메뉴 건너뛰기




Volumn 382, Issue 1, 2014, Pages 424-451

Structural biology of glycoprotein hormones and their receptors: Insights to signaling

Author keywords

'Seat' sequence; Allosteric modulator; GPCR trimer; LRR curvature estimation; Receptor activation mechanism; Reproductive

Indexed keywords

CHORIONIC GONADOTROPIN; CYSTINE KNOT GROWTH FACTOR; FOLLITROPIN; FOLLITROPIN RECEPTOR; G PROTEIN COUPLED RECEPTOR; GLYCOPROTEIN; GLYCOPROTEIN HORMONE; GLYCOPROTEIN HORMONE RECEPTOR; GROWTH FACTOR; HORMONE RECEPTOR; PEPTIDE HORMONE; TYROSINE; UNCLASSIFIED DRUG;

EID: 84888287689     PISSN: 03037207     EISSN: 18728057     Source Type: Journal    
DOI: 10.1016/j.mce.2013.08.021     Document Type: Review
Times cited : (160)

References (264)
  • 1
    • 59149099367 scopus 로고    scopus 로고
    • Critical involvement of the hinge region of the follicle-stimulating hormone receptor in the activation of the receptor
    • Agrawal G., Dighe R.R. Critical involvement of the hinge region of the follicle-stimulating hormone receptor in the activation of the receptor. J. Biol. Chem. 2009, 284:2636-2647.
    • (2009) J. Biol. Chem. , vol.284 , pp. 2636-2647
    • Agrawal, G.1    Dighe, R.R.2
  • 3
    • 24644449168 scopus 로고    scopus 로고
    • Main-chain conformational tendencies of amino acids
    • Anderson R.J., Weng Z., Campbell R.K., Jiang X. Main-chain conformational tendencies of amino acids. Proteins 2005, 60:679-689.
    • (2005) Proteins , vol.60 , pp. 679-689
    • Anderson, R.J.1    Weng, Z.2    Campbell, R.K.3    Jiang, X.4
  • 4
    • 0032539644 scopus 로고    scopus 로고
    • The human follitropin alpha-subunit C terminus collaborates with a beta-subunit cystine noose and an alpha-subunit loop to assemble a receptor-binding domain competent for signal transduction
    • Arnold C.J., Liu C., Lindau-Shepard B., Losavio M.L., Patrascu M.T., Dias J.A. The human follitropin alpha-subunit C terminus collaborates with a beta-subunit cystine noose and an alpha-subunit loop to assemble a receptor-binding domain competent for signal transduction. Biochemistry 1998, 37:1762-1768.
    • (1998) Biochemistry , vol.37 , pp. 1762-1768
    • Arnold, C.J.1    Liu, C.2    Lindau-Shepard, B.3    Losavio, M.L.4    Patrascu, M.T.5    Dias, J.A.6
  • 5
    • 8544259258 scopus 로고
    • Hypophysenvorderlappenhormon und Ovarialhormon im Harn von Schwangeren
    • Aschheim S., Zondek B. Hypophysenvorderlappenhormon und Ovarialhormon im Harn von Schwangeren. Klin. Wochenschr. 1927, 6:1322.
    • (1927) Klin. Wochenschr. , vol.6 , pp. 1322
    • Aschheim, S.1    Zondek, B.2
  • 6
    • 8844282885 scopus 로고
    • Ueber die Beziehungen zwischen Hypophysis und Genitale
    • Aschner B. Ueber die Beziehungen zwischen Hypophysis und Genitale. Arch. Gynäkol. 1912, 97:200-227.
    • (1912) Arch. Gynäkol. , vol.97 , pp. 200-227
    • Aschner, B.1
  • 7
    • 0001581868 scopus 로고
    • Glycosylation and glycoprotein hormone function
    • Springer-Verlag, New York, J.W.P.D. Lustbader, R.W. Ruddon (Eds.)
    • Baenziger J.U. Glycosylation and glycoprotein hormone function. Glycoprotein Hormones: Structure, Function and Clinical Implications 1994, Springer-Verlag, New York, pp. 167-174. J.W.P.D. Lustbader, R.W. Ruddon (Eds.).
    • (1994) Glycoprotein Hormones: Structure, Function and Clinical Implications , pp. 167-174
    • Baenziger, J.U.1
  • 8
    • 34447509986 scopus 로고    scopus 로고
    • Transducin activation by nanoscale lipid bilayers containing one and two rhodopsins
    • Bayburt T.H., Leitz A.J., Xie G., Oprian D.D., Sligar S.G. Transducin activation by nanoscale lipid bilayers containing one and two rhodopsins. J. Biol. Chem. 2007, 282:14875-14881.
    • (2007) J. Biol. Chem. , vol.282 , pp. 14875-14881
    • Bayburt, T.H.1    Leitz, A.J.2    Xie, G.3    Oprian, D.D.4    Sligar, S.G.5
  • 9
    • 0030462561 scopus 로고    scopus 로고
    • Crystal structure of a coagulogen, the clotting protein from horseshoe crab: a structural homologue of nerve growth factor
    • Bergner A., Oganessyan V., Muta T., Iwanaga S., Typke D., Huber R., Bode W. Crystal structure of a coagulogen, the clotting protein from horseshoe crab: a structural homologue of nerve growth factor. EMBO J. 1996, 15:6789-6797.
    • (1996) EMBO J. , vol.15 , pp. 6789-6797
    • Bergner, A.1    Oganessyan, V.2    Muta, T.3    Iwanaga, S.4    Typke, D.5    Huber, R.6    Bode, W.7
  • 12
    • 0029757509 scopus 로고    scopus 로고
    • Determination of residues important in hormone binding to the extracellular domain of the luteinizing hormone/chorionic gonadotropin receptor by site-directed mutagenesis and modeling
    • Bhowmick N., Huang J., Puett D., Isaacs N.W., Lapthorn A.J. Determination of residues important in hormone binding to the extracellular domain of the luteinizing hormone/chorionic gonadotropin receptor by site-directed mutagenesis and modeling. Mol. Endocrinol. 1996, 10:1147-1159.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 1147-1159
    • Bhowmick, N.1    Huang, J.2    Puett, D.3    Isaacs, N.W.4    Lapthorn, A.J.5
  • 14
    • 0025280694 scopus 로고
    • Carbohydrate composition of the α-subunit of human choriogonadotropin (hCGα) and the free α molecules produced in pregnancy: most free α and some combined hCGα molecules are fucosylated
    • Blithe D.L. Carbohydrate composition of the α-subunit of human choriogonadotropin (hCGα) and the free α molecules produced in pregnancy: most free α and some combined hCGα molecules are fucosylated. Endocrinology 1990, 126:2788-2799.
    • (1990) Endocrinology , vol.126 , pp. 2788-2799
    • Blithe, D.L.1
  • 15
    • 0026045952 scopus 로고
    • Free alpha molecules from pregnancy stimulate secretion of prolactin from human decidual cells: a novel function for free alpha in pregnancy
    • Blithe D.L., Richards R.G., Skarulis M.C. Free alpha molecules from pregnancy stimulate secretion of prolactin from human decidual cells: a novel function for free alpha in pregnancy. Endocrinology 1991, 129:2257-2259.
    • (1991) Endocrinology , vol.129 , pp. 2257-2259
    • Blithe, D.L.1    Richards, R.G.2    Skarulis, M.C.3
  • 16
    • 0033118334 scopus 로고    scopus 로고
    • Molecular tinkering of G protein-coupled receptors: an evolutionary success
    • Bockaert J., Pin J.P. Molecular tinkering of G protein-coupled receptors: an evolutionary success. EMBO J. 1999, 18:1723-1729.
    • (1999) EMBO J. , vol.18 , pp. 1723-1729
    • Bockaert, J.1    Pin, J.P.2
  • 17
    • 33751530407 scopus 로고    scopus 로고
    • Structural differences in the hinge region of the glycoprotein hormone receptors: evidence from the sulfated tyrosine residues
    • Bonomi M., Busnelli M., Persani L., Vassart G., Costagliola S. Structural differences in the hinge region of the glycoprotein hormone receptors: evidence from the sulfated tyrosine residues. Mol. Endocrinol. 2006, 20:3351-3363.
    • (2006) Mol. Endocrinol. , vol.20 , pp. 3351-3363
    • Bonomi, M.1    Busnelli, M.2    Persani, L.3    Vassart, G.4    Costagliola, S.5
  • 18
    • 34248998448 scopus 로고    scopus 로고
    • Sick leave for follow-up control in thyroid cancer patients: comparison between stimulation with Thyrogen and thyroid hormone withdrawal
    • Borget I., Corone C., Nocaudie M., Allyn M., Iacobelli S., Schlumberger M., De Pouvourville G. Sick leave for follow-up control in thyroid cancer patients: comparison between stimulation with Thyrogen and thyroid hormone withdrawal. Eur. J. Endocrinol. 2007, 156:531-538.
    • (2007) Eur. J. Endocrinol. , vol.156 , pp. 531-538
    • Borget, I.1    Corone, C.2    Nocaudie, M.3    Allyn, M.4    Iacobelli, S.5    Schlumberger, M.6    De Pouvourville, G.7
  • 20
    • 0025847496 scopus 로고
    • Amino-terminal leucine-rich repeats in gonadotropin receptors determine hormone selectivity
    • Braun T., Schofield P.R., Sprengel R. Amino-terminal leucine-rich repeats in gonadotropin receptors determine hormone selectivity. EMBO J. 1991, 10:1885-1890.
    • (1991) EMBO J. , vol.10 , pp. 1885-1890
    • Braun, T.1    Schofield, P.R.2    Sprengel, R.3
  • 21
    • 30044433479 scopus 로고    scopus 로고
    • Promoter cloning and characterisation of the transcriptional regulation of the human thyrostimulin A2 subunit
    • Breous E., Wenzel A., Loos U. Promoter cloning and characterisation of the transcriptional regulation of the human thyrostimulin A2 subunit. Mol. Cell. Endocrinol. 2005, 245:169-180.
    • (2005) Mol. Cell. Endocrinol. , vol.245 , pp. 169-180
    • Breous, E.1    Wenzel, A.2    Loos, U.3
  • 23
    • 54449086544 scopus 로고    scopus 로고
    • Asp330 and Tyr331 in the C-terminal cysteine-rich region of the luteinizing hormone receptor are key residues in hormone-induced receptor activation
    • Bruysters M., Verhoef-Post M., Themmen A.P. Asp330 and Tyr331 in the C-terminal cysteine-rich region of the luteinizing hormone receptor are key residues in hormone-induced receptor activation. J. Biol. Chem. 2008, 283:25821-25828.
    • (2008) J. Biol. Chem. , vol.283 , pp. 25821-25828
    • Bruysters, M.1    Verhoef-Post, M.2    Themmen, A.P.3
  • 24
    • 0015251023 scopus 로고
    • Primary structure of the ovine hypothalamic luteinizing hormone-releasing factor (LRF) (LH-hypothalamus-LRF-gas chromatography-mass spectrometry-decapeptide-Edman degradation)
    • Burgus R., Butcher M., Amoss M., Ling N., Monahan M., Rivier J., Fellows R., Blackwell R., Vale W., Guillemin R. Primary structure of the ovine hypothalamic luteinizing hormone-releasing factor (LRF) (LH-hypothalamus-LRF-gas chromatography-mass spectrometry-decapeptide-Edman degradation). Proc. Natl. Acad. Sci. USA 1972, 69:278-282.
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 278-282
    • Burgus, R.1    Butcher, M.2    Amoss, M.3    Ling, N.4    Monahan, M.5    Rivier, J.6    Fellows, R.7    Blackwell, R.8    Vale, W.9    Guillemin, R.10
  • 25
    • 0036121842 scopus 로고    scopus 로고
    • Truncated equine LH beta and asparagine(56)-deglycosylated equine LH alpha combine to produce a potent FSH antagonist
    • Butnev V.Y., Singh V., Nguyen V.T., Bousfield G.R. Truncated equine LH beta and asparagine(56)-deglycosylated equine LH alpha combine to produce a potent FSH antagonist. J. Endocrinol. 2002, 172:545-555.
    • (2002) J. Endocrinol. , vol.172 , pp. 545-555
    • Butnev, V.Y.1    Singh, V.2    Nguyen, V.T.3    Bousfield, G.R.4
  • 26
    • 0026081701 scopus 로고
    • Conversion of human choriogonadotropin into a follitropin by protein engineering
    • Campbell R.K., Dean-Emig D.M., Moyle W.R. Conversion of human choriogonadotropin into a follitropin by protein engineering. Proc. Natl. Acad. Sci. USA 1991, 88:760-764.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 760-764
    • Campbell, R.K.1    Dean-Emig, D.M.2    Moyle, W.R.3
  • 27
    • 0028103275 scopus 로고
    • CCP4, The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D: Biol. Crystallogr.
    • CCP4, 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D: Biol. Crystallogr. 50, 760-763.
    • (1994) , vol.50 , pp. 760-763
  • 28
    • 0031710845 scopus 로고    scopus 로고
    • Follicle stimulating hormone and its receptor: future perspectives
    • Chappel S., Buckler D., Kelton C., Tayar N.E. Follicle stimulating hormone and its receptor: future perspectives. Hum. Reprod. 1998, 13(Suppl. 3):18-35.
    • (1998) Hum. Reprod. , vol.13 , Issue.3 SUPPL. , pp. 18-35
    • Chappel, S.1    Buckler, D.2    Kelton, C.3    Tayar, N.E.4
  • 29
    • 0025720537 scopus 로고
    • Contributions of arginines-43 and -94 of human choriogonadotropin beta to receptor binding and activation as determined by oligonucleotide-based mutagenesis
    • Chen F., Puett D. Contributions of arginines-43 and -94 of human choriogonadotropin beta to receptor binding and activation as determined by oligonucleotide-based mutagenesis. Biochemistry 1991, 30:10171-10175.
