메뉴 건너뛰기




Volumn 7, Issue 8, 1996, Pages 277-286

Structure-function studies of human TSH: New advances in design of glycoprotein hormone analogs

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVIN A; INHIBIN; MYELOPID; PLATELET DERIVED GROWTH FACTOR AA; PLATELET DERIVED GROWTH FACTOR BB; THYROTROPIN; TRANSFORMING GROWTH FACTOR BETA RECEPTOR;

EID: 0030272080     PISSN: 10432760     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1043-2760(96)00129-4     Document Type: Short Survey
Times cited : (30)

References (68)
  • 1
    • 0020021127 scopus 로고
    • Carbohydrate-specific receptors in the liver
    • Ashwell G, Harford J: 1982. Carbohydrate-specific receptors in the liver. Annu Rev Biochem 51:531-554.
    • (1982) Annu Rev Biochem , vol.51 , pp. 531-554
    • Ashwell, G.1    Harford, J.2
  • 2
    • 0001581868 scopus 로고
    • Glycosylation and glycoprotein hormone function
    • Lustbader JW, Puett D, Ruddon RW, eds. New York, Springer-Verlag
    • Baenziger JU: 1994. Glycosylation and glycoprotein hormone function. In Lustbader JW, Puett D, Ruddon RW, eds. Glycoprotein Hormones. New York, Springer-Verlag, pp 167-174.
    • (1994) Glycoprotein Hormones , pp. 167-174
    • Baenziger, J.U.1
  • 3
    • 0030139513 scopus 로고    scopus 로고
    • Glycosylation: To what end for the glycoprotein hormones?
    • Baenziger JU: 1996. Glycosylation: to what end for the glycoprotein hormones? Endocrinology 137:1520-1522.
    • (1996) Endocrinology , vol.137 , pp. 1520-1522
    • Baenziger, J.U.1
  • 4
    • 0021928235 scopus 로고
    • Decreased receptor binding of biologically inactive thyrotropin in central hypothyroidism: Effect of treatment with thyrotropin releasing hormone
    • Beck-Peccoz P, Amr S, Menzes-Ferreira M, Faglia G, Weintraub BD: 1985. Decreased receptor binding of biologically inactive thyrotropin in central hypothyroidism: effect of treatment with thyrotropin releasing hormone. N Engl J Med 312:1085-1090.
    • (1985) N Engl J Med , vol.312 , pp. 1085-1090
    • Beck-Peccoz, P.1    Amr, S.2    Menzes-Ferreira, M.3    Faglia, G.4    Weintraub, B.D.5
  • 5
    • 0027966921 scopus 로고
    • Variable biological activity of thyroid-stimulating hormone (TSH)
    • Beck-Peccoz P, Persani L: 1994. Variable biological activity of thyroid-stimulating hormone (TSH). Eur J Endocrinol 130:331-340.
    • (1994) Eur J Endocrinol , vol.130 , pp. 331-340
    • Beck-Peccoz, P.1    Persani, L.2
  • 6
    • 77956802616 scopus 로고
    • The glycoprotein hormone family: Structure and function of the carbohydrate chains
    • Montrreuil J, Schachter H, Vliegenthart JFG, eds. Amsterdam, Elsevier
    • Bielinska M, Boime I: 1995. The glycoprotein hormone family: structure and function of the carbohydrate chains. In Montrreuil J, Schachter H, Vliegenthart JFG, eds. Glycoproteins. Amsterdam, Elsevier, pp 565-587.
    • (1995) Glycoproteins
    • Bielinska, M.1    Boime, I.2
  • 7
    • 0028978687 scopus 로고
    • Both of the β-subunit carbohydrate residues of follicle-stimulating hormone determine the metabolic clearance rate and in vivo potency
    • Bishop LA, Nguyen TV, Schofield PR: 1995. Both of the β-subunit carbohydrate residues of follicle-stimulating hormone determine the metabolic clearance rate and in vivo potency. Endocrinology 136:2635-2640.
    • (1995) Endocrinology , vol.136 , pp. 2635-2640
    • Bishop, L.A.1    Nguyen, T.V.2    Schofield, P.R.3
  • 8
    • 0024532757 scopus 로고
    • A molecular basis for bidirectional communication between the immune and neuroendocrine system
    • Blalock JE: 1989. A molecular basis for bidirectional communication between the immune and neuroendocrine system. Physiol Rev 69: 1-32.
