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Volumn 12, Issue 2, 2001, Pages 72-77

Novel recombinant gonadotropins

Author keywords

[No Author keywords available]

Indexed keywords

CHORIONIC GONADOTROPIN; FOLLITROPIN; GONADOTROPIN; LUTEINIZING HORMONE; RECOMBINANT PROTEIN;

EID: 0035292797     PISSN: 10432760     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1043-2760(00)00338-6     Document Type: Review
Times cited : (41)

References (59)
  • 1
    • 0002441052 scopus 로고
    • Gonadotropin hormones: Biosynthesis, secretion, receptors and action
    • Yen, S. and Jaffe, R., eds, WS Saunders
    • Catt, K.J. and Dufau, M.L. (1991) Gonadotropin hormones: biosynthesis, secretion, receptors and action. In Reproductive Endocrinology(Yen, S. and Jaffe, R., eds), pp. 105-155, WS Saunders
    • (1991) Reproductive Endocrinology , pp. 105-155
    • Catt, K.J.1    Dufau, M.L.2
  • 2
    • 0024408258 scopus 로고
    • Granulosa cells as hormone targets: The role of biologically active follicle-stimulating hormones in reproduction
    • Hsueh, A.J.W. et al. (1989) Granulosa cells as hormone targets: the role of biologically active follicle-stimulating hormones in reproduction. Recent Prog. Horm. Res. 45, 209-273
    • (1989) Recent Prog. Horm. Res. , vol.45 , pp. 209-273
    • Hsueh, A.J.W.1
  • 4
    • 0001181429 scopus 로고
    • The thyroid gland and reproduction
    • Yen, S. and Jaffe, R., eds, WS Saunders
    • Burrow, G.N. (1991) The thyroid gland and reproduction. In Reproductive Endocrinology (Yen, S. and Jaffe, R., eds), pp. 555-575, WS Saunders
    • (1991) Reproductive Endocrinology , pp. 555-575
    • Burrow, G.N.1
  • 5
    • 0019729482 scopus 로고
    • Glycoprotein hormones: Structure and function
    • Pierce, J.G. and Parsons, T.F. (1981) Glycoprotein hormones: structure and function. Annu. Rev. Biochem. 50, 465-495
    • (1981) Annu. Rev. Biochem. , vol.50 , pp. 465-495
    • Pierce, J.G.1    Parsons, T.F.2
  • 6
    • 0021118043 scopus 로고
    • Structure, expression, and evolution of the genes for the human glycoprotein hormones
    • Fiddes, J.C. and Talmadge, A. (1984) Structure, expression, and evolution of the genes for the human glycoprotein hormones. Recent Prog. Horm. Res. 40, 43-78
    • (1984) Recent Prog. Horm. Res. , vol.40 , pp. 43-78
    • Fiddes, J.C.1    Talmadge, A.2
  • 7
    • 0017723084 scopus 로고
    • Isolation and amino acid sequence of COOH-terminal fragments from the β subunit of human choriogonadotropin
    • Birken, S. and Canfield, R.E. (1977) Isolation and amino acid sequence of COOH-terminal fragments from the β subunit of human choriogonadotropin. J. Biol. Chem. 252, 5386-5392
    • (1977) J. Biol. Chem. , vol.252 , pp. 5386-5392
    • Birken, S.1    Canfield, R.E.2
  • 8
    • 0022408484 scopus 로고
    • Demonstration of a COOH-terminal extension on equine lutropin by means of a common acid-labile bond in equine lutropin and equine chorionic gonadotropin
    • Bousfield, G.R. et al. (1985) Demonstration of a COOH-terminal extension on equine lutropin by means of a common acid-labile bond in equine lutropin and equine chorionic gonadotropin. J. Biol. Chem. 260, 9531-9533
    • (1985) J. Biol. Chem. , vol.260 , pp. 9531-9533
    • Bousfield, G.R.1
  • 9
    • 0018675127 scopus 로고
    • Structure and location of the O-glycosidic carbohydrate units of human chorionic gonadotropin
    • Kessler, M.J. et al. (1979) Structure and location of the O-glycosidic carbohydrate units of human chorionic gonadotropin. J. Biol. Chem. 254, 7909-7914
