메뉴 건너뛰기




Volumn , Issue , 2009, Pages 35-55

The Gonadotropin Hormones and Their Receptors

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84884013649     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-1-4160-4907-4.00002-4     Document Type: Chapter
Times cited : (13)

References (493)
  • 1
    • 0033829535 scopus 로고    scopus 로고
    • Molecular architecture and biorecognition processes of the cystine knot protein superfamily: Part I. The glycoprotein hormones
    • Hearn M.T.W., Gomme P.T. Molecular architecture and biorecognition processes of the cystine knot protein superfamily: Part I. The glycoprotein hormones. J Mol Recognit 2000, 13:223-278.
    • (2000) J Mol Recognit , vol.13 , pp. 223-278
    • Hearn, M.T.W.1    Gomme, P.T.2
  • 2
    • 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
  • 3
    • 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
  • 4
    • 20444449695 scopus 로고    scopus 로고
    • The LH beta gene of several mammals embeds a carboxyl-terminal peptide-like sequence revealing a critical role for mucin oligosaccharides in the evolution of lutropin to chorionic gonadotropin in the animal phyla
    • Nakav S., Jablonka-Shariff A., Kaner S., et al. The LH beta gene of several mammals embeds a carboxyl-terminal peptide-like sequence revealing a critical role for mucin oligosaccharides in the evolution of lutropin to chorionic gonadotropin in the animal phyla. J Biol Chem 2005, 280:16676-16684.
    • (2005) J Biol Chem , vol.280 , pp. 16676-16684
    • Nakav, S.1    Jablonka-Shariff, A.2    Kaner, S.3
  • 5
    • 0028239813 scopus 로고
    • Crystal-structure of human chorionic-gonadotropin
    • Lapthorn A.J., Harris D.C., Littlejohn A., et al. Crystal-structure of human chorionic-gonadotropin. Nature 1994, 369:455-461.
    • (1994) Nature , vol.369 , pp. 455-461
    • Lapthorn, A.J.1    Harris, D.C.2    Littlejohn, A.3
  • 6
    • 0028773646 scopus 로고
    • Structure of human chorionic-gonadotropin at 2.6-angstrom resolution from MAD analysis of the selenomethionyl protein
    • Wu H., Lustbader J.W., Liu Y., et al. Structure of human chorionic-gonadotropin at 2.6-angstrom 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
  • 7
    • 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., et al. 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
  • 8
    • 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
  • 9
    • 24644464170 scopus 로고    scopus 로고
    • Structural biology of glycoprotein hormones and their receptors
    • Fan Q.R., Hendrickson W.A. Structural biology of glycoprotein hormones and their receptors. Endocrine 2005, 26:179-188.
    • (2005) Endocrine , vol.26 , pp. 179-188
    • Fan, Q.R.1    Hendrickson, W.A.2
  • 10
    • 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
  • 11
    • 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
  • 12
    • 0008792636 scopus 로고
    • Chorionic gonadotropin: comparative studies and comments on relationships to other glycoprotein hormones
    • Plenum Press, New York, S.J. Segal (Ed.)
    • Moore W.T., Burleigh B.D., Ward D.N. Chorionic gonadotropin: comparative studies and comments on relationships to other glycoprotein hormones. Chorionic Gonadotropin 1980, 89-126. Plenum Press, New York. S.J. Segal (Ed.).
    • (1980) Chorionic Gonadotropin , pp. 89-126
    • Moore, W.T.1    Burleigh, B.D.2    Ward, D.N.3
  • 13
    • 0029824825 scopus 로고    scopus 로고
    • NMR studies of the free alpha subunit of human chorionic gonadotropin: structural influences of N-glycosylation and the beta subunit on the conformation of the alpha subunit
    • DeBeer T., VanZuylen C., Leeflang B.R., et al. NMR studies of the free alpha subunit of human chorionic gonadotropin: structural influences of N-glycosylation and the beta subunit on the conformation of the alpha subunit. Eur J Biochem 1996, 241:229-242.
    • (1996) Eur J Biochem , vol.241 , pp. 229-242
    • DeBeer, T.1    VanZuylen, C.2    Leeflang, B.R.3
  • 14
    • 0343607059 scopus 로고    scopus 로고
    • Solution structure of the alpha-subunit of human chorionic gonadotropin
    • Erbel P.J.A., Karimi-Nejad Y., De Beer T., et al. Solution structure of the alpha-subunit of human chorionic gonadotropin. Eur J Biochem 1999, 260:490-498.
    • (1999) Eur J Biochem , vol.260 , pp. 490-498
    • Erbel, P.J.A.1    Karimi-Nejad, Y.2    De Beer, T.3
  • 15
    • 0020328269 scopus 로고
    • Circular dichroic and immunological properties of human chorio-gonadotropin beta carboxyl terminal peptides
    • Puett D., Ryan R.J., Stevens V.C. Circular dichroic and immunological properties of human chorio-gonadotropin beta carboxyl terminal peptides. Int J Peptide Protein Res 1982, 19:506-513.
    • (1982) Int J Peptide Protein Res , vol.19 , pp. 506-513
    • Puett, D.1    Ryan, R.J.2    Stevens, V.C.3
  • 16
    • 0029881867 scopus 로고    scopus 로고
    • Structural analysis of the carboxyl terminal peptide from human chorionic gonadotropin beta-subunit by two-dimensional nuclear magnetic resonance spectroscopy
    • Rock E.P., Czaplicki J., Milon A. Structural analysis of the carboxyl terminal peptide from human chorionic gonadotropin beta-subunit by two-dimensional nuclear magnetic resonance spectroscopy. Am J Reprod Immunol 1996, 35:156-162.
    • (1996) Am J Reprod Immunol , vol.35 , pp. 156-162
    • Rock, E.P.1    Czaplicki, J.2    Milon, A.3
  • 17
    • 0031692251 scopus 로고    scopus 로고
    • Expression of a bioactive, single-chain choriogonadotropin in dictyostelium discoideum
    • Heikoop J.C., Grootenhuis P.D.J., Blaauw M., et al. Expression of a bioactive, single-chain choriogonadotropin in dictyostelium discoideum. Eur J Biochem 1998, 256:359-363.
    • (1998) Eur J Biochem , vol.256 , pp. 359-363
    • Heikoop, J.C.1    Grootenhuis, P.D.J.2    Blaauw, M.3
  • 18
    • 0036606845 scopus 로고    scopus 로고
    • Studies on the relevance of the glycan at Asn-52 of the alpha-subunit of human chorionic gonadotropin in the alpha-beta dimer
    • Erbel P.J.A., Haseley S.R., Kamerling J.P., et al. Studies on the relevance of the glycan at Asn-52 of the alpha-subunit of human chorionic gonadotropin in the alpha-beta dimer. Biochem J 2002, 364:485-495.
    • (2002) Biochem J , vol.364 , pp. 485-495
    • Erbel, P.J.A.1    Haseley, S.R.2    Kamerling, J.P.3
  • 19
    • 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.A., Karimi-Nejad Y., van Kuik J.A., et al. 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.A.1    Karimi-Nejad, Y.2    van Kuik, J.A.3
  • 22
    • 0035002425 scopus 로고    scopus 로고
    • Is there any physiological role for gonadotrophin oligosaccharide heterogeneity in humans? II. A biochemical point of view
    • Dias J.A. Is there any physiological role for gonadotrophin oligosaccharide heterogeneity in humans? II. A biochemical point of view. Hum Reprod 2001, 16:825-830.
    • (2001) Hum Reprod , vol.16 , pp. 825-830
    • Dias, J.A.1
  • 23
    • 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
  • 24
    • 33751214528 scopus 로고    scopus 로고
    • Carbohydrate complexity and proportions of serum FSH isoforms in the male: lectin-based studies
    • Campo S., Ambao V., Creus S., et al. Carbohydrate complexity and proportions of serum FSH isoforms in the male: lectin-based studies. Mol Cell Endocrinol 2007, 260:197-204.
    • (2007) Mol Cell Endocrinol , vol.260 , pp. 197-204
    • Campo, S.1    Ambao, V.2    Creus, S.3
  • 25
    • 33751226291 scopus 로고    scopus 로고
    • Hyperglycosylated hCG: a variant with separate biological functions to regular hCG
    • Cole L.A., Khanlian S.A. Hyperglycosylated hCG: a variant with separate biological functions to regular hCG. Mol Cell Endocrinol 2007, 260:228-236.
    • (2007) Mol Cell Endocrinol , vol.260 , pp. 228-236
    • Cole, L.A.1    Khanlian, S.A.2
  • 26
    • 34748926103 scopus 로고    scopus 로고
    • Human chorionic gonadotropin produced by the invasive trophoblast but not the villous trophoblast promotes cell invasion and is down-regulated by peroxisome proliferator-activated receptor-gamma
    • Handschuh K., Guibourdenche J., Tsatsaris V., et al. Human chorionic gonadotropin produced by the invasive trophoblast but not the villous trophoblast promotes cell invasion and is down-regulated by peroxisome proliferator-activated receptor-gamma. Endocrinology 2007, 148:5011-5019.
    • (2007) Endocrinology , vol.148 , pp. 5011-5019
    • Handschuh, K.1    Guibourdenche, J.2    Tsatsaris, V.3
  • 27
    • 0022858517 scopus 로고
    • Differential processing of asn-linked oligosaccharides on pituitary glycoprotein hormones: implications for biologic function
    • Green E.D., Boime I., Baenziger J.U. Differential processing of asn-linked oligosaccharides on pituitary glycoprotein hormones: implications for biologic function. Mol Cell Biochem 1986, 72:81-100.
    • (1986) Mol Cell Biochem , vol.72 , pp. 81-100
    • Green, E.D.1    Boime, I.2    Baenziger, J.U.3
  • 28
    • 33751256292 scopus 로고    scopus 로고
    • All-or-none N-glycosylationin primate follicle-stimulating hormone beta-subunits
    • Bousfield G.R., Butnev V.Y., Walton W.J., et al. All-or-none N-glycosylationin primate follicle-stimulating hormone beta-subunits. Mol Cell Endocrinol 2007, 260:40-48.
    • (2007) Mol Cell Endocrinol , vol.260 , pp. 40-48
    • Bousfield, G.R.1    Butnev, V.Y.2    Walton, W.J.3
  • 29
    • 0037367679 scopus 로고    scopus 로고
    • Glycosylation of human recombinant gonadotrophins: characterization and batch-to-batch consistency
    • Gervais A., Hammel Y.A., Pelloux S., et al. Glycosylation of human recombinant gonadotrophins: characterization and batch-to-batch consistency. Glycobiology 2003, 13:179-189.
    • (2003) Glycobiology , vol.13 , pp. 179-189
    • Gervais, A.1    Hammel, Y.A.2    Pelloux, S.3
  • 30
    • 84883940209 scopus 로고    scopus 로고
    • Site-specific glycosylation analysis of hFSH isoforms
    • 1120-1120
    • Bousfield G.R., Butnev V.Y., Dalpathado D.S., et al. Site-specific glycosylation analysis of hFSH isoforms. Glycobiology 2006, 16. 1120-1120.
    • (2006) Glycobiology , vol.16
    • Bousfield, G.R.1    Butnev, V.Y.2    Dalpathado, D.S.3
  • 31
    • 33745961481 scopus 로고    scopus 로고
    • Glycosylation patterns of human chorionic gonadotropin revealed by liquid chromatography-mass spectrometry and bioinformatics
    • Toll H., Berger P., Hofmann A., et al. Glycosylation patterns of human chorionic gonadotropin revealed by liquid chromatography-mass spectrometry and bioinformatics. Electrophoresis 2006, 27:2734-2746.
    • (2006) Electrophoresis , vol.27 , pp. 2734-2746
    • Toll, H.1    Berger, P.2    Hofmann, A.3
  • 32
    • 33746034592 scopus 로고    scopus 로고
    • Comparative glycomics of the glycoprotein follicle stimulating hormone: glycopeptide analysis of isolates from two mammalian species
    • Dalpathado D.S., Irungu J., Go E.P., et al. Comparative glycomics of the glycoprotein follicle stimulating hormone: glycopeptide analysis of isolates from two mammalian species. Biochemistry 2006, 45:8665-8673.
    • (2006) Biochemistry , vol.45 , pp. 8665-8673
    • Dalpathado, D.S.1    Irungu, J.2    Go, E.P.3
  • 33
    • 33751383272 scopus 로고    scopus 로고
    • Site-specific glycan analysis of human chorionic gonadotropin beta-subunit from malignancies and pregnancy by liquid chromatography-electrospray mass spectrometry
    • Valmu L., Alfthan H., Hotakainen K., et al. Site-specific glycan analysis of human chorionic gonadotropin beta-subunit from malignancies and pregnancy by liquid chromatography-electrospray mass spectrometry. Glycobiology 2006, 16:1207-1218.
    • (2006) Glycobiology , vol.16 , pp. 1207-1218
    • Valmu, L.1    Alfthan, H.2    Hotakainen, K.3
  • 34
    • 33751371491 scopus 로고    scopus 로고
    • An introduction to mass spectrometry based proteomics: detection and characterization of gonadotropins and related molecules
    • Kicman A.T., Parkin M.C., Iles R.K. An introduction to mass spectrometry based proteomics: detection and characterization of gonadotropins and related molecules. Mol Cell Endocrinol 2007, 260:212-227.
    • (2007) Mol Cell Endocrinol , vol.260 , pp. 212-227
    • Kicman, A.T.1    Parkin, M.C.2    Iles, R.K.3
  • 35
    • 0031013738 scopus 로고    scopus 로고
    • Mass spectrometric characterization of the beta-subunit of human chorionic gonadotropin
    • Liu C.L., Bowers L.D. Mass spectrometric characterization of the beta-subunit of human chorionic gonadotropin. J Mass Spectrom 1997, 32:33-42.
    • (1997) J Mass Spectrom , vol.32 , pp. 33-42
    • Liu, C.L.1    Bowers, L.D.2
  • 36
    • 0018675127 scopus 로고
    • Structure and location of the o-glycosidic carbohydrate units of human chorionic-gonadotropin
    • Kessler M.J., Mise T., Ghai R.D., et al. Structure and location of the o-glycosidic carbohydrate units of human chorionic-gonadotropin. J Biol Chem 1979, 254:7909-7914.
    • (1979) J Biol Chem , vol.254 , pp. 7909-7914
    • Kessler, M.J.1    Mise, T.2    Ghai, R.D.3
  • 37
    • 0027182764 scopus 로고
    • Protein-folding and assembly in-vitro parallel intracellular folding and assembly: catalysis of folding and assembly of the human chorionic-gonadotropin alpha-beta dimer by protein disulfide-isomerase
    • Huth J.R., Perini F., Lockridge O., et al. Protein-folding and assembly in-vitro parallel intracellular folding and assembly: catalysis of folding and assembly of the human chorionic-gonadotropin alpha-beta dimer by protein disulfide-isomerase. J Biol Chem 1993, 268:16472-16482.
    • (1993) J Biol Chem , vol.268 , pp. 16472-16482
    • Huth, J.R.1    Perini, F.2    Lockridge, O.3
  • 38
    • 0031030579 scopus 로고    scopus 로고
    • Assisted protein folding
    • Ruddon R.W., Bedows E. Assisted protein folding. J Biol Chem 1997, 272:3125-3128.
    • (1997) J Biol Chem , vol.272 , pp. 3125-3128
    • Ruddon, R.W.1    Bedows, E.2
  • 39
    • 0030037083 scopus 로고    scopus 로고
    • Protein folding in the endoplasmic reticulum: lessons from the human chorionic gonadotropin beta subunit
    • Ruddon R.W., Sherman S.A., Bedows E. Protein folding in the endoplasmic reticulum: lessons from the human chorionic gonadotropin beta subunit. Protein Sci 1996, 5:1443-1452.
    • (1996) Protein Sci , vol.5 , pp. 1443-1452
    • Ruddon, R.W.1    Sherman, S.A.2    Bedows, E.3
  • 40
    • 0034686019 scopus 로고    scopus 로고
    • Cystine knot mutations affect the folding of the glycoprotein hormone alpha-subunit: differential secretion and assembly of partially folded intermediates
    • Darling R.J., Ruddon R.W., Perini F., et al. Cystine knot mutations affect the folding of the glycoprotein hormone alpha-subunit: differential secretion and assembly of partially folded intermediates. J Biol Chem 2000, 275:15413-15421.
    • (2000) J Biol Chem , vol.275 , pp. 15413-15421
    • Darling, R.J.1    Ruddon, R.W.2    Perini, F.3
  • 41
    • 0035815690 scopus 로고    scopus 로고
    • Functional contributions of noncysteine residues within the cystine knots of human chorionic gonadotropin subunits
    • Darling R.J., Wilken J.A., Miller-Lindbolm A.K., et al. Functional contributions of noncysteine residues within the cystine knots of human chorionic gonadotropin subunits. J Biol Chem 2001, 276:10692-10699.
    • (2001) J Biol Chem , vol.276 , pp. 10692-10699
    • Darling, R.J.1    Wilken, J.A.2    Miller-Lindbolm, A.K.3
  • 42
    • 0035895338 scopus 로고    scopus 로고
    • Intracellular folding pathway of the cystine knot-containing glycoprotein hormone alpha-subunit
    • Darling R.J., Wilken J.A., Ruddon R.W., et al. Intracellular folding pathway of the cystine knot-containing glycoprotein hormone alpha-subunit. Biochemistry 2001, 40:577-585.
    • (2001) Biochemistry , vol.40 , pp. 577-585
    • Darling, R.J.1    Wilken, J.A.2    Ruddon, R.W.3
  • 43
    • 2142764423 scopus 로고    scopus 로고
    • Disulfide bond rearrangement during formation of the chorionic gonadotropin beta-subunit cystine knot in vivo
    • Wilken J.A., Bedows E. Disulfide bond rearrangement during formation of the chorionic gonadotropin beta-subunit cystine knot in vivo. Biochemistry 2004, 43:5109-5118.
    • (2004) Biochemistry , vol.43 , pp. 5109-5118
    • Wilken, J.A.1    Bedows, E.2
  • 44
    • 34147125379 scopus 로고    scopus 로고
    • A novel four-amino acid determinant defines conformational freedom within chorionic gonadotropin beta-subunits
    • Wilken J.A., Bedows E. A novel four-amino acid determinant defines conformational freedom within chorionic gonadotropin beta-subunits. Biochemistry 2007, 46:4417-4424.
    • (2007) Biochemistry , vol.46 , pp. 4417-4424
    • Wilken, J.A.1    Bedows, E.2
  • 45
    • 0035107847 scopus 로고    scopus 로고
    • Threading of a glycosylated protein loop through a protein hole: implications for combination of human chorionic gonadotropin subunits
    • Xing Y.N., Williams C., Campbell R.K., et al. Threading of a glycosylated protein loop through a protein hole: implications for combination of human chorionic gonadotropin subunits. Protein Sci 2001, 10:226-235.
    • (2001) Protein Sci , vol.10 , pp. 226-235
    • Xing, Y.N.1    Williams, C.2    Campbell, R.K.3
  • 46
    • 4143088137 scopus 로고    scopus 로고
    • Glycoprotein hormone assembly in the endoplasmic reticulum: I. The glycosylated end of human alpha-subunit loop 2 is threaded through a beta-subunit hole
    • Xing Y.N., Myers R.V., Cao D.H., et al. Glycoprotein hormone assembly in the endoplasmic reticulum: I. The glycosylated end of human alpha-subunit loop 2 is threaded through a beta-subunit hole. J Biol Chem 2004, 279:35426-35436.
    • (2004) J Biol Chem , vol.279 , pp. 35426-35436
    • Xing, Y.N.1    Myers, R.V.2    Cao, D.H.3
  • 47
    • 4143090403 scopus 로고    scopus 로고
    • Glycoprotein hormone assembly in the endoplasmic reticulum: II. Multiple roles of a redox sensitive beta-subunit disulfide switch
    • Xing Y.N., Myers R.V., Cao D.H., et al. Glycoprotein hormone assembly in the endoplasmic reticulum: II. Multiple roles of a redox sensitive beta-subunit disulfide switch. J Biol Chem 2004, 279:35437-35448.
    • (2004) J Biol Chem , vol.279 , pp. 35437-35448
    • Xing, Y.N.1    Myers, R.V.2    Cao, D.H.3
  • 48
    • 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.N., Myers R.V., Cao D.H., et al. 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.N.1    Myers, R.V.2    Cao, D.H.3
  • 49
    • 4143117844 scopus 로고    scopus 로고
    • Glycoprotein hormone assembly in the endoplasmic reticulum: IV. Probable mechanism of subunit docking and completion of assembly
    • Xing Y.N., Myers R.V., Cao D.H., et al. Glycoprotein hormone assembly in the endoplasmic reticulum: IV. Probable mechanism of subunit docking and completion of assembly. J Biol Chem 2004, 279:35458-35468.
    • (2004) J Biol Chem , vol.279 , pp. 35458-35468
    • Xing, Y.N.1    Myers, R.V.2    Cao, D.H.3
  • 50
    • 0034697117 scopus 로고    scopus 로고
    • Disulfide bond formation is not required for human chorionic gonadotropin subunit association: studies with dithiothreitol in JEG-3 cells
    • Singh V., Merz W.E. Disulfide bond formation is not required for human chorionic gonadotropin subunit association: studies with dithiothreitol in JEG-3 cells. J Biol Chem 2000, 275:11765-11770.
    • (2000) J Biol Chem , vol.275 , pp. 11765-11770
    • Singh, V.1    Merz, W.E.2
  • 51
    • 33751211226 scopus 로고    scopus 로고
    • Time-dependent folding of immunological epitopes of the human chorionic gonadotropin beta-subunit
    • Roig J., Krause J.M., Berger P., et al. Time-dependent folding of immunological epitopes of the human chorionic gonadotropin beta-subunit. Mol Cell Endocrinol 2007, 260:12-22.
    • (2007) Mol Cell Endocrinol , vol.260 , pp. 12-22
    • Roig, J.1    Krause, J.M.2    Berger, P.3
  • 52
    • 36348986740 scopus 로고    scopus 로고
    • Non-assembled human chorionic gonadotropin subunits and αα-homodimers use fast-track processing in the secretory pathway in contrast to {αβ}-heterodimers
    • Merz W.E., Krause J.M., Roig J., et al. Non-assembled human chorionic gonadotropin subunits and αα-homodimers use fast-track processing in the secretory pathway in contrast to {αβ}-heterodimers. Endocrinology 2007, 148:5831-5841.
    • (2007) Endocrinology , vol.148 , pp. 5831-5841
    • Merz, W.E.1    Krause, J.M.2    Roig, J.3
  • 53
    • 34948877981 scopus 로고    scopus 로고
    • Rapid maturation of glycoprotein hormone free alpha-subunit (gphalpha) and gphalpha alpha homodimers
    • Krause J.M., Berger P., Roig J., et al. Rapid maturation of glycoprotein hormone free alpha-subunit (gphalpha) and gphalpha alpha homodimers. Mol Endocrinol 2007, 21:2551-2564.
    • (2007) Mol Endocrinol , vol.21 , pp. 2551-2564
    • Krause, J.M.1    Berger, P.2    Roig, J.3
  • 54
    • 0030980393 scopus 로고    scopus 로고
    • Homodimer formation by the individual subunits of bovine lutropin as determined by sedimentation equilibrium
    • Peng K.C., Puett D., Brewer J.M. Homodimer formation by the individual subunits of bovine lutropin as determined by sedimentation equilibrium. J Mol Endocrinol 1997, 18:259-265.
    • (1997) J Mol Endocrinol , vol.18 , pp. 259-265
    • Peng, K.C.1    Puett, D.2    Brewer, J.M.3
  • 55
    • 0032931758 scopus 로고    scopus 로고
    • The beta-subunit of human chorionic gonadotrophin exists as a homodimer
    • Butler S.A., Laidler P., Porter J.R., et al. The beta-subunit of human chorionic gonadotrophin exists as a homodimer. J Mol Endocrinol 1999, 22:185-192.
    • (1999) J Mol Endocrinol , vol.22 , pp. 185-192
    • Butler, S.A.1    Laidler, P.2    Porter, J.R.3
  • 56
    • 0032806224 scopus 로고    scopus 로고
    • Expression and characterization of recombinant beta-subunit hCG homodimer
    • Lobel L., Pollak S., Wang S.J., et al. Expression and characterization of recombinant beta-subunit hCG homodimer. Endocrine 1999, 10:261-270.
    • (1999) Endocrine , vol.10 , pp. 261-270
    • Lobel, L.1    Pollak, S.2    Wang, S.J.3
  • 57
    • 33751234956 scopus 로고    scopus 로고
    • Human chorionic gonadotropin (hCG) in the male reproductive tract
    • Berger P., Gruschwitz M., Spoettl G., et al. Human chorionic gonadotropin (hCG) in the male reproductive tract. Mol Cell Endocrinol 2007, 260:190-196.
    • (2007) Mol Cell Endocrinol , vol.260 , pp. 190-196
    • Berger, P.1    Gruschwitz, M.2    Spoettl, G.3
  • 58
    • 0031763854 scopus 로고    scopus 로고
    • Human endometrial stromal cells generate uncombined alpha-subunit from human chorionic gonadotropin, which can synergize with progesterone to induce decidualization
    • Nemansky M., Moy E., Lyons C.D., et al. Human endometrial stromal cells generate uncombined alpha-subunit from human chorionic gonadotropin, which can synergize with progesterone to induce decidualization. J Clin Endocrinol Metab 1998, 83:575-581.
    • (1998) J Clin Endocrinol Metab , vol.83 , pp. 575-581
    • Nemansky, M.1    Moy, E.2    Lyons, C.D.3
  • 59
    • 0037169071 scopus 로고    scopus 로고
    • Activation of orphan receptors by the hormone relaxin
    • Hsu S.Y., Nakabayashi K., Nishi S., et al. Activation of orphan receptors by the hormone relaxin. Science 2002, 295:671-674.
    • (2002) Science , vol.295 , pp. 671-674
    • Hsu, S.Y.1    Nakabayashi, K.2    Nishi, S.3
  • 60
    • 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., et al. 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
  • 61
    • 0029785186 scopus 로고    scopus 로고
    • Engineering human glycoprotein hormone superactive analogues
    • Szkudlinski M.W., Teh N.G., Grossmann M., et al. Engineering human glycoprotein hormone superactive analogues. Nat Biotechnol 1996, 14:1257-1263.
    • (1996) Nat Biotechnol , vol.14 , pp. 1257-1263
    • Szkudlinski, M.W.1    Teh, N.G.2    Grossmann, M.3
  • 62
    • 0030592256 scopus 로고    scopus 로고
    • Effect of modification of all loop regions in the alpha- and beta-subunits of human choriogonadotropin on its signal transduction activity
    • Shao K., Purohit S., Bahl O.P. Effect of modification of all loop regions in the alpha- and beta-subunits of human choriogonadotropin on its signal transduction activity. Mol Cell Endocrinol 1996, 122:173-182.
    • (1996) Mol Cell Endocrinol , vol.122 , pp. 173-182
    • Shao, K.1    Purohit, S.2    Bahl, O.P.3
  • 63
    • 0024340857 scopus 로고
    • Role of carbohydrates in glycoprotein hormone signal transduction
    • Sairam M.R. Role of carbohydrates in glycoprotein hormone signal transduction. FASEB J 1989, 3:1915-1926.
    • (1989) FASEB J , vol.3 , pp. 1915-1926
    • Sairam, M.R.1
  • 64
    • 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
  • 65
    • 0028890259 scopus 로고
    • Glycoprotein hormones: glycobiology of gonadotropins, thyrotropin and free alpha-subunit
    • Thotakura N.R., Blithe D.L. Glycoprotein hormones: glycobiology of gonadotropins, thyrotropin and free alpha-subunit. Glycobiology 1995, 5:3-10.
    • (1995) Glycobiology , vol.5 , pp. 3-10
    • Thotakura, N.R.1    Blithe, D.L.2
  • 66
    • 0026867982 scopus 로고
    • Identification of a subunit contact site of the alpha-subunit of follitropin
    • Krystek S.R., Dias J.A., Andersen T.T. Identification of a subunit contact site of the alpha-subunit of follitropin. Pept Res 1992, 5:165-168.
    • (1992) Pept Res , vol.5 , pp. 165-168
    • Krystek, S.R.1    Dias, J.A.2    Andersen, T.T.3
  • 67
    • 0027370711 scopus 로고
    • Site-directed alanine mutagenesis of Phe(33), Arg(35), and Arg(42)-Ser(43)-Lys(44) in the human gonadotropin alpha-subunit
    • Liu C., Roth K.E., Shepard B.A.L., et al. Site-directed alanine mutagenesis of Phe(33), Arg(35), and Arg(42)-Ser(43)-Lys(44) in the human gonadotropin alpha-subunit. J Biol Chem 1993, 268:21613-21617.
    • (1993) J Biol Chem , vol.268 , pp. 21613-21617
    • Liu, C.1    Roth, K.E.2    Shepard, B.A.L.3
  • 68
    • 0028218007 scopus 로고
    • A region in the human glycoprotein hormone alpha-subunit important in holoprotein formation and receptor-binding
    • Xia H.Y., Chen F., Puett D. A region in the human glycoprotein hormone alpha-subunit important in holoprotein formation and receptor-binding. Endocrinology 1994, 134:1768-1770.
    • (1994) Endocrinology , vol.134 , pp. 1768-1770
    • Xia, H.Y.1    Chen, F.2    Puett, D.3
  • 69
    • 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
  • 70
    • 0027493757 scopus 로고
    • COOH-terminal amino-acids of the alpha-subunit play common and different roles in human choriogonadotropin and follitropin
    • Yoo J.K., Zeng H.W., Ji I.H., et al. 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.K.1    Zeng, H.W.2    Ji, I.H.3
  • 71
    • 0025020754 scopus 로고
    • The biological role of the carboxyl-terminal extension of human chorionic-gonadotropin beta-subunit
    • Matzuk M.M., Hsueh A.J.W., Lapolt P., et al. The biological role of the carboxyl-terminal extension of human chorionic-gonadotropin beta-subunit. Endocrinology 1990, 126:376-383.