    • (1989) Physiol Rev , vol.69 , pp. 1-32
    • Blalock, J.E.1
  • 9
    • 0026045952 scopus 로고
    • Free alpha molecules from pregnancy stimulate secretion of prolactin from human decidual cells: A novel function for free alpha in pregnancy
    • Blithe DL, Richards RG, Skarulis MC: 1991. Free alpha molecules from pregnancy stimulate secretion of prolactin from human decidual cells: a novel function for free alpha in pregnancy. Endocrinology 129:2257-2259.
    • (1991) Endocrinology , vol.129 , pp. 2257-2259
    • Blithe, D.L.1    Richards, R.G.2    Skarulis, M.C.3
  • 10
    • 0028852501 scopus 로고
    • Anti-HIV effect of beta subunit of human chorionic gonadotropin (βhCG) in vitro
    • Bourinbaiar AS, Lee-Huang S: 1995. Anti-HIV effect of beta subunit of human chorionic gonadotropin (βhCG) in vitro. Immunol Lett 44:13-18.
    • (1995) Immunol Lett , vol.44 , pp. 13-18
    • Bourinbaiar, A.S.1    Lee-Huang, S.2
  • 11
    • 0027177562 scopus 로고
    • Recombinant human thyroid stimulating hormone: Development of a biotechnology product for detection of metastatic lesions of thyroid carcinoma
    • Cole ES, Lee K, Lauziere K, et al.: 1993. Recombinant human thyroid stimulating hormone: development of a biotechnology product for detection of metastatic lesions of thyroid carcinoma. Biotechnology 11:1014-1024.
    • (1993) Biotechnology , vol.11 , pp. 1014-1024
    • Cole, E.S.1    Lee, K.2    Lauziere, K.3
  • 12
    • 0026440307 scopus 로고
    • Molecular basis of the specificity of binding of glycoprotein hormones to their receptors
    • Combarnous Y: 1992. Molecular basis of the specificity of binding of glycoprotein hormones to their receptors. Endocrine Rev 13: 670-691.
    • (1992) Endocrine Rev , vol.13 , pp. 670-691
    • Combarnous, Y.1
  • 14
    • 0026518265 scopus 로고
    • Progress and approaches in mapping the surfaces of human follicle-stimulating hormone: Comparison with the other human pituitary glycoprotein hormones
    • Dias JA: 1992. Progress and approaches in mapping the surfaces of human follicle-stimulating hormone: comparison with the other human pituitary glycoprotein hormones. Trends Endocrinol Metab 3:24-29.
    • (1992) Trends Endocrinol Metab , vol.3 , pp. 24-29
    • Dias, J.A.1
  • 15
    • 0026342559 scopus 로고
    • Clearing up glycoprotein hormones
    • Drickamer K: 1991. Clearing up glycoprotein hormones. Cell 67:1029-1032.
    • (1991) Cell , vol.67 , pp. 1029-1032
    • Drickamer, K.1
  • 16
    • 0026551294 scopus 로고
    • Design of a long-acting follitropin agonist by fusing the C-terminal sequence of the chorionic gonadotropin β subunit to the follitropin β subunit
    • Fares FA, Suganuma N, Nishimori K, LaPolt PS, Hsueh AJW, Boime I: 1992. Design of a long-acting follitropin agonist by fusing the C-terminal sequence of the chorionic gonadotropin β subunit to the follitropin β subunit. Proc Natl Acad Sci USA 89:4304-4308.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 4304-4308
    • Fares, F.A.1    Suganuma, N.2    Nishimori, K.3    LaPolt, P.S.4    Hsueh, A.J.W.5    Boime, I.6
  • 17
    • 0030051344 scopus 로고    scopus 로고
    • The role of the asparagine-linked oligosaccharides of the α-subunit in human thyrotropin bioactivity
    • Fares FA, Gruener N, Kraiem Z: 1996. The role of the asparagine-linked oligosaccharides of the α-subunit in human thyrotropin bioactivity. Endocrinology 137:555-560.
    • (1996) Endocrinology , vol.137 , pp. 555-560
    • Fares, F.A.1    Gruener, N.2    Kraiem, Z.3
  • 18
    • 0019831147 scopus 로고
    • The gene encoding the common alpha subunit of the four human glycoprotein hormones
    • Fiddes JC, Goodman HM: 1981. The gene encoding the common alpha subunit of the four human glycoprotein hormones. J Mol App Gen 1:3-18.