    • (1991) Biochemistry , vol.30 , pp. 10171-10175
    • Chen, F.1    Puett, D.2
  • 30
    • 0026635335 scopus 로고
    • The carboxy-terminal region of the glycoprotein hormone alpha-subunit: contributions to receptor binding and signaling in human chorionic gonadotropin
    • Chen F., Wang Y., Puett D. The carboxy-terminal region of the glycoprotein hormone alpha-subunit: contributions to receptor binding and signaling in human chorionic gonadotropin. Mol. Endocrinol. 1992, 6:914-919.
    • (1992) Mol. Endocrinol. , vol.6 , pp. 914-919
    • Chen, F.1    Wang, Y.2    Puett, D.3
  • 31
    • 0042421851 scopus 로고    scopus 로고
    • Evidence that the C terminus of the A subunit suppresses thyrotropin receptor constitutive activity
    • Chen C.R., Chazenbalk G.D., McLachlan S.M., Rapoport B. Evidence that the C terminus of the A subunit suppresses thyrotropin receptor constitutive activity. Endocrinology 2003, 144:3821-3827.
    • (2003) Endocrinology , vol.144 , pp. 3821-3827
    • Chen, C.R.1    Chazenbalk, G.D.2    McLachlan, S.M.3    Rapoport, B.4
  • 32
    • 77950194483 scopus 로고    scopus 로고
    • Thyrotropin (TSH) receptor residue E251 in the extracellular leucine-rich repeat domain is critical for linking TSH binding to receptor activation
    • Chen C.R., McLachlan S.M., Rapoport B. Thyrotropin (TSH) receptor residue E251 in the extracellular leucine-rich repeat domain is critical for linking TSH binding to receptor activation. Endocrinology 2010, 151:1940-1947.
    • (2010) Endocrinology , vol.151 , pp. 1940-1947
    • Chen, C.R.1    McLachlan, S.M.2    Rapoport, B.3
  • 33
    • 79952790394 scopus 로고    scopus 로고
    • Evidence that the thyroid-stimulating hormone (TSH) receptor transmembrane domain influences kinetics of TSH binding to the receptor ectodomain
    • Chen C.R., McLachlan S.M., Rapoport B. Evidence that the thyroid-stimulating hormone (TSH) receptor transmembrane domain influences kinetics of TSH binding to the receptor ectodomain. J. Biol. Chem. 2011, 286:6219-6224.
    • (2011) J. Biol. Chem. , vol.286 , pp. 6219-6224
    • Chen, C.R.1    McLachlan, S.M.2    Rapoport, B.3
  • 34
    • 84884503107 scopus 로고    scopus 로고
    • Platelet-derived growth factors and their receptors: structural and functional perspectives
    • doi: 10.1016/j.bbapap.2012.10.015
    • Chen P.-H., Chen X., He X. Platelet-derived growth factors and their receptors: structural and functional perspectives. Biochim. Biophy. Acta (BBA) - Proteins Proteomics 2012, doi: 10.1016/j.bbapap.2012.10.015.
    • (2012) Biochim. Biophy. Acta (BBA) - Proteins Proteomics
    • Chen, P.-H.1    Chen, X.2    He, X.3
  • 35
    • 84879160899 scopus 로고    scopus 로고
    • The structural basis of R-spondin recognition by LGR5 and RNF43
    • Chen P.-H., Chen X., Lin Z., Fang D., He X. The structural basis of R-spondin recognition by LGR5 and RNF43. Genes Dev 2013, 27:1345-1350.
    • (2013) Genes Dev , vol.27 , pp. 1345-1350
    • Chen, P.-H.1    Chen, X.2    Lin, Z.3    Fang, D.4    He, X.5
  • 36
    • 0026347382 scopus 로고
    • The biological and clinical significance of nicks in human chorionic gonadotropin and its free beta-subunit
    • Cole L.A., Kardana A., Ying F.C., Birken S. The biological and clinical significance of nicks in human chorionic gonadotropin and its free beta-subunit. Yale J. Biol. Med. 1991, 64:627-637.
    • (1991) Yale J. Biol. Med. , vol.64 , pp. 627-637
    • Cole, L.A.1    Kardana, A.2    Ying, F.C.3    Birken, S.4
  • 38
    • 33746015378 scopus 로고    scopus 로고
    • Gestational trophoblastic diseases: 3. Human chorionic gonadotropin-free beta-subunit, a reliable marker of placental site trophoblastic tumors
    • Cole L.A., Khanlian S.A., Muller C.Y., Giddings A., Kohorn E., Berkowitz R. Gestational trophoblastic diseases: 3. Human chorionic gonadotropin-free beta-subunit, a reliable marker of placental site trophoblastic tumors. Gynecol. Oncol. 2006, 102:160-164.
    • (2006) Gynecol. Oncol. , vol.102 , pp. 160-164
    • Cole, L.A.1    Khanlian, S.A.2    Muller, C.Y.3    Giddings, A.4    Kohorn, E.5    Berkowitz, R.6
  • 39
    • 28644438570 scopus 로고    scopus 로고
    • An intuitive approach to measuring protein surface curvature
    • Coleman R.G., Burr M.A., Souvaine D.L., Cheng A.C. An intuitive approach to measuring protein surface curvature. Proteins 2005, 61:1068-1074.
    • (2005) Proteins , vol.61 , pp. 1068-1074
    • Coleman, R.G.1    Burr, M.A.2    Souvaine, D.L.3    Cheng, A.C.4
  • 40
    • 0026440307 scopus 로고
    • Molecular basis of the specificity of binding of glycoprotein hormones to their receptors
    • Combarnous Y. Molecular basis of the specificity of binding of glycoprotein hormones to their receptors. Endocr. Rev. 1992, 13:670-691.
    • (1992) Endocr. Rev. , vol.13 , pp. 670-691
    • Combarnous, Y.1
  • 41
    • 0016221603 scopus 로고
    • Studies on the disulfide bonds of glycoprotein hormones. Locations in the alpha chain based on partial reductions and formation of 14C-labeled S-carboxymethyl derivatives
    • Cornell J.S., Pierce J.G. Studies on the disulfide bonds of glycoprotein hormones. Locations in the alpha chain based on partial reductions and formation of 14C-labeled S-carboxymethyl derivatives. J. Biol. Chem. 1974, 249:4166-4174.
    • (1974) J. Biol. Chem. , vol.249 , pp. 4166-4174
    • Cornell, J.S.1    Pierce, J.G.2
  • 42
    • 0037084011 scopus 로고    scopus 로고
    • Tyrosine sulfation is required for agonist recognition by glycoprotein hormone receptors
    • Costagliola S., Panneels V., Bonomi M., Koch J., Many M.C., Smits G., Vassart G. Tyrosine sulfation is required for agonist recognition by glycoprotein hormone receptors. EMBO J. 2002, 21:504-513.
    • (2002) EMBO J. , vol.21 , pp. 504-513
    • Costagliola, S.1    Panneels, V.2    Bonomi, M.3    Koch, J.4    Many, M.C.5    Smits, G.6    Vassart, G.7
  • 45
    • 33845720603 scopus 로고    scopus 로고
    • Asymmetric conformational changes in a GPCR dimer controlled by G-proteins
    • Damian M., Martin A., Mesnier D., Pin J.P., Baneres J.L. Asymmetric conformational changes in a GPCR dimer controlled by G-proteins. EMBO J. 2006, 25:5693-5702.
    • (2006) EMBO J. , vol.25 , pp. 5693-5702
    • Damian, M.1    Martin, A.2    Mesnier, D.3    Pin, J.P.4    Baneres, J.L.5
  • 46
    • 0027122245 scopus 로고
    • Crystal structure of transforming growth factor-beta 2: an unusual fold for the superfamily
    • Daopin S., Piez K.A., Ogawa Y., Davies D.R. Crystal structure of transforming growth factor-beta 2: an unusual fold for the superfamily. Science 1992, 257:369-373.
    • (1992) Science , vol.257 , pp. 369-373
    • Daopin, S.1    Piez, K.A.2    Ogawa, Y.3    Davies, D.R.4
  • 47
    • 0026702741 scopus 로고
    • The size of the mature membrane receptor for follicle-stimulating hormone is larger than that predicted from its cDNA
    • Dattatreyamurty B., Smith R.A., Zhang S.B., Santa-Coloma T.A., Reichert L.E. The size of the mature membrane receptor for follicle-stimulating hormone is larger than that predicted from its cDNA. J. Mol. Endocrinol. 1992, 9:115-121.
    • (1992) J. Mol. Endocrinol. , vol.9 , pp. 115-121
    • Dattatreyamurty, B.1    Smith, R.A.2    Zhang, S.B.3    Santa-Coloma, T.A.4    Reichert, L.E.5
  • 49
    • 0026656681 scopus 로고
    • Recent progress in structure-function and molecular analyses of the pituitary/placental glycoprotein hormone receptors
    • Dias J.A. Recent progress in structure-function and molecular analyses of the pituitary/placental glycoprotein hormone receptors. Biochim. Biophys. Acta 1992, 1135:287-294.
    • (1992) Biochim. Biophys. Acta , vol.1135 , pp. 287-294
    • Dias, J.A.1
  • 50
    • 12744279354 scopus 로고    scopus 로고
    • Endocrinology: fertility hormone in repose
    • Dias J.A. Endocrinology: fertility hormone in repose. Nature 2005, 433:203-204.
    • (2005) Nature , vol.433 , pp. 203-204
    • Dias, J.A.1
  • 51
    • 0027999473 scopus 로고
    • Receptor binding and functional properties of chimeric human follitropin prepared by an exchange between a small hydrophilic intercysteine loop of human follitropin and human lutropin
    • Dias J.A., Zhang Y., Liu X. Receptor binding and functional properties of chimeric human follitropin prepared by an exchange between a small hydrophilic intercysteine loop of human follitropin and human lutropin. J. Biol. Chem. 1994, 269:25289-25294.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25289-25294
    • Dias, J.A.1    Zhang, Y.2    Liu, X.3
  • 52
    • 0031811584 scopus 로고    scopus 로고
    • Human follicle-stimulating hormone structure-activity relationships
    • Dias J.A., Lindau-Shepard B., Hauer C., Auger I. Human follicle-stimulating hormone structure-activity relationships. Biol. Reprod. 1998, 58:1331-1336.
    • (1998) Biol. Reprod. , vol.58 , pp. 1331-1336
    • Dias, J.A.1    Lindau-Shepard, B.2    Hauer, C.3    Auger, I.4
  • 55
    • 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., Vassart G. Constitutive activation of the TSH receptor by spontaneous mutations affecting the N-terminal extracellular domain. FEBS Lett. 1997, 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
  • 58
    • 0034705002 scopus 로고    scopus 로고
    • Effects of the N-linked glycans on the 3D structure of the free alpha-subunit of human chorionic gonadotropin
    • Erbel P.J., Karimi-Nejad Y., van Kuik J.A., Boelens R., Kamerling J.P., Vliegenthart J.F. Effects of the N-linked glycans on the 3D structure of the free alpha-subunit of human chorionic gonadotropin. Biochemistry 2000, 39:6012-6021.
    • (2000) Biochemistry , vol.39 , pp. 6012-6021
    • Erbel, P.J.1    Karimi-Nejad, Y.2    van Kuik, J.A.3    Boelens, R.4    Kamerling, J.P.5    Vliegenthart, J.F.6
  • 60
    • 34547434085 scopus 로고    scopus 로고
    • Monomeric G protein-coupled receptor rhodopsin in solution activates its G protein transducin at the diffusion limit
    • Ernst O.P., Gramse V., Kolbe M., Hofmann K.P., Heck M. Monomeric G protein-coupled receptor rhodopsin in solution activates its G protein transducin at the diffusion limit. Proc. Natl. Acad. Sci. USA 2007, 104:10859-10864.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 10859-10864
    • Ernst, O.P.1    Gramse, V.2    Kolbe, M.3    Hofmann, K.P.4    Heck, M.5
  • 61
    • 12744280744 scopus 로고    scopus 로고
    • Structure of human follicle-stimulating hormone in complex with its receptor
    • Fan Q.R., Hendrickson W.A. Structure of human follicle-stimulating hormone in complex with its receptor. Nature 2005, 433:269-277.
    • (2005) Nature , vol.433 , pp. 269-277
    • Fan, Q.R.1    Hendrickson, W.A.2
  • 62
    • 33751243638 scopus 로고    scopus 로고
    • Assembly and structural characterization of an authentic complex between human follicle stimulating hormone and a hormone-binding ectodomain of its receptor
    • Fan Q.R., Hendrickson W.A. Assembly and structural characterization of an authentic complex between human follicle stimulating hormone and a hormone-binding ectodomain of its receptor. Mol. Cell. Endocrinol. 2007, 260:73-82.
    • (2007) Mol. Cell. Endocrinol. , vol.260 , pp. 73-82
    • Fan, Q.R.1    Hendrickson, W.A.2
  • 63
    • 33646108350 scopus 로고    scopus 로고
    • The role of O-linked and N-linked oligosaccharides on the structure-function of glycoprotein hormones: development of agonists and antagonists
    • Fares F. The role of O-linked and N-linked oligosaccharides on the structure-function of glycoprotein hormones: development of agonists and antagonists. Biochim. Biophys. Acta 2006, 1760:560-567.
