Sci U S A 1999;96:13801-6.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 13801-13806
    • Tadokoro, S.1    Tachibana, T.2    Imanaka, T.3
  • 142
    • 0033964384 scopus 로고    scopus 로고
    • Homer-1c/Vesl-1L modulates the cell surface targeting of metabotropic glutamate receptor type 1alpha: Evidence for an anchoring function
    • Ciruela F, Soloviev MM, Chan WY, McIlhinney RA. Homer-1c/Vesl-1L modulates the cell surface targeting of metabotropic glutamate receptor type 1alpha: evidence for an anchoring function. Mol Cell Neurosci 2000;15:36-50.
    • (2000) Mol Cell Neurosci , vol.15 , pp. 36-50
    • Ciruela, F.1    Soloviev, M.M.2    Chan, W.Y.3    McIlhinney, R.A.4
  • 143
    • 0037093469 scopus 로고    scopus 로고
    • Synaptic multiprotein complexes associated with 5-HT(2C) receptors: A proteomic approach
    • Becamel C, Alonso G, Galeotti N, et al. Synaptic multiprotein complexes associated with 5-HT(2C) receptors: a proteomic approach. EMBO J 2002;21:2332-42.
    • (2002) EMBO J , vol.21 , pp. 2332-2342
    • Becamel, C.1    Alonso, G.2    Galeotti, N.3
  • 144
    • 0032498963 scopus 로고    scopus 로고
    • The beta2-adrenergic receptor interacts with the Na+/H+-exchanger regulatory factor to control Na+/H+ exchange
    • Hall RA, Premont RT, Chow CW, et al. The beta2-adrenergic receptor interacts with the Na+/H+-exchanger regulatory factor to control Na+/H+ exchange. Nature 1998;392:626-30.
    • (1998) Nature , vol.392 , pp. 626-630
    • Hall, R.A.1    Premont, R.T.2    Chow, C.W.3
  • 146
    • 0035013840 scopus 로고    scopus 로고
    • Regulator of G protein signaling proteins: Novel multifunctional drug targets
    • Zhong H, Neubig RR. Regulator of G protein signaling proteins: novel multifunctional drug targets. J Pharmacol Exp Ther 2001;297:837-45.
    • (2001) J Pharmacol Exp Ther , vol.297 , pp. 837-845
    • Zhong, H.1    Neubig, R.R.2
  • 147
    • 0036937166 scopus 로고    scopus 로고
    • Regulators of G protein signaling (RGS proteins): Novel central nervous system drug targets
    • Neubig RR. Regulators of G protein signaling (RGS proteins): novel central nervous system drug targets. J Pept Res 2002;60:312-36.
    • (2002) J Pept Res , vol.60 , pp. 312-336
    • Neubig, R.R.1
  • 148
    • 0035101820 scopus 로고    scopus 로고
    • Evolving concepts in G protein-coupled receptor endocytosis: The role in receptor desensitization and signaling
    • Ferguson SS. Evolving concepts in G protein-coupled receptor endocytosis: the role in receptor desensitization and signaling. Pharmacol Rev 2001;53:1-24.
    • (2001) Pharmacol Rev , vol.53 , pp. 1-24
    • Ferguson, S.S.1
  • 149
    • 0035487327 scopus 로고    scopus 로고
    • Classical and new roles of beta-arrestins in the regulation of G-protein-coupled receptors
    • Pierce KL, Lefkowitz RJ. Classical and new roles of beta-arrestins in the regulation of G-protein-coupled receptors. Nat Rev Neurosci 2001;2:727-33.
    • (2001) Nat Rev Neurosci , vol.2 , pp. 727-733
    • Pierce, K.L.1    Lefkowitz, R.J.2
  • 150
    • 0029864554 scopus 로고    scopus 로고
    • Carboxyl-terminal fragments of phospholipase C-beta1 with intrinsic Gq GTPase-activating protein (GAP) activity
    • Paulssen RH, Woodson J, Liu Z, Ross EM. Carboxyl-terminal fragments of phospholipase C-beta1 with intrinsic Gq GTPase-activating protein (GAP) activity. J Biol Chem 1996;271:26622-9.
    • (1996) J Biol Chem , vol.271 , pp. 26622-26629
    • Paulssen, R.H.1    Woodson, J.2    Liu, Z.3    Ross, E.M.4
  • 153
    • 0032480888 scopus 로고    scopus 로고
    • Epac is a Rap1 guanine-nucleotide-exchange factor directly activated by cyclic AMP
    • de Rooij J, Zwartkruis FJ, Verheijen MH, et al. Epac is a Rap1 guanine-nucleotide-exchange factor directly activated by cyclic AMP. Nature 1998;396:474-7.