    • (1981) J Mol App Gen , vol.1 , pp. 3-18
    • Fiddes, J.C.1    Goodman, H.M.2
  • 19
    • 0022987152 scopus 로고
    • Mechanisms and regulation of TSH glycosylation
    • Gesundheit N, Weintraub BD: 1986. Mechanisms and regulation of TSH glycosylation. Adv Exp Med Biol 205:87-105.
    • (1986) Adv Exp Med Biol , vol.205 , pp. 87-105
    • Gesundheit, N.1    Weintraub, B.D.2
  • 20
    • 11944272604 scopus 로고
    • Environmental effects on protein glycosylation
    • Goochee CF, Monica T: 1990. Environmental effects on protein glycosylation. Biotechnology 8:421-427.
    • (1990) Biotechnology , vol.8 , pp. 421-427
    • Goochee, C.F.1    Monica, T.2
  • 21
    • 0028805384 scopus 로고
    • Expression of human thyrotropin in cell lines with different glycosylation patterns combined with mutagenesis of specific glycosylation sites: Characterization of a novel role for the oligosaccharides in the in vitro and in vivo bioactivity
    • Grossmann M, Szkudlinski MW, Tropea JE, et al.: 1995a. Expression of human thyrotropin in cell lines with different glycosylation patterns combined with mutagenesis of specific glycosylation sites: characterization of a novel role for the oligosaccharides in the in vitro and in vivo bioactivity. J Biol Chem 270:29,378-29,385.
    • (1995) J Biol Chem , vol.270 , Issue.29 , pp. 378-429
    • Grossmann, M.1    Szkudlinski, M.W.2    Tropea, J.E.3
  • 22
    • 0029135420 scopus 로고
    • Role of the carboxy-terminal residues of the α-subunit in the expression and bioactivity of human thyroid-stimulating hormone
    • Grossmann M, Szkudlinski MW, Zeng H, et al.: 1995b. Role of the carboxy-terminal residues of the α-subunit in the expression and bioactivity of human thyroid-stimulating hormone. Mol Endocrinol 9:948-958.
    • (1995) Mol Endocrinol , vol.9 , pp. 948-958
    • Grossmann, M.1    Szkudlinski, M.W.2    Zeng, H.3
  • 23
    • 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
    • Grossmann M, Szkudlinski MW, Dias JA, 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
    • Grossmann, M.1    Szkudlinski, M.W.2    Dias, J.A.3
  • 25
    • 0024447839 scopus 로고
    • Thyroid-stimulating hormone (TSH) deficiency caused by a single base substitution in the CAGYC region of the β-subunit
    • Hayashizaki Y, Hiraoka Y, Endo Y, Matsubara K: 1989. Thyroid-stimulating hormone (TSH) deficiency caused by a single base substitution in the CAGYC region of the β-subunit. EMBO J 8:2291-2296.
    • (1989) Embo J , vol.8 , pp. 2291-2296
    • Hayashizaki, Y.1    Hiraoka, Y.2    Endo, Y.3    Matsubara, K.4
  • 26
    • 0026355620 scopus 로고
    • Asialoagalacto-human chorionic gonadotropin, a carbohydrate-modified variant of human chorionic gonadotropin, antagonizes the stimulatory actions of bovine thyroid-stimulating hormone on thyroid function and hla-dr expression in human thyroid in vitro and in vivo
    • Hoermann R, Schumm-Draeger PM, Rehbach K, Mann K: 1991. Asialoagalacto-human chorionic gonadotropin, a carbohydrate-modified variant of human chorionic gonadotropin, antagonizes the stimulatory actions of bovine thyroid-stimulating hormone on thyroid function and HLA-DR expression in human thyroid in vitro and in vivo. J Clin Invest 88:1947-1954.
    • (1991) J Clin Invest , vol.88 , pp. 1947-1954
    • Hoermann, R.1    Schumm-Draeger, P.M.2    Rehbach, K.3    Mann, K.4
  • 27
    • 0027371827 scopus 로고
    • Receptor activation of and signal generation by the lutropin/choriogonadotropin receptor
    • Ji I, Zeng H, Ji TH: 1993. Receptor activation of and signal generation by the lutropin/choriogonadotropin receptor. J Biol Chem 268: 22,971-22,974.