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 560-567
    • Fares, F.1
  • 64
    • 0026551294 scopus 로고
    • Design of a long-acting follitropin agonist by fusing the C-terminal sequence of the chorionic gonadotropin beta subunit to the follitropin beta subunit
    • Fares F.A., Suganuma N., Nishimori K., LaPolt P.S., Hsueh A.J., Boime I. Design of a long-acting follitropin agonist by fusing the C-terminal sequence of the chorionic gonadotropin beta subunit to the follitropin beta subunit. Proc. Natl. Acad. Sci. USA 1992, 89:4304-4308.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4304-4308
    • Fares, F.A.1    Suganuma, N.2    Nishimori, K.3    LaPolt, P.S.4    Hsueh, A.J.5    Boime, I.6
  • 65
    • 0028861254 scopus 로고
    • Asparagine-linked oligosaccharides facilitate human chorionic gonadotropin beta-subunit folding but not assembly of prefolded beta with alpha
    • Feng W., Huth J.R., Norton S.E., Ruddon R.W. Asparagine-linked oligosaccharides facilitate human chorionic gonadotropin beta-subunit folding but not assembly of prefolded beta with alpha. Endocrinology 1995, 136:52-61.
    • (1995) Endocrinology , vol.136 , pp. 52-61
    • Feng, W.1    Huth, J.R.2    Norton, S.E.3    Ruddon, R.W.4
  • 66
    • 0029040839 scopus 로고
    • The asparagine-linked oligosaccharides of the human chorionic gonadotropin beta subunit facilitate correct disulfide bond pairing
    • Feng W., Matzuk M.M., Mountjoy K., Bedows E., Ruddon R.W., Boime I. The asparagine-linked oligosaccharides of the human chorionic gonadotropin beta subunit facilitate correct disulfide bond pairing. J. Biol. Chem. 1995, 270:11851-11859.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11851-11859
    • Feng, W.1    Matzuk, M.M.2    Mountjoy, K.3    Bedows, E.4    Ruddon, R.W.5    Boime, I.6
  • 67
    • 0000302448 scopus 로고
    • The gonad stimulating and the luteinizing hormones of the anterior lobe of the hypophesis
    • Fevold H.L., Hisaw F.L., Leonard S.L. The gonad stimulating and the luteinizing hormones of the anterior lobe of the hypophesis. Am. J. Physiol. 1931, 97:291-301.
    • (1931) Am. J. Physiol. , vol.97 , pp. 291-301
    • Fevold, H.L.1    Hisaw, F.L.2    Leonard, S.L.3
  • 68
    • 0019166519 scopus 로고
    • The cDNA for the beta-subunit of human chorionic gonadotropin suggests evolution of a gene by readthrough into the 3'-untranslated region
    • Fiddes J.C., Goodman H.M. The cDNA for the beta-subunit of human chorionic gonadotropin suggests evolution of a gene by readthrough into the 3'-untranslated region. Nature 1980, 286:684-687.
    • (1980) Nature , vol.286 , pp. 684-687
    • Fiddes, J.C.1    Goodman, H.M.2
  • 70
    • 0035105355 scopus 로고    scopus 로고
    • Three-dimensional structure of human follicle-stimulating hormone
    • Fox K.M., Dias J.A., Van Roey P. Three-dimensional structure of human follicle-stimulating hormone. Mol. Endocrinol. 2001, 15:378-389.
    • (2001) Mol. Endocrinol. , vol.15 , pp. 378-389
    • Fox, K.M.1    Dias, J.A.2    Van Roey, P.3
  • 71
    • 0038024615 scopus 로고    scopus 로고
    • The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints
    • Fredriksson R., Lagerstrom M.C., Lundin L.G., Schioth H.B. The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints. Mol. Pharmacol. 2003, 63:1256-1272.
    • (2003) Mol. Pharmacol. , vol.63 , pp. 1256-1272
    • Fredriksson, R.1    Lagerstrom, M.C.2    Lundin, L.G.3    Schioth, H.B.4
  • 72
    • 0019306186 scopus 로고
    • Studies on the disulfide bonds in human pituitary follicle-stimulating hormone
    • Fujiki Y., Rathnam P., Saxena B.B. Studies on the disulfide bonds in human pituitary follicle-stimulating hormone. Biochim. Biophys. Acta 1980, 624:428-435.
    • (1980) Biochim. Biophys. Acta , vol.624 , pp. 428-435
    • Fujiki, Y.1    Rathnam, P.2    Saxena, B.B.3
  • 73
    • 33751247356 scopus 로고    scopus 로고
    • The antigen binding sites of various hCG monoclonal antibodies show homology to different domains of LH receptor
    • Gadkari R.A., Sandhya S., Sowdhamini R., Dighe R.R. The antigen binding sites of various hCG monoclonal antibodies show homology to different domains of LH receptor. Mol. Cell. Endocrinol. 2007, 260-262:23-32.
    • (2007) Mol. Cell. Endocrinol. , pp. 23-32
    • Gadkari, R.A.1    Sandhya, S.2    Sowdhamini, R.3    Dighe, R.R.4
  • 74
    • 0008750202 scopus 로고
    • Molecular aspects of the subunit assembly of glycoprotein hormones
    • Plenum Press, New York, K.W. McKerns (Ed.)
    • Garnier J. Molecular aspects of the subunit assembly of glycoprotein hormones. Structure and Function of Gonadotropins 1978, 381-414. Plenum Press, New York. K.W. McKerns (Ed.).
    • (1978) Structure and Function of Gonadotropins , pp. 381-414
    • Garnier, J.1
  • 77
    • 0036780743 scopus 로고    scopus 로고
    • G-protein-coupled receptor oligomerization and its potential for drug discovery
    • George S.R., O'Dowd B.F., Lee S.P. G-protein-coupled receptor oligomerization and its potential for drug discovery. Nat. Rev. Drug Discov. 2002, 1:808-820.
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 808-820
    • George, S.R.1    O'Dowd, B.F.2    Lee, S.P.3
  • 78
    • 0034464742 scopus 로고    scopus 로고
    • Uncovering molecular mechanisms involved in activation of G protein-coupled receptors
    • Gether U. Uncovering molecular mechanisms involved in activation of G protein-coupled receptors. Endocr. Rev. 2000, 21:90-113.
    • (2000) Endocr. Rev. , vol.21 , pp. 90-113
    • Gether, U.1
  • 79
    • 0017176823 scopus 로고
    • Studies on the disulfide bonds of glycoprotein hormones. Complete reduction and reoxidation of the disulfide bonds of the alpha subunit of bovine luteinizing hormone
    • Giudice L.C., Pierce J.G. Studies on the disulfide bonds of glycoprotein hormones. Complete reduction and reoxidation of the disulfide bonds of the alpha subunit of bovine luteinizing hormone. J. Biol. Chem. 1976, 251:6392-6399.
    • (1976) J. Biol. Chem. , vol.251 , pp. 6392-6399
    • Giudice, L.C.1    Pierce, J.G.2
  • 80
    • 0018147290 scopus 로고
    • Studies on the reduction and reoxidation of the disulfide bonds of the alpha and beta subunits of human choriogonadotropin
    • Giudice L.C., Pierce J.G. Studies on the reduction and reoxidation of the disulfide bonds of the alpha and beta subunits of human choriogonadotropin. Biochim. Biophys. Acta 1978, 533:140-146.
    • (1978) Biochim. Biophys. Acta , vol.533 , pp. 140-146
    • Giudice, L.C.1    Pierce, J.G.2
  • 81
    • 0018800332 scopus 로고
    • Studies on the disulfide bonds of glycoprotein hormones. Formation and properties of 11,35-bis(S-alkyl) derivatives of the alpha subunit
    • Giudice L.C., Pierce J.G. Studies on the disulfide bonds of glycoprotein hormones. Formation and properties of 11,35-bis(S-alkyl) derivatives of the alpha subunit. J. Biol. Chem. 1979, 254:1164-1169.
    • (1979) J. Biol. Chem. , vol.254 , pp. 1164-1169
    • Giudice, L.C.1    Pierce, J.G.2
  • 82
    • 0002336164 scopus 로고
    • Ring closure and local conformational deformations of chain molecules
    • Go N., Scheraga H.A. Ring closure and local conformational deformations of chain molecules. Macromolecules 1970, 3:178-187.
    • (1970) Macromolecules , vol.3 , pp. 178-187
    • Go, N.1    Scheraga, H.A.2
  • 83
    • 6044267464 scopus 로고    scopus 로고
    • Discovery of the luteinizing hormone of the anterior pituitary gland
    • Goodman H.M. Discovery of the luteinizing hormone of the anterior pituitary gland. Am. J. Physiol. Endocrinol. Metab. 2004, 287:E818-E819.
    • (2004) Am. J. Physiol. Endocrinol. Metab. , vol.287
    • Goodman, H.M.1
  • 84
    • 0028624664 scopus 로고
    • Bending and curvature calculations in B-DNA
    • Goodsell D.S., Dickerson R.E. Bending and curvature calculations in B-DNA. Nucleic Acids Res. 1994, 22:5497-5503.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 5497-5503
    • Goodsell, D.S.1    Dickerson, R.E.2
  • 85
    • 0030586238 scopus 로고    scopus 로고
    • The structure and organization of the human follicle-stimulating hormone receptor (FSHR) gene
    • Gromoll J., Pekel E., Nieschlag E. The structure and organization of the human follicle-stimulating hormone receptor (FSHR) gene. Genomics 1996, 35:308-311.
    • (1996) Genomics , vol.35 , pp. 308-311
    • Gromoll, J.1    Pekel, E.2    Nieschlag, E.3
  • 86
    • 0029135420 scopus 로고
    • Role of the carboxy-terminal residues of the alpha-subunit in the expression and bioactivity of human thyroid-stimulating hormone
    • Grossmann M., Szkudlinski M.W., Zeng H., Kraiem Z., Ji I., Tropea J.E., Ji T.H., Weintraub B.D. Role of the carboxy-terminal residues of the alpha-subunit in the expression and bioactivity of human thyroid-stimulating hormone. Mol. Endocrinol. 1995, 9:948-958.
    • (1995) Mol. Endocrinol. , vol.9 , pp. 948-958
    • Grossmann, M.1    Szkudlinski, M.W.2    Zeng, H.3    Kraiem, Z.4    Ji, I.5    Tropea, J.E.6    Ji, T.H.7    Weintraub, B.D.8
  • 87
    • 0030969880 scopus 로고    scopus 로고
    • Substitution of the seat-belt region of the thyroid-stimulating hormone (TSH) beta-subunit with the corresponding regions of choriogonadotropin or follitropin confers luteotropic but not follitropic activity to chimeric TSH
    • Grossmann M., Szkudlinski M.W., Wong R., Dias J.A., Ji T.H., Weintraub B.D. Substitution of the seat-belt region of the thyroid-stimulating hormone (TSH) beta-subunit with the corresponding regions of choriogonadotropin or follitropin confers luteotropic but not follitropic activity to chimeric TSH. J. Biol. Chem. 1997, 272:15532-15540.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15532-15540
    • Grossmann, M.1    Szkudlinski, M.W.2    Wong, R.3    Dias, J.A.4    Ji, T.H.5    Weintraub, B.D.6
  • 89
    • 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., Gudermann T. Severe congenital hyperthyroidism caused by a germ-line neo mutation in the extracellular portion of the thyrotropin receptor. J. Clin. Endocrinol. Metab. 1998, 83:1431-1436.
    • (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
  • 90
    • 70450233609 scopus 로고    scopus 로고
    • Structural determinants underlying constitutive dimerization of unoccupied human follitropin receptors
    • Guan R., Wu X., Feng X., Zhang M., Hebert T.E., Segaloff D.L. Structural determinants underlying constitutive dimerization of unoccupied human follitropin receptors. Cell. Signal. 2010, 22:247-256.
    • (2010) Cell. Signal. , vol.22 , pp. 247-256
    • Guan, R.1    Wu, X.2    Feng, X.3    Zhang, M.4    Hebert, T.E.5    Segaloff, D.L.6
  • 91
    • 0014134935 scopus 로고
    • Chemistry and physiology of hypothalamic releasing factors for gonadotrophins
    • Guillemin R. Chemistry and physiology of hypothalamic releasing factors for gonadotrophins. Int. J. Fertil. 1967, 12:359-367.
    • (1967) Int. J. Fertil. , vol.12 , pp. 359-367
    • Guillemin, R.1
  • 92
    • 0026582231 scopus 로고
    • Synthetic peptides based upon a three-dimensional model for the receptor recognition site of follicle-stimulating hormone exhibit antagonistic or agonistic activity at low concentrations
    • Hage-van Noort M., Puijk W.C., Plasman H.H., Kuperus D., Schaaper W.M., Beekman N.J., Grootegoed J.A., Meloen R.H. Synthetic peptides based upon a three-dimensional model for the receptor recognition site of follicle-stimulating hormone exhibit antagonistic or agonistic activity at low concentrations. Proc. Natl. Acad. Sci. USA 1992, 89:3922-3926.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3922-3926
    • Hage-van Noort, M.1    Puijk, W.C.2    Plasman, H.H.3    Kuperus, D.4    Schaaper, W.M.5    Beekman, N.J.6    Grootegoed, J.A.7    Meloen, R.H.8
  • 93
    • 65249117514 scopus 로고    scopus 로고
    • Identifying and characterizing binding sites and assessing druggability
    • Halgren T.A. Identifying and characterizing binding sites and assessing druggability. J. Chem. Inf. Model. 2009, 49:377-389.
    • (2009) J. Chem. Inf. Model. , vol.49 , pp. 377-389
    • Halgren, T.A.1
  • 94
    • 0004398535 scopus 로고
    • Treatment of hypo-ovarianism by the sequential and cyclic administration of equine and chorionic gonadotropins-so-called one-two cylic gonadotropic therapy Summary of 5 years' results
    • Hamblen E.C., Davis C.D., Durham N.C. Treatment of hypo-ovarianism by the sequential and cyclic administration of equine and chorionic gonadotropins-so-called one-two cylic gonadotropic therapy Summary of 5 years' results. Am. J. Obstet. Gynecol. 1945, 50:137-146.
