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Volumn 14, Issue 3, 2011, Pages 170-181

Central dogma in thyroid dysfunction: A review on structure modification of TSHR as a cornerstone for thyroid abnormalities

Author keywords

Alteration; Hyperthyroidism; Hypothyroidism; Mutation; Receptor

Indexed keywords

THYROTROPIN; THYROTROPIN RECEPTOR;

EID: 79957471905     PISSN: 10288880     EISSN: 18125735     Source Type: Journal    
DOI: 10.3923/pjbs.2011.170.181     Document Type: Review
Times cited : (15)

References (136)
  • 1
    • 0030994365 scopus 로고    scopus 로고
    • Familial congenital hypothyroidism due to inactivating mutation of the thyrotropin receptor causing profound hypoplasia of the thyroid gland
    • Abramowicz, M.J., L. Duprez, J. Parma, G. Vassart and C. Heinrichs, 1997. Familial congenital hypothyroidism due to inactivating mutation of the thyrotropin receptor causing profound hypoplasia of the thyroid gland. J. Clin. Invest., 99: 3018-3024.
    • (1997) J. Clin. Invest , vol.99 , pp. 3018-3024
    • Abramowicz, M.J.1    Duprez, L.2    Parma, J.3    Vassart, G.4    Heinrichs, C.5
  • 2
    • 0028354607 scopus 로고
    • Further studies of amino acids (268-304) in thyrotropin (TSH)-lutropin/chorionic gonadotropin (LH/CG) receptor chimeras: Cysteine-301 is important in TSH binding and receptor tertiary structure
    • Akamizu, T., D. Inoue, S. Kosugi, L.D. Kohn and T. Mori, 1994. Further studies of amino acids (268-304) in thyrotropin (TSH)-lutropin/chorionic gonadotropin (LH/CG) receptor chimeras: Cysteine-301 is important in TSH binding and receptor tertiary structure. Thyroid., 4: 43-48.
    • (1994) Thyroid , vol.4 , pp. 43-48
    • Akamizu, T.1    Inoue, D.2    Kosugi, S.3    Kohn, L.D.4    Mori, T.5
  • 5
    • 0023199539 scopus 로고
    • In vitro conversion of blocking type anti-TSH receptor antibody to the stimulating type by anti-human IgG antibodies
    • Amino, N., Y. Watanabe, H. Tamaki, Y. Iwatani and K. Miyai, 1987. In vitro conversion of blocking type anti-TSH receptor antibody to the stimulating type by anti-human IgG antibodies. Clin. Endocrinol., 27: 615-624.
    • (1987) Clin. Endocrinol , vol.27 , pp. 615-624
    • Amino, N.1    Watanabe, Y.2    Tamaki, H.3    Iwatani, Y.4    Miyai, K.5
  • 6
    • 13844271908 scopus 로고    scopus 로고
    • Review thyrotropin receptor antibodies: New insights into their actions and clinical relevance
    • Ando, T., R. Latif and T.F. Davies, 2005. Review thyrotropin receptor antibodies: New insights into their actions and clinical relevance. Best Pract. Res. Clin. Endocrinol. Metab., 19: 33-52.
    • (2005) Best Pract. Res. Clin. Endocrinol. Metab , vol.19 , pp. 33-52
    • Ando, T.1    Latif, R.2    Davies, T.F.3
  • 7
    • 0033924756 scopus 로고    scopus 로고
    • Genomic DNA analysis of thyrotropin receptor in a family with hereditary hyperthyroidism
    • Aoshima, H., T. Yoshida, S. Kobayashi, Y. Mizushima and S. Kawai, 2000. Genomic DNA analysis of thyrotropin receptor in a family with hereditary hyperthyroidism. Endocr. J., 47: 365-372.
    • (2000) Endocr. J , vol.47 , pp. 365-372
    • Aoshima, H.1    Yoshida, T.2    Kobayashi, S.3    Mizushima, Y.4    Kawai, S.5
  • 8
    • 0030983833 scopus 로고    scopus 로고
    • Mutations of the human thyrotropin receptor gene causing thyroid hypoplasia and persistent congenital hypothyroidism
    • Biebermann, H., T. Schoneberg, H. Krude, G. Schultz, T. Gudermann and A. Gruters, 1997. Mutations of the human thyrotropin receptor gene causing thyroid hypoplasia and persistent congenital hypothyroidism. J. Clin. Endocrinol. Metab., 82: 3471-3480.