    • (1979) J. Biol. Chem. , vol.254 , pp. 7909-7914
    • Kessler, M.J.1
  • 10
    • 0024282581 scopus 로고
    • Pituitary glycoprotein hormone oligosaccharides: Structure, synthesis and function of asparaginelinked oligosaccharides on lutropin, follitropin and thyrotropin
    • Baenziger, J.U. and Green, E.D. (1988) Pituitary glycoprotein hormone oligosaccharides: structure, synthesis and function of asparaginelinked oligosaccharides on lutropin, follitropin and thyrotropin. Biochim. Biophys. Acta 947, 287-306
    • (1988) Biochim. Biophys. Acta , vol.947 , pp. 287-306
    • Baenziger, J.U.1    Green, E.D.2
  • 11
    • 0026485387 scopus 로고
    • Molecular structures of glycoprotein hormones and functions of their carbohydrate components
    • Stockell-Hartee, A. and Renwick, A.G.C. (1992) Molecular structures of glycoprotein hormones and functions of their carbohydrate components. Biochem. J. 287, 665-679
    • (1992) Biochem. J. , vol.287 , pp. 665-679
    • Stockell-Hartee, A.1    Renwick, A.G.C.2
  • 12
    • 77956802616 scopus 로고
    • The glycoprotein hormone family: Structure and function of the carbohydrate chains
    • Montreuil, J. et al., eds, Elsevier Science
    • Bielinska, M. and Boime, I. (1995) The glycoprotein hormone family: structure and function of the carbohydrate chains. In Glycoproteins (Vol. 29A) (Montreuil, J. et al., eds), pp. 565-587, Elsevier Science
    • (1995) Glycoproteins , vol.29 A , pp. 565-587
    • Bielinska, M.1    Boime, I.2
  • 13
    • 0008274497 scopus 로고
    • Combination of rat lutropin subunits occurs early in the secretory pathway
    • Hoshina, H. and Boime, I. (1982) Combination of rat lutropin subunits occurs early in the secretory pathway. Proc. Natl. Acad. Sci. U. S. A. 79, 7649-7653
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 7649-7653
    • Hoshina, H.1    Boime, I.2
  • 14
    • 0019974454 scopus 로고
    • Thyroidstimulating hormone subunit processing and combination in microsomal subfractions of mouse pituitary tumor
    • Magner, J.A. and Weintraub, B.D. (1982) Thyroidstimulating hormone subunit processing and combination in microsomal subfractions of mouse pituitary tumor. J. Biol. Chem. 257, 6709-6715
    • (1982) J. Biol. Chem. , vol.257 , pp. 6709-6715
    • Magner, J.A.1    Weintraub, B.D.2
  • 15
    • 0023835289 scopus 로고
    • The glycoprotein asubunit is critical for secretion and stability of the human thyrotropin β-subunit
    • Matzuk, M.M. et al. (1988) The glycoprotein asubunit is critical for secretion and stability of the human thyrotropin β-subunit. Mol. Endrocrinol. 2, 95-100
    • (1988) Mol. Endrocrinol. , vol.2 , pp. 95-100
    • Matzuk, M.M.1
  • 16
    • 0023277697 scopus 로고
    • LH and hCG β subunits determine the rate of assembly and the oligosaccharide processing of hormone dimer in transfected cells
    • Corless, C.L. et al. (1987) LH and hCG β subunits determine the rate of assembly and the oligosaccharide processing of hormone dimer in transfected cells. J. Cell. Biol. 104, 1173-1181
    • (1987) J. Cell. Biol. , vol.104 , pp. 1173-1181
    • Corless, C.L.1
  • 17
    • 0028239813 scopus 로고
    • Crystal structure of human chorionic gonadotropin
    • Lapthorn, AJ. et al. (1994) Crystal structure of human chorionic gonadotropin. Nature 369, 455-461
    • (1994) Nature , vol.369 , pp. 455-461
    • Lapthorn, A.J.1
  • 18
    • 0028773646 scopus 로고
    • Structure of the human chorionic gonadotropin at 2.6 Å resolution from MAD analysis of the selenomethionyl protein
