메뉴 건너뛰기




Volumn 12, Issue 4, 2011, Pages 289-302

Synthesis and secretion of gonadotropins including structure-function correlates

Author keywords

Common a subunit; FSH ; GnRH; LH ; Transcription

Indexed keywords

FOLLITROPIN; GONADORELIN; GONADOTROPIN; GONADOTROPIN DERIVATIVE; RECOMBINANT CHORIONIC GONADOTROPIN; RECOMBINANT FOLLITROPIN; RECOMBINANT LUTEINIZING HORMONE;

EID: 84855644683     PISSN: 13899155     EISSN: 15732606     Source Type: Journal    
DOI: 10.1007/s11154-011-9191-3     Document Type: Article
Times cited : (39)

References (110)
  • 1
  • 2
    • 34249951808 scopus 로고    scopus 로고
    • Hypopituitarism
    • DOI 10.1007/s11102-006-0416-5, Management Updates
    • Ascoli P, Cavagnini T. Hypopituitarism. Pituitary. 2006;9:335-42. (Pubitemid 44823903)
    • (2006) Pituitary , vol.9 , Issue.4 , pp. 335-342
    • Ascoli, P.1    Cavagnini, F.2
  • 3
    • 62149105580 scopus 로고    scopus 로고
    • New discoveries on the biology and detection of human chorionic gonadotropin
    • Cole LA. New discoveries on the biology and detection of human chorionic gonadotropin. Reprod Biol Endocrinol. 2009;7:8.
    • (2009) Reprod Biol Endocrinol , vol.7 , pp. 8
    • Cole, L.A.1
  • 4
    • 58049206780 scopus 로고    scopus 로고
    • Human choriogonadotrphin protein core and sugar branches heterogeneity: Basic and clinical insights
    • de Medeiros SF, Norman RJ. Human choriogonadotrphin protein core and sugar branches heterogeneity: Basic and clinical insights. Hum Reprod Update. 2009;15:69-95.
    • (2009) Hum Reprod Update , vol.15 , pp. 69-95
    • De Medeiros, S.F.1    Norman, R.J.2
  • 5
    • 84884006741 scopus 로고    scopus 로고
    • Gonadotropins: Chemistry and biosynthesis
    • In: Neill JD, editor 3rd ed San Diego: Elsevier
    • Bousfield GR, Jia L, Ward DN. Gonadotropins: Chemistry and biosynthesis. In: Neill JD, editor. Knobil and Neill: Physiology of reproduction. 3rd ed. San Diego: Elsevier; 2006. p. 1581- 634.
    • (2006) Knobil and Neill: Physiology of reproduction , pp. 1581-1634
    • Bousfield, G.R.1    Jia, L.2    Ward, D.N.3
  • 6
    • 77952108994 scopus 로고    scopus 로고
    • Mechanisms of FSH synthesis: What we know, what we don't, and why you should care
    • Bernard DJ, Fortin J, Wang Y, Lamba P. Mechanisms of FSH synthesis: What we know, what we don't, and why you should care. Fertil Steril. 2010;93:2465-85.
    • (2010) Fertil Steril , vol.93 , pp. 2465-2485
    • Bernard, D.J.1    Fortin, J.2    Wang, Y.3    Lamba, P.4
  • 8
    • 77957265789 scopus 로고    scopus 로고
    • LIM homeodomain transcription factor Isl-1 enhances folliclestimulating hormone-beta and luteinizing hormone-beta gene expression and mediatse the activation of leptin on gonadotropin synthesis
    • Wu Y, Luo H, Liu J, Kang D, McNeilly AS, Cui S. LIM homeodomain transcription factor Isl-1 enhances folliclestimulating hormone-beta and luteinizing hormone-beta gene expression and mediatse the activation of leptin on gonadotropin synthesis. Endocrinology. 2010;151:4787-800.
    • (2010) Endocrinology , vol.151 , pp. 4787-4800
    • Wu, Y.1    Luo, H.2    Liu, J.3    Kang, D.4    McNeilly, A.S.5    Cui, S.6
  • 9
    • 65949117611 scopus 로고    scopus 로고
    • Gene expression and secretion of LH and FSH in relation to gene expression of GnRH receptors in the brushtail possum (Tricosurus vulpecula) demonstrates highly conserved mechanisms
    • Crawford JL, Heath DA, Haydon LJ, Thompson BP, Eckery DC. Gene expression and secretion of LH and FSH in relation to gene expression of GnRH receptors in the brushtail possum (Tricosurus vulpecula) demonstrates highly conserved mechanisms. Reproduction. 2009;137(1):129-40.
    • (2009) Reproduction , vol.137 , Issue.1 , pp. 129-140
    • Crawford, J.L.1    Heath, D.A.2    Haydon, L.J.3    Thompson, B.P.4    Eckery, D.C.5
  • 10
    • 0023881509 scopus 로고
    • The neuroendocrine control of ovulation
    • Knobil E. The neuroendocrine control of ovulation. Hum Reprod. 1988;3(4):469-72.
    • (1988) Hum Reprod , vol.3 , Issue.4 , pp. 469-472
    • Knobil, E.1
  • 11
    • 69849115040 scopus 로고    scopus 로고
    • Pulse frequency-dependent gonadotropin gene expression by adenylate cyclase-activating polypeptide 1 in perifused mouse pituitary gonadotroph LbetaT2 cells
    • Kanasaki H, Mutiara S, Oride A, Purwana IN, Miyazaki K. Pulse frequency-dependent gonadotropin gene expression by adenylate cyclase-activating polypeptide 1 in perifused mouse pituitary gonadotroph LbetaT2 cells. Biol Reprod. 2009;81(3):465-72.
    • (2009) Biol Reprod , vol.81 , Issue.3 , pp. 465-472
    • Kanasaki, H.1    Mutiara, S.2    Oride, A.3    Purwana, I.N.4    Miyazaki, K.5
  • 12
    • 73949106310 scopus 로고    scopus 로고
    • Regulation of LHa and Egr1 gene expression by GnRH pulses in rat pituitaries is both c-Jun N-terminal kinase (JNK)- and extracellular signal-regulated kinase (ERK)-dependent
    • Burger LL, Halsenleder DJ, Aylor KW, Marshall JC. Regulation of LHa and Egr1 gene expression by GnRH pulses in rat pituitaries is both c-Jun N-terminal kinase (JNK)- and extracellular signal-regulated kinase (ERK)-dependent. Biol Reprod. 2009;81(6):1206-15.
    • (2009) Biol Reprod , vol.81 , Issue.6 , pp. 1206-1215
    • Burger, L.L.1    Halsenleder, D.J.2    Aylor, K.W.3    Marshall, J.C.4
  • 13
    • 75749128630 scopus 로고    scopus 로고
    • Frequencydependent regulation of follicle-stimulating hormone beta by pulsatile gonadotropin-releasing hormone ismediated by functional antagonism of bZIP transcription factors
    • Ciccone NA, Xu SY, Lacza T, Carroll RS, Kaiser UB. Frequencydependent regulation of follicle-stimulating hormone beta by pulsatile gonadotropin-releasing hormone ismediated by functional antagonism of bZIP transcription factors. Mol Cell Biol. 2010;30 (4):1028-40.
