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Volumn 12, Issue 12, 1998, Pages 1830-1845

Characterization of two LGR genes homologous to gonadotropin and thyrotropin receptors with extracellular leucine-rich repeats and a G protein-coupled, seven-transmembrane region

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; LEUCINE; THYROTROPIN RECEPTOR;

EID: 0000437998     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/mend.12.12.0211     Document Type: Article
Times cited : (254)

References (64)
  • 1
    • 0026321529 scopus 로고
    • Structure and function of the adrenergic receptor family
    • Roth NS, Lefkowitz RJ, Caron MG 1991 Structure and function of the adrenergic receptor family. Adv Exp Med Biol 308:223-238
    • (1991) Adv Exp Med Biol , vol.308 , pp. 223-238
    • Roth, N.S.1    Lefkowitz, R.J.2    Caron, M.G.3
  • 4
    • 0026743033 scopus 로고
    • The thyrotropin receptor and the regulation of thyrocyte function and growth
    • Vassart G, Dumont JE 1992 The thyrotropin receptor and the regulation of thyrocyte function and growth. Endocr Rev 13:596-611
    • (1992) Endocr Rev , vol.13 , pp. 596-611
    • Vassart, G.1    Dumont, J.E.2
  • 5
    • 0025237466 scopus 로고
    • The testicular receptor for follicle stimulating hormone: Structure and functional expression of cloned cDNA
    • Sprengel R, Braun T, Nikolics K, Segaloff DL, Seeburg PH 1990 The testicular receptor for follicle stimulating hormone: structure and functional expression of cloned cDNA. Mol Endocrinol 4:525-530
    • (1990) Mol Endocrinol , vol.4 , pp. 525-530
    • Sprengel, R.1    Braun, T.2    Nikolics, K.3    Segaloff, D.L.4    Seeburg, P.H.5
  • 6
    • 0031893949 scopus 로고    scopus 로고
    • The pathways connecting G protein-coupled receptors to the nucleus through divergent mitogen-activated protein kinase cascades
    • Gutkind JS 1998 The pathways connecting G protein-coupled receptors to the nucleus through divergent mitogen-activated protein kinase cascades. J Biol Chem 273:1839-1842
    • (1998) J Biol Chem , vol.273 , pp. 1839-1842
    • Gutkind, J.S.1
  • 7
    • 0032033682 scopus 로고    scopus 로고
    • G protein-coupled-receptor cross-talk: The fine-tuning of multiple receptor-signalling pathways
    • Selbie LA, Hill SJ 1998 G protein-coupled-receptor cross-talk: the fine-tuning of multiple receptor-signalling pathways. Trends Pharmacol Sci 19:87-93
    • (1998) Trends Pharmacol Sci , vol.19 , pp. 87-93
    • Selbie, L.A.1    Hill, S.J.2
  • 8
    • 0030626053 scopus 로고    scopus 로고
    • Interaction, signal generation, signal divergence, and signal transduction of LH/CG and the receptor
    • Ji TH, Ryu KS, Gilchrist R, Ji I 1997 Interaction, signal generation, signal divergence, and signal transduction of LH/CG and the receptor. Recent Prog Horm Res 52:431-453
    • (1997) Recent Prog Horm Res , vol.52 , pp. 431-453
    • Ji, T.H.1    Ryu, K.S.2    Gilchrist, R.3    Ji, I.4
  • 9
    • 0031916977 scopus 로고    scopus 로고
    • The lutenizing hormone receptor
    • Dufau ML 1998 The lutenizing hormone receptor. Annu Rev Physiol 60:461-496
    • (1998) Annu Rev Physiol , vol.60 , pp. 461-496
    • Dufau, M.L.1
  • 11
    • 0031457992 scopus 로고    scopus 로고
    • The follicle-stimulating hormone receptor: Biochemistry, molecular biology, physiology, and pathophysiology