    • (1998) Nature , vol.396 , pp. 474-477
    • De Rooij, J.1    Zwartkruis, F.J.2    Verheijen, M.H.3
  • 154
    • 0034268796 scopus 로고    scopus 로고
    • Src tyrosine kinase is a novel direct effector of G proteins
    • Ma YC, Huang JY, All S, et al. Src tyrosine kinase is a novel direct effector of G proteins. Cell 2000;102:635-46.
    • (2000) Cell , vol.102 , pp. 635-646
    • Ma, Y.C.1    Huang, J.Y.2    All, S.3
  • 155
    • 0034721868 scopus 로고    scopus 로고
    • Stabilization of the GDP-bound conformation of Gialpha by a peptide derived from the G-protein regulatory motif of AGS3
    • Peterson YK, Bernard ML, Ma H, et al. Stabilization of the GDP-bound conformation of Gialpha by a peptide derived from the G-protein regulatory motif of AGS3. J Biol Chem 2000;275:33193-6.
    • (2000) J Biol Chem , vol.275 , pp. 33193-33196
    • Peterson, Y.K.1    Bernard, M.L.2    Ma, H.3
  • 156
    • 0035340989 scopus 로고    scopus 로고
    • Inhibition of GDP/GTP exchange on G alpha subunits by proteins containing G-protein regulatory motifs
    • Natochin M, Gasimov KG, Artemyev NO. Inhibition of GDP/GTP exchange on G alpha subunits by proteins containing G-protein regulatory motifs. Biochemistry 2001;40:5322-8.
    • (2001) Biochemistry , vol.40 , pp. 5322-5328
    • Natochin, M.1    Gasimov, K.G.2    Artemyev, N.O.3
  • 157
    • 0037171778 scopus 로고    scopus 로고
    • Structural determinants for GoLoco-induced inhibition of nucleotide release by Galpha subunits
    • Kimple RJ, Kimple ME, Betts L, et al. Structural determinants for GoLoco-induced inhibition of nucleotide release by Galpha subunits. Nature 2002;416:878-81.
    • (2002) Nature , vol.416 , pp. 878-881
    • Kimple, R.J.1    Kimple, M.E.2    Betts, L.3
  • 158
    • 0028122479 scopus 로고
    • Missense rhodopsin mutation in a family with recessive RP
    • Kumaramanickavel G, Maw M, Denton MJ, et al. Missense rhodopsin mutation in a family with recessive RP. Nat Genet 1994;8:10-1.
    • (1994) Nat Genet , vol.8 , pp. 10-11
    • Kumaramanickavel, G.1    Maw, M.2    Denton, M.J.3
  • 159
    • 0028820045 scopus 로고
    • Mutations in the gene encoding the alpha subunit of the rod cGMP-gated channel in autosomal recessive retinitis pigmentosa
    • Dryja TP, Finn JT, Peng YW, et al. Mutations in the gene encoding the alpha subunit of the rod cGMP-gated channel in autosomal recessive retinitis pigmentosa. Proc Natl Acad Sci U S A 1995;92:10177-81.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 10177-10181
    • Dryja, T.P.1    Finn, J.T.2    Peng, Y.W.3
  • 160
    • 0024449541 scopus 로고
    • Molecular genetics of human blue cone monochromacy
    • Nathans J, Davenport CM, Maumenee IH, et al. Molecular genetics of human blue cone monochromacy. Science 1989;245:831-88.
    • (1989) Science , vol.245 , pp. 831-888
    • Nathans, J.1    Davenport, C.M.2    Maumenee, I.H.3
  • 161
    • 0027436009 scopus 로고
    • Genetic heterogeneity among blue-cone monochromats
    • Nathans J, Maumenee IH, Zrenner E, et al. Genetic heterogeneity among blue-cone monochromats. Am J Hum Genet 1993;53:987-1000.
    • (1993) Am J Hum Genet , vol.53 , pp. 987-1000
    • Nathans, J.1    Maumenee, I.H.2    Zrenner, E.3
  • 162
    • 0026581759 scopus 로고
    • Human tritanopia associated with two amino acid substitutions in the blue-sensitive opsin
    • Weitz CJ, Miyake Y, Shinzato K, et al. Human tritanopia associated with two amino acid substitutions in the blue-sensitive opsin. Am J Hum Genet 1992;50:498-507.