    • (2010) Mol Cell Biol , vol.30 , Issue.4 , pp. 1028-1040
    • Ciccone, N.A.1    Xu, S.Y.2    Lacza, T.3    Carroll, R.S.4    Kaiser, U.B.5
  • 14
    • 33846638321 scopus 로고    scopus 로고
    • Reciprocal cross talk between gonadotropin-releasing hormone (GnRH) and prostaglandin receptors regulates GnRH receptor expression and differential gonadotropin secretion
    • DOI 10.1210/me.2006-0253
    • Naor Z, Jabbour HN, NaidichM, Pawson AJ,Morgan K, Battersby S, et al. Reciprocal cross talk between gonadotropin-releasing hormone (GnRH) and prostaglandin receptors regulates GnRH receptor expression and differential gonadotropin secretion. Mol Endocrinol. 2007;21(2):524-37. (Pubitemid 46184900)
    • (2007) Molecular Endocrinology , vol.21 , Issue.2 , pp. 524-537
    • Naor, Z.1    Jabbour, H.N.2    Naidich, M.3    Pawson, A.J.4    Morgan, K.5    Battersby, S.6    Millar, M.R.7    Brown, P.8    Millar, R.P.9
  • 15
  • 16
    • 40849134161 scopus 로고    scopus 로고
    • Non-gonadotropin-releasing hormone-mediated transcription and secretion of large human glycoprotein hormone α-subunit in human embryonic kidney-293 cells
    • DOI 10.1210/en.2007-1529
    • Casella I, Lindner H, Zenzmaler C, Ritano D, Berger P, Costa T. Non-gonadotropin-releasing hormone-mediated transcription and secretions of large human glycoprotein hormone alpha-subunit in human embryonic kidney-293 cells. Endocrinology. 2008;149 (3):1144-54. (Pubitemid 351397933)
    • (2008) Endocrinology , vol.149 , Issue.3 , pp. 1144-1154
    • Casella, I.1    Lindner, H.2    Zenzmaier, C.3    Riitano, D.4    Berger, P.5    Costa, T.6
  • 17
    • 33747846303 scopus 로고    scopus 로고
    • Androgens, progestins, and glucocorticoids induce follicle-stimulating hormone β-subunit gene expression at the level of the gonadotrope
    • DOI 10.1210/me.2005-0316
    • ThackrayVG,McGillivray SM,Mellon PL. Androgens, progestins, and glucocorticoids induce follicle-stimulating hormone betasubunit gene expression at the level of the gonadotrope. Mol Endocrinol. 2006;20(9):2062-79. (Pubitemid 44286705)
    • (2006) Molecular Endocrinology , vol.20 , Issue.9 , pp. 2062-2079
    • Thackray, V.G.1    McGillivray, S.M.2    Mellon, P.L.3
  • 18
    • 66449126366 scopus 로고    scopus 로고
    • Progesterone inhibits basal and gonadotropin-releasing hormone induction of luteinizing hormone beta-subunit gene expression
    • Thackray VG, Hunnicutt JL, Memon AK, Ghochani Y, Mellon PL. Progesterone inhibits basal and gonadotropin-releasing hormone induction of luteinizing hormone beta-subunit gene expression. Endocrinology. 2009;150(5):2395-403.
    • (2009) Endocrinology , vol.150 , Issue.5 , pp. 2395-2403
    • Thackray, V.G.1    Hunnicutt, J.L.2    Memon, A.K.3    Ghochani, Y.4    Mellon, P.L.5
  • 19
    • 67149123561 scopus 로고    scopus 로고
    • Ovarian-steroid modulation of Locus Coeruleus activity in female rats: Involvement in luteinising hormone regulation
    • Szawka RE, Rodovalho GV, Monteiro PM, Carrer HF, Anselmo- Franci JA. Ovarian-steroid modulation of Locus Coeruleus activity in female rats: Involvement in luteinising hormone regulation. J Neuroendocrinol. 2009;21(7):629-39.
    • (2009) J Neuroendocrinol , vol.21 , Issue.7 , pp. 629-639
    • Szawka, R.E.1    Rodovalho, G.V.2    Monteiro, P.M.3    Carrer, H.F.4    Anselmo- Franci, J.A.5
  • 20
    • 79955949750 scopus 로고    scopus 로고
    • Kispeptins and the neuroendocrine control of reproduction
    • Navarro VM, Tena-Sempere M. Kispeptins and the neuroendocrine control of reproduction. Front Biosci (Shol Ed). 2011;3:267-75.
    • Front Biosci (Shol Ed) , vol.2011 , Issue.3 , pp. 267-275
    • Navarro, V.M.1    Tena-Sempere, M.2
  • 21
    • 77950620742 scopus 로고    scopus 로고
    • Gonadotropin inhibitory hormone function in mammals
    • Smith JT, Clarke IJ. Gonadotropin inhibitory hormone function in mammals. Trends Endocrinol Meta. 2010;21(4):255-60.
    • (2010) Trends Endocrinol Meta , vol.21 , Issue.4 , pp. 255-260
    • Smith, J.T.1    Clarke, I.J.2
  • 22
    • 79960555999 scopus 로고    scopus 로고
    • Control of GnRH secretion: One step back
    • Epub(Jan 7)
    • Clarke IJ. Control of GnRH secretion: one step back. Front Neuroendocrinol. 2011;Epub(Jan 7).
    • (2011) Front Neuroendocrinol
    • Clarke, I.J.1
  • 23
    • 77949494829 scopus 로고    scopus 로고
    • Identification of human GnIH homologs, RFRP-1 and RFRP-3, and the congnate receptor, GPR147 in the human hypothalamic pituitary axis
    • Ubuka T, Morgan K, Pawson AJ, Osugi T, Chowdry VS, Minakata H, et al. Identification of human GnIH homologs, RFRP-1 and RFRP-3, and the congnate receptor, GPR147 in the human hypothalamic pituitary axis. PLoS One. 2009;4(12):e8400.
