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Volumn 8, Issue 1, 2008, Pages

The repertoire of G protein-coupled receptors in the sea squirt Ciona intestinalis

Author keywords

[No Author keywords available]

Indexed keywords

CELL ADHESION MOLECULE; FRIZZLED PROTEIN; G PROTEIN COUPLED RECEPTOR; GENE PRODUCT; GLUTAMIC ACID; RHODOPSIN; SECRETIN; PROTEOME;

EID: 44349180840     PISSN: None     EISSN: 14712148     Source Type: Journal    
DOI: 10.1186/1471-2148-8-129     Document Type: Article
Times cited : (85)

References (112)
  • 1
    • 0038153935 scopus 로고    scopus 로고
    • The first tunicate from the Early Cambrian of South China
    • 12835415. 10.1073/pnas.1431177100
    • The first tunicate from the Early Cambrian of South China. JY Chen DY Huang QQ Peng HM Chi XQ Wang M Feng, Proc Natl Acad Sci USA 2003 100 8314 8318 12835415 10.1073/pnas.1431177100
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 8314-8318
    • Chen, J.Y.1    Huang, D.Y.2    Peng, Q.Q.3    Chi, H.M.4    Wang, X.Q.5    Feng, M.6
  • 2
    • 33644536713 scopus 로고    scopus 로고
    • Tunicates and not cephalochordates are the closest living relatives of vertebrates
    • 10.1038/nature04336. 16495997
    • Tunicates and not cephalochordates are the closest living relatives of vertebrates. F Delsuc H Brinkmann D Chourrout H Philippe, Nature 2006 439 965 968 10.1038/nature04336 16495997
    • (2006) Nature , vol.439 , pp. 965-968
    • Delsuc, F.1    Brinkmann, H.2    Chourrout, D.3    Philippe, H.4
  • 3
    • 17444397689 scopus 로고    scopus 로고
    • Ciona intestinalis: Chordate development made simple
    • 10.1002/dvdy.20300. 15765512
    • Ciona intestinalis: chordate development made simple. YJ Passamaneck A Di Gregorio, Dev Dyn 2005 233 1 19 10.1002/dvdy.20300 15765512
    • (2005) Dev Dyn , vol.233 , pp. 1-19
    • Passamaneck, Y.J.1    Di Gregorio, A.2
  • 5
    • 0038024615 scopus 로고    scopus 로고
    • The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints
    • 10.1124/mol.63.6.1256. 12761335
    • The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints. R Fredriksson MC Lagerstrom LG Lundin HB Schioth, Mol Pharmacol 2003 63 1256 1272 10.1124/mol.63.6.1256 12761335
    • (2003) Mol Pharmacol , vol.63 , pp. 1256-1272
    • Fredriksson, R.1    Lagerstrom, M.C.2    Lundin, L.G.3    Schioth, H.B.4
  • 6
    • 23944456921 scopus 로고    scopus 로고
    • Genome wide survey of G protein-coupled receptors in Tetraodon nigroviridis
    • 16022726. 10.1186/1471-2148-5-41
    • Genome wide survey of G protein-coupled receptors in Tetraodon nigroviridis. RP Metpally R Sowdhamini, BMC Evol Biol 2005 5 41 16022726 10.1186/1471-2148-5-41
    • (2005) BMC Evol Biol , vol.5 , pp. 41
    • Metpally, R.P.1    Sowdhamini, R.2
  • 9
    • 36949011636 scopus 로고    scopus 로고
    • The G protein-coupled receptor subset of the rat genome
    • 17892602. 10.1186/1471-2164-8-338
    • The G protein-coupled receptor subset of the rat genome. DE Gloriam R Fredriksson HB Schioth, BMC Genomics 2007 8 338 17892602 10.1186/1471-2164-8-338
    • (2007) BMC Genomics , vol.8 , pp. 338
    • Gloriam, D.E.1    Fredriksson, R.2    Schioth, H.B.3
  • 10
    • 33747754105 scopus 로고    scopus 로고
    • Comprehensive repertoire and phylogenetic analysis of the G protein-coupled receptors in human and mouse
    • 10.1016/j.ygeno.2006.04.001. 16753280
    • Comprehensive repertoire and phylogenetic analysis of the G protein-coupled receptors in human and mouse. TK Bjarnadottir DE Gloriam SH Hellstrand H Kristiansson R Fredriksson HB Schioth, Genomics 2006 88 263 273 10.1016/j.ygeno.2006.04.001 16753280
    • (2006) Genomics , vol.88 , pp. 263-273
    • Bjarnadottir, T.K.1    Gloriam, D.E.2    Hellstrand, S.H.3    Kristiansson, H.4    Fredriksson, R.5    Schioth, H.B.6
  • 11
    • 25444440081 scopus 로고    scopus 로고
    • Cross genome phylogenetic analysis of human and Drosophila G protein-coupled receptors: Application to functional annotation of orphan receptors
    • 16091152. 10.1186/1471-2164-6-106
    • Cross genome phylogenetic analysis of human and Drosophila G protein-coupled receptors: application to functional annotation of orphan receptors. RP Metpally R Sowdhamini, BMC Genomics 2005 6 106 16091152 10.1186/1471-2164-6-106
    • (2005) BMC Genomics , vol.6 , pp. 106
    • Metpally, R.P.1    Sowdhamini, R.2
  • 12
    • 39549117195 scopus 로고    scopus 로고
    • The Branchiostoma genome contains a highly diversified set of G protein-coupled receptors
    • 18199322. 10.1186/1471-2148-8-9
    • The Branchiostoma genome contains a highly diversified set of G protein-coupled receptors. K Nordstrom R Fredriksson H Schioth, BMC Evol Biol 2008 8 1 9 18199322 10.1186/1471-2148-8-9
    • (2008) BMC Evol Biol , vol.8 , Issue.1 , pp. 9
    • Nordstrom, K.1    Fredriksson, R.2    Schioth, H.3
  • 13
    • 17844400914 scopus 로고    scopus 로고
    • The repertoire of G-protein-coupled receptors in fully sequenced genomes
    • 10.1124/mol.104.009001. 15687224
    • The repertoire of G-protein-coupled receptors in fully sequenced genomes. R Fredriksson HB Schioth, Mol Pharmacol 2005 67 1414 1425 10.1124/mol.104. 009001 15687224
    • (2005) Mol Pharmacol , vol.67 , pp. 1414-1425
    • Fredriksson, R.1    Schioth, H.B.2
  • 14
    • 34147167613 scopus 로고    scopus 로고
    • Mining the gene repertoire and ESTs for G protein-coupled receptors with evolutionary perspective