    • (1945) Am. J. Obstet. Gynecol. , vol.50 , pp. 137-146
    • Hamblen, E.C.1    Davis, C.D.2    Durham, N.C.3
  • 95
    • 78650891915 scopus 로고    scopus 로고
    • Relationship between thyrotropin receptor hinge region proteolytic posttranslational modification and receptor physiological function
    • Hamidi S., Chen C.R., Mizutori-Sasai Y., McLachlan S.M., Rapoport B. Relationship between thyrotropin receptor hinge region proteolytic posttranslational modification and receptor physiological function. Mol. Endocrinol. 2011, 25:184-194.
    • (2011) Mol. Endocrinol. , vol.25 , pp. 184-194
    • Hamidi, S.1    Chen, C.R.2    Mizutori-Sasai, Y.3    McLachlan, S.M.4    Rapoport, B.5
  • 96
    • 69249158290 scopus 로고    scopus 로고
    • Allosteric communication between protomers of dopamine class A GPCR dimers modulates activation
    • Han Y., Moreira I.S., Urizar E., Weinstein H., Javitch J.A. Allosteric communication between protomers of dopamine class A GPCR dimers modulates activation. Nat. Chem. Biol. 2009, 5:688-695.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 688-695
    • Han, Y.1    Moreira, I.S.2    Urizar, E.3    Weinstein, H.4    Javitch, J.A.5
  • 98
    • 0032053545 scopus 로고    scopus 로고
    • Partially deglycosylated human choriogonadotropin, stabilized by intersubunit disulfide bonds, shows full bioactivity
    • Heikoop J.C., van den Boogaart P., de Leeuw R., Rose U.M., Mulders J.W., Grootenhuis P.D. Partially deglycosylated human choriogonadotropin, stabilized by intersubunit disulfide bonds, shows full bioactivity. Eur. J. Biochem. 1998, 253:354-356.
    • (1998) Eur. J. Biochem. , vol.253 , pp. 354-356
    • Heikoop, J.C.1    van den Boogaart, P.2    de Leeuw, R.3    Rose, U.M.4    Mulders, J.W.5    Grootenhuis, P.D.6
  • 100
    • 0034987731 scopus 로고    scopus 로고
    • Effects of mutations involving the highly conserved S281HCC motif in the extracellular domain of the thyrotropin (TSH) receptor on TSH binding and constitutive activity
    • Ho S.C., Van Sande J., Lefort A., Vassart G., Costagliola S. Effects of mutations involving the highly conserved S281HCC motif in the extracellular domain of the thyrotropin (TSH) receptor on TSH binding and constitutive activity. Endocrinology 2001, 142:2760-2767.
    • (2001) Endocrinology , vol.142 , pp. 2760-2767
    • Ho, S.C.1    Van Sande, J.2    Lefort, A.3    Vassart, G.4    Costagliola, S.5
  • 101
    • 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., Khoo D.H. 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. 2005, 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
  • 102
    • 84873109084 scopus 로고    scopus 로고
    • Molecular sampling of the allosteric binding pocket of the TSH receptor provides discriminative pharmacophores for antagonist and agonists
    • Hoyer I., Haas A.K., Kreuchwig A., Schulein R., Krause G. Molecular sampling of the allosteric binding pocket of the TSH receptor provides discriminative pharmacophores for antagonist and agonists. Biochem. Soc. Trans. 2013, 41:213-217.
    • (2013) Biochem. Soc. Trans. , vol.41 , pp. 213-217
    • Hoyer, I.1    Haas, A.K.2    Kreuchwig, A.3    Schulein, R.4    Krause, G.5
  • 103
    • 0000437998 scopus 로고    scopus 로고
    • Characterization of two LGR genes homologous to gonadotropin and thyrotropin receptors with extracellular leucine-rich repeats and a G protein-coupled, seven-transmembrane region
    • Hsu S.Y., Liang S.G., Hsueh A.J. Characterization of two LGR genes homologous to gonadotropin and thyrotropin receptors with extracellular leucine-rich repeats and a G protein-coupled, seven-transmembrane region. Mol. Endocrinol. 1998, 12:1830-1845.
    • (1998) Mol. Endocrinol. , vol.12 , pp. 1830-1845
    • Hsu, S.Y.1    Liang, S.G.2    Hsueh, A.J.3
  • 104
    • 0034464024 scopus 로고    scopus 로고
    • The three subfamilies of leucine-rich repeat-containing G protein-coupled receptors (LGR): identification of LGR6 and LGR7 and the signaling mechanism for LGR7
    • Hsu S.Y., Kudo M., Chen T., Nakabayashi K., Bhalla A., van der Spek P.J., van Duin M., Hsueh A.J. The three subfamilies of leucine-rich repeat-containing G protein-coupled receptors (LGR): identification of LGR6 and LGR7 and the signaling mechanism for LGR7. Mol. Endocrinol. 2000, 14:1257-1271.
    • (2000) Mol. Endocrinol. , vol.14 , pp. 1257-1271
    • Hsu, S.Y.1    Kudo, M.2    Chen, T.3    Nakabayashi, K.4    Bhalla, A.5    van der Spek, P.J.6    van Duin, M.7    Hsueh, A.J.8
  • 108
    • 77957168150 scopus 로고    scopus 로고
    • Does hCG or hCGbeta play a role in cancer cell biology?
    • Iles R.K., Delves P.J., Butler S.A. Does hCG or hCGbeta play a role in cancer cell biology?. Mol. Cell. Endocrinol. 2010, 329:62-70.
    • (2010) Mol. Cell. Endocrinol. , vol.329 , pp. 62-70
    • Iles, R.K.1    Delves, P.J.2    Butler, S.A.3
  • 110
    • 85047686522 scopus 로고    scopus 로고
    • Cis- and trans-activation of hormone receptors: the LH receptor
    • Ji I., Lee C., Song Y., Conn P.M., Ji T.H. Cis- and trans-activation of hormone receptors: the LH receptor. Mol. Endocrinol. 2002, 16:1299-1308.
    • (2002) Mol. Endocrinol. , vol.16 , pp. 1299-1308
    • Ji, I.1    Lee, C.2    Song, Y.3    Conn, P.M.4    Ji, T.H.5
  • 111
    • 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 D.R., Cheng S., Ythier A., Wu H., Hendrickson W.A., el Tayar N. Structural predictions for the ligand-binding region of glycoprotein hormone receptors and the nature of hormone-receptor interactions. Structure 1995, 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
  • 114
    • 0037126208 scopus 로고    scopus 로고
    • Phylogenetic analysis of 277 human G-protein-coupled receptors as a tool for the prediction of orphan receptor ligands
    • 3, research0063.1-6.
    • Joost, P., Methner, A., 2002. Phylogenetic analysis of 277 human G-protein-coupled receptors as a tool for the prediction of orphan receptor ligands. Genome Biol. 3, research0063.1-6.
    • (2002) Genome Biol.
    • Joost, P.1    Methner, A.2
  • 115
    • 0032478536 scopus 로고    scopus 로고
    • Structural diversity of leucine-rich repeat proteins
    • Kajava A.V. Structural diversity of leucine-rich repeat proteins. J. Mol. Biol. 1998, 277:519-527.
    • (1998) J. Mol. Biol. , vol.277 , pp. 519-527
    • Kajava, A.V.1
  • 116
    • 0029645408 scopus 로고
    • Modeling of the three-dimensional structure of proteins with the typical leucine-rich repeats
    • Kajava A.V., Vassart G., Wodak S.J. Modeling of the three-dimensional structure of proteins with the typical leucine-rich repeats. Structure 1995, 3:867-877.
    • (1995) Structure , vol.3 , pp. 867-877
    • Kajava, A.V.1    Vassart, G.2    Wodak, S.J.3
  • 117
    • 84855799592 scopus 로고    scopus 로고
    • Diversity and modularity of G protein-coupled receptor structures
    • Katritch V., Cherezov V., Stevens R.C. Diversity and modularity of G protein-coupled receptor structures. Trends Pharmacol. Sci. 2012, 33:17-27.
    • (2012) Trends Pharmacol. Sci. , vol.33 , pp. 17-27
    • Katritch, V.1    Cherezov, V.2    Stevens, R.C.3
  • 119
    • 0024550731 scopus 로고
    • Role of the beta 93-100 determinant loop sequence in receptor binding and biological activity of human luteinizing hormone and chorionic gonadotropin
    • Keutmann H.T., Mason K.A., Kitzmann K., Ryan R.J. Role of the beta 93-100 determinant loop sequence in receptor binding and biological activity of human luteinizing hormone and chorionic gonadotropin. Mol. Endocrinol. 1989, 3:526-531.
    • (1989) Mol. Endocrinol. , vol.3 , pp. 526-531
    • Keutmann, H.T.1    Mason, K.A.2    Kitzmann, K.3    Ryan, R.J.4
  • 121
  • 122
    • 65249116958 scopus 로고    scopus 로고
    • Thyrotropin and homologous glycoprotein hormone receptors: structural and functional aspects of extracellular signaling mechanisms
    • Kleinau G., Krause G. Thyrotropin and homologous glycoprotein hormone receptors: structural and functional aspects of extracellular signaling mechanisms. Endocr. Rev. 2009, 30:133-151.
    • (2009) Endocr. Rev. , vol.30 , pp. 133-151
    • Kleinau, G.1    Krause, G.2
  • 123
    • 10944228424 scopus 로고    scopus 로고
    • Identification of a novel epitope in the thyroid-stimulating hormone receptor ectodomain acting as intramolecular signaling interface
    • Kleinau G., Jaschke H., Neumann S., Lattig J., Paschke R., Krause G. Identification of a novel epitope in the thyroid-stimulating hormone receptor ectodomain acting as intramolecular signaling interface. J. Biol. Chem. 2004, 279:51590-51600.
    • (2004) J. Biol. Chem. , vol.279 , pp. 51590-51600
    • Kleinau, G.1    Jaschke, H.2    Neumann, S.3    Lattig, J.4    Paschke, R.5    Krause, G.6
  • 124
    • 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., Krause G. Contacts between extracellular loop two and transmembrane helix six determine basal activity of the thyroid-stimulating hormone receptor. J. Biol. Chem. 2007, 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
  • 126
    • 84886293598 scopus 로고    scopus 로고
    • Novel insights on thyroid stimulating hormone receptor signal transduction
    • doi: 10.1210/er.2012-1072.
    • Kleinau, G., Neumann, S., Grüters, A., Krude, H., Biebermann, H., 2013. Novel insights on thyroid stimulating hormone receptor signal transduction, Endocr. Rev. doi: 10.1210/er.2012-1072.
    • (2013) Endocr. Rev.
    • Kleinau, G.1    Neumann, S.2    Grüters, A.3    Krude, H.4    Biebermann, H.5
  • 127
    • 3543036363 scopus 로고    scopus 로고
    • Closed state of both binding domains of homodimeric mGlu receptors is required for full activity
    • Kniazeff J., Bessis A.S., Maurel D., Ansanay H., Prezeau L., Pin J.P. Closed state of both binding domains of homodimeric mGlu receptors is required for full activity. Nat. Struct. Mol. Biol. 2004, 11:706-713.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 706-713
    • Kniazeff, J.1    Bessis, A.S.2    Maurel, D.3    Ansanay, H.4    Prezeau, L.5    Pin, J.P.6
  • 128
    • 0027718173 scopus 로고
    • Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats
    • Kobe B., Deisenhofer J. Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats. Nature 1993, 366:751-756.
    • (1993) Nature , vol.366 , pp. 751-756
    • Kobe, B.1    Deisenhofer, J.2
  • 129
    • 32144449896 scopus 로고    scopus 로고
    • Mean curvature as a major determinant of beta-sheet propensity
    • Koh E., Kim T., Cho H.S. Mean curvature as a major determinant of beta-sheet propensity. Bioinformatics 2006, 22:297-302.
    • (2006) Bioinformatics , vol.22 , pp. 297-302
    • Koh, E.1    Kim, T.2    Cho, H.S.3
  • 131
    • 0025729583 scopus 로고
    • Structure of the luteinizing hormone receptor gene and multiple exons of the coding sequence
    • Koo Y.B., Ji I., Slaughter R.G., Ji T.H. Structure of the luteinizing hormone receptor gene and multiple exons of the coding sequence. Endocrinology 1991, 128:2297-2308.
    • (1991) Endocrinology , vol.128 , pp. 2297-2308
    • Koo, Y.B.1    Ji, I.2    Slaughter, R.G.3    Ji, T.H.4
  • 132
    • 0030830146 scopus 로고    scopus 로고
    • Congenital hyperthyroidism caused by a solitary toxic adenoma harboring a novel somatic mutation (serine281→isoleucine) in the extracellular domain of the thyrotropin receptor
    • Kopp P., Muirhead S., Jourdain N., Gu W.X., Jameson J.L., Rodd C. Congenital hyperthyroidism caused by a solitary toxic adenoma harboring a novel somatic mutation (serine281→isoleucine) in the extracellular domain of the thyrotropin receptor. J. Clin. Invest. 1997, 100:1634-1639.