    • (1997) J. Clin. Endocrinol. Metab , vol.82 , pp. 3471-3480
    • Biebermann, H.1    Schoneberg, T.2    Krude, H.3    Schultz, G.4    Gudermann, T.5    Gruters, A.6
  • 9
    • 0034853605 scopus 로고    scopus 로고
    • The first activating TSH receptor mutation in transmembrane domain 1 identified in a family with nonautoimmune hyperthyroidism
    • Biebermann, H., T. Schoneberg, C. Hess, J. Germak, T. Gudermann and A. Gruters, 2001. The first activating TSH receptor mutation in transmembrane domain 1 identified in a family with nonautoimmune hyperthyroidism. J. Clin. Endocrinol. Metab., 86: 4429-4433.
    • (2001) J. Clin. Endocrinol. Metab , vol.86 , pp. 4429-4433
    • Biebermann, H.1    Schoneberg, T.2    Hess, C.3    Germak, J.4    Gudermann, T.5    Gruters, A.6
  • 10
    • 0027414794 scopus 로고
    • Thyroid function and hyperfunction during gestation
    • Burrow, G.N., 1993. Thyroid function and hyperfunction during gestation. Endocrinol. Rev., 14: 194-202.
    • (1993) Endocrinol. Rev , vol.14 , pp. 194-202
    • Burrow, G.N.1
  • 11
    • 27544481186 scopus 로고    scopus 로고
    • Intracellular entrapment of wild-type TSH receptor by oligomerization with mutants linked to dominant TSH resistance
    • Calebiro, D., T. de Filippis, S. Lucchi, C. Covino and L. Persani et al., 2005. Intracellular entrapment of wild-type TSH receptor by oligomerization with mutants linked to dominant TSH resistance. Hum. Mol. Genet., 14: 2991-3002.
    • (2005) Hum. Mol. Genet , vol.14 , pp. 2991-3002
    • Calebiro, D.1    de Filippis, T.2    Lucchi, S.3    Covino, C.4    Persani, L.5
  • 12
    • 0028936425 scopus 로고
    • Expression of the extracellular region of the thyrotropin receptor in a baculovirus vector using a promoter active earlier than the polyhedrin promoter: Implications for the expression of functional, highly glycosylated proteins
    • Chazenbalk, G.D. and B. Rapoport, 1995. Expression of the extracellular region of the thyrotropin receptor in a baculovirus vector using a promoter active earlier than the polyhedrin promoter: Implications for the expression of functional, highly glycosylated proteins. J. Biol. Chem., 270: 1543-1549.
    • (1995) J. Biol. Chem , vol.270 , pp. 1543-1549
    • Chazenbalk, G.D.1    Rapoport, B.2
  • 13
    • 0029802727 scopus 로고    scopus 로고
    • Evidence for negative cooperativity among human thyrotropin receptors overexpressed in mammalian cells
    • Chazenbalk, G.D., A. Kakinuma, J.C. Jaume, S.M. McLachlan and B. Rapoport, 1996. Evidence for negative cooperativity among human thyrotropin receptors overexpressed in mammalian cells. Endocrinology, 137: 4586-4591.
    • (1996) Endocrinology , vol.137 , pp. 4586-4591
    • Chazenbalk, G.D.1    Kakinuma, A.2    Jaume, J.C.3    McLachlan, S.M.4    Rapoport, B.5
  • 15
    • 35348872590 scopus 로고    scopus 로고
    • Maternal dietary iodide influences turkey embryo thyroid function
    • Christensen, V.L. and G.S. Davis, 2004. Maternal dietary iodide influences turkey embryo thyroid function. Int. J. Poult. Sci., 3: 550-557.
    • (2004) Int. J. Poult. Sci , vol.3 , pp. 550-557
    • Christensen, V.L.1    Davis, G.S.2
  • 16
    • 0030053238 scopus 로고    scopus 로고
    • Shedding of human thyrotropin receptor ectodomain: Involvement of a matrix metalloprotease
    • Couet, J., S. Sar, A. Jolivet, M.T. VuHai, E. Milgrom and M. Misrahi, 1996. Shedding of human thyrotropin receptor ectodomain: Involvement of a matrix metalloprotease. J. Biol. Chem., 271: 4545-4552.
    • (1996) J. Biol. Chem , vol.271 , pp. 4545-4552
    • Couet, J.1    Sar, S.2    Jolivet, A.3    Vuhai, M.T.4    Milgrom, E.5    Misrahi, M.6
  • 18
    • 0032496269 scopus 로고    scopus 로고
    • Production of the thyrotrophin receptor extracellular domain as a glycosylphosphatidylinositol-anchored membrane protein and its interaction with thyrotrophin and autoantibodies
    • Da Costa, C.R. and A.P. Johnstone, 1998. Production of the thyrotrophin receptor extracellular domain as a glycosylphosphatidylinositol-anchored membrane protein and its interaction with thyrotrophin and autoantibodies. J. Biol. Chem., 273: 11874-11880.