    • (2009) PLoS One , vol.4 , Issue.12
    • Ubuka, T.1    Morgan, K.2    Pawson, A.J.3    Osugi, T.4    Chowdry, V.S.5    Minakata, H.6
  • 24
    • 0024840149 scopus 로고
    • Inhibin, activin, and follistatin: Regulation of follicle-stimulating hormone messenger ribonucleic acid levels
    • Carroll TS, Corrigan AZ, Gharib SD, Vale W, Chin WW. Inhibin, activin, follistatin-regulation of follicle-stimulating hormone messenger-ribonucleic- acid levels. Mol Endocrinol. 1989;3 (12):1969-76. (Pubitemid 20036902)
    • (1989) Molecular Endocrinology , vol.3 , Issue.12 , pp. 1969-1976
    • Carroll, R.S.1    Corrigan, A.Z.2    Gharib, S.D.3    Vale, W.4    Chin, W.W.5
  • 25
    • 41149145126 scopus 로고    scopus 로고
    • Bone morphogenetic protein-4 interacts with activin and GnRH to modulate gonadotrophin secretion in LβT2 gonadotrophs
    • DOI 10.1677/JOE-07-0542
    • Nicol L, Faure MO, McNeilly JR, Fontaine J, Taragnat C, McNeilly AS. Bone morphogenetic protein-4 interacts with activin and GnRH to modulate gonadotrophin secretion in L beta T2 gonadotrophs. J Endocrinol. 2008;196(3):497-507. (Pubitemid 351425505)
    • (2008) Journal of Endocrinology , vol.196 , Issue.3 , pp. 497-507
    • Nicol, L.1    Faure, M.-O.2    McNeilly, J.R.3    Fontaine, J.4    Taragnat, C.5    McNeilly, A.S.6
  • 26
    • 1542330973 scopus 로고    scopus 로고
    • Chorionic gonadotrophin β subunit mRNA but not luteinising hormone β subunit mRNA is expressed in the pituitary of the common marmoset (Callithrix jacchus)
    • DOI 10.1677/jme.0.0320115
    • Muller T, Simoni M, Pekel E, Luetjens CM, Chandolia R, Amato F, 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(1):115-28. (Pubitemid 38312625)
    • (2004) Journal of Molecular Endocrinology , vol.32 , Issue.1 , pp. 115-128
    • Muller, T.1    Simoni, M.2    Pekel, E.3    Luetjens, C.M.4    Chandolia, R.5    Amato, F.6    Norman, R.J.7    Gromoll, J.8
  • 27
    • 38849163585 scopus 로고    scopus 로고
    • Molecular cloning of pituitary glycoprotein α-subunit and follicle stimulating hormone and chorionic gonadotropin β-subunits from New World squirrel monkey and owl monkey
    • DOI 10.1016/j.ygcen.2007.08.004, PII S0016648007003061
    • Scammell JG, Funkhouser JD, Moyer FS, Gibson SV, Willis DL. Molecular cloning of pituitary glycoprotein a-subunit and follicle stimulating hormone and chorionic gonadotropin ß- subunits from new world squirrel mnokey and owl monkey. Gen Comp Endocrinol. 2008;155(3):534-41. (Pubitemid 351191908)
    • (2008) General and Comparative Endocrinology , vol.155 , Issue.3 , pp. 534-541
    • Scammell, J.G.1    Funkhouser, J.D.2    Moyer, F.S.3    Gibson, S.V.4    Willis, D.L.5
  • 28
    • 0029959986 scopus 로고    scopus 로고
    • Isolation and characterization of human pituitary chorionic gonadotropin
    • DOI 10.1210/en.137.4.1402
    • Birken S, Maydelman Y, Gawinowicz MA, Pound A, Liu Y, Hartree AS. Isolation and characterization of human pituitary chorionic gonadotropin. Endocrinology. 1996;137(4):1402-11. (Pubitemid 26095259)
    • (1996) Endocrinology , vol.137 , Issue.4 , pp. 1402-1411
    • Birken, S.1    Maydelman, Y.2    Gawinowicz, M.A.3    Pound, A.4    Liu, Y.5    Hartree, A.S.6
  • 30
    • 0021739703 scopus 로고
    • A kinetic comparison of the processing and secretion of the αβ dimer and the uncombined α and β subunits of chorionic gonadotropin synthesized by human choriocarcinoma cells
    • Peters BP, Krzesicki RF, Hartle RJ, Perini F, Ruddon RW. A kinetic comparison of the processing and secretion of the aß dimer and the uncombined a and ß subunits of chorionic gonadotropin synthesized by human choriocarcinoma cells. J Biol Chem. 1984;259(24):15123-30. (Pubitemid 15191311)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.24 , pp. 15123-15130
    • Peters, B.P.1    Krzesicki, R.F.2    Hartle, R.J.3
  • 31
    • 0019974454 scopus 로고
    • Thyroid-stimulating hormone subunit processing and combination in microsomal subfractions of mouse pituitary tumor
    • Magner JA, Weintraub BD. Thyroid-stimulating hormone subunit processing and combination in microsomal subfractions of mouse pituitary tumor. J Biol Chem. 1982;257(12):6709-15. (Pubitemid 12022267)
    • (1982) Journal of Biological Chemistry , vol.257 , Issue.12 , pp. 6709-6715
    • Magner, J.A.1    Weintraub, B.D.2
  • 32
    • 0021099901 scopus 로고
    • Imbalanced synthesis of human choriogonadotropin alpha and beta subunits reflects the steady state levels of the corresponding mRNAs
    • Boothby M, Kukowaska J, Boime I. Imbalanced synthesis of human choriogonadotropin alpha and beta subunits reflects the steady state levels of the corresponding mRNAs. J Biol Chem. 1983;258(15):9250-3.
    • (1983) J Biol Chem , vol.258 , Issue.15 , pp. 9250-9253
    • Boothby, M.1    Kukowaska, J.2    Boime, I.3
  • 33
    • 12744279354 scopus 로고    scopus 로고
    • Endocrinology: Fertility hormone in repose
    • Dias JA. Endocrinology: Fertility hormone in repose. Nature. 2005;433(7023):203-4.
    • (2005) Nature , vol.433 , Issue.7023 , pp. 203-204
    • Dias, J.A.1
  • 34
    • 23944524663 scopus 로고    scopus 로고
    • Glycoprotein hormones tied but not tethered like other cysteine-knot cytokines
    • DOI 10.1016/j.tips.2005.07.005, PII S016561470500177X
    • Krystek SR, Dias JA. Glycoprotein hormones tied but not tethered like other cysteine-knot cytokines. Trends Pharmacol Sci. 2005;26(9):439-42. (Pubitemid 41207874)
    • (2005) Trends in Pharmacological Sciences , vol.26 , Issue.9 , pp. 439-442
    • Krystek Jr., S.R.1    Dias, J.A.2
  • 36
    • 0028773646 scopus 로고
    • Structure of human chorionic gonadotropin at 2.6Å resolution from MAD analysis of the selenomethionyl protein
    • Wu H, Lustbader JW, Liu Y, Canfield RE, Hendrickson WA. Structure of human chorionic gonadotropin at 2.6Å resolution from MAD analysis of the selenomethionyl protein. Structure. 1994;2:545-58.
