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Volumn 65, Issue 22, 2008, Pages 3664-3676

Molecular and structural effects of inverse agonistic mutations on signaling of the thyrotropin receptor - A basally active GPCR

Author keywords

Activation mechanism; Endocrinology; FSHR; Glycoprotein hormone receptors; Inverse agonism; LHCGR; LHR; Signal transduction; TSHR

Indexed keywords

FOLLITROPIN RECEPTOR BINDING INHIBITOR; G PROTEIN COUPLED RECEPTOR; LUTEINIZING HORMONE RECEPTOR; OPSIN; PROTIRELIN RECEPTOR; RHODOPSIN; THYROTROPIN; THYROTROPIN RECEPTOR;

EID: 56549103329     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-008-8450-2     Document Type: Article
Times cited : (20)

References (73)
  • 2
    • 0036033424 scopus 로고    scopus 로고
    • Constitutive activity of G-protein-coupled receptors: Cause of disease and common property of wild-type receptors
    • Seifert, R. and Wenzel-Seifert, K. (2002) Constitutive activity of G-protein-coupled receptors: cause of disease and common property of wild-type receptors. Naunyn Schmiedebergs Arch. Pharmacol. 366, 381-416.
    • (2002) Naunyn Schmiedebergs Arch. Pharmacol , vol.366 , pp. 381-416
    • Seifert, R.1    Wenzel-Seifert, K.2
  • 3
    • 4344626047 scopus 로고    scopus 로고
    • Constitutively active G protein-coupled receptor mutants: Implications on receptor function and drug action
    • Cotecchia, S., Fanelli, F., and Costa, T. (2003) Constitutively active G protein-coupled receptor mutants: implications on receptor function and drug action. Assay. Drug Dev. Technol. 1, 311-316.
    • (2003) Assay. Drug Dev. Technol , vol.1 , pp. 311-316
    • Cotecchia, S.1    Fanelli, F.2    Costa, T.3
  • 4
    • 0347627709 scopus 로고    scopus 로고
    • Constitutive activity and inverse agonists of G protein-coupled receptors: A current perspective
    • Milligan, G. (2003) Constitutive activity and inverse agonists of G protein-coupled receptors: a current perspective. Mol. Pharmacol. 64, 1271-1276.
    • (2003) Mol. Pharmacol , vol.64 , pp. 1271-1276
    • Milligan, G.1
  • 5
    • 31844446495 scopus 로고    scopus 로고
    • Recent developments in constitutive receptor activity and inverse agonism, and their potential for GPCR drug discovery
    • Bond, R. A. and Ijzerman, A. P. (2006) Recent developments in constitutive receptor activity and inverse agonism, and their potential for GPCR drug discovery. Trends Pharmacol. Sci. 27, 92-96.
    • (2006) Trends Pharmacol. Sci , vol.27 , pp. 92-96
    • Bond, R.A.1    Ijzerman, A.P.2
  • 6
    • 0036366975 scopus 로고    scopus 로고
    • The structural basis of G-protein-coupled receptor function and dysfunction in human diseases
    • Schoneberg, T., Schulz, A., and Gudermann, T. (2002) The structural basis of G-protein-coupled receptor function and dysfunction in human diseases. Rev. Physiol. Biochem. Pharmacol. 144, 143-227.
    • (2002) Rev. Physiol. Biochem. Pharmacol , vol.144 , pp. 143-227
    • Schoneberg, T.1    Schulz, A.2    Gudermann, T.3
  • 7
    • 9644279627 scopus 로고    scopus 로고
    • Constitutive activity of the melanocortin-4 receptor is maintained by its N-terminal domain and plays a role in energy homeostasis in humans
    • Srinivasan, S., Lubrano-Berthelier, C., Govaerts, C., Picard, F., Santiago, P., Conklin, B. R., and Vaisse, C. (2004) Constitutive activity of the melanocortin-4 receptor is maintained by its N-terminal domain and plays a role in energy homeostasis in humans. J. Clin. Invest. 114, 1158-1164.
    • (2004) J. Clin. Invest , vol.114 , pp. 1158-1164
    • Srinivasan, S.1    Lubrano-Berthelier, C.2    Govaerts, C.3    Picard, F.4    Santiago, P.5    Conklin, B.R.6    Vaisse, C.7
  • 8
    • 27744483068 scopus 로고    scopus 로고
    • The physiological significance of constitutive receptor activity
    • Kenakin, T. (2005) The physiological significance of constitutive receptor activity. Trends in Pharmacological Sciences 26, 603-605.