    • (1990) Endocrinology , vol.126 , pp. 376-383
    • Matzuk, M.M.1    Hsueh, A.J.W.2    Lapolt, P.3
  • 72
    • 0025993392 scopus 로고
    • Role of the invariant aspartic acid-99 of human choriogonadotropin-beta in receptor-binding and biological activity
    • Chen F., Wang Y., Puett D. Role of the invariant aspartic acid-99 of human choriogonadotropin-beta in receptor-binding and biological activity. J Biol Chem 1991, 266:19357-19361.
    • (1991) J Biol Chem , vol.266 , pp. 19357-19361
    • Chen, F.1    Wang, Y.2    Puett, D.3
  • 73
    • 0027441915 scopus 로고
    • A receptor-binding site identified in the region 81-95 of the beta-subunit of human luteinizing-hormone (LH) and chorionic-gonadotropin (HCG)
    • Morbeck D.E., Roche P.C., Keutmann H.T., et al. A receptor-binding site identified in the region 81-95 of the beta-subunit of human luteinizing-hormone (LH) and chorionic-gonadotropin (HCG). Mol Cell Endocrinol 1993, 97:173-181.
    • (1993) Mol Cell Endocrinol , vol.97 , pp. 173-181
    • Morbeck, D.E.1    Roche, P.C.2    Keutmann, H.T.3
  • 74
    • 0027316042 scopus 로고
    • The flanking amino-acids of the human follitropin beta-subunit 33-53 region are involved in assembly of the follitropin heterodimer
    • Roth K.E., Liu C., Shepard B.A., et al. The flanking amino-acids of the human follitropin beta-subunit 33-53 region are involved in assembly of the follitropin heterodimer. Endocrinology 1993, 132:2571-2577.
    • (1993) Endocrinology , vol.132 , pp. 2571-2577
    • Roth, K.E.1    Liu, C.2    Shepard, B.A.3
  • 75
    • 0027193414 scopus 로고
    • Amino carboxyl-terminal deletion mutants of human choriogonadotropin-beta
    • Huang J.N., Chen F., Puett D. Amino carboxyl-terminal deletion mutants of human choriogonadotropin-beta. J Biol Chem 1993, 268:9311-9315.
    • (1993) J Biol Chem , vol.268 , pp. 9311-9315
    • Huang, J.N.1    Chen, F.2    Puett, D.3
  • 76
    • 0028149524 scopus 로고
    • On the role of the invariant glutamine at position-54 in the human choriogonadotropin beta-subunit
    • Huang J.N., Puett D. On the role of the invariant glutamine at position-54 in the human choriogonadotropin beta-subunit. Mol Cell Biochem 1994, 136:183-186.
    • (1994) Mol Cell Biochem , vol.136 , pp. 183-186
    • Huang, J.N.1    Puett, D.2
  • 77
    • 0027479558 scopus 로고
    • Replacement of the invariant tyrosine in the cagy region of the human chorionic-gonadotropin beta subunit
    • Xia H.Y., Fernandez L.M., Puett D. Replacement of the invariant tyrosine in the cagy region of the human chorionic-gonadotropin beta subunit. Mol Cell Endocrinol 1993, 92:R1-R5.
    • (1993) Mol Cell Endocrinol , vol.92
    • Xia, H.Y.1    Fernandez, L.M.2    Puett, D.3
  • 78
    • 0028361815 scopus 로고
    • Identification of conserved amino-acid-residues in the beta-subunit of human choriogonadotropin important in holoprotein formation
    • Xia H.Y., Puett D. Identification of conserved amino-acid-residues in the beta-subunit of human choriogonadotropin important in holoprotein formation. J Biol Chem 1994, 269:17944-17953.
    • (1994) J Biol Chem , vol.269 , pp. 17944-17953
    • Xia, H.Y.1    Puett, D.2
  • 79
    • 0030898767 scopus 로고    scopus 로고
    • A functional determinant in human luteinizing hormone and chorionic gonadotropin: differential effect of mutations about beta-gln-s4
    • Hu S.B., Johnson L., Roche P.C., et al. A functional determinant in human luteinizing hormone and chorionic gonadotropin: differential effect of mutations about beta-gln-s4. Endocrinology 1997, 138:1627-1633.
    • (1997) Endocrinology , vol.138 , pp. 1627-1633
    • Hu, S.B.1    Johnson, L.2    Roche, P.C.3
  • 80
    • 34547118332 scopus 로고    scopus 로고
    • Translational fusion of two beta-subunits of human chorionic gonadotropin results in production of a novel antagonist of the hormone
    • Roy S., Setlur S., Gadkari R.A., et al. Translational fusion of two beta-subunits of human chorionic gonadotropin results in production of a novel antagonist of the hormone. Endocrinology 2007, 148:3977-3986.
    • (2007) Endocrinology , vol.148 , pp. 3977-3986
    • Roy, S.1    Setlur, S.2    Gadkari, R.A.3
  • 81
    • 0024438106 scopus 로고
    • Site-directed mutagenesis of the human chorionic-gonadotropin beta-subunit: bioactivity of a heterologous hormone, bovine alpha-human des-(122-145)-beta
    • Eldeiry S., Kaetzel D., Kennedy G., et al. Site-directed mutagenesis of the human chorionic-gonadotropin beta-subunit: bioactivity of a heterologous hormone, bovine alpha-human des-(122-145)-beta. Mol Endocrinol 1989, 3:1523-1528.
    • (1989) Mol Endocrinol , vol.3 , pp. 1523-1528
    • Eldeiry, S.1    Kaetzel, D.2    Kennedy, G.3
  • 82
    • 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., et al. 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
  • 83
    • 0026081701 scopus 로고
    • Conversion of human choriogonadotropin into a follitropin by protein engineering
    • Campbell R.K., Deanemig D.M., Moyle W.R. Conversion of human choriogonadotropin into a follitropin by protein engineering. Proc Natl Acad Sci U S A 1991, 88:760-764.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 760-764
    • Campbell, R.K.1    Deanemig, D.M.2    Moyle, W.R.3
  • 84
    • 0031003340 scopus 로고    scopus 로고
    • Chimeric proteins can exceed the sum of their parts: implications for evolution and protein design
    • Campbell R.K., Bergert E.R., Wang Y.H., et al. Chimeric proteins can exceed the sum of their parts: implications for evolution and protein design. Nat Biotechnol 1997, 15:439-443.
    • (1997) Nat Biotechnol , vol.15 , pp. 439-443
    • Campbell, R.K.1    Bergert, E.R.2    Wang, Y.H.3
  • 85
    • 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.Q., Liu X.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.Q.2    Liu, X.X.3
  • 86
    • 0028983425 scopus 로고
    • The lutropin beta-subunit n-terminus facilitates subunit combination by offsetting the inhibitory effects of residues needed for LH activity
    • Slaughter S., Wang Y.H., Myers R.V., et al. The lutropin beta-subunit n-terminus facilitates subunit combination by offsetting the inhibitory effects of residues needed for LH activity. Mol Cell Endocrinol 1995, 112:21-25.
    • (1995) Mol Cell Endocrinol , vol.112 , pp. 21-25
    • Slaughter, S.1    Wang, Y.H.2    Myers, R.V.3
  • 87
    • 0030606149 scopus 로고    scopus 로고
    • HCG beta residues 94-96 alter LH activity without appearing to make key receptor contacts
    • Han Y., Bernard M.P., Moyle W.R. hCG beta residues 94-96 alter LH activity without appearing to make key receptor contacts. Mol Cell Endocrinol 1996, 124:151-161.
    • (1996) Mol Cell Endocrinol , vol.124 , pp. 151-161
    • Han, Y.1    Bernard, M.P.2    Moyle, W.R.3
  • 88
    • 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., et al. 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
  • 89
    • 0031032647 scopus 로고    scopus 로고
    • Influence of subunit interactions on lutropin specificity: implications for studies of glycoprotein hormone function
    • Cosowsky L., Lin W., Han Y., et al. Influence of subunit interactions on lutropin specificity: implications for studies of glycoprotein hormone function. J Biol Chem 1997, 272:3309-3314.
    • (1997) J Biol Chem , vol.272 , pp. 3309-3314
    • Cosowsky, L.1    Lin, W.2    Han, Y.3
  • 90
    • 0034704346 scopus 로고    scopus 로고
    • Bifunctional hCG analogs adopt different conformations in LH and FSH receptor complexes
    • Wang Y.H., Bernard M.P., Moyle W.R. Bifunctional hCG analogs adopt different conformations in LH and FSH receptor complexes. Mol Cell Endocrinol 2000, 170:67-77.
    • (2000) Mol Cell Endocrinol , vol.170 , pp. 67-77
    • Wang, Y.H.1    Bernard, M.P.2    Moyle, W.R.3
  • 91
    • 0028882196 scopus 로고
    • Functional expression of yoked human chorionic-gonadotropin in baculovirus-infected insect cells
    • Narayan P., Wu C.B., Puett D. Functional expression of yoked human chorionic-gonadotropin in baculovirus-infected insect cells. Mol Endocrinol 1995, 9:1720-1726.
    • (1995) Mol Endocrinol , vol.9 , pp. 1720-1726
    • Narayan, P.1    Wu, C.B.2    Puett, D.3
  • 92
    • 0028948846 scopus 로고
    • Biosynthesis of a biologically-active single peptide-chain containing the human common alpha-subunits and chorionic-gonadotropin beta-subunits in tandem
    • Sugahara T., Pixley M.R., Minami S., et al. Biosynthesis of a biologically-active single peptide-chain containing the human common alpha-subunits and chorionic-gonadotropin beta-subunits in tandem. Proc Natl Acad Sci U S A 1995, 92:2041-2045.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 2041-2045
    • Sugahara, T.1    Pixley, M.R.2    Minami, S.3
  • 93
    • 0030596069 scopus 로고    scopus 로고
    • Expression of biologically active fusion genes encoding the common alpha subunit and either the CG beta or FSH beta subunits: role of a linker sequence
    • Sugahara T., Grootenhuis P.D.J., Sato A., et al. Expression of biologically active fusion genes encoding the common alpha subunit and either the CG beta or FSH beta subunits: role of a linker sequence. Mol Cell Endocrinol 1996, 125:71-77.
    • (1996) Mol Cell Endocrinol , vol.125 , pp. 71-77
    • Sugahara, T.1    Grootenhuis, P.D.J.2    Sato, A.3
  • 94
    • 0030816072 scopus 로고    scopus 로고
    • Design of stable biologically active recombinant lutropin analogs
    • Garcia Campayo V., Sato A., Hirsch B., et al. Design of stable biologically active recombinant lutropin analogs. Nat Biotechnol 1997, 15:663-667.
    • (1997) Nat Biotechnol , vol.15 , pp. 663-667
    • Garcia Campayo, V.1    Sato, A.2    Hirsch, B.3
  • 95
    • 0030920571 scopus 로고    scopus 로고
    • Evaluation of subunit truncation and the nature of the spacer for single chain human gonadotropins
    • Heikoop J.C., van Beuningen de Vaan M., van den Boogaart P., et al. Evaluation of subunit truncation and the nature of the spacer for single chain human gonadotropins. Eur J Biochem 1997, 245:656-662.
    • (1997) Eur J Biochem , vol.245 , pp. 656-662
    • Heikoop, J.C.1    Van Beuningen De Vaan, M.2    van den Boogaart, P.3
  • 96
    • 0030873203 scopus 로고    scopus 로고
    • Structure-based design and protein engineering of intersubunit disulfide bonds in gonadotropins
    • Heikoop J.C., van den Boogaart P., Mulders J.W.M., et al. Structure-based design and protein engineering of intersubunit disulfide bonds in gonadotropins. Nat Biotechnol 1997, 15:658-662.
    • (1997) Nat Biotechnol , vol.15 , pp. 658-662
    • Heikoop, J.C.1    Van Den Boogaart, P.2    Mulders, J.W.M.3
  • 98
    • 84884104877 scopus 로고    scopus 로고
    • The orientation of the gonadotropin alpha and beta domains in a single chain affects the heterodimeric interaction of the subunits
    • 274-274
    • Ben-Menahem D., Jablonka-Shariff A., Hyde R., et al. The orientation of the gonadotropin alpha and beta domains in a single chain affects the heterodimeric interaction of the subunits. Biol Reprod 1999, 60. 274-274.
    • (1999) Biol Reprod , vol.60
    • Ben-Menahem, D.1    Jablonka-Shariff, A.2    Hyde, R.3
  • 99
    • 0035839426 scopus 로고    scopus 로고
    • The position of the alpha and beta subunits in a single chain variant of human chorionic gonadotropin affects the heterodimeric interaction of the subunits and receptor-binding epitopes
    • Ben-Menahem D., Jablonka-Shariff A., Hyde R.K., et al. The position of the alpha and beta subunits in a single chain variant of human chorionic gonadotropin affects the heterodimeric interaction of the subunits and receptor-binding epitopes. J Biol Chem 2001, 276:29871-29879.
    • (2001) J Biol Chem , vol.276 , pp. 29871-29879
    • Ben-Menahem, D.1    Jablonka-Shariff, A.2    Hyde, R.K.3
  • 100
    • 85047681976 scopus 로고    scopus 로고
    • A biologically active single chain human chorionic gonadotropin analog with altered receptor binding properties
    • Narayan P., Gray J., Puett D. A biologically active single chain human chorionic gonadotropin analog with altered receptor binding properties. Endocrinology 2000, 141:67-71.
    • (2000) Endocrinology , vol.141 , pp. 67-71
    • Narayan, P.1    Gray, J.2    Puett, D.3
  • 101
    • 0034427047 scopus 로고    scopus 로고
    • Genetic engineering of single-chain gonadotropins and hormone-receptor fusion proteins
    • Narayan P., Wu C.B., Puett D. Genetic engineering of single-chain gonadotropins and hormone-receptor fusion proteins. Methods 2000, 21:59-66.
    • (2000) Methods , vol.21 , pp. 59-66
    • Narayan, P.1    Wu, C.B.2    Puett, D.3
  • 102
    • 0034078160 scopus 로고    scopus 로고
    • Biological activity of single chain chorionic gonadotropin, hCG alpha beta, is decreased upon deletion of five carboxyl terminal amino acids of the alpha subunit without affecting its receptor binding
    • Sen Gupta C., Dighe R.R. Biological activity of single chain chorionic gonadotropin, hCG alpha beta, is decreased upon deletion of five carboxyl terminal amino acids of the alpha subunit without affecting its receptor binding. J Mol Endocrinol 2000, 24:157-164.
    • (2000) J Mol Endocrinol , vol.24 , pp. 157-164
    • Sen Gupta, C.1    Dighe, R.R.2
  • 103
    • 0033782752 scopus 로고    scopus 로고
    • Expression of an in vitro biologically active equine LH/CG without c-terminal peptide (CTP) and/or beta 26-110 disulphide bridge
    • Galet C., Chopineau M., Martinat N., et al. Expression of an in vitro biologically active equine LH/CG without c-terminal peptide (CTP) and/or beta 26-110 disulphide bridge. J Endocrinol 2000, 167:117-124.
    • (2000) J Endocrinol , vol.167 , pp. 117-124
    • Galet, C.1    Chopineau, M.2    Martinat, N.3
  • 104
    • 0037634482 scopus 로고    scopus 로고
    • Structural analysis of yoked chorionic gonadotropin-luteinizing hormone receptor ectodomain complexes by circular dichroic spectroscopy
    • Fralish G.B., Dattilo B., Puett D. Structural analysis of yoked chorionic gonadotropin-luteinizing hormone receptor ectodomain complexes by circular dichroic spectroscopy. Mol Endocrinol 2003, 17:1192-1202.
    • (2003) Mol Endocrinol , vol.17 , pp. 1192-1202
    • Fralish, G.B.1    Dattilo, B.2    Puett, D.3
  • 105
    • 0037384140 scopus 로고    scopus 로고
    • Consequences of single-chain translation on the structures of two chorionic gonadotropin yoked analogs in alpha-beta and beta-alpha configurations
    • Fralish G.B., Narayan P., Puett D. Consequences of single-chain translation on the structures of two chorionic gonadotropin yoked analogs in alpha-beta and beta-alpha configurations. Mol Endocrinol 2003, 17:757-767.
    • (2003) Mol Endocrinol , vol.17 , pp. 757-767
    • Fralish, G.B.1    Narayan, P.2    Puett, D.3
  • 106
    • 33845597768 scopus 로고    scopus 로고
    • Single chain human chorionic gonadotropin, hCG alpha beta: effects of mutations in the alpha subunit on structure and bioactivity
    • Setlur S.R., Dighe R.R. Single chain human chorionic gonadotropin, hCG alpha beta: effects of mutations in the alpha subunit on structure and bioactivity. Glycoconj J 2007, 24:97-106.
    • (2007) Glycoconj J , vol.24 , pp. 97-106
    • Setlur, S.R.1    Dighe, R.R.2
  • 107
    • 0030959878 scopus 로고    scopus 로고
    • The biologic action of single-chain choriogonadotropin is not dependent on the individual disulfide bonds of the beta subunit
    • Ben Menahem D., Kudo M., Pixley M.B., et al. The biologic action of single-chain choriogonadotropin is not dependent on the individual disulfide bonds of the beta subunit. J Biol Chem 1997, 272:6827-6830.
    • (1997) J Biol Chem , vol.272 , pp. 6827-6830
    • Ben Menahem, D.1    Kudo, M.2    Pixley, M.B.3
  • 108
    • 0030739370 scopus 로고    scopus 로고
    • Cystine knot of the gonadotropin alpha subunit is critical for intracellular behavior but not for in vitro biological activity
    • Sato A., Perlas E., Ben Menahem D., et al. Cystine knot of the gonadotropin alpha subunit is critical for intracellular behavior but not for in vitro biological activity. J Biol Chem 1997, 272:18098-18103.
    • (1997) J Biol Chem , vol.272 , pp. 18098-18103
    • Sato, A.1    Perlas, E.2    Ben Menahem, D.3
  • 109
    • 33744472176 scopus 로고    scopus 로고
    • Single-chain, triple-domain gonadotropin analogs with disulfide bond mutations in the alpha-subunit elicit dual follitropin and lutropin activities in vivo
    • Jablonka-Shariff A., Kumar T.R., Eklund J., et al. Single-chain, triple-domain gonadotropin analogs with disulfide bond mutations in the alpha-subunit elicit dual follitropin and lutropin activities in vivo. Mol Endocrinol 2006, 20:1437-1446.
    • (2006) Mol Endocrinol , vol.20 , pp. 1437-1446
    • Jablonka-Shariff, A.1    Kumar, T.R.2    Eklund, J.3
  • 110
    • 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., et al. 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
  • 111
    • 0034990963 scopus 로고    scopus 로고
    • Partial restoration of lutropin activity by an intersubunit disulfide bond: implications for structure/function studies
    • Einstein M., Lin W., Macdonald G.J., et al. Partial restoration of lutropin activity by an intersubunit disulfide bond: implications for structure/function studies. Exp Biol Med 2001, 226:581-590.
    • (2001) Exp Biol Med , vol.226 , pp. 581-590
    • Einstein, M.1    Lin, W.2    Macdonald, G.J.3
  • 112
    • 17644401739 scopus 로고    scopus 로고
    • Crosslinked bifunctional gonadotropin analogs with reduced efficacy
    • Bernard M.P., Lin W., Myers R., et al. Crosslinked bifunctional gonadotropin analogs with reduced efficacy. Mol Cell Endocrinol 2005, 233:25-31.
    • (2005) Mol Cell Endocrinol , vol.233 , pp. 25-31
    • Bernard, M.P.1    Lin, W.2    Myers, R.3
  • 113
    • 0033304953 scopus 로고    scopus 로고
    • Genetic fusion of an alpha-subunit gene to the follicle-stimulating hormone and chorionic gonadotropin-beta subunit genes: production of a bifunctional protein
    • Kanda M., Jablonka-Shariff A., Sato A., et al. Genetic fusion of an alpha-subunit gene to the follicle-stimulating hormone and chorionic gonadotropin-beta subunit genes: production of a bifunctional protein. Mol Endocrinol 1999, 13:1873-1881.
    • (1999) Mol Endocrinol , vol.13 , pp. 1873-1881
    • Kanda, M.1    Jablonka-Shariff, A.2    Sato, A.3
  • 114
    • 0035210681 scopus 로고    scopus 로고
    • Independent activities of FSH and LH structurally confined in a single polypeptide: selective modification of the relative potencies of the hormones
    • Garcia-Campayo V., Boime I. Independent activities of FSH and LH structurally confined in a single polypeptide: selective modification of the relative potencies of the hormones. Endocrinology 2001, 142:5203-5211.
    • (2001) Endocrinology , vol.142 , pp. 5203-5211
    • Garcia-Campayo, V.1    Boime, I.2
  • 115
    • 84884021733 scopus 로고    scopus 로고
    • Construction and expression of an ovine single chain triple-domain chimeric gonadotropin: tandem linkage of the genes encoding the alpha- and FSH beta and LH beta subunits
    • Jablonka-Shariff A., Comstock A., Colgin M., et al. Construction and expression of an ovine single chain triple-domain chimeric gonadotropin: tandem linkage of the genes encoding the alpha- and FSH beta and LH beta subunits. Biol Reprod 2007, 131-132.
    • (2007) Biol Reprod , pp. 131-132
    • Jablonka-Shariff, A.1    Comstock, A.2    Colgin, M.3
  • 116
    • 7244250222 scopus 로고    scopus 로고
    • A single-chain bifunctional gonadotropin analog is secreted from Chinese hamster ovary cells as two distinct bioactive species
    • Garcia-Campayo V., Jablonka-Shariff A., Boime I. A single-chain bifunctional gonadotropin analog is secreted from Chinese hamster ovary cells as two distinct bioactive species. J Biol Chem 2004, 279:44286-44293.
    • (2004) J Biol Chem , vol.279 , pp. 44286-44293
    • Garcia-Campayo, V.1    Jablonka-Shariff, A.2    Boime, I.3
  • 117
    • 0036773467 scopus 로고    scopus 로고
    • Thyrotropin, follitropin, and chorionic gonadotropin expressed as a single multifunctional unit reveal remarkable permissiveness in receptor-ligand interactions
    • Garcia-Campayo V., Kumar T.R., Boime I. Thyrotropin, follitropin, and chorionic gonadotropin expressed as a single multifunctional unit reveal remarkable permissiveness in receptor-ligand interactions. Endocrinology 2002, 143:3773-3778.
    • (2002) Endocrinology , vol.143 , pp. 3773-3778
    • Garcia-Campayo, V.1    Kumar, T.R.2    Boime, I.3
  • 118
    • 12344278940 scopus 로고    scopus 로고
    • A single-chain tetradomain glycoprotein hormone analog elicits multiple hormone activities in vivo
    • Garcia-Campayo V., Boime I., Ma X.P., et al. A single-chain tetradomain glycoprotein hormone analog elicits multiple hormone activities in vivo. Biol Reprod 2005, 72:301-308.
    • (2005) Biol Reprod , vol.72 , pp. 301-308
    • Garcia-Campayo, V.1    Boime, I.2    Ma, X.P.3
  • 119
    • 0029856730 scopus 로고    scopus 로고
    • Protein engineering of a novel constitutively active hormone-receptor complex
    • Wu C.B., Narayan P., Puett D. Protein engineering of a novel constitutively active hormone-receptor complex. J Biol Chem 1996, 271:31638-31642.
    • (1996) J Biol Chem , vol.271 , pp. 31638-31642
    • Wu, C.B.1    Narayan, P.2    Puett, D.3
  • 120
    • 0031864755 scopus 로고    scopus 로고
    • The tie that binds: design of biologically active single-chain human chorionic gonadotropins and a gonadotropin-receptor complex using protein engineering
    • Puett D., Wu C.B., Narayan P. The tie that binds: design of biologically active single-chain human chorionic gonadotropins and a gonadotropin-receptor complex using protein engineering. Biol Reprod 1998, 58:1337-1342.
    • (1998) Biol Reprod , vol.58 , pp. 1337-1342
    • Puett, D.1    Wu, C.B.2    Narayan, P.3
  • 121
    • 17844374094 scopus 로고    scopus 로고
    • Gonadal defects and hormonal alterations in transgenic mice expressing a single chain human chorionic gonadotropin-lutropin receptor complex
    • Meehan T.P., Harmon B.G., Overcast M.E., et al. Gonadal defects and hormonal alterations in transgenic mice expressing a single chain human chorionic gonadotropin-lutropin receptor complex. J Mol Endocrinol 2005, 34:489-503.
    • (2005) J Mol Endocrinol , vol.34 , pp. 489-503
    • Meehan, T.P.1    Harmon, B.G.2    Overcast, M.E.3
  • 122
    • 0036913852 scopus 로고    scopus 로고
    • Yoked complexes of human choriogonadotropin and the lutropin receptor: evidence that monomeric individual subunits are inactive
    • Narayan P., Gray J., Puett D. Yoked complexes of human choriogonadotropin and the lutropin receptor: evidence that monomeric individual subunits are inactive. Mol Endocrinol 2002, 16:2733-2745.
    • (2002) Mol Endocrinol , vol.16 , pp. 2733-2745
    • Narayan, P.1    Gray, J.2    Puett, D.3
  • 123
    • 0020473793 scopus 로고
    • Human chorionic-gonadotropin beta-subunit is encoded by at least eight genes arranged in tandem and inverted pairs
    • Boorstein W.R., Vamvakopoulos N.C., Fiddes J.C. Human chorionic-gonadotropin beta-subunit is encoded by at least eight genes arranged in tandem and inverted pairs. Nature 1982, 300:419-422.
    • (1982) Nature , vol.300 , pp. 419-422
    • Boorstein, W.R.1    Vamvakopoulos, N.C.2    Fiddes, J.C.3
  • 124
  • 125
    • 0031889436 scopus 로고    scopus 로고
    • A comprehensive evolutionary analysis based on nucleotide and amino acid sequences of the alpha- and beta-subunitsof glycoprotein hormone gene family
    • Li M.D., Ford J.J. A comprehensive evolutionary analysis based on nucleotide and amino acid sequences of the alpha- and beta-subunitsof glycoprotein hormone gene family. J Endocrinol 1998, 156:529-542.
    • (1998) J Endocrinol , vol.156 , pp. 529-542
    • Li, M.D.1    Ford, J.J.2
  • 126
    • 0020888557 scopus 로고
    • The human genome contains 7 genes for the beta-subunit of chorionic-gonadotropin but only one gene for the beta-subunit of luteinizing-hormone
    • Talmadge K., Boorstein W.R., Fiddes J.C. The human genome contains 7 genes for the beta-subunit of chorionic-gonadotropin but only one gene for the beta-subunit of luteinizing-hormone. DNA Cell Biol 1983, 2:281-289.
    • (1983) DNA Cell Biol , vol.2 , pp. 281-289
    • Talmadge, K.1    Boorstein, W.R.2    Fiddes, J.C.3
  • 127
    • 0021771522 scopus 로고
    • Only 3 of the 7 human chorionic-gonadotropin beta-subunit genes can be expressed in the placenta
    • Talmadge K., Boorstein W.R., Vamvakopoulos N.C., et al. Only 3 of the 7 human chorionic-gonadotropin beta-subunit genes can be expressed in the placenta. Nucleic Acids Res 1984, 12:8415-8436.
    • (1984) Nucleic Acids Res , vol.12 , pp. 8415-8436
    • Talmadge, K.1    Boorstein, W.R.2    Vamvakopoulos, N.C.3
  • 128
    • 28544442017 scopus 로고    scopus 로고
    • Expression of beta-subunit of HCG genes during normal and failed pregnancy
    • Rull K., Laan M. Expression of beta-subunit of HCG genes during normal and failed pregnancy. Hum Reprod 2005, 20:3360-3368.
    • (2005) Hum Reprod , vol.20 , pp. 3360-3368
    • Rull, K.1    Laan, M.2
  • 129
    • 27544480956 scopus 로고    scopus 로고
    • Segmental duplications and gene conversion: human luteinizing hormone/chorionic gonadotropin beta gene cluster
    • Hallast P., Nagirnaja L., Margus T., et al. Segmental duplications and gene conversion: human luteinizing hormone/chorionic gonadotropin beta gene cluster. Genome Res 2005, 15:1535-1546.
    • (2005) Genome Res , vol.15 , pp. 1535-1546
    • Hallast, P.1    Nagirnaja, L.2    Margus, T.3
  • 130
    • 33751232342 scopus 로고    scopus 로고
    • The evolution and genomic landscape of CGB1 and CGB2 genes
    • Hallast P., Rull K., Laan M. The evolution and genomic landscape of CGB1 and CGB2 genes. Mol Cell Endocrinol 2007, 260:2-11.
    • (2007) Mol Cell Endocrinol , vol.260 , pp. 2-11
    • Hallast, P.1    Rull, K.2    Laan, M.3
  • 131
    • 0026687324 scopus 로고
    • Identification of the transcriptionally active genes of the chorionic gonadotropin-beta gene-cluster invivo
    • Bo M., Boime I. Identification of the transcriptionally active genes of the chorionic gonadotropin-beta gene-cluster invivo. J Biol Chem 1992, 267:3179-3184.
    • (1992) J Biol Chem , vol.267 , pp. 3179-3184
    • Bo, M.1    Boime, I.2
  • 132
    • 0030670914 scopus 로고    scopus 로고
    • Human chorionic gonadotropin-beta gene expression in first trimester placenta
    • Miller Lindholm A.K., LaBenz C.J., Ramey J., et al. Human chorionic gonadotropin-beta gene expression in first trimester placenta. Endocrinology 1997, 138:5459-5465.
    • (1997) Endocrinology , vol.138 , pp. 5459-5465
    • Miller Lindholm, A.K.1    LaBenz, C.J.2    Ramey, J.3
  • 133
    • 0023446832 scopus 로고
    • Tissue-specific enhancer of the human glycoprotein hormone alpha-subunit gene: dependence on cyclic amp-inducible elements
    • Delegeane A.M., Ferland L.H., Mellon P.L. Tissue-specific enhancer of the human glycoprotein hormone alpha-subunit gene: dependence on cyclic amp-inducible elements. Mol Cell Biol 1987, 7:3994-4002.