    • 17428229
    • Mining the gene repertoire and ESTs for G protein-coupled receptors with evolutionary perspective. HB Schioth KJ Nordstrom R Fredriksson, Acta Physiol (Oxf) 2007 190 21 31 17428229
    • (2007) Acta Physiol (Oxf) , vol.190 , pp. 21-31
    • Schioth, H.B.1    Nordstrom, K.J.2    Fredriksson, R.3
  • 16
    • 0029913807 scopus 로고    scopus 로고
    • An evolutionary trace method defines binding surfaces common to protein families
    • 10.1006/jmbi.1996.0167. 8609628
    • An evolutionary trace method defines binding surfaces common to protein families. O Lichtarge HR Bourne FE Cohen, J Mol Biol 1996 257 342 358 10.1006/jmbi.1996.0167 8609628
    • (1996) J Mol Biol , vol.257 , pp. 342-358
    • Lichtarge, O.1    Bourne, H.R.2    Cohen, F.E.3
  • 17
    • 0032735188 scopus 로고    scopus 로고
    • Modelling G-protein-coupled receptors for drug design
    • 10548717
    • Modelling G-protein-coupled receptors for drug design. DR Flower, Biochim Biophys Acta 1999 1422 207 234 10548717
    • (1999) Biochim Biophys Acta , vol.1422 , pp. 207-234
    • Flower, D.R.1
  • 18
    • 0034677966 scopus 로고    scopus 로고
    • Drug discovery: A historical perspective
    • 10.1126/science.287.5460.1960. 10720314
    • Drug discovery: a historical perspective. J Drews, Science 2000 287 1960 1964 10.1126/science.287.5460.1960 10720314
    • (2000) Science , vol.287 , pp. 1960-1964
    • Drews, J.1
  • 19
    • 33748671369 scopus 로고    scopus 로고
    • The 7 TM G-protein-coupled receptor target family
    • 10.1002/cmdc.200600134. 16902930
    • The 7 TM G-protein-coupled receptor target family. E Jacoby R Bouhelal M Gerspacher K Seuwen, ChemMedChem 2006 1 761 782 10.1002/cmdc.200600134 16902930
    • (2006) ChemMedChem , vol.1 , pp. 761-782
    • Jacoby, E.1    Bouhelal, R.2    Gerspacher, M.3    Seuwen, K.4
  • 23
    • 0028362192 scopus 로고
    • A G protein-coupled receptor with low density lipoprotein-binding motifs suggests a role for lipoproteins in G-linked signal transduction
    • 8197140. 10.1073/pnas.91.11.4816
    • A G protein-coupled receptor with low density lipoprotein-binding motifs suggests a role for lipoproteins in G-linked signal transduction. CP Tensen ER Van Kesteren RJ Planta KJ Cox JF Burke H van Heerikhuizen E Vreugdenhil, Proc Natl Acad Sci USA 1994 91 4816 4820 8197140 10.1073/pnas.91.11.4816
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 4816-4820
    • Tensen, C.P.1    Van Kesteren, E.R.2    Planta, R.J.3    Cox, K.J.4    Burke, J.F.5    Van Heerikhuizen, H.6    Vreugdenhil, E.7
  • 24
    • 17744381347 scopus 로고    scopus 로고
    • Glutamate receptor subtypes: Promising new pharmacotherapeutic targets
    • 10.1007/s00213-005-2246-y. 15761696
    • Glutamate receptor subtypes: promising new pharmacotherapeutic targets. GA Higgins KA Miczek, Psychopharmacology (Berl) 2005 179 1 3 10.1007/s00213-005-2246-y 15761696
    • (2005) Psychopharmacology (Berl) , vol.179 , pp. 1-3
    • Higgins, G.A.1    Miczek, K.A.2
  • 25
    • 33846634186 scopus 로고    scopus 로고
    • Evolution of Secretin family GPCR members in the metazoa
    • 17166275. 10.1186/1471-2148-6-108
    • Evolution of Secretin family GPCR members in the metazoa. JC Cardoso VC Pinto FA Vieira MS Clark DM Power, BMC Evol Biol 2006 6 108 17166275 10.1186/1471-2148-6-108
    • (2006) BMC Evol Biol , vol.6 , pp. 108
    • Cardoso, J.C.1    Pinto, V.C.2    Vieira, F.A.3    Clark, M.S.4    Power, D.M.5
  • 26
    • 4844230621 scopus 로고    scopus 로고
    • The Frizzled family: Receptors for multiple signal transduction pathways
    • 15239825. 10.1186/gb-2004-5-7-234
    • The Frizzled family: receptors for multiple signal transduction pathways. HC Huang PS Klein, Genome Biol 2004 5 234 15239825 10.1186/gb-2004-5-7-234
    • (2004) Genome Biol , vol.5 , pp. 234
    • Huang, H.C.1    Klein, P.S.2
  • 27
    • 0024972122 scopus 로고
    • A Drosophila tissue polarity locus encodes a protein containing seven potential transmembrane domains
    • 10.1038/338263a0. 2493583
    • A Drosophila tissue polarity locus encodes a protein containing seven potential transmembrane domains. CR Vinson S Conover PN Adler, Nature 1989 338 263 264 10.1038/338263a0 2493583
    • (1989) Nature , vol.338 , pp. 263-264
    • Vinson, C.R.1    Conover, S.2    Adler, P.N.3
  • 28
    • 0034665045 scopus 로고    scopus 로고
    • The C-terminal cytoplasmic Lys-thr-X-X-X-Trp motif in Frizzled receptors mediates Wnt/beta-catenin signalling
    • 10990458. 10.1093/emboj/19.18.4944
    • The C-terminal cytoplasmic Lys-thr-X-X-X-Trp motif in Frizzled receptors mediates Wnt/beta-catenin signalling. M Umbhauer A Djiane C Goisset A Penzo-Mendez JF Riou JC Boucaut DL Shi, EMBO J 2000 19 4944 4954 10990458 10.1093/emboj/19.18.4944
    • (2000) EMBO J , vol.19 , pp. 4944-4954
    • Umbhauer, M.1    Djiane, A.2    Goisset, C.3    Penzo-Mendez, A.4    Riou, J.F.5    Boucaut, J.C.6    Shi, D.L.7
  • 29
    • 2942590647 scopus 로고    scopus 로고
    • The human and mouse repertoire of the Adhesion family of G-protein-coupled receptors
    • 10.1016/j.ygeno.2003.12.004. 15203201
    • The human and mouse repertoire of the Adhesion family of G-protein-coupled receptors. TK Bjarnadottir R Fredriksson PJ Hoglund DE Gloriam MC Lagerstrom HB Schioth, Genomics 2004 84 23 33 10.1016/j.ygeno.2003.12.004 15203201
    • (2004) Genomics , vol.84 , pp. 23-33