    • (2005) Trends in Pharmacological Sciences , vol.26 , pp. 603-605
    • Kenakin, T.1
  • 9
    • 0030725173 scopus 로고    scopus 로고
    • The thyrotropin receptor in thyroid diseases
    • Paschke, R. and Ludgate, M. (1997) The thyrotropin receptor in thyroid diseases. N. Engl. J. Med. 337, 1675-1681.
    • (1997) N. Engl. J. Med , vol.337 , pp. 1675-1681
    • Paschke, R.1    Ludgate, M.2
  • 13
    • 45549109545 scopus 로고    scopus 로고
    • Constitutive activity of the cannabinoid CB1 receptor regulates the function of co-expressed Mu opioid receptors
    • Canals, M. and Milligan, G. (2008) Constitutive activity of the cannabinoid CB1 receptor regulates the function of co-expressed Mu opioid receptors. J. Biol. Chem. 283, 11424-11434.
    • (2008) J. Biol. Chem , vol.283 , pp. 11424-11434
    • Canals, M.1    Milligan, G.2
  • 14
    • 11144225093 scopus 로고    scopus 로고
    • Common structural basis for constitutive activity of the ghrelin receptor family
    • Holst, B., Holliday, N. D., Bach, A., Elling, C. E., Cox, H. M., and Schwartz, T. W. (2004) Common structural basis for constitutive activity of the ghrelin receptor family. J. Biol. Chem. 279, 53806-53817.
    • (2004) J. Biol. Chem , vol.279 , pp. 53806-53817
    • Holst, B.1    Holliday, N.D.2    Bach, A.3    Elling, C.E.4    Cox, H.M.5    Schwartz, T.W.6
  • 15
    • 3042798261 scopus 로고    scopus 로고
    • Molecular mechanisms of ligand binding, signaling, and regulation within the superfamily of G-protein-coupled receptors: Molecular modeling and mutagenesis approaches to receptor structure and function
    • Kristiansen, K. (2004) Molecular mechanisms of ligand binding, signaling, and regulation within the superfamily of G-protein-coupled receptors: molecular modeling and mutagenesis approaches to receptor structure and function. Pharmacol. Ther. 103, 21-80.
    • (2004) Pharmacol. Ther , vol.103 , pp. 21-80
    • Kristiansen, K.1
  • 16
    • 0034663812 scopus 로고    scopus 로고
    • Dominant-negative activity of an alpha(1B)-adrenergic receptor signal-inactivating point mutation
    • Chen, S., Lin, F., Xu, M., Hwa, J., and Graham, R. M. (2000) Dominant-negative activity of an alpha(1B)-adrenergic receptor signal-inactivating point mutation. EMBO J. 19, 4265-4271.
    • (2000) EMBO J , vol.19 , pp. 4265-4271
    • Chen, S.1    Lin, F.2    Xu, M.3    Hwa, J.4    Graham, R.M.5
  • 17
    • 41149160907 scopus 로고    scopus 로고
    • Understanding the structural and functional differences between mouse thyrotropin-releasing hormone receptors 1 and 2
    • Deflorian, F., Engel, S., Colson, A. O., Raaka, B. M., Gershengorn, M. C., and Costanzi, S. (2008) Understanding the structural and functional differences between mouse thyrotropin-releasing hormone receptors 1 and 2. Proteins 71, 783-794.
    • (2008) Proteins , vol.71 , pp. 783-794
    • Deflorian, F.1    Engel, S.2    Colson, A.O.3    Raaka, B.M.4    Gershengorn, M.C.5    Costanzi, S.6
  • 19
    • 35948944223 scopus 로고    scopus 로고
    • The thyrotropin receptor in Graves' disease
    • Rapoport, B. and McLachlan, S. M. (2007) The thyrotropin receptor in Graves' disease. Thyroid 17, 911-922.