    • Simoni M, Gromoll J, Nieschlag E 1997 The follicle-stimulating hormone receptor: biochemistry, molecular biology, physiology, and pathophysiology. Endocr Rev 18:739-773
    • (1997) Endocr Rev , vol.18 , pp. 739-773
    • Simoni, M.1    Gromoll, J.2    Nieschlag, E.3
  • 12
    • 0031033312 scopus 로고    scopus 로고
    • Molecular cloning, genomic organization, and developmental regulation of a novel receptor from Drosophila melanogaster, structurally related to members of the thyroid-stimulating hormone, follicle-stimulating hormone, luteinizing hormone/choriogonadotropin receptor family from mammals
    • Hauser F, Nothacker H, Grimmelikhuijzen CJP 1997 Molecular cloning, genomic organization, and developmental regulation of a novel receptor from Drosophila melanogaster, structurally related to members of the thyroid-stimulating hormone, follicle-stimulating hormone, luteinizing hormone/choriogonadotropin receptor family from mammals. J Biol Chem 272:1002-1010
    • (1997) J Biol Chem , vol.272 , pp. 1002-1010
    • Hauser, F.1    Nothacker, H.2    Grimmelikhuijzen, C.J.P.3
  • 13
    • 0027751626 scopus 로고
    • Molecular cloning of a novel, putative G protein-coupled receptor from sea anemones structurally related to members of the FSH, TSH, LH/CG receptor family from mammals
    • Nothacker HP, Grimmelikhuijzen CJ 1993 Molecular cloning of a novel, putative G protein-coupled receptor from sea anemones structurally related to members of the FSH, TSH, LH/CG receptor family from mammals. Biochem Biophys Res Commun 197:1062-1069
    • (1993) Biochem Biophys Res Commun , vol.197 , pp. 1062-1069
    • Nothacker, H.P.1    Grimmelikhuijzen, C.J.2
  • 14
    • 0028885124 scopus 로고
    • Purified rat acid-labile subunit and recombinant human insulin-like growth factor (IGF)-binding protein-3 can form a 150-kilodalton binary complex in vitro in the absence of IGFs
    • Lee CY, Rechler MM 1995 Purified rat acid-labile subunit and recombinant human insulin-like growth factor (IGF)-binding protein-3 can form a 150-kilodalton binary complex in vitro in the absence of IGFs. Endocrinology 136:4982-4989
    • (1995) Endocrinology , vol.136 , pp. 4982-4989
    • Lee, C.Y.1    Rechler, M.M.2
  • 15
    • 0026637765 scopus 로고
    • Structure and functional expression of the acid-labile subunit of the insulin-like growth factor-binding protein complex
    • Leong SR, Baxter RC, Camerato T, Dai J, Wood WI 1992 Structure and functional expression of the acid-labile subunit of the insulin-like growth factor-binding protein complex. Mol Endocrinol 6:870-876
    • (1992) Mol Endocrinol , vol.6 , pp. 870-876
    • Leong, S.R.1    Baxter, R.C.2    Camerato, T.3    Dai, J.4    Wood, W.I.5
  • 16
    • 0032513133 scopus 로고    scopus 로고
    • Insulin-like growth factor (IGF)-binding protein 5 forms an alternative ternary complex with IGFs and the acid-labile subunit
    • Twigg SM, Baxter RC 1998 Insulin-like growth factor (IGF)-binding protein 5 forms an alternative ternary complex with IGFs and the acid-labile subunit. J Biol Chem 273:6074-6079
    • (1998) J Biol Chem , vol.273 , pp. 6074-6079
    • Twigg, S.M.1    Baxter, R.C.2
  • 17
    • 0025608587 scopus 로고
    • Slit: An extracellular protein necessary for development of midline glia and commissural axon pathways contains both EGF and LRR domains