    • (1997) J. Clin. Invest. , vol.100 , pp. 1634-1639
    • Kopp, P.1    Muirhead, S.2    Jourdain, N.3    Gu, W.X.4    Jameson, J.L.5    Rodd, C.6
  • 133
    • 0026002412 scopus 로고
    • Site-directed mutagenesis of a portion of the extracellular domain of the rat thyrotropin receptor important in autoimmune thyroid disease and nonhomologous with gonadotropin receptors. Relationship of functional and immunogenic domains
    • Kosugi S., Ban T., Akamizu T., Kohn L.D. Site-directed mutagenesis of a portion of the extracellular domain of the rat thyrotropin receptor important in autoimmune thyroid disease and nonhomologous with gonadotropin receptors. Relationship of functional and immunogenic domains. J. Biol. Chem. 1991, 266:19413-19418.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19413-19418
    • Kosugi, S.1    Ban, T.2    Akamizu, T.3    Kohn, L.D.4
  • 134
    • 84871648298 scopus 로고    scopus 로고
    • Extended and structurally supported insights into extracellular hormone binding, signal transduction and organization of the thyrotropin receptor
    • Krause G., Kreuchwig A., Kleinau G. Extended and structurally supported insights into extracellular hormone binding, signal transduction and organization of the thyrotropin receptor. PLoS ONE 2012, 7:e52920.
    • (2012) PLoS ONE , vol.7
    • Krause, G.1    Kreuchwig, A.2    Kleinau, G.3
  • 136
    • 62749104387 scopus 로고    scopus 로고
    • The thyroid-stimulating hormone receptor: impact of thyroid-stimulating hormone and thyroid-stimulating hormone receptor antibodies on multimerization, cleavage, and signaling
    • Latif R., Morshed S.A., Zaidi M., Davies T.F. The thyroid-stimulating hormone receptor: impact of thyroid-stimulating hormone and thyroid-stimulating hormone receptor antibodies on multimerization, cleavage, and signaling. Endocrinol. Metab. Clin. North Am. 2009, 38:319-341.
    • (2009) Endocrinol. Metab. Clin. North Am. , vol.38 , pp. 319-341
    • Latif, R.1    Morshed, S.A.2    Zaidi, M.3    Davies, T.F.4
  • 137
    • 77949700065 scopus 로고    scopus 로고
    • A tyrosine residue on the TSH receptor stabilizes multimer formation
    • Latif R., Michalek K., Morshed S.A., Davies T.F. A tyrosine residue on the TSH receptor stabilizes multimer formation. PLoS ONE 2010, 5:e9449.
    • (2010) PLoS ONE , vol.5
    • Latif, R.1    Michalek, K.2    Morshed, S.A.3    Davies, T.F.4
  • 139
    • 0025950132 scopus 로고
    • Further characterization of the receptor-binding region of the thyroid-stimulating hormone alpha subunit: a comprehensive synthetic peptide study of the alpha-subunit 26-46 sequence
    • Leinung M.C., Reed D.K., McCormick D.J., Ryan R.J., Morris J.C. Further characterization of the receptor-binding region of the thyroid-stimulating hormone alpha subunit: a comprehensive synthetic peptide study of the alpha-subunit 26-46 sequence. Proc. Natl. Acad. Sci. USA 1991, 88:9707-9711.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9707-9711
    • Leinung, M.C.1    Reed, D.K.2    McCormick, D.J.3    Ryan, R.J.4    Morris, J.C.5
  • 141
    • 0029882185 scopus 로고    scopus 로고
    • Long loop residues 33-58 in the human glycoprotein hormone common alpha subunit contain structural components for subunit heterodimerization and human follitropin-receptor binding
    • Liu C., Dias J.A. Long loop residues 33-58 in the human glycoprotein hormone common alpha subunit contain structural components for subunit heterodimerization and human follitropin-receptor binding. Arch. Biochem. Biophys. 1996, 329:127-135.
    • (1996) Arch. Biochem. Biophys. , vol.329 , pp. 127-135
    • Liu, C.1    Dias, J.A.2
  • 142
    • 33846987130 scopus 로고    scopus 로고
    • Structural basis for stem cell factor-KIT signaling and activation of class III receptor tyrosine kinases
    • Liu H., Chen X., Focia P.J., He X. Structural basis for stem cell factor-KIT signaling and activation of class III receptor tyrosine kinases. EMBO J. 2007, 26:891-901.
    • (2007) EMBO J. , vol.26 , pp. 891-901
    • Liu, H.1    Chen, X.2    Focia, P.J.3    He, X.4
  • 144
  • 145
    • 0036045124 scopus 로고    scopus 로고
    • Development of gonadotrophins for clinical use
    • Lunenfeld B. Development of gonadotrophins for clinical use. Reprod. Biomed. Online 2002, 4(Suppl. 1):11-17.
    • (2002) Reprod. Biomed. Online , vol.4 , Issue.1 SUPPL. , pp. 11-17
    • Lunenfeld, B.1
  • 146
    • 8844263790 scopus 로고    scopus 로고
    • Historical perspectives in gonadotrophin therapy
    • Lunenfeld B. Historical perspectives in gonadotrophin therapy. Hum. Reprod. Update 2004, 10:453-467.
    • (2004) Hum. Reprod. Update , vol.10 , pp. 453-467
    • Lunenfeld, B.1
  • 147
    • 0000140415 scopus 로고
    • L'induction de l'ovulation dans les amenorrhees hypophysaires par un traitement combine de gonadotrophines urinaires menopausiques et de gonadotrophines chorioniques
    • Lunenfeld B., Sulimovici S., Rabau E., Eshkol A. L'induction de l'ovulation dans les amenorrhees hypophysaires par un traitement combine de gonadotrophines urinaires menopausiques et de gonadotrophines chorioniques. CR Soc. Franc Gynecol 1962, 325-346.
    • (1962) CR Soc. Franc Gynecol , pp. 325-346
    • Lunenfeld, B.1    Sulimovici, S.2    Rabau, E.3    Eshkol, A.4
  • 148
    • 0027256170 scopus 로고
    • The application of chemical studies of human chorionic gonadotropin to visualize its three-dimensional structure
    • Lustbader J.W., Yarmush D.L., Birken S., Puett D., Canfield R.E. The application of chemical studies of human chorionic gonadotropin to visualize its three-dimensional structure. Endocr. Rev. 1993, 14:291-311.
    • (1993) Endocr. Rev. , vol.14 , pp. 291-311
    • Lustbader, J.W.1    Yarmush, D.L.2    Birken, S.3    Puett, D.4    Canfield, R.E.5
  • 149
    • 84858698405 scopus 로고    scopus 로고
    • Insights into differential modulation of receptor function by hinge region using novel agonistic lutropin receptor and inverse agonistic thyrotropin receptor antibodies
    • Majumdar R., Railkar R., Dighe R.R. Insights into differential modulation of receptor function by hinge region using novel agonistic lutropin receptor and inverse agonistic thyrotropin receptor antibodies. FEBS Lett. 2012, 586:810-817.
    • (2012) FEBS Lett. , vol.586 , pp. 810-817
    • Majumdar, R.1    Railkar, R.2    Dighe, R.R.3
  • 150
    • 48749126827 scopus 로고    scopus 로고
    • Ligand sensitivity in dimeric associations of the serotonin 5HT2c receptor
    • Mancia F., Assur Z., Herman A.G., Siegel R., Hendrickson W.A. Ligand sensitivity in dimeric associations of the serotonin 5HT2c receptor. EMBO Rep. 2008, 9:363-369.
    • (2008) EMBO Rep. , vol.9 , pp. 363-369
    • Mancia, F.1    Assur, Z.2    Herman, A.G.3    Siegel, R.4    Hendrickson, W.A.5
  • 151
    • 18744411809 scopus 로고    scopus 로고
    • The second extracellular loop: a damper for G protein-coupled receptors?
    • Massotte D., Kieffer B.L. The second extracellular loop: a damper for G protein-coupled receptors?. Nat. Struct. Mol. Biol. 2005, 12:287-288.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 287-288
    • Massotte, D.1    Kieffer, B.L.2
  • 152
    • 0024510014 scopus 로고
    • Mutagenesis and gene transfer define site-specific roles of the gonadotropin oligosaccharides
    • Matzuk M.M., Boime I. Mutagenesis and gene transfer define site-specific roles of the gonadotropin oligosaccharides. Biol. Reprod. 1989, 40:48-53.
    • (1989) Biol. Reprod. , vol.40 , pp. 48-53
    • Matzuk, M.M.1    Boime, I.2
  • 153
    • 0024511030 scopus 로고
    • Site specificity of the chorionic gonadotropin N-linked oligosaccharides in signal transduction
    • Matzuk M.M., Keene J.L., Boime I. Site specificity of the chorionic gonadotropin N-linked oligosaccharides in signal transduction. J. Biol. Chem. 1989, 264:2409-2414.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2409-2414
    • Matzuk, M.M.1    Keene, J.L.2    Boime, I.3
  • 154
    • 0027251256 scopus 로고
    • A structural superfamily of growth factors containing a cystine knot motif
    • McDonald N.Q., Hendrickson W.A. A structural superfamily of growth factors containing a cystine knot motif. Cell 1993, 73:421-424.
    • (1993) Cell , vol.73 , pp. 421-424
    • McDonald, N.Q.1    Hendrickson, W.A.2
  • 155
    • 0025986121 scopus 로고
    • New protein fold revealed by a 2.3-A resolution crystal structure of nerve growth factor
    • McDonald N.Q., Lapatto R., Murray-Rust J., Gunning J., Wlodawer A., Blundell T.L. New protein fold revealed by a 2.3-A resolution crystal structure of nerve growth factor. Nature 1991, 354:411-414.
    • (1991) Nature , vol.354 , pp. 411-414
    • McDonald, N.Q.1    Lapatto, R.2    Murray-Rust, J.3    Gunning, J.4    Wlodawer, A.5    Blundell, T.L.6
  • 156
    • 33344470222 scopus 로고    scopus 로고
    • Follicle-stimulating hormone-induced aromatase in immature rat Sertoli cells requires an active phosphatidylinositol 3-kinase pathway and is inhibited via the mitogen-activated protein kinase signaling pathway
    • McDonald C.A., Millena A.C., Reddy S., Finlay S., Vizcarra J., Khan S.A., Davis J.S. Follicle-stimulating hormone-induced aromatase in immature rat Sertoli cells requires an active phosphatidylinositol 3-kinase pathway and is inhibited via the mitogen-activated protein kinase signaling pathway. Mol. Endocrinol. 2006, 20:608-618.
    • (2006) Mol. Endocrinol. , vol.20 , pp. 608-618
    • McDonald, C.A.1    Millena, A.C.2    Reddy, S.3    Finlay, S.4    Vizcarra, J.5    Khan, S.A.6    Davis, J.S.7
  • 158
    • 84889387512 scopus 로고    scopus 로고
    • Huang, Z. (Ed.), Drug Discovery Research: New Frontiers in the Post-Genomic Era. John Wiley & Sons, New York
    • McGregor, M.J., Luo, Z., Jiang, X., 2007. Virtual Screening in Drug Discovery, in: Huang, Z. (Ed.), Drug Discovery Research: New Frontiers in the Post-Genomic Era. John Wiley & Sons, New York, pp. 63-88.
    • (2007) Virtual Screening in Drug Discovery , pp. 63-88
    • McGregor, M.J.1    Luo, Z.2    Jiang, X.3
  • 160
    • 55749106015 scopus 로고    scopus 로고
    • FSH and TSH binding to their respective receptors: similarities, differences and implication for glycoprotein hormone specificity
    • Miguel R.N., Sanders J., Chirgadze D., Blundell T., Furmaniak J., Smith B.R. FSH and TSH binding to their respective receptors: similarities, differences and implication for glycoprotein hormone specificity. J. Mol. Endocrinol. 2008, 41:145-164.
    • (2008) J. Mol. Endocrinol. , vol.41 , pp. 145-164
    • Miguel, R.N.1    Sanders, J.2    Chirgadze, D.3    Blundell, T.4    Furmaniak, J.5    Smith, B.R.6
  • 161
    • 0019159694 scopus 로고
    • Assignment of disulfide bonds in the alpha subunit of human chorionic gonadotropin
    • Mise T., Bahl O.P. Assignment of disulfide bonds in the alpha subunit of human chorionic gonadotropin. J. Biol. Chem. 1980, 255:8516-8522.
    • (1980) J. Biol. Chem. , vol.255 , pp. 8516-8522
    • Mise, T.1    Bahl, O.P.2
  • 162
    • 0019870057 scopus 로고
    • Assignment of disulfide bonds in the beta subunit of human chorionic gonadotropin
    • Mise T., Bahl O.P. Assignment of disulfide bonds in the beta subunit of human chorionic gonadotropin. J. Biol. Chem. 1981, 256:6587-6592.
    • (1981) J. Biol. Chem. , vol.256 , pp. 6587-6592
    • Mise, T.1    Bahl, O.P.2
  • 163
    • 43049109876 scopus 로고    scopus 로고
    • The thyrotropin receptor hinge region is not simply a scaffold for the leucine-rich domain but contributes to ligand binding and signal transduction
    • Mizutori Y., Chen C.R., McLachlan S.M., Rapoport B. The thyrotropin receptor hinge region is not simply a scaffold for the leucine-rich domain but contributes to ligand binding and signal transduction. Mol. Endocrinol. 2008, 22:1171-1182.
    • (2008) Mol. Endocrinol. , vol.22 , pp. 1171-1182
    • Mizutori, Y.1    Chen, C.R.2    McLachlan, S.M.3    Rapoport, B.4
  • 164
    • 0025309387 scopus 로고
    • Localization of residues that confer antibody binding specificity using human chorionic gonadotropin/luteinizing hormone beta subunit chimeras and mutants
    • Moyle W.R., Matzuk M.M., Campbell R.K., Cogliani E., Dean-Emig D.M., Krichevsky A., Barnett R.W., Boime I. Localization of residues that confer antibody binding specificity using human chorionic gonadotropin/luteinizing hormone beta subunit chimeras and mutants. J. Biol. Chem. 1990, 265:8511-8518.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8511-8518
    • Moyle, W.R.1    Matzuk, M.M.2    Campbell, R.K.3    Cogliani, E.4    Dean-Emig, D.M.5    Krichevsky, A.6    Barnett, R.W.7    Boime, I.8
  • 166
    • 0029093909 scopus 로고
    • Model of human chorionic gonadotropin and lutropin receptor interaction that explains signal transduction of the glycoprotein hormones
    • Moyle W.R., Campbell R.K., Rao S.N., Ayad N.G., Bernard M.P., Han Y., Wang Y. Model of human chorionic gonadotropin and lutropin receptor interaction that explains signal transduction of the glycoprotein hormones. J. Biol. Chem. 1995, 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
  • 169
    • 84888289994 scopus 로고    scopus 로고
    • FSH Mutants. U.S. Patent 7,740,862.