    • (1994) Structure , vol.2 , pp. 545-558
    • Wu, H.1    Lustbader, J.W.2    Liu, Y.3    Canfield, R.E.4    Hendrickson, W.A.5
  • 37
    • 0035105355 scopus 로고    scopus 로고
    • Three-dimensional structure of human follicle-stimulating hormone
    • DOI 10.1210/me.15.3.378
    • Fox KM, Dias JA, Van Roey P. Three-dimensional structure of human follicle-stimulating hormone. Mol Endocrinol. 2001;15:378-89. (Pubitemid 32221915)
    • (2001) Molecular Endocrinology , vol.15 , Issue.3 , pp. 378-389
    • Fox, K.M.1    Dias, J.A.2    Van Roey, P.3
  • 38
    • 4143088137 scopus 로고    scopus 로고
    • Glycoprotein hormone assembly in the endoplasmic reticulum: I. The glycosylated end of human α-subunit loop 2 is threaded through a β-subunit hole
    • DOI 10.1074/jbc.M403052200
    • Xing Y, Myers R, Cao D, Lin W, Jiang M, Bernard M, 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(34):35426-36. (Pubitemid 39100542)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.34 , pp. 35426-35436
    • Xing, Y.1    Myers, R.V.2    Cao, D.3    Lin, W.4    Jiang, M.5    Bernard, M.P.6    Moyle, W.R.7
  • 39
    • 4143090403 scopus 로고    scopus 로고
    • Glycoprotein hormone assembly in the endoplasmic reticulum: II. Multiple roles of a redox sensitive β-subunit disulfide switch
    • DOI 10.1074/jbc.M403053200
    • Xing Y, Myers R, Cao D, Lin W, Jiang M, Bernard M, 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(34):35437-48. (Pubitemid 39100543)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.34 , pp. 35437-35448
    • Xing, Y.1    Myers, R.V.2    Cao, D.3    Lin, W.4    Jiang, M.5    Bernard, M.P.6    Moyle, W.R.7
  • 40
    • 0025689177 scopus 로고
    • N-linked oligosaccharides on free a interfere with its ability to combine with human chorionic gonadotropin-β subunit
    • Blithe DL. N-linked oligosaccharides on free a interfere with its ability to combine with human chorionic gonadotropin-ß subunit. J Biol Chem. 1990;265:21951-6. (Pubitemid 120014248)
    • (1990) Journal of Biological Chemistry , vol.265 , Issue.35 , pp. 21951-21956
    • Blithe, D.L.1
  • 41
    • 0031933747 scopus 로고    scopus 로고
    • 56 oligosaccharide on in vitro subunit association and follicle-stimulating hormone receptor binding of equine gonadotropins
    • DOI 10.1095/biolreprod58.2.458
    • Butnev VY, Gotschall RR, Butnev VY, Baker VL, Moore WT, Bousfield GR. Hormone-specific inhibitory influence of a- subunit Asn56 oligosaccharide on in vitro subunit association and FSH receptor binding of equine gonadotropins. Biol Reprod. 1998;58(2):458-69. (Pubitemid 28099112)
    • (1998) Biology of Reproduction , vol.58 , Issue.2 , pp. 458-469
    • Butnev, V.Y.1    Gotschall, R.R.2    Butnev, V.Y.3    Baker, V.L.4    Moore, W.T.5    Bousfield, G.R.6
  • 42
    • 0037470737 scopus 로고    scopus 로고
    • Efficient preparation of glycoprotein hormones lacking an α-subunit oligosaccharide
    • DOI 10.1016/S0006-291X(03)00322-X
    • Xing Y, Moyle WR. Efficient preparation of glycoprotein hormones lacking an alpha-subunit oligosaccharide. Biochem Biophys Res Commun. 2003;303(1):201-5. (Pubitemid 36338227)
    • (2003) Biochemical and Biophysical Research Communications , vol.303 , Issue.1 , pp. 201-205
    • Xing, Y.1    Moyle, W.R.2
  • 43
    • 4143052436 scopus 로고    scopus 로고
    • Glycoprotein hormone assembly in the endoplasmic reticulum: III. The seatbelt and its latch site determine the assembly pathway
    • DOI 10.1074/jbc.M403054200
    • Xing Y, Myers R, Cao D, Lin W, Jiang M, Bernard M, 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(34):35449-57. (Pubitemid 39100544)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.34 , pp. 35449-35457
    • Xing, Y.1    Myers, R.V.2    Cao, D.3    Lin, W.4    Jiang, M.5    Bernard, M.P.6    Moyle, W.R.7
  • 44
    • 4143117844 scopus 로고    scopus 로고
    • Glycoprotein hormone assembly in the endoplasmic reticulum: IV. Probable mechanism of subunit docking and completion of assembly
    • DOI 10.1074/jbc.M403055200
    • Xing Y, Myers R, Cao D, Lin W, Jiang M, Bernard M, et al. Glycoprotein hormone assembly in the endoplasmic reticulum: IV. Probable mechanism of subunit docking and completion of assembly. J Biol Chem. 2004;279(34):35458-68. (Pubitemid 39100545)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.34 , pp. 35458-35468
    • Xing, Y.1    Myers, R.V.2    Cao, D.3    Lin, W.4    Jiang, M.5    Bernard, M.P.6    Moyle, W.R.7
  • 45
    • 84855710332 scopus 로고    scopus 로고
    • Polarized secretion of gonadotropins by transfected MDCK cells
    • Jablonka-Shariff A, Pixley M, Boime I. Polarized secretion of gonadotropins by transfected MDCK cells. Mol Biol Cell. 2000;11:1654.
    • (2000) Mol Biol Cell , vol.11 , pp. 1654
    • Jablonka-Shariff, A.1    Pixley, M.2    Boime, I.3
  • 46
    • 0037059830 scopus 로고    scopus 로고
    • Evolution of lutropin to chorionic gonadotropin generates a specific routing signal for apical release in vivo
    • DOI 10.1074/jbc.C100402200
    • 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(2):879-82. (Pubitemid 34968829)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.2 , pp. 879-882
    • Jablonka-Shariff, A.1    Garcia-Campayo, V.2    Boime, I.3
  • 47
    • 61449158735 scopus 로고    scopus 로고
    • Secretory trafficking signal encoded in the carboxyl-terminal region of the CG betasubunit
    • Jablonka-Shariff A, Boime I. Secretory trafficking signal encoded in the carboxyl-terminal region of the CG betasubunit. Mol Endocrinol. 2009;23(3):316-23.
    • (2009) Mol Endocrinol , vol.23 , Issue.3 , pp. 316-323
    • Jablonka-Shariff, A.1    Boime, I.2
  • 48
    • 1242298811 scopus 로고    scopus 로고
    • Luteinizing Hormone and Follicle-Stimulating Hormone Exhibit Different Secretion Patterns from Cultured Madin-Darby Canine Kidney Cells
    • DOI 10.1095/biolreprod.103.022699
    • Jablonka-Shariff A, Boime I. Luteinizing hormone and folliclestimulating hormone exhibit different secretion patterns from cultured Madin-Darby canine kidney cells. Biol Reprod. 2004;70 (3):649-55. (Pubitemid 38233702)
    • (2004) Biology of Reproduction , vol.70 , Issue.3 , pp. 649-655
    • Jablonka-Shariff, A.1    Boime, I.2
  • 49
    • 45549085836 scopus 로고    scopus 로고
    • A carboxylterminal sequence in the lutropin beta subunit contributes to the sorting of lutropin to the regulated pathway
    • Jablonka-Shariff A, Pearl CA, Comstock A, Boime I. A carboxylterminal sequence in the lutropin beta subunit contributes to the sorting of lutropin to the regulated pathway. J Biol Chem. 2008;283 (17):11485-92.
    • (2008) J Biol Chem , vol.283 , Issue.17 , pp. 11485-11492
    • Jablonka-Shariff, A.1    Pearl, C.A.2    Comstock, A.3    Boime, I.4
  • 50
    • 73649107301 scopus 로고    scopus 로고
    • Rerouting of a folliclestimulating hormone analog to the regulated secretory pathway
    • Pearl CA, Jablonka-Shariff A, Boime I. Rerouting of a folliclestimulating hormone analog to the regulated secretory pathway. Endocrinology. 2010;151(1):388-93.
    • (2010) Endocrinology , vol.151 , Issue.1 , pp. 388-393
    • Pearl, C.A.1    Jablonka-Shariff, A.2    Boime, I.3
  • 51
    • 46449127677 scopus 로고    scopus 로고
    • Disruption of lipid rafts induces gonadotropin release in ovine pituitary and LbetaT2 gonadotroph cells
    • DOI 10.1095/biolreprod.107.064881
    • Robin E, Cognie J, Foulon-Gauze F, Fontaine J, Cayla X. Disruption of lipid rafts induces gonadotropin release in ovine pituitary and LbetaT2 gonadotroph cells. Biol Reprod. 2008;79 (1):17-25. (Pubitemid 351931036)
    • (2008) Biology of Reproduction , vol.79 , Issue.1 , pp. 17-25
    • Robin, E.1    Cognie, J.2    Foulon-Gauze, F.3    Fontaine, J.4    Cayla, X.5
  • 52
    • 0025976986 scopus 로고
    • NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin
    • Weisshaar G, Hiyama J, Renwick AGC, Nimtz M. NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin. Eur J Biochem. 1991;195:257-68.