    • Rothberg JM, Jacobs JR, Goodman CS, Artavanis-Tsakonas S 1990 Slit: an extracellular protein necessary for development of midline glia and commissural axon pathways contains both EGF and LRR domains. Genes Dev 4:2169-2187
    • (1990) Genes Dev , vol.4 , pp. 2169-2187
    • Rothberg, J.M.1    Jacobs, J.R.2    Goodman, C.S.3    Artavanis-Tsakonas, S.4
  • 18
    • 0030437795 scopus 로고    scopus 로고
    • Structural and functional diversity in the leucine-rich repeat family of proteins
    • Buchanan SG, Gay NJ 1996 Structural and functional diversity in the leucine-rich repeat family of proteins. Prog Biophys Mol Biol 65:1-44
    • (1996) Prog Biophys Mol Biol , vol.65 , pp. 1-44
    • Buchanan, S.G.1    Gay, N.J.2
  • 20
    • 0029645408 scopus 로고
    • Modeling of the three-dimensional structure of proteins with the typical leucine-rich repeats
    • Kajava AV, Vassart G, Wodak SJ 1995 Modeling of the three-dimensional structure of proteins with the typical leucine-rich repeats. Structure 3:867-877
    • (1995) Structure , vol.3 , pp. 867-877
    • Kajava, A.V.1    Vassart, G.2    Wodak, S.J.3
  • 21
    • 0032478536 scopus 로고    scopus 로고
    • Structural diversity of leucine-rich repeat proteins
    • Kajava AV 1998 Structural diversity of leucine-rich repeat proteins. J Mol Biol 277:519-527
    • (1998) J Mol Biol , vol.277 , pp. 519-527
    • Kajava, A.V.1
  • 23
    • 0027533741 scopus 로고
    • Antagonism of catecholamine receptor signaling by expression of cytoplasmic domains of the receptors
    • Luttrell LM, Ostrowski J, Cotecchia S, Kendall H, Lefkowitz RJ 1993 Antagonism of catecholamine receptor signaling by expression of cytoplasmic domains of the receptors. Science 259:1453-1457
    • (1993) Science , vol.259 , pp. 1453-1457
    • Luttrell, L.M.1    Ostrowski, J.2    Cotecchia, S.3    Kendall, H.4    Lefkowitz, R.J.5
  • 24
    • 0029563626 scopus 로고
    • Identification of two amino acid residues on the extracellular domain of the lutropin/ choriogonadotropin receptor important in signaling
    • Huang J, Puett D 1995 Identification of two amino acid residues on the extracellular domain of the lutropin/ choriogonadotropin receptor important in signaling. J Biol Chem 270:30023-30028
    • (1995) J Biol Chem , vol.270 , pp. 30023-30028
    • Huang, J.1    Puett, D.2
  • 25
    • 0028909714 scopus 로고
    • Receptors and G proteins as primary components of transmembrane signal transduction. I. G-protein-coupled receptors: Structure and function
    • Gudermann T, Nurnberg B, Schultz G 1995 Receptors and G proteins as primary components of transmembrane signal transduction. I. G-protein-coupled receptors: structure and function. J Mol Med 73:51-63
    • (1995) J Mol Med , vol.73 , pp. 51-63
    • Gudermann, T.1    Nurnberg, B.2    Schultz, G.3
  • 26
    • 0031047328 scopus 로고    scopus 로고
    • Roles of transmembrane prolines and proline-induced kinks of the lutropin/choriogonadotropin receptor
    • Hong S, Ryu KS, Oh MS, Ji I, Ji TH 1997 Roles of transmembrane prolines and proline-induced kinks of the lutropin/choriogonadotropin receptor. J Biol Chem 272:4166-4171
    • (1997) J Biol Chem , vol.272 , pp. 4166-4171
    • Hong, S.1    Ryu, K.S.2    Oh, M.S.3    Ji, I.4    Ji, T.H.5