    • (1992) Am J Hum Genet , vol.50 , pp. 498-507
    • Weitz, C.J.1    Miyake, Y.2    Shinzato, K.3
  • 163
    • 0036071242 scopus 로고    scopus 로고
    • Mutations in the cone photoreceptor G-protein alpha-subunit gene GNAT2 in patients with achromatopsia
    • Kohl S, Baumann B, Rosenberg T, et al. Mutations in the cone photoreceptor G-protein alpha-subunit gene GNAT2 in patients with achromatopsia. Am J Hum Genet 2002;71:422-45.
    • (2002) Am J Hum Genet , vol.71 , pp. 422-445
    • Kohl, S.1    Baumann, B.2    Rosenberg, T.3
  • 164
    • 0031803762 scopus 로고    scopus 로고
    • Total colourblindness is caused by mutations in the gene encoding the alpha-subunit of the cone photoreceptor cGMP-gated cation channel
    • Kohl S, Marx T, Giddings I, et al. Total colourblindness is caused by mutations in the gene encoding the alpha-subunit of the cone photoreceptor cGMP-gated cation channel. Nat Genet 1998;19:257-9.
    • (1998) Nat Genet , vol.19 , pp. 257-259
    • Kohl, S.1    Marx, T.2    Giddings, I.3
  • 165
    • 0034284696 scopus 로고    scopus 로고
    • Mutations in the CNGB3 gene encoding the beta-subunit of the cone photoreceptor cGMP-gated channel are responsible for achromatopsia (ACHM3) linked to chromosome 8q21
    • Kohl S, Baumann B, Broghammer M, et al. Mutations in the CNGB3 gene encoding the beta-subunit of the cone photoreceptor cGMP-gated channel are responsible for achromatopsia (ACHM3) linked to chromosome 8q21. Hum Mol Genet 2000;9:2107-16.
    • (2000) Hum Mol Genet , vol.9 , pp. 2107-2116
    • Kohl, S.1    Baumann, B.2    Broghammer, M.3
  • 166
    • 0033211151 scopus 로고    scopus 로고
    • Single nucleotide polymorphisms of the N-formyl peptide receptor in localized juvenile periodontitis
    • Gwinn MR, Sharma A, De Nardin E. Single nucleotide polymorphisms of the N-formyl peptide receptor in localized juvenile periodontitis. J Periodontol 1999;70:1194-201.
    • (1999) J Periodontol , vol.70 , pp. 1194-1201
    • Gwinn, M.R.1    Sharma, A.2    De Nardin, E.3
  • 167
    • 0035834685 scopus 로고    scopus 로고
    • Defective Gi protein coupling in two formyl peptide receptor mutants associated with localized juvenile periodontitis
    • Seifert R, Wenzel-Seifert K. Defective Gi protein coupling in two formyl peptide receptor mutants associated with localized juvenile periodontitis. J Biol Chem 2001;276:42043-9.
    • (2001) J Biol Chem , vol.276 , pp. 42043-42049
    • Seifert, R.1    Wenzel-Seifert, K.2
  • 168
    • 17344366286 scopus 로고    scopus 로고
    • Association of a human G-protein b3 subunit variant with hypertension
    • Siffert W, Rosskopf D, Siffert G, et al. Association of a human G-protein b3 subunit variant with hypertension. Nat Genet 1998;18:45-8.
    • (1998) Nat Genet , vol.18 , pp. 45-48
    • Siffert, W.1    Rosskopf, D.2    Siffert, G.3
  • 169
    • 0037391281 scopus 로고    scopus 로고
    • Identification and characterization of Gbeta3s2, a novel splice variant of the G-protein beta3 subunit
    • Rosskopf D, Manthey I, Habich C, et al. Identification and characterization of Gbeta3s2, a novel splice variant of the G-protein beta3 subunit. Biochem J 2003;371:223-32.
    • (2003) Biochem J , vol.371 , pp. 223-232
    • Rosskopf, D.1    Manthey, I.2    Habich, C.3
  • 170
    • 0028909901 scopus 로고
    • G-protein mutations in human pituitary adrenocorticotrophic hormone-secreting adenomas
    • Williamson EA, Ince PG, Harrison D, et al. G-protein mutations in human pituitary adrenocorticotrophic hormone-secreting adenomas. Eur J Clin Invest 1995;25:128-31.
    • (1995) Eur J Clin Invest , vol.25 , pp. 128-131
    • Williamson, E.A.1    Ince, P.G.2    Harrison, D.3
  • 171
    • 0036159168 scopus 로고    scopus 로고
    • An R201H activating mutation of the GNAS1 (Gsalpha) gene in a corticotroph pituitary adenoma
    • Riminucci M, Collins MT, Lala R, et al. An R201H activating mutation of the GNAS1 (Gsalpha) gene in a corticotroph pituitary adenoma. Mol Pathol 2002;55:58-60.