    • Muda, M., Jiang, X., McKenna, S.D., 2010. FSH Mutants. U.S. Patent 7,740,862.
    • (2010)
    • Muda, M.1    Jiang, X.2    McKenna, S.D.3
  • 170
    • 84888303454 scopus 로고    scopus 로고
    • FSH Glycosylation Variant D3N. U.S. Patent 7,956,034.
    • Muda, M., Jiang, X., McKenna, S.D., 2011. FSH Glycosylation Variant D3N. U.S. Patent 7,956,034.
    • (2011)
    • Muda, M.1    Jiang, X.2    McKenna, S.D.3
  • 171
    • 49649125175 scopus 로고    scopus 로고
    • Extended hormone binding site of the human thyroid stimulating hormone receptor: distinctive acidic residues in the hinge region are involved in bovine thyroid stimulating hormone binding and receptor activation
    • Mueller S., Kleinau G., Jaeschke H., Paschke R., Krause G. Extended hormone binding site of the human thyroid stimulating hormone receptor: distinctive acidic residues in the hinge region are involved in bovine thyroid stimulating hormone binding and receptor activation. J. Biol. Chem. 2008, 283:18048-18055.
    • (2008) J. Biol. Chem. , vol.283 , pp. 18048-18055
    • Mueller, S.1    Kleinau, G.2    Jaeschke, H.3    Paschke, R.4    Krause, G.5
  • 173
    • 0026568620 scopus 로고
    • The thyrotropin receptor 25 years after its discovery: new insight after its molecular cloning
    • Nagayama Y., Rapoport B. The thyrotropin receptor 25 years after its discovery: new insight after its molecular cloning. Mol. Endocrinol. 1992, 6:145-156.
    • (1992) Mol. Endocrinol. , vol.6 , pp. 145-156
    • Nagayama, Y.1    Rapoport, B.2
  • 174
    • 0034730516 scopus 로고    scopus 로고
    • Activation of the luteinizing hormone receptor following substitution of Ser-277 with selective hydrophobic residues in the ectodomain hinge region
    • Nakabayashi K., Kudo M., Kobilka B., Hsueh A.J. Activation of the luteinizing hormone receptor following substitution of Ser-277 with selective hydrophobic residues in the ectodomain hinge region. J. Biol. Chem. 2000, 275:30264-30271.
    • (2000) J. Biol. Chem. , vol.275 , pp. 30264-30271
    • Nakabayashi, K.1    Kudo, M.2    Kobilka, B.3    Hsueh, A.J.4
  • 175
    • 0036259465 scopus 로고    scopus 로고
    • Thyrostimulin, a heterodimer of two new human glycoprotein hormone subunits, activates the thyroid-stimulating hormone receptor
    • Nakabayashi K., Matsumi H., Bhalla A., Bae J., Mosselman S., Hsu S.Y., Hsueh A.J. Thyrostimulin, a heterodimer of two new human glycoprotein hormone subunits, activates the thyroid-stimulating hormone receptor. J. Clin. Invest. 2002, 109:1445-1452.
    • (2002) J. Clin. Invest. , vol.109 , pp. 1445-1452
    • Nakabayashi, K.1    Matsumi, H.2    Bhalla, A.3    Bae, J.4    Mosselman, S.5    Hsu, S.Y.6    Hsueh, A.J.7
  • 176
    • 79960902373 scopus 로고    scopus 로고
    • Understanding the effect of different assay formats on agonist parameters: a study using the micro-opioid receptor
    • Nickolls S.A., Waterfield A., Williams R.E., Kinloch R.A. Understanding the effect of different assay formats on agonist parameters: a study using the micro-opioid receptor. J. Biomol. Screen. 2011, 16:706-716.
    • (2011) J. Biomol. Screen. , vol.16 , pp. 706-716
    • Nickolls, S.A.1    Waterfield, A.2    Williams, R.E.3    Kinloch, R.A.4
  • 177
    • 0026744790 scopus 로고
    • Crystal structure of human platelet-derived growth factor BB
    • Oefner C., D'Arcy A., Winkler F.K., Eggimann B., Hosang M. Crystal structure of human platelet-derived growth factor BB. EMBO J. 1992, 11:3921-3926.
    • (1992) EMBO J. , vol.11 , pp. 3921-3926
    • Oefner, C.1    D'Arcy, A.2    Winkler, F.K.3    Eggimann, B.4    Hosang, M.5
  • 179
    • 44349121122 scopus 로고    scopus 로고
    • Biochemical roles of the oligosaccharide chains in thyrostimulin, a heterodimeric hormone of glycoprotein hormone subunits alpha 2 (GPA2) and beta 5 (GPB5)
    • Okajima Y., Nagasaki H., Suzuki C., Suga H., Ozaki N., Arima H., Hamada Y., Civelli O., Oiso Y. Biochemical roles of the oligosaccharide chains in thyrostimulin, a heterodimeric hormone of glycoprotein hormone subunits alpha 2 (GPA2) and beta 5 (GPB5). Regul. Pept. 2008, 148:62-67.
    • (2008) Regul. Pept. , vol.148 , pp. 62-67
    • Okajima, Y.1    Nagasaki, H.2    Suzuki, C.3    Suga, H.4    Ozaki, N.5    Arima, H.6    Hamada, Y.7    Civelli, O.8    Oiso, Y.9
  • 180
    • 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 A.J. Co-expression of defective luteinizing hormone receptor fragments partially reconstitutes ligand-induced signal generation. J. Biol. Chem. 1997, 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.6
  • 181
    • 0027202198 scopus 로고
    • Unmasking of an immunoreactive site on the alpha subunit of human choriogonadotropin bound to the extracellular domain of its receptor
    • Pantel J., Remy J.J., Salesse R., Jolivet A., Bidart J.M. Unmasking of an immunoreactive site on the alpha subunit of human choriogonadotropin bound to the extracellular domain of its receptor. Biochem. Biophys. Res. Commun. 1993, 195:588-593.
    • (1993) Biochem. Biophys. Res. Commun. , vol.195 , pp. 588-593
    • Pantel, J.1    Remy, J.J.2    Salesse, R.3    Jolivet, A.4    Bidart, J.M.5
  • 183
    • 0020696020 scopus 로고
    • Purification of an alternate form of the alpha subunit of the glycoprotein hormones from bovine pituitaries and identification of its O-linked oligosaccharide
    • Parsons T.F., Bloomfield G., Pierce J. Purification of an alternate form of the alpha subunit of the glycoprotein hormones from bovine pituitaries and identification of its O-linked oligosaccharide. J. Biol. Chem. 1983, 258:240-244.
    • (1983) J. Biol. Chem. , vol.258 , pp. 240-244
    • Parsons, T.F.1    Bloomfield, G.2    Pierce, J.3
  • 184
    • 84888287580 scopus 로고    scopus 로고
    • PDR, Physicians' Desk Reference 2013, 2013 ed. PDR Network.
    • PDR, 2013. Physicians' Desk Reference 2013, 2013 ed. PDR Network.
    • (2013)
  • 185
    • 79551650974 scopus 로고    scopus 로고
    • GPCR structure and activation: an essential role for the first extracellular loop in activating the adenosine A2B receptor
    • Peeters M.C., van Westen G.J., Guo D., Wisse L.E., Muller C.E., Beukers M.W., Ijzerman A.P. GPCR structure and activation: an essential role for the first extracellular loop in activating the adenosine A2B receptor. FASEB J. 2011, 25:632-643.
    • (2011) FASEB J. , vol.25 , pp. 632-643
    • Peeters, M.C.1    van Westen, G.J.2    Guo, D.3    Wisse, L.E.4    Muller, C.E.5    Beukers, M.W.6    Ijzerman, A.P.7
  • 186
    • 0019729482 scopus 로고
    • Glycoprotein hormones: structure and function
    • Pierce J.G., Parsons T.F. Glycoprotein hormones: structure and function. Annu. Rev. Biochem. 1981, 50:465-495.
    • (1981) Annu. Rev. Biochem. , vol.50 , pp. 465-495
    • Pierce, J.G.1    Parsons, T.F.2
  • 187
    • 0017107463 scopus 로고
    • Studies on the disulfide bonds of glycoprotein hormones. Course of reduction of bovine luteinizing hormone, bovine thyroid-stimulating hormone, and their subunits
    • Pierce J.G., Giudice L.C., Reeve J.R. Studies on the disulfide bonds of glycoprotein hormones. Course of reduction of bovine luteinizing hormone, bovine thyroid-stimulating hormone, and their subunits. J. Biol. Chem. 1976, 251:6388-6391.
    • (1976) J. Biol. Chem. , vol.251 , pp. 6388-6391
    • Pierce, J.G.1    Giudice, L.C.2    Reeve, J.R.3
  • 189
    • 77952757509 scopus 로고    scopus 로고
    • Oligomeric size of the m2 muscarinic receptor in live cells as determined by quantitative fluorescence resonance energy transfer
    • Pisterzi L.F., Jansma D.B., Georgiou J., Woodside M.J., Chou J.T., Angers S., Raicu V., Wells J.W. Oligomeric size of the m2 muscarinic receptor in live cells as determined by quantitative fluorescence resonance energy transfer. J. Biol. Chem. 2010, 285:16723-16738.
    • (2010) J. Biol. Chem. , vol.285 , pp. 16723-16738
    • Pisterzi, L.F.1    Jansma, D.B.2    Georgiou, J.3    Woodside, M.J.4    Chou, J.T.5    Angers, S.6    Raicu, V.7    Wells, J.W.8
  • 191
    • 33751331631 scopus 로고    scopus 로고
    • A functional transmembrane complex: the luteinizing hormone receptor with bound ligand and G protein
    • Puett D., Li Y., DeMars G., Angelova K., Fanelli F. A functional transmembrane complex: the luteinizing hormone receptor with bound ligand and G protein. Mol. Cell. Endocrinol. 2007, 260-262:126-136.
    • (2007) Mol. Cell. Endocrinol. , pp. 126-136
    • Puett, D.1    Li, Y.2    DeMars, G.3    Angelova, K.4    Fanelli, F.5
  • 192
    • 77957104740 scopus 로고    scopus 로고
    • The luteinizing hormone receptor: insights into structure-function relationships and hormone-receptor-mediated changes in gene expression in ovarian cancer cells
    • Puett D., Angelova K., da Costa M.R., Warrenfeltz S.W., Fanelli F. The luteinizing hormone receptor: insights into structure-function relationships and hormone-receptor-mediated changes in gene expression in ovarian cancer cells. Mol. Cell. Endocrinol. 2010, 329:47-55.
    • (2010) Mol. Cell. Endocrinol. , vol.329 , pp. 47-55
    • Puett, D.1    Angelova, K.2    da Costa, M.R.3    Warrenfeltz, S.W.4    Fanelli, F.5
  • 193
    • 35948944223 scopus 로고    scopus 로고
    • The thyrotropin receptor in Graves' disease
    • Rapoport B., McLachlan S.M. The thyrotropin receptor in Graves' disease. Thyroid 2007, 17:911-922.
    • (2007) Thyroid , vol.17 , pp. 911-922
    • Rapoport, B.1    McLachlan, S.M.2
  • 194
    • 0032247323 scopus 로고    scopus 로고
    • The thyrotropin (TSH) receptor: interaction with TSH and autoantibodies
    • Rapoport B., Chazenbalk G.D., Jaume J.C., McLachlan S.M. The thyrotropin (TSH) receptor: interaction with TSH and autoantibodies. Endocr. Rev. 1998, 19:673-716.
    • (1998) Endocr. Rev. , vol.19 , pp. 673-716
    • Rapoport, B.1    Chazenbalk, G.D.2    Jaume, J.C.3    McLachlan, S.M.4
  • 196
    • 0020410298 scopus 로고
    • Elucidation of the disulfide bond positions of the beta-subunit of human follicle-stimulating hormone
    • Rathnam P., Tolvo A., Saxena B.B. Elucidation of the disulfide bond positions of the beta-subunit of human follicle-stimulating hormone. Biochim. Biophys. Acta 1982, 708:160-166.
    • (1982) Biochim. Biophys. Acta , vol.708 , pp. 160-166
    • Rathnam, P.1    Tolvo, A.2    Saxena, B.B.3
  • 197
    • 0023225506 scopus 로고
    • Antibody binding to the beta-subunit of deglycosylated chorionic gonadotropin converts the antagonist to an agonist
    • Rebois R.V., Liss M.T. Antibody binding to the beta-subunit of deglycosylated chorionic gonadotropin converts the antagonist to an agonist. J. Biol. Chem. 1987, 262:3891-3896.
    • (1987) J. Biol. Chem. , vol.262 , pp. 3891-3896
    • Rebois, R.V.1    Liss, M.T.2
  • 198
    • 0019447666 scopus 로고
    • Disulfide bonds of glycoprotein hormones. Their selective reduction in the beta subunits of bovine lutropin and thyrotropin
    • Reeve J.R., Pierce J.G. Disulfide bonds of glycoprotein hormones. Their selective reduction in the beta subunits of bovine lutropin and thyrotropin. Int. J. Pept. Protein Res. 1981, 18:79-87.