    • (1993) J Biol Chem , vol.268 , pp. 22971-22974
    • Ji, I.1    Zeng, H.2    Ji, T.H.3
  • 28
    • 0028861715 scopus 로고
    • Activation of membrane receptors
    • Ji TH, Murdoch W, Ji I: 1995. Activation of membrane receptors. Endocrine 3:187-194.
    • (1995) Endocrine , vol.3 , pp. 187-194
    • Ji, T.H.1    Murdoch, W.2    Ji, I.3
  • 29
    • 0021025507 scopus 로고
    • Naturally occuring forms of thyrotropin with low bioactivity and altered carbohydrate content act as competitive antagonists to more bioactive forms
    • Joshi LR, Weintraub BD: 1983. Naturally occuring forms of thyrotropin with low bioactivity and altered carbohydrate content act as competitive antagonists to more bioactive forms. Endocrinology 113:2145-2154.
    • (1983) Endocrinology , vol.113 , pp. 2145-2154
    • Joshi, L.R.1    Weintraub, B.D.2
  • 30
    • 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, Murata Y, Wondisford F, Szkudlinski MW, Desai R, Weintraub BD: 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    Murata, Y.2    Wondisford, F.3    Szkudlinski, M.W.4    Desai, R.5    Weintraub, B.D.6
  • 31
    • 0026724205 scopus 로고
    • Receptor-binding regions in human glycoprotein hormones
    • Keutmann HT: 1992. Receptor-binding regions in human glycoprotein hormones. Mol Cell Endocrinol 186:C1-C6.
    • (1992) Mol Cell Endocrinol , vol.186
    • Keutmann, H.T.1
  • 33
    • 0028239813 scopus 로고
    • Crystal structure of human chorionic gonadotropin
    • Lapthorn AJ, Harris DC, Littlejohn A, et al.: 1994. Crystal structure of human chorionic gonadotropin. Nature 369:455-461.
    • (1994) Nature , vol.369 , pp. 455-461
    • Lapthorn, A.J.1    Harris, D.C.2    Littlejohn, A.3
  • 34
    • 0026776964 scopus 로고
    • Mutations of the human thyrotropin-β subunit glycosylation site reduce thyrotropin synthesis independent of changes in glycosylation status
    • Lash RW, Desai RK, Zimmermann CA, et al.: 1992. Mutations of the human thyrotropin-β subunit glycosylation site reduce thyrotropin synthesis independent of changes in glycosylation status. J Endocrinol Invest 15:225-263.
    • (1992) J Endocrinol Invest , vol.15 , pp. 225-263
    • Lash, R.W.1    Desai, R.K.2    Zimmermann, C.A.3
  • 35
    • 0029619433 scopus 로고
    • Thyrotropin with decreased biological activity, a delayed consequence of cranial irradiation for nasopharyngeal carcinoma
    • Lee KO, Persani L, Tan M, Sundram FX, Beck-Peccoz P: 1995. Thyrotropin with decreased biological activity, a delayed consequence of cranial irradiation for nasopharyngeal carcinoma. J Endocrinol Invest 18:800-805.
    • (1995) J Endocrinol Invest , vol.18 , pp. 800-805
    • Lee, K.O.1    Persani, L.2    Tan, M.3    Sundram, F.X.4    Beck-Peccoz, P.5
  • 36
    • 0025950132 scopus 로고
    • Further characterization of the receptor-binding region of the thyroid-stimulating hormone α subunit: A comprehensive synthetic peptide study of the α-subunit 26-46 sequence
    • Leinung MC, Reed DK, McCormick DJ, Ryan RJ, Morris JC: 1991. Further characterization of the receptor-binding region of the thyroid-stimulating hormone α subunit: a comprehensive synthetic peptide study of the α-subunit 26-46 sequence. Proc Natl Acad Sci USA 88:9707-9711.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 9707-9711
    • Leinung, M.C.1    Reed, D.K.2    McCormick, D.J.3    Ryan, R.J.4    Morris, J.C.5
  • 37
    • 0028968845 scopus 로고
    • Effects of continous, pulsatile, and bolus administration of pituitary rat thyrotropin and recombinant human thyrotropin in a chronically cannulated continuous
    • Leitolf H, Szkudlinski MW, Hoang-vu C, et al.: 1995. Effects of continous, pulsatile, and bolus administration of pituitary rat thyrotropin and recombinant human thyrotropin in a chronically cannulated continuous. Horm Metab Res 27:173-178.