  • 27
    • 0030613761 scopus 로고    scopus 로고
    • Switching of the coupling of the beta2-adrenergic receptor to different G proteins by protein kinase A
    • Daaka Y, Luttrell LM, Lefkowitz RJ 1997 Switching of the coupling of the beta2-adrenergic receptor to different G proteins by protein kinase A. Nature 390:88-91
    • (1997) Nature , vol.390 , pp. 88-91
    • Daaka, Y.1    Luttrell, L.M.2    Lefkowitz, R.J.3
  • 28
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • Pawson T, Scott JD 1997 Signaling through scaffold, anchoring, and adaptor proteins. Science 278: 2075-2080
    • (1997) Science , vol.278 , pp. 2075-2080
    • Pawson, T.1    Scott, J.D.2
  • 29
    • 0029832901 scopus 로고    scopus 로고
    • Transmembrane regions V and VI of the human luteinizing hormone receptor are required for constitutive activation by a mutation in the third intracellular loop
    • Kudo M, Osuga Y, Kobilka BK, Hsueh AJW 1996 Transmembrane regions V and VI of the human luteinizing hormone receptor are required for constitutive activation by a mutation in the third intracellular loop. J Biol Chem 271:22470-22478
    • (1996) J Biol Chem , vol.271 , pp. 22470-22478
    • Kudo, M.1    Osuga, Y.2    Kobilka, B.K.3    Hsueh, A.J.W.4
  • 32
    • 0028825276 scopus 로고
    • Automated construction and graphical presentation of protein blocks from unaligned sequences
    • Henikoff S, Henikoff JG, Alford WJ, Pietrokovski S 1995 Automated construction and graphical presentation of protein blocks from unaligned sequences. Gene 163:GC17-GC26
    • (1995) Gene , vol.163
    • Henikoff, S.1    Henikoff, J.G.2    Alford, W.J.3    Pietrokovski, S.4
  • 33
    • 0032513016 scopus 로고    scopus 로고
    • Modulation of high affinity hormone binding. Human choriogonadotropin binding to the exodomain of the receptor is influenced by exoloop 2 of the receptor
    • Ryu K, Lee H, Kim S, Beauchamp J, Tung CS, Isaacs NW, Ji I, Ji TH 1998 Modulation of high affinity hormone binding. Human choriogonadotropin binding to the exodomain of the receptor is influenced by exoloop 2 of the receptor. J Biol Chem 273:6285-6291
    • (1998) J Biol Chem , vol.273 , pp. 6285-6291
    • Ryu, K.1    Lee, H.2    Kim, S.3    Beauchamp, J.4    Tung, C.S.5    Isaacs, N.W.6    Ji, I.7    Ji, T.H.8
  • 34
    • 0028286342 scopus 로고
    • Localization of the human FSH receptor to chromosome 2 p21 using a genomic probe comprising exon 10
    • Gromoll J, Ried T, Holtgreve-Grez H, Nieschlag E, Gudermann T 1994 Localization of the human FSH receptor to chromosome 2 p21 using a genomic probe comprising exon 10. J Mol Endocrinol 12:265-271
    • (1994) J Mol Endocrinol , vol.12 , pp. 265-271
    • Gromoll, J.1    Ried, T.2    Holtgreve-Grez, H.3    Nieschlag, E.4    Gudermann, T.5
  • 35
    • 0027718173 scopus 로고
    • Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats
    • Kobe B, Deisenhofer J 1993 Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats. Nature 366:751-756
    • (1993) Nature , vol.366 , pp. 751-756
    • Kobe, B.1    Deisenhofer, J.2
  • 36
    • 0030831210 scopus 로고    scopus 로고
    • A human homologue of the Drosophila Toll protein signals activation of adaptive immunity
    • Medzhitov R, Preston-Hurlburt P, Janeway Jr CA 1997 A human homologue of the Drosophila Toll protein signals activation of adaptive immunity. Nature 388:394-397