    • (2002) Mol Pathol , vol.55 , pp. 58-60
    • Riminucci, M.1    Collins, M.T.2    Lala, R.3
  • 172
    • 0027340743 scopus 로고
    • Activating mutations of the Gs alpha-gene in nonfunctioning pituitary tumors
    • Tordjman K, Stern N, Ouaknine G, et al. Activating mutations of the Gs alpha-gene in nonfunctioning pituitary tumors. J Clin Endocrinol Metab 1993;77:765-79.
    • (1993) J Clin Endocrinol Metab , vol.77 , pp. 765-779
    • Tordjman, K.1    Stern, N.2    Ouaknine, G.3
  • 173
    • 0028670141 scopus 로고
    • Gs alpha and Gi2 alpha mutations in clinically non-functioning pituitary tumours
    • Williamson EA, Daniels M, Foster S, et al. Gs alpha and Gi2 alpha mutations in clinically non-functioning pituitary tumours. Clin Endocrinol (Oxf) 1994;41:815-20.
    • (1994) Clin Endocrinol (Oxf) , vol.41 , pp. 815-820
    • Williamson, E.A.1    Daniels, M.2    Foster, S.3
  • 174
    • 0026003074 scopus 로고
    • Activating mutations of the stimulatory G protein in the McCune-Albright syndrome
    • Weinstein LS, Shenker A, Gejman PV, et al. Activating mutations of the stimulatory G protein in the McCune-Albright syndrome. N Engl J Med 1991;325:1688-95.
    • (1991) N Engl J Med , vol.325 , pp. 1688-1695
    • Weinstein, L.S.1    Shenker, A.2    Gejman, P.V.3
  • 175
  • 176
    • 0026664955 scopus 로고
    • Mutational activation of RAS and GSP oncogenes in differentiated thyroid cancer and their biological implications
    • Goretzki PE, Lyons J, Stacy-Phipps S, et al. Mutational activation of RAS and GSP oncogenes in differentiated thyroid cancer and their biological implications. World J Surg 1992;16:576-81.
    • (1992) World J Surg , vol.16 , pp. 576-581
    • Goretzki, P.E.1    Lyons, J.2    Stacy-Phipps, S.3
  • 177
    • 0029821316 scopus 로고    scopus 로고
    • Absence of the previously reported G protein oncogene (gip2) in ovarian granulosa cell tumors
    • Shen Y, Mamers P, Jobling T, et al. Absence of the previously reported G protein oncogene (gip2) in ovarian granulosa cell tumors. J Clin Endocrinol Metab 1996;81:4159-61.
    • (1996) J Clin Endocrinol Metab , vol.81 , pp. 4159-4161
    • Shen, Y.1    Mamers, P.2    Jobling, T.3
  • 178
    • 0030266415 scopus 로고    scopus 로고
    • Mutation analysis of gonadotropin receptor and G protein genes in various types of human ovarian tumors
    • Ichikawa Y, Yoshida S, Suzuki H, et al. Mutation analysis of gonadotropin receptor and G protein genes in various types of human ovarian tumors. Jpn J Clin Oncol 1996;26:298-302.
    • (1996) Jpn J Clin Oncol , vol.26 , pp. 298-302
    • Ichikawa, Y.1    Yoshida, S.2    Suzuki, H.3
  • 179
    • 0028983355 scopus 로고
    • Oncogenic mutations of alpha-Gi2 protein are not determinant for human adrenocortical tumourigenesis
    • Gicquel C, Dib A, Bertagna X, et al. Oncogenic mutations of alpha-Gi2 protein are not determinant for human adrenocortical tumourigenesis. Eur J Endocrinol 1995;133:166-72.
    • (1995) Eur J Endocrinol , vol.133 , pp. 166-172
    • Gicquel, C.1    Dib, A.2    Bertagna, X.3
  • 180
    • 0027368204 scopus 로고
    • No evidence for oncogenic mutations in guanine nucleotide-binding proteins of human adrenocortical neoplasms
    • Reincke M, Karl M, Travis W, Chrousos GP. No evidence for oncogenic mutations in guanine nucleotide-binding proteins of human adrenocortical neoplasms. J Clin Endocrinol Metab 1993;77:1419-22.