    • (1995) Horm Metab Res , vol.27 , pp. 173-178
    • Leitolf, H.1    Szkudlinski, M.W.2    Hoang-Vu, C.3
  • 39
    • 0029024279 scopus 로고
    • Tumorigenesis and metastasis of neoplastic kaposi's sarcoma cell line in immunodeficient mice blocked by a human pregnancy hormone
    • Lunardi-Iskandar Y, Bryant JL, Zeman RA, et al.: 1995. Tumorigenesis and metastasis of neoplastic Kaposi's sarcoma cell line in immunodeficient mice blocked by a human pregnancy hormone. Nature 375:64-68.
    • (1995) Nature , vol.375 , pp. 64-68
    • Lunardi-Iskandar, Y.1    Bryant, J.L.2    Zeman, R.A.3
  • 40
    • 0025358072 scopus 로고
    • Thyroid-stimulating hormone: Biosynthesis, cell biology, and bioactivity
    • Magner JA: 1990. Thyroid-stimulating hormone: biosynthesis, cell biology, and bioactivity. Endocr Rev 11:354-385.
    • (1990) Endocr Rev , vol.11 , pp. 354-385
    • Magner, J.A.1
  • 41
    • 0002764888 scopus 로고
    • Biosynthesis, cell biology, and bioactivity of thyroid-stimulating hormone: Update 1994
    • Braverman L, Refetoff S., eds. Bethesda, MD, The Endocrine Society, vol
    • Magner JA: 1994. Biosynthesis, cell biology, and bioactivity of thyroid-stimulating hormone: update 1994. In Braverman L, Refetoff S., eds. Endocrine Reviews Monographs. Bethesda, MD, The Endocrine Society, vol 3:55-60.
    • (1994) Endocrine Reviews Monographs , vol.3 , pp. 55-60
    • Magner, J.A.1
  • 42
    • 0024511030 scopus 로고
    • Site specificity of the chorionic gonadotropin N-linked oligosaccharides in signal transduction
    • Matzuk MM, Keene JL, Boime I: 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    Keene, J.L.2    Boime, I.3
  • 43
    • 13344295090 scopus 로고    scopus 로고
    • A circulating biologically inactive thyrotropin caused by a mutation in the beta subunit gene
    • Medeiros-Neto G, Herodotou DT, Rajan S, et al.: 1996. A circulating biologically inactive thyrotropin caused by a mutation in the beta subunit gene. J Clin Invest 97:1250-1256.
    • (1996) J Clin Invest , vol.97 , pp. 1250-1256
    • Medeiros-Neto, G.1    Herodotou, D.T.2    Rajan, S.3
  • 44
    • 84995867590 scopus 로고
    • Diagnostic use of recombinant human thyrotropin in patients with thyroid carcinoma (phase I/II study)
    • Meier CA, Braverman LE, Ebner SA, et al.: 1994. Diagnostic use of recombinant human thyrotropin in patients with thyroid carcinoma (phase I/II study). J Clin Endocrinol Metab 78:188-196.
    • (1994) J Clin Endocrinol Metab , vol.78 , pp. 188-196
    • Meier, C.A.1    Braverman, L.E.2    Ebner, S.A.3
  • 45
  • 47
    • 0029093909 scopus 로고
    • Model of human chorionic gonadotropin and lutropin receptor interaction that explains signal transduction of the glycoprotein hormones
    • Moyle WR, Campbell RK, Rao SN, et al.: 1995. Model of human chorionic gonadotropin and lutropin receptor interaction that explains signal transduction of the glycoprotein hormones. J Biol Chem 270:20,020-20,031.
    • (1995) J Biol Chem , vol.270 , Issue.20 , pp. 20-20
    • Moyle, W.R.1    Campbell, R.K.2    Rao, S.N.3
  • 48
    • 0019729482 scopus 로고
    • Glycoprotein hormones: Structure and function
    • Pierce JG, Parsons TF: 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
  • 49
    • 0028217351 scopus 로고
    • The functional relationship between FSH, its receptors as studied by synthetic peptide strategies
    • Reichert Jr, L: 1994. The functional relationship between FSH, its receptors as studied by synthetic peptide strategies. Mol Cell Endocrinol 100:21-27.