    • Bjarnadottir, T.K.1    Fredriksson, R.2    Hoglund, P.J.3    Gloriam, D.E.4    Lagerstrom, M.C.5    Schioth, H.B.6
  • 30
    • 0024290095 scopus 로고
    • A chemoattractant receptor controls development in Dictyostelium discoideum
    • 10.1126/science.3047871. 3047871
    • A chemoattractant receptor controls development in Dictyostelium discoideum. PS Klein TJ Sun CL Saxe 3rd AR Kimmel RL Johnson PN Devreotes, Science 1988 241 1467 1472 10.1126/science.3047871 3047871
    • (1988) Science , vol.241 , pp. 1467-1472
    • Klein, P.S.1    Sun, T.J.2    Saxe III, C.L.3    Kimmel, A.R.4    Johnson, R.L.5    Devreotes, P.N.6
  • 31
    • 0027510551 scopus 로고
    • CAR2, a prestalk cAMP receptor required for normal tip formation and late development of Dictyostelium discoideum
    • 10.1101/gad.7.2.262. 8436297
    • CAR2, a prestalk cAMP receptor required for normal tip formation and late development of Dictyostelium discoideum. CL Saxe 3rd GT Ginsburg JM Louis R Johnson PN Devreotes AR Kimmel, Genes Dev 1993 7 262 272 10.1101/gad.7.2.262 8436297
    • (1993) Genes Dev , vol.7 , pp. 262-272
    • Saxe III, C.L.1    Ginsburg, G.T.2    Louis, J.M.3    Johnson, R.4    Devreotes, P.N.5    Kimmel, A.R.6
  • 32
    • 0027405826 scopus 로고
    • Identification and targeted gene disruption of cAR3, a cAMP receptor subtype expressed during multicellular stages of Dictyostelium development
    • 10.1101/gad.7.2.273. 8382181
    • Identification and targeted gene disruption of cAR3, a cAMP receptor subtype expressed during multicellular stages of Dictyostelium development. RL Johnson CL Saxe 3rd R Gollop AR Kimmel PN Devreotes, Genes Dev 1993 7 273 282 10.1101/gad.7.2.273 8382181
    • (1993) Genes Dev , vol.7 , pp. 273-282
    • Johnson, R.L.1    Saxe III, C.L.2    Gollop, R.3    Kimmel, A.R.4    Devreotes, P.N.5
  • 33
    • 0346022965 scopus 로고    scopus 로고
    • A cAMP receptor-like G protein-coupled receptor with roles in growth regulation and development
    • 10.1016/j.ydbio.2003.09.035. 14732403
    • A cAMP receptor-like G protein-coupled receptor with roles in growth regulation and development. B Raisley M Zhang D Hereld JA Hadwiger, Dev Biol 2004 265 433 445 10.1016/j.ydbio.2003.09.035 14732403
    • (2004) Dev Biol , vol.265 , pp. 433-445
    • Raisley, B.1    Zhang, M.2    Hereld, D.3    Hadwiger, J.A.4
  • 34
    • 0032582489 scopus 로고    scopus 로고
    • Extended life-span and stress resistance in the Drosophila mutant methuselah
    • 10.1126/science.282.5390.943. 9794765
    • Extended life-span and stress resistance in the Drosophila mutant methuselah. YJ Lin L Seroude S Benzer, Science 1998 282 943 946 10.1126/science.282.5390.943 9794765
    • (1998) Science , vol.282 , pp. 943-946
    • Lin, Y.J.1    Seroude, L.2    Benzer, S.3
  • 35
    • 29644433719 scopus 로고    scopus 로고
    • Defining the origins and evolution of the chemokine/chemokine receptor system
    • 16365434
    • Defining the origins and evolution of the chemokine/chemokine receptor system. ME DeVries AA Kelvin L Xu L Ran J Robinson DJ Kelvin, J Immunol 2006 176 401 415 16365434
    • (2006) J Immunol , vol.176 , pp. 401-415
    • Devries, M.E.1    Kelvin, A.A.2    Xu, L.3    Ran, L.4    Robinson, J.5    Kelvin, D.J.6
  • 36
    • 0032823306 scopus 로고    scopus 로고
    • Prostanoid receptors: Structures, properties, and functions
    • 10508233
    • Prostanoid receptors: structures, properties, and functions. S Narumiya Y Sugimoto F Ushikubi, Physiol Rev 1999 79 1193 1226 10508233
    • (1999) Physiol Rev , vol.79 , pp. 1193-1226
    • Narumiya, S.1    Sugimoto, Y.2    Ushikubi, F.3
  • 37
    • 19944407537 scopus 로고    scopus 로고
    • Tachykinin and tachykinin receptor of an ascidian, Ciona intestinalis: Evolutionary origin of the vertebrate tachykinin family
    • 10.1074/jbc.M408161200. 15485888
    • Tachykinin and tachykinin receptor of an ascidian, Ciona intestinalis: evolutionary origin of the vertebrate tachykinin family. H Satake M Ogasawara T Kawada K Masuda M Aoyama H Minakata T Chiba H Metoki Y Satou N Satoh, J Biol Chem 2004 279 53798 53805 10.1074/jbc.M408161200 15485888
    • (2004) J Biol Chem , vol.279 , pp. 53798-53805
    • Satake, H.1    Ogasawara, M.2    Kawada, T.3    Masuda, K.4    Aoyama, M.5    Minakata, H.6    Chiba, T.7    Metoki, H.8    Satou, Y.9    Satoh, N.10
  • 38
    • 23844511239 scopus 로고    scopus 로고
    • Tunicate gonadotropin-releasing hormone (GnRH) peptides selectively activate Ciona intestinalis GnRH receptors and the green monkey type II GnRH receptor
    • 10.1210/en.2004-1558. 15961566
    • Tunicate gonadotropin-releasing hormone (GnRH) peptides selectively activate Ciona intestinalis GnRH receptors and the green monkey type II GnRH receptor. JA Tello JE Rivier NM Sherwood, Endocrinology 2005 146 4061 4073 10.1210/en.2004-1558 15961566
    • (2005) Endocrinology , vol.146 , pp. 4061-4073
    • Tello, J.A.1    Rivier, J.E.2    Sherwood, N.M.3
  • 41
    • 33746820446 scopus 로고    scopus 로고
    • Sphingosine-1-phosphate: An emerging therapeutic target
    • 10.1517/14728222.5.1.109. 15992170
    • Sphingosine-1-phosphate: an emerging therapeutic target. RE Toman S Milstien S Spiegel, Expert Opin Ther Targets 2001 5 109 123 10.1517/14728222.5. 1.109 15992170
    • (2001) Expert Opin Ther Targets , vol.5 , pp. 109-123
    • Toman, R.E.1    Milstien, S.2    Spiegel, S.3
  • 43
    • 0018263844 scopus 로고
    • Why genes in pieces?