    • Wu, H. et al. (1994) Structure of the human chorionic gonadotropin at 2.6 Å resolution from MAD analysis of the selenomethionyl protein. Structure 2, 545-558
    • (1994) Structure , vol.2 , pp. 545-558
    • Wu, H.1
  • 19
    • 0024454312 scopus 로고
    • Mutagenesis and chimeric genes define determinants in the β-subunits of human chorionic gonadotropin and Iutropin for secretion and assembly
    • Matzuk, M. et al. (1989) Mutagenesis and chimeric genes define determinants in the β-subunits of human chorionic gonadotropin and Iutropin for secretion and assembly. J. Cell Biol. 109, 1429-1438
    • (1989) J. Cell Biol. , vol.109 , pp. 1429-1438
    • Matzuk, M.1
  • 20
    • 0024813415 scopus 로고
    • Elimination of disulfide bonds affects assembly and secretion of the human chorionic gonadotropin β-subunit
    • Suganuma, N. et al. (1989) Elimination of disulfide bonds affects assembly and secretion of the human chorionic gonadotropin β-subunit. J. Biol. Chem. 264, 19302-19307
    • (1989) J. Biol. Chem. , vol.264 , pp. 19302-19307
    • Suganuma, N.1
  • 21
    • 0025993392 scopus 로고
    • Role of the invariant aspartic acid 99 of human chorionic gonadotropin β in receptor binding and biological activity
    • Chen, F. et al. (1991) Role of the invariant aspartic acid 99 of human chorionic gonadotropin β in receptor binding and biological activity. J. Biol. Chem. 266, 19357-19361
    • (1991) J. Biol. Chem. , vol.266 , pp. 19357-19361
    • Chen, F.1
  • 22
    • 0025020754 scopus 로고
    • The biological role of the carboxyl-terminal extension of human chorionic gonadotropin β-subunit
    • Matzuk, M.M. et al. (1990) The biological role of the carboxyl-terminal extension of human chorionic gonadotropin β-subunit. Endocrinology 126, 376-383
    • (1990) Endocrinology , vol.126 , pp. 376-383
    • Matzuk, M.M.1
  • 23
    • 0024404680 scopus 로고
    • Disruption of TV-linked glycosylation of bovine luteinizing hormone β-subunit by site-directed mutagenesis dramatically increases its intracellular stability but does not affect biological activity of the secreted heterodimer
    • Kaetzel, D.M. et al. (1989) Disruption of TV-linked glycosylation of bovine luteinizing hormone β-subunit by site-directed mutagenesis dramatically increases its intracellular stability but does not affect biological activity of the secreted heterodimer. Mol. Endrocrinol. 3, 1765-1774
    • (1989) Mol. Endrocrinol. , vol.3 , pp. 1765-1774
    • Kaetzel, D.M.1
  • 24
    • 0024511030 scopus 로고
    • Site-specificity of the chorionic gonadotropin N-linked oligosaccharides in signal transduction
    • Matzuk, M.M. et al. (1989) Site-specificity of the chorionic gonadotropin N-linked oligosaccharides in signal transduction. J. Biol. Chem. 264, 2409-2414
    • (1989) J. Biol. Chem. , vol.264 , pp. 2409-2414
    • Matzuk, M.M.1
  • 25
    • 0018404329 scopus 로고
    • Metabolism of exogenous human chorionic gonadotropin in men
    • Sowers, J.R. et al. (1979) Metabolism of exogenous human chorionic gonadotropin in men. J. Endocrinol. 80, 83-89
    • (1979) J. Endocrinol. , vol.80 , pp. 83-89
    • Sowers, J.R.1
  • 26
    • 0014872812 scopus 로고
    • Human pituitary follicle stimulating hormone distribution, plasma clearance and urinary excretion as determined by radioimmunoassay
    • Amin, H.K. and Hunter, W.M. (1970) Human pituitary follicle stimulating hormone distribution, plasma clearance and urinary excretion as determined by radioimmunoassay J. Endocrinol. 48, 307-317
    • (1970) J. Endocrinol. , vol.48 , pp. 307-317