    • (1994) Mol Cell Endocrinol , vol.100 , pp. 21-27
    • Reichert L., Jr.1
  • 50
    • 0023225506 scopus 로고
    • Antibody binding to the beta-subunit of deglycosylated chorionic gonadotropin converts the antagonist to an agonist
    • Rebois RV, Liss MT: 1987. Antibody binding to the beta-subunit of deglycosylated chorionic gonadotropin converts the antagonist to an agonist. J Biol Chem 262:3891-3896.
    • (1987) J Biol Chem , vol.262 , pp. 3891-3896
    • Rebois, R.V.1    Liss, M.T.2
  • 52
    • 0026485387 scopus 로고
    • Molecular structures of glycoprotein hormones and functions of their carbohydrate components
    • Stockell Hartee A, Renwick AGC: 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
  • 53
    • 0027517557 scopus 로고
    • Purification and characterization of recombinant human thyrotropin isoforms produced by chinese hamster ovary cells: The role of sialylation and sulfation in thyrotropin bioactivity
    • Szkudlinski MW, Thotakura NR, Bucci I, et al.: 1993. Purification and characterization of recombinant human thyrotropin isoforms produced by Chinese hamster ovary cells: the role of sialylation and sulfation in thyrotropin bioactivity. Endocrinology 133:1490-1503.
    • (1993) Endocrinology , vol.133 , pp. 1490-1503
    • Szkudlinski, M.W.1    Thotakura, N.R.2    Bucci, I.3
  • 54
    • 0029079758 scopus 로고
    • Subunit-specific functions of n-linked oligosaccharides in human thyrotropin: Role of terminal residues of α- and β-subunit in metabolic clearance and bioactivity
    • Szkudlinski MW, Thotakura NR, Weintraub BD: 1995a. Subunit-specific functions of N-linked oligosaccharides in human thyrotropin: role of terminal residues of α- and β-subunit in metabolic clearance and bioactivity. Proc Natl Acad Sci USA 92:9062-9066.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9062-9066
    • Szkudlinski, M.W.1    Thotakura, N.R.2    Weintraub, B.D.3
  • 55
    • 0029112363 scopus 로고
    • Asparagine-linked oligosaccharide structures determine clearance and organ distribution of pituitary and recombinant thyrotropins (TSH)
    • Szkudlinski MW, Thotakura NR, Tropea JE, Grossmann M, Weintraub BD: 1995b. Asparagine-linked oligosaccharide structures determine clearance and organ distribution of pituitary and recombinant thyrotropins (TSH). Endocrinology 136:3325-3330.
    • (1995) Endocrinology , vol.136 , pp. 3325-3330
    • Szkudlinski, M.W.1    Thotakura, N.R.2    Tropea, J.E.3    Grossmann, M.4    Weintraub, B.D.5
  • 56
    • 0011814568 scopus 로고
    • Superagonists of recombinant human tsh provide a model of rational design of glycoprotein hormone analogs: Site-specific bovinization of the alpha subunit increases in vitro and in vivo bioactivity
    • Szkudlinski MW, Teh NG, Grossmann M, et al.: 1995c. Superagonists of recombinant human TSH provide a model of rational design of glycoprotein hormone analogs: site-specific bovinization of the alpha subunit increases in vitro and in vivo bioactivity. Thyroid 5(Suppl 1):72.
    • (1995) Thyroid , vol.5 , Issue.SUPPL. 1 , pp. 72
    • Szkudlinski, M.W.1    Teh, N.G.2    Grossmann, M.3
  • 58
    • 0011866795 scopus 로고    scopus 로고
    • Role of the 40-51 region of the alpha-subunit in the bioactivity of human thyrotropin and gonadotropins. Implications for the design of new hormone analogs based on simultaneous mutagenesis of multiple domains [abst or1-4]
    • San Francisco, USA. Bethesda, MD, The Endocrine Society
    • Szkudlinski MW, Witta J, Grossmann M, et al.: 1996b. Role of the 40-51 region of the alpha-subunit in the bioactivity of human thyrotropin and gonadotropins. Implications for the design of new hormone analogs based on simultaneous mutagenesis of multiple domains [abst OR1-4]. Proceedings of the 10th International Congress of Endocrinology, San Francisco, USA. Bethesda, MD, The Endocrine Society, p. 43.