    • (2007) Thyroid , vol.17 , pp. 911-922
    • Rapoport, B.1    McLachlan, S.M.2
  • 20
    • 41549162492 scopus 로고    scopus 로고
    • An intracellular loop (IL2) residue confers different basal constitutive activities to the human lutropin receptor and human thyrotropin receptor through structural communication between IL2 and helix 6, via helix 3
    • Feng, X., Muller, T., Mizrachi, D., Fanelli, F., and Segaloff, D. L. (2008) An intracellular loop (IL2) residue confers different basal constitutive activities to the human lutropin receptor and human thyrotropin receptor through structural communication between IL2 and helix 6, via helix 3. Endocrinology 149, 1705-1717.
    • (2008) Endocrinology , vol.149 , pp. 1705-1717
    • Feng, X.1    Muller, T.2    Mizrachi, D.3    Fanelli, F.4    Segaloff, D.L.5
  • 22
    • 0029056743 scopus 로고
    • Constitutive activation of the thyrotropin receptor by deletion of a portion of the extracellular domain
    • Zhang, M. L., Sugawa, H., Kosugi, S., and Mori, T. (1995) Constitutive activation of the thyrotropin receptor by deletion of a portion of the extracellular domain. Biochem. Biophys. Res. Commun. 211, 205-210.
    • (1995) Biochem. Biophys. Res. Commun , vol.211 , pp. 205-210
    • Zhang, M.L.1    Sugawa, H.2    Kosugi, S.3    Mori, T.4
  • 23
    • 0030805829 scopus 로고    scopus 로고
    • Constitutive activation of the TSH receptor by spontaneous mutations affecting the N-terminal extracellular domain
    • Duprez, L., Parma, J., Costagliola, S., Hermans, J., Van Sande, J., Dumont, J. E., and Vassart, G. (1997) Constitutive activation of the TSH receptor by spontaneous mutations affecting the N-terminal extracellular domain. FEBS Lett. 409, 469-474.
    • (1997) FEBS Lett , vol.409 , pp. 469-474
    • Duprez, L.1    Parma, J.2    Costagliola, S.3    Hermans, J.4    Van Sande, J.5    Dumont, J.E.6    Vassart, G.7
  • 24
    • 2642703472 scopus 로고    scopus 로고
    • Deletions in the third intracellular loop of the thyrotropin receptor. A new mechanism for constitutive activation
    • Wonerow, P., Schoneberg, T., Schultz, G., Gudermann, T., and Paschke, R. (1998) Deletions in the third intracellular loop of the thyrotropin receptor. A new mechanism for constitutive activation. J. Biol. Chem. 273, 7900-7905.
    • (1998) J. Biol. Chem , vol.273 , pp. 7900-7905
    • Wonerow, P.1    Schoneberg, T.2    Schultz, G.3    Gudermann, T.4    Paschke, R.5
  • 25
    • 0031790855 scopus 로고    scopus 로고
    • A conserved tyrosine residue (Y601) in transmembrane domain 5 of the human thyrotropin receptor serves as a molecular switch to determine G-protein coupling
    • Biebermann, H., Schoneberg, T., Schulz, A., Krause, G., Gruters, A., Schultz, G., and Gudermann, T. (1998) A conserved tyrosine residue (Y601) in transmembrane domain 5 of the human thyrotropin receptor serves as a molecular switch to determine G-protein coupling. FASEB J. 12, 1461-1471.
    • (1998) FASEB J , vol.12 , pp. 1461-1471
    • Biebermann, H.1    Schoneberg, T.2    Schulz, A.3    Krause, G.4    Gruters, A.5    Schultz, G.6    Gudermann, T.7
  • 26
    • 0034895145 scopus 로고    scopus 로고
    • A free carboxylate oxygen in the side chain of position 674 in transmembrane domain 7 is necessary for TSH receptor activation
    • Neumann, S., Krause, G., Chey, S., and Paschke, R. (2001) A free carboxylate oxygen in the side chain of position 674 in transmembrane domain 7 is necessary for TSH receptor activation. Mol. Endocrinol. 15, 1294-1305.
    • (2001) Mol. Endocrinol , vol.15 , pp. 1294-1305
    • Neumann, S.1    Krause, G.2    Chey, S.3    Paschke, R.4
  • 27
    • 0037165664 scopus 로고    scopus 로고
    • A conserved Asn in TM7 of the thyrotropin receptor is a common requirement for activation by both mutations and its natural agonist
    • Claeysen, S., Govaerts, C., Lefort, A., Van Sande, J., Costagliola, S., Pardo, L., and Vassart, G. (2002) A conserved Asn in TM7 of the thyrotropin receptor is a common requirement for activation by both mutations and its natural agonist. FEBS Lett. 517, 195-200.