    • (1998) J. Biol. Chem , vol.273 , pp. 11874-11880
    • da Costa, C.R.1    Johnstone, A.P.2
  • 19
    • 0032898172 scopus 로고    scopus 로고
    • Sequential cleavage and excision of a segment of the thyrotropin receptor ectodomain
    • De Bernard, S., M. Misrahi, J.C. Huet, I. Beau and E. Milgrom etal, 1999. Sequential cleavage and excision of a segment of the thyrotropin receptor ectodomain. J. Biol. Chem., 274: 101-107.
    • (1999) J. Biol. Chem , vol.274 , pp. 101-107
    • de Bernard, S.1    Misrahi, M.2    Huet, J.C.3    Beau, I.4    Milgrom, E.5
  • 20
    • 0030596139 scopus 로고    scopus 로고
    • Human follitropin heterodimerization and receptor binding structural motifs: Identification and analysis by a combination of synthetic peptide and mutagenesis approaches
    • Dias, J.A., 1996. Human follitropin heterodimerization and receptor binding structural motifs: Identification and analysis by a combination of synthetic peptide and mutagenesis approaches. Mol. Cell. Endocrinol., 125: 45-54.
    • (1996) Mol. Cell. Endocrinol , vol.125 , pp. 45-54
    • Dias, J.A.1
  • 21
    • 0030805829 scopus 로고    scopus 로고
    • Constitutive activation of the TSH receptor by spontaneous mutations affecting the N-terminal extracellular domain
    • Duprez, L., J. Parma, S. Costagliola, J. Hermans, J. van Sande, J.E. Dumont and G. Vassart, 1997. Constitutive activation of the TSH receptor by spontaneous mutations affecting the N-terminal extracellular domain. FEBSLett, 409: 469-474.
    • (1997) FEBSLett , vol.409 , pp. 469-474
    • Duprez, L.1    Parma, J.2    Costagliola, S.3    Hermans, J.4    van Sande, J.5    Dumont, J.E.6    Vassart, G.7
  • 26
    • 0033910867 scopus 로고    scopus 로고
    • The human thyrotropin receptor is highly mutable: A review of gain-of-function mutations
    • Farid, N.R., V. Kascur and C. Balazs, 2000. The human thyrotropin receptor is highly mutable: A review of gain-of-function mutations. Eur. J. Endocrinol., 143: 25-30.
    • (2000) Eur. J. Endocrinol , vol.143 , pp. 25-30
    • Farid, N.R.1    Kascur, V.2    Balazs, C.3
  • 27
    • 0029053448 scopus 로고
    • The role of N-Glycans in the secretory pathway
    • Fiedler, K. and K. Simons, 1995. The role of N-Glycans in the secretory pathway. Cell, 81: 309-312.
    • (1995) Cell , vol.81 , pp. 309-312
    • Fiedler, K.1    Simons, K.2
  • 29
    • 0030710212 scopus 로고    scopus 로고
    • Somatic mutations in the thyrotropin receptor gene and not in the Gs alpha protein gene in31 toxic thyroid nodules
    • Fuhrer, D., H.P. Holzapfel, P. Wonerow, W.A. Scherbaum and R. Paschke, 1997a. Somatic mutations in the thyrotropin receptor gene and not in the Gs alpha protein gene in31 toxic thyroid nodules. J. Clin. Endocrinol. Metab., 82: 3885-3891.
    • (1997) J. Clin. Endocrinol. Metab , vol.82 , pp. 3885-3891
    • Fuhrer, D.1    Holzapfel, H.P.2    Wonerow, P.3    Scherbaum, W.A.4    Paschke, R.5
  • 30
    • 0030734932 scopus 로고    scopus 로고
    • Identification of a new thyrotropin receptor germline mutation (Leu629Phe) in a family with neonatal onset of autosomal dominant nonautoimmune hyperthyroidism
    • Fuhrer, D., P. Wonerow, H. Willgerodt and R. Paschke, 1997b. Identification of a new thyrotropin receptor germline mutation (Leu629Phe) in a family with neonatal onset of autosomal dominant nonautoimmune hyperthyroidism. J. Clin. Endocrinol. Metab., 82: 4234-4238.