    • (1991) Eur J Biochem , vol.195 , pp. 257-268
    • Weisshaar, G.1    Hiyama, J.2    Renwick, A.G.C.3    Nimtz, M.4
  • 53
    • 0016304913 scopus 로고
    • The isolation and properties of a rabbit liver binding protein specific for asialoglycoproteins
    • Hudgin RL, Pricer Jr.WE, Ashwell G, Stockert RJ, Morell AG. The isolation and properties of a rabbit liver binding protein specific for asialoglycoproteins. J Biol Chem. 1974;249:5536-43.
    • (1974) J Biol Chem , vol.249 , pp. 5536-5543
    • Hudgin, R.L.1    Pricer, Jr.W.E.2    Ashwell, G.3    Stockert, R.J.4    Morell, A.G.5
  • 54
    • 0015217323 scopus 로고
    • The role of sialic acid in determining the survival of glycoproteins in the circulation
    • Morell AG, Gregoriadis G, Scheinberg IH, Hickman J, Ashwell G. The role of sialic acid in determining the survival of glycoproteins in the circulation. J Biol Chem. 1971;246:1461-7.
    • (1971) J Biol Chem , vol.246 , pp. 1461-1467
    • Morell, A.G.1    Gregoriadis, G.2    Scheinberg, I.H.3    Hickman, J.4    Ashwell, G.5
  • 55
    • 0021159599 scopus 로고
    • Evidence that desialylation and uptake by hepatic receptors for galactose-terminated glycoproteins are immaterial to the metabolism of human choriogonadotropin in the rat
    • Lefort GP, Stolk JM, Nisula BC. Evidence that desialylation and uptake by hepatic receptors for galactose-terminated glycoproteins are immaterial to the metabolism of human choriogonadotropin in the rat. Endocrinology. 1984;115(4):1551-7. (Pubitemid 14000325)
    • (1984) Endocrinology , vol.115 , Issue.4 , pp. 1551-1557
    • Lefort, G.P.1    Stolk, J.M.2    Nisula, B.C.3
  • 56
    • 0023930204 scopus 로고
    • Asparagine-linked oligosaccharides on lutropin, follitropin, and thyrotropin. II. Distributions of sulfated and sialylated oligosaccharides on bovine, ovine, and human pituitary glycoprotein hormones
    • Green ED, Baenziger JU. Asparagine-linked oligosaccharides on lutropin, follitropin, and thyrotropin II. Distributions of sulfated and sialylated oligosaccharides on bovine, ovine, and human pituitary glycoprotein hormones. J Biol Chem. 1988;263:36-44. (Pubitemid 18041039)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.1 , pp. 36-44
    • Green, E.D.1    Baenziger, J.U.2
  • 59
    • 0026314891 scopus 로고
    • 4-4GalNAcβ1,4GlcNAcβ1,2Manα that mediates rapid clearance of lutropin
    • Fiete D, Srivastava V, Hindsgaul O, Baenziger JU. A hepatic reticuloendothelial cell receptor specific for SO4-4Gal- NAcß1, 4GlcNAcß1,2Mana that mediates rapid clearance of lutropin. Cell. 1991;67:1103-10. (Pubitemid 121001523)
    • (1991) Cell , vol.67 , Issue.6 , pp. 1103-1110
    • Fiele, D.1    Srivastava, V.2    Hindsgaul, O.3    Baenziger, J.U.4
  • 60
    • 67651149519 scopus 로고    scopus 로고
    • Sulfation of LH does not affect intracellular trafficking
    • Pearl CA, Boime I. Sulfation of LH does not affect intracellular trafficking. Mol Cell Endocrinol. 2009;309(1-2):76-81.
    • (2009) Mol Cell Endocrinol , vol.309 , Issue.1-2 , pp. 76-81
    • Pearl, C.A.1    Boime, I.2
  • 61
    • 0023928616 scopus 로고
    • Asparagine-linked oligosaccharides on lutropin, follitropin, and thyrotropin. I. Structural elucidation of the sulfated and sialylated oligosaccharides on bovine, ovine, and human pituitary glycoprotein hormones
    • Green ED, Baenziger JU. Asparagine-linked oligosaccharides on lutropin, follitropin, and thyrotropin: I. structural elucidation of the sulfated and sialylated oligosaccharides on bovine, ovine and human pituitary glycoprotein hormones. J Biol Chem. 1988;263:25-35. (Pubitemid 18041038)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.1 , pp. 25-35
    • Green, E.D.1    Baenziger, J.U.2
  • 62
    • 33746034592 scopus 로고    scopus 로고
    • Comparative glycomics of the glycoprotein follicle stimulating hormone: Glycopeptide analysis of isolates from two mammalian species
    • DOI 10.1021/bi060435k
    • Dalpathado DS, Irungu JA, Go EP, Butnev VY, Norton K, Bousfield GR, et al. Comparative glycomics of the glycoprotein hormone follicle-stimulating hormone (FSH): Glycopeptide analysis of isolates from two mammalian species. Biochemistry. 2006;45(28):8665-73. (Pubitemid 44078887)
    • (2006) Biochemistry , vol.45 , Issue.28 , pp. 8665-8673
    • Dalpathado, D.S.1    Irungu, J.2    Go, E.P.3    Butnev, V.Y.4    Norton, K.5    Bousfield, G.R.6    Desaire, H.7
  • 63
    • 4344574965 scopus 로고    scopus 로고
    • Fast renal trapping of porcine luteinizing hormone (pLH) shown by 123I-scintigraphic imaging in rats explains its short circulatory half-life
    • Klett D, Bernard S, Lecompte F, Leroux H, Magallon T, Locatelli A, et al. Fast renal trapping of porcine luteinizing hormone (pLH) shown by 123I-scintigraphic imaging in rats explains its short circulatory half-life. Reprod Biol Endocrinol. 2003;1:64.
    • (2003) Reprod Biol Endocrinol , vol.1 , pp. 64
    • Klett, D.1    Bernard, S.2    Lecompte, F.3    Leroux, H.4    Magallon, T.5    Locatelli, A.6
  • 65
    • 0025043857 scopus 로고
    • Isolation and structure determination of the intact sialylated N-linked carbohydrate chains of recombinant human follitropin expressed in Chinese hamster ovary cells
    • Hard K, Mekking A, Damm JB, Kammerling JP, De Boer W, Wijnands RA, et al. Isolation and structure determination of the intact sialylated N-linked carbohydrate chains of recombinant human follitropin expressed in Chinese hamster ovary cells. Eur J Biochem. 1990;193(1):263-71. (Pubitemid 20331638)
    • (1990) European Journal of Biochemistry , vol.193 , Issue.1 , pp. 263-271
    • Hard, K.1    Mekking, A.2    Damm, J.B.L.3    Kamerling, J.P.4    De Boer, W.5    Wijnands, R.A.6    Vliegenthart, J.F.G.7
  • 66
    • 0028878246 scopus 로고
    • Pharmacokinetics of recombinant human luteinizing hormone after intravenous, intramuscular, and subcutaneous administration in monkeys and comparison with intravenous administration of pituitary human luteinizing hormone
    • Porchet HC, Le Cotonnec JY, Neuteboom B, Canali S, Zanolo G. Pharmacokinetics of recombinant human luteinizing hormone after intravenous, intramuscular, and subcutaneous administration in monkeys and comparison with intravenous administration of pituitary human luteinizing hormone. J Clin Endocrinol Metab. 1995;80(2):667-73.