    • 10.1038/271501a0. 622185
    • Why genes in pieces? W Gilbert, Nature 1978 271 501 10.1038/271501a0 622185
    • (1978) Nature , vol.271 , pp. 501
    • Gilbert, W.1
  • 44
    • 0021801342 scopus 로고
    • Genes-in-pieces revisited
    • 10.1126/science.4001923. 4001923
    • Genes-in-pieces revisited. W Gilbert, Science 1985 228 823 824 10.1126/science.4001923 4001923
    • (1985) Science , vol.228 , pp. 823-824
    • Gilbert, W.1
  • 45
    • 18044378198 scopus 로고    scopus 로고
    • Multiple binding sites revealed by interaction of relaxin family peptides with native and chimeric relaxin family peptide receptors 1 and 2 (LGR7 and LGR8)
    • 10.1124/jpet.104.080655. 15649866
    • Multiple binding sites revealed by interaction of relaxin family peptides with native and chimeric relaxin family peptide receptors 1 and 2 (LGR7 and LGR8). ML Halls CP Bond S Sudo J Kumagai T Ferraro S Layfield RA Bathgate RJ Summers, J Pharmacol Exp Ther 2005 313 677 687 10.1124/jpet.104.080655 15649866
    • (2005) J Pharmacol Exp Ther , vol.313 , pp. 677-687
    • Halls, M.L.1    Bond, C.P.2    Sudo, S.3    Kumagai, J.4    Ferraro, T.5    Layfield, S.6    Bathgate, R.A.7    Summers, R.J.8
  • 46
    • 33845933437 scopus 로고    scopus 로고
    • Characterization of novel splice variants of LGR7 and LGR8 reveals that receptor signaling is mediated by their unique low density lipoprotein class a modules
    • 10.1074/jbc.M602728200. 16963451
    • Characterization of novel splice variants of LGR7 and LGR8 reveals that receptor signaling is mediated by their unique low density lipoprotein class A modules. DJ Scott S Layfield Y Yan S Sudo AJ Hsueh GW Tregear RA Bathgate, J Biol Chem 2006 281 34942 34954 10.1074/jbc.M602728200 16963451
    • (2006) J Biol Chem , vol.281 , pp. 34942-34954
    • Scott, D.J.1    Layfield, S.2    Yan, Y.3    Sudo, S.4    Hsueh, A.J.5    Tregear, G.W.6    Bathgate, R.A.7
  • 47
    • 0027718173 scopus 로고
    • Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats
    • 10.1038/366751a0. 8264799
    • Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats. B Kobe J Deisenhofer, Nature 1993 366 751 756 10.1038/366751a0 8264799
    • (1993) Nature , vol.366 , pp. 751-756
    • Kobe, B.1    Deisenhofer, J.2
  • 48
    • 0023750089 scopus 로고
    • Mutational analysis of the ligand binding domain of the low density lipoprotein receptor
    • 3417658
    • Mutational analysis of the ligand binding domain of the low density lipoprotein receptor. V Esser LE Limbird MS Brown JL Goldstein DW Russell, J Biol Chem 1988 263 13282 13290 3417658
    • (1988) J Biol Chem , vol.263 , pp. 13282-13290
    • Esser, V.1    Limbird, L.E.2    Brown, M.S.3    Goldstein, J.L.4    Russell, D.W.5
  • 49
    • 0024806811 scopus 로고
    • Different combinations of cysteine-rich repeats mediate binding of low density lipoprotein receptor to two different proteins
    • 2600087
    • Different combinations of cysteine-rich repeats mediate binding of low density lipoprotein receptor to two different proteins. DW Russell MS Brown JL Goldstein, J Biol Chem 1989 264 21682 21688 2600087
    • (1989) J Biol Chem , vol.264 , pp. 21682-21688
    • Russell, D.W.1    Brown, M.S.2    Goldstein, J.L.3
  • 50
    • 0022259920 scopus 로고
    • The LDL receptor gene: A mosaic of exons shared with different proteins
    • 10.1126/science.2988123. 2988123
    • The LDL receptor gene: a mosaic of exons shared with different proteins. TC Sudhof JL Goldstein MS Brown DW Russell, Science 1985 228 815 822 10.1126/science.2988123 2988123
    • (1985) Science , vol.228 , pp. 815-822
    • Sudhof, T.C.1    Goldstein, J.L.2    Brown, M.S.3    Russell, D.W.4
  • 51
    • 0021742599 scopus 로고
    • The human LDL receptor: A cysteine-rich protein with multiple Alu sequences in its mRNA
    • 10.1016/0092-8674(84)90188-0. 6091915
    • The human LDL receptor: a cysteine-rich protein with multiple Alu sequences in its mRNA. T Yamamoto CG Davis MS Brown WJ Schneider ML Casey JL Goldstein DW Russell, Cell 1984 39 27 38 10.1016/0092-8674(84)90188-0 6091915
    • (1984) Cell , vol.39 , pp. 27-38
    • Yamamoto, T.1    Davis, C.G.2    Brown, M.S.3    Schneider, W.J.4    Casey, M.L.5    Goldstein, J.L.6    Russell, D.W.7
  • 52
    • 0001665337 scopus 로고
    • Surface location and high affinity for calcium of a 500-kd liver membrane protein closely related to the LDL-receptor suggest a physiological role as lipoprotein receptor
    • 3266596
    • Surface location and high affinity for calcium of a 500-kd liver membrane protein closely related to the LDL-receptor suggest a physiological role as lipoprotein receptor. J Herz U Hamann S Rogne O Myklebost H Gausepohl KK Stanley, EMBO J 1988 7 4119 4127 3266596
    • (1988) EMBO J , vol.7 , pp. 4119-4127
    • Herz, J.1    Hamann, U.2    Rogne, S.3    Myklebost, O.4    Gausepohl, H.5    Stanley, K.K.6
  • 53
    • 0001353920 scopus 로고
    • Purified alpha 2-macroglobulin receptor/LDL receptor-related protein binds urokinase.plasminogen activator inhibitor type-1 complex. Evidence that the alpha 2-macroglobulin receptor mediates cellular degradation of urokinase receptor-bound complexes
    • 1378833
    • Purified alpha 2-macroglobulin receptor/LDL receptor-related protein binds urokinase.plasminogen activator inhibitor type-1 complex. Evidence that the alpha 2-macroglobulin receptor mediates cellular degradation of urokinase receptor-bound complexes. A Nykjaer CM Petersen B Moller PH Jensen SK Moestrup TL Holtet M Etzerodt HC Thogersen M Munch PA Andreasen J Gliemann, J Biol Chem 1992 267 14543 14546 1378833
    • (1992) J Biol Chem , vol.267 , pp. 14543-14546
    • Nykjaer, A.1    Petersen, C.M.2    Moller, B.3    Jensen, P.H.4    Moestrup, S.K.5    Holtet, T.L.6    Etzerodt, M.7    Thogersen, H.C.8    Munch, M.9    Andreasen, P.A.10    Gliemann, J.11
  • 54
    • 0027229924 scopus 로고