    • (2002) FEBS Lett , vol.517 , pp. 195-200
    • Claeysen, S.1    Govaerts, C.2    Lefort, A.3    Van Sande, J.4    Costagliola, S.5    Pardo, L.6    Vassart, G.7
  • 28
    • 30044447924 scopus 로고    scopus 로고
    • Cysteine 390 mutation of the TSH receptor modulates its ectodomain as an inverse agonist on the serpentine domain with decrease in basal constitutive activity
    • Ho, S. C., Goh, S. S., Su, Q., and Khoo, D. H. (2005) Cysteine 390 mutation of the TSH receptor modulates its ectodomain as an inverse agonist on the serpentine domain with decrease in basal constitutive activity. Mol. Cell Endocrinol. 245, 158-168.
    • (2005) Mol. Cell Endocrinol , vol.245 , pp. 158-168
    • Ho, S.C.1    Goh, S.S.2    Su, Q.3    Khoo, D.H.4
  • 29
    • 33645406071 scopus 로고    scopus 로고
    • Repulsive separation of the cytoplasmic ends of transmembrane helices 3 and 6 is linked to receptor activation in a novel thyrotropin receptor mutant (M626I)
    • Ringkananont, U., Van Durme, J., Montanelli, L., Ugrasbul, F., Yu, Y. M., Weiss, R. E., Refetoff, S., and Grasberger, H. (2006) Repulsive separation of the cytoplasmic ends of transmembrane helices 3 and 6 is linked to receptor activation in a novel thyrotropin receptor mutant (M626I). Mol. Endocrinol. 20, 893-903.
    • (2006) Mol. Endocrinol , vol.20 , pp. 893-903
    • Ringkananont, U.1    Van Durme, J.2    Montanelli, L.3    Ugrasbul, F.4    Yu, Y.M.5    Weiss, R.E.6    Refetoff, S.7    Grasberger, H.8
  • 30
    • 33846978093 scopus 로고    scopus 로고
    • Contacts between extracellular loop two and transmembrane helix six determine basal activity of the thyroid-stimulating hormone receptor
    • Kleinau, G., Claus, M., Jaeschke, H., Mueller, S., Neumann, S., Paschke, R., and Krause, G. (2007) Contacts between extracellular loop two and transmembrane helix six determine basal activity of the thyroid-stimulating hormone receptor. J. Biol. Chem. 282, 518-525.
    • (2007) J. Biol. Chem , vol.282 , pp. 518-525
    • Kleinau, G.1    Claus, M.2    Jaeschke, H.3    Mueller, S.4    Neumann, S.5    Paschke, R.6    Krause, G.7
  • 31
    • 0036020508 scopus 로고    scopus 로고
    • Chimeras of the rat and human FSH receptors (FSHRs) identify residues that permit or suppress transmembrane 6 mutation-induced constitutive activation of the FSHR via rearrangements of hydrophobic interactions between helices 6 and 7
    • Tao, Y. X., Mizrachi, D., and Segaloff, D. L. (2002) Chimeras of the rat and human FSH receptors (FSHRs) identify residues that permit or suppress transmembrane 6 mutation-induced constitutive activation of the FSHR via rearrangements of hydrophobic interactions between helices 6 and 7. Mol. Endocrinol. 16, 1881-1892.
    • (2002) Mol. Endocrinol , vol.16 , pp. 1881-1892
    • Tao, Y.X.1    Mizrachi, D.2    Segaloff, D.L.3
  • 32
    • 17744366823 scopus 로고    scopus 로고
    • Interactions between the extracellular domain and the extracellular loops as well as the 6th transmembrane domain are necessary for TSH receptor activation
    • Neumann, S., Claus, M., and Paschke, R. (2005) Interactions between the extracellular domain and the extracellular loops as well as the 6th transmembrane domain are necessary for TSH receptor activation. Eur. J. Endocrinol. 152, 625-634.