    • (1987) Mol Cell Biol , vol.7 , pp. 3994-4002
    • Delegeane, A.M.1    Ferland, L.H.2    Mellon, P.L.3
  • 134
    • 84884105051 scopus 로고
    • Cyclic-amp effects on chorionic-gonadotropin alpha-subunit and beta-subunit gene-transcription and messenger-RNA stability
    • A359-A359
    • Jameson J.L., Fuh V.L., Burrin J.M. Cyclic-amp effects on chorionic-gonadotropin alpha-subunit and beta-subunit gene-transcription and messenger-RNA stability. Clin Res 1989, 37. A359-A359.
    • (1989) Clin Res , vol.37
    • Jameson, J.L.1    Fuh, V.L.2    Burrin, J.M.3
  • 135
    • 0026752378 scopus 로고
    • Analysis of DNA-sequences required for pituitary-specific expression of the glycoprotein hormone alpha-subunit gene
    • Schoderbek W.E., Kim K.E., Ridgway E.C., et al. Analysis of DNA-sequences required for pituitary-specific expression of the glycoprotein hormone alpha-subunit gene. Mol Endocrinol 1992, 6:893-903.
    • (1992) Mol Endocrinol , vol.6 , pp. 893-903
    • Schoderbek, W.E.1    Kim, K.E.2    Ridgway, E.C.3
  • 136
    • 0027467420 scopus 로고
    • 2 different DNA elements mediate gonadotropin-releasing-hormone effects on expression of the glycoprotein hormone alpha-subunit gene
    • Schoderbek W.E., Roberson M.S., Maurer R.A. 2 different DNA elements mediate gonadotropin-releasing-hormone effects on expression of the glycoprotein hormone alpha-subunit gene. J Biol Chem 1993, 268:3903-3910.
    • (1993) J Biol Chem , vol.268 , pp. 3903-3910
    • Schoderbek, W.E.1    Roberson, M.S.2    Maurer, R.A.3
  • 137
    • 0028365295 scopus 로고
    • The orphan nuclear receptor, steroidogenic factor-I, regulates the glycoprotein hormone alpha-subunit gene in pituitary gonadotropes
    • Barnhart K.M., Mellon P.L. The orphan nuclear receptor, steroidogenic factor-I, regulates the glycoprotein hormone alpha-subunit gene in pituitary gonadotropes. Mol Endocrinol 1994, 8:878-885.
    • (1994) Mol Endocrinol , vol.8 , pp. 878-885
    • Barnhart, K.M.1    Mellon, P.L.2
  • 138
    • 0029717882 scopus 로고    scopus 로고
    • The gonadotropin genes: evolution of distinct mechanisms for hormonal control
    • Albanese C., Colin I.M., Crowley W.F., et al. The gonadotropin genes: evolution of distinct mechanisms for hormonal control. Recent Prog Horm Res 1996, 51:23-61.
    • (1996) Recent Prog Horm Res , vol.51 , pp. 23-61
    • Albanese, C.1    Colin, I.M.2    Crowley, W.F.3
  • 139
    • 0036721166 scopus 로고    scopus 로고
    • Regulation of human glycoprotein hormone alpha-subunit gene transcription in LβT2 gonadotropes by protein kinase c and extracellular signal-regulated kinase 1/2
    • Fowkes R.C., King P., Burrin J.M. Regulation of human glycoprotein hormone alpha-subunit gene transcription in LβT2 gonadotropes by protein kinase c and extracellular signal-regulated kinase 1/2. Biol Reprod 2002, 67:725-734.
    • (2002) Biol Reprod , vol.67 , pp. 725-734
    • Fowkes, R.C.1    King, P.2    Burrin, J.M.3
  • 140
    • 0242330293 scopus 로고    scopus 로고
    • Steroidogenic factor-1 and the gonadotrope-specific element enhance basal and pituitary adenylate cyclase-activating polypeptide-stimulated transcription of the human glycoprotein hormone alpha-subunit gene in gonadotropes
    • Fowkes R.C., Desclozeaux M., Patel M.V., et al. Steroidogenic factor-1 and the gonadotrope-specific element enhance basal and pituitary adenylate cyclase-activating polypeptide-stimulated transcription of the human glycoprotein hormone alpha-subunit gene in gonadotropes. Mol Endocrinol 2003, 17:2177-2188.
    • (2003) Mol Endocrinol , vol.17 , pp. 2177-2188
    • Fowkes, R.C.1    Desclozeaux, M.2    Patel, M.V.3
  • 142
    • 0028558673 scopus 로고
    • Multiple promoter elements in the human chorionic-gonadotropin beta-subunit genes distinguish their expression from the luteinizing-hormone beta-gene
    • Hollenberg A.N., Pestell R.G., Albanese C., et al. Multiple promoter elements in the human chorionic-gonadotropin beta-subunit genes distinguish their expression from the luteinizing-hormone beta-gene. Mol Cell Endocrinol 1994, 106:111-119.
    • (1994) Mol Cell Endocrinol , vol.106 , pp. 111-119
    • Hollenberg, A.N.1    Pestell, R.G.2    Albanese, C.3
  • 143
    • 12144287700 scopus 로고    scopus 로고
    • Transcriptional regulation of the human chorionic gonadotropin beta gene during villous trophoblast differentiation
    • Knofler M., Saleh L., Bauer S., et al. Transcriptional regulation of the human chorionic gonadotropin beta gene during villous trophoblast differentiation. Endocrinology 2004, 145:1685-1694.
    • (2004) Endocrinology , vol.145 , pp. 1685-1694
    • Knofler, M.1    Saleh, L.2    Bauer, S.3
  • 144
    • 0025361333 scopus 로고
    • Molecular-biology of the pituitary gonadotropins
    • Gharib S.D., Wierman M.E., Shupnik M.A., et al. Molecular-biology of the pituitary gonadotropins. Endocr Rev 1990, 11:177-199.
    • (1990) Endocr Rev , vol.11 , pp. 177-199
    • Gharib, S.D.1    Wierman, M.E.2    Shupnik, M.A.3
  • 145
    • 17144426646 scopus 로고    scopus 로고
    • X-chromosome as a marker for population history: linkage disequilibrium and haplotype study in Eurasian populations
    • Laan M., Wiebe V., Khusnutdinova E., et al. X-chromosome as a marker for population history: linkage disequilibrium and haplotype study in Eurasian populations. Eur J Hum Genet 2005, 13:452-462.
    • (2005) Eur J Hum Genet , vol.13 , pp. 452-462
    • Laan, M.1    Wiebe, V.2    Khusnutdinova, E.3
  • 146
    • 0029801625 scopus 로고    scopus 로고
    • Expression of the human chorionic gonadotropin-beta gene cluster in human pituitaries and alternate use of exon 1
    • Dirnhofer S., Hermann M., Hittmair A., et al. Expression of the human chorionic gonadotropin-beta gene cluster in human pituitaries and alternate use of exon 1. J Clin Endocrinol Metab 1996, 81:4212-4217.
    • (1996) J Clin Endocrinol Metab , vol.81 , pp. 4212-4217
    • Dirnhofer, S.1    Hermann, M.2    Hittmair, A.3
  • 147
    • 0028230138 scopus 로고
    • Eutopic production of human chorionic-gonadotropin-beta (hCG-beta) and luteinizing-hormone-beta (hLH-beta) in the human testis
    • Berger P., Kranewitter W., Madersbacher S., et al. Eutopic production of human chorionic-gonadotropin-beta (hCG-beta) and luteinizing-hormone-beta (hLH-beta) in the human testis. FEBS Lett 1994, 343:229-233.
    • (1994) FEBS Lett , vol.343 , pp. 229-233
    • Berger, P.1    Kranewitter, W.2    Madersbacher, S.3
  • 148
    • 0035838587 scopus 로고    scopus 로고
    • Analysis of the human CGB/LHB gene cluster in breast tumors by real-time quantitative RT-PCR assays
    • Giovangrandi Y., Parfait B., Asheuer M., et al. Analysis of the human CGB/LHB gene cluster in breast tumors by real-time quantitative RT-PCR assays. Cancer Lett 2001, 168:93-100.
    • (2001) Cancer Lett , vol.168 , pp. 93-100
    • Giovangrandi, Y.1    Parfait, B.2    Asheuer, M.3
  • 149
    • 0027969321 scopus 로고
    • Expression of the beta-subunit of chorionic-gonadotropin in transgenic mice
    • Strauss B.L., Pittman R., Pixley M.R., et al. Expression of the beta-subunit of chorionic-gonadotropin in transgenic mice. J Biol Chem 1994, 269:4968-4973.
    • (1994) J Biol Chem , vol.269 , pp. 4968-4973
    • Strauss, B.L.1    Pittman, R.2    Pixley, M.R.3
  • 150
    • 0022998351 scopus 로고
    • A single amino acid substitution in an ectopic alpha subunit of a human carcinoma choriogonadotropin
    • Nishimura R., Shin J., Ji I., et al. A single amino acid substitution in an ectopic alpha subunit of a human carcinoma choriogonadotropin. J Biol Chem 1986, 261:10475-10477.
    • (1986) J Biol Chem , vol.261 , pp. 10475-10477
    • Nishimura, R.1    Shin, J.2    Ji, I.3
  • 151
    • 0030596185 scopus 로고    scopus 로고
    • Inherited disorders of the gonadotropin hormones
    • Jameson J.L. Inherited disorders of the gonadotropin hormones. Mol Cell Endocrinol 1996, 125:143-149.
    • (1996) Mol Cell Endocrinol , vol.125 , pp. 143-149
    • Jameson, J.L.1
  • 152
    • 0036193520 scopus 로고    scopus 로고
    • Human gene mutations causing infertility
    • Layman L.C. Human gene mutations causing infertility. J Med Genet 2002, 39:153-161.
    • (2002) J Med Genet , vol.39 , pp. 153-161
    • Layman, L.C.1
  • 153
    • 0036345561 scopus 로고    scopus 로고
    • FSH beta gene mutations in a female with partial breast development and a male sibling with normal puberty and azoospermia
    • Layman L.C., Porto A.L.A., Xie J., et al. FSH beta gene mutations in a female with partial breast development and a male sibling with normal puberty and azoospermia. J Clin Endocrinol Metab 2002, 87:3702-3707.
    • (2002) J Clin Endocrinol Metab , vol.87 , pp. 3702-3707
    • Layman, L.C.1    Porto, A.L.A.2    Xie, J.3
  • 154
    • 0033602938 scopus 로고    scopus 로고
    • Mutations and polymorphisms in gonadotropin genes
    • Huhtaniemi I., Jiang M., Nilsson C., et al. Mutations and polymorphisms in gonadotropin genes. Mol Cell Endocrinol 1999, 151:89-94.
    • (1999) Mol Cell Endocrinol , vol.151 , pp. 89-94
    • Huhtaniemi, I.1    Jiang, M.2    Nilsson, C.3
  • 155
    • 24644461526 scopus 로고    scopus 로고
    • Mutations in human gonadotropin and gonadotropin-receptor genes
    • Huhtaniemi I.T., Themmen A.P.N. Mutations in human gonadotropin and gonadotropin-receptor genes. Endocrine 2005, 26:207-217.
    • (2005) Endocrine , vol.26 , pp. 207-217
    • Huhtaniemi, I.T.1    Themmen, A.P.N.2
  • 157
    • 24944501149 scopus 로고    scopus 로고
    • An update of the pathophysiology of human gonadotrophin subunit and receptor gene mutations and polymorphisms
    • Themmen A.P.N. An update of the pathophysiology of human gonadotrophin subunit and receptor gene mutations and polymorphisms. Reproduction 2005, 130:263-274.
    • (2005) Reproduction , vol.130 , pp. 263-274
    • Themmen, A.P.N.1
  • 158
    • 34447289150 scopus 로고    scopus 로고
    • The genetics of hypogonadotropic hypogonadism
    • Bhagavath B., Layman L.C. The genetics of hypogonadotropic hypogonadism. Semin Reprod Med 2007, 25:272-285.
    • (2007) Semin Reprod Med , vol.25 , pp. 272-285
    • Bhagavath, B.1    Layman, L.C.2
  • 159
    • 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., et al. 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
  • 160
    • 10344262033 scopus 로고    scopus 로고
    • Brief report: hypogonadism in a patient with a mutation in the luteinizing hormone beta-subunit gene
    • Valdes-Socin H., Salvi R., Daly A.F., et al. Brief report: hypogonadism in a patient with a mutation in the luteinizing hormone beta-subunit gene. N Engl J Med 2004, 351:2619-2625.
    • (2004) N Engl J Med , vol.351 , pp. 2619-2625
    • Valdes-Socin, H.1    Salvi, R.2    Daly, A.F.3
  • 161
    • 34548313698 scopus 로고    scopus 로고
    • Luteinizing hormone beta mutation and hypogonadism in men and women
    • Lofrano-Porto A., Barra G.B., Giacomini L.A., et al. Luteinizing hormone beta mutation and hypogonadism in men and women. N Engl J Med 2007, 357:897-904.
    • (2007) N Engl J Med , vol.357 , pp. 897-904
    • Lofrano-Porto, A.1    Barra, G.B.2    Giacomini, L.A.3
  • 162
    • 0027324274 scopus 로고
    • Primary amenorrhea and infertility due to a mutation in the beta-subunit of follicle-stimulating-hormone
    • Matthews C.H., Borgato S., Beckpeccoz P., et al. Primary amenorrhea and infertility due to a mutation in the beta-subunit of follicle-stimulating-hormone. Nat Genet 1993, 5:83-86.
    • (1993) Nat Genet , vol.5 , pp. 83-86
    • Matthews, C.H.1    Borgato, S.2    Beckpeccoz, P.3
  • 163
    • 0032508059 scopus 로고    scopus 로고
    • Male hypogonadism due to a mutation in the gene for the beta-subunit of follicle-stimulating hormone
    • Phillip M., Arbelle J.E., Segev Y., et al. Male hypogonadism due to a mutation in the gene for the beta-subunit of follicle-stimulating hormone. N Engl J Med 1998, 338:1729-1732.
    • (1998) N Engl J Med , vol.338 , pp. 1729-1732
    • Phillip, M.1    Arbelle, J.E.2    Segev, Y.3
  • 164
    • 0030744037 scopus 로고    scopus 로고
    • Delayed puberty and hypogonadism caused by mutations in the follicle-stimulating hormone beta-subunit gene
    • Layman L.C., Lee E.J., Peak D.B., et al. Delayed puberty and hypogonadism caused by mutations in the follicle-stimulating hormone beta-subunit gene. N Engl J Med 1997, 337:607-611.
    • (1997) N Engl J Med , vol.337 , pp. 607-611
    • Layman, L.C.1    Lee, E.J.2    Peak, D.B.3
  • 165
    • 0031712880 scopus 로고    scopus 로고
    • Follitropin (FSH) deficiency in an infertile male due to FSH beta gene mutation: a syndrome of normal puberty and virilization but underdeveloped testicles with azoospermia, low FSH but high lutropin and normal serum testosterone concentrations
    • Lindstedt G., Nystrom E., Matthews C., et al. Follitropin (FSH) deficiency in an infertile male due to FSH beta gene mutation: a syndrome of normal puberty and virilization but underdeveloped testicles with azoospermia, low FSH but high lutropin and normal serum testosterone concentrations. Clin Chem Lab Med 1998, 36:663-665.
    • (1998) Clin Chem Lab Med , vol.36 , pp. 663-665
    • Lindstedt, G.1    Nystrom, E.2    Matthews, C.3
  • 166
    • 0032892646 scopus 로고    scopus 로고
    • Carbohydrate-deficient glycoprotein syndromes: inborn errors of protein glycosylation
    • Keir G., Winchester B.G., Clayton P. Carbohydrate-deficient glycoprotein syndromes: inborn errors of protein glycosylation. Ann Clin Biochem 1999, 36:20-36.
    • (1999) Ann Clin Biochem , vol.36 , pp. 20-36
    • Keir, G.1    Winchester, B.G.2    Clayton, P.3
  • 167
    • 84995842414 scopus 로고
    • Identification of 2 point mutations in the gene coding luteinizing-hormone (LH) beta-subunit, associated with immunologically anomalous LH variants
    • Furui K., Suganuma N., Tsukahara S., et al. Identification of 2 point mutations in the gene coding luteinizing-hormone (LH) beta-subunit, associated with immunologically anomalous LH variants. J Clin Endocrinol Metab 1994, 78:107-113.
    • (1994) J Clin Endocrinol Metab , vol.78 , pp. 107-113
    • Furui, K.1    Suganuma, N.2    Tsukahara, S.3
  • 168
    • 0028919465 scopus 로고
    • Screening of the mutations in luteinizing-hormone beta-subunit in patients with menstrual disorders
    • Suganuma N., Furui K., Furuhashi M., et al. Screening of the mutations in luteinizing-hormone beta-subunit in patients with menstrual disorders. Fertil Steril 1995, 63:989-995.
    • (1995) Fertil Steril , vol.63 , pp. 989-995
    • Suganuma, N.1    Furui, K.2    Furuhashi, M.3
  • 169
    • 0029669973 scopus 로고    scopus 로고
    • Effects of the mutations (Trp(8)>Arg and Ile(15)>Thr) in human luteinizing hormone (LH) beta-subunit on LH bioactivity in vitro and in vivo
    • Suganuma N., Furui K., Kikkawa F., et al. Effects of the mutations (Trp(8)>Arg and Ile(15);Thr) in human luteinizing hormone (LH) beta-subunit on LH bioactivity in vitro and in vivo. Endocrinology 1996, 137:831-838.
    • (1996) Endocrinology , vol.137 , pp. 831-838
    • Suganuma, N.1    Furui, K.2    Kikkawa, F.3
  • 170
    • 0343742651 scopus 로고    scopus 로고
    • Worldwide frequency of a common genetic variant of luteinizing hormone: an international collaborative research
    • Nilsson C., Pettersson K., Millar R.P., et al. Worldwide frequency of a common genetic variant of luteinizing hormone: an international collaborative research. Fertil Steril 1997, 67:998-1004.
    • (1997) Fertil Steril , vol.67 , pp. 998-1004
    • Nilsson, C.1    Pettersson, K.2    Millar, R.P.3
  • 171
    • 0031751442 scopus 로고    scopus 로고
    • Determination of a common genetic variant of luteinizing hormone using DNA hybridization and immunoassays
    • Nilsson C., Jiang M., Pettersson K., et al. Determination of a common genetic variant of luteinizing hormone using DNA hybridization and immunoassays. Clin Endocrinol 1998, 49:369-376.
    • (1998) Clin Endocrinol , vol.49 , pp. 369-376
    • Nilsson, C.1    Jiang, M.2    Pettersson, K.3
  • 172
    • 0032883294 scopus 로고    scopus 로고
    • A common polymorphic allele of the human luteinizing hormone beta-subunit gene: additional mutations and differential function of the promoter sequence
    • Jiang M., Pakarainen P., Zhang F.P., et al. A common polymorphic allele of the human luteinizing hormone beta-subunit gene: additional mutations and differential function of the promoter sequence. Hum Mol Genet 1999, 8:2037-2046.
    • (1999) Hum Mol Genet , vol.8 , pp. 2037-2046
    • Jiang, M.1    Pakarainen, P.2    Zhang, F.P.3
  • 173
    • 0035936874 scopus 로고    scopus 로고
    • A common variant of luteinizing hormone: relation to normal and aberrant pituitary-gonadal function
    • Lamminen T., Huhtaniemi I. A common variant of luteinizing hormone: relation to normal and aberrant pituitary-gonadal function. Eur J Pharmacol 2001, 414:1-7.
    • (2001) Eur J Pharmacol , vol.414 , pp. 1-7
    • Lamminen, T.1    Huhtaniemi, I.2
  • 174
    • 0034124344 scopus 로고    scopus 로고
    • Association of molecular variants of luteinizing hormone with male infertility
    • Ramanujam L.N., Liao W.X., Roy A.C., et al. Association of molecular variants of luteinizing hormone with male infertility. Hum Reprod 2000, 15:925-928.
    • (2000) Hum Reprod , vol.15 , pp. 925-928
    • Ramanujam, L.N.1    Liao, W.X.2    Roy, A.C.3
  • 175
    • 0033772188 scopus 로고    scopus 로고
    • Reproductive hormones, cancers, and conditions in relation to a common genetic variant of luteinizing hormone
    • Cramer D.W., Petterson K.S.I., Barbieri R.L., et al. Reproductive hormones, cancers, and conditions in relation to a common genetic variant of luteinizing hormone. Hum Reprod 2000, 15:2103-2107.
    • (2000) Hum Reprod , vol.15 , pp. 2103-2107
    • Cramer, D.W.1    Petterson, K.S.I.2    Barbieri, R.L.3
  • 176
    • 0033799699 scopus 로고    scopus 로고
    • Pituitary response to luteinizing hormone-releasing hormone in women with variant luteinizing hormone
    • Takahashi K., Kurioka H., Ozaki T., et al. Pituitary response to luteinizing hormone-releasing hormone in women with variant luteinizing hormone. Eur J Endocrinol 2000, 143:375-381.
    • (2000) Eur J Endocrinol , vol.143 , pp. 375-381
    • Takahashi, K.1    Kurioka, H.2    Ozaki, T.3
  • 177
    • 0037336772 scopus 로고    scopus 로고
    • Genetic analysis of three polymorphic sites of the luteinizing hormone beta-subunit gene in infertile Korean men with nonbstructive azoospermia
    • Lee S., Kim N.K., Kim H.J., et al. Genetic analysis of three polymorphic sites of the luteinizing hormone beta-subunit gene in infertile Korean men with nonbstructive azoospermia. Fertil Steril 2003, 79:517-521.
    • (2003) Fertil Steril , vol.79 , pp. 517-521
    • Lee, S.1    Kim, N.K.2    Kim, H.J.3
  • 178
    • 0038021577 scopus 로고    scopus 로고
    • Luteinizing hormone signaling and breast cancer: polymorphisms and age of onset
    • Powell B.L., Piersma D., Kevenaar M.E., et al. Luteinizing hormone signaling and breast cancer: polymorphisms and age of onset. J Clin Endocrinol Metab 2003, 88:1653-1657.
    • (2003) J Clin Endocrinol Metab , vol.88 , pp. 1653-1657
    • Powell, B.L.1    Piersma, D.2    Kevenaar, M.E.3
  • 179
    • 0036472169 scopus 로고    scopus 로고
    • Synthesis, purification and structural and functional characterization of recombinant form of a common genetic variant of human luteinizing hormone
    • Manna P.R., Joshi L., Reinhold V.N., et al. Synthesis, purification and structural and functional characterization of recombinant form of a common genetic variant of human luteinizing hormone. Hum Mol Genet 2002, 11:301-315.
    • (2002) Hum Mol Genet , vol.11 , pp. 301-315
    • Manna, P.R.1    Joshi, L.2    Reinhold, V.N.3
  • 180
    • 0029772109 scopus 로고    scopus 로고
    • Identification of seven novel mutations in LH beta-subunit gene by SSCP
    • Roy A.C., Liao W.X., Chen Y., et al. Identification of seven novel mutations in LH beta-subunit gene by SSCP. Mol Cell Biochem 1996, 165:151-153.
    • (1996) Mol Cell Biochem , vol.165 , pp. 151-153
    • Roy, A.C.1    Liao, W.X.2    Chen, Y.3
  • 181
    • 0031929585 scopus 로고    scopus 로고
    • A new molecular variant of luteinizing hormone associated with female infertility
    • Liao W.X., Roy A.C., Chan C., et al. A new molecular variant of luteinizing hormone associated with female infertility. Fertil Steril 1998, 69:102-106.
    • (1998) Fertil Steril , vol.69 , pp. 102-106
    • Liao, W.X.1    Roy, A.C.2    Chan, C.3
  • 182
    • 0031926595 scopus 로고    scopus 로고
    • Molecular variants of luteinizing hormone in three populations of southeast Asia
    • Ramanujam L., Liao W.X., Roy A.C., et al. Molecular variants of luteinizing hormone in three populations of southeast Asia. Hum Hered 1998, 48:232-234.
    • (1998) Hum Hered , vol.48 , pp. 232-234
    • Ramanujam, L.1    Liao, W.X.2    Roy, A.C.3
  • 183
    • 0036798245 scopus 로고    scopus 로고
    • Functional study of a recombinant form of human LH beta-subunit variant carrying the Gly(102)Ser mutation found in asian populations
    • Lamminen T., Jiang M., Manna P.R., et al. Functional study of a recombinant form of human LH beta-subunit variant carrying the Gly(102)Ser mutation found in asian populations. Mol Hum Reprod 2002, 8:887-892.
    • (2002) Mol Hum Reprod , vol.8 , pp. 887-892
    • Lamminen, T.1    Jiang, M.2    Manna, P.R.3
  • 184
    • 0036705559 scopus 로고    scopus 로고
    • Functional characterization of a natural variant of luteinizing hormone
    • Liao W.X., Goh H.H., Roy A.C. Functional characterization of a natural variant of luteinizing hormone. Hum Genet 2002, 111:219-224.
    • (2002) Hum Genet , vol.111 , pp. 219-224
    • Liao, W.X.1    Goh, H.H.2    Roy, A.C.3
  • 185
    • 0036187866 scopus 로고    scopus 로고
    • A novel Ala(-3)Thr mutation in the signal peptide of human luteinizing hormone beta-subunit: potentiation of the inositol phosphate signalling pathway and attenuation of the adenylate cyclase pathway by recombinant variant hormone
    • Jiang M., Lamminen T., Pakarinen P., et al. A novel Ala(-3)Thr mutation in the signal peptide of human luteinizing hormone beta-subunit: potentiation of the inositol phosphate signalling pathway and attenuation of the adenylate cyclase pathway by recombinant variant hormone. Mol Hum Reprod 2002, 8:201-212.
    • (2002) Mol Hum Reprod , vol.8 , pp. 201-212
    • Jiang, M.1    Lamminen, T.2    Pakarinen, P.3
  • 186
    • 0033305129 scopus 로고    scopus 로고
    • A naturally occurring genetic variant in the human chorionic gonadotropin-beta gene 5 is assembly inefficient
    • Miller-Lindholm A.K., Bedows E., Bartels C.F., et al. A naturally occurring genetic variant in the human chorionic gonadotropin-beta gene 5 is assembly inefficient. Endocrinology 1999, 140:3496-3506.
    • (1999) Endocrinology , vol.140 , pp. 3496-3506
    • Miller-Lindholm, A.K.1    Bedows, E.2    Bartels, C.F.3
  • 187
    • 5044241112 scopus 로고    scopus 로고
    • Absence of the genetic variant val(79)met in human chorionic gonadotropin-beta gene 5 in five European populations
    • Jiang M., Savontaus M.L., Simonsen H., et al. Absence of the genetic variant val(79)met in human chorionic gonadotropin-beta gene 5 in five European populations. Mol Human Reprod 2004, 10:763-766.
    • (2004) Mol Human Reprod , vol.10 , pp. 763-766
    • Jiang, M.1    Savontaus, M.L.2    Simonsen, H.3
  • 188
    • 0033616206 scopus 로고    scopus 로고
    • Genetics of human hypogonadotropic hypogonadism
    • Layman L.C. Genetics of human hypogonadotropic hypogonadism. Am J Med Genet 1999, 89:240-248.
    • (1999) Am J Med Genet , vol.89 , pp. 240-248
    • Layman, L.C.1
  • 189
    • 33750916941 scopus 로고    scopus 로고
    • Kiss-1 and reproduction: focus on its role in the metabolic regulation of fertility
    • Tena-Sempere M. Kiss-1 and reproduction: focus on its role in the metabolic regulation of fertility. Neuroendocrinology 2006, 83:275-281.
    • (2006) Neuroendocrinology , vol.83 , pp. 275-281
    • Tena-Sempere, M.1
  • 190
    • 34047226334 scopus 로고    scopus 로고
    • Kisspeptin expression in the brain: catalyst for the initiation of puberty
    • Smith J.T., Clarke I.J. Kisspeptin expression in the brain: catalyst for the initiation of puberty. Rev Endocr Metab Disord 2007, 8:1-9.
    • (2007) Rev Endocr Metab Disord , vol.8 , pp. 1-9
    • Smith, J.T.1    Clarke, I.J.2
  • 191
    • 34047218346 scopus 로고    scopus 로고
    • Neuroendocrine factors in the initiation of puberty: the emergent role of kisspeptin
    • Navarro V.M., Castellano J.M., Garcia-Galiano D., et al. Neuroendocrine factors in the initiation of puberty: the emergent role of kisspeptin. Rev Endocr Metab Disord 2007, 8:11-20.
    • (2007) Rev Endocr Metab Disord , vol.8 , pp. 11-20
    • Navarro, V.M.1    Castellano, J.M.2    Garcia-Galiano, D.3
  • 192
    • 33748535456 scopus 로고    scopus 로고
    • Mechanisms for pulsatile regulation of the gonadotropin subunit genes by GNRH1
    • Ferris H.A., Shupnik M.A. Mechanisms for pulsatile regulation of the gonadotropin subunit genes by GNRH1. Biol Reprod 2006, 74:993-998.
    • (2006) Biol Reprod , vol.74 , pp. 993-998
    • Ferris, H.A.1    Shupnik, M.A.2
  • 193
    • 4143096239 scopus 로고    scopus 로고
    • Multiple and overlapping combinatorial codes orchestrate hormonal responsiveness and dictate cell-specific expression of the genes encoding luteinizing hormone
    • Jorgensen J.S., Quirk C.C., Nilson J.H. Multiple and overlapping combinatorial codes orchestrate hormonal responsiveness and dictate cell-specific expression of the genes encoding luteinizing hormone. Endocr Rev 2004, 25:521-542.
    • (2004) Endocr Rev , vol.25 , pp. 521-542
    • Jorgensen, J.S.1    Quirk, C.C.2    Nilson, J.H.3
  • 194
    • 11244325727 scopus 로고    scopus 로고
    • Regulation of gonadotropin subunit gene transcription
    • Burger L.L., Haisenleder D.J., Dalkin A.C., et al. Regulation of gonadotropin subunit gene transcription. J Mol Endocrinol 2004, 33:559-584.