    • Amin, H.K.1    Hunter, W.M.2
  • 27
    • 0026551294 scopus 로고
    • Design of a long-acting follitropin agonist by fusing the C-terminal sequence of the chorionic gonadotropin β subunit
    • Fares, F.A. et al. (1992) Design of a long-acting follitropin agonist by fusing the C-terminal sequence of the chorionic gonadotropin β subunit. Proc. Natl. Acad. Sci. U. S. A. 89, 4303-4308
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 4303-4308
    • Fares, F.A.1
  • 28
    • 0029166316 scopus 로고
    • Recombinant thyrotropin containing a β-subunit chimera with the human chorionic gonadotropin-β carboxy-terminus is biologically active, with a prolonged plasma half-life: Role of carbohydrate in bioactivity and metabolic clearance
    • Joshi, L. et al. (1995) Recombinant thyrotropin containing a β-subunit chimera with the human chorionic gonadotropin-β carboxy-terminus is biologically active, with a prolonged plasma half-life: role of carbohydrate in bioactivity and metabolic clearance. Endocrinology 136, 3839-3848
    • (1995) Endocrinology , vol.136 , pp. 3839-3848
    • Joshi, L.1
  • 29
    • 0029785186 scopus 로고    scopus 로고
    • Engineering human glycoprotein hormone superactive analogues
    • Szkudlinski, M.W. et al. (1996) Engineering human glycoprotein hormone superactive analogues. Nat. Biotechnol. 14, 1257-1263
    • (1996) Nat. Biotechnol. , vol.14 , pp. 1257-1263
    • Szkudlinski, M.W.1
  • 30
    • 0025291299 scopus 로고
    • In vitro and in vivo bioactivity of recombinant human follicle-stimulating hormone and partially deglycosylated variants secreted by transfected eukaryotic cell lines
    • Galway A.B. et al. (1990) In vitro and in vivo bioactivity of recombinant human follicle-stimulating hormone and partially deglycosylated variants secreted by transfected eukaryotic cell lines. Endocrinology 127, 93-100
    • (1990) Endocrinology , vol.127 , pp. 93-100
    • Galway, A.B.1
  • 31
    • 0030132712 scopus 로고    scopus 로고
    • Molecular biology and biochemistry of human recombinant follicle stimulating hormone (Puregon)
    • Olijve, W. et al. (1996) Molecular biology and biochemistry of human recombinant follicle stimulating hormone (Puregon). Mol. Hum. Reprod. 2, 371-382
    • (1996) Mol. Hum. Reprod. , vol.2 , pp. 371-382
    • Olijve, W.1
  • 32
    • 0028948846 scopus 로고
    • Biosynthesis of a biologically active single pep tide chain containing the human common α and chorionic gonadotropin β subunits in tandem
    • Sugahara, T. et al. (1995) Biosynthesis of a biologically active single pep tide chain containing the human common α and chorionic gonadotropin β subunits in tandem. Proc. Natl. Acad. Sci. U. S. A. 92, 2041-2045
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 2041-2045
    • Sugahara, T.1
  • 33
    • 0018786891 scopus 로고
    • Biologically active covalently cross-linked glycoprotein hormones and the effects of modification of the COOH-terminal region of their α subunits
    • Parsons, T.F. and Pierce, J.G. (1979) Biologically active covalently cross-linked glycoprotein hormones and the effects of modification of the COOH-terminal region of their α subunits. J. Biol. Chem. 254, 6010-6015
    • (1979) J. Biol. Chem. , vol.254 , pp. 6010-6015
    • Parsons, T.F.1    Pierce, J.G.2
  • 34
    • 0018639424 scopus 로고
    • Studies of the specific role of the subunits of choriogonadotropin for biological, immunological and physical properties of the hormone: Digestion of the α-subunit with carboxypeptidase A