    • (2005) Eur. J. Endocrinol , vol.152 , pp. 625-634
    • Neumann, S.1    Claus, M.2    Paschke, R.3
  • 33
    • 11144225829 scopus 로고    scopus 로고
    • Structural determinants for g protein activation and selectivity in the second intracellular loop of the thyrotropin receptor
    • Neumann, S., Krause, G., Claus, M., and Paschke, R. (2005) Structural determinants for g protein activation and selectivity in the second intracellular loop of the thyrotropin receptor. Endocrinology 146, 477-485.
    • (2005) Endocrinology , vol.146 , pp. 477-485
    • Neumann, S.1    Krause, G.2    Claus, M.3    Paschke, R.4
  • 34
    • 33750488472 scopus 로고    scopus 로고
    • Structural determinants for G-protein activation and specificity in the third intracellular loop of the thyroid-stimulating hormone receptor
    • Claus, M., Neumann, S., Kleinau, G., Krause, G., and Paschke, R. (2006) Structural determinants for G-protein activation and specificity in the third intracellular loop of the thyroid-stimulating hormone receptor. J. Mol. Med. 84, 943-954.
    • (2006) J. Mol. Med , vol.84 , pp. 943-954
    • Claus, M.1    Neumann, S.2    Kleinau, G.3    Krause, G.4    Paschke, R.5
  • 36
    • 47049130668 scopus 로고    scopus 로고
    • Crystal structure of the ligand-free G-protein-coupled receptor opsin
    • Park, J. H., Scheerer, P., Hofmann, K. P., Choe, H. W., and Ernst, O. P. (2008) Crystal structure of the ligand-free G-protein-coupled receptor opsin. Nature 454, 183-187.
    • (2008) Nature , vol.454 , pp. 183-187
    • Park, J.H.1    Scheerer, P.2    Hofmann, K.P.3    Choe, H.W.4    Ernst, O.P.5
  • 37
    • 33645515699 scopus 로고    scopus 로고
    • An aromatic environment in the vicinity of serine 281 is a structural requirement for thyrotropin receptor function
    • Jaeschke, H., Neumann, S., Kleinau, G., Mueller, S., Claus, M., Krause, G., and Paschke, R. (2006) An aromatic environment in the vicinity of serine 281 is a structural requirement for thyrotropin receptor function. Endocrinology 147, 1753-1760.
    • (2006) Endocrinology , vol.147 , pp. 1753-1760
    • Jaeschke, H.1    Neumann, S.2    Kleinau, G.3    Mueller, S.4    Claus, M.5    Krause, G.6    Paschke, R.7
  • 38
    • 0035800850 scopus 로고    scopus 로고
    • Activation of the beta 2-adrenergic receptor involves disruption of an ionic lock between the cytoplasmic ends of transmembrane segments 3 and 6
    • Ballesteros, J. A., Jensen, A. D., Liapakis, G., Rasmussen, S. G., Shi, L., Gether, U., and Javitch, J. A. (2001) Activation of the beta 2-adrenergic receptor involves disruption of an ionic lock between the cytoplasmic ends of transmembrane segments 3 and 6. J. Biol. Chem. 276, 29171-29177.
    • (2001) J. Biol. Chem , vol.276 , pp. 29171-29177
    • Ballesteros, J.A.1    Jensen, A.D.2    Liapakis, G.3    Rasmussen, S.G.4    Shi, L.5    Gether, U.6    Javitch, J.A.7
  • 41
    • 38749131545 scopus 로고    scopus 로고
    • New G-protein-coupled receptor crystal structures: Insights and limitations
    • Kobilka, B. and Schertler, G. F. (2008) New G-protein-coupled receptor crystal structures: insights and limitations. Trends Pharmacol. Sci. 29, 79-83.
    • (2008) Trends Pharmacol. Sci , vol.29 , pp. 79-83
    • Kobilka, B.1    Schertler, G.F.2
  • 44
    • 77957055780 scopus 로고
    • Integrated Methods for the Construction of Three-Dimensional Models and Computational Probing of Structure-Function Relationships in G-Protein Coupled Receptors
    • Ballesteros, J. A. and Weinstein, H. (1995) Integrated Methods for the Construction of Three-Dimensional Models and Computational Probing of Structure-Function Relationships in G-Protein Coupled Receptors. Methods Neurosci. 25, 366-428.