    • (1981) Int. J. Pept. Protein Res. , vol.18 , pp. 79-87
    • Reeve, J.R.1    Pierce, J.G.2
  • 199
    • 0016722739 scopus 로고
    • Partial reduction of disulfide bonds in the hormone-specific subunits of TSH and LH
    • Reeve J.R., Cheng K.W., Pierce J.G. Partial reduction of disulfide bonds in the hormone-specific subunits of TSH and LH. Biochem. Biophys. Res. Commun. 1975, 67:149-155.
    • (1975) Biochem. Biophys. Res. Commun. , vol.67 , pp. 149-155
    • Reeve, J.R.1    Cheng, K.W.2    Pierce, J.G.3
  • 202
    • 0344739567 scopus 로고    scopus 로고
    • Self-association and raft localization of functional luteinizing hormone receptors
    • Roess D.A., Smith S.M. Self-association and raft localization of functional luteinizing hormone receptors. Biol. Reprod. 2003, 69:1765-1770.
    • (2003) Biol. Reprod. , vol.69 , pp. 1765-1770
    • Roess, D.A.1    Smith, S.M.2
  • 203
    • 0034522937 scopus 로고    scopus 로고
    • Luteinizing hormone receptors are self-associated in the plasma membrane
    • Roess D.A., Horvat R.D., Munnelly H., Barisas B.G. Luteinizing hormone receptors are self-associated in the plasma membrane. Endocrinology 2000, 141:4518-4523.
    • (2000) Endocrinology , vol.141 , pp. 4518-4523
    • Roess, D.A.1    Horvat, R.D.2    Munnelly, H.3    Barisas, B.G.4
  • 204
    • 66249144426 scopus 로고    scopus 로고
    • The structure and function of G-protein-coupled receptors
    • Rosenbaum D.M., Rasmussen S.G., Kobilka B.K. The structure and function of G-protein-coupled receptors. Nature 2009, 459:356-363.
    • (2009) Nature , vol.459 , pp. 356-363
    • Rosenbaum, D.M.1    Rasmussen, S.G.2    Kobilka, B.K.3
  • 205
    • 0032962457 scopus 로고    scopus 로고
    • Twilight zone of protein sequence alignments
    • Rost B. Twilight zone of protein sequence alignments. Protein Eng. 1999, 12:85-94.
    • (1999) Protein Eng. , vol.12 , pp. 85-94
    • Rost, B.1
  • 206
    • 0028933948 scopus 로고
    • Scanning-alanine mutagenesis of long loop residues 33-53 in follicle stimulating hormone beta subunit
    • Roth K.E., Dias J.A. Scanning-alanine mutagenesis of long loop residues 33-53 in follicle stimulating hormone beta subunit. Mol. Cell. Endocrinol. 1995, 109:143-149.
    • (1995) Mol. Cell. Endocrinol. , vol.109 , pp. 143-149
    • Roth, K.E.1    Dias, J.A.2
  • 207
    • 73049085563 scopus 로고    scopus 로고
    • The asymmetric/symmetric activation of GPCR dimers as a possible mechanistic rationale for multiple signalling pathways
    • Rovira X., Pin J.P., Giraldo J. The asymmetric/symmetric activation of GPCR dimers as a possible mechanistic rationale for multiple signalling pathways. Trends Pharmacol. Sci. 2010, 31:15-21.
    • (2010) Trends Pharmacol. Sci. , vol.31 , pp. 15-21
    • Rovira, X.1    Pin, J.P.2    Giraldo, J.3
  • 208
    • 0037033014 scopus 로고    scopus 로고
    • Structural requirements for mutational lutropin/choriogonadotropin receptor activation
    • Sangkuhl K., Schulz A., Schultz G., Schoneberg T. Structural requirements for mutational lutropin/choriogonadotropin receptor activation. J. Biol. Chem. 2002, 277:47748-47755.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47748-47755
    • Sangkuhl, K.1    Schulz, A.2    Schultz, G.3    Schoneberg, T.4
  • 209
    • 0030780763 scopus 로고    scopus 로고
    • Differences in active site gorge dimensions of cholinesterases revealed by binding of inhibitors to human butyrylcholinesterase
    • Saxena A., Redman A.M., Jiang X., Lockridge O., Doctor B. Differences in active site gorge dimensions of cholinesterases revealed by binding of inhibitors to human butyrylcholinesterase. Biochemistry 1997, 36:14642-14651.
    • (1997) Biochemistry , vol.36 , pp. 14642-14651
    • Saxena, A.1    Redman, A.M.2    Jiang, X.3    Lockridge, O.4    Doctor, B.5
  • 210
    • 0015219017 scopus 로고
    • Isolation of the luteinizing hormone and follicle-stimulating hormone-releasing hormone from porcine hypothalami
    • Schally A.V., Nair R.M., Redding T.W., Arimura A. Isolation of the luteinizing hormone and follicle-stimulating hormone-releasing hormone from porcine hypothalami. J. Biol. Chem. 1971, 246:7230-7236.
    • (1971) J. Biol. Chem. , vol.246 , pp. 7230-7236
    • Schally, A.V.1    Nair, R.M.2    Redding, T.W.3    Arimura, A.4
  • 211
    • 0026633842 scopus 로고
    • An unusual feature revealed by the crystal structure at 2.2Å resolution of human transforming growth factor-beta 2
    • Schlunegger M.P., Grutter M.G. An unusual feature revealed by the crystal structure at 2.2Å resolution of human transforming growth factor-beta 2. Nature 1992, 358:430-434.
    • (1992) Nature , vol.358 , pp. 430-434
    • Schlunegger, M.P.1    Grutter, M.G.2
  • 212
    • 8844282097 scopus 로고
    • Hormone production by placental cells maintained in continuous culture
    • Seegar-Jones G.E., Gey G.O., Ghisletta M. Hormone production by placental cells maintained in continuous culture. Bull. John Hopkins Hosp. 1943, 72:26-38.
    • (1943) Bull. John Hopkins Hosp. , vol.72 , pp. 26-38
    • Seegar-Jones, G.E.1    Gey, G.O.2    Ghisletta, M.3
  • 213
    • 0027158153 scopus 로고
    • The lutropin/choriogonadotropin receptor... 4 years later
    • Segaloff D.L., Ascoli M. The lutropin/choriogonadotropin receptor... 4 years later. Endocr. Rev. 1993, 14:324-347.
    • (1993) Endocr. Rev. , vol.14 , pp. 324-347
    • Segaloff, D.L.1    Ascoli, M.2
  • 214
    • 77954911810 scopus 로고    scopus 로고
    • Structures of a platelet-derived growth factor/propeptide complex and a platelet-derived growth factor/receptor complex
    • Shim A.H., Liu H., Focia P.J., Chen X., Lin P.C., He X. Structures of a platelet-derived growth factor/propeptide complex and a platelet-derived growth factor/receptor complex. Proc. Natl. Acad. Sci. USA 2010, 107:11307-11312.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 11307-11312
    • Shim, A.H.1    Liu, H.2    Focia, P.J.3    Chen, X.4    Lin, P.C.5    He, X.6
  • 215
    • 0031457992 scopus 로고    scopus 로고
    • The follicle-stimulating hormone receptor: biochemistry, molecular biology, physiology, and pathophysiology
    • Simoni M., Gromoll J., Nieschlag E. The follicle-stimulating hormone receptor: biochemistry, molecular biology, physiology, and pathophysiology. Endocr. Rev. 1997, 18:739-773.
    • (1997) Endocr. Rev. , vol.18 , pp. 739-773
    • Simoni, M.1    Gromoll, J.2    Nieschlag, E.3
  • 217
    • 0001523352 scopus 로고
    • Ablation and transplantation of the hypophyses of the rat
    • Smith P.E. Ablation and transplantation of the hypophyses of the rat. Anat. Rec. 1926, 32:221.
    • (1926) Anat. Rec. , vol.32 , pp. 221
    • Smith, P.E.1
  • 218
    • 84964098129 scopus 로고
    • Hastening development of female genital system by daily hymoplastic pituitary transplants
    • Smith P.E. Hastening development of female genital system by daily hymoplastic pituitary transplants. Proc. Soc. Exp. Biol. Med. 1926, 24:131-132.
    • (1926) Proc. Soc. Exp. Biol. Med. , vol.24 , pp. 131-132
    • Smith, P.E.1
  • 220
    • 0035793620 scopus 로고    scopus 로고
    • Hormone interactions to Leu-rich repeats in the gonadotropin receptors. I. Analysis of Leu-rich repeats of human luteinizing hormone/chorionic gonadotropin receptor and follicle-stimulating hormone receptor
    • Song Y.S., Ji I., Beauchamp J., Isaacs N.W., Ji T.H. Hormone interactions to Leu-rich repeats in the gonadotropin receptors. I. Analysis of Leu-rich repeats of human luteinizing hormone/chorionic gonadotropin receptor and follicle-stimulating hormone receptor. J. Biol. Chem. 2001, 276:3426-3435.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3426-3435
    • Song, Y.S.1    Ji, I.2    Beauchamp, J.3    Isaacs, N.W.4    Ji, T.H.5
  • 221
    • 0025237466 scopus 로고
    • The testicular receptor for follicle stimulating hormone: structure and functional expression of cloned cDNA
    • Sprengel R., Braun T., Nikolics K., Segaloff D.L., Seeburg P.H. The testicular receptor for follicle stimulating hormone: structure and functional expression of cloned cDNA. Mol. Endocrinol. 1990, 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
  • 222
    • 0018091794 scopus 로고
    • Birth after the reimplantation of a human embryo
    • Steptoe P.C., Edwards R.G. Birth after the reimplantation of a human embryo. Lancet 1978, 2:366.
    • (1978) Lancet , vol.2 , pp. 366
    • Steptoe, P.C.1    Edwards, R.G.2
  • 224
    • 0029112363 scopus 로고
    • Asparagine-linked oligosaccharide structures determine clearance and organ distribution of pituitary and recombinant thyrotropin
    • Szkudlinski M.W., Thotakura N.R., Tropea J.E., Grossmann M., Weintraub B.D. Asparagine-linked oligosaccharide structures determine clearance and organ distribution of pituitary and recombinant thyrotropin. Endocrinology 1995, 136:3325-3330.
    • (1995) Endocrinology , vol.136 , pp. 3325-3330
    • Szkudlinski, M.W.1    Thotakura, N.R.2    Tropea, J.E.3    Grossmann, M.4    Weintraub, B.D.5
  • 226
    • 0036083401 scopus 로고    scopus 로고
    • Thyroid-stimulating hormone and thyroid-stimulating hormone receptor structure-function relationships
    • Szkudlinski M.W., Fremont V., Ronin C., Weintraub B.D. Thyroid-stimulating hormone and thyroid-stimulating hormone receptor structure-function relationships. Physiol. Rev. 2002, 82:473-502.
    • (2002) Physiol. Rev. , vol.82 , pp. 473-502
    • Szkudlinski, M.W.1    Fremont, V.2    Ronin, C.3    Weintraub, B.D.4
  • 227
    • 0032561127 scopus 로고    scopus 로고
    • A novel three-dimensional crystal of bacteriorhodopsin obtained by successive fusion of the vesicular assemblies
    • Takeda K., Sato H., Hino T., Kono M., Fukuda K., Sakurai I., Okada T., Kouyama T. A novel three-dimensional crystal of bacteriorhodopsin obtained by successive fusion of the vesicular assemblies. J. Mol. Biol. 1998, 283:463-474.
    • (1998) J. Mol. Biol. , vol.283 , pp. 463-474
    • Takeda, K.1    Sato, H.2    Hino, T.3    Kono, M.4    Fukuda, K.5    Sakurai, I.6    Okada, T.7    Kouyama, T.8
  • 228
    • 0021265260 scopus 로고
    • Evolution of the genes for the beta subunits of human chorionic gonadotropin and luteinizing hormone
    • Talmadge K., Vamvakopoulos N.C., Fiddes J.C. Evolution of the genes for the beta subunits of human chorionic gonadotropin and luteinizing hormone. Nature 1984, 307:37-40.
    • (1984) Nature , vol.307 , pp. 37-40
    • Talmadge, K.1    Vamvakopoulos, N.C.2    Fiddes, J.C.3
  • 229
    • 77957040480 scopus 로고    scopus 로고
    • Follicle stimulating hormone receptor mutations and reproductive disorders
    • Tao Y.X., Segaloff D.L. Follicle stimulating hormone receptor mutations and reproductive disorders. Prog. Mol. Biol. Transl. Sci. 2009, 89:115-131.
    • (2009) Prog. Mol. Biol. Transl. Sci. , vol.89 , pp. 115-131
    • Tao, Y.X.1    Segaloff, D.L.2
  • 230
    • 1242272013 scopus 로고    scopus 로고
    • Constitutive and agonist-dependent self-association of the cell surface human lutropin receptor
    • Tao Y.X., Johnson N.B., Segaloff D.L. Constitutive and agonist-dependent self-association of the cell surface human lutropin receptor. J. Biol. Chem. 2004, 279:5904-5914.
    • (2004) J. Biol. Chem. , vol.279 , pp. 5904-5914
    • Tao, Y.X.1    Johnson, N.B.2    Segaloff, D.L.3
  • 232
    • 0033603623 scopus 로고    scopus 로고
    • Crystal structure of a ternary complex between human chorionic gonadotropin (hCG) and two Fv fragments specific for the alpha and beta-subunits
    • Tegoni M., Spinelli S., Verhoeyen M., Davis P., Cambillau C. Crystal structure of a ternary complex between human chorionic gonadotropin (hCG) and two Fv fragments specific for the alpha and beta-subunits. J. Mol. Biol. 1999, 289:1375-1385.