    • (1997) Nature , vol.388 , pp. 394-397
    • Medzhitov, R.1    Preston-Hurlburt, P.2    Janeway Jr., C.A.3
  • 37
    • 0030663332 scopus 로고    scopus 로고
    • The 18-wheeler mutation reveals complex antibacterial gene regulation in Drosophila host defense
    • Williams MJ, Rodriguez A, Kimbrell DA, Eldon ED 1997 The 18-wheeler mutation reveals complex antibacterial gene regulation in Drosophila host defense. EMBO J 16:6120-6130
    • (1997) EMBO J , vol.16 , pp. 6120-6130
    • Williams, M.J.1    Rodriguez, A.2    Kimbrell, D.A.3    Eldon, E.D.4
  • 38
    • 0029646089 scopus 로고
    • Structural predictions for the ligand-binding region of glycoprotein hormone receptors and the nature of hormone-receptor interactions
    • Jiang X, Dreano M, Buckler DR, Cheng S, Ythier A, Wu H, Hendrickson WA, el Tayar N 1995 Structural predictions for the ligand-binding region of glycoprotein hormone receptors and the nature of hormone-receptor interactions. Structure 3:1341-1353
    • (1995) Structure , vol.3 , pp. 1341-1353
    • Jiang, X.1    Dreano, M.2    Buckler, D.R.3    Cheng, S.4    Ythier, A.5    Wu, H.6    Hendrickson, W.A.7    El Tayar, N.8
  • 39
    • 0029093909 scopus 로고
    • Model of human chorionic gonadotropin and lutropin receptor interaction that explains signal transduction of the glycoprotein hormones
    • Moyle WR, Campbell RK, Rao SN, Ayad NG, Bernard MP, Han Y, Wang, Y 1995 Model of human chorionic gonadotropin and lutropin receptor interaction that explains signal transduction of the glycoprotein hormones. J Biol Chem 270:20020-20031
    • (1995) J Biol Chem , vol.270 , pp. 20020-20031
    • Moyle, W.R.1    Campbell, R.K.2    Rao, S.N.3    Ayad, N.G.4    Bernard, M.P.5    Han, Y.6    Wang, Y.7
  • 40
    • 0031442972 scopus 로고    scopus 로고
    • Insulin-like growth factor-binding proteins in serum and other biological fluids: Regulation and functions
    • Rajaram S, Baylink DJ, Mohan S 1997 Insulin-like growth factor-binding proteins in serum and other biological fluids: regulation and functions. Endocr Rev 18:801-831
    • (1997) Endocr Rev , vol.18 , pp. 801-831
    • Rajaram, S.1    Baylink, D.J.2    Mohan, S.3
  • 41
    • 0028600614 scopus 로고
    • Bone matrix decorin binds transforming growth factor-beta and enhances its bioactivity
    • Takeuchi Y, Kodama Y, Matsumoto T 1994 Bone matrix decorin binds transforming growth factor-beta and enhances its bioactivity. J Biol Chem 269:32634-32638
    • (1994) J Biol Chem , vol.269 , pp. 32634-32638
    • Takeuchi, Y.1    Kodama, Y.2    Matsumoto, T.3
  • 42
    • 0028167111 scopus 로고
    • Signaling pathways that establish the dorsal-ventral pattern of the Drosophila embryo
    • Morisato D, Anderson KV 1994 Signaling pathways that establish the dorsal-ventral pattern of the Drosophila embryo. Cell 76:677-688
    • (1994) Cell , vol.76 , pp. 677-688
    • Morisato, D.1    Anderson, K.V.2
  • 43
    • 0030843296 scopus 로고    scopus 로고
    • Localization of a binding site for the proteoglycan decorin on collagen XIV (undulin)
    • Ehnis T, Dieterich W, Bauer M, Kresse H, Schuppan D 1997 Localization of a binding site for the proteoglycan decorin on collagen XIV (undulin). J Biol Chem 272:20414-20419
    • (1997) J Biol Chem , vol.272 , pp. 20414-20419