    • Merz, W.E. (1979) Studies of the specific role of the subunits of choriogonadotropin for biological, immunological and physical properties of the hormone: digestion of the α-subunit with carboxypeptidase A. Eur. J. Biochem. 101, 541-553
    • (1979) Eur. J. Biochem. , vol.101 , pp. 541-553
    • Merz, W.E.1
  • 35
    • 0001605979 scopus 로고
    • Structural aspects of luteinizing hormone action
    • Ascoli, M., eds, CRC Press
    • Gordon, W.L. and Ward, D.N. (1985) Structural aspects of luteinizing hormone action. In Luteinizing Hormone Action and Receptors (Ascoli, M., eds), pp. 173-198, CRC Press
    • (1985) Luteinizing Hormone Action and Receptors , pp. 173-198
    • Gordon, W.L.1    Ward, D.N.2
  • 36
    • 0023264867 scopus 로고
    • Inhibition of human choriotropin binding to receptor by human choriotropin α peptides: A comprehensive synthetic approach
    • Charlesworth, M.C. et al. (1987) Inhibition of human choriotropin binding to receptor by human choriotropin α peptides: a comprehensive synthetic approach. J. Biol. Chem. 262, 13409-13416
    • (1987) J. Biol. Chem. , vol.262 , pp. 13409-13416
    • Charlesworth, M.C.1
  • 37
    • 0242520134 scopus 로고
    • Site-directed mutagenesis identifies two receptor binding domains in the human chorionic gonadotropin α subunit
    • Bielinska, M. et al. (1990) Site-directed mutagenesis identifies two receptor binding domains in the human chorionic gonadotropin α subunit. J. Cell. Biol. 111, 330a
    • (1990) J. Cell. Biol. , vol.111
    • Bielinska, M.1
  • 38
    • 0025990729 scopus 로고
    • Conversion of lysine 91 to methionine or glutamic acid in human choriogonadotropin α results in the loss of cAMP inducibility
    • Yoo, J. et al. (1991) Conversion of lysine 91 to methionine or glutamic acid in human choriogonadotropin α results in the loss of cAMP inducibility J. Biol. Chem. 266, 17741-17743
    • (1991) J. Biol. Chem. , vol.266 , pp. 17741-17743
    • Yoo, J.1
  • 39
    • 0026635335 scopus 로고
    • The carboxy-terminal region of the glycoprotein hormone α-subunit: Contributions to receptor binding and signaling in human chorionic gonadotropin
    • Chen, F. et al. (1992) The carboxy-terminal region of the glycoprotein hormone α-subunit: contributions to receptor binding and signaling in human chorionic gonadotropin. Mol. Endocrinol. 6, 914-919
    • (1992) Mol. Endocrinol. , vol.6 , pp. 914-919
    • Chen, F.1
  • 40
    • 0028882196 scopus 로고
    • Functional expression of yoked human chorionic gonadotropin in baculovirus-infected insect cells
    • Narayan, P et al. (1995) Functional expression of yoked human chorionic gonadotropin in baculovirus-infected insect cells. Mol. Endocrinol. 9, 1720-1726
    • (1995) Mol. Endocrinol. , vol.9 , pp. 1720-1726
    • Narayan, P.1
  • 41
    • 0030816072 scopus 로고    scopus 로고
    • Design of stable biologically active recombinant lutropin analogs
    • Garcia-Campayo, V. et al. (1997) Design of stable biologically active recombinant lutropin analogs. Nat. Biotechnol. 15, 663-667
    • (1997) Nat. Biotechnol. , vol.15 , pp. 663-667
    • Garcia-Campayo, V.1
  • 42
    • 15844427850 scopus 로고    scopus 로고
    • Expression of biologically active fusion genes encoding the common α subunit and the follicle-stimulating hormone β subunit: Role of linker sequence
    • Sugahara, T. et al. (1996) Expression of biologically active fusion genes encoding the common α subunit and the follicle-stimulating hormone β subunit: role of linker sequence. J. Biol. Chem. 271, 10445-10448
    • (1996) J. Biol. Chem. , vol.271 , pp. 10445-10448