    • (1993) J Clin Endocrinol Metab , vol.77 , pp. 1419-1422
    • Reincke, M.1    Karl, M.2    Travis, W.3    Chrousos, G.P.4
  • 181
    • 0027934280 scopus 로고
    • Activating mutation in the stimulatory guanine nucleotide-binding protein in an infant with Cushing's syndrome and nodular adrenal hyperplasia
    • Boston BA, Mandel S, LaFranchi S, Bliziotes M. Activating mutation in the stimulatory guanine nucleotide-binding protein in an infant with Cushing's syndrome and nodular adrenal hyperplasia. J Clin Endocrinol Metab 1994;79:890-3.
    • (1994) J Clin Endocrinol Metab , vol.79 , pp. 890-893
    • Boston, B.A.1    Mandel, S.2    LaFranchi, S.3    Bliziotes, M.4
  • 182
    • 0033762171 scopus 로고    scopus 로고
    • A GNAS1 imprinting defect in pseudohypoparathyroidism type IB
    • Liu J, Litman D, Rosenberg MJ, et al. A GNAS1 imprinting defect in pseudohypoparathyroidism type IB. J Clin Invest 2000;106:1167-74.
    • (2000) J Clin Invest , vol.106 , pp. 1167-1174
    • Liu, J.1    Litman, D.2    Rosenberg, M.J.3
  • 183
    • 0027423948 scopus 로고
    • Hereditary isolated glucocorticoid deficiency is associated with abnormalities of the adrenocorticotropin receptor gene
    • Tsigos C, Arai K, Hung W, Chrousos GP. Hereditary isolated glucocorticoid deficiency is associated with abnormalities of the adrenocorticotropin receptor gene. J Clin Invest 1993;92:2458-61.
    • (1993) J Clin Invest , vol.92 , pp. 2458-2461
    • Tsigos, C.1    Arai, K.2    Hung, W.3    Chrousos, G.P.4
  • 184
    • 0027396787 scopus 로고
    • Familial glucocorticoid deficiency associated with point mutation in the adrenocorticotropin receptor
    • Clark AJ, McLoughlin L, Grossman A. Familial glucocorticoid deficiency associated with point mutation in the adrenocorticotropin receptor. Lancet 1993;341:461-2.
    • (1993) Lancet , vol.341 , pp. 461-462
    • Clark, A.J.1    McLoughlin, L.2    Grossman, A.3
  • 185
    • 0030829977 scopus 로고    scopus 로고
    • The dwarfs of Sindh: Severe growth hormone (GH) deficiency caused by a mutation in the GH-releasing hormone receptor gene
    • Baumann G, Maheshwari H. The dwarfs of Sindh: severe growth hormone (GH) deficiency caused by a mutation in the GH-releasing hormone receptor gene. Acta Paediatr Suppl 1997;423:33-8.
    • (1997) Acta Paediatr Suppl , vol.423 , pp. 33-38
    • Baumann, G.1    Maheshwari, H.2
  • 186
    • 0030994365 scopus 로고    scopus 로고
    • Familial congenital hypothyroidism due to inactivating mutation of the thyrotropin receptor causing profound hypoplasia of the thyroid gland
    • Abramowicz MJ, Duprez L, Parma J, et al. Familial congenital hypothyroidism due to inactivating mutation of the thyrotropin receptor causing profound hypoplasia of the thyroid gland. J Clin Invest 1997;99:3018-24.
    • (1997) J Clin Invest , vol.99 , pp. 3018-3024
    • Abramowicz, M.J.1    Duprez, L.2    Parma, J.3
  • 187
    • 17144439793 scopus 로고    scopus 로고
    • Mutations in gonadotropin-releasing hormone receptor gene cause hypogonadotropic hypogonadism
    • Layman LC, Cohen DP, Jin M, et al. Mutations in gonadotropin-releasing hormone receptor gene cause hypogonadotropic hypogonadism. Nat Genet 1998;18:14-5.
    • (1998) Nat Genet , vol.18 , pp. 14-15
    • Layman, L.C.1    Cohen, D.P.2    Jin, M.3
  • 188
    • 0030698188 scopus 로고    scopus 로고
    • A family with hypogonadotropic hypogonadism and mutations in the gonadotropin-releasing hormone receptor
    • de Roux N, Young J, Misrahi M, et al. A family with hypogonadotropic hypogonadism and mutations in the gonadotropin-releasing hormone receptor. N Engl J Med 1997;337:1597-602.
    • (1997) N Engl J Med , vol.337 , pp. 1597-1602
    • De Roux, N.1    Young, J.2    Misrahi, M.3
  • 189
    • 0028835899 scopus 로고
    • Male pseudohermaphroditism due to a homozygous missense mutation of the luteinizing hormone receptor gene
    • Kremer H, Kraaij R, Toledo SP, et al. Male pseudohermaphroditism due to a homozygous missense mutation of the luteinizing hormone receptor gene. Nat Genet 1995;9:160-4.