    • (1997) J. Clin. Endocrinol. Metab , vol.82 , pp. 4234-4238
    • Fuhrer, D.1    Wonerow, P.2    Willgerodt, H.3    Paschke, R.4
  • 31
    • 0034505679 scopus 로고    scopus 로고
    • TSHR germline mutation (Met463Val) masquerading as Graves disease in a large Welsh kindred with hyperthyroidism
    • Fuhrer, D., J. Warner, M. Sequerira, R. Paschke, J. Gregory and M. Ludgate, 2000. TSHR germline mutation (Met463Val) masquerading as Graves disease in a large Welsh kindred with hyperthyroidism. Thyroid., 10: 1035-1041.
    • (2000) Thyroid , vol.10 , pp. 1035-1041
    • Fuhrer, D.1    Warner, J.2    Sequerira, M.3    Paschke, R.4    Gregory, J.5    Ludgate, M.6
  • 32
    • 0031755047 scopus 로고    scopus 로고
    • Apparent congenital athyreosis contrasting with normal plasma thyroglobulin levels and associated with inactivating mutations in the thyrotropin receptor gene: Are athyreosis and ectopic thyroid distinct entities
    • Gagne, N., J. Parma, C. Deal, G. Vassar and G. van Vliet, 1998. Apparent congenital athyreosis contrasting with normal plasma thyroglobulin levels and associated with inactivating mutations in the thyrotropin receptor gene: Are athyreosis and ectopic thyroid distinct entities. J. Clin. Endocrinol. Metab., 83: 1771-1775.
    • (1998) J. Clin. Endocrinol. Metab , vol.83 , pp. 1771-1775
    • Gagne, N.1    Parma, J.2    Deal, C.3    Vassar, G.4    van Vliet, G.5
  • 33
    • 0030947645 scopus 로고    scopus 로고
    • The regulation of thyroid function in pregnancy: Pathways of endocrine adaptation from physiology to pathology
    • Golinor, D., 1997. The regulation of thyroid function in pregnancy: Pathways of endocrine adaptation from physiology to pathology. Endocrine Rev., 18: 404-433.
    • (1997) Endocrine Rev , vol.18 , pp. 404-433
    • Golinor, D.1
  • 35
    • 0026664955 scopus 로고
    • Mutational activation of RAS and GSP oncogenes in differentiated thyroid cancer and their biological implications
    • Goretzki, P.E., J. Lyons, S. Stacy Phipps, W. Rosenau and M. Demeure et al., 1992. Mutational activation of RAS and GSP oncogenes in differentiated thyroid cancer and their biological implications. World J. Surg., 16: 576-581.
    • (1992) World J. Surg , vol.16 , pp. 576-581
    • Goretzki, P.E.1    Lyons, J.2    Stacy Phipps, S.3    Rosenau, W.4    Demeure, M.5
  • 36
    • 23044482192 scopus 로고    scopus 로고
    • Autosomal dominant resistance to thyrotropin as a distinct entity in five multigenerational kindreds: Clinical characterization and exclusion of candidate loci
    • Grasberger, H., A. Mimouni-Bloch, M.C. Vantyghem, G. van Vliet and M. Bramowicz et al., 2005a. Autosomal dominant resistance to thyrotropin as a distinct entity in five multigenerational kindreds: Clinical characterization and exclusion of candidate loci. J. Clin. Endocrinol. Metab., 90: 4025-4034.
    • (2005) J. Clin. Endocrinol. Metab , vol.90 , pp. 4025-4034
    • Grasberger, H.1    Mimouni-Bloch, A.2    Vantyghem, M.C.3    van Vliet, G.4    Bramowicz, M.5
  • 37
    • 30744462580 scopus 로고    scopus 로고
    • Identification of a locus for nongoitrous congenital hypothyroidism on chromosome 15q25.3-26.1
    • Grasberger, H., M.M. Vaxillaire, S. Pannain, J.C. Beck and A. Mimouni-Bloch et al., 2005b. Identification of a locus for nongoitrous congenital hypothyroidism on chromosome 15q25.3-26.1. Hum. Genet, 118: 348-355.
    • (2005) Hum. Genet , vol.118 , pp. 348-355
    • Grasberger, H.1    Vaxillaire, M.M.2    Pannain, S.3    Beck, J.C.4    Mimouni-Bloch, A.5
  • 38
    • 0030852648 scopus 로고    scopus 로고
    • Novel insights into the molecular mechanisms of human thyrotropin action: Structural, physiological and therapeutic implications for the glycoprotein hormone family
    • Grossmann, M., B.D. Weintraub and M.W. Szkudlinski, 1997. Novel insights into the molecular mechanisms of human thyrotropin action: Structural, physiological and therapeutic implications for the glycoprotein hormone family. Endocr. Rev., 18: 476-501.