    • Sugahara, T.1
  • 43
    • 0030881847 scopus 로고    scopus 로고
    • Human thyroid stimulating hormone (hTSH) subunit gene fusion produces hTSH with increased stability and serum half-life and compensates for mutagenesisinduced defects in subunit association
    • Grossman, M. et al. (1997) Human thyroid stimulating hormone (hTSH) subunit gene fusion produces hTSH with increased stability and serum half-life and compensates for mutagenesisinduced defects in subunit association. J. Biol. Chem. 272, 21312-21316
    • (1997) J. Biol. Chem. , vol.272 , pp. 21312-21316
    • Grossman, M.1
  • 44
    • 0030873203 scopus 로고    scopus 로고
    • Structure-based design and protein engineering of intersubunit disulfide bonds in gonadotropins
    • Heikoop, J.C. et al. (1997) Structure-based design and protein engineering of intersubunit disulfide bonds in gonadotropins. Nat. Biotechnol. 15, 658-662
    • (1997) Nat. Biotechnol. , vol.15 , pp. 658-662
    • Heikoop, J.C.1
  • 45
    • 0033310391 scopus 로고    scopus 로고
    • The biological action of choriogonadotropin is not dependent on the complete native quaternary interactions between the subunits
    • Jackson, A.M. et al. (1999) The biological action of choriogonadotropin is not dependent on the complete native quaternary interactions between the subunits. Mol. Endocrinol. 13, 2175-2188
    • (1999) Mol. Endocrinol. , vol.13 , pp. 2175-2188
    • Jackson, A.M.1
  • 46
    • 0030959878 scopus 로고    scopus 로고
    • The biologic action of single-chain choriogonadotropin is not dependent on the individual disulfide bonds of the β subunit
    • Ben-Menahem, D. et al. (1997) The biologic action of single-chain choriogonadotropin is not dependent on the individual disulfide bonds of the β subunit. J. Biol. Chem. 272, 6827-6830
    • (1997) J. Biol. Chem. , vol.272 , pp. 6827-6830
    • Ben-Menahem, D.1
  • 47
    • 0030739370 scopus 로고    scopus 로고
    • Cystine knot of the gonadotropin α subunit is critical for intracellular behavior but not for in vitro biological activity
    • Sato, A. et al. (1997) Cystine knot of the gonadotropin α subunit is critical for intracellular behavior but not for in vitro biological activity. J. Biol. Chem. 272, 18098-18103
    • (1997) J. Biol. Chem. , vol.272 , pp. 18098-18103
    • Sato, A.1
  • 48
    • 9444236174 scopus 로고    scopus 로고
    • Small peptidesas potent mimetics of the protein hormone erythropoietin
    • Wrighton, N.C. et al. (1996) Small peptidesas potent mimetics of the protein hormone erythropoietin. Science 273, 458-463
    • (1996) Science , vol.273 , pp. 458-463
    • Wrighton, N.C.1
  • 49
    • 0011958990 scopus 로고    scopus 로고
    • High affinity type I interleukin 1 receptor antagonists discovered by screening recombinant peptide libraries
    • Yanofsky, S.D. et al. (1996) High affinity type I interleukin 1 receptor antagonists discovered by screening recombinant peptide libraries. Proc. Natl. Acad. Sci. U. S. A. 93, 7381-7386
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 7381-7386
    • Yanofsky, S.D.1
  • 50
    • 0029619255 scopus 로고
    • Minimization of polypeptide hormone
    • Li, B. et al. (1995) Minimization of polypeptide hormone. Science 270, 1657-1660
    • (1995) Science , vol.270 , pp. 1657-1660
    • Li, B.1
  • 52
    • 0013663164 scopus 로고    scopus 로고
    • Towards minimized gonadotropins with full bioactivity
    • Heikoop, J.C. et al. (1999) Towards minimized gonadotropins with full bioactivity Eur. J. Biochem. 261, 81-83
    • (1999) Eur. J. Biochem. , vol.261 , pp. 81-83