    • (1995) Nat Genet , vol.9 , pp. 160-164
    • Kremer, H.1    Kraaij, R.2    Toledo, S.P.3
  • 190
    • 0030596101 scopus 로고    scopus 로고
    • Functional and clinical consequences of mutations in the FSH receptor
    • Gromoll J, Simoni M, Nordhoff V, et al. Functional and clinical consequences of mutations in the FSH receptor. Mol Cell Endocrinol 1996;125:177-82.
    • (1996) Mol Cell Endocrinol , vol.125 , pp. 177-182
    • Gromoll, J.1    Simoni, M.2    Nordhoff, V.3
  • 191
    • 0027956207 scopus 로고
    • sa in patients with gain and loss of endocrine function
    • sa in patients with gain and loss of endocrine function. Nature 1994;371:164-8.
    • (1994) Nature , vol.371 , pp. 164-168
    • Iiri, T.1    Herzmark, P.2    Nakamoto, J.M.3
  • 192
    • 0028037143 scopus 로고
    • Autosomal dominant hypocalcaemia caused by a Ca(2+)-sensing receptor gene mutation
    • Pollak MR, Brown EM, Estep HL, et al. Autosomal dominant hypocalcaemia caused by a Ca(2+)-sensing receptor gene mutation. Nat Genet 1994;8:303-37.
    • (1994) Nat Genet , vol.8 , pp. 303-337
    • Pollak, M.R.1    Brown, E.M.2    Estep, H.L.3
  • 193
    • 0032961258 scopus 로고    scopus 로고
    • A heterozygous frameshift mutation in the endothelin-3 (EDN-3) gene in isolated Hirschsprung's disease
    • Svensson PJ, Von Tell D, Molander ML, et al. A heterozygous frameshift mutation in the endothelin-3 (EDN-3) gene in isolated Hirschsprung's disease. Pediatr Res 1999;45:714-77.
    • (1999) Pediatr Res , vol.45 , pp. 714-777
    • Svensson, P.J.1    Von Tell, D.2    Molander, M.L.3
  • 194
    • 0028618372 scopus 로고
    • A missense mutation of the endothelin-B receptor gene in multigenic Hirschsprung's disease
    • Puffenberger EG, Hosoda K, Washington SS, et al. A missense mutation of the endothelin-B receptor gene in multigenic Hirschsprung's disease. Cell 1994;79:1257-66.
    • (1994) Cell , vol.79 , pp. 1257-1266
    • Puffenberger, E.G.1    Hosoda, K.2    Washington, S.S.3
  • 195
    • 0028862473 scopus 로고
    • Mutation of the endothelin-receptor B gene in Waardenburg-Hirschsprung disease
    • Attie T, Till M, Pelet A, et al. Mutation of the endothelin-receptor B
    • (1995) Hum Mol Genet , vol.4 , pp. 2407-2409
    • Attie, T.1    Till, M.2    Pelet, A.3
  • 196
    • 0034726747 scopus 로고    scopus 로고
    • Functional analysis of five endothelin-B receptor mutations found in human Hirschsprung disease patients
    • Abe Y, Sakurai T, Yamada T, et al. Functional analysis of five endothelin-B receptor mutations found in human Hirschsprung disease patients. Biochem Biophys Res Commun 2000;275:524-31.
    • (2000) Biochem Biophys Res Commun , vol.275 , pp. 524-531
    • Abe, Y.1    Sakurai, T.2    Yamada, T.3
  • 197
    • 0006457459 scopus 로고    scopus 로고
    • Mutation of the endothelin-3 gene in the Waardenburg-Hirschsprung disease (Shah-Waardenburg syndrome)
    • Edery P, Attie T, Amiel J, et al. Mutation of the endothelin-3 gene in the Waardenburg-Hirschsprung disease (Shah-Waardenburg syndrome). Nat Genet 1996;12:442-4.
    • (1996) Nat Genet , vol.12 , pp. 442-444
    • Edery, P.1    Attie, T.2    Amiel, J.3
  • 198
    • 0009675716 scopus 로고    scopus 로고
    • A homozygous mutation in the endothelin-3 gene associated with a combined Waardenburg type 2 and Hirschsprung phenotype (Shah-Waardenburg syndrome)
    • Hofstra RM, Osinga J, Tan-Sindhunata G, et al. A homozygous mutation in the endothelin-3 gene associated with a combined Waardenburg type 2 and Hirschsprung phenotype (Shah-Waardenburg syndrome). Nat Genet 1996;12:445-7.