    • (1996) Proceedings of the 10th International Congress of Endocrinology , pp. 43
    • Szkudlinski, M.W.1    Witta, J.2    Grossmann, M.3
  • 59
    • 0028890259 scopus 로고
    • Glycoprotein hormones: Glycobiology of gonadotrophins, thyrotropin, and free α subunit
    • Thotakura NR, Blithe DL: 1995. Glycoprotein hormones: glycobiology of gonadotrophins, thyrotropin, and free α subunit. Glycobiology 5:3-10.
    • (1995) Glycobiology , vol.5 , pp. 3-10
    • Thotakura, N.R.1    Blithe, D.L.2
  • 60
    • 0026634306 scopus 로고
    • The role of the oligosaccharide chains of thyrotropin α- and β-subunits in hormone action
    • Thotakura NR, Desai RK, Szkudlinski MW, Weintraub BD: 1992. The role of the oligosaccharide chains of thyrotropin α- and β-subunits in hormone action. Endocrinology 141: 82-88.
    • (1992) Endocrinology , vol.141 , pp. 82-88
    • Thotakura, N.R.1    Desai, R.K.2    Szkudlinski, M.W.3    Weintraub, B.D.4
  • 61
    • 0028041190 scopus 로고
    • Structure-function studies of oligosaccharides of recombinant human thyrotropin by sequential deglycosylation and resialylation
    • Thotakura NR, Szkudlinski MW, Weintraub BD: 1994. Structure-function studies of oligosaccharides of recombinant human thyrotropin by sequential deglycosylation and resialylation. Glycobiology 4:525-533.
    • (1994) Glycobiology , vol.4 , pp. 525-533
    • Thotakura, N.R.1    Szkudlinski, M.W.2    Weintraub, B.D.3
  • 62
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • Varki A: 1993. Biological roles of oligosaccharides: all of the theories are correct. Glycobiology 3:97-130.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 63
    • 0021776162 scopus 로고
    • Glycosylation and post-translational processing of thyroid-stimulating hormone: Clinical implications
    • Weintraub BD, Stannard BS, Magner JA, et al.: 1985. Glycosylation and post-translational processing of thyroid-stimulating hormone: clinical implications. Recent Prog Horm Res 41:577-606.
    • (1985) Recent Prog Horm Res , vol.41 , pp. 577-606
    • Weintraub, B.D.1    Stannard, B.S.2    Magner, J.A.3
  • 64
    • 0026335545 scopus 로고
    • Hypogonadism caused by a single amino acid substitution in the beta subunit of luteinizing hormone
    • Weiss J, Axelrod L, Whitcomb RW, Harris PE, Crowley WF, Jameson JL: 1992. Hypogonadism caused by a single amino acid substitution in the beta subunit of luteinizing hormone. N Engl J Med 326:179-183.
    • (1992) N Engl J Med , vol.326 , pp. 179-183
    • Weiss, J.1    Axelrod, L.2    Whitcomb, R.W.3    Harris, P.E.4    Crowley, W.F.5    Jameson, J.L.6
  • 66
    • 0028773646 scopus 로고
    • Structure of human chorionic gonadotropin at 2.6 å resolution from MAD analysis of the selenomethionyl protein
    • Wu H, Lustbader JW, Liu Y, Canfield RE, Hendrickson WA: 1994. Structure of 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    Lustbader, J.W.2    Liu, Y.3    Canfield, R.E.4    Hendrickson, W.A.5
  • 67
    • 0028218007 scopus 로고
    • A region in the human glycoprotein hormone α subunit important in holoprotein formation and receptor binding
    • Xia H, Chen F, Puett D: 1994. A region in the human glycoprotein hormone α subunit important in holoprotein formation and receptor binding. Endocrinology 134:1768-1770.
    • (1994) Endocrinology , vol.134 , pp. 1768-1770
    • Xia, H.1    Chen, F.2    Puett, D.3
  • 68
    • 0027493757 scopus 로고
    • COOH-terminal amino acids of the α-subunit play common and different roles in human choriogonadotropin and follitropin
    • Yoo J, Zeng H, Ji I, Murdoch WJ, Ji TH: 1993. COOH-terminal amino acids of the α-subunit play common and different roles in human choriogonadotropin and follitropin. J Biol Chem 268:13,034-13,042. TEM
    • (1993) J Biol Chem , vol.268 , Issue.13 , pp. 34-113
    • Yoo, J.1    Zeng, H.2    Ji, I.3    Murdoch, W.J.4    Ji, T.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.