    • (2004) J Mol Endocrinol , vol.33 , pp. 559-584
    • Burger, L.L.1    Haisenleder, D.J.2    Dalkin, A.C.3
  • 195
    • 34547130298 scopus 로고    scopus 로고
    • The regulation of FSH beta transcription by gonadal steroids: testosterone and estradiol modulation of the activin intracellular signaling pathway
    • Burger L.L., Haisenleder D.J., Wotton G.M., et al. The regulation of FSH beta transcription by gonadal steroids: testosterone and estradiol modulation of the activin intracellular signaling pathway. Am J Physiol Endocrinol Metab 2007, 293:E277-E285.
    • (2007) Am J Physiol Endocrinol Metab , vol.293
    • Burger, L.L.1    Haisenleder, D.J.2    Wotton, G.M.3
  • 196
    • 33745212905 scopus 로고    scopus 로고
    • Transcription of gonadotropin beta subunit genes involves cross-talk between the transcription factors and co-regulators that mediate actions of the regulatory hormones
    • Melamed P., Kadir M.N.A., Wijeweera A., et al. Transcription of gonadotropin beta subunit genes involves cross-talk between the transcription factors and co-regulators that mediate actions of the regulatory hormones. Mol Cell Endocrinol 2006, 252:167-183.
    • (2006) Mol Cell Endocrinol , vol.252 , pp. 167-183
    • Melamed, P.1    Kadir, M.N.A.2    Wijeweera, A.3
  • 197
    • 0028783348 scopus 로고
    • Different composite regulatory elements direct expression of the human alpha-subunit gene to pituitary and placenta
    • Heckert L.L., Schultz K., Nilson J.H. Different composite regulatory elements direct expression of the human alpha-subunit gene to pituitary and placenta. J Biol Chem 1995, 270:26497-26504.
    • (1995) J Biol Chem , vol.270 , pp. 26497-26504
    • Heckert, L.L.1    Schultz, K.2    Nilson, J.H.3
  • 198
    • 34247882674 scopus 로고    scopus 로고
    • Maximal activity of the luteinizing hormone beta-subunit gene requires beta-catenin
    • Salisbury T.B., Binder A.K., Grammer J.C., et al. Maximal activity of the luteinizing hormone beta-subunit gene requires beta-catenin. Mol Endocrinol 2007, 21:963-971.
    • (2007) Mol Endocrinol , vol.21 , pp. 963-971
    • Salisbury, T.B.1    Binder, A.K.2    Grammer, J.C.3
  • 199
    • 2342539822 scopus 로고    scopus 로고
    • Activin regulation of the follicle-stimulating hormone beta-subunit gene involves smads and the tale homeodomain proteins pbx1 and prep1
    • Bailey J.S., Rave-Harel N., McGillivray S.M., et al. Activin regulation of the follicle-stimulating hormone beta-subunit gene involves smads and the tale homeodomain proteins pbx1 and prep1. Mol Endocrinol 2004, 18:1158-1170.
    • (2004) Mol Endocrinol , vol.18 , pp. 1158-1170
    • Bailey, J.S.1    Rave-Harel, N.2    McGillivray, S.M.3
  • 200
    • 0027416348 scopus 로고
    • Regulation of chorionic-gonadotropin gene-expression
    • Jameson J.L., Hollenberg A.N. Regulation of chorionic-gonadotropin gene-expression. Endocr Rev 1993, 14:203-221.
    • (1993) Endocr Rev , vol.14 , pp. 203-221
    • Jameson, J.L.1    Hollenberg, A.N.2
  • 201
    • 85003156760 scopus 로고
    • Coordinate control of the alpha-subunit and beta-subunit genes of human chorionic-gonadotropin by trophoblast specific element-binding protein
    • Steger D.J., Buscher M., Hecht J.H., et al. Coordinate control of the alpha-subunit and beta-subunit genes of human chorionic-gonadotropin by trophoblast specific element-binding protein. Mol Endocrinol 1993, 7:1579-1588.
    • (1993) Mol Endocrinol , vol.7 , pp. 1579-1588
    • Steger, D.J.1    Buscher, M.2    Hecht, J.H.3
  • 202
    • 15444368206 scopus 로고    scopus 로고
    • Coordinate regulation of basal and cyclic 5́-adenosine monophosphate (cAMP)-activated expression of human chorionic gonadotropin-alpha by ets-2 and cAMP-responsive element binding protein
    • Ghosh D., Sachdev S., Hannick M., et al. Coordinate regulation of basal and cyclic 5́-adenosine monophosphate (cAMP)-activated expression of human chorionic gonadotropin-alpha by ets-2 and cAMP-responsive element binding protein. Mol Endocrinol 2005, 19:1049-1066.
    • (2005) Mol Endocrinol , vol.19 , pp. 1049-1066
    • Ghosh, D.1    Sachdev, S.2    Hannick, M.3
  • 203
    • 0028302016 scopus 로고
    • A change in the isoforms of human chorionic-gonadotropin occurs around the 13th week of gestation
    • Wide L., Lee J.Y., Rasmussen C. A change in the isoforms of human chorionic-gonadotropin occurs around the 13th week of gestation. J Clin Endocrinol Metab 1994, 78:1419-1423.
    • (1994) J Clin Endocrinol Metab , vol.78 , pp. 1419-1423
    • Wide, L.1    Lee, J.Y.2    Rasmussen, C.3
  • 204
    • 0032935044 scopus 로고    scopus 로고
    • Early pregnancy human chorionic gonadotropin (hCG) isoforms measured by an immunometric assay for choriocarcinoma-like hCG
    • Kovalevskaya G., Birken S., Kakuma T., et al. Early pregnancy human chorionic gonadotropin (hCG) isoforms measured by an immunometric assay for choriocarcinoma-like hCG. J Endocrinol 1999, 161:99-106.
    • (1999) J Endocrinol , vol.161 , pp. 99-106
    • Kovalevskaya, G.1    Birken, S.2    Kakuma, T.3
  • 205
    • 0037200677 scopus 로고    scopus 로고
    • Trophoblast origin of hCG isoforms: cytotrophoblasts are the primary source of choriocarcinoma-like hCG
    • Kovalevskaya G., Genbacev O., Fisher S.J., et al. Trophoblast origin of hCG isoforms: cytotrophoblasts are the primary source of choriocarcinoma-like hCG. Mol Cell Endocrinol 2002, 194:147-155.
    • (2002) Mol Cell Endocrinol , vol.194 , pp. 147-155
    • Kovalevskaya, G.1    Genbacev, O.2    Fisher, S.J.3
  • 206
    • 33751254761 scopus 로고    scopus 로고
    • Patterns of LH beta cf among women in health and disease
    • Birken S., McChesney R., Yershova O., et al. Patterns of LH beta cf among women in health and disease. Mol Cell Endocrinol 2007, 260:172-182.
    • (2007) Mol Cell Endocrinol , vol.260 , pp. 172-182
    • Birken, S.1    McChesney, R.2    Yershova, O.3
  • 207
    • 33751200662 scopus 로고    scopus 로고
    • Determination of hyperglycosylated human chorionic gonadotropin produced by malignant gestational trophoblastic neoplasias and male germ cell tumors using a lectin-based immunoassay and surface plasmon resonance
    • Kelly L.S., Birken S., Puett D. Determination of hyperglycosylated human chorionic gonadotropin produced by malignant gestational trophoblastic neoplasias and male germ cell tumors using a lectin-based immunoassay and surface plasmon resonance. Mol Cell Endocrinol 2007, 260:33-39.
    • (2007) Mol Cell Endocrinol , vol.260 , pp. 33-39
    • Kelly, L.S.1    Birken, S.2    Puett, D.3
  • 208
    • 0005546915 scopus 로고
    • Luteinizing hormone microheterogeneity
    • CRC Press, Boca Raton, FL, B.A. Keel, H.E. Grotjan (Eds.)
    • Keel B.A., Grotjan H.E. Luteinizing hormone microheterogeneity. Microheterogeneity of Glycoprotein Hormones 1989, 149-184. CRC Press, Boca Raton, FL. B.A. Keel, H.E. Grotjan (Eds.).
    • (1989) Microheterogeneity of Glycoprotein Hormones , pp. 149-184
    • Keel, B.A.1    Grotjan, H.E.2
  • 209
    • 0028020550 scopus 로고
    • Protein-specific glycosyltransferases: how and why they do it
    • Baenziger J.U. Protein-specific glycosyltransferases: how and why they do it. FASEB J 1994, 8:1019-1025.
    • (1994) FASEB J , vol.8 , pp. 1019-1025
    • Baenziger, J.U.1
  • 210
    • 0031196046 scopus 로고    scopus 로고
    • Carbohydrate and peptide structure of the alpha -and beta-subunits of human chorionic gonadotropin from normal and aberrant pregnancy and choriocarcinoma
    • Elliott M.M., Kardana A., Lustbader J.W., et al. Carbohydrate and peptide structure of the alpha -and beta-subunits of human chorionic gonadotropin from normal and aberrant pregnancy and choriocarcinoma. Endocrine 1997, 7:15-32.
    • (1997) Endocrine , vol.7 , pp. 15-32
    • Elliott, M.M.1    Kardana, A.2    Lustbader, J.W.3
  • 211
    • 33751217743 scopus 로고    scopus 로고
    • Hyperglycosylated hCG in gestational implantation and in choriocarcinoma and testicular germ cell malignancy tumorigenesis
    • Cole L.A., Khanlian S.A., Riley J.M., et al. Hyperglycosylated hCG in gestational implantation and in choriocarcinoma and testicular germ cell malignancy tumorigenesis. J Reprod Med 2006, 51:919-928.
    • (2006) J Reprod Med , vol.51 , pp. 919-928
    • Cole, L.A.1    Khanlian, S.A.2    Riley, J.M.3
  • 212
    • 33751203568 scopus 로고    scopus 로고
    • Hyperglycosylated HCG expression in pregnancy: cellular origin and clinical applications
    • Kovalevskaya G., Kakuma T., Schlatterer J., et al. Hyperglycosylated HCG expression in pregnancy: cellular origin and clinical applications. Mol Cell Endocrinol 2007, 260:237-243.
    • (2007) Mol Cell Endocrinol , vol.260 , pp. 237-243
    • Kovalevskaya, G.1    Kakuma, T.2    Schlatterer, J.3
  • 213
    • 0018733914 scopus 로고
    • Structures of n-glycosidic carbohydrate units of human chorionic-gonadotropin
    • Kessler M.J., Reddy M.S., Shah R.H., et al. Structures of n-glycosidic carbohydrate units of human chorionic-gonadotropin. J Biol Chem 1979, 254:7901-7908.
    • (1979) J Biol Chem , vol.254 , pp. 7901-7908
    • Kessler, M.J.1    Reddy, M.S.2    Shah, R.H.3
  • 214
    • 0025976986 scopus 로고
    • NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin
    • Weisshaar G., Hiyama J., Renwick A.G.C., et al. NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin. Eur J Biochem 1991, 195:257-268.
    • (1991) Eur J Biochem , vol.195 , pp. 257-268
    • Weisshaar, G.1    Hiyama, J.2    Renwick, A.G.C.3
  • 215
    • 0026487123 scopus 로고
    • Human chorionic-gonadotropin and subunit composition of maternal serum and celomic and amniotic fluids in the 1st trimester of pregnancy
    • Iles R.K., Wathen N.C., Campbell D.J., et al. Human chorionic-gonadotropin and subunit composition of maternal serum and celomic and amniotic fluids in the 1st trimester of pregnancy. J Endocrinol 1992, 135:563-569.
    • (1992) J Endocrinol , vol.135 , pp. 563-569
    • Iles, R.K.1    Wathen, N.C.2    Campbell, D.J.3
  • 216
    • 45549085836 scopus 로고    scopus 로고
    • A carboxyl-terminal sequence in the lutropin β subunit contributes to the sorting of lutropin to the regulated pathway
    • Jablonka-Shariff A., Pearl C.A., Comstock A., Boime I. A carboxyl-terminal sequence in the lutropin β subunit contributes to the sorting of lutropin to the regulated pathway. J Biol Chem 2008, 283:11485-11492.
    • (2008) J Biol Chem , vol.283 , pp. 11485-11492
    • Jablonka-Shariff, A.1    Pearl, C.A.2    Comstock, A.3    Boime, I.4
  • 217
    • 0037059830 scopus 로고    scopus 로고
    • Evolution of lutropin to chorionic gonadotropin generates a specific routing signal for apical release in vivo
    • Jablonka-Shariff A., Garcia-Campayo V., Boime I. Evolution of lutropin to chorionic gonadotropin generates a specific routing signal for apical release in vivo. J Biol Chem 2002, 277:879-882.
    • (2002) J Biol Chem , vol.277 , pp. 879-882
    • Jablonka-Shariff, A.1    Garcia-Campayo, V.2    Boime, I.3
  • 218
    • 84883998710 scopus 로고    scopus 로고
    • Role of the LH beta carboxyl terminus in the secretion and assembly with the alpha subunit in pituitary-derived gh3 cells
    • 175-175
    • Jablonka-Shariff A., Daphna-Iken D., Boime I. Role of the LH beta carboxyl terminus in the secretion and assembly with the alpha subunit in pituitary-derived gh3 cells. Biol Reprod 2004, 175-175.
    • (2004) Biol Reprod
    • Jablonka-Shariff, A.1    Daphna-Iken, D.2    Boime, I.3
  • 219
    • 0022884332 scopus 로고
    • Biosynthesis of sulfated asparagine-linked oligosaccharides on bovine lutropin
    • Green E.D., Boime I., Baenziger J.U. Biosynthesis of sulfated asparagine-linked oligosaccharides on bovine lutropin. J Biol Chem 1986, 261:6309-6316.
    • (1986) J Biol Chem , vol.261 , pp. 6309-6316
    • Green, E.D.1    Boime, I.2    Baenziger, J.U.3
  • 220
    • 0023928616 scopus 로고
    • Asparagine-linked oligosaccharides on lutropin, follitropin, and thyrotropin: 1. Structural elucidation of the sulfated and sialylated oligosaccharides on bovine, ovine, and human pituitary glycoprotein hormones
    • Green E.D., Baenziger J.U. Asparagine-linked oligosaccharides on lutropin, follitropin, and thyrotropin: 1. Structural elucidation of the sulfated and sialylated oligosaccharides on bovine, ovine, and human pituitary glycoprotein hormones. J Biol Chem 1988, 263:25-35.
    • (1988) J Biol Chem , vol.263 , pp. 25-35
    • Green, E.D.1    Baenziger, J.U.2
  • 221
    • 0023930204 scopus 로고
    • Asparagine-linked oligosaccharides on lutropin, follitropin, and thyrotropin: 2. Distributions of sulfated and sialylated oligosaccharides on bovine, ovine, and human pituitary glycoprotein hormones
    • Green E.D., Baenziger J.U. Asparagine-linked oligosaccharides on lutropin, follitropin, and thyrotropin: 2. Distributions of sulfated and sialylated oligosaccharides on bovine, ovine, and human pituitary glycoprotein hormones. J Biol Chem 1988, 263:36-44.
    • (1988) J Biol Chem , vol.263 , pp. 36-44
    • Green, E.D.1    Baenziger, J.U.2
  • 222
    • 33947577452 scopus 로고    scopus 로고
    • The gonadotropins: tissue-specific angiogenic factors?
    • Reisinger K., Baal N., McKinnon T., et al. The gonadotropins: tissue-specific angiogenic factors?. Mol Cell Endocrinol 2007, 269:65-80.
    • (2007) Mol Cell Endocrinol , vol.269 , pp. 65-80
    • Reisinger, K.1    Baal, N.2    McKinnon, T.3
  • 223
    • 0029959986 scopus 로고    scopus 로고
    • Isolation and characterization of human pituitary chorionic gonadotropin
    • Birken S., Maydelman Y., Gawinowicz M.A., et al. Isolation and characterization of human pituitary chorionic gonadotropin. Endocrinology 1996, 137:1402-1411.
    • (1996) Endocrinology , vol.137 , pp. 1402-1411
    • Birken, S.1    Maydelman, Y.2    Gawinowicz, M.A.3
  • 224
    • 0021745685 scopus 로고
    • Unusual molecular-forms of HCG in gestational trophoblastic neoplasia
    • Amr S., Rosa C., Wehmann R., et al. Unusual molecular-forms of HCG in gestational trophoblastic neoplasia. Ann Endocrinol (Paris) 1984, 45:321-326.
    • (1984) Ann Endocrinol (Paris) , vol.45 , pp. 321-326
    • Amr, S.1    Rosa, C.2    Wehmann, R.3
  • 225
    • 0023835120 scopus 로고
    • Comparative study of the mucin-type sugar chains of human chorionic-gonadotropin present in the urine of patients with trophoblastic diseases and healthy pregnant women
    • Amano J., Nishimura R., Mochizuki M., et al. Comparative study of the mucin-type sugar chains of human chorionic-gonadotropin present in the urine of patients with trophoblastic diseases and healthy pregnant women. J Biol Chem 1988, 263:1157-1165.
    • (1988) J Biol Chem , vol.263 , pp. 1157-1165
    • Amano, J.1    Nishimura, R.2    Mochizuki, M.3
  • 226
    • 33751345056 scopus 로고    scopus 로고
    • Discrepancies between commercially available immunoassays in the detection of tumour-derived hCG
    • Mitchell H., Seckl M.J. Discrepancies between commercially available immunoassays in the detection of tumour-derived hCG. Mol Cell Endocrinol 2007, 260:310-313.
    • (2007) Mol Cell Endocrinol , vol.260 , pp. 310-313
    • Mitchell, H.1    Seckl, M.J.2
  • 227
    • 0032409467 scopus 로고    scopus 로고
    • Gonadotrophin secretion patterns in testicular cancer patients with greatly increased human chorionic gonadotrophin serum concentrations
    • Madersbacher S., Gerth R., Mann K., et al. Gonadotrophin secretion patterns in testicular cancer patients with greatly increased human chorionic gonadotrophin serum concentrations. J Endocrinol 1998, 159:451-458.
    • (1998) J Endocrinol , vol.159 , pp. 451-458
    • Madersbacher, S.1    Gerth, R.2    Mann, K.3
  • 229
    • 33751210312 scopus 로고    scopus 로고
    • Ectopic hCG beta expression by epithelial cancer: malignant behaviour, metastasis and inhibition of tumor cell apoptosis
    • Iles R.K. Ectopic hCG beta expression by epithelial cancer: malignant behaviour, metastasis and inhibition of tumor cell apoptosis. Mol Cell Endocrinol 2007, 260:264-270.
    • (2007) Mol Cell Endocrinol , vol.260 , pp. 264-270
    • Iles, R.K.1
  • 230
    • 0035909525 scopus 로고    scopus 로고
    • The CGA gene as new predictor of the response to endocrine therapy in ER alpha-positive postmenopausal breast cancer patients
    • Bieche I., Parfait B., Nogues C., et al. The CGA gene as new predictor of the response to endocrine therapy in ER alpha-positive postmenopausal breast cancer patients. Oncogene 2001, 20:6955-6959.
    • (2001) Oncogene , vol.20 , pp. 6955-6959
    • Bieche, I.1    Parfait, B.2    Nogues, C.3
  • 231
    • 0036522580 scopus 로고    scopus 로고
    • CGA gene (coding for the alpha subunit of glycoprotein hormones) overexpression in ER alpha-positive prostate tumors
    • Bieche I., Latil A., Parfait B., et al. CGA gene (coding for the alpha subunit of glycoprotein hormones) overexpression in ER alpha-positive prostate tumors. Eur Urol 2002, 41:335-341.
    • (2002) Eur Urol , vol.41 , pp. 335-341
    • Bieche, I.1    Latil, A.2    Parfait, B.3
  • 232
    • 0031923081 scopus 로고    scopus 로고
    • Prognostic value of chorionic gonadotropin beta gene transcripts in human breast carcinoma
    • Bieche I., Lazar V., Nogues C., et al. Prognostic value of chorionic gonadotropin beta gene transcripts in human breast carcinoma. Clin Cancer Res 1998, 4:671-676.
    • (1998) Clin Cancer Res , vol.4 , pp. 671-676
    • Bieche, I.1    Lazar, V.2    Nogues, C.3
  • 233
    • 0032736474 scopus 로고    scopus 로고
    • Hyperglycosylated human chorionic gonadotropin (invasive trophoblast antigen) immunoassay: a new basis for gestational Down syndrome screening
    • Cole L.A., Shahabi S., Oz U.A., et al. Hyperglycosylated human chorionic gonadotropin (invasive trophoblast antigen) immunoassay: a new basis for gestational Down syndrome screening. Clin Chem 1999, 45:2109-2119.
    • (1999) Clin Chem , vol.45 , pp. 2109-2119
    • Cole, L.A.1    Shahabi, S.2    Oz, U.A.3
  • 234
    • 3242763029 scopus 로고    scopus 로고
    • Second-trimester maternal serum invasive trophoblast antigen: a marker for Down syndrome screening
    • Pandian R., Cole L.A., Palomaki G.E. Second-trimester maternal serum invasive trophoblast antigen: a marker for Down syndrome screening. Clin Chem 2004, 50:1433-1435.
    • (2004) Clin Chem , vol.50 , pp. 1433-1435
    • Pandian, R.1    Cole, L.A.2    Palomaki, G.E.3
  • 235
    • 0033672037 scopus 로고    scopus 로고
    • Comparison of urinary hyperglycosylated human chorionic gonadotropin concentration with the serum triple screen for Down syndrome detection in high-risk pregnancies
    • Bahado-Singh R.O., Oz U., Shahabi S., et al. Comparison of urinary hyperglycosylated human chorionic gonadotropin concentration with the serum triple screen for Down syndrome detection in high-risk pregnancies. Am J Obstet Gynecol 2000, 183:1114-1118.
    • (2000) Am J Obstet Gynecol , vol.183 , pp. 1114-1118
    • Bahado-Singh, R.O.1    Oz, U.2    Shahabi, S.3
  • 236
    • 33751243637 scopus 로고    scopus 로고
    • Standardization of FSH, LH and hCG: current position and future prospects
    • Sturgeon C.M., Ellis A.R. Standardization of FSH, LH and hCG: current position and future prospects. Mol Cell Endocrinol 2007, 260:301-309.
    • (2007) Mol Cell Endocrinol , vol.260 , pp. 301-309
    • Sturgeon, C.M.1    Ellis, A.R.2
  • 237
    • 0035668894 scopus 로고    scopus 로고
    • Immunochemical measurement of early pregnancy isoforms of hCG: potential applications to fertility research, prenatal diagnosis, and cancer
    • Birken S., Kovalevskaya G., O'Connor J. Immunochemical measurement of early pregnancy isoforms of hCG: potential applications to fertility research, prenatal diagnosis, and cancer. Arch Med Res 2001, 32:635-643.
    • (2001) Arch Med Res , vol.32 , pp. 635-643
    • Birken, S.1    Kovalevskaya, G.2    O'Connor, J.3
  • 238
    • 0036124932 scopus 로고    scopus 로고
    • The isobm td-7 workshop on hCG and related molecules: towards user-oriented standardization of pregnancy and tumor diagnosis. Assignment of epitopes to the three-dimensional structure of diagnostically and commercially relevant monoclonal antibodies directed against human chorionic gonadotropin and derivatives
    • Berger P., Sturgeon C., Bidart J.M., et al. The isobm td-7 workshop on hCG and related molecules: towards user-oriented standardization of pregnancy and tumor diagnosis. Assignment of epitopes to the three-dimensional structure of diagnostically and commercially relevant monoclonal antibodies directed against human chorionic gonadotropin and derivatives. Tumor Biol 2002, 23:1-38.
    • (2002) Tumor Biol , vol.23 , pp. 1-38
    • Berger, P.1    Sturgeon, C.2    Bidart, J.M.3
  • 239
    • 11144348654 scopus 로고    scopus 로고
    • Establishment, value assignment, and characterization of new WHO reference reagents for six molecular forms of human chorionic gonadotropin
    • Bristow A., Berger P., Bidart J.M., et al. Establishment, value assignment, and characterization of new WHO reference reagents for six molecular forms of human chorionic gonadotropin. Clin Chem 2005, 51:177-182.
    • (2005) Clin Chem , vol.51 , pp. 177-182
    • Bristow, A.1    Berger, P.2    Bidart, J.M.3
  • 240
    • 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., et al. 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 U S A 1992, 89:4304-4308.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 4304-4308
    • Fares, F.A.1    Suganuma, N.2    Nishimori, K.3
  • 241
    • 0026465141 scopus 로고
    • Enhanced stimulation of follicle maturation and ovulatory potential by long-acting follicle-stimulating-hormone agonists with extended carboxyl-terminal peptides
    • Lapolt P.S., Nishimori K., Fares F.A., et al. Enhanced stimulation of follicle maturation and ovulatory potential by long-acting follicle-stimulating-hormone agonists with extended carboxyl-terminal peptides. Endocrinology 1992, 131:2514-2520.
    • (1992) Endocrinology , vol.131 , pp. 2514-2520
    • Lapolt, P.S.1    Nishimori, K.2    Fares, F.A.3
  • 242
    • 0034883220 scopus 로고    scopus 로고
    • First human exposure to FSH-CTP in hypogonadotrophic hypogonadal males
    • Bouloux P.M.G., Handelsman D.J., Jockenhovel F., et al. First human exposure to FSH-CTP in hypogonadotrophic hypogonadal males. Hum Reprod 2001, 16:1592-1597.
    • (2001) Hum Reprod , vol.16 , pp. 1592-1597
    • Bouloux, P.M.G.1    Handelsman, D.J.2    Jockenhovel, F.3
  • 243
    • 0035988486 scopus 로고    scopus 로고
    • Single dose pharmacokinetics and effects on follicular growth and serum hormones of a long-acting recombinant FSH preparation (FSH-CTP) in healthy pituitary-suppressed females
    • Duijkers I.J.M., Klipping C., Boerrigter P.J., et al. Single dose pharmacokinetics and effects on follicular growth and serum hormones of a long-acting recombinant FSH preparation (FSH-CTP) in healthy pituitary-suppressed females. Hum Reprod 2002, 17:1987-1993.
    • (2002) Hum Reprod , vol.17 , pp. 1987-1993
    • Duijkers, I.J.M.1    Klipping, C.2    Boerrigter, P.J.3
  • 244
    • 58149204341 scopus 로고    scopus 로고
    • The expanding role of recombinant gonadotropins in assisted reproduction
    • Adams T.E., Boime I. The expanding role of recombinant gonadotropins in assisted reproduction. Reprod Dom Animals 2008, 186-192.
    • (2008) Reprod Dom Animals , pp. 186-192
    • Adams, T.E.1    Boime, I.2
  • 245
    • 0037622799 scopus 로고    scopus 로고
    • Glycosylation of an N-terminal extension prolongs the half-life and increases the in vivo activity of follicle stimulating hormone
    • Perlman S., van den Hazel B., Christiansen J., et al. Glycosylation of an N-terminal extension prolongs the half-life and increases the in vivo activity of follicle stimulating hormone. J Clin Endocrinol Metab 2003, 88:3227-3235.
    • (2003) J Clin Endocrinol Metab , vol.88 , pp. 3227-3235
    • Perlman, S.1    van den Hazel, B.2    Christiansen, J.3
  • 246
    • 33947591136 scopus 로고    scopus 로고
    • Human chorionic gonadotropin (hCG) and prevention of breast cancer
    • Janssens J.P., Russo J., Irma R.D., et al. Human chorionic gonadotropin (hCG) and prevention of breast cancer. Mol Cell Endocrinol 2007, 269:93-98.
    • (2007) Mol Cell Endocrinol , vol.269 , pp. 93-98
    • Janssens, J.P.1    Russo, J.2    Irma, R.D.3
  • 247
    • 0034602808 scopus 로고    scopus 로고
    • Luteinizing hormone induction of ovarian tumors: oligogenic differences between mouse strains dictates tumor disposition
    • Keri R.A., Lozada K.L., Abdul-Karim F.W., et al. Luteinizing hormone induction of ovarian tumors: oligogenic differences between mouse strains dictates tumor disposition. Proc Natl Acad Sci U S A 2000, 97:383-387.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 383-387
    • Keri, R.A.1    Lozada, K.L.2    Abdul-Karim, F.W.3
  • 248
    • 0036772574 scopus 로고    scopus 로고
    • Reproductive disturbances, pituitary lactotrope adenomas, and mammary gland tumors in transgenic female mice producing high levels of human chorionic gonadotropin
    • Rulli S.B., Kuorelahti A., Karaer O., et al. Reproductive disturbances, pituitary lactotrope adenomas, and mammary gland tumors in transgenic female mice producing high levels of human chorionic gonadotropin. Endocrinology 2002, 143:4084-4095.
    • (2002) Endocrinology , vol.143 , pp. 4084-4095
    • Rulli, S.B.1    Kuorelahti, A.2    Karaer, O.3
  • 249
    • 24944532006 scopus 로고    scopus 로고
    • What have gonadotrophin overexpressing transgenic mice taught us about gonadal function?
    • Rulli S.B., Huhtaniemi I. What have gonadotrophin overexpressing transgenic mice taught us about gonadal function?. Reproduction 2005, 130:283-291.
    • (2005) Reproduction , vol.130 , pp. 283-291
    • Rulli, S.B.1    Huhtaniemi, I.2
  • 250
    • 0038112173 scopus 로고    scopus 로고
    • Overexpression of human chorionic gonadotropin causes multiple reproductive defects in transgenic mice
    • Matzuk M.M., DeMayo F.J., Hadsell L.A., et al. Overexpression of human chorionic gonadotropin causes multiple reproductive defects in transgenic mice. Biol Reprod 2003, 69:338-346.
    • (2003) Biol Reprod , vol.69 , pp. 338-346
    • Matzuk, M.M.1    DeMayo, F.J.2    Hadsell, L.A.3
  • 251
    • 0038621388 scopus 로고    scopus 로고
    • High levels of luteinizing hormone analog stimulate gonadal and adrenal tumorigenesis in mice transgenic for the mouse inhibin-alpha-subunit promoter simian virus 40 t-antigen fusion gene
    • Mikola M., Kero J., Nilson J.H., et al. High levels of luteinizing hormone analog stimulate gonadal and adrenal tumorigenesis in mice transgenic for the mouse inhibin-alpha-subunit promoter simian virus 40 t-antigen fusion gene. Oncogene 2003, 22:3269-3278.