    • Ehnis, T.1    Dieterich, W.2    Bauer, M.3    Kresse, H.4    Schuppan, D.5
  • 44
    • 0028973403 scopus 로고
    • Similarities between trunk and spatzle, putative extracellular ligands specifying body pattern in Drosophila
    • Casanova J, Furriols M, McCormick CA, Struhl G 1995 Similarities between trunk and spatzle, putative extracellular ligands specifying body pattern in Drosophila. Genes Dev 9:2539-2544
    • (1995) Genes Dev , vol.9 , pp. 2539-2544
    • Casanova, J.1    Furriols, M.2    McCormick, C.A.3    Struhl, G.4
  • 46
    • 1842376911 scopus 로고    scopus 로고
    • Men homozygous for an inactivating mutation of the follicle-stimulating hormone (FSH) receptor gene present variable suppression of spermatogenesis and fertility
    • Tapanainen JS, Aittomaki K, Min J, Vaskivuo T, Huhtaniemi IT 1997 Men homozygous for an inactivating mutation of the follicle-stimulating hormone (FSH) receptor gene present variable suppression of spermatogenesis and fertility. Nat Genet 15:205-206
    • (1997) Nat Genet , vol.15 , pp. 205-206
    • Tapanainen, J.S.1    Aittomaki, K.2    Min, J.3    Vaskivuo, T.4    Huhtaniemi, I.T.5
  • 48
    • 0030868842 scopus 로고    scopus 로고
    • Co-expression of defective luteinizing hormone receptor fragments partially reconstitutes ligand-induced signal generation
    • Osuga Y, Hayashi M, Kudo M, Conti M, Kobilka B, Hsueh AJW 1997 Co-expression of defective luteinizing hormone receptor fragments partially reconstitutes ligand-induced signal generation. J Biol Chem 272: 25006-25012
    • (1997) J Biol Chem , vol.272 , pp. 25006-25012
    • Osuga, Y.1    Hayashi, M.2    Kudo, M.3    Conti, M.4    Kobilka, B.5    Hsueh, A.J.W.6
  • 49
    • 0027506471 scopus 로고
    • The probable arrangement of the helices in G protein-coupled receptors
    • Baldwin JM 1993 The probable arrangement of the helices in G protein-coupled receptors. EMBO J 12:1693-1703
    • (1993) EMBO J , vol.12 , pp. 1693-1703
    • Baldwin, J.M.1
  • 50
    • 0027440025 scopus 로고
    • Three-dimensional models of gonado-thyrotropin hormone receptor transmembrane domain
    • Hoflack J, Hibert MF, Trumpp-Kallmeyer S, Bidart JM 1993 Three-dimensional models of gonado-thyrotropin hormone receptor transmembrane domain. Drug Des Discov 10:157-171
    • (1993) Drug des Discov , vol.10 , pp. 157-171
    • Hoflack, J.1    Hibert, M.F.2    Trumpp-Kallmeyer, S.3    Bidart, J.M.4
  • 51
    • 0030912536 scopus 로고    scopus 로고
    • A model of the lutropin/choriogonadotropin receptor: Insights into the structural and functional effects of constitutively activating mutations
    • Lin Z, Shenker A, Pearlstein R 1997 A model of the lutropin/choriogonadotropin receptor: insights into the structural and functional effects of constitutively activating mutations. Protein Eng 10:501-510
    • (1997) Protein Eng , vol.10 , pp. 501-510
    • Lin, Z.1    Shenker, A.2    Pearlstein, R.3
  • 52
    • 0032543410 scopus 로고    scopus 로고
    • Identification and cloning of an orphan G protein-coupled receptor of the glycoprotein hormone receptor subfamily
    • McDonald T, Wang R, Bailey W, Xie G, Chen F, Caskey CT, Liu Q 1998 Identification and cloning of an orphan G protein-coupled receptor of the glycoprotein hormone receptor subfamily. Biochem Biophys Res Commun 247:266-270