    • (1996) Nat Genet , vol.12 , pp. 445-447
    • Hofstra, R.M.1    Osinga, J.2    Tan-Sindhunata, G.3
  • 199
    • 0023598429 scopus 로고
    • Hemorrhagic thrombocytopathy with platelet thromboxane A2 receptor abnormality: Defective signal transduction with normal binding activity
    • Ushikubi F, Okuma M, Kanaji K, et al. Hemorrhagic thrombocytopathy with platelet thromboxane A2 receptor abnormality: defective signal transduction with normal binding activity. Thromb Haemost 1987;57:158-64.
    • (1987) Thromb Haemost , vol.57 , pp. 158-164
    • Ushikubi, F.1    Okuma, M.2    Kanaji, K.3
  • 200
    • 0028170151 scopus 로고
    • Arg60 to Leu mutation of the human thromboxane A2 receptor in a dominantly inherited bleeding disorder
    • Hirata T, Kakizuka A, Ushikubi F, et al. Arg60 to Leu mutation of the human thromboxane A2 receptor in a dominantly inherited bleeding disorder. J Clin Invest 1994;94:1662-7.
    • (1994) J Clin Invest , vol.94 , pp. 1662-1667
    • Hirata, T.1    Kakizuka, A.2    Ushikubi, F.3
  • 201
    • 0026935109 scopus 로고
    • Mutations in the vasopressin type 2 receptor gene (AVPR2) associated with nephrogenic diabetes insipidus
    • van den Ouweland AM, Dreesen JC, Verdijk M, et al. Mutations in the vasopressin type 2 receptor gene (AVPR2) associated with nephrogenic diabetes insipidus. Nat Genet 1992;2:99-102.
    • (1992) Nat Genet , vol.2 , pp. 99-102
    • Van den Ouweland, A.M.1    Dreesen, J.C.2    Verdijk, M.3
  • 202
    • 0026937176 scopus 로고
    • Mutations in the V2 vasopressin receptor gene are associated with X-linked nephrogenic diabetes insipidus
    • Pan Y, Metzenberg A, Das S, et al. Mutations in the V2 vasopressin receptor gene are associated with X-linked nephrogenic diabetes insipidus. Nat Genet 1992;2:103-16.
    • (1992) Nat Genet , vol.2 , pp. 103-116
    • Pan, Y.1    Metzenberg, A.2    Das, S.3
  • 203
    • 0026744306 scopus 로고
    • Molecular identification of the gene responsible for congenital nephrogenic diabetes insipidus
    • Rosenthal W, Seibold A, Antaramian A, et al. Molecular identification of the gene responsible for congenital nephrogenic diabetes insipidus. Nature 1992;359:233-5.
    • (1992) Nature , vol.359 , pp. 233-235
    • Rosenthal, W.1    Seibold, A.2    Antaramian, A.3
  • 204
    • 0033869518 scopus 로고    scopus 로고
    • Activating Gs (alpha) mutation in intramuscular myxomas with and without fibrous dysplasia of bone
    • Okamoto S, Hisaoka M, Ushijima M, et al. Activating Gs (alpha) mutation in intramuscular myxomas with and without fibrous dysplasia of bone. Virchows Arch 2000;437:133-7.
    • (2000) Virchows Arch , vol.437 , pp. 133-137
    • Okamoto, S.1    Hisaoka, M.2    Ushijima, M.3
  • 205
    • 0033793009 scopus 로고    scopus 로고
    • Deficiency of the alpha-subunit of the stimulatory G protein and severe extraskeletal ossification
    • Eddy MC, Jan De Beur SM, Yandow SM, et al. Deficiency of the alpha-subunit of the stimulatory G protein and severe extraskeletal ossification. J Bone Miner Res 2000;15:2074-83.
    • (2000) J Bone Miner Res , vol.15 , pp. 2074-2083
    • Eddy, M.C.1    Jan De Beur, S.M.2    Yandow, S.M.3
  • 206
    • 0037050365 scopus 로고    scopus 로고
    • Paternally inherited inactivating mutations of the GNAS1 gene in progressive osseous heteroplasia
    • Shore EM, Ahn J, Jan de Beur S, et al. Paternally inherited inactivating mutations of the GNAS1 gene in progressive osseous heteroplasia. N Engl J Med 2002;346:99-106.
    • (2002) N Engl J Med , vol.346 , pp. 99-106
    • Shore, E.M.1    Ahn, J.2    Jan de Beur, S.3
  • 207
    • 0037162114 scopus 로고    scopus 로고
    • GNAS1 mutations and progressive osseous heteroplasia
    • Ahmed SF, Barr DG, Bonthron DT. GNAS1 mutations and progressive osseous heteroplasia. N Engl J Med 2002;346:1669-71.