    • (2003) Oncogene , vol.22 , pp. 3269-3278
    • Mikola, M.1    Kero, J.2    Nilson, J.H.3
  • 252
    • 33751242027 scopus 로고    scopus 로고
    • Destruction of breast cancers and their metastases by lytic peptide conjugates in vitro and in vivo
    • 183-189
    • Hansel W., Enright F., Leuschner C. Destruction of breast cancers and their metastases by lytic peptide conjugates in vitro and in vivo. Mol Cell Endocrinol 2007, 260. 183-189.
    • (2007) Mol Cell Endocrinol , vol.260
    • Hansel, W.1    Enright, F.2    Leuschner, C.3
  • 253
    • 0037367239 scopus 로고    scopus 로고
    • Membrane disrupting lytic peptide conjugates destroy hormone dependent and independent breast cancer cells in vitro and in vivo
    • Leuschner C., Enright F.M., Gawronska B., et al. Membrane disrupting lytic peptide conjugates destroy hormone dependent and independent breast cancer cells in vitro and in vivo. Breast Cancer Res Treat 2003, 78:17-27.
    • (2003) Breast Cancer Res Treat , vol.78 , pp. 17-27
    • Leuschner, C.1    Enright, F.M.2    Gawronska, B.3
  • 254
    • 0036229112 scopus 로고    scopus 로고
    • Effects of a lytic peptide conjugated to beta hCG on ovarian cancer: studies in vitro and in vivo
    • Gawronska B., Leuschner C., Enright F.M., et al. Effects of a lytic peptide conjugated to beta hCG on ovarian cancer: studies in vitro and in vivo. Gynecol Oncol 2002, 85:45-52.
    • (2002) Gynecol Oncol , vol.85 , pp. 45-52
    • Gawronska, B.1    Leuschner, C.2    Enright, F.M.3
  • 255
    • 33947603270 scopus 로고    scopus 로고
    • Conjugates of lytic peptides and LHRH or PCG target and cause necrosis of prostate cancers and metastases
    • Hansel W., Leuschner C., Enright F. Conjugates of lytic peptides and LHRH or PCG target and cause necrosis of prostate cancers and metastases. Mol Cell Endocrinol 2007, 269:26-33.
    • (2007) Mol Cell Endocrinol , vol.269 , pp. 26-33
    • Hansel, W.1    Leuschner, C.2    Enright, F.3
  • 256
    • 33947574542 scopus 로고    scopus 로고
    • Use of hecate-chorionic gonadotropin beta conjugate in therapy of lutenizing hormone receptor expressing gonadal somatic cell tumors
    • Rivero-Muller A., Vuorenoja S., Tuominen M., et al. Use of hecate-chorionic gonadotropin beta conjugate in therapy of lutenizing hormone receptor expressing gonadal somatic cell tumors. Mol Cell Endocrinol 2007, 269:17-25.
    • (2007) Mol Cell Endocrinol , vol.269 , pp. 17-25
    • Rivero-Muller, A.1    Vuorenoja, S.2    Tuominen, M.3
  • 257
    • 84883952612 scopus 로고
    • Human chorionic gonadotropin (hCG) induces apoptosis of neoplastic Kaposi's sarcoma cell lines (ks y-1 and ks slk)
    • 1514-1514
    • Lunardi Iskandar Y., Bryant J.L., Zeman R.A., et al. Human chorionic gonadotropin (hCG) induces apoptosis of neoplastic Kaposi's sarcoma cell lines (ks y-1 and ks slk). Blood 1995, 86. 1514-1514.
    • (1995) Blood , vol.86
    • Lunardi Iskandar, Y.1    Bryant, J.L.2    Zeman, R.A.3
  • 258
    • 0033585494 scopus 로고    scopus 로고
    • Induction of programmed cell death in Kaposi's sarcoma cells by preparations of human chorionic gonadotropin
    • Samaniego F., Bryant J.L., Liu N., et al. Induction of programmed cell death in Kaposi's sarcoma cells by preparations of human chorionic gonadotropin. J Natl Cancer Inst 1999, 91:135-143.
    • (1999) J Natl Cancer Inst , vol.91 , pp. 135-143
    • Samaniego, F.1    Bryant, J.L.2    Liu, N.3
  • 259
    • 0036321006 scopus 로고    scopus 로고
    • Human chorionic gonadotropin inhibits Kaposi's sarcoma associated angiogenesis, matrix metalloprotease activity, and tumor growth
    • Pfeffer U., Bisacchi D., Morini M., et al. Human chorionic gonadotropin inhibits Kaposi's sarcoma associated angiogenesis, matrix metalloprotease activity, and tumor growth. Endocrinology 2002, 143:3114-3121.
    • (2002) Endocrinology , vol.143 , pp. 3114-3121
    • Pfeffer, U.1    Bisacchi, D.2    Morini, M.3
  • 260
    • 33644759357 scopus 로고    scopus 로고
    • Luteinizing hormone modulates cognition and amyloid-deposition in Alzheimer APP transgenic mice
    • Casadesus G., Webber K.M., Atwood C.S., et al. Luteinizing hormone modulates cognition and amyloid-deposition in Alzheimer APP transgenic mice. Biochim Biophys Acta 2006, 1762:447-452.
    • (2006) Biochim Biophys Acta , vol.1762 , pp. 447-452
    • Casadesus, G.1    Webber, K.M.2    Atwood, C.S.3
  • 261
    • 33947593994 scopus 로고    scopus 로고
    • Increases in luteinizing hormone are associated with declines in cognitive performance
    • Casadesus G., Milliken E.L., Webber K.M., et al. Increases in luteinizing hormone are associated with declines in cognitive performance. Mol Cell Endocrinol 2007, 269:107-111.
    • (2007) Mol Cell Endocrinol , vol.269 , pp. 107-111
    • Casadesus, G.1    Milliken, E.L.2    Webber, K.M.3
  • 262
    • 33751251056 scopus 로고    scopus 로고
    • Gonadotropins: a cohesive gender-based etiology of Alzheimer disease
    • Webber K.M., Casadesus G., Atwood C.S., et al. Gonadotropins: a cohesive gender-based etiology of Alzheimer disease. Mol Cell Endocrinol 2007, 260:271-275.
    • (2007) Mol Cell Endocrinol , vol.260 , pp. 271-275
    • Webber, K.M.1    Casadesus, G.2    Atwood, C.S.3
  • 264
    • 0026042543 scopus 로고
    • Expression of human luteinizing hormone (LH) receptor: interaction with LH and chorionic gonadotropin from human but not equine, rat, and ovine species
    • Jia X.-C., Oikawa M., Bo M., et al. Expression of human luteinizing hormone (LH) receptor: interaction with LH and chorionic gonadotropin from human but not equine, rat, and ovine species. Mol Endocrinol 1991, 5:759-768.
    • (1991) Mol Endocrinol , vol.5 , pp. 759-768
    • Jia, X.-C.1    Oikawa, M.2    Bo, M.3
  • 266
    • 0026800702 scopus 로고
    • The cloning of the human follicle stimulating hormone receptor and its expression in cos-7, cho, and y-1 cells
    • Kelton C., Cheng S.V.Y., Nugent N.P., et al. The cloning of the human follicle stimulating hormone receptor and its expression in cos-7, cho, and y-1 cells. Mol Cell Endocrinol 1992, 89:141-151.
    • (1992) Mol Cell Endocrinol , vol.89 , pp. 141-151
    • Kelton, C.1    Cheng, S.V.Y.2    Nugent, N.P.3
  • 267
    • 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
  • 268
    • 0037446894 scopus 로고    scopus 로고
    • The G protein-coupled receptor repertoires of human and mouse
    • Vassilatis D.K., Hohmann J.G., Zeng H., et al. The G protein-coupled receptor repertoires of human and mouse. Proc Natl Acad Sci U S A 2003, 100:4903-4908.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 4903-4908
    • Vassilatis, D.K.1    Hohmann, J.G.2    Zeng, H.3
  • 269
    • 0034948696 scopus 로고    scopus 로고
    • Structural mimicry in G protein coupled receptors: implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors
    • Ballesteros J.A., Shi L., Javitch J.A. Structural mimicry in G protein coupled receptors: implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors. Mol Pharmacol 2001, 60:1-19.
    • (2001) Mol Pharmacol , vol.60 , pp. 1-19
    • Ballesteros, J.A.1    Shi, L.2    Javitch, J.A.3
  • 270
    • 0036217072 scopus 로고    scopus 로고
    • The lutropin/choriogonadotropin receptor: a 2002 perspective
    • Ascoli M., Fanelli F., Segaloff D.L. The lutropin/choriogonadotropin receptor: a 2002 perspective. Endocr Rev 2002, 23:141-174.
    • (2002) Endocr Rev , vol.23 , pp. 141-174
    • Ascoli, M.1    Fanelli, F.2    Segaloff, D.L.3
  • 271
    • 34249941108 scopus 로고    scopus 로고
    • Crystal structure of the TSH receptor in complex with a thyroid-stimulating autoantibody
    • Sanders J., Chirgadze D.Y., Sanders P., et al. Crystal structure of the TSH receptor in complex with a thyroid-stimulating autoantibody. Thyroid 2007, 17:395-410.
    • (2007) Thyroid , vol.17 , pp. 395-410
    • Sanders, J.1    Chirgadze, D.Y.2    Sanders, P.3
  • 272
    • 0037084011 scopus 로고    scopus 로고
    • Tyrosine sulfation is required for agonist recognition by glycoprotein hormone receptors
    • Costagliola S., Panneels V., Bonomi M., et al. 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
  • 273
    • 0034604451 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: a G protein-coupled receptor
    • Palczewski K., Kumasaka T., Hori T., et al. Crystal structure of rhodopsin: a G protein-coupled receptor. Science 2000, 289:739-745.
    • (2000) Science , vol.289 , pp. 739-745
    • Palczewski, K.1    Kumasaka, T.2    Hori, T.3
  • 274
    • 33846631365 scopus 로고    scopus 로고
    • Implications for molecular mechanisms of glycoprotein hormone receptors using a new sequence-structure-function analysis resource
    • Kleinau G., Brehm M., Wiedemann U., et al. Implications for molecular mechanisms of glycoprotein hormone receptors using a new sequence-structure-function analysis resource. Mol Endocrinol 2007, 21:574-580.
    • (2007) Mol Endocrinol , vol.21 , pp. 574-580
    • Kleinau, G.1    Brehm, M.2    Wiedemann, U.3
  • 275
    • 33747864226 scopus 로고    scopus 로고
    • Gris: glycoprotein-hormone receptor information system
    • Van Durme J., Horn F., Costagliola S., et al. Gris: glycoprotein-hormone receptor information system. Mol Endocrinol 2006, 20:2247-2255.
    • (2006) Mol Endocrinol , vol.20 , pp. 2247-2255
    • Van Durme, J.1    Horn, F.2    Costagliola, S.3
  • 276
    • 33751200969 scopus 로고    scopus 로고
    • Insights learned from l457(3.43)r, an activating mutant of the human lutropin receptor
    • Latronico A.C., Segaloff D.L. Insights learned from l457(3.43)r, an activating mutant of the human lutropin receptor. Mol Cell Endocrinol 2007, 260-262:287-293.
    • (2007) Mol Cell Endocrinol , vol.260-262 , pp. 287-293
    • Latronico, A.C.1    Segaloff, D.L.2
  • 277
    • 33744550356 scopus 로고    scopus 로고
    • A low molecular weight agonist signals by binding to the transmembrane domain of thyroid-stimulating hormone receptor (TSHR) and luteinizing hormone/chorionic gonadotropin receptor (LHCGR)
    • Jaschke H., Neumann S., Moore S., et al. A low molecular weight agonist signals by binding to the transmembrane domain of thyroid-stimulating hormone receptor (TSHR) and luteinizing hormone/chorionic gonadotropin receptor (LHCGR). J Biol Chem 2006, 281:9841-9844.
    • (2006) J Biol Chem , vol.281 , pp. 9841-9844
    • Jaschke, H.1    Neumann, S.2    Moore, S.3
  • 278
    • 38549139769 scopus 로고    scopus 로고
    • [3H]Org 43553, the first low molecular weight agonistic and allosteric radioligand for the human luteinizing hormone receptor
    • Heitman L., Oosterom J., Bonger K., et al. [3H]Org 43553, the first low molecular weight agonistic and allosteric radioligand for the human luteinizing hormone receptor. Mol Pharmacol 2008, 73:518-524.
    • (2008) Mol Pharmacol , vol.73 , pp. 518-524
    • Heitman, L.1    Oosterom, J.2    Bonger, K.3
  • 279
    • 0028872763 scopus 로고
    • The lutropin/choriogonadotropin (LH/CG) receptor is palmitoylated at intracellular cysteine residues
    • Zhu H., Wang H., Ascoli M. The lutropin/choriogonadotropin (LH/CG) receptor is palmitoylated at intracellular cysteine residues. Mol Endocrinol 1995, 9:141-150.
    • (1995) Mol Endocrinol , vol.9 , pp. 141-150
    • Zhu, H.1    Wang, H.2    Ascoli, M.3
  • 280
    • 0027999333 scopus 로고
    • Palmitoylation of luteinizing hormone/human choriogonadotropin receptors in transfected cells
    • Kawate N., Menon K.M.J. Palmitoylation of luteinizing hormone/human choriogonadotropin receptors in transfected cells. J Biol Chem 1994, 269:30651-30658.
    • (1994) J Biol Chem , vol.269 , pp. 30651-30658
    • Kawate, N.1    Menon, K.M.J.2
  • 281
    • 0031046907 scopus 로고    scopus 로고
    • Post-translational processing in the Golgi plays a critical role in the trafficking of the luteinizing hormone/human chorionic gonadotropin receptor to the cell surface
    • Bradbury F.A., Kawate N., Foster C.M., et al. Post-translational processing in the Golgi plays a critical role in the trafficking of the luteinizing hormone/human chorionic gonadotropin receptor to the cell surface. J Biol Chem 1997, 272:5921-5926.
    • (1997) J Biol Chem , vol.272 , pp. 5921-5926
    • Bradbury, F.A.1    Kawate, N.2    Foster, C.M.3
  • 282
    • 14844291405 scopus 로고    scopus 로고
    • Evidence that palmitoylation of carboxyl terminus cysteine residues of the human luteinizing hormone receptor regulates postendocytic processing
    • Munshi U.M., Clouser C.L., Peegel H., et al. Evidence that palmitoylation of carboxyl terminus cysteine residues of the human luteinizing hormone receptor regulates postendocytic processing. Mol Endocrinol 2005, 19:749-758.
    • (2005) Mol Endocrinol , vol.19 , pp. 749-758
    • Munshi, U.M.1    Clouser, C.L.2    Peegel, H.3
  • 283
    • 0034624958 scopus 로고    scopus 로고
    • Posttranslational modifications of the lutropin receptor: mass spectrometric analysis
    • Vu-Hai M.T., Huet J.C., Echasserieau K., et al. Posttranslational modifications of the lutropin receptor: mass spectrometric analysis. Biochemistry 2000, 39:5509-5517.
    • (2000) Biochemistry , vol.39 , pp. 5509-5517
    • Vu-Hai, M.T.1    Huet, J.C.2    Echasserieau, K.3
  • 284
    • 0030948572 scopus 로고    scopus 로고
    • The six N-linked carbohydraes of the lutropin/choriogonadotropin receptor are not absolutely required for correct folding, cell surface expression, hormone binding or signal transduction
    • Davis D.P., Rozell T.G., Liu X., et al. The six N-linked carbohydraes of the lutropin/choriogonadotropin receptor are not absolutely required for correct folding, cell surface expression, hormone binding or signal transduction. Mol Endocrinol 1997, 11:550-562.
    • (1997) Mol Endocrinol , vol.11 , pp. 550-562
    • Davis, D.P.1    Rozell, T.G.2    Liu, X.3
  • 285
    • 0029094166 scopus 로고
    • Functional glycosylation sites of the rat luteinizing hormone receptor required for ligand binding
    • Zhang R., Cai H., Fatima N., et al. Functional glycosylation sites of the rat luteinizing hormone receptor required for ligand binding. J Biol Chem 1995, 270:21722-21728.
    • (1995) J Biol Chem , vol.270 , pp. 21722-21728
    • Zhang, R.1    Cai, H.2    Fatima, N.3
  • 286
    • 0028883286 scopus 로고
    • Identification of the sites of N-linked glycosylation on the follicle-stimulating hormone (FSH) receptor and assesment of their role in FSH receptor function
    • Davis D., Liu X., Segaloff D.L. Identification of the sites of N-linked glycosylation on the follicle-stimulating hormone (FSH) receptor and assesment of their role in FSH receptor function. Mol Endocrinol 1995, 9:159-170.
    • (1995) Mol Endocrinol , vol.9 , pp. 159-170
    • Davis, D.1    Liu, X.2    Segaloff, D.L.3
  • 287
    • 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
  • 288
    • 0030059066 scopus 로고    scopus 로고
    • Anti-human FSH receptor monoclonal antibodies: immunochemical and immunocytochemical characterization of the receptor
    • Vannier B., Loosfelt H., Meduri G., et al. Anti-human FSH receptor monoclonal antibodies: immunochemical and immunocytochemical characterization of the receptor. Biochemistry 1996, 35:1358-1366.
    • (1996) Biochemistry , vol.35 , pp. 1358-1366
    • Vannier, B.1    Loosfelt, H.2    Meduri, G.3
  • 289
    • 0027524728 scopus 로고
    • A polyclonal antibody to a synthetic peptide derived from the rat FSH receptor reveals the recombinant receptor as a 74 kda protein
    • Quintana J., Hipkin R.W., Ascoli M. A polyclonal antibody to a synthetic peptide derived from the rat FSH receptor reveals the recombinant receptor as a 74 kda protein. Endocrinology 1993, 133:2098-2104.
    • (1993) Endocrinology , vol.133 , pp. 2098-2104
    • Quintana, J.1    Hipkin, R.W.2    Ascoli, M.3
  • 290
    • 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., et al. 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
  • 291
    • 0000518608 scopus 로고
    • Deglycosylation of the human luteinizing hormone receptor does not affect ligand binding and signal transduction
    • Tapanainen J.S., Bo M., Dunkel L., et al. Deglycosylation of the human luteinizing hormone receptor does not affect ligand binding and signal transduction. Endocrine 1993, 1:219-225.
    • (1993) Endocrine , vol.1 , pp. 219-225
    • Tapanainen, J.S.1    Bo, M.2    Dunkel, L.3
  • 292
    • 0032512441 scopus 로고    scopus 로고
    • Transfected cells express mostly the intracellular precursor of the lutropin/choriogonadotropin receptor but this precursor binds choriogonadotropin with high affinity
    • Fabritz J., Ryan S., Ascoli M. Transfected cells express mostly the intracellular precursor of the lutropin/choriogonadotropin receptor but this precursor binds choriogonadotropin with high affinity. Biochemistry 1998, 37:664-672.
    • (1998) Biochemistry , vol.37 , pp. 664-672
    • Fabritz, J.1    Ryan, S.2    Ascoli, M.3
  • 293
    • 0030043737 scopus 로고    scopus 로고
    • Deletions of portions of the extracellular loops of the lutropin/choriogonadotropin receptor decrease the binding affinity for ovine luteinizing hormone, but not for human choriogonadotropin, by preventing the formation of mature cell surface receptor
    • Abell A., Liu X., Segaloff D.L. Deletions of portions of the extracellular loops of the lutropin/choriogonadotropin receptor decrease the binding affinity for ovine luteinizing hormone, but not for human choriogonadotropin, by preventing the formation of mature cell surface receptor. J Biol Chem 1996, 271:4518-4527.
    • (1996) J Biol Chem , vol.271 , pp. 4518-4527
    • Abell, A.1    Liu, X.2    Segaloff, D.L.3
  • 294
    • 0028842897 scopus 로고
    • Intracellular retention of mutant gonadotropin receptors results in loss of hormone binding activity of the follitropin receptor but not the lutropin/choriogonadotropin receptor
    • Rozell T.G., Wang H., Liu X., et al. Intracellular retention of mutant gonadotropin receptors results in loss of hormone binding activity of the follitropin receptor but not the lutropin/choriogonadotropin receptor. Mol Endocrinol 1995, 9:1727-1736.
    • (1995) Mol Endocrinol , vol.9 , pp. 1727-1736
    • Rozell, T.G.1    Wang, H.2    Liu, X.3
  • 295
    • 0025096001 scopus 로고
    • Monoclonal antibodies against luteinizing hormone receptor: immunochemical characterization of the receptor
    • Vu Hai-Luu Thi M.T., Jolivet A., Jallal B., et al. Monoclonal antibodies against luteinizing hormone receptor: immunochemical characterization of the receptor. Endocrinology 1990, 127:2090-2098.
    • (1990) Endocrinology , vol.127 , pp. 2090-2098
    • Vu Hai-Luu Thi, M.T.1    Jolivet, A.2    Jallal, B.3
  • 296
    • 0026756979 scopus 로고
    • Variant forms of the pig lutropin/choriogonadotropin receptor
    • Vu Hai-Luu Thi M.T., Misrahi M., Houillier A., et al. Variant forms of the pig lutropin/choriogonadotropin receptor. Biochemistry 1992, 31:8377-8383.
    • (1992) Biochemistry , vol.31 , pp. 8377-8383
    • Vu Hai-Luu Thi, M.T.1    Misrahi, M.2    Houillier, A.3
  • 297
    • 0027093726 scopus 로고
    • Identification and characterization of a luteinizing hormone/chorionic gonadotropin (LH/CG) receptor precursor in a human kidney cell line stably transfected with the rat luteal LH/CG receptor complementary DNA
    • Hipkin R.W., Sánchez-Yagüe J., Ascoli M. Identification and characterization of a luteinizing hormone/chorionic gonadotropin (LH/CG) receptor precursor in a human kidney cell line stably transfected with the rat luteal LH/CG receptor complementary DNA. Mol Endocrinol 1992, 6:2210-2218.
    • (1992) Mol Endocrinol , vol.6 , pp. 2210-2218
    • Hipkin, R.W.1    Sánchez-Yagüe, J.2    Ascoli, M.3
  • 298
    • 0345826101 scopus 로고    scopus 로고
    • Identification and structural characterization of the neuronal luteinizing hormone receptor associated with sensory systems
    • Apaja P.M., Harju K.T., Aatsinki J.T., et al. Identification and structural characterization of the neuronal luteinizing hormone receptor associated with sensory systems. J Biol Chem 2004, 279:1899-1906.
    • (2004) J Biol Chem , vol.279 , pp. 1899-1906
    • Apaja, P.M.1    Harju, K.T.2    Aatsinki, J.T.3
  • 299
    • 1542316313 scopus 로고    scopus 로고
    • A molecular dissection of the glycoprotein hormone receptors
    • Vassart G., Pardo L., Costagliola S. A molecular dissection of the glycoprotein hormone receptors. Trends Biochem Sci 2004, 29:119-126.
    • (2004) Trends Biochem Sci , vol.29 , pp. 119-126
    • Vassart, G.1    Pardo, L.2    Costagliola, S.3
  • 300
    • 24944502148 scopus 로고    scopus 로고
    • Specificity and promiscuity of gonadotropin receptors
    • Costagliola S., Urizar E., Mendive F., et al. Specificity and promiscuity of gonadotropin receptors. Reproduction 2005, 130:275-281.
    • (2005) Reproduction , vol.130 , pp. 275-281
    • Costagliola, S.1    Urizar, E.2    Mendive, F.3
  • 301
    • 0042836864 scopus 로고    scopus 로고
    • New insights into the evolution of the relaxin-lgr signaling system
    • Hsu S.Y.T. New insights into the evolution of the relaxin-lgr signaling system. Trends Endocrinol Metab 2003, 14:303-309.
    • (2003) Trends Endocrinol Metab , vol.14 , pp. 303-309
    • Hsu, S.Y.T.1
  • 303
    • 33644589069 scopus 로고    scopus 로고
    • International union of pharmacology: LVII. Recommendations for the nomenclature of receptors for relaxin family peptides
    • Bathgate R.A., Ivell R., Sanborn B.M., et al. International union of pharmacology: LVII. Recommendations for the nomenclature of receptors for relaxin family peptides. Pharmacol Rev 2006, 58:7-31.
    • (2006) Pharmacol Rev , vol.58 , pp. 7-31
    • Bathgate, R.A.1    Ivell, R.2    Sanborn, B.M.3
  • 304
    • 49549116724 scopus 로고    scopus 로고
    • The luteinizing hormone receptor
    • Humana Press, Totowa, NJ, A.H. Payne, M.P. Hardy (Eds.)
    • Dufau M.L., Tsai-Morris C.H. The luteinizing hormone receptor. The Leydig Cell in Health and Disease 2007, 227-252. Humana Press, Totowa, NJ. A.H. Payne, M.P. Hardy (Eds.).
    • (2007) The Leydig Cell in Health and Disease , pp. 227-252
    • Dufau, M.L.1    Tsai-Morris, C.H.2
  • 305
    • 33751226609 scopus 로고    scopus 로고
    • Transcriptional regulation of the FSH receptor: new perspectives
    • Herman B.P., Heckert L.L. Transcriptional regulation of the FSH receptor: new perspectives. Mol Cell Endocrinol 2007, 260-262:100-108.
    • (2007) Mol Cell Endocrinol , vol.260-262 , pp. 100-108
    • Herman, B.P.1    Heckert, L.L.2
  • 306
    • 0033600880 scopus 로고    scopus 로고
    • The human luteinizing hormone receptor gene promoter: activation by sp1 and sp3 and inhibitory regulation
    • Geng Y., Tsai-Morris C.H., Zhang Y., et al. The human luteinizing hormone receptor gene promoter: activation by sp1 and sp3 and inhibitory regulation. Biochem Biophys Res Commun 1999, 263:366-371.
    • (1999) Biochem Biophys Res Commun , vol.263 , pp. 366-371
    • Geng, Y.1    Tsai-Morris, C.H.2    Zhang, Y.3
  • 307
    • 0034723283 scopus 로고    scopus 로고
    • Nuclear orphan receptors regulate transcription of the gene for the human luteinizing hormone receptor
    • Zhang Y., Dufau M.L. Nuclear orphan receptors regulate transcription of the gene for the human luteinizing hormone receptor. J Biol Chem 2000, 275:2763-2770.
    • (2000) J Biol Chem , vol.275 , pp. 2763-2770
    • Zhang, Y.1    Dufau, M.L.2
  • 308
    • 0034750680 scopus 로고    scopus 로고
    • EAR2 and EAR3/COUP-TF1 regulate transcription of the rat LH receptor
    • Zhang Y., Dufau M. EAR2 and EAR3/COUP-TF1 regulate transcription of the rat LH receptor. Mol Endocrinol 2001, 15:1891-1905.
    • (2001) Mol Endocrinol , vol.15 , pp. 1891-1905
    • Zhang, Y.1    Dufau, M.2
  • 309
    • 17844395674 scopus 로고    scopus 로고
    • An upstream initiator-like element suppresses transcription of the rat luteinizing hormone receptor gene
    • Youn H., Koo Y., Ji I., et al. An upstream initiator-like element suppresses transcription of the rat luteinizing hormone receptor gene. Mol Endocrinol 2005, 19:1318-1328.
    • (2005) Mol Endocrinol , vol.19 , pp. 1318-1328
    • Youn, H.1    Koo, Y.2    Ji, I.3
  • 310
    • 5044226671 scopus 로고    scopus 로고
    • Adrenocortical tumorigenesis in transgenic mice expressing the inhibin α-subunit promoter/simian virus 40 t-antigen transgene: relationship between ectopic expression of luteinizing hormone receptor and transcription factor gata-4
    • Rahman N.A., Kiiveri S., Rivero-Muller A., et al. Adrenocortical tumorigenesis in transgenic mice expressing the inhibin α-subunit promoter/simian virus 40 t-antigen transgene: relationship between ectopic expression of luteinizing hormone receptor and transcription factor gata-4. Mol Endocrinol 2004, 18:2553-2569.
    • (2004) Mol Endocrinol , vol.18 , pp. 2553-2569
    • Rahman, N.A.1    Kiiveri, S.2    Rivero-Muller, A.3
  • 311
    • 0034997311 scopus 로고    scopus 로고
    • '-flanking region in transfected gonadal cells and in transgenic mice
    • '-flanking region in transfected gonadal cells and in transgenic mice. Endocrinology 2001, 142:2427-2434.
    • (2001) Endocrinology , vol.142 , pp. 2427-2434
    • Hamalainen, T.1    Poutanen, M.2    Huhtaniemi, I.3
  • 312
    • 23044484256 scopus 로고    scopus 로고
    • Expression of the mature luteinizing hormone receptor in rodent urogenital and adrenal tissues is developmentally regulated at a posttranslational level
    • Apaja P.M., Aatsinki J.T., Rajaniemi H.J., et al. Expression of the mature luteinizing hormone receptor in rodent urogenital and adrenal tissues is developmentally regulated at a posttranslational level. Endocrinology 2005, 146:3224-3232.
    • (2005) Endocrinology , vol.146 , pp. 3224-3232
    • Apaja, P.M.1    Aatsinki, J.T.2    Rajaniemi, H.J.3
  • 313
    • 0027949728 scopus 로고
    • Follicle-stimulating hormone receptor gene promoter activity
    • Linder C.C., Heckert L.L., Goetz T.L., et al. Follicle-stimulating hormone receptor gene promoter activity. Endocrine 1994, 2:957-966.
    • (1994) Endocrine , vol.2 , pp. 957-966
    • Linder, C.C.1    Heckert, L.L.2    Goetz, T.L.3
  • 314
    • 0035143154 scopus 로고    scopus 로고
    • Kim J-S. Site-specific methylation of the promoter alters deoxyribonucleic acid-protein interactions and prevents follicle-stimulating hormone receptor gene transcription
    • Griswold M.D. Kim J-S. Site-specific methylation of the promoter alters deoxyribonucleic acid-protein interactions and prevents follicle-stimulating hormone receptor gene transcription. Biol Reprod 2001, 64:602-610.
    • (2001) Biol Reprod , vol.64 , pp. 602-610
    • Griswold, M.D.1
  • 315
    • 0036377906 scopus 로고    scopus 로고
    • The expression of the follicle-stimulating hormone receptor in spermatogenesis
    • Heckert L.L., Griswold M.D. The expression of the follicle-stimulating hormone receptor in spermatogenesis. Recent Prog Horm Res 2002, 57:129-148.