    • (1995) J Clin Endocrinol Metab , vol.80 , Issue.2 , pp. 667-673
    • Porchet, H.C.1    Le Cotonnec, J.Y.2    Neuteboom, B.3    Canali, S.4    Zanolo, G.5
  • 67
    • 38949180281 scopus 로고    scopus 로고
    • Chromatofocusing fails to separate hFSH isoforms on the basis of glycan structure
    • DOI 10.1021/bi701764w
    • Bousfield GR, Butnev VY, Bidart JM, Dalpathado D, Irungu J, Desaire H. Chromatofocusing fails to separate hFSH isoforms on the basis of glycan structure. Biochemistry. 2008;47(6):1708-20. (Pubitemid 351231220)
    • (2008) Biochemistry , vol.47 , Issue.6 , pp. 1708-1720
    • Bousfield, G.R.1    Butnev, V.Y.2    Bidart, J.-M.3    Dalpathado, D.4    Irungu, J.5    Desaire, H.6
  • 69
    • 0023179051 scopus 로고
    • The asparagine-linked sugar chains of human follicle-stimulating hormone
    • Renwick AGC, Mizuochi T, Kochibe N, Kobata A. The asparagine-linked sugar chains of human follicle-stimulating hormone. J Biochem. 1987;101:1209-21. (Pubitemid 17060307)
    • (1987) Journal of Biochemistry , vol.101 , Issue.5 , pp. 1209-1221
    • Renwick, A.G.C.1    Mizuochi, T.2    Kochibe, N.3    Kobata, A.4
  • 70
    • 25144501600 scopus 로고    scopus 로고
    • The animal sialyltransferases and sialyltransferase-related genes: A phylogenetic approach
    • DOI 10.1093/glycob/cwi063
    • Harduin-Lepers A, Mollicone R, Delannoy P, Oriol R. The animal sialyltransferases and sialyltransferase-related genes: A phylogenetic approach. Glycobiology. 2005;15(8):805-17. (Pubitemid 41417983)
    • (2005) Glycobiology , vol.15 , Issue.8 , pp. 805-817
    • Harduin-Lepers, A.1    Mollicone, R.2    Delannoy, P.3    Oriol, R.4
  • 71
    • 60149097254 scopus 로고    scopus 로고
    • Derivatization of sialic acids for stabilization in matrix-assistes laser desorption/ionization mass spectrometry and concomitant differentiation of a(2-3)- and a(2-6)-isomers
    • Wheeler SF, Domann P, Havey DJ. Derivatization of sialic acids for stabilization in matrix-assistes laser desorption/ionization mass spectrometry and concomitant differentiation of a(2-3)- and a(2-6)-isomers. Rapid Commun Mass Spectrom. 2009;23:303-12.
    • (2009) Rapid Commun Mass Spectrom , vol.23 , pp. 303-312
    • Wheeler, S.F.1    Domann, P.2    Havey, D.J.3
  • 72
    • 60149097254 scopus 로고    scopus 로고
    • Derivatization of sialic acids for stabilization in matrix-assisted laser desorption/ionization mass spectrometry and concomitant differentiation of alpha(2 ->3)- and alpha(2 -> 6)-isomers
    • doi:10.1002/rcm.3867
    • Wheeler SF, Domann P, Harvey DJ. Derivatization of sialic acids for stabilization in matrix-assisted laser desorption/ionization mass spectrometry and concomitant differentiation of alpha(2 ->3)- and alpha(2 ->6)-isomers. Rapid Commun Mass Spectrom. 2009;23 (2):303-12. doi:10.1002/rcm.3867.
    • (2009) Rapid Commun Mass Spectrom , vol.23 , Issue.2 , pp. 303-312
    • Wheeler, S.F.1    Domann, P.2    Harvey, D.J.3
  • 73
    • 30944467214 scopus 로고    scopus 로고
    • The molecular basis of coupling of translocation and N-glycosylation
    • DOI 10.1016/j.tibs.2005.11.010, PII S0968000405003385
    • Chavan M, Lennarz W. The molecular basis of coupling of translocation and N-glycosylation. Trends Biochem Sci. 2006;31 (1):17-20. (Pubitemid 43117537)
    • (2006) Trends in Biochemical Sciences , vol.31 , Issue.1 , pp. 17-20
    • Chavan, M.1    Lennarz, W.2
  • 74
    • 33645103490 scopus 로고    scopus 로고
    • An evolving view of the eukaryotic oligosaccharyltransferase
    • Kelleher DJ, Gilmore R. An evolving view of the eukaryotic oligosaccharyltransferase. Glycobiology. 2006;16(4):47R-62.
    • (2006) Glycobiology , vol.16 , Issue.4
    • Kelleher, D.J.1    Gilmore, R.2
  • 75
    • 0034886490 scopus 로고    scopus 로고
    • Characterization of human FSH isoforms reveals a nonglycosylated β-subunit in addition to the conventional glycosylated β-subunit
    • DOI 10.1210/jc.86.8.3675
    • Walton WJ, Nguyen VT, Butnev VY, Singh V, Moore WT, Bousfield GR. Characterization of human follicle-stimulating hormone isoforms reveals a non-glycosylated ß-subunit In addition to the conventional glycosylated ß-subunit. J Clin Endocrinol Metab. 2001;86:3675-85. (Pubitemid 32755960)
    • (2001) Journal of Clinical Endocrinology and Metabolism , vol.86 , Issue.8 , pp. 3675-3685
    • Walton, W.J.1    Nguyen, V.T.2    Butnev, V.Y.3    Singh, V.4    Moore, W.T.5    Bousfield, G.R.6
  • 76
    • 13544268336 scopus 로고    scopus 로고
    • Unraveling the mechanism of protein Nglycosylation
    • Yan A, Lennarz WJ. Unraveling the mechanism of protein Nglycosylation. J Biol Chem. 2005;280(5):3121-4.
    • (2005) J Biol Chem , vol.280 , Issue.5 , pp. 3121-3124
    • Yan, A.1    Lennarz, W.J.2
  • 77
    • 58249093866 scopus 로고    scopus 로고
    • Cotranslational and posttranslational N-glycosylation of polyppetides by distinct mammalian OST isoforms
    • Ruiz-Canada C, Kelleher DJ, Gilmore R. Cotranslational and posttranslational N-glycosylation of polyppetides by distinct mammalian OST isoforms. Cell. 2009;136(2):272-83.