    • (1995) Methods Neurosci , vol.25 , pp. 366-428
    • Ballesteros, J.A.1    Weinstein, H.2
  • 45
    • 0029044073 scopus 로고
    • Somatic mutations causing constitutive activity of the thyrotropin receptor are the major cause of hyperfunctioning thyroid adenomas: Identification of additional mutations activating both the cyclic adenosine 3′,5′-monophosphate and inositol phosphate-Ca2+ cascades
    • Parma, J., Van Sande, J., Swillens, S., Tonacchera, M., Dumont, J., and Vassart, G. (1995) Somatic mutations causing constitutive activity of the thyrotropin receptor are the major cause of hyperfunctioning thyroid adenomas: identification of additional mutations activating both the cyclic adenosine 3′,5′-monophosphate and inositol phosphate-Ca2+ cascades. Mol. Endocrinol. 9, 725-733.
    • (1995) Mol. Endocrinol , vol.9 , pp. 725-733
    • Parma, J.1    Van Sande, J.2    Swillens, S.3    Tonacchera, M.4    Dumont, J.5    Vassart, G.6
  • 46
    • 0034463802 scopus 로고    scopus 로고
    • Detection of thyroid-stimulating hormone receptor and Gsalpha mutations: In 75 toxic thyroid nodules by denaturing gradient gel electrophoresis
    • Trulzsch, B., Krohn, K., Wonerow, P., Chey, S., Holzapfel, H. P., Ackermann, F., Fuhrer, D., and Paschke, R. (2001) Detection of thyroid-stimulating hormone receptor and Gsalpha mutations: in 75 toxic thyroid nodules by denaturing gradient gel electrophoresis. J. Mol. Med. 78, 684-691.
    • (2001) J. Mol. Med , vol.78 , pp. 684-691
    • Trulzsch, B.1    Krohn, K.2    Wonerow, P.3    Chey, S.4    Holzapfel, H.P.5    Ackermann, F.6    Fuhrer, D.7    Paschke, R.8
  • 47
    • 0028588698 scopus 로고
    • Identification and functional characterization of two new somatic mutations causing constitutive activation of the thyrotropin receptor in hyperfunctioning autonomous adenomas of the thyroid
    • Paschke, R., Tonacchera, M., Van Sande, J., Parma, J., and Vassart, G. (1994) Identification and functional characterization of two new somatic mutations causing constitutive activation of the thyrotropin receptor in hyperfunctioning autonomous adenomas of the thyroid. J. Clin. Endocrinol. Metab. 79, 1785-1789.
    • (1994) J. Clin. Endocrinol. Metab , vol.79 , pp. 1785-1789
    • Paschke, R.1    Tonacchera, M.2    Van Sande, J.3    Parma, J.4    Vassart, G.5
  • 48
    • 0030710212 scopus 로고    scopus 로고
    • Somatic mutations in the thyrotropin receptor gene and not in the Gs alpha protein gene in 31 toxic thyroid nodules
    • Fuhrer, D., Holzapfel, H. P., Wonerow, P., Scherbaum, W. A., and Paschke, R. (1997) Somatic mutations in the thyrotropin receptor gene and not in the Gs alpha protein gene in 31 toxic thyroid nodules. J. Clin. Endocrinol. Metab 82, 3885-3891.
    • (1997) J. Clin. Endocrinol. Metab , vol.82 , pp. 3885-3891
    • Fuhrer, D.1    Holzapfel, H.P.2    Wonerow, P.3    Scherbaum, W.A.4    Paschke, R.5
  • 49
    • 33846631365 scopus 로고    scopus 로고
    • Implications for molecular mechanisms of glycoprotein hormone receptors using a new sequence-structure-function analysis resource
    • Kleinau, G., Brehm, M., Wiedemann, U., Labudde, D., Leser, U., and Krause, G. (2007) Implications for molecular mechanisms of glycoprotein hormone receptors using a new sequence-structure-function analysis resource. Mol. Endocrinol. 21, 574-580.
    • (2007) Mol. Endocrinol , vol.21 , pp. 574-580
    • Kleinau, G.1    Brehm, M.2    Wiedemann, U.3    Labudde, D.4    Leser, U.5    Krause, G.6
  • 51
    • 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., Krude, H., Krohn, H. P., Dralle, H., and Gudermann, T. (1998) Severe congenital hyperthyroidism caused by a germ-line neo mutation in the extracellular portion of the thyrotropin receptor. J. Clin. Endocrinol. Metab 83, 1431-1436.