    • Heikoop, J.C.1
  • 53
    • 0029856730 scopus 로고    scopus 로고
    • Protein engineering of a novel constitutively active hormone-receptor complex
    • Wu, C. et al. (1996) Protein engineering of a novel constitutively active hormone-receptor complex. J. Biol. Chem. 271, 31638-31642
    • (1996) J. Biol. Chem. , vol.271 , pp. 31638-31642
    • Wu, C.1
  • 54
    • 0029768832 scopus 로고    scopus 로고
    • Disulfide bonds 7-31 and 59-87 of the α-subunit play a different role in assembly of human chorionic gonadotropin and lutropin
    • Furuhashi, M. et al. (1996) Disulfide bonds 7-31 and 59-87 of the α-subunit play a different role in assembly of human chorionic gonadotropin and lutropin. Endocrinology 137, 4196-4200
    • (1996) Endocrinology , vol.137 , pp. 4196-4200
    • Furuhashi, M.1
  • 55
    • 0030013815 scopus 로고    scopus 로고
    • Site-directed mutagenesis of amino acids 33-44 of the common α-subunit reveals different structural requirements for heterodimer expression among the glycoprotein hormones and suggests that cyclic adenosine 3′ 5′-monophosphate production and growth promotion are potentially dissociable functions of human thyrotropin
    • Grossman, M. et al. (1996) Site-directed mutagenesis of amino acids 33-44 of the common α-subunit reveals different structural requirements for heterodimer expression among the glycoprotein hormones and suggests that cyclic adenosine 3′ 5′-monophosphate production and growth promotion are potentially dissociable functions of human thyrotropin. Mol. Endocrinol. 10, 769-779
    • (1996) Mol. Endocrinol. , vol.10 , pp. 769-779
    • Grossman, M.1
  • 56
    • 0033304953 scopus 로고    scopus 로고
    • Genetic fusion of an α-subunit gene to the follicle-stimulating hormone and chorionic gonadotropin β-subunit genes: Production of a bifunctional protein
    • Kanda, M. et al. (1999) Genetic fusion of an α-subunit gene to the follicle-stimulating hormone and chorionic gonadotropin β-subunit genes: production of a bifunctional protein. Mol. Endocrinol. 13, 1873-1881
    • (1999) Mol. Endocrinol. , vol.13 , pp. 1873-1881
    • Kanda, M.1
  • 57
    • 0033576304 scopus 로고    scopus 로고
    • Synthesis of multisubunit domain gonadotropin complexes: A model of α/β heterodimer formation
    • Ben-Menahem, D. et al. (1999) Synthesis of multisubunit domain gonadotropin complexes: a model of α/β heterodimer formation. Biochemistry 38, 15070-15077
    • (1999) Biochemistry , vol.38 , pp. 15070-15077
    • Ben-Menahem, D.1
  • 58
    • 0029125838 scopus 로고
    • The groove between the α and β-subunits of hormones with lutropin (LH) activity appears to contact the LH receptor, and its conformation is changed during hormone binding
    • Cosowsky, L. et al. (1995) The groove between the α and β-subunits of hormones with lutropin (LH) activity appears to contact the LH receptor, and its conformation is changed during hormone binding. J. Biol. Chem. 270, 20011-20019
    • (1995) J. Biol. Chem. , vol.270 , pp. 20011-20019
    • Cosowsky, L.1
  • 59
    • 0029093909 scopus 로고
    • Model of human chorionic gonadotropin and lutropin receptor interaction that explains signal transduction of the glycoprotein hormones
    • Moyle, W.R. et al. (1995) Model of human chorionic gonadotropin and lutropin receptor interaction that explains signal transduction of the glycoprotein hormones. J. Biol. Chem. 270, 20020-20031
    • (1995) J. Biol. Chem. , vol.270 , pp. 20020-20031
    • Moyle, W.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.