    • Correction: LDL receptor-related protein internalizes and degrades uPA-PAI-1 complexes and is essential for embryo implantation
    • 10.1016/0092-8674(93)90130-I. 8490961
    • Correction: LDL receptor-related protein internalizes and degrades uPA-PAI-1 complexes and is essential for embryo implantation. J Herz DE Couthier RE Hammer, Cell 1993 73 428 10.1016/0092-8674(93)90130-I 8490961
    • (1993) Cell , vol.73 , pp. 428
    • Herz, J.1    Couthier, D.E.2    Hammer, R.E.3
  • 55
    • 0025264752 scopus 로고
    • Low-density lipoprotein elevates intracellular calcium and pH in vascular smooth muscle cells and fibroblasts without mediation of LDL receptor
    • 10.1016/0006-291X(90)91772-K. 2310398
    • Low-density lipoprotein elevates intracellular calcium and pH in vascular smooth muscle cells and fibroblasts without mediation of LDL receptor. A Sachinidis R Locher T Mengden W Vetter, Biochem Biophys Res Commun 1990 167 353 359 10.1016/0006-291X(90)91772-K 2310398
    • (1990) Biochem Biophys Res Commun , vol.167 , pp. 353-359
    • Sachinidis, A.1    Locher, R.2    Mengden, T.3    Vetter, W.4
  • 57
    • 0023783475 scopus 로고
    • High density lipoproteins stimulate placental lactogen release and adenosine 3',5'-monophosphate (cAMP) production in human trophoblast cells: Evidence for cAMP as a second messenger in human placental lactogen release
    • 2843350
    • High density lipoproteins stimulate placental lactogen release and adenosine 3',5'-monophosphate (cAMP) production in human trophoblast cells: evidence for cAMP as a second messenger in human placental lactogen release. YQ Wu EV Jorgensen S Handwerger, Endocrinology 1988 123 1879 1884 2843350
    • (1988) Endocrinology , vol.123 , pp. 1879-1884
    • Wu, Y.Q.1    Jorgensen, E.V.2    Handwerger, S.3
  • 58
    • 33750040019 scopus 로고    scopus 로고
    • Three insulin-relaxin-like genes in Ciona intestinalis
    • 10.1016/j.peptides.2006.06.008. 16920224
    • Three insulin-relaxin-like genes in Ciona intestinalis. RP Olinski C Dahlberg M Thorndyke F Hallbook, Peptides 2006 27 2535 2546 10.1016/j.peptides. 2006.06.008 16920224
    • (2006) Peptides , vol.27 , pp. 2535-2546
    • Olinski, R.P.1    Dahlberg, C.2    Thorndyke, M.3    Hallbook, F.4
  • 59
    • 0034760668 scopus 로고    scopus 로고
    • The flamingo-related mouse Celsr family (Celsr1-3) genes exhibit distinct patterns of expression during embryonic development
    • 10.1016/S0925-4773(01)00515-9. 11677057
    • The flamingo-related mouse Celsr family (Celsr1-3) genes exhibit distinct patterns of expression during embryonic development. CJ Formstone PF Little, Mech Dev 2001 109 91 94 10.1016/S0925-4773(01)00515-9 11677057
    • (2001) Mech Dev , vol.109 , pp. 91-94
    • Formstone, C.J.1    Little, P.F.2
  • 60
    • 0033037979 scopus 로고    scopus 로고
    • The latrophilin family: Multiply spliced G protein-coupled receptors with differential tissue distribution
    • 10.1016/S0014-5793(99)00005-8. 10025961
    • The latrophilin family: multiply spliced G protein-coupled receptors with differential tissue distribution. H Matsushita V Lelianova Y Ushkaryov, FEBS Lett 1999 443 3 348 352 10.1016/S0014-5793(99)00005-8 10025961
    • (1999) FEBS Lett , vol.443 , Issue.3 , pp. 348-352
    • Matsushita, H.1    Lelianova, V.2    Ushkaryov, Y.3
  • 61
    • 35248884458 scopus 로고    scopus 로고
    • The Adhesion GPCRs: A unique family of G protein-coupled receptors with important roles in both central and peripheral tissues
    • 10.1007/s00018-007-7067-1. 17502995
    • The Adhesion GPCRs: a unique family of G protein-coupled receptors with important roles in both central and peripheral tissues. TK Bjarnadottir R Fredriksson HB Schioth, Cell Mol Life Sci 2007 64 2104 2119 10.1007/s00018-007- 7067-1 17502995
    • (2007) Cell Mol Life Sci , vol.64 , pp. 2104-2119
    • Bjarnadottir, T.K.1    Fredriksson, R.2    Schioth, H.B.3
  • 63
    • 44349095985 scopus 로고    scopus 로고
    • Pfam. http://www.sanger.ac.uk/Software/Pfam/
    • Pfam
  • 64
    • 33748253906 scopus 로고    scopus 로고
    • The Dictyostelium repertoire of seven transmembrane domain receptors
    • 10.1016/j.ejcb.2006.04.003. 16735079
    • The Dictyostelium repertoire of seven transmembrane domain receptors. Y Prabhu L Eichinger, Eur J Cell Biol 2006 85 937 946 10.1016/j.ejcb.2006.04.003 16735079
    • (2006) Eur J Cell Biol , vol.85 , pp. 937-946
    • Prabhu, Y.1    Eichinger, L.2
  • 65
    • 44349093323 scopus 로고    scopus 로고
    • FingerPRINTScan. http://www.bioinf.manchester.ac.uk/fingerPRINTScan/
    • FingerPRINTScan
  • 67
    • 33947379232 scopus 로고    scopus 로고
    • Impact of GPCRs in clinical medicine: Monogenic diseases, genetic variants and drug targets
    • 17081496. 10.1016/j.bbamem.2006.09.029
    • Impact of GPCRs in clinical medicine: monogenic diseases, genetic variants and drug targets. PA Insel CM Tang I Hahntow MC Michel, Biochim Biophys Acta 2007 1768 994 1005 17081496 10.1016/j.bbamem.2006.09.029
    • (2007) Biochim Biophys Acta , vol.1768 , pp. 994-1005
    • Insel, P.A.1    Tang, C.M.2    Hahntow, I.3    Michel, M.C.4
  • 68
    • 0032735547 scopus 로고    scopus 로고
    • Receptors for PTH and PTHrP: Their biological importance and functional properties
    • 10564229
    • Receptors for PTH and PTHrP: their biological importance and functional properties. M Mannstadt H Juppner TJ Gardella, Am J Physiol 1999 277 F665 675 10564229
    • (1999) Am J Physiol , vol.277 , pp. 665-675
    • Mannstadt, M.1    Juppner, H.2    Gardella, T.J.3
  • 69
    • 0038702484 scopus 로고    scopus 로고
    • PTHrP, PTHr, and FGFR3 are involved in the process of endochondral ossification in human osteophytes
    • 12692671
    • PTHrP, PTHr, and FGFR3 are involved in the process of endochondral ossification in human osteophytes. K Huch S Kleffner J Stove W Puhl KP Gunther RE Brenner, Histochem Cell Biol 2003 119 281 287 12692671