    • (2002) Recent Prog Horm Res , vol.57 , pp. 129-148
    • Heckert, L.L.1    Griswold, M.D.2
  • 316
    • 0035145723 scopus 로고    scopus 로고
    • Characterization of regulatory elements of ovine follicle-stimulating hormone (FSH) receptor gene: the role of e-box in the regulation of ovine FSH receptor expression
    • Xing W., Ram Sairam M. Characterization of regulatory elements of ovine follicle-stimulating hormone (FSH) receptor gene: the role of e-box in the regulation of ovine FSH receptor expression. Biol Reprod 2001, 64:579-589.
    • (2001) Biol Reprod , vol.64 , pp. 579-589
    • Xing, W.1    Ram Sairam, M.2
  • 317
    • 0035021909 scopus 로고    scopus 로고
    • Activation of the rat follicle-stimulating hormone receptor promoter by steroidogenic factor 1 is blocked by protein kinase a and requires upstream stimulatory factor binding to a proximal e box element
    • Heckert L.L. Activation of the rat follicle-stimulating hormone receptor promoter by steroidogenic factor 1 is blocked by protein kinase a and requires upstream stimulatory factor binding to a proximal e box element. Mol Endocrinol 2001, 15:704-715.
    • (2001) Mol Endocrinol , vol.15 , pp. 704-715
    • Heckert, L.L.1
  • 318
    • 0032230277 scopus 로고    scopus 로고
    • Multiple promoter elements contribute to activity of the follicle-stimulating hormone receptor (FSHR) gene in testicular Sertoli cells
    • Heckert L.L., Daggett M.A.F., Chen J. Multiple promoter elements contribute to activity of the follicle-stimulating hormone receptor (FSHR) gene in testicular Sertoli cells. Mol Endocrinol 1998, 12:1499-1512.
    • (1998) Mol Endocrinol , vol.12 , pp. 1499-1512
    • Heckert, L.L.1    Daggett, M.A.F.2    Chen, J.3
  • 319
    • 0026530252 scopus 로고
    • Structural organization of the follicle-stimulating hormone receptor gene
    • Heckert L.L., Daley I.J., Griswold M.D. Structural organization of the follicle-stimulating hormone receptor gene. Mol Endocrinol 1992, 6:70-80.
    • (1992) Mol Endocrinol , vol.6 , pp. 70-80
    • Heckert, L.L.1    Daley, I.J.2    Griswold, M.D.3
  • 321
    • 0025915915 scopus 로고
    • Expression of follicle-stimulating hormone receptor mrna in rat testes and Sertoli cells
    • Heckert L.L., Griswold M.D. Expression of follicle-stimulating hormone receptor mrna in rat testes and Sertoli cells. Mol Endocrinol 1991, 5:670-677.
    • (1991) Mol Endocrinol , vol.5 , pp. 670-677
    • Heckert, L.L.1    Griswold, M.D.2
  • 322
    • 0027220106 scopus 로고
    • Cloning of alternately spliced mrna transcripts coding for variants of ovine testicular follitropin receptor lacking the G protein coupling domains
    • Khan H., Yarney T.A., Sairam M.R. Cloning of alternately spliced mrna transcripts coding for variants of ovine testicular follitropin receptor lacking the G protein coupling domains. Biochem Biophys Res Commun 1993, 190:888-894.
    • (1993) Biochem Biophys Res Commun , vol.190 , pp. 888-894
    • Khan, H.1    Yarney, T.A.2    Sairam, M.R.3
  • 323
    • 33751252829 scopus 로고    scopus 로고
    • The tale of follitropin receptor diversity: a recipe for fine tuning gonadotropin responses?
    • Sairam M.R., Babu P.S. The tale of follitropin receptor diversity: a recipe for fine tuning gonadotropin responses?. Mol Cell Endocrinol 2007, 260-262:163-171.
    • (2007) Mol Cell Endocrinol , vol.260-262 , pp. 163-171
    • Sairam, M.R.1    Babu, P.S.2
  • 324
    • 0033361906 scopus 로고    scopus 로고
    • Naturally occurring mutations of the luteinizing-hormone receptor: lessons learned about reproductive physiology and G protein-coupled receptors
    • Latronico A.C., Segaloff D.L. Naturally occurring mutations of the luteinizing-hormone receptor: lessons learned about reproductive physiology and G protein-coupled receptors. Am J Hum Genet 1999, 65:949-958.
    • (1999) Am J Hum Genet , vol.65 , pp. 949-958
    • Latronico, A.C.1    Segaloff, D.L.2
  • 325
    • 0033711033 scopus 로고    scopus 로고
    • Mutations of gonadotropins and gonadotropin receptors: elucidating the physiology and pathophysiology of pituitary-gonadal function
    • Themmen A.P.N., Huhtaniemi I.T. Mutations of gonadotropins and gonadotropin receptors: elucidating the physiology and pathophysiology of pituitary-gonadal function. Endocr Rev 2000, 21:551-583.
    • (2000) Endocr Rev , vol.21 , pp. 551-583
    • Themmen, A.P.N.1    Huhtaniemi, I.T.2
  • 326
    • 33751234526 scopus 로고    scopus 로고
    • LH receptor gene mutations and polymorphisms: an overview
    • Piersma D., Verhoef-Post M., Berns E.M.J.J., et al. LH receptor gene mutations and polymorphisms: an overview. Mol Cell Endocrinol 2007, 260-262:282-286.
    • (2007) Mol Cell Endocrinol , vol.260-262 , pp. 282-286
    • Piersma, D.1    Verhoef-Post, M.2    Berns, E.M.J.J.3
  • 327
    • 0034456625 scopus 로고    scopus 로고
    • Male hypogonadism caused by homozygous deletion of exon 10 of the luteinizing hormone (LH) receptor: differential action of human chorionic gonadotropin and LH
    • Gromoll J., Eiholzer U., Nieschlag E., et al. Male hypogonadism caused by homozygous deletion of exon 10 of the luteinizing hormone (LH) receptor: differential action of human chorionic gonadotropin and LH. J Clin Endocrinol Metab 2000, 85:2281-2286.
    • (2000) J Clin Endocrinol Metab , vol.85 , pp. 2281-2286
    • Gromoll, J.1    Eiholzer, U.2    Nieschlag, E.3
  • 328
    • 0038368875 scopus 로고    scopus 로고
    • Absence of exon 10 of the human luteinizing hormone (LH) receptor impairs LH, but not human chorionic gonadotropin action
    • Muller T., Gromoll J., Simoni M. Absence of exon 10 of the human luteinizing hormone (LH) receptor impairs LH, but not human chorionic gonadotropin action. J Clin Endocrinol Metab 2003, 88:2242-2249.
    • (2003) J Clin Endocrinol Metab , vol.88 , pp. 2242-2249
    • Muller, T.1    Gromoll, J.2    Simoni, M.3
  • 329
    • 1542330973 scopus 로고    scopus 로고
    • Chorionic gonadotrophin beta subunit mrna but not luteinising hormone beta subunit mrna is expressed in the pituitary of the common marmoset (
    • Muller T., Simoni M., Pekel E., et al. Chorionic gonadotrophin beta subunit mrna but not luteinising hormone beta subunit mrna is expressed in the pituitary of the common marmoset (. Callithrix jacchus). J Mol Endocrinol 2004, 32:115-128.
    • (2004) Callithrix jacchus). J Mol Endocrinol , vol.32 , pp. 115-128
    • Muller, T.1    Simoni, M.2    Pekel, E.3
  • 330
    • 0030912607 scopus 로고    scopus 로고
    • Cloning and functional expression of the luteinizing hormone receptor complementary deoxyribonucleic acid from the marmoset monkey testis: absence of sequences encoding exon 10 in other species
    • Zhang F.-P., Rannikko A.S., Manna P.R., et al. Cloning and functional expression of the luteinizing hormone receptor complementary deoxyribonucleic acid from the marmoset monkey testis: absence of sequences encoding exon 10 in other species. Endocrinology 1997, 138:2481-2490.
    • (1997) Endocrinology , vol.138 , pp. 2481-2490
    • Zhang, F.-P.1    Rannikko, A.S.2    Manna, P.R.3
  • 331
    • 34547411000 scopus 로고    scopus 로고
    • Genomic checkpoints for exon 10 usage in the luteinizing hormone receptor type 1 and type 2
    • Gromoll J., Lahrmann L., Godmann M., et al. Genomic checkpoints for exon 10 usage in the luteinizing hormone receptor type 1 and type 2. Mol Endocrinol 2007, 21:1984-1996.
    • (2007) Mol Endocrinol , vol.21 , pp. 1984-1996
    • Gromoll, J.1    Lahrmann, L.2    Godmann, M.3
  • 332
    • 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., et al. 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
  • 333
    • 0035793543 scopus 로고    scopus 로고
    • The role of the hinge region of the luteinizing hormone receptor in hormone interaction and signal generation
    • Zeng H., Phang T., Song Y.S., et al. The role of the hinge region of the luteinizing hormone receptor in hormone interaction and signal generation. J Biol Chem 2001, 276:3451-3458.
    • (2001) J Biol Chem , vol.276 , pp. 3451-3458
    • Zeng, H.1    Phang, T.2    Song, Y.S.3
  • 334
    • 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., et al. 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
  • 335
    • 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., et al. 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, 100:1634-1649.
    • (1997) J Clin Invest , vol.100 , pp. 1634-1649
    • Kopp, P.1    Muirhead, S.2    Jourdain, N.3
  • 336
    • 0031772403 scopus 로고    scopus 로고
    • Severe congenital hyperthyroidism caused by a germ-line neo mutation in the extracellular portion of the thyrotropin receptor
    • Gruters A., Schoneberg T., Biebermann H., et al. Severe congenital hyperthyroidism caused by a germ-line neo mutation in the extracellular portion of the thyrotropin receptor. J Clin Endocrinol Metab 1998, 83:1431-1436.
    • (1998) J Clin Endocrinol Metab , vol.83 , pp. 1431-1436
    • Gruters, A.1    Schoneberg, T.2    Biebermann, H.3
  • 337
    • 0033518280 scopus 로고    scopus 로고
    • Leydig-cell tumors caused by an activating mutation of the gene encoding the luteinizing hormone receptor
    • Liu G., Duranteau L., Carel J.-C., et al. Leydig-cell tumors caused by an activating mutation of the gene encoding the luteinizing hormone receptor. N Engl J Med 1999, 341:1731-1736.
    • (1999) N Engl J Med , vol.341 , pp. 1731-1736
    • Liu, G.1    Duranteau, L.2    Carel, J.-C.3
  • 338
    • 0036962992 scopus 로고    scopus 로고
    • Male LH-independent sexual precocity in a 3.5-year-old boy caused by a somatic activating mutation of the LH receptor in a Leydig cell tumor
    • Richter-Unruh A., Wessels H.T., Menken U., et al. Male LH-independent sexual precocity in a 3.5-year-old boy caused by a somatic activating mutation of the LH receptor in a Leydig cell tumor. J Clin Endocrinol Metab 2002, 87:1052-1056.
    • (2002) J Clin Endocrinol Metab , vol.87 , pp. 1052-1056
    • Richter-Unruh, A.1    Wessels, H.T.2    Menken, U.3
  • 339
    • 0036498632 scopus 로고    scopus 로고
    • Mutational analysis of the luteinizing hormone receptor gene in two individuals with Leydig cell tumors
    • Canto P., Soderlund D., Ramon G., et al. Mutational analysis of the luteinizing hormone receptor gene in two individuals with Leydig cell tumors. Am J Med Genet 2002, 108:148-152.
    • (2002) Am J Med Genet , vol.108 , pp. 148-152
    • Canto, P.1    Soderlund, D.2    Ramon, G.3
  • 340
    • 0036964948 scopus 로고    scopus 로고
    • A novel mutation in the FSH receptor inhibiting signal transduction and causing primary ovarian failure
    • Doherty E., Pakarinen P., Tiitinen A., et al. A novel mutation in the FSH receptor inhibiting signal transduction and causing primary ovarian failure. J Clin Endocrinol Metab 2002, 87:1151-1155.
    • (2002) J Clin Endocrinol Metab , vol.87 , pp. 1151-1155
    • Doherty, E.1    Pakarinen, P.2    Tiitinen, A.3
  • 341
    • 0029913238 scopus 로고    scopus 로고
    • An activating mutation of the follicle-stimulating hormone receptor autonomously sustains spermatogenesis in hypophysectomized man
    • Gromoll J., Simoni M., Nieschlag E. An activating mutation of the follicle-stimulating hormone receptor autonomously sustains spermatogenesis in hypophysectomized man. J Clin Endocrinol Metab 1996, 81:1367-1370.
    • (1996) J Clin Endocrinol Metab , vol.81 , pp. 1367-1370
    • Gromoll, J.1    Simoni, M.2    Nieschlag, E.3
  • 342
    • 0041464853 scopus 로고    scopus 로고
    • Ovarian hyperstimulation syndrome due to a mutation in the follicle stimulating hormone receptor
    • Smits G., Latunbosun O., Delbaere A., et al. Ovarian hyperstimulation syndrome due to a mutation in the follicle stimulating hormone receptor. N Engl J Med 2003, 349:760-766.
    • (2003) N Engl J Med , vol.349 , pp. 760-766
    • Smits, G.1    Latunbosun, O.2    Delbaere, A.3
  • 343
    • 1642294189 scopus 로고    scopus 로고
    • A mutation in the follicle-stimulating hormone receptor as a cause of familial spontaneous ovarian hyperstimulation syndrome
    • Montanelli L., Delbaere A., Di Carlo C., et al. A mutation in the follicle-stimulating hormone receptor as a cause of familial spontaneous ovarian hyperstimulation syndrome. J Clin Endocrinol Metab 2004, 89:1255-1258.
    • (2004) J Clin Endocrinol Metab , vol.89 , pp. 1255-1258
    • Montanelli, L.1    Delbaere, A.2    Di Carlo, C.3
  • 344
    • 3442886235 scopus 로고    scopus 로고
    • Modulation of ligand selectivity associated with activation of the transmembrane region of the human follitropin receptor
    • Montanelli L., Van Durme J.J.J., Smits G., et al. Modulation of ligand selectivity associated with activation of the transmembrane region of the human follitropin receptor. Mol Endocrinol 2004, 18:2061-2073.
    • (2004) Mol Endocrinol , vol.18 , pp. 2061-2073
    • Montanelli, L.1    Van Durme, J.J.J.2    Smits, G.3
  • 345
    • 0032542355 scopus 로고    scopus 로고
    • Familial gestational hyperthyroidism caused by a mutant thyrotropin receptor hypersensitive to human chorionic gonadotropin
    • Rodien P., Bremont C., Sanson M.L., et al. Familial gestational hyperthyroidism caused by a mutant thyrotropin receptor hypersensitive to human chorionic gonadotropin. N Engl J Med 1998, 339:1823-1826.
    • (1998) N Engl J Med , vol.339 , pp. 1823-1826
    • Rodien, P.1    Bremont, C.2    Sanson, M.L.3
  • 346
    • 0032452362 scopus 로고    scopus 로고
    • Evidences for an allelic variant of the human lc/CG receptor rather than a gene duplication: functional comparison of wild-type and variant receptors
    • Rodien P., Cetani F., Costagliola S., et al. Evidences for an allelic variant of the human lc/CG receptor rather than a gene duplication: functional comparison of wild-type and variant receptors. J Clin Endocrinol Metab 1998, 83:4431-4434.
    • (1998) J Clin Endocrinol Metab , vol.83 , pp. 4431-4434
    • Rodien, P.1    Cetani, F.2    Costagliola, S.3
  • 349
    • 33646054591 scopus 로고    scopus 로고
    • A common polymorphism renders the luteinizing hormone receptor protein more active by improving signal peptide function and predicts adverse outcome in breast cancer patients
    • Piersma D., Berns E.M.J.J., Verhoef-Post M., et al. A common polymorphism renders the luteinizing hormone receptor protein more active by improving signal peptide function and predicts adverse outcome in breast cancer patients. J Clin Endocrinol Metab 2006, 91:1470-1476.
    • (2006) J Clin Endocrinol Metab , vol.91 , pp. 1470-1476
    • Piersma, D.1    Berns, E.M.J.J.2    Verhoef-Post, M.3
  • 350
    • 34548246470 scopus 로고    scopus 로고
    • Polymorphic variations in exon 10 of the luteinizing hormone receptor: functional consequences and associations with breast cancer
    • Piersma D., Verhoef-Post M., Look M.P., et al. Polymorphic variations in exon 10 of the luteinizing hormone receptor: functional consequences and associations with breast cancer. Mol Cell Endocrinol 2007, 276:63-70.
    • (2007) Mol Cell Endocrinol , vol.276 , pp. 63-70
    • Piersma, D.1    Verhoef-Post, M.2    Look, M.P.3
  • 351
    • 0030220018 scopus 로고    scopus 로고
    • Heterogeneity of activating mutations of the human luteinizing hormone receptor in male-limited precocious puberty
    • Laue L., Wu S.M., Kudo M., et al. Heterogeneity of activating mutations of the human luteinizing hormone receptor in male-limited precocious puberty. Biochem Mol Med 1996, 58:192-198.
    • (1996) Biochem Mol Med , vol.58 , pp. 192-198
    • Laue, L.1    Wu, S.M.2    Kudo, M.3
  • 352
    • 34547684660 scopus 로고    scopus 로고
    • Polymorphism of the FSH receptor and ovarian response to FSH
    • Wunsch A., Sonntag B., Simoni M. Polymorphism of the FSH receptor and ovarian response to FSH. Ann Endocrinol (Paris) 2007, 68:160-166.
    • (2007) Ann Endocrinol (Paris) , vol.68 , pp. 160-166
    • Wunsch, A.1    Sonntag, B.2    Simoni, M.3
  • 353
    • 33745618981 scopus 로고    scopus 로고
    • Single nucleotide polymorphisms of follicle-stimulating hormone receptor are associated with ovarian cancer susceptibility
    • Yang C.Q., Chan K.Y.K., Ngan H.Y.S., et al. Single nucleotide polymorphisms of follicle-stimulating hormone receptor are associated with ovarian cancer susceptibility. Carcinogenesis 2006, 27:1502-1506.
    • (2006) Carcinogenesis , vol.27 , pp. 1502-1506
    • Yang, C.Q.1    Chan, K.Y.K.2    Ngan, H.Y.S.3
  • 354
    • 0033018934 scopus 로고    scopus 로고
    • Mutational analysis of the follicle-stimulating hormone (FSH) receptor in normal men: identification and characterization of two discrete FSH receptor isoforms
    • Simoni M., Gromoll J., Höppner W., et al. Mutational analysis of the follicle-stimulating hormone (FSH) receptor in normal men: identification and characterization of two discrete FSH receptor isoforms. J Clin Endocrinol Metab 1999, 84:751-755.
    • (1999) J Clin Endocrinol Metab , vol.84 , pp. 751-755
    • Simoni, M.1    Gromoll, J.2    Höppner, W.3
  • 355
    • 0036796339 scopus 로고    scopus 로고
    • Genetic and functional analyses of polymorphisms in the human FSH receptor gene
    • Sudo S., Kudo M., Wada S., et al. Genetic and functional analyses of polymorphisms in the human FSH receptor gene. Mol Hum Reprod 2002, 8:893-899.
    • (2002) Mol Hum Reprod , vol.8 , pp. 893-899
    • Sudo, S.1    Kudo, M.2    Wada, S.3
  • 356
    • 0025643101 scopus 로고
    • Hormonal regulation of luteinizing hormone/chorionic gonadotropin receptor mRNA in rat ovarian cells during follicular development and luteinization
    • Segaloff D.L., Wang H., Richards J.S. Hormonal regulation of luteinizing hormone/chorionic gonadotropin receptor mRNA in rat ovarian cells during follicular development and luteinization. Mol Endocrinol 1990, 4:1856-1865.
    • (1990) Mol Endocrinol , vol.4 , pp. 1856-1865
    • Segaloff, D.L.1    Wang, H.2    Richards, J.S.3
  • 357
    • 0029004635 scopus 로고
    • A role for increased lutropin/choriogonadotropin receptor (LHR) gene transcription in the follitropin-stimulated induction of the LHR in granulosa cells
    • Shi H., Segaloff D.L. A role for increased lutropin/choriogonadotropin receptor (LHR) gene transcription in the follitropin-stimulated induction of the LHR in granulosa cells. Mol Endocrinol 1995, 9:734-744.
    • (1995) Mol Endocrinol , vol.9 , pp. 734-744
    • Shi, H.1    Segaloff, D.L.2
  • 358
    • 0033313940 scopus 로고    scopus 로고
    • Multiple elements and protein factors coordinate the basal and cyclic adenosine 3',5'-monophosphate-induced transcription of the lutropin receptor gene in rat granulosa cells
    • Chen S., Shi H., Liu X., et al. Multiple elements and protein factors coordinate the basal and cyclic adenosine 3',5'-monophosphate-induced transcription of the lutropin receptor gene in rat granulosa cells. Endocrinology 1999, 140:2100-2109.
    • (1999) Endocrinology , vol.140 , pp. 2100-2109
    • Chen, S.1    Shi, H.2    Liu, X.3
  • 359
    • 0033744016 scopus 로고    scopus 로고
    • A novel cyclic adenosine 3',5'-monophosphate-responsive element involved in the transcriptional regulation of the lutropin receptor gene in granulosa cells
    • Chen S., Liu X., Segaloff D.L. A novel cyclic adenosine 3',5'-monophosphate-responsive element involved in the transcriptional regulation of the lutropin receptor gene in granulosa cells. Mol Endocrinol 2000, 14:1498-1508.
    • (2000) Mol Endocrinol , vol.14 , pp. 1498-1508
    • Chen, S.1    Liu, X.2    Segaloff, D.L.3
  • 360
    • 0036376131 scopus 로고    scopus 로고
    • Novel signaling pathways that control ovarian follicular development, ovulation, and luteinization
    • Richards J.S., Russell D.L., Ochsner S., et al. Novel signaling pathways that control ovarian follicular development, ovulation, and luteinization. Recent Prog Horm Res 2002, 57:195-220.
    • (2002) Recent Prog Horm Res , vol.57 , pp. 195-220
    • Richards, J.S.1    Russell, D.L.2    Ochsner, S.3
  • 361
    • 0028590162 scopus 로고
    • Hormonal control of gene expression in the ovary
    • Richards J.S. Hormonal control of gene expression in the ovary. Endocr Rev 1994, 15:725-751.
    • (1994) Endocr Rev , vol.15 , pp. 725-751
    • Richards, J.S.1
  • 362
    • 1642268837 scopus 로고    scopus 로고
    • Regulation of luteinizing hormone/human chorionic gonadotropin receptor expression: a perspective
    • Menon K.M.J., Munshi U.M., Clouser C.L., et al. Regulation of luteinizing hormone/human chorionic gonadotropin receptor expression: a perspective. Biol Reprod 2004, 70:861-866.
    • (2004) Biol Reprod , vol.70 , pp. 861-866
    • Menon, K.M.J.1    Munshi, U.M.2    Clouser, C.L.3
  • 363
    • 0027989335 scopus 로고
    • In situ hybridization of luteinizing hormone/human chorionic gonadotropin receptor messenger ribonucleic acid during hormone-induced down-regulation and the subsequent recovery in rat corpus luteum
    • Peegel H., Randolph J.J., Midgley R., et al. In situ hybridization of luteinizing hormone/human chorionic gonadotropin receptor messenger ribonucleic acid during hormone-induced down-regulation and the subsequent recovery in rat corpus luteum. Endocrinology 1994, 135:1044-1051.
    • (1994) Endocrinology , vol.135 , pp. 1044-1051
    • Peegel, H.1    Randolph, J.J.2    Midgley, R.3
  • 364
    • 0025285734 scopus 로고
    • Gonadotropin-induced up- and down-regulation of rat ovarian LH receptor message levels during follicular growth, ovulation and luteinization
    • LaPolt P.S., Oikawa M., Xiao-Chi J., et al. Gonadotropin-induced up- and down-regulation of rat ovarian LH receptor message levels during follicular growth, ovulation and luteinization. Endocrinology 1990, 126:3277-3279.
    • (1990) Endocrinology , vol.126 , pp. 3277-3279
    • LaPolt, P.S.1    Oikawa, M.2    Xiao-Chi, J.3
  • 365
    • 0027458991 scopus 로고
    • Loss of lutropin/human choriogonadotropin receptor messenger ribonucleic acid during ligand-induced down-regulation occurs post transcriptionally
    • Lu D.L., Peegel H., Mosier S.M., et al. Loss of lutropin/human choriogonadotropin receptor messenger ribonucleic acid during ligand-induced down-regulation occurs post transcriptionally. Endocrinology 1993, 132:235-240.
    • (1993) Endocrinology , vol.132 , pp. 235-240
    • Lu, D.L.1    Peegel, H.2    Mosier, S.M.3
  • 366
    • 17644373467 scopus 로고    scopus 로고
    • A novel mechanism for the modulation of luteinizing hormone receptor mRNA expression in the rat ovary
    • Peegel H., Towns R., Nair A., et al. A novel mechanism for the modulation of luteinizing hormone receptor mRNA expression in the rat ovary. Mol Cell Endocrinol 2005, 233:65-72.
    • (2005) Mol Cell Endocrinol , vol.233 , pp. 65-72
    • Peegel, H.1    Towns, R.2    Nair, A.3
  • 367
    • 0033592970 scopus 로고    scopus 로고
    • Sequence-specific binding of a hormonally regulated mRNA binding protein to cytidine-rich sequences in the lutropin receptor open reading frame
    • Kash J.C., Menon K.M. Sequence-specific binding of a hormonally regulated mRNA binding protein to cytidine-rich sequences in the lutropin receptor open reading frame. Biochemistry 1999, 38:16889-16897.
    • (1999) Biochemistry , vol.38 , pp. 16889-16897
    • Kash, J.C.1    Menon, K.M.2
  • 368
    • 0032562638 scopus 로고    scopus 로고
    • Identification of a hormonally regulated luteinizing hormone/human chorionic gonadotropin receptor mRNA binding protein: increased mRNA binding during receptor down-regulation
    • Kash J.C., Menon K.M. Identification of a hormonally regulated luteinizing hormone/human chorionic gonadotropin receptor mRNA binding protein: increased mRNA binding during receptor down-regulation. J Biol Chem 1998, 273:10658-10664.
    • (1998) J Biol Chem , vol.273 , pp. 10658-10664
    • Kash, J.C.1    Menon, K.M.2
  • 369
    • 30044444828 scopus 로고    scopus 로고
    • Regulation of luteinizing hormone receptor expression: evidence of translational suppression in vitro by a hormonally regulated mRNA-binding protein and its endogenous association with luteinizing hormone receptor mRNA in the ovary
    • Nair A.K., Menon K.M.J. Regulation of luteinizing hormone receptor expression: evidence of translational suppression in vitro by a hormonally regulated mRNA-binding protein and its endogenous association with luteinizing hormone receptor mRNA in the ovary. J Biol Chem 2005, 280:42809-42816.
    • (2005) J Biol Chem , vol.280 , pp. 42809-42816
    • Nair, A.K.1    Menon, K.M.J.2
  • 370
    • 2442450689 scopus 로고    scopus 로고
    • Isolation and characterization of a novel trans-factor for luteinizing hormone receptor mRNA from ovary
    • Nair A.K., Menon K.M.J. Isolation and characterization of a novel trans-factor for luteinizing hormone receptor mRNA from ovary. J Biol Chem 2004, 279:14937-14944.
    • (2004) J Biol Chem , vol.279 , pp. 14937-14944
    • Nair, A.K.1    Menon, K.M.J.2
  • 371
    • 0037077271 scopus 로고    scopus 로고
    • Post-transcriptional regulation of luteinizing hormone receptor mRNA in the ovary by a novel mRNA-binding protein
    • Nair A.K., Kash J.C., Peegel H., et al. Post-transcriptional regulation of luteinizing hormone receptor mRNA in the ovary by a novel mRNA-binding protein. J Biol Chem 2002, 277:21468-21473.
    • (2002) J Biol Chem , vol.277 , pp. 21468-21473
    • Nair, A.K.1    Kash, J.C.2    Peegel, H.3
  • 372
    • 33751324797 scopus 로고    scopus 로고
    • Regulation of luteinizing hormone receptor mRNA expression by a specific RNA binding protein in the ovary
    • Menon K.M.J., Nair A.K., Wang L., et al. Regulation of luteinizing hormone receptor mRNA expression by a specific RNA binding protein in the ovary. Mol Cell Endocrinol 2007, 260-262:109-116.
    • (2007) Mol Cell Endocrinol , vol.260-262 , pp. 109-116
    • Menon, K.M.J.1    Nair, A.K.2    Wang, L.3
  • 373
    • 0035133266 scopus 로고    scopus 로고
    • Normal prenatal but arrested postnatal sexual development of luteinizing hormone receptor knockout (LuRKO) mice
    • Zhang F.-P., Poutanen M., Wilbertz J., et al. Normal prenatal but arrested postnatal sexual development of luteinizing hormone receptor knockout (LuRKO) mice. Mol Endocrinol 2001, 15:172-183.
    • (2001) Mol Endocrinol , vol.15 , pp. 172-183
    • Zhang, F.-P.1    Poutanen, M.2    Wilbertz, J.3
  • 374
    • 0035136888 scopus 로고    scopus 로고
    • Targeted disruption of luteinizing hormone/human chorionic gonadotropin receptor gene
    • Lei Z.M., Mishra S., Zou W., et al. Targeted disruption of luteinizing hormone/human chorionic gonadotropin receptor gene. Mol Endocrinol 2001, 15:184-200.
    • (2001) Mol Endocrinol , vol.15 , pp. 184-200
    • Lei, Z.M.1    Mishra, S.2    Zou, W.3
  • 375
    • 22544435246 scopus 로고    scopus 로고
    • Inefficient maturation of the rat luteinizing hormone receptor: a putative way to regulate receptor numbers at the cell surface
    • Pietila E.M., Tuusa J.T., Apaja P.M., et al. Inefficient maturation of the rat luteinizing hormone receptor: a putative way to regulate receptor numbers at the cell surface. J Biol Chem 2005, 28:26622-26629.