    • (2009) Cell , vol.136 , Issue.2 , pp. 272-283
    • Ruiz-Canada, C.1    Kelleher, D.J.2    Gilmore, R.3
  • 79
    • 0033860694 scopus 로고    scopus 로고
    • Evidence for interaction of yeast protein kinase C with several subunits of oligosaccharyl transferase
    • Park H, Lennarz WJ. Evidence for interaction of yeast protein kinase C with several subunits of oligosaccharyl transferase. Glycobiology. 2000;10(7):737-44. (Pubitemid 30616207)
    • (2000) Glycobiology , vol.10 , Issue.7 , pp. 737-744
    • Park, H.1    Lennarz, W.J.2
  • 80
    • 28444451884 scopus 로고    scopus 로고
    • Two oligosaccharyl transferase complexes exist in yeast and associate with two different translocons
    • DOI 10.1093/glycob/cwj026
    • Yan A, Lennarz W. Two oligosaccharyl tranferase complexes exist in yeast and associate with two different translocons. Glycobiology. 2005;15(12):1407-15. (Pubitemid 41724345)
    • (2005) Glycobiology , vol.15 , Issue.12 , pp. 1407-1415
    • Yan, A.1    Lennarz, W.J.2
  • 81
    • 0038294237 scopus 로고    scopus 로고
    • Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties
    • DOI 10.1016/S1097-2765(03)00243-0
    • Kelleher DJ, Karaoglu D, Mandon EC, Gilmore R. Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties. Mol Cell. 2003;12:101-11. (Pubitemid 36945039)
    • (2003) Molecular Cell , vol.12 , Issue.1 , pp. 101-111
    • Kelleher, D.J.1    Karaoglu, D.2    Mandon, E.C.3    Gilmore, R.4
  • 82
    • 0028566990 scopus 로고
    • Secretion of lutropin and follitropin from transfected GH3 cells: Evidence for separate secretory pathways
    • Muyan M, Ryzmkiewicz DM, Boime I. Secretion of lutropin and follitropin from transfected GH3 cells: Evidence for separate secretory pathways. Mol Endocrinol. 1994;8:1789-97.
    • (1994) Mol Endocrinol , vol.8 , pp. 1789-1797
    • Muyan, M.1    Ryzmkiewicz, D.M.2    Boime, I.3
  • 83
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • DOI 10.1146/annurev.biochem.73.011303.073752
    • Helenius A, Aebi M. Roles of N-linked glycans in the endoplasmic reticulum. Annu Rev Biochem. 2004;73:1019-49. (Pubitemid 39050393)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 84
    • 0028012014 scopus 로고
    • Mice lacking N-acetylglucosaminyltransferase I activity die at mid-gestation, revealing an essential role for complex or hybrid N-linked carbohydrates
    • Ioffe E, Stanley P. Mice lacking N-acetylglucosaminyltransferase I activity die at mid-gestation, revealing an essential role for complex or hybrid N-linked carbohydrates. Proc Natl Acad Sci USA. 1994;91(2):728-32.
    • (1994) Proc Natl Acad Sci USA , vol.91 , Issue.2 , pp. 728-732
    • Ioffe, E.1    Stanley, P.2
  • 85
    • 62449297943 scopus 로고    scopus 로고
    • Oocyte -specific deletion of complex and N-glycans leads to defects in preovulatory and cumulus mass development
    • Williams SA, Stanley P. Oocyte -specific deletion of complex and N-glycans leads to defects in preovulatory and cumulus mass development. Reproduction. 2009;137:321-31.
    • (2009) Reproduction , vol.137 , pp. 321-331
    • Williams, S.A.1    Stanley, P.2
  • 87
    • 77951072143 scopus 로고    scopus 로고
    • The bisecting GlcNAc on N-glycans inhibits growth factor signaling and retards mammary tumor progression
    • Song Y, Aglipay JA, Goswami S, Stanley P. The bisecting GlcNAc on N-glycans inhibits growth factor signaling and retards mammary tumor progression. Cancer Res. 2010;70(8):3361-71.
    • (2010) Cancer Res , vol.70 , Issue.8 , pp. 3361-3371
    • Song, Y.1    Aglipay, J.A.2    Goswami, S.3    Stanley, P.4
  • 88
    • 67649859659 scopus 로고    scopus 로고
    • The role of N-acetylglycosaminyltransferase III and V in post-transcriptional modifications of E-cadherin
    • Pinho SS, Teis CS, Paredes J, Magalhaes AM, Ferreira AC, Figueiredo J, et al. The role of N-acetylglycosaminyltransferase III and V in post-transcriptional modifications of E-cadherin. Hum Mol Genet. 2009;18(14):2599-608.
    • (2009) Hum Mol Genet , vol.18 , Issue.14 , pp. 2599-2608
    • Pinho, S.S.1    Teis, C.S.2    Paredes, J.3    Magalhaes, A.M.4    Ferreira, A.C.5    Figueiredo, J.6
  • 89
    • 4644307096 scopus 로고    scopus 로고
    • Effects of galectin-1 on regulation of progesterone production in granulosa cells from pig ovaries in vitro
    • DOI 10.1093/glycob/cwh101
    • Walzel H, Brock J, Pohland R, Vanselow J, Tomek W, Schneider F, et al. Effects of galectin-1 on regulation of progesterone production in granulosa cells from pig ovaries in vitro. Glycobiology. 2004;14(10):871-81. (Pubitemid 39264012)
    • (2004) Glycobiology , vol.14 , Issue.10 , pp. 871-881
    • Walzel, H.1    Brock, J.2    Pohland, R.3    Vanselow, J.4    Tomek, W.5    Schneider, F.6    Tiemann, U.7
  • 90
    • 77952302417 scopus 로고    scopus 로고
    • Physiological and glycomic characterization of Nacetylglycosaminyltransferase- IVa and -IVb double deficient mice
    • Takamatsu S, Antonopoulos A, Ohtsubo K, Ditto D, Chiba Y, Le DT, et al. Physiological and glycomic characterization of Nacetylglycosaminyltransferase- IVa and -IVb double deficient mice. Glycobiology. 2010;20(4):485-97.
    • (2010) Glycobiology , vol.20 , Issue.4 , pp. 485-497
    • Takamatsu, S.1    Antonopoulos, A.2    Ohtsubo, K.3    Ditto, D.4    Chiba Y Le, D.T.5
  • 91
    • 0037137493 scopus 로고    scopus 로고
    • UDP-N-acetylglucosamine: Alpha-6-D-mannoside beta1,6 Nacetylglucosaminyltransferase V (Mgat5) deficient mice
    • Dennis JW, Pawling J, Cheung P, Partdige E, Demetriou M. UDP-N-acetylglucosamine: Alpha-6-D-mannoside beta1,6 Nacetylglucosaminyltransferase V (Mgat5) deficient mice. Biochim Biophys Acta. 2002;1573(3):414-22.
    • (2002) Biochim Biophys Acta , vol.1573 , Issue.3 , pp. 414-422
    • Dennis, J.W.1    Pawling, J.2    Cheung, P.3    Partdige, E.4    Demetriou, M.5
  • 93
    • 77955818331 scopus 로고    scopus 로고
    • Biological functions of hCG and hCG-related molecules
    • Cole LA. Biological functions of hCG and hCG-related molecules. Reprod Biol Endocrinol. 2010;8:102.