    • (1999) J. Mol. Biol. , vol.289 , pp. 1375-1385
    • Tegoni, M.1    Spinelli, S.2    Verhoeyen, M.3    Davis, P.4    Cambillau, C.5
  • 233
    • 34249792937 scopus 로고    scopus 로고
    • Follice-stimulating hormone receptor forms oligomers and shows evidence of carboxyl-terminal proteolytic processing
    • Thomas R.M., Nechamen C.A., Mazurkiewicz J.E., Muda M., Palmer S., Dias J.A. Follice-stimulating hormone receptor forms oligomers and shows evidence of carboxyl-terminal proteolytic processing. Endocrinology 2007, 148:1987-1995.
    • (2007) Endocrinology , vol.148 , pp. 1987-1995
    • Thomas, R.M.1    Nechamen, C.A.2    Mazurkiewicz, J.E.3    Muda, M.4    Palmer, S.5    Dias, J.A.6
  • 235
    • 2142832504 scopus 로고
    • The morphology and physiology of the salamander thyroid gland II. The anterior lobe of the hypophysis as a control mechanism of the function of the thyroid gland
    • Uhlenhuth E., Schwartzbach S. The morphology and physiology of the salamander thyroid gland II. The anterior lobe of the hypophysis as a control mechanism of the function of the thyroid gland. J. Exp. Biol. 1927, 5:1-5.
    • (1927) J. Exp. Biol. , vol.5 , pp. 1-5
    • Uhlenhuth, E.1    Schwartzbach, S.2
  • 236
  • 240
    • 0031555865 scopus 로고    scopus 로고
    • Glycosylation beyond the Asn78-linked GlcNAc residue has a significant enhancing effect on the stability of the alpha subunit of human chorionic gonadotropin
    • van Zuylen C.W., Kamerling J.P., Vliegenthart J.F. Glycosylation beyond the Asn78-linked GlcNAc residue has a significant enhancing effect on the stability of the alpha subunit of human chorionic gonadotropin. Biochem. Biophys. Res. Commun. 1997, 232:117-120.
    • (1997) Biochem. Biophys. Res. Commun. , vol.232 , pp. 117-120
    • van Zuylen, C.W.1    Kamerling, J.P.2    Vliegenthart, J.F.3
  • 241
    • 76649138642 scopus 로고    scopus 로고
    • An in vivo demonstration of functional G protein-coupled receptor dimers
    • Vassart G. An in vivo demonstration of functional G protein-coupled receptor dimers. Proc. Natl. Acad. Sci. USA 2010, 107:1819-1820.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 1819-1820
    • Vassart, G.1
  • 242
    • 79957562543 scopus 로고    scopus 로고
    • G protein-coupled receptors: mutations and endocrine diseases
    • Vassart G., Costagliola S. G protein-coupled receptors: mutations and endocrine diseases. Nat. Rev. Endocrinol. 2011, 7:362-372.
    • (2011) Nat. Rev. Endocrinol. , vol.7 , pp. 362-372
    • Vassart, G.1    Costagliola, S.2
  • 243
    • 0142056956 scopus 로고    scopus 로고
    • Opposite contribution of two ligand-selective determinants in the N-terminal hormone-binding exodomain of human gonadotropin receptors
    • Vischer H.F., Granneman J.C., Bogerd J. Opposite contribution of two ligand-selective determinants in the N-terminal hormone-binding exodomain of human gonadotropin receptors. Mol. Endocrinol. 2003, 17:1972-1981.
    • (2003) Mol. Endocrinol. , vol.17 , pp. 1972-1981
    • Vischer, H.F.1    Granneman, J.C.2    Bogerd, J.3
  • 244
    • 0036214718 scopus 로고    scopus 로고
    • Activation of the cAMP pathway by the TSH receptor involves switching of the ectodomain from a tethered inverse agonist to an agonist
    • Vlaeminck-Guillem V., Ho S.C., Rodien P., Vassart G., Costagliola S. Activation of the cAMP pathway by the TSH receptor involves switching of the ectodomain from a tethered inverse agonist to an agonist. Mol. Endocrinol. 2002, 16:736-746.
    • (2002) Mol. Endocrinol. , vol.16 , pp. 736-746
    • Vlaeminck-Guillem, V.1    Ho, S.C.2    Rodien, P.3    Vassart, G.4    Costagliola, S.5
  • 245
    • 0034886490 scopus 로고    scopus 로고
    • Characterization of human FSH isoforms reveals a nonglycosylated beta-subunit in addition to the conventional glycosylated beta-subunit
    • Walton W.J., Nguyen V.T., Butnev V.Y., Singh V., Moore W.T., Bousfield G.R. Characterization of human FSH isoforms reveals a nonglycosylated beta-subunit in addition to the conventional glycosylated beta-subunit. J. Clin. Endocrinol. Metab. 2001, 86:3675-3685.
    • (2001) J. Clin. Endocrinol. Metab. , vol.86 , pp. 3675-3685
    • Walton, W.J.1    Nguyen, V.T.2    Butnev, V.Y.3    Singh, V.4    Moore, W.T.5    Bousfield, G.R.6
  • 246
    • 84879189812 scopus 로고    scopus 로고
    • Structural basis for R-spondin recognition by LGR4/5/6 receptors
    • Wang D., Huang B., Zhang S., Yu X., Wu W., Wang X. Structural basis for R-spondin recognition by LGR4/5/6 receptors. Genes Dev. 2013, 27:1339-1344.
    • (2013) Genes Dev. , vol.27 , pp. 1339-1344
    • Wang, D.1    Huang, B.2    Zhang, S.3    Yu, X.4    Wu, W.5    Wang, X.6
  • 247
    • 0011238705 scopus 로고
    • Animal models for research
    • Harper and Row, Baltimore, MD, N.J. Alexander (Ed.)
    • Ward D.N., Moore W.T. Animal models for research. Fertility and Contraception 1979, Harper and Row, Baltimore, MD, pp. 151-164. N.J. Alexander (Ed.).
    • (1979) Fertility and Contraception , pp. 151-164
    • Ward, D.N.1    Moore, W.T.2
  • 248
    • 0022637883 scopus 로고
    • Characterization of cleavage products in selected human lutropin preparations
    • Ward D.N., Glenn S.D., Nahm H.S., Wen T. Characterization of cleavage products in selected human lutropin preparations. Int. J. Pept. Protein Res. 1986, 27:70-78.
    • (1986) Int. J. Pept. Protein Res. , vol.27 , pp. 70-78
    • Ward, D.N.1    Glenn, S.D.2    Nahm, H.S.3    Wen, T.4
  • 249
    • 0018373262 scopus 로고
    • Conformations of twisted parallel beta-sheets and the origin of chirality in protein structures
    • Weatherford D.W., Salemme F.R. Conformations of twisted parallel beta-sheets and the origin of chirality in protein structures. Proc. Natl. Acad. Sci. USA 1979, 76:19-23.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 19-23
    • Weatherford, D.W.1    Salemme, F.R.2
  • 250
    • 0026335545 scopus 로고
    • Hypogonadism caused by a single amino acid substitution in the beta subunit of luteinizing hormone
    • Weiss J., Axelrod L., Whitcomb R.W., Harris P.E., Crowley W.F., Jameson J.L. Hypogonadism caused by a single amino acid substitution in the beta subunit of luteinizing hormone. N. Engl. J. Med. 1992, 326:179-183.
    • (1992) N. Engl. J. Med. , vol.326 , pp. 179-183
    • Weiss, J.1    Axelrod, L.2    Whitcomb, R.W.3    Harris, P.E.4    Crowley, W.F.5    Jameson, J.L.6
  • 251
  • 252
    • 0024351072 scopus 로고
    • Functionally distinct agonist and receptor-binding regions in human chorionic gonadotropin. Development of a tertiary structure model
    • Willey K.P., Leidenberger F. Functionally distinct agonist and receptor-binding regions in human chorionic gonadotropin. Development of a tertiary structure model. J. Biol. Chem. 1989, 264:19716-19729.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19716-19729
    • Willey, K.P.1    Leidenberger, F.2
  • 253
    • 0028773646 scopus 로고
    • Structure of human chorionic gonadotropin at 2.6Å resolution from MAD analysis of the selenomethionyl protein
    • Wu H., Lustbader J.W., Liu Y., Canfield R.E., Hendrickson W.A. Structure of human chorionic gonadotropin at 2.6Å resolution from MAD analysis of the selenomethionyl protein. Structure 1994, 2:545-558.
    • (1994) Structure , vol.2 , pp. 545-558
    • Wu, H.1    Lustbader, J.W.2    Liu, Y.3    Canfield, R.E.4    Hendrickson, W.A.5
  • 254
    • 0037470737 scopus 로고    scopus 로고
    • Efficient preparation of glycoprotein hormones lacking an alpha-subunit oligosaccharide
    • Xing Y., Moyle W.R. Efficient preparation of glycoprotein hormones lacking an alpha-subunit oligosaccharide. Biochem. Biophys. Res. Commun. 2003, 303:201-205.
    • (2003) Biochem. Biophys. Res. Commun. , vol.303 , pp. 201-205
    • Xing, Y.1    Moyle, W.R.2
  • 255
    • 7244236581 scopus 로고    scopus 로고
    • Use of protein knobs to characterize the position of conserved alpha-subunit regions in lutropin receptor complexes
    • Xing Y., Lin W., Jiang M., Cao D., Myers R.V., Bernard M.P., Moyle W.R. Use of protein knobs to characterize the position of conserved alpha-subunit regions in lutropin receptor complexes. J. Biol. Chem. 2004, 279:44427-44437.
    • (2004) J. Biol. Chem. , vol.279 , pp. 44427-44437
    • Xing, Y.1    Lin, W.2    Jiang, M.3    Cao, D.4    Myers, R.V.5    Bernard, M.P.6    Moyle, W.R.7
  • 256
    • 4143052436 scopus 로고    scopus 로고
    • Glycoprotein hormone assembly in the endoplasmic reticulum: III. The seatbelt and its latch site determine the assembly pathway
    • Xing Y., Myers R.V., Cao D., Lin W., Jiang M., Bernard M.P., Moyle W.R. Glycoprotein hormone assembly in the endoplasmic reticulum: III. The seatbelt and its latch site determine the assembly pathway. J. Biol. Chem. 2004, 279:35449-35457.
    • (2004) J. Biol. Chem. , vol.279 , pp. 35449-35457
    • Xing, Y.1    Myers, R.V.2    Cao, D.3    Lin, W.4    Jiang, M.5    Bernard, M.P.6    Moyle, W.R.7
  • 258
    • 0027493757 scopus 로고
    • COOH-terminal amino acids of the alpha subunit play common and different roles in human choriogonadotropin and follitropin
    • Yoo J., Zeng H., Ji I., Murdoch W.J., Ji T.H. COOH-terminal amino acids of the alpha subunit play common and different roles in human choriogonadotropin and follitropin. J. Biol. Chem. 1993, 268:13034-13042.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13034-13042
    • Yoo, J.1    Zeng, H.2    Ji, I.3    Murdoch, W.J.4    Ji, T.H.5
  • 259
    • 0034457935 scopus 로고    scopus 로고
    • The extracellular domain suppresses constitutive activity of the transmembrane domain of the human TSH receptor: implications for hormone-receptor interaction and antagonist design
    • Zhang M., Tong K.P., Fremont V., Chen J., Narayan P., Puett D., Weintraub B.D., Szkudlinski M.W. The extracellular domain suppresses constitutive activity of the transmembrane domain of the human TSH receptor: implications for hormone-receptor interaction and antagonist design. Endocrinology 2000, 141:3514-3517.
    • (2000) Endocrinology , vol.141 , pp. 3514-3517
    • Zhang, M.1    Tong, K.P.2    Fremont, V.3    Chen, J.4    Narayan, P.5    Puett, D.6    Weintraub, B.D.7    Szkudlinski, M.W.8
  • 261
    • 84866107252 scopus 로고    scopus 로고
    • Evidence for activity-regulated hormone-binding cooperativity across glycoprotein hormone receptor homomers
    • Zoenen M., Urizar E., Swillens S., Vassart G., Costagliola S. Evidence for activity-regulated hormone-binding cooperativity across glycoprotein hormone receptor homomers. Nat. Commun. 2012, 3:1007.
    • (2012) Nat. Commun. , vol.3 , pp. 1007
    • Zoenen, M.1    Urizar, E.2    Swillens, S.3    Vassart, G.4    Costagliola, S.5
  • 262
    • 26644438991 scopus 로고
    • Ueber die Funktion des Ovariums
    • Zondek B. Ueber die Funktion des Ovariums. Z. Geburtsh. Gynäkol. 1926, 90:372-376.
    • (1926) Z. Geburtsh. Gynäkol. , vol.90 , pp. 372-376
    • Zondek, B.1
  • 263
    • 8844229148 scopus 로고
    • Weitere Untersuchungen zur Darstellung, Biologie und Klinik des Hypophysenvorderlappen-hormons (Prolan)
    • Zondek B. Weitere Untersuchungen zur Darstellung, Biologie und Klinik des Hypophysenvorderlappen-hormons (Prolan). Z. Gynäkol. 1929, 14:834-848.
    • (1929) Z. Gynäkol. , vol.14 , pp. 834-848
    • Zondek, B.1
  • 264
    • 6044222112 scopus 로고
    • Über die Hormone des Hypophysenvorderlappens. II. Follikelreifungshormon Prolan A-Klimakterium-Kastration
    • Zondek B. Über die Hormone des Hypophysenvorderlappens. II. Follikelreifungshormon Prolan A-Klimakterium-Kastration. Klin. Wochenschr. 1930, 9:393-396.
    • (1930) Klin. Wochenschr. , vol.9 , pp. 393-396
    • Zondek, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.