    • (2003) Histochem Cell Biol , vol.119 , pp. 281-287
    • Huch, K.1    Kleffner, S.2    Stove, J.3    Puhl, W.4    Gunther, K.P.5    Brenner, R.E.6
  • 70
    • 0022000808 scopus 로고
    • A case of lethal congenital dwarfism with accelerated skeletal maturation
    • 10.1007/BF02388725. 3975110
    • A case of lethal congenital dwarfism with accelerated skeletal maturation. S Blomstrand I Claesson J Save-Soderbergh, Pediatr Radiol 1985 15 141 143 10.1007/BF02388725 3975110
    • (1985) Pediatr Radiol , vol.15 , pp. 141-143
    • Blomstrand, S.1    Claesson, I.2    Save-Soderbergh, J.3
  • 71
    • 0031725947 scopus 로고    scopus 로고
    • Inactivating mutation in the human parathyroid hormone receptor type 1 gene in Blomstrand chondrodysplasia
    • 10.1210/en.139.12.5255. 9832466
    • Inactivating mutation in the human parathyroid hormone receptor type 1 gene in Blomstrand chondrodysplasia. AC Karaplis B He MT Nguyen ID Young D Semeraro H Ozawa N Amizuka, Endocrinology 1998 139 5255 5258 10.1210/en.139.12.5255 9832466
    • (1998) Endocrinology , vol.139 , pp. 5255-5258
    • Karaplis, A.C.1    He, B.2    Nguyen, M.T.3    Young, I.D.4    Semeraro, D.5    Ozawa, H.6    Amizuka, N.7
  • 72
    • 0031769483 scopus 로고    scopus 로고
    • A homozygous inactivating mutation in the parathyroid hormone/parathyroid hormone-related peptide receptor causing Blomstrand chondrodysplasia
    • 10.1210/jc.83.9.3373. 9745456
    • A homozygous inactivating mutation in the parathyroid hormone/parathyroid hormone-related peptide receptor causing Blomstrand chondrodysplasia. P Zhang AS Jobert A Couvineau C Silve, J Clin Endocrinol Metab 1998 83 3365 3368 10.1210/jc.83.9.3373 9745456
    • (1998) J Clin Endocrinol Metab , vol.83 , pp. 3365-3368
    • Zhang, P.1    Jobert, A.S.2    Couvineau, A.3    Silve, C.4
  • 73
    • 0028943780 scopus 로고
    • A constitutively active mutant PTH-PTHrP receptor in Jansen-type metaphyseal chondrodysplasia
    • 10.1126/science.7701349. 7701349
    • A constitutively active mutant PTH-PTHrP receptor in Jansen-type metaphyseal chondrodysplasia. E Schipani K Kruse H Juppner, Science 1995 268 98 100 10.1126/science.7701349 7701349
    • (1995) Science , vol.268 , pp. 98-100
    • Schipani, E.1    Kruse, K.2    Juppner, H.3
  • 74
    • 0033305322 scopus 로고    scopus 로고
    • A novel parathyroid hormone (PTH)/PTH-related peptide receptor mutation in Jansen's metaphyseal chondrodysplasia
    • 10.1210/jc.84.9.3052. 10487664
    • A novel parathyroid hormone (PTH)/PTH-related peptide receptor mutation in Jansen's metaphyseal chondrodysplasia. E Schipani C Langman J Hunzelman M Le Merrer KY Loke MJ Dillon C Silve H Juppner, J Clin Endocrinol Metab 1999 84 3052 3057 10.1210/jc.84.9.3052 10487664
    • (1999) J Clin Endocrinol Metab , vol.84 , pp. 3052-3057
    • Schipani, E.1    Langman, C.2    Hunzelman, J.3    Le Merrer, M.4    Loke, K.Y.5    Dillon, M.J.6    Silve, C.7    Juppner, H.8
  • 75
    • 0029849784 scopus 로고    scopus 로고
    • Constitutively activated receptors for parathyroid hormone and parathyroid hormone-related peptide in Jansen's metaphyseal chondrodysplasia
    • 10.1056/NEJM199609053351004. 8703170
    • Constitutively activated receptors for parathyroid hormone and parathyroid hormone-related peptide in Jansen's metaphyseal chondrodysplasia. E Schipani CB Langman AM Parfitt GS Jensen S Kikuchi SW Kooh WG Cole H Juppner, N Engl J Med 1996 335 708 714 10.1056/NEJM199609053351004 8703170
    • (1996) N Engl J Med , vol.335 , pp. 708-714
    • Schipani, E.1    Langman, C.B.2    Parfitt, A.M.3    Jensen, G.S.4    Kikuchi, S.5    Kooh, S.W.6    Cole, W.G.7    Juppner, H.8
  • 77
    • 0035072551 scopus 로고    scopus 로고
    • Clustering of highly homologous sequences to reduce the size of large protein databases
    • 10.1093/bioinformatics/17.3.282. 11294794
    • Clustering of highly homologous sequences to reduce the size of large protein databases. W Li L Jaroszewski A Godzik, Bioinformatics 2001 17 282 283 10.1093/bioinformatics/17.3.282 11294794
    • (2001) Bioinformatics , vol.17 , pp. 282-283
    • Li, W.1    Jaroszewski, L.2    Godzik, A.3
  • 78
    • 0034786532 scopus 로고    scopus 로고
    • The HMMTOP transmembrane topology prediction server
    • 10.1093/bioinformatics/17.9.849. 11590105
    • The HMMTOP transmembrane topology prediction server. GE Tusnady I Simon, Bioinformatics 2001 17 849 850 10.1093/bioinformatics/17.9.849 11590105
    • (2001) Bioinformatics , vol.17 , pp. 849-850
    • Tusnady, G.E.1    Simon, I.2
  • 79
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • 10.1006/jmbi.2000.4315. 11152613
    • Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. A Krogh B Larsson G von Heijne EL Sonnhammer, J Mol Biol 2001 305 567 580 10.1006/jmbi.2000.4315 11152613
    • (2001) J Mol Biol , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.4
  • 80
    • 0031826040 scopus 로고    scopus 로고
    • SOSUI: Classification and secondary structure prediction system for membrane proteins
    • 10.1093/bioinformatics/14.4.378. 9632836
    • SOSUI: classification and secondary structure prediction system for membrane proteins. T Hirokawa S Boon-Chieng S Mitaku, Bioinformatics 1998 14 378 379 10.1093/bioinformatics/14.4.378 9632836
    • (1998) Bioinformatics , vol.14 , pp. 378-379
    • Hirokawa, T.1    Boon-Chieng, S.2    Mitaku, S.3
  • 83
    • 0031743421 scopus 로고    scopus 로고
    • Profile hidden Markov models
    • 10.1093/bioinformatics/14.9.755. 9918945
    • Profile hidden Markov models. SR Eddy, Bioinformatics 1998 14 755 763 10.1093/bioinformatics/14.9.755 9918945
    • (1998) Bioinformatics , vol.14 , pp. 755-763
    • Eddy, S.R.1
  • 87
    • 0034800374 scopus 로고    scopus 로고
    • InterProScan - an integration platform for the signature-recognition methods in InterPro
    • 10.1093/bioinformatics/17.9.847. 11590104