    • (2005) J Biol Chem , vol.28 , pp. 26622-26629
    • Pietila, E.M.1    Tuusa, J.T.2    Apaja, P.M.3
  • 376
    • 33744923745 scopus 로고    scopus 로고
    • Luteinizing hormone receptor ectodomain splice variant misroutes the full-length receptor into a subcompartment of the endoplasmic reticulum
    • Apaja P.M., Tuusa J.T., Pietila E.M., et al. Luteinizing hormone receptor ectodomain splice variant misroutes the full-length receptor into a subcompartment of the endoplasmic reticulum. Mol Biol Cell 2006, 17:2243-2255.
    • (2006) Mol Biol Cell , vol.17 , pp. 2243-2255
    • Apaja, P.M.1    Tuusa, J.T.2    Pietila, E.M.3
  • 377
    • 2542496712 scopus 로고    scopus 로고
    • A splice variant of the human luteinizing hormone (LH) receptor modulates the expression of wild-type human LH receptor
    • Nakamura K., Yamashita S., Omori Y., et al. A splice variant of the human luteinizing hormone (LH) receptor modulates the expression of wild-type human LH receptor. Mol Endocrinol 2004, 18:1461-1470.
    • (2004) Mol Endocrinol , vol.18 , pp. 1461-1470
    • Nakamura, K.1    Yamashita, S.2    Omori, Y.3
  • 378
    • 23744480235 scopus 로고    scopus 로고
    • Association of human follitropin (FSH) receptor with splicing variant of human lutropin/choriogonadotropin receptor negatively controls the expression of human FSH receptor
    • Yamashita S., Nakamura K., Omori Y., et al. Association of human follitropin (FSH) receptor with splicing variant of human lutropin/choriogonadotropin receptor negatively controls the expression of human FSH receptor. Mol Endocrinol 2005, 19:2099-2111.
    • (2005) Mol Endocrinol , vol.19 , pp. 2099-2111
    • Yamashita, S.1    Nakamura, K.2    Omori, Y.3
  • 380
    • 0036839745 scopus 로고    scopus 로고
    • Dancing with different partners: protein kinase A phosphorylation of seven membrane-spanning receptors regulates their G protein-coupling specificity
    • Lefkowitz R.J., Pierce K.L., Luttrell L.M. Dancing with different partners: protein kinase A phosphorylation of seven membrane-spanning receptors regulates their G protein-coupling specificity. Mol Pharmacol 2002, 62:971-974.
    • (2002) Mol Pharmacol , vol.62 , pp. 971-974
    • Lefkowitz, R.J.1    Pierce, K.L.2    Luttrell, L.M.3
  • 382
    • 0028920668 scopus 로고
    • Protein kinases that phosphorylate activated G protein-coupled receptors
    • Premont R.T., Inglese J., Lefkowitz R.J. Protein kinases that phosphorylate activated G protein-coupled receptors. FASEB J 1995, 9:175-182.
    • (1995) FASEB J , vol.9 , pp. 175-182
    • Premont, R.T.1    Inglese, J.2    Lefkowitz, R.J.3
  • 383
    • 0027219322 scopus 로고
    • Agonist-induced phosphorylation of the luteinizing hormone/chorionic gonadotropin (LH/CG) receptor expressed in a stably transfected cell line
    • Hipkin R.W., Sánchez-Yagüe J., Ascoli M. Agonist-induced phosphorylation of the luteinizing hormone/chorionic gonadotropin (LH/CG) receptor expressed in a stably transfected cell line. Mol Endocrinol 1993, 7:823-832.
    • (1993) Mol Endocrinol , vol.7 , pp. 823-832
    • Hipkin, R.W.1    Sánchez-Yagüe, J.2    Ascoli, M.3
  • 384
    • 0033645593 scopus 로고    scopus 로고
    • Effect of activating and inactivating mutations on the phosphorylation and trafficking of the human lutropin/choriogonadotropin receptor
    • Min L., Ascoli M. Effect of activating and inactivating mutations on the phosphorylation and trafficking of the human lutropin/choriogonadotropin receptor. Mol Endocrinol 2000, 14:1797-1810.
    • (2000) Mol Endocrinol , vol.14 , pp. 1797-1810
    • Min, L.1    Ascoli, M.2
  • 385
    • 0031019920 scopus 로고    scopus 로고
    • Phosphorylation of the lutropin/choriogonadotropin receptor facilitates uncoupling of the receptor from adenylyl cyclase and endocytosis of the bound hormone
    • Wang Z., Liu X., Ascoli M. Phosphorylation of the lutropin/choriogonadotropin receptor facilitates uncoupling of the receptor from adenylyl cyclase and endocytosis of the bound hormone. Mol Endocrinol 1997, 11:183-192.
    • (1997) Mol Endocrinol , vol.11 , pp. 183-192
    • Wang, Z.1    Liu, X.2    Ascoli, M.3
  • 386
    • 0029889283 scopus 로고    scopus 로고
    • Progressive cytoplasmic tail truncations of the lutropin-choriogonadotropin receptor prevent agonist- or phorbol ester-induced phosphorylation, impair agonist- or phorbol ester-induced desensitization and enhance agonist-induced receptor down-regulation
    • Wang Z., Hipkin R.W., Ascoli M. Progressive cytoplasmic tail truncations of the lutropin-choriogonadotropin receptor prevent agonist- or phorbol ester-induced phosphorylation, impair agonist- or phorbol ester-induced desensitization and enhance agonist-induced receptor down-regulation. Mol Endocrinol 1996, 10:748-759.
    • (1996) Mol Endocrinol , vol.10 , pp. 748-759
    • Wang, Z.1    Hipkin, R.W.2    Ascoli, M.3
  • 387
    • 0033304637 scopus 로고    scopus 로고
    • Role of G protein-coupled receptor kinases on the agonist-induced phosphorylation, and internalization of the follitropin receptor
    • Lazari M.F.M., Liu X., Nakamura K., et al. Role of G protein-coupled receptor kinases on the agonist-induced phosphorylation, and internalization of the follitropin receptor. Mol Endocrinol 1999, 13:866-878.
    • (1999) Mol Endocrinol , vol.13 , pp. 866-878
    • Lazari, M.F.M.1    Liu, X.2    Nakamura, K.3
  • 388
    • 0032230332 scopus 로고    scopus 로고
    • The agonist-induced phosphorylation of the rat follitropin receptor (rFSHR) maps to the first and third intracellular loops
    • Nakamura K., Hipkin R.W., Ascoli M. The agonist-induced phosphorylation of the rat follitropin receptor (rFSHR) maps to the first and third intracellular loops. Mol Endocrinol 1998, 12:580-591.
    • (1998) Mol Endocrinol , vol.12 , pp. 580-591
    • Nakamura, K.1    Hipkin, R.W.2    Ascoli, M.3
  • 389
    • 0028785484 scopus 로고
    • Truncation of the c-terminal tail of the follitropin (FSH) receptor does not impair the agonist- or phorbol ester-induced receptor phosphorylation and uncoupling
    • Hipkin R.W., Liu X., Ascoli M. Truncation of the c-terminal tail of the follitropin (FSH) receptor does not impair the agonist- or phorbol ester-induced receptor phosphorylation and uncoupling. J Biol Chem 1995, 270:26683-26689.
    • (1995) J Biol Chem , vol.270 , pp. 26683-26689
    • Hipkin, R.W.1    Liu, X.2    Ascoli, M.3
  • 390
    • 0028245033 scopus 로고
    • Follitropin (FSH) and a phorbol ester stimulate the phosphorylation of the FSH receptor in intact cells
    • Quintana J., Hipkin R.W., Sánchez-Yagüe J., et al. Follitropin (FSH) and a phorbol ester stimulate the phosphorylation of the FSH receptor in intact cells. J Biol Chem 1994, 269:8772-8779.
    • (1994) J Biol Chem , vol.269 , pp. 8772-8779
    • Quintana, J.1    Hipkin, R.W.2    Sánchez-Yagüe, J.3
  • 391
    • 33751509646 scopus 로고    scopus 로고
    • A phosphorylation cluster of five serine and threonine residues in the c-terminus of the follicle-stimulating hormone receptor is important for desensitization but not for β-arrestin-mediated erk activation
    • Kara E., Crepieux P., Gauthier C., et al. A phosphorylation cluster of five serine and threonine residues in the c-terminus of the follicle-stimulating hormone receptor is important for desensitization but not for β-arrestin-mediated erk activation. Mol Endocrinol 2006, 20:3014-3026.
    • (2006) Mol Endocrinol , vol.20 , pp. 3014-3026
    • Kara, E.1    Crepieux, P.2    Gauthier, C.3
  • 392
    • 0028809315 scopus 로고
    • Human chorionic gonadotropin- and phorbol ester stimulated phosphorylation of the LH/CG receptor maps to serines 635, 639, 645 and 652 in the c-terminal cytoplasmic tail
    • Hipkin R.W., Wang Z., Ascoli M. Human chorionic gonadotropin- and phorbol ester stimulated phosphorylation of the LH/CG receptor maps to serines 635, 639, 645 and 652 in the c-terminal cytoplasmic tail. Mol Endocrinol 1995, 9:151-158.
    • (1995) Mol Endocrinol , vol.9 , pp. 151-158
    • Hipkin, R.W.1    Wang, Z.2    Ascoli, M.3
  • 393
    • 0032541044 scopus 로고    scopus 로고
    • Mutation of individual serine residues in the c-terminal tail of the lutropin/choriogonadotropin (LH/CG) receptor reveal distinct structural requirements for agonist-induced uncoupling and agonist-induced internalization
    • Lazari M.F.M., Bertrand J.E., Nakamura K., et al. Mutation of individual serine residues in the c-terminal tail of the lutropin/choriogonadotropin (LH/CG) receptor reveal distinct structural requirements for agonist-induced uncoupling and agonist-induced internalization. J Biol Chem 1998, 273:18316-18324.
    • (1998) J Biol Chem , vol.273 , pp. 18316-18324
    • Lazari, M.F.M.1    Bertrand, J.E.2    Nakamura, K.3
  • 394
    • 0033620487 scopus 로고    scopus 로고
    • Heptahelical receptor signaling: beyond the G protein paradigm
    • Hall R.A., Premont R.T., Lefkowitz R.J. Heptahelical receptor signaling: beyond the G protein paradigm. J Cell Biol 1999, 145:927-932.
    • (1999) J Cell Biol , vol.145 , pp. 927-932
    • Hall, R.A.1    Premont, R.T.2    Lefkowitz, R.J.3
  • 395
    • 0036499130 scopus 로고    scopus 로고
    • Arresting developments in heptahelical receptor signaling and regulation
    • Perry S.J., Lefkowitz R.J. Arresting developments in heptahelical receptor signaling and regulation. Trends Cell Biol 2002, 12:130-138.
    • (2002) Trends Cell Biol , vol.12 , pp. 130-138
    • Perry, S.J.1    Lefkowitz, R.J.2
  • 396
    • 0037016682 scopus 로고    scopus 로고
    • The association of arrestin-3 with the human lutropin/choriogonadotropin receptor depends mostly on receptor activation rather than on receptor phosphorylation
    • Min L., Galet C., Ascoli M. The association of arrestin-3 with the human lutropin/choriogonadotropin receptor depends mostly on receptor activation rather than on receptor phosphorylation. J Biol Chem 2002, 277:702-710.
    • (2002) J Biol Chem , vol.277 , pp. 702-710
    • Min, L.1    Galet, C.2    Ascoli, M.3
  • 397
    • 0345275892 scopus 로고    scopus 로고
    • Studies with chimeras of the gonadotropin receptors reveal the importance of third intracellular loop threonines on the formation of the receptor/non-visual arrestin complex
    • Bhaskaran R.S., Min L., Krishnamurthy H., et al. Studies with chimeras of the gonadotropin receptors reveal the importance of third intracellular loop threonines on the formation of the receptor/non-visual arrestin complex. Biochemistry 2003, 42:13950-13959.
    • (2003) Biochemistry , vol.42 , pp. 13950-13959
    • Bhaskaran, R.S.1    Min, L.2    Krishnamurthy, H.3
  • 398
    • 0035896538 scopus 로고    scopus 로고
    • Mutations of the second extracellular loop of the human lutropin receptor emphasize the importance of receptor activation and de-emphasize the importance of receptor phosphorylation in agonist-induced internalization
    • Li S., Liu X., Min L., et al. Mutations of the second extracellular loop of the human lutropin receptor emphasize the importance of receptor activation and de-emphasize the importance of receptor phosphorylation in agonist-induced internalization. J Biol Chem 2001, 276:7968-7973.
    • (2001) J Biol Chem , vol.276 , pp. 7968-7973
    • Li, S.1    Liu, X.2    Min, L.3
  • 399
    • 0034613334 scopus 로고    scopus 로고
    • Multiple distant amino acid residues present in the serpentine region of the follitropin receptor modulate the rate of agonist-induced internalization
    • Kishi H., Ascoli M. Multiple distant amino acid residues present in the serpentine region of the follitropin receptor modulate the rate of agonist-induced internalization. J Biol Chem 2000, 275:31030-31037.
    • (2000) J Biol Chem , vol.275 , pp. 31030-31037
    • Kishi, H.1    Ascoli, M.2
  • 400
    • 0037077222 scopus 로고    scopus 로고
    • Identification of a short linear sequence present in the c-terminal tail of the rat follitropin receptor that modulates arrestin-3 binding in a phosphorylation-independent fashion
    • Kishi H., Krishnamurthy H., Galet C., et al. Identification of a short linear sequence present in the c-terminal tail of the rat follitropin receptor that modulates arrestin-3 binding in a phosphorylation-independent fashion. J Biol Chem 2002, 277:21939-21946.
    • (2002) J Biol Chem , vol.277 , pp. 21939-21946
    • Kishi, H.1    Krishnamurthy, H.2    Galet, C.3
  • 401
    • 0037769052 scopus 로고    scopus 로고
    • The association of arrestin-3 with the follitropin receptor depends on receptor activation and phosphorylation
    • Krishnamurthy H., Galet C., Ascoli M. The association of arrestin-3 with the follitropin receptor depends on receptor activation and phosphorylation. Mol Cell Endocrinol 2003, 204:127-140.
    • (2003) Mol Cell Endocrinol , vol.204 , pp. 127-140
    • Krishnamurthy, H.1    Galet, C.2    Ascoli, M.3
  • 402
    • 0021702460 scopus 로고
    • Lysosomal accumulation of the hormone-receptor complex during receptor-mediated endocytosis of human choriogonadotropin
    • Ascoli M. Lysosomal accumulation of the hormone-receptor complex during receptor-mediated endocytosis of human choriogonadotropin. J Cell Biol 1984, 99:1242-1250.
    • (1984) J Cell Biol , vol.99 , pp. 1242-1250
    • Ascoli, M.1
  • 403
    • 0032836647 scopus 로고    scopus 로고
    • A dileucine-based motif in the c-terminal tail of the lutropin/choriogonadotropin receptor inhibits endocytosis of the agonist-receptor complex
    • Nakamura K., Ascoli M. A dileucine-based motif in the c-terminal tail of the lutropin/choriogonadotropin receptor inhibits endocytosis of the agonist-receptor complex. Mol Pharmacol 1999, 56:728-736.
    • (1999) Mol Pharmacol , vol.56 , pp. 728-736
    • Nakamura, K.1    Ascoli, M.2
  • 404
    • 0034463062 scopus 로고    scopus 로고
    • The c-terminal tail of the rat lutropin/choriogonadotropin receptor independently modulates hCG-induced internalization of the cell surface receptor and the lysosomal targeting of the internalized hCG-receptor complex
    • Kishi M., Ascoli M. The c-terminal tail of the rat lutropin/choriogonadotropin receptor independently modulates hCG-induced internalization of the cell surface receptor and the lysosomal targeting of the internalized hCG-receptor complex. Mol Endocrinol 2000, 14:926-936.
    • (2000) Mol Endocrinol , vol.14 , pp. 926-936
    • Kishi, M.1    Ascoli, M.2
  • 405
    • 0026731460 scopus 로고
    • Pathways of internalization of the hCG/LH receptor: immunoelectron microscopic studies in Leydig cells and transfected l cells
    • Ghinea N., Vuhai M.T., Groyer-Picard M.-T., et al. Pathways of internalization of the hCG/LH receptor: immunoelectron microscopic studies in Leydig cells and transfected l cells. J Cell Biol 1992, 118:1347-1358.
    • (1992) J Cell Biol , vol.118 , pp. 1347-1358
    • Ghinea, N.1    Vuhai, M.T.2    Groyer-Picard, M.-T.3
  • 406
    • 0033304941 scopus 로고    scopus 로고
    • Internalization and recycling pathways of the thyrotropin receptor
    • Baratti-Elbaz C., Chinea N., Lahuna O., et al. Internalization and recycling pathways of the thyrotropin receptor. Mol Endocrinol 1999, 13:1751-1765.
    • (1999) Mol Endocrinol , vol.13 , pp. 1751-1765
    • Baratti-Elbaz, C.1    Chinea, N.2    Lahuna, O.3
  • 407
    • 0020625309 scopus 로고
    • On the mechanisms involved in the regulation of the cell surface receptors for human choriogonadotropin and mouse epidermal growth factor in cultured Leydig tumor cells
    • Lloyd C.E., Ascoli M. On the mechanisms involved in the regulation of the cell surface receptors for human choriogonadotropin and mouse epidermal growth factor in cultured Leydig tumor cells. J Cell Biol 1983, 96:521-526.
    • (1983) J Cell Biol , vol.96 , pp. 521-526
    • Lloyd, C.E.1    Ascoli, M.2
  • 408
    • 0026025792 scopus 로고
    • Lutropin/choriogonadotropin down-regulates its receptor by both receptor mediated endocytosis and a cAMP-dependent reduction in receptor mRNA
    • Wang H., Segaloff D.L., Ascoli M. Lutropin/choriogonadotropin down-regulates its receptor by both receptor mediated endocytosis and a cAMP-dependent reduction in receptor mRNA. J Biol Chem 1991, 266:780-785.
    • (1991) J Biol Chem , vol.266 , pp. 780-785
    • Wang, H.1    Segaloff, D.L.2    Ascoli, M.3
  • 409
    • 0033304965 scopus 로고    scopus 로고
    • Role of the rate of internalization of the agonist-receptor complex on the agonist-induced down-regulation of the lutropin/choriogonadotropin receptor
    • Nakamura K., Lazari M.F.M., Li S., et al. Role of the rate of internalization of the agonist-receptor complex on the agonist-induced down-regulation of the lutropin/choriogonadotropin receptor. Mol Endocrinol 1999, 13:1295-1304.
    • (1999) Mol Endocrinol , vol.13 , pp. 1295-1304
    • Nakamura, K.1    Lazari, M.F.M.2    Li, S.3
  • 410
    • 17844390142 scopus 로고    scopus 로고
    • The post-endocytotic fate of the gonadotropin receptors is an important determinant of the desensitization of gonadotropin responses
    • Bhaskaran R.S., Ascoli M. The post-endocytotic fate of the gonadotropin receptors is an important determinant of the desensitization of gonadotropin responses. J Mol Endocrinol 2005, 34:447-457.
    • (2005) J Mol Endocrinol , vol.34 , pp. 447-457
    • Bhaskaran, R.S.1    Ascoli, M.2
  • 411
    • 0034823954 scopus 로고    scopus 로고
    • Identification of two distinct structural motifs that, when added to the c-terminal tail of the rat lutropin receptor, redirect the internalized hormone-receptor complex from a degradation to a recycling pathway
    • Kishi M., Liu X., Hirakawa T., et al. Identification of two distinct structural motifs that, when added to the c-terminal tail of the rat lutropin receptor, redirect the internalized hormone-receptor complex from a degradation to a recycling pathway. Mol Endocrinol 2001, 15:1624-1635.
    • (2001) Mol Endocrinol , vol.15 , pp. 1624-1635
    • Kishi, M.1    Liu, X.2    Hirakawa, T.3
  • 412
    • 0037341727 scopus 로고    scopus 로고
    • Identification of a transferable two amino acid motif (gt) present in the c-terminal tail of the human lutropin receptor that redirects internalized G protein-coupled receptors from a degradation to a recycling pathway
    • Galet C., Min L., Narayanan R., et al. Identification of a transferable two amino acid motif (gt) present in the c-terminal tail of the human lutropin receptor that redirects internalized G protein-coupled receptors from a degradation to a recycling pathway. Mol Endocrinol 2003, 17:411-422.
    • (2003) Mol Endocrinol , vol.17 , pp. 411-422
    • Galet, C.1    Min, L.2    Narayanan, R.3
  • 413
    • 0842290983 scopus 로고    scopus 로고
    • The postendocytotic trafficking of the hLHR is mediated by a transferable motif consisting of the c-terminal cysteine and an upstream leucine
    • Galet C., Hirakawa T., Ascoli M. The postendocytotic trafficking of the hLHR is mediated by a transferable motif consisting of the c-terminal cysteine and an upstream leucine. Mol Endocrinol 2004, 18:434-446.
    • (2004) Mol Endocrinol , vol.18 , pp. 434-446
    • Galet, C.1    Hirakawa, T.2    Ascoli, M.3
  • 414
    • 0242267063 scopus 로고    scopus 로고
    • Post-endocytotic trafficking of the FSH/FSH receptor complex
    • Krishnamurthy H., Kishi H., Shi M., et al. Post-endocytotic trafficking of the FSH/FSH receptor complex. Mol Endocrinol 2003, 17:2162-2176.
    • (2003) Mol Endocrinol , vol.17 , pp. 2162-2176
    • Krishnamurthy, H.1    Kishi, H.2    Shi, M.3
  • 415
    • 0842292006 scopus 로고    scopus 로고
    • GIPC binds to the human lutropin receptor (LHR) through an unusual PDZ domain binding motif and it regulates the sorting of the internalized human choriogonadotropin (hCG) and the density of cell surface LHR
    • Hirakawa T., Galet C., Kishi M., et al. GIPC binds to the human lutropin receptor (LHR) through an unusual PDZ domain binding motif and it regulates the sorting of the internalized human choriogonadotropin (hCG) and the density of cell surface LHR. J Biol Chem 2003, 278:49348-49357.
    • (2003) J Biol Chem , vol.278 , pp. 49348-49357
    • Hirakawa, T.1    Galet, C.2    Kishi, M.3
  • 416
    • 0032506018 scopus 로고    scopus 로고
    • Impairing follicle-stimulating hormone (FSH) signaling in vivo: targeted disruption of the FSH receptor leads to aberrant gametogenesis and hormonal imbalance
    • Dierich A., Sairam M.R., Monaco L., et al. Impairing follicle-stimulating hormone (FSH) signaling in vivo: targeted disruption of the FSH receptor leads to aberrant gametogenesis and hormonal imbalance. Proc Natl Acad Sci U S A 1998, 95:13612-13617.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 13612-13617
    • Dierich, A.1    Sairam, M.R.2    Monaco, L.3
  • 417
    • 0034457577 scopus 로고    scopus 로고
    • The effect of a null mutation in the follicle-stimulating hormone receptor gene on mouse reproduction
    • Abel M.H., Wootton A.N., Wilkins V., et al. The effect of a null mutation in the follicle-stimulating hormone receptor gene on mouse reproduction. Endocrinology 2000, 141:1795-1803.
    • (2000) Endocrinology , vol.141 , pp. 1795-1803
    • Abel, M.H.1    Wootton, A.N.2    Wilkins, V.3
  • 418
    • 33947609974 scopus 로고    scopus 로고
    • The past, present and future of nongonadal LH/hCG actions in reproductive biology and medicine
    • Rao C.V., Lei Z.M. The past, present and future of nongonadal LH/hCG actions in reproductive biology and medicine. Mol Cell Endocrinol 2007, 269:2-8.
    • (2007) Mol Cell Endocrinol , vol.269 , pp. 2-8
    • Rao, C.V.1    Lei, Z.M.2
  • 419
    • 0642307054 scopus 로고    scopus 로고
    • Clinical importance of vascular LH/hCG receptors: a review
    • Toth P., Lukacs H., Gimes G., et al. Clinical importance of vascular LH/hCG receptors: a review. Reprod Biol 2001, 1:5-11.
    • (2001) Reprod Biol , vol.1 , pp. 5-11
    • Toth, P.1    Lukacs, H.2    Gimes, G.3
  • 420
    • 0035013450 scopus 로고    scopus 로고
    • An overview of the past, present, and future of nongonadal LH/hCG actions in reproductive biology and medicine
    • Rao C.V. An overview of the past, present, and future of nongonadal LH/hCG actions in reproductive biology and medicine. Semin Reprod Med 2001, 19:7-17.
    • (2001) Semin Reprod Med , vol.19 , pp. 7-17
    • Rao, C.V.1
  • 421
    • 23744447683 scopus 로고    scopus 로고
    • Novel concepts of human chorionic gonadotropin: reproductive system interactions and potential in the management of infertility
    • Filicori M., Fazleabas A.T., Huhtaniemi I., et al. Novel concepts of human chorionic gonadotropin: reproductive system interactions and potential in the management of infertility. Fertil Steril 2005, 84:275-284.
    • (2005) Fertil Steril , vol.84 , pp. 275-284
    • Filicori, M.1    Fazleabas, A.T.2    Huhtaniemi, I.3
  • 422
    • 33751248755 scopus 로고    scopus 로고
    • Phenotypic characterisation of mice with exaggerated and missing LH/hCG action
    • Ahtiainen P., Rulli S., Pakarainen T., et al. Phenotypic characterisation of mice with exaggerated and missing LH/hCG action. Mol Cell Endocrinol 2007, 260-262:255-263.
    • (2007) Mol Cell Endocrinol , vol.260-262 , pp. 255-263
    • Ahtiainen, P.1    Rulli, S.2    Pakarainen, T.3
  • 423
    • 33845662625 scopus 로고    scopus 로고
    • Angiogenic activity of human chorionic gonadotropin through LH receptor activation on endothelial and epithelial cells of the endometrium
    • Berndt S., d'Hauterive S.P., Blacher S., et al. Angiogenic activity of human chorionic gonadotropin through LH receptor activation on endothelial and epithelial cells of the endometrium. FASEB J 2006, 20:2630-2632.
    • (2006) FASEB J , vol.20 , pp. 2630-2632
    • Berndt, S.1    d'Hauterive, S.P.2    Blacher, S.3
  • 424
    • 0032734209 scopus 로고    scopus 로고
    • Leuprolide acetate therapy in luteinizing hormone-dependent Cushing's syndrome
    • Lacroix A., Hamet P., Boutin J.M. Leuprolide acetate therapy in luteinizing hormone-dependent Cushing's syndrome. N Engl J Med 1999, 341:1577-1581.
    • (1999) N Engl J Med , vol.341 , pp. 1577-1581
    • Lacroix, A.1    Hamet, P.2    Boutin, J.M.3
  • 425
    • 0035118956 scopus 로고    scopus 로고
    • Ectopic and abnormal hormone receptors in adrenal Cushing's syndrome
    • Lacroix A., N'Diaye N., Tremblay J., et al. Ectopic and abnormal hormone receptors in adrenal Cushing's syndrome. Endocr Rev 2001, 22:75-110.
    • (2001) Endocr Rev , vol.22 , pp. 75-110
    • Lacroix, A.1    N'Diaye, N.2    Tremblay, J.3
  • 426
    • 0029742472 scopus 로고    scopus 로고
    • Gonadotropins are essential modifier factors for gonadal tumor development in inhibin-deficient mice
    • Kumar T.R., Wang Y., Matzuk M.M. Gonadotropins are essential modifier factors for gonadal tumor development in inhibin-deficient mice. Endocrinology 1996, 137:4210-4216.
    • (1996) Endocrinology , vol.137 , pp. 4210-4216
    • Kumar, T.R.1    Wang, Y.2    Matzuk, M.M.3
  • 427
    • 0030787593 scopus 로고    scopus 로고
    • Suppression of gonadotropins inhibits gonadal tumorogenesis in mice transgenic for the mouse inhibin-a subunit promoter/sv40 t-antigen fusion gene
    • Kananen K., Rillianawati Paukku T., Markkular M., et al. Suppression of gonadotropins inhibits gonadal tumorogenesis in mice transgenic for the mouse inhibin-a subunit promoter/sv40 t-antigen fusion gene. Endocrinology 1997, 138:3521-3531.
    • (1997) Endocrinology , vol.138 , pp. 3521-3531
    • Kananen, K.1    Rillianawati Paukku, T.2    Markkular, M.3
  • 428
    • 0032230319 scopus 로고    scopus 로고
    • Direct luteinizing hormone action triggers adrenocortical tumorigenesis in castrated mice transgenic for the murine inhibin α-subunit promoter/simian virus 40 t-antigen fusion gene
    • Rilianawati Paukku T., Kero J., et al. Direct luteinizing hormone action triggers adrenocortical tumorigenesis in castrated mice transgenic for the murine inhibin α-subunit promoter/simian virus 40 t-antigen fusion gene. Mol Cell Endocrinol 1998, 12:801-809.
    • (1998) Mol Cell Endocrinol , vol.12 , pp. 801-809
    • Rilianawati, P.T.1    Kero, J.2
  • 429
    • 0034064198 scopus 로고    scopus 로고
    • Elevated luteinizing hormone induces expression of its receptor and promotes steroidogenesis in the adrenal cortex
    • Kero J., Poutanen M., Zhang F.P., et al. Elevated luteinizing hormone induces expression of its receptor and promotes steroidogenesis in the adrenal cortex. J Clin Invest 2000, 105:633-641.
    • (2000) J Clin Invest , vol.105 , pp. 633-641
    • Kero, J.1    Poutanen, M.2    Zhang, F.P.3
  • 430
    • 33646036678 scopus 로고    scopus 로고
    • FSH directly regulates bone mass
    • Sun L., Peng Y., Sharrow A.C., et al. FSH directly regulates bone mass. Cell 2006, 125:247-260.
    • (2006) Cell , vol.125 , pp. 247-260
    • Sun, L.1    Peng, Y.2    Sharrow, A.C.3
  • 431
    • 34250887411 scopus 로고    scopus 로고
    • Hypogonadal bone loss: sex steroids or gonadotropins?