    • (1998) J. Clin. Endocrinol. Metab , vol.83 , pp. 1431-1436
    • Gruters, A.1    Schoneberg, T.2    Biebermann, H.3    Krude, H.4    Krohn, H.P.5    Dralle, H.6    Gudermann, T.7
  • 53
    • 34548484560 scopus 로고    scopus 로고
    • Intrinsic differences in the response of the human lutropin receptor versus the human follitropin receptor to activating mutations
    • Zhang, M., Tao, Y. X., Ryan, G. L., Feng, X., Fanelli, F., and Segaloff, D. L. (2007) Intrinsic differences in the response of the human lutropin receptor versus the human follitropin receptor to activating mutations. J. Biol. Chem. 282, 25527-25539.
    • (2007) J. Biol. Chem , vol.282 , pp. 25527-25539
    • Zhang, M.1    Tao, Y.X.2    Ryan, G.L.3    Feng, X.4    Fanelli, F.5    Segaloff, D.L.6
  • 54
    • 0037040202 scopus 로고    scopus 로고
    • The ectodomain of the luteinizing hormone receptor interacts with exoloop 2 to constrain the transmembrane region: Studies using chimeric human and fly receptors
    • Nishi, S., Nakabayashi, K., Kobilka, B., and Hsueh, A. J. (2002) The ectodomain of the luteinizing hormone receptor interacts with exoloop 2 to constrain the transmembrane region: studies using chimeric human and fly receptors. J. Biol. Chem. 277, 3958-3964.
    • (2002) J. Biol. Chem , vol.277 , pp. 3958-3964
    • Nishi, S.1    Nakabayashi, K.2    Kobilka, B.3    Hsueh, A.J.4
  • 55
    • 18744411809 scopus 로고    scopus 로고
    • The second extracellular loop: A damper for G protein-coupled receptors?
    • Massotte, D. and Kieffer, B. L. (2005) The second extracellular loop: a damper for G protein-coupled receptors? Nat. Struct. Mol. Biol. 12, 287-288.
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 287-288
    • Massotte, D.1    Kieffer, B.L.2
  • 56
    • 1642618157 scopus 로고    scopus 로고
    • Substitutions of tyrosine 601 in the human thyrotropin receptor result in increase or loss of basal activation of the cyclic adenosine monophosphate pathway and disrupt coupling to Gq/11
    • Arseven, O. K., Wilkes, W. P., Jameson, J. L., and Kopp, P. (2000) Substitutions of tyrosine 601 in the human thyrotropin receptor result in increase or loss of basal activation of the cyclic adenosine monophosphate pathway and disrupt coupling to Gq/11. Thyroid 10, 3-10.
    • (2000) Thyroid , vol.10 , pp. 3-10
    • Arseven, O.K.1    Wilkes, W.P.2    Jameson, J.L.3    Kopp, P.4
  • 59
    • 33646404622 scopus 로고    scopus 로고
    • Melanocortin 4 receptor mutations in a large cohort of severely obese adults: Prevalence, functional classification, genotype-phenotype relationship, and lack of association with binge eating
    • Lubrano-Berthelier, C., Dubern, B., Lacorte, J. M., Picard, F., Shapiro, A., Zhang, S., Bertrais, S., Hercberg, S., Basdevant, A., Clement, K., and Vaisse, C. (2006) Melanocortin 4 receptor mutations in a large cohort of severely obese adults: prevalence, functional classification, genotype-phenotype relationship, and lack of association with binge eating. J. Clin. Endocrinol. Metab. 91, 1811-1818.
    • (2006) J. Clin. Endocrinol. Metab , vol.91 , pp. 1811-1818
    • Lubrano-Berthelier, C.1    Dubern, B.2    Lacorte, J.M.3    Picard, F.4    Shapiro, A.5    Zhang, S.6    Bertrais, S.7    Hercberg, S.8    Basdevant, A.9    Clement, K.10    Vaisse, C.11
  • 60
    • 33644658516 scopus 로고    scopus 로고
    • Ghrelin receptor mutations-too little height and too much hunger
    • Holst, B. and Schwartz, T. W. (2006) Ghrelin receptor mutations-too little height and too much hunger. J. Clin. Invest. 116, 637-641.