    • (2002) N Engl J Med , vol.346 , pp. 1669-1671
    • Ahmed, S.F.1    Barr, D.G.2    Bonthron, D.T.3
  • 208
    • 0031725947 scopus 로고    scopus 로고
    • Inactivating mutation in the human parathyroid hormone receptor type 1 gene in Blomstrand chondrodysplasia
    • Karaplis AC, He B, Nguyen MT, et al. Inactivating mutation in the human parathyroid hormone receptor type 1 gene in Blomstrand chondrodysplasia. Endocrinology 1998;139:5255-8.
    • (1998) Endocrinology , vol.139 , pp. 5255-5258
    • Karaplis, A.C.1    He, B.2    Nguyen, M.T.3
  • 209
    • 0031769483 scopus 로고    scopus 로고
    • A homozygous inactivating mutation in the parathyroid hormone/parathyroid hormone-related peptide receptor causing Blomstrand chondrodysplasia
    • Zhang P, Jobert AS, Couvineau A, Silve C. A homozygous inactivating mutation in the parathyroid hormone/parathyroid hormone-related peptide receptor causing Blomstrand chondrodysplasia. J Clin Endocrinol Metab 1998;83:3365-8.
    • (1998) J Clin Endocrinol Metab , vol.83 , pp. 3365-3368
    • Zhang, P.1    Jobert, A.S.2    Couvineau, A.3    Silve, C.4
  • 210
    • 0028943780 scopus 로고
    • A constitutively active mutant PTH-PTHrP receptor in Jansen-type metaphyseal chondrodysplasia
    • Schipani E, Kruse K, Juppner H. A constitutively active mutant PTH-PTHrP receptor in Jansen-type metaphyseal chondrodysplasia. Science 1995;268:98-100.
    • (1995) Science , vol.268 , pp. 98-100
    • Schipani, E.1    Kruse, K.2    Juppner, H.3
  • 211
    • 0028133063 scopus 로고
    • Distinct patterns of bidirectional regulation of mammalian adenylyl cyclases
    • Taussig R, Tang WJ, Hepler JR, Gilman AG. Distinct patterns of bidirectional regulation of mammalian adenylyl cyclases. J Biol Chem 1994;269:6093-100.
    • (1994) J Biol Chem , vol.269 , pp. 6093-6100
    • Taussig, R.1    Tang, W.J.2    Hepler, J.R.3    Gilman, A.G.4
  • 212
    • 0033618396 scopus 로고    scopus 로고
    • Modulation of rap activity by direct interaction of Galpha(o) with Rap1 GTPase-activating protein
    • Jordan JD, Carey KD, Stork PJ, Iyengar R. Modulation of rap activity by direct interaction of Galpha(o) with Rap1 GTPase-activating protein. J Biol Chem 1999;274:21507-10.
    • (1999) J Biol Chem , vol.274 , pp. 21507-21510
    • Jordan, J.D.1    Carey, K.D.2    Stork, P.J.3    Iyengar, R.4
  • 213
    • 0033578884 scopus 로고    scopus 로고
    • A candidate target for G protein action in brain
    • Chen LT Gilman AG, Kozasa T. A candidate target for G protein action in brain. J Biol Chem 1999;274:26931-8.
    • (1999) J Biol Chem , vol.274 , pp. 26931-26938
    • Chen, L.T.1    Gilman, A.G.2    Kozasa, T.3
  • 214
    • 0025836752 scopus 로고
    • Characterization of G-protein alpha subunits in the Gq class: Expression in murine tissues and in stromal and hematopoietic cell lines
    • Wilkie TM, Scherle PA, Strathmann MP, et al. Characterization of G-protein alpha subunits in the Gq class: expression in murine tissues and in stromal and hematopoietic cell lines. Proc Natl Acad Sci U S A 1991;88:10049-53.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 10049-10053
    • Wilkie, T.M.1    Scherle, P.A.2    Strathmann, M.P.3
  • 215
    • 0029985041 scopus 로고    scopus 로고
    • A novel form of the G protein beta subunit Gbeta5 is specifically expressed in the vertebrate retina
    • Watson AJ, Aragay AM, Slepak VZ, Simon MI. A novel form of the G protein beta subunit Gbeta5 is specifically expressed in the vertebrate retina. J Biol Chem 1996;271:28154-60.
    • (1996) J Biol Chem , vol.271 , pp. 28154-28160
    • Watson, A.J.1    Aragay, A.M.2    Slepak, V.Z.3    Simon, M.I.4


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