    • InterProScan - an integration platform for the signature-recognition methods in InterPro. EM Zdobnov R Apweiler, Bioinformatics 2001 17 847 848 10.1093/bioinformatics/17.9.847 11590104
    • (2001) Bioinformatics , vol.17 , pp. 847-848
    • Zdobnov, E.M.1    Apweiler, R.2
  • 88
    • 44349163666 scopus 로고    scopus 로고
    • UniProt. http://www.ebi.uniprot.org/index.shtml
    • UniProt
  • 89
    • 84874649906 scopus 로고    scopus 로고
    • NCBI UniGene. ftp://ftp.ncbi.nih.gov/repository/UniGene/
    • NCBI UniGene
  • 90
    • 13744252890 scopus 로고    scopus 로고
    • MAFFT version 5: Improvement in accuracy of multiple sequence alignment
    • 15661851. 10.1093/nar/gki198
    • MAFFT version 5: improvement in accuracy of multiple sequence alignment. K Katoh K Kuma H Toh T Miyata, Nucleic Acids Res 2005 33 511 518 15661851 10.1093/nar/gki198
    • (2005) Nucleic Acids Res , vol.33 , pp. 511-518
    • Katoh, K.1    Kuma, K.2    Toh, H.3    Miyata, T.4
  • 91
    • 0000122573 scopus 로고
    • PHYLIP - Phylogeny Inference Package (Version3.2)
    • PHYLIP - Phylogeny Inference Package (Version3.2). J Felsenstein, Cladistics 1989 5 164 166
    • (1989) Cladistics , vol.5 , pp. 164-166
    • Felsenstein, J.1
  • 92
    • 0038204408 scopus 로고    scopus 로고
    • Phylogeny for the faint of heart: A tutorial
    • 10.1016/S0168-9525(03)00112-4. 12801728
    • Phylogeny for the faint of heart: a tutorial. SL Baldauf, Trends Genet 2003 19 345 351 10.1016/S0168-9525(03)00112-4 12801728
    • (2003) Trends Genet , vol.19 , pp. 345-351
    • Baldauf, S.L.1
  • 93
    • 0036205377 scopus 로고    scopus 로고
    • TREE-PUZZLE: Maximum likelihood phylogenetic analysis using quartets and parallel computing
    • 10.1093/bioinformatics/18.3.502. 11934758
    • TREE-PUZZLE: maximum likelihood phylogenetic analysis using quartets and parallel computing. HA Schmidt K Strimmer M Vingron A von Haeseler, Bioinformatics 2002 18 502 504 10.1093/bioinformatics/18.3.502 11934758
    • (2002) Bioinformatics , vol.18 , pp. 502-504
    • Schmidt, H.A.1    Strimmer, K.2    Vingron, M.3    Von Haeseler, A.4
  • 94
    • 30744470609 scopus 로고    scopus 로고
    • Application of phylogenetic networks in evolutionary studies
    • 10.1093/molbev/msj030. 16221896
    • Application of phylogenetic networks in evolutionary studies. DH Huson D Bryant, Mol Biol Evol 2006 23 254 267 10.1093/molbev/msj030 16221896
    • (2006) Mol Biol Evol , vol.23 , pp. 254-267
    • Huson, D.H.1    Bryant, D.2
  • 95
    • 0030203863 scopus 로고    scopus 로고
    • TreeView: An application to display phylogenetic trees on personal computers
    • 8902363
    • TreeView: an application to display phylogenetic trees on personal computers. RD Page, Comput Appl Biosci 1996 12 357 358 8902363
    • (1996) Comput Appl Biosci , vol.12 , pp. 357-358
    • Page, R.D.1
  • 97
    • 44349104395 scopus 로고    scopus 로고
    • GTPred. http://gdds.pharm.kyoto-u.ac.jp/services/gtpred/
    • GTPred
  • 98
    • 15844371700 scopus 로고    scopus 로고
    • Transmembrane residues of the parathyroid hormone (PTH)/PTH-related peptide receptor that specifically affect binding and signaling by agonist ligands
    • 10.1074/jbc.271.43.26469. 8662729
    • Transmembrane residues of the parathyroid hormone (PTH)/PTH-related peptide receptor that specifically affect binding and signaling by agonist ligands. TJ Gardella MD Luck MH Fan C Lee, J Biol Chem 1996 271 12820 12825 10.1074/jbc.271.43.26469 8662729
    • (1996) J Biol Chem , vol.271 , pp. 12820-12825
    • Gardella, T.J.1    Luck, M.D.2    Fan, M.H.3    Lee, C.4
  • 99
    • 0033527567 scopus 로고    scopus 로고
    • The hydrophobic residues phenylalanine 184 and leucine 187 in the type-1 parathyroid hormone (PTH) receptor functionally interact with the amino-terminal portion of PTH-(1-34)
    • 10.1074/jbc.274.45.31955. 10542224
    • The hydrophobic residues phenylalanine 184 and leucine 187 in the type-1 parathyroid hormone (PTH) receptor functionally interact with the amino-terminal portion of PTH-(1-34). PH Carter M Shimizu MD Luck TJ Gardella, J Biol Chem 1999 274 31955 31960 10.1074/jbc.274.45.31955 10542224
    • (1999) J Biol Chem , vol.274 , pp. 31955-31960
    • Carter, P.H.1    Shimizu, M.2    Luck, M.D.3    Gardella, T.J.4
  • 100
    • 0030703626 scopus 로고    scopus 로고
    • Residues in the membrane-spanning and extracellular loop regions of the parathyroid hormone (PTH)-2 receptor determine signaling selectivity for PTH and PTH-related peptide
    • 10.1074/jbc.272.46.28861. 9360953
    • Residues in the membrane-spanning and extracellular loop regions of the parathyroid hormone (PTH)-2 receptor determine signaling selectivity for PTH and PTH-related peptide. C Bergwitz SA Jusseaume MD Luck H Juppner TJ Gardella, J Biol Chem 1997 272 28861 28868 10.1074/jbc.272.46.28861 9360953
    • (1997) J Biol Chem , vol.272 , pp. 28861-28868
    • Bergwitz, C.1    Jusseaume, S.A.2    Luck, M.D.3    Juppner, H.4    Gardella, T.J.5
  • 101
    • 0032512751 scopus 로고    scopus 로고
    • Transmembrane residues together with the amino terminus limit the response of the parathyroid hormone (PTH) 2 receptor to PTH-related peptide
    • 10.1074/jbc.273.7.3830. 9461563
    • Transmembrane residues together with the amino terminus limit the response of the parathyroid hormone (PTH) 2 receptor to PTH-related peptide. PR Turner S Mefford T Bambino RA Nissenson, J Biol Chem 1998 273 3830 3837 10.1074/jbc.273.7.3830 9461563
    • (1998) J Biol Chem , vol.273 , pp. 3830-3837
    • Turner, P.R.1    Mefford, S.2    Bambino, T.3    Nissenson, R.A.4
  • 102
    • 33846454003 scopus 로고    scopus 로고
    • Structural features of parathyroid hormone receptor coupled to Galpha(s)-protein
    • 17040990. 10.1529/biophysj.106.094813
    • Structural features of parathyroid hormone receptor coupled to Galpha(s)-protein. J Plati N Tsomaia A Piserchio DF Mierke, Biophys J 2007 92 535 540 17040990 10.1529/biophysj.106.094813