    • (2006) J. Clin. Invest , vol.116 , pp. 637-641
    • Holst, B.1    Schwartz, T.W.2
  • 63
    • 35348858942 scopus 로고    scopus 로고
    • Garcia-Jimenez, C. and Santisteban, P. (2007) TSH signalling and cancer. Arq Bras. Endocrinol. Metabol. 51, 654-671.
    • Garcia-Jimenez, C. and Santisteban, P. (2007) TSH signalling and cancer. Arq Bras. Endocrinol. Metabol. 51, 654-671.
  • 64
    • 33746527488 scopus 로고    scopus 로고
    • Inactivating mutations of G protein-coupled receptors and diseases: Structure-function insights and therapeutic implications
    • Tao, Y. X. (2006) Inactivating mutations of G protein-coupled receptors and diseases: structure-function insights and therapeutic implications. Pharmacol. Ther. 111, 949-973.
    • (2006) Pharmacol. Ther , vol.111 , pp. 949-973
    • Tao, Y.X.1
  • 65
    • 0030601152 scopus 로고    scopus 로고
    • Constitutively activating mutations of the thyrotropin receptor and thyroid disease
    • Fuhrer, D., Holzapfel, H. P., Wonerow, P., and Paschke, R. (1996) Constitutively activating mutations of the thyrotropin receptor and thyroid disease. Eur. J. Med. Res. 1, 460-464.
    • (1996) Eur. J. Med. Res , vol.1 , pp. 460-464
    • Fuhrer, D.1    Holzapfel, H.P.2    Wonerow, P.3    Paschke, R.4
  • 66
    • 23644456322 scopus 로고    scopus 로고
    • Thyrotropin receptor-associated diseases: From adenomata to Graves disease
    • Davies, T. F., Ando, T., Lin, R. Y., Tomer, Y., and Latif, R. (2005) Thyrotropin receptor-associated diseases: from adenomata to Graves disease. J. Clin. Invest 115, 1972-1983.
    • (2005) J. Clin. Invest , vol.115 , pp. 1972-1983
    • Davies, T.F.1    Ando, T.2    Lin, R.Y.3    Tomer, Y.4    Latif, R.5
  • 68
    • 0031457992 scopus 로고    scopus 로고
    • The follicle-stimulating hormone receptor: Biochemistry, molecular biology, physiology, and pathophysiology
    • Simoni, M., Gromoll, J., and 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
  • 69
    • 0033823170 scopus 로고    scopus 로고
    • Activating and inactivating hormone receptor mutations
    • Huhtaniemi, I. (2000) Activating and inactivating hormone receptor mutations. Horm. Res. 53 Suppl 3, 9-16.
    • (2000) Horm. Res , vol.53 , Issue.SUPPL. 3 , pp. 9-16
    • Huhtaniemi, I.1
  • 70
    • 0033711033 scopus 로고    scopus 로고
    • Mutations of gonadotropins and gonadotropin receptors: Elucidating the physiology and pathophysiology of pituitary-gonadal function
    • Themmen, A. P. N. and Huhtaniemi, I. T. (2000) Mutations of gonadotropins and gonadotropin receptors: elucidating the physiology and pathophysiology of pituitary-gonadal function. Endocr. Rev. 21, 551-583.
    • (2000) Endocr. Rev , vol.21 , pp. 551-583
    • Themmen, A.P.N.1    Huhtaniemi, I.T.2
  • 71
    • 0027409289 scopus 로고
    • Acquired ocular visual impairment in children. 1960-1989
    • Robinson, G. C. and Jan, J. E. (1993) Acquired ocular visual impairment in children. 1960-1989. Am. J. Dis. Child 147, 325-328.
    • (1993) Am. J. Dis. Child , vol.147 , pp. 325-328
    • Robinson, G.C.1    Jan, J.E.2
  • 72
    • 29444444012 scopus 로고    scopus 로고
    • Vilardaga, J. P., Steinmeyer, R., Harms, G. S., and Lohse, M. J. (2005) Molecular basis of inverse agonism in a G protein-coupled receptor. Nat. Chem. Biol. 1, 25-28.
    • Vilardaga, J. P., Steinmeyer, R., Harms, G. S., and Lohse, M. J. (2005) Molecular basis of inverse agonism in a G protein-coupled receptor. Nat. Chem. Biol. 1, 25-28.


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