    • (2010) Reprod Biol Endocrinol , vol.8 , pp. 102
    • Cole, L.A.1
  • 95
    • 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-γ
    • DOI 10.1210/en.2007-0286
    • Handschuh K, Guibourdenche J, Tsatsaris V, Guesnon M, Laurendeau I, Evain-Brion D, 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;149(10):5011-9. (Pubitemid 47481552)
    • (2007) Endocrinology , vol.148 , Issue.10 , pp. 5011-5019
    • Handschuh, K.1    Guibourdenche, J.2    Tsatsaris, V.3    Guesnon, M.4    Laurendeau, I.5    Evain-Brion, D.6    Fournier, T.7
  • 96
    • 18344364663 scopus 로고    scopus 로고
    • Differential expression of human chorionic gonadotropin (hCG) glycosylation isoforms in failing and continuing pregnancies: Preliminary characterization of the hyperglycosylated hCG epitope
    • DOI 10.1677/joe.0.1720497
    • Kovalevskaya G, Birken S, Kakuma T, Ozaki N, Sauer M, Lindheim S, et al. Differential expression of human chorinonic gonadotropin (hCG) glycosylation isoforms in failing and continuing pregnancies: Preliminary characterization of the hyperglycosylated hCG epitope. J Endocrinol. 2002;172:497-506. (Pubitemid 34232691)
    • (2002) Journal of Endocrinology , vol.172 , Issue.3 , pp. 497-506
    • Kovalevskaya, G.1    Birken, S.2    Kakuma, T.3    Ozaki, N.4    Sauer, M.5    Lindheim, S.6    Cohen, M.7    Kelly, A.8    Schlatterer, J.9    O'Connor, J.F.10
  • 97
    • 33751383272 scopus 로고    scopus 로고
    • Site-specific glycan analysis of human chorionic gonadotropin β-subunit from malignancies and pregnancy by liquid chromatography - Electrospray mass spectrometry
    • DOI 10.1093/glycob/cwl034
    • Valmu L, Alfthan H, Hotakainen K, Birken S, Stenman UH. Site-specific glycan analysis of human chorionic gonadotropin beta-subunit from malignancies and pregnancy by liquid chromatography-electrospray mass spectrometry. Glycobiology. 2006;16(12):1207-18. (Pubitemid 44811584)
    • (2006) Glycobiology , vol.16 , Issue.12 , pp. 1207-1218
    • Valmu, L.1    Alfthan, H.2    Hotakainen, K.3    Birken, S.4    Stenman, U.-H.5
  • 98
    • 0030982537 scopus 로고    scopus 로고
    • Glycosylation variants of human TSH selectively activate signal transduction pathways
    • DOI 10.1016/S0303-7207(97)00136-6, PII S0303720797001366
    • Schaaf L, Leiprecht A, Saji M, Huber U, Usadel KH, Kohn LD. Glycosylation variants of human TSH selectively activate signal transduction pathways. Mol Cell Endocrinol. 1997;132:185-94. (Pubitemid 27420313)
    • (1997) Molecular and Cellular Endocrinology , vol.132 , Issue.1-2 , pp. 185-194
    • Schaaf, L.1    Leiprecht, A.2    Saji, M.3    Hubner, U.4    Usadel, K.H.5    Kohn, L.D.6
  • 101
    • 4344581396 scopus 로고    scopus 로고
    • FSH isoform composition of commercial gonadotrophin preparations: A neglected aspect?
    • Andersen CY, Westergaard LG, van Wely M. FSH isoform composition of commercial gonadotrophin preparations: A neglected aspect? Reprod Biomed Online. 2004;9(2):231-6. (Pubitemid 39157491)
    • (2004) Reproductive BioMedicine Online , vol.9 , Issue.2 , pp. 231-236
    • Andersen, C.Y.1    Westergaard, L.G.2    Van Wely, M.3
  • 103
    • 58149204341 scopus 로고    scopus 로고
    • The expanding role of recombinant gonadotropins in assisted reproduction
    • Adams TE, Boime I. The expanding role of recombinant gonadotropins in assisted reproduction. Reprod Domest Anim. 2008;43:186-92.
    • (2008) Reprod Domest Anim , vol.43 , pp. 186-192
    • Adams, T.E.1    Boime, I.2
  • 104
    • 70149089001 scopus 로고    scopus 로고
    • Toward fully synthetic homogeneous betahuman follicle-stimulating hormone (beta-hFSH) with a biantennary N-linked dodecasaccharide. Synthesis of beta-hFSH with chitobiose units at the natural linkage sites
    • Nagorny P, Fasching B, Li XC, Chen G, Aussedat B, Danishefsky SJ. Toward fully synthetic homogeneous betahuman follicle-stimulating hormone (beta-hFSH) with a biantennary N-linked dodecasaccharide. Synthesis of beta-hFSH with chitobiose units at the natural linkage sites. J Am ChemSoc. 2009;131(16):5792-9.
    • (2009) J Am ChemSoc , vol.131 , Issue.16 , pp. 5792-5799
    • Nagorny, P.1    Fasching, B.2    Li, X.C.3    Chen, G.4    Aussedat, B.5    Danishefsky, S.J.6
  • 105
    • 77249123446 scopus 로고    scopus 로고
    • Partially deglycosylated equine LH preferentially activates ß-arrestin-dependent signaling at the folliclestimulating hormone receptor
    • Wehbi V, Tranchant T, Durand G, Musnier A, Decourtye J, Piketty V, et al. Partially deglycosylated equine LH preferentially activates ß-arrestin-dependent signaling at the folliclestimulating hormone receptor. Mol Endocrinol. 2010;24 (3):561-73.
    • (2010) Mol Endocrinol , vol.24 , Issue.3 , pp. 561-573
    • Wehbi, V.1    Tranchant, T.2    Durand, G.3    Musnier, A.4    Decourtye, J.5    Piketty, V.6
  • 107
    • 0030037083 scopus 로고    scopus 로고
    • Protein folding in the endoplasmic reticulum: Lessons from the human chorionic gonadotropin β subunit
    • Ruddon RW, Sherman SA, Bedows E. Protein folding in the endoplasmic reticulum: Lessons from the human chorionic gonadotropin ß subunit. Protein Sci. 1996;5:1443-52. (Pubitemid 26257210)
    • (1996) Protein Science , vol.5 , Issue.8 , pp. 1443-1452
    • Ruddon, R.W.1    Sherman, S.A.2    Bedows, E.3
  • 108
    • 0025992391 scopus 로고
    • Site-specific Nglycosylation of human chorionic gonadotropin-structural analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy
    • Weisshaar G, Hiyama J, Renwick AGC. Site-specific Nglycosylation of human chorionic gonadotropin-structural analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy. Glycobiology. 1991;1(4):393-404.
    • (1991) Glycobiology , vol.1 , Issue.4 , pp. 393-404
    • Weisshaar, G.1    Hiyama, J.2    Renwick, A.G.C.3
  • 109
    • 68549091059 scopus 로고    scopus 로고
    • Proposal for a standard system for drawing structural diagrams of N- and O-linked carbohydrates and related compounds
    • Harvey DJ, Merry AH, Royle L, Campbell MP, Dwek RA, Rudd PM. Proposal for a standard system for drawing structural diagrams of N- and O-linked carbohydrates and related compounds. Proteomics. 2009;9(15):3796-801.
    • (2009) Proteomics , vol.9 , Issue.15 , pp. 3796-3801
    • Harvey, D.J.1    Merry, A.H.2    Royle, L.3    Campbell, M.P.4    Dwek, R.A.5    Rudd, P.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.