    • (2007) Biophys J , vol.92 , pp. 535-540
    • Plati, J.1    Tsomaia, N.2    Piserchio, A.3    Mierke, D.F.4
  • 103
    • 0030895863 scopus 로고    scopus 로고
    • Mutations in the second cytoplasmic loop of the rat parathyroid hormone (PTH)/PTH-related protein receptor result in selective loss of PTH-stimulated phospholipase C activity
    • 10.1074/jbc.272.11.6882. 9054374
    • Mutations in the second cytoplasmic loop of the rat parathyroid hormone (PTH)/PTH-related protein receptor result in selective loss of PTH-stimulated phospholipase C activity. A Iida-Klein J Guo M Takemura MT Drake JT Potts Jr A Abou-Samra FR Bringhurst GV Segre, J Biol Chem 1997 272 6882 6889 10.1074/jbc.272.11.6882 9054374
    • (1997) J Biol Chem , vol.272 , pp. 6882-6889
    • Iida-Klein, A.1    Guo, J.2    Takemura, M.3    Drake, M.T.4    Potts Jr., J.T.5    Abou-Samra, A.6    Bringhurst, F.R.7    Segre, G.V.8
  • 104
    • 0030460776 scopus 로고    scopus 로고
    • The N-terminal region of the third intracellular loop of the parathyroid hormone (PTH)/PTH-related peptide receptor is critical for coupling to cAMP and inositol phosphate/Ca2+ signal transduction pathways
    • 10.1074/jbc.271.52.33382. 8969199
    • The N-terminal region of the third intracellular loop of the parathyroid hormone (PTH)/PTH-related peptide receptor is critical for coupling to cAMP and inositol phosphate/Ca2+ signal transduction pathways. Z Huang Y Chen S Pratt TH Chen T Bambino RA Nissenson DM Shoback, J Biol Chem 1996 271 33382 33389 10.1074/jbc.271.52.33382 8969199
    • (1996) J Biol Chem , vol.271 , pp. 33382-33389
    • Huang, Z.1    Chen, Y.2    Pratt, S.3    Chen, T.H.4    Bambino, T.5    Nissenson, R.A.6    Shoback, D.M.7
  • 106
    • 0032479306 scopus 로고    scopus 로고
    • Evidence for a ligand interaction site at the amino-terminus of the parathyroid hormone (PTH)/PTH-related protein receptor from cross-linking and mutational studies
    • 10.1074/jbc.273.27.16890. 9642250
    • Evidence for a ligand interaction site at the amino-terminus of the parathyroid hormone (PTH)/PTH-related protein receptor from cross-linking and mutational studies. M Mannstadt MD Luck TJ Gardella H Juppner, J Biol Chem 1998 273 16890 16896 10.1074/jbc.273.27.16890 9642250
    • (1998) J Biol Chem , vol.273 , pp. 16890-16896
    • Mannstadt, M.1    Luck, M.D.2    Gardella, T.J.3    Juppner, H.4
  • 107
    • 0029165117 scopus 로고
    • Homolog-scanning mutagenesis of the parathyroid hormone (PTH) receptor reveals PTH-(1-34) binding determinants in the third extracellular loop
    • 10.1210/me.9.10.1269. 8544835
    • Homolog-scanning mutagenesis of the parathyroid hormone (PTH) receptor reveals PTH-(1-34) binding determinants in the third extracellular loop. C Lee MD Luck H Juppner JT Potts Jr HM Kronenberg TJ Gardella, Mol Endocrinol 1995 9 1269 1278 10.1210/me.9.10.1269 8544835
    • (1995) Mol Endocrinol , vol.9 , pp. 1269-1278
    • Lee, C.1    Luck, M.D.2    Juppner, H.3    Potts Jr., J.T.4    Kronenberg, H.M.5    Gardella, T.J.6
  • 108
    • 0347480255 scopus 로고    scopus 로고
    • Identification of a contact site for residue 19 of parathyroid hormone (PTH) and PTH-related protein analogs in transmembrane domain two of the type 1 PTH receptor
    • 10.1210/me.2003-0275. 12947048
    • Identification of a contact site for residue 19 of parathyroid hormone (PTH) and PTH-related protein analogs in transmembrane domain two of the type 1 PTH receptor. RC Gensure N Shimizu J Tsang TJ Gardella, Mol Endocrinol 2003 17 2647 2658 10.1210/me.2003-0275 12947048
    • (2003) Mol Endocrinol , vol.17 , pp. 2647-2658
    • Gensure, R.C.1    Shimizu, N.2    Tsang, J.3    Gardella, T.J.4
  • 109
    • 0031724680 scopus 로고    scopus 로고
    • Arginine 186 in the extracellular N-terminal region of the human parathyroid hormone 1 receptor is essential for contact with position 13 of the hormone
    • 10.1210/me.12.11.1673. 9817594
    • Arginine 186 in the extracellular N-terminal region of the human parathyroid hormone 1 receptor is essential for contact with position 13 of the hormone. AE Adams A Bisello M Chorev M Rosenblatt LJ Suva, Mol Endocrinol 1998 12 1673 1683 10.1210/me.12.11.1673 9817594
    • (1998) Mol Endocrinol , vol.12 , pp. 1673-1683
    • Adams, A.E.1    Bisello, A.2    Chorev, M.3    Rosenblatt, M.4    Suva, L.J.5
  • 110
    • 0032575523 scopus 로고    scopus 로고
    • Parathyroid hormone-receptor interactions identified directly by photocross-linking and molecular modeling studies
    • 10.1074/jbc.273.35.22498. 9712875
    • Parathyroid hormone-receptor interactions identified directly by photocross-linking and molecular modeling studies. A Bisello AE Adams DF Mierke M Pellegrini M Rosenblatt LJ Suva M Chorev, J Biol Chem 1998 273 22498 22505 10.1074/jbc.273.35.22498 9712875
    • (1998) J Biol Chem , vol.273 , pp. 22498-22505
    • Bisello, A.1    Adams, A.E.2    Mierke, D.F.3    Pellegrini, M.4    Rosenblatt, M.5    Suva, L.J.6    Chorev, M.7
  • 111
    • 0034682641 scopus 로고    scopus 로고
    • Mapping the bimolecular interface of the parathyroid hormone (PTH)-PTH1 receptor complex: Spatial proximity between Lys(27) (of the hormone principal binding domain) and leu(261) (of the first extracellular loop) of the human PTH1 receptor
    • 10.1021/bi000195n. 10889020
    • Mapping the bimolecular interface of the parathyroid hormone (PTH)-PTH1 receptor complex: spatial proximity between Lys(27) (of the hormone principal binding domain) and leu(261) (of the first extracellular loop) of the human PTH1 receptor. Z Greenberg A Bisello DF Mierke M Rosenblatt M Chorev, Biochemistry 2000 39 8142 8152 10.1021/bi000195n 10889020
    • (2000) Biochemistry , vol.39 , pp. 8142-8152
    • Greenberg, Z.1    Bisello, A.2    Mierke, D.F.3    Rosenblatt, M.4    Chorev, M.5
  • 112


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