    • Williams G.R. Hypogonadal bone loss: sex steroids or gonadotropins?. Endocrinology 2007, 148:2610-2612.
    • (2007) Endocrinology , vol.148 , pp. 2610-2612
    • Williams, G.R.1
  • 432
    • 34250824919 scopus 로고    scopus 로고
    • Altered ovarian function affects skeletal homeostasis independent of the action of follicle-stimulating hormone
    • Gao J., Tiwari-Pandey R., Samadfam R., et al. Altered ovarian function affects skeletal homeostasis independent of the action of follicle-stimulating hormone. Endocrinology 2007, 148:2613-2621.
    • (2007) Endocrinology , vol.148 , pp. 2613-2621
    • Gao, J.1    Tiwari-Pandey, R.2    Samadfam, R.3
  • 433
    • 0034966945 scopus 로고    scopus 로고
    • FACRO, Ben-Josef E. Humoral mechanisms in prostate cancer: a role for FSH
    • Porter A.T. FACRO, Ben-Josef E. Humoral mechanisms in prostate cancer: a role for FSH. Urol Oncol 2001, 6:131-138.
    • (2001) Urol Oncol , vol.6 , pp. 131-138
    • Porter, A.T.1
  • 434
    • 24944486224 scopus 로고    scopus 로고
    • What have we learned about gonadotropin function from gonadotropin subunit and receptor knockout mice?
    • Kumar T.R. What have we learned about gonadotropin function from gonadotropin subunit and receptor knockout mice?. Reproduction 2005, 130:293-302.
    • (2005) Reproduction , vol.130 , pp. 293-302
    • Kumar, T.R.1
  • 435
    • 22144464436 scopus 로고    scopus 로고
    • Fertility in luteinizing hormone receptor-knockout mice after wild-type ovary transplantation demonstrates redundancy of extragonadal luteinizing hormone action
    • Pakarainen T., Zhang F.-P., Poutanen M., et al. Fertility in luteinizing hormone receptor-knockout mice after wild-type ovary transplantation demonstrates redundancy of extragonadal luteinizing hormone action. J Clin Invest 2005, 115:1862-1868.
    • (2005) J Clin Invest , vol.115 , pp. 1862-1868
    • Pakarainen, T.1    Zhang, F.-P.2    Poutanen, M.3
  • 436
    • 24344446906 scopus 로고    scopus 로고
    • Orthotopic transplantation of LH receptor knockout and wild-type ovaries
    • Chudgar D., Lei Z., Rao C.V. Orthotopic transplantation of LH receptor knockout and wild-type ovaries. Life Sci 2005, 77:2656-2662.
    • (2005) Life Sci , vol.77 , pp. 2656-2662
    • Chudgar, D.1    Lei, Z.2    Rao, C.V.3
  • 437
    • 0027170277 scopus 로고
    • The regulation of the binding affinity of the luteinizing hormone/choriogonadotropin receptor by sodium ions is mediated by a highly conserved aspartate located in the second transmembrane domain of G protein-coupled receptors
    • Quintana J., Wang H., Ascoli M. The regulation of the binding affinity of the luteinizing hormone/choriogonadotropin receptor by sodium ions is mediated by a highly conserved aspartate located in the second transmembrane domain of G protein-coupled receptors. Mol Endocrinol 1993, 7:767-775.
    • (1993) Mol Endocrinol , vol.7 , pp. 767-775
    • Quintana, J.1    Wang, H.2    Ascoli, M.3
  • 438
    • 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., et al. 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
  • 439
    • 85047686522 scopus 로고    scopus 로고
    • Cis- and trans-activation of hormone receptors: the LH receptor
    • Ji I., Lee C., Song Y., et al. 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
  • 440
    • 21244460359 scopus 로고    scopus 로고
    • Glycoprotein hormone receptors: link between receptor homodimerization and negative cooperativity
    • Urizar E., Montanelli L., Loy T., et al. Glycoprotein hormone receptors: link between receptor homodimerization and negative cooperativity. EMBO J 2005, 24:1954-1964.
    • (2005) EMBO J , vol.24 , pp. 1954-1964
    • Urizar, E.1    Montanelli, L.2    Loy, T.3
  • 442
    • 0026611368 scopus 로고
    • +2 mobilization by the LH receptor expressed in Xenopus oocytes independent of 3',5'-cyclic adenosine monophosphate formation: evidence for parallel activation of two signaling pathways
    • +2 mobilization by the LH receptor expressed in Xenopus oocytes independent of 3',5'-cyclic adenosine monophosphate formation: evidence for parallel activation of two signaling pathways. Mol Endocrinol 1992, 6:272-278.
    • (1992) Mol Endocrinol , vol.6 , pp. 272-278
    • Gudermann, T.1    Nichols, C.2    Levy, F.O.3
  • 443
    • 0024533488 scopus 로고
    • The inositol phosphate/diacylglycerol pathway in ma-10 Leydig tumor cells: activation by arginine vasopressin and lack of effect of epidermal growth factor and human choriogonadotropin
    • Ascoli M., Pignataro O.P., Segaloff D.L. The inositol phosphate/diacylglycerol pathway in ma-10 Leydig tumor cells: activation by arginine vasopressin and lack of effect of epidermal growth factor and human choriogonadotropin. J Biol Chem 1989, 264:6674-6681.
    • (1989) J Biol Chem , vol.264 , pp. 6674-6681
    • Ascoli, M.1    Pignataro, O.P.2    Segaloff, D.L.3
  • 444
    • 0022363890 scopus 로고
    • Phorbol ester causes desensitization of gonadotropin-responsive adenylate cyclase in a murine Leydig tumor cell line
    • Rebois R.V., Patel J. Phorbol ester causes desensitization of gonadotropin-responsive adenylate cyclase in a murine Leydig tumor cell line. J Biol Chem 1985, 260:8026-8031.
    • (1985) J Biol Chem , vol.260 , pp. 8026-8031
    • Rebois, R.V.1    Patel, J.2
  • 445
    • 0028030774 scopus 로고
    • Dual signaling potential is common among Gs-coupled receptors and dependent on receptor density
    • Zhu X., Gilbert S., Birnbaumer M., et al. Dual signaling potential is common among Gs-coupled receptors and dependent on receptor density. Mol Pharmacol 1994, 46:460-469.
    • (1994) Mol Pharmacol , vol.46 , pp. 460-469
    • Zhu, X.1    Gilbert, S.2    Birnbaumer, M.3
  • 446
    • 0036171565 scopus 로고    scopus 로고
    • MA-10 cells transfected with the human lutropin/choriogonadotropin receptor (hLHR): a novel experimental paradigm to study the functional properties of the hLHR
    • Hirakawa T., Galet C., Ascoli M. MA-10 cells transfected with the human lutropin/choriogonadotropin receptor (hLHR): a novel experimental paradigm to study the functional properties of the hLHR. Endocrinology 2002, 143:1026-1035.
    • (2002) Endocrinology , vol.143 , pp. 1026-1035
    • Hirakawa, T.1    Galet, C.2    Ascoli, M.3
  • 447
    • 23844456672 scopus 로고    scopus 로고
    • The differential effects of the gonadotropin receptors on aromatase expression in primary cultures of immature rat granulosa cells are highly dependent on the density of receptors expressed and the activation of the inositol phosphate cascade
    • Donadeu F.X., Ascoli M. The differential effects of the gonadotropin receptors on aromatase expression in primary cultures of immature rat granulosa cells are highly dependent on the density of receptors expressed and the activation of the inositol phosphate cascade. Endocrinology 2005, 146:3907-3916.
    • (2005) Endocrinology , vol.146 , pp. 3907-3916
    • Donadeu, F.X.1    Ascoli, M.2
  • 448
    • 33751533169 scopus 로고    scopus 로고
    • A delayed, gonadotropin-dependent and growth-factor mediated activation of the erk1/2 cascade negatively regulates aromatase expression in granulosa cells
    • Andric N., Ascoli M. A delayed, gonadotropin-dependent and growth-factor mediated activation of the erk1/2 cascade negatively regulates aromatase expression in granulosa cells. Mol Endocrinol 2006, 20:3308-3320.
    • (2006) Mol Endocrinol , vol.20 , pp. 3308-3320
    • Andric, N.1    Ascoli, M.2
  • 449
    • 0029666283 scopus 로고    scopus 로고
    • Involvement of Gs and Gi proteins in dual coupling of the luteinizing hormone receptor to adenylyl cyclase and phospholipase C
    • Herrlich A., Kuhn B., Grosse R., et al. Involvement of Gs and Gi proteins in dual coupling of the luteinizing hormone receptor to adenylyl cyclase and phospholipase C. J Biol Chem 1996, 271:16764-16772.
    • (1996) J Biol Chem , vol.271 , pp. 16764-16772
    • Herrlich, A.1    Kuhn, B.2    Grosse, R.3
  • 451
    • 0031735628 scopus 로고    scopus 로고
    • Luteinizing hormone/choriogonadotropin receptor-mediated activation of heterotrimeric guanine nucleotide binding proteins in ovarian follicular membranes
    • Rajagopalan-Gupta R., Lamm M.L.G., Mukherjee S., et al. Luteinizing hormone/choriogonadotropin receptor-mediated activation of heterotrimeric guanine nucleotide binding proteins in ovarian follicular membranes. Endocrinology 1998, 139:4547-4555.
    • (1998) Endocrinology , vol.139 , pp. 4547-4555
    • Rajagopalan-Gupta, R.1    Lamm, M.L.G.2    Mukherjee, S.3
  • 452
    • 0041920692 scopus 로고    scopus 로고
    • A constitutively active somatic mutation of the human lutropin receptor found in Leydig cell tumors activates the same families of G proteins as germ line mutations associated with Leydig cell hyperplasia
    • Hirakawa T., Ascoli M. A constitutively active somatic mutation of the human lutropin receptor found in Leydig cell tumors activates the same families of G proteins as germ line mutations associated with Leydig cell hyperplasia. Endocrinology 2003, 144:3872-3878.
    • (2003) Endocrinology , vol.144 , pp. 3872-3878
    • Hirakawa, T.1    Ascoli, M.2
  • 453
    • 2542509528 scopus 로고    scopus 로고
    • The luteinizing hormone receptor activates phospholipase C via preferential coupling to Gi2
    • Kühn B., Gudermann T. The luteinizing hormone receptor activates phospholipase C via preferential coupling to Gi2. Biochemistry 1999, 38:12490-12498.
    • (1999) Biochemistry , vol.38 , pp. 12490-12498
    • Kühn, B.1    Gudermann, T.2
  • 454
    • 0028944310 scopus 로고
    • Genetic heterogeneity of constitutively activating mutations of the human luteinizing hormone receptor in familial male-limited precoious puberty
    • Laue L., Chan W.-Y., Hsueh A.J.W., et al. Genetic heterogeneity of constitutively activating mutations of the human luteinizing hormone receptor in familial male-limited precoious puberty. Proc Natl Acad Sci U S A 1995, 92:1906-1910.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 1906-1910
    • Laue, L.1    Chan, W.-Y.2    Hsueh, A.J.W.3
  • 455
    • 0031976756 scopus 로고    scopus 로고
    • Severe testotoxicosis phenotype associated with Asp578>Tyr mutation of the lutrophin/choriogonadotrophin receptor gene
    • Muller J., Gondos B., Kosugi S., et al. Severe testotoxicosis phenotype associated with Asp578>Tyr mutation of the lutrophin/choriogonadotrophin receptor gene. J Med Genet 1998, 35:340-341.
    • (1998) J Med Genet , vol.35 , pp. 340-341
    • Muller, J.1    Gondos, B.2    Kosugi, S.3
  • 456
    • 0029992481 scopus 로고    scopus 로고
    • A case of male-limited precocious puberty caused by a point mutaion in the second transmembrane domain of the luteinizing hormone choriogonadotropin receptor gene
    • Yano K., Kohn L., Saji M., et al. A case of male-limited precocious puberty caused by a point mutaion in the second transmembrane domain of the luteinizing hormone choriogonadotropin receptor gene. Biochem Biophys Res Commun 1996, 220:1036-1042.
    • (1996) Biochem Biophys Res Commun , vol.220 , pp. 1036-1042
    • Yano, K.1    Kohn, L.2    Saji, M.3
  • 457
    • 0031728024 scopus 로고    scopus 로고
    • A unique constitutively activating mutation in third transmembrane helix of luteinizing hormone receptor causes sporadic male gonadotropin-independent precocious puberty
    • Latronico A.C., Abell A.N., Arnhold I.J.P., et al. A unique constitutively activating mutation in third transmembrane helix of luteinizing hormone receptor causes sporadic male gonadotropin-independent precocious puberty. J Clin Endocrinol Metab 1998, 83:2435-2440.
    • (1998) J Clin Endocrinol Metab , vol.83 , pp. 2435-2440
    • Latronico, A.C.1    Abell, A.N.2    Arnhold, I.J.P.3
  • 458
    • 33744810660 scopus 로고    scopus 로고
    • FSH signaling pathways in immature granulosa cells that regulate target gene expression: branching out from protein kinase A
    • Hunzicker-Dunn M., Maizels E.T. FSH signaling pathways in immature granulosa cells that regulate target gene expression: branching out from protein kinase A. Cell Signal 2006, 18:1351-1359.
    • (2006) Cell Signal , vol.18 , pp. 1351-1359
    • Hunzicker-Dunn, M.1    Maizels, E.T.2
  • 459
    • 2442485795 scopus 로고    scopus 로고
    • Follicle-stimulating hormone activation of hypoxia-inducible factor-1 by the phosphatidylinositol 3-kinase/akt/ras homolog enriched in brain (Rheb)/mammalian target of rapamycin (mTOR) pathway is necessary for induction of select protein markers of follicular differentiation
    • Alam H., Maizels E.T., Park Y., et al. Follicle-stimulating hormone activation of hypoxia-inducible factor-1 by the phosphatidylinositol 3-kinase/akt/ras homolog enriched in brain (Rheb)/mammalian target of rapamycin (mTOR) pathway is necessary for induction of select protein markers of follicular differentiation. J Biol Chem 2004, 279:19431-19440.
    • (2004) J Biol Chem , vol.279 , pp. 19431-19440
    • Alam, H.1    Maizels, E.T.2    Park, Y.3
  • 460
    • 0037470090 scopus 로고    scopus 로고
    • Follicle-stimulating hormone activates extracellular signal-regulated kinase but not extracellular signal-regulated kinase kinase through a 100-kda phosphotyrosine phosphatase
    • Cottom J., Salvador L.M., Maizels E.T., et al. Follicle-stimulating hormone activates extracellular signal-regulated kinase but not extracellular signal-regulated kinase kinase through a 100-kda phosphotyrosine phosphatase. J Biol Chem 2003, 278:7167-7179.
    • (2003) J Biol Chem , vol.278 , pp. 7167-7179
    • Cottom, J.1    Salvador, L.M.2    Maizels, E.T.3
  • 461
    • 0036320795 scopus 로고    scopus 로고
    • Acute signaling by the LH receptor is independent of protein kinase C activation
    • Salvador L.M., Maizels E., Hales D.B., et al. Acute signaling by the LH receptor is independent of protein kinase C activation. Endocrinology 2002, 143:2986-2994.
    • (2002) Endocrinology , vol.143 , pp. 2986-2994
    • Salvador, L.M.1    Maizels, E.2    Hales, D.B.3
  • 462
    • 22144448594 scopus 로고    scopus 로고
    • Luteinizing hormone-induced extracellular-signal regulated kinase activation differently modulates progesterone and androstenedione production in bovine theca cells
    • Tajima K., Yoshii K., Fukuda S., et al. Luteinizing hormone-induced extracellular-signal regulated kinase activation differently modulates progesterone and androstenedione production in bovine theca cells. Endocrinology 2005, 146:2903-2910.
    • (2005) Endocrinology , vol.146 , pp. 2903-2910
    • Tajima, K.1    Yoshii, K.2    Fukuda, S.3
  • 463
    • 0242298720 scopus 로고    scopus 로고
    • The lutropin/choriogonadotropin receptor-induced phosphorylation of the extracellular signal regulated kinases in Leydig cells is mediated by a protein kinase A-dependent activation of ras
    • Hirakawa T., Ascoli M. The lutropin/choriogonadotropin receptor-induced phosphorylation of the extracellular signal regulated kinases in Leydig cells is mediated by a protein kinase A-dependent activation of ras. Mol Endocrinol 2003, 17:2189-2200.
    • (2003) Mol Endocrinol , vol.17 , pp. 2189-2200
    • Hirakawa, T.1    Ascoli, M.2
  • 464
    • 36549059723 scopus 로고    scopus 로고
    • co-culture system reveals the involvement of intercellular pathways as mediators of the lutropin receptor (LHR)-stimulated ERK1/2 phosphorylation in leydig cells.
    • 10.1016/j.yexcr.2007.06.025
    • Shiraishi K, Ascoli M. A co-culture system reveals the involvement of intercellular pathways as mediators of the lutropin receptor (LHR)-stimulated ERK1/2 phosphorylation in leydig cells. Exp Cell Res doi:10.1016/j.yexcr.2007.06.025 2007.
    • (2007) Exp Cell Res doi
    • Shiraishi, K.1    Ascoli, M.A.2
  • 465
    • 34347252268 scopus 로고    scopus 로고
    • Lutropin/choriogonadotropin (LH/CG) stimulates the proliferation of primary cultures of rat Leydig cells through a pathway that involves activation of the ERK1/2 cascade
    • Shiraishi K., Ascoli M. Lutropin/choriogonadotropin (LH/CG) stimulates the proliferation of primary cultures of rat Leydig cells through a pathway that involves activation of the ERK1/2 cascade. Endocrinology 2007, 148:3214-3225.
    • (2007) Endocrinology , vol.148 , pp. 3214-3225
    • Shiraishi, K.1    Ascoli, M.2
  • 466
    • 33745167984 scopus 로고    scopus 로고
    • Activation of the lutropin/choriogonadotropin receptor (LHR) in MA-10 cells stimulates tyrosine kinase cascades that activate ras and the extracellular signal regulated kinases (ERK1/2)
    • Shiraishi K., Ascoli M. Activation of the lutropin/choriogonadotropin receptor (LHR) in MA-10 cells stimulates tyrosine kinase cascades that activate ras and the extracellular signal regulated kinases (ERK1/2). Endocrinology 2006, 147:3419-3427.
    • (2006) Endocrinology , vol.147 , pp. 3419-3427
    • Shiraishi, K.1    Ascoli, M.2
  • 467
    • 4644293240 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinases are involved in the acute activation of steroidogenesis in immature rat Leydig cells by human chorionic gonadotropin
    • Martinelle N., Holst M., Soder O., et al. Extracellular signal-regulated kinases are involved in the acute activation of steroidogenesis in immature rat Leydig cells by human chorionic gonadotropin. Endocrinology 2004, 145:4629-4634.
    • (2004) Endocrinology , vol.145 , pp. 4629-4634
    • Martinelle, N.1    Holst, M.2    Soder, O.3
  • 468
    • 22544432534 scopus 로고    scopus 로고
    • FSH and testosterone signaling in Sertoli cells
    • Walker W.H., Cheng J. FSH and testosterone signaling in Sertoli cells. Reproduction 2005, 130:15-28.
    • (2005) Reproduction , vol.130 , pp. 15-28
    • Walker, W.H.1    Cheng, J.2
  • 469
    • 33344475112 scopus 로고    scopus 로고
    • Activation of the lutropin/choriogonadotropin receptor in MA-10 cells leads to the tyrosine phosphorylation of the focal adhesion kinase by a pathway that involves Src family kinases
    • Mizutani T., Shiraishi K., Welsh T., et al. Activation of the lutropin/choriogonadotropin receptor in MA-10 cells leads to the tyrosine phosphorylation of the focal adhesion kinase by a pathway that involves Src family kinases. Mol Endocrinol 2006, 20:619-630.
    • (2006) Mol Endocrinol , vol.20 , pp. 619-630
    • Mizutani, T.1    Shiraishi, K.2    Welsh, T.3
  • 470
    • 0037320295 scopus 로고    scopus 로고
    • Novel signal transduction pathway for luteinizing hormone and its interaction with insulin: activation of Janus kinase/signal transducer and activator of transcription and phosphoinositol 3-kinase/Akt pathways
    • Carvalho C.R.O., Carvalheira J.B.C., Lima M.H.M., et al. Novel signal transduction pathway for luteinizing hormone and its interaction with insulin: activation of Janus kinase/signal transducer and activator of transcription and phosphoinositol 3-kinase/Akt pathways. Endocrinology 2003, 144:638-647.
    • (2003) Endocrinology , vol.144 , pp. 638-647
    • Carvalho, C.R.O.1    Carvalheira, J.B.C.2    Lima, M.H.M.3
  • 471
    • 0942301323 scopus 로고    scopus 로고
    • EGF-like growth factors as mediators of LH action in the ovulatory follicle
    • Park J.-Y., Su Y.-Q., Ariga M., et al. EGF-like growth factors as mediators of LH action in the ovulatory follicle. Science 2004, 303:682-684.
    • (2004) Science , vol.303 , pp. 682-684
    • Park, J.-Y.1    Su, Y.-Q.2    Ariga, M.3
  • 472
    • 11144227264 scopus 로고    scopus 로고
    • Epidermal growth factor family members: endogenous mediators of the ovulatory response
    • Ashkenazi H., Cao X., Motola S., et al. Epidermal growth factor family members: endogenous mediators of the ovulatory response. Endocrinology 2005, 146:77-84.
    • (2005) Endocrinology , vol.146 , pp. 77-84
    • Ashkenazi, H.1    Cao, X.2    Motola, S.3
  • 473
    • 33645391525 scopus 로고    scopus 로고
    • Role of the epidermal growth factor network in ovarian follicles
    • Conti M., Hsieh M., Park J.Y., et al. Role of the epidermal growth factor network in ovarian follicles. Mol Endocrinol 2005, 20:715-723.
    • (2005) Mol Endocrinol , vol.20 , pp. 715-723
    • Conti, M.1    Hsieh, M.2    Park, J.Y.3
  • 474
    • 23944432412 scopus 로고    scopus 로고
    • G-protein-coupled receptor signaling and the EGF network in endocrine systems
    • Hsieh M., Conti M. G-protein-coupled receptor signaling and the EGF network in endocrine systems. Trends Endocrinol Metab 2005, 16:320-326.
    • (2005) Trends Endocrinol Metab , vol.16 , pp. 320-326
    • Hsieh, M.1    Conti, M.2
  • 475
    • 33847188090 scopus 로고    scopus 로고
    • Luteinizing hormone-dependent activation of the epidermal growth factor network is essential for ovulation
    • Hsieh M., Lee D., Panigone S., et al. Luteinizing hormone-dependent activation of the epidermal growth factor network is essential for ovulation. Mol Cell Biol 2007, 27:1914-1924.
    • (2007) Mol Cell Biol , vol.27 , pp. 1914-1924
    • Hsieh, M.1    Lee, D.2    Panigone, S.3
  • 476
    • 34547483968 scopus 로고    scopus 로고
    • Follicle-stimulating hormone induces multiple signaling cascades: evidence that activation of Rous sarcoma oncogene, RAS, and the epidermal growth factor receptor are critical for granulosa cell differentiation
    • Wayne C.M., Fan H.-Y., Cheng X., et al. Follicle-stimulating hormone induces multiple signaling cascades: evidence that activation of Rous sarcoma oncogene, RAS, and the epidermal growth factor receptor are critical for granulosa cell differentiation. Mol Endocrinol 2007, 21:1940-1957.
    • (2007) Mol Endocrinol , vol.21 , pp. 1940-1957
    • Wayne, C.M.1    Fan, H.-Y.2    Cheng, X.3
  • 477
    • 0035006882 scopus 로고    scopus 로고
    • Perspective: the ovarian follicle. A perspective in 2001
    • Richards J.S. Perspective: the ovarian follicle. A perspective in 2001. Endocrinology 2001, 142:2184-2193.
    • (2001) Endocrinology , vol.142 , pp. 2184-2193
    • Richards, J.S.1
  • 478
    • 33751202427 scopus 로고    scopus 로고
    • Potential Leydig cell mitogenic signals generated by the wild-type and constitutively active mutants of the lutropin/choriogonadotropin receptor
    • Ascoli M. Potential Leydig cell mitogenic signals generated by the wild-type and constitutively active mutants of the lutropin/choriogonadotropin receptor. Mol Cell Endocrinol 2007, 260-262:244-248.
    • (2007) Mol Cell Endocrinol , vol.260-262 , pp. 244-248
    • Ascoli, M.1
  • 479
    • 33751248755 scopus 로고    scopus 로고
    • Phenotypic characterization of mice with exaggerated and missing LH/hCG action
    • Ahtiainen P., Rulli S., Pakarainen T., et al. Phenotypic characterization of mice with exaggerated and missing LH/hCG action. Mol Cell Endocrinol 2007, 260-262:255-263.
    • (2007) Mol Cell Endocrinol , vol.260-262 , pp. 255-263
    • Ahtiainen, P.1    Rulli, S.2    Pakarainen, T.3
  • 480
    • 33751202427 scopus 로고    scopus 로고
    • Potential Leydig cell mitogenic signals generated by the wild-type and constitutively active mutants of the lutropin/choriogonadotropin receptor
    • Ascoli M. Potential Leydig cell mitogenic signals generated by the wild-type and constitutively active mutants of the lutropin/choriogonadotropin receptor. Mol Cell Endocrinol 2007, 260-262:244-248.
    • (2007) Mol Cell Endocrinol , vol.260-262 , pp. 244-248
    • Ascoli, M.1
  • 481
    • 0036217072 scopus 로고    scopus 로고
    • The lutropin/choriogonadotropin receptor: a 2002 perspective
    • Ascoli M., Fanelli F., Segaloff D.L. The lutropin/choriogonadotropin receptor: a 2002 perspective. Endocr Rev 2002, 23:141-174.
    • (2002) Endocr Rev , vol.23 , pp. 141-174
    • Ascoli, M.1    Fanelli, F.2    Segaloff, D.L.3
  • 483
    • 33645391525 scopus 로고    scopus 로고
    • Role of the EGF network in ovarian follicles
    • Conti M., Hsieh M., Park J.Y., et al. Role of the EGF network in ovarian follicles. Mol Endocrinol 2005, 20:715-723.
    • (2005) Mol Endocrinol , vol.20 , pp. 715-723
    • Conti, M.1    Hsieh, M.2    Park, J.Y.3
  • 484
    • 24944502148 scopus 로고    scopus 로고
    • Specificity and promiscuity of gonadotropin receptors
    • Costagliola S., Urizar E., Mendive F., et al. Specificity and promiscuity of gonadotropin receptors. Reproduction 2005, 130:275-281.
    • (2005) Reproduction , vol.130 , pp. 275-281
    • Costagliola, S.1    Urizar, E.2    Mendive, F.3
  • 485
    • 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
  • 486
    • 0033829535 scopus 로고    scopus 로고
    • Molecular architecture and biorecognition processes of the cystine knot protein superfamily: Part I. The glycoprotein hormones
    • Hearn M.T.W., Gomme P.T. Molecular architecture and biorecognition processes of the cystine knot protein superfamily: Part I. The glycoprotein hormones. J Mol Recog 2000, 13:223-278.
    • (2000) J Mol Recog , vol.13 , pp. 223-278
    • Hearn, M.T.W.1    Gomme, P.T.2
  • 487
    • 33744810660 scopus 로고    scopus 로고
    • FSH signaling pathways in immature granulosa cells that regulate target gene expression: branching out from protein kinase A
    • Hunzicker-Dunn M., Maizels E.T. FSH signaling pathways in immature granulosa cells that regulate target gene expression: branching out from protein kinase A. Cell Signal 2006, 18:1351-1359.
    • (2006) Cell Signal , vol.18 , pp. 1351-1359
    • Hunzicker-Dunn, M.1    Maizels, E.T.2
  • 488
    • 0028239813 scopus 로고
    • Crystal-structure of human chorionic-gonadotropin
    • Lapthorn A.J., Harris D.C., Littlejohn A., et al. Crystal-structure of human chorionic-gonadotropin. Nature 1994, 369:455-461.
    • (1994) Nature , vol.369 , pp. 455-461
    • Lapthorn, A.J.1    Harris, D.C.2    Littlejohn, A.3
  • 489
    • 33751200969 scopus 로고    scopus 로고
    • Insights learned from L457(3.43)R, an activating mutant of the human lutropin receptor
    • Latronico A.C., Segaloff D.L. Insights learned from L457(3.43)R, an activating mutant of the human lutropin receptor. Mol Cell Endocrinol 2007, 260-262:287-293.
    • (2007) Mol Cell Endocrinol , vol.260-262 , pp. 287-293
    • Latronico, A.C.1    Segaloff, D.L.2
  • 490
    • 0031864755 scopus 로고    scopus 로고
    • The tie that binds: design of biologically active single-chain human chorionic gonadotropins and a gonadotropin-receptor complex using protein engineering
    • Puett D., Wu C.B., Narayan P. The tie that binds: design of biologically active single-chain human chorionic gonadotropins and a gonadotropin-receptor complex using protein engineering. Biol Reprod 1998, 58:1337-1342.
    • (1998) Biol Reprod , vol.58 , pp. 1337-1342
    • Puett, D.1    Wu, C.B.2    Narayan, P.3
  • 491
    • 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., et al. 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
  • 492
    • 24944501149 scopus 로고    scopus 로고
    • An update of the pathophysiology of human gonadotrophin subunit and receptor gene mutations and polymorphisms
    • Themmen A.P.N. An update of the pathophysiology of human gonadotrophin subunit and receptor gene mutations and polymorphisms. Reproduction 2005, 130:263-274.
    • (2005) Reproduction , vol.130 , pp. 263-274
    • Themmen, A.P.N.1
  • 493
    • 0028773646 scopus 로고
    • Structure of human chorionic-gonadotropin at 2.6-Angstrom resolution from MAD analysis of theselenomethionyl protein
    • Wu H., Lustbader J.W., Liu Y., et al. Structure of human chorionic-gonadotropin at 2.6-Angstrom resolution from MAD analysis of theselenomethionyl protein. Structure 1994, 2:545-558.
    • (1994) Structure , vol.2 , pp. 545-558
    • Wu, H.1    Lustbader, J.W.2    Liu, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.