    • (1998) Biochem Biophys Res Commun , vol.247 , pp. 266-270
    • McDonald, T.1    Wang, R.2    Bailey, W.3    Xie, G.4    Chen, F.5    Caskey, C.T.6    Liu, Q.7
  • 53
    • 0009603660 scopus 로고
    • An arginine residue conserved in most G protein-coupled receptors is essential for the function of the ml muscarinic receptor
    • Zhu SZ, Wang SZ, Hu J, el-Fakahany EE 1994 An arginine residue conserved in most G protein-coupled receptors is essential for the function of the ml muscarinic receptor. Mol Pharmacol 45:517-523
    • (1994) Mol Pharmacol , vol.45 , pp. 517-523
    • Zhu, S.Z.1    Wang, S.Z.2    Hu, J.3    El-Fakahany, E.E.4
  • 55
    • 0025848033 scopus 로고
    • Structural organization of the rat luteinizing hormone (LH) receptor gene
    • Tsai-Morris CH, Buczko E, Wang W, Xie XZ, Dufau ML 1991 Structural organization of the rat luteinizing hormone (LH) receptor gene. J Biol Chem 266:11355-11359
    • (1991) J Biol Chem , vol.266 , pp. 11355-11359
    • Tsai-Morris, C.H.1    Buczko, E.2    Wang, W.3    Xie, X.Z.4    Dufau, M.L.5
  • 56
    • 0030852475 scopus 로고    scopus 로고
    • Derivation of functional antagonists using N-terminal extracellular domain of gonadotropin and thyrotropin receptors
    • Osuga Y, Kudo M, Kaipia A, Kobilka B, Hsueh AJW 1997 Derivation of functional antagonists using N-terminal extracellular domain of gonadotropin and thyrotropin receptors. Mol Endocrinol 11:1659-1668
    • (1997) Mol Endocrinol , vol.11 , pp. 1659-1668
    • Osuga, Y.1    Kudo, M.2    Kaipia, A.3    Kobilka, B.4    Hsueh, A.J.W.5
  • 58
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ, Thompson JD, Higgins DG, Gibson TJ 1994 CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22:4673-4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3    Thompson, J.D.4    Higgins, D.G.5    Gibson, T.J.6
  • 60
    • 0029902780 scopus 로고    scopus 로고
    • Bridging the protein sequence-structure gap by structure predictions
    • Rost B, Sander C 1996 Bridging the protein sequence-structure gap by structure predictions. Annu Rev Biophys Biomol Struct 25:113-136
    • (1996) Annu Rev Biophys Biomol Struct , vol.25 , pp. 113-136
    • Rost, B.1    Sander, C.2
  • 61
    • 0029804192 scopus 로고    scopus 로고
    • Identification and application of the concepts important for accurate and reliable protein secondary structure prediction
    • King RD, Sternberg MJ 1996 Identification and application of the concepts important for accurate and reliable protein secondary structure prediction. Protein Sci 5:2298-2310
    • (1996) Protein Sci , vol.5 , pp. 2298-2310
    • King, R.D.1    Sternberg, M.J.2
  • 64
    • 0026042543 scopus 로고
    • Expression of human luteinizing hormone (LH) receptor: Interaction with LH and chorionic gonadotropin from human but not equine, rat, and ovine species
    • Jia XC, Oikawa M, Bo M, Tanaka T, Ny T, Boime I, Hsueh AJW 1991 Expression of human luteinizing hormone (LH) receptor: interaction with LH and chorionic gonadotropin from human but not equine, rat, and ovine species. Mol Endocrinol 5:759-768
    • (1991) Mol Endocrinol , vol.5 , pp. 759-768
    • Jia, X.C.1    Oikawa, M.2    Bo, M.3    Tanaka, T.4    Ny, T.5    Boime, I.6    Hsueh, A.J.W.7


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