    • (1997) Endocr. Rev , vol.18 , pp. 476-501
    • Grossmann, M.1    Weintraub, B.D.2    Szkudlinski, M.W.3
  • 39
    • 0031772403 scopus 로고    scopus 로고
    • Severe congenital hyperthyroidism caused by a germ-line neo mutation in the extracellular portion of the thyrotropin receptor
    • Gruters, A., T. Schoneberg, H. Biebermann, H. Krude, H.P. Krohn, H. Dralle and T. Gudermann, 1998. Severe congenital hyperthyroidism caused by a germ-line neo mutation in the extracellular portion of the thyrotropin receptor. J. Clin. Endocrinol. Metab., 83: 1431-1436.
    • (1998) J. Clin. Endocrinol. Metab , vol.83 , pp. 1431-1436
    • Gruters, A.1    Schoneberg, T.2    Biebermann, H.3    Krude, H.4    Krohn, H.P.5    Dralle, H.6    Gudermann, T.7
  • 40
    • 70350303252 scopus 로고    scopus 로고
    • Expression of tuberalin II, a-subunit of glycoprotein hormones and a-thyrotropin hormone in the pars tuberalis of the rat: Immunocytochemical evidence for pars tuberalis-specific cell types
    • Guerra, M.M. and E.M. Rodriguez, 2009. Expression of tuberalin II, a-subunit of glycoprotein hormones and a-thyrotropin hormone in the pars tuberalis of the rat: Immunocytochemical evidence for pars tuberalis-specific cell types. Neuroendocrinology, 90: 269-282.
    • (2009) Neuroendocrinology , vol.90 , pp. 269-282
    • Guerra, M.M.1    Rodriguez, E.M.2
  • 41
    • 78650891915 scopus 로고    scopus 로고
    • Relationship between thyrotropin receptor hinge region proteolytic posttranslational modification and receptor physiological function
    • Hamidi, S., C.R. Chen, Y. Mizutori-Sasai, S.M. Mclachan and B. Rapoport, 2011. Relationship between thyrotropin receptor hinge region proteolytic posttranslational modification and receptor physiological function. Mol. Endocrinol., 25: 184-194.
    • (2011) Mol. Endocrinol , vol.25 , pp. 184-194
    • Hamidi, S.1    Chen, C.R.2    Mizutori-Sasai, Y.3    McLachan, S.M.4    Rapoport, B.5
  • 45
    • 37549003693 scopus 로고    scopus 로고
    • Cleavage of the human thyrotropin receptor by AD AMI 0 is regulated by thyrotropin
    • Kaczur, V., L.G. Puskas, Z.U. Nagy, N. Miled and A. Rebai et al, 2007. Cleavage of the human thyrotropin receptor by AD AMI 0 is regulated by thyrotropin. J. Mol. Recognition, 20: 392-404.
    • (2007) J. Mol. Recognition , vol.20 , pp. 392-404
    • Kaczur, V.1    Puskas, L.G.2    Nagy, Z.U.3    Miled, N.4    Rebai, A.5
  • 46
    • 0029645408 scopus 로고
    • Modeling of the three-dimensional structure of proteins with the typical leucine-rich repeats
    • Kajava, A.V., G. Vassart and S. J. Wodak, 1995. Modeling of the three-dimensional structure of proteins with the typical leucine-rich repeats. Structure, 3: 867-877.
    • (1995) Structure , vol.3 , pp. 867-877
    • Kajava, A.V.1    Vassart, G.2    Wodak, S.J.3
  • 47
    • 0021797466 scopus 로고
    • Analysis of thyrotropin receptors by photoaffinity labelling. Orientation of receptor subunits in the cell membrane
    • Kajita, Y., C.R. Rickards, P.R. Buckland, R.D. Howells and B. Rees Smith, 1995. Analysis of thyrotropin receptors by photoaffinity labelling. Orientation of receptor subunits in the cell membrane. Biochem. J., 227: 413-420.
    • (1995) Biochem. J , vol.227 , pp. 413-420
    • Kajita, Y.1    Rickards, C.R.2    Buckland, P.R.3    Howells, R.D.4    Rees Smith, B.5
  • 48
    • 23844467711 scopus 로고    scopus 로고
    • TSH 6 receptor mutation V509A causes familial hyperthyroidism by release of interhelical constraints between transmembrane helices TMH3 and TMH5
    • Karges, B., G. Krause, J. Homoki, K.M. Debatin, N. De Roux and W. Karges, 2005. TSH 6 receptor mutation V509A causes familial hyperthyroidism by release of interhelical constraints between transmembrane helices TMH3 and TMH5. J. Endocrinol, 186: 377-385.
    • (2005) J. Endocrinol , vol.186 , pp. 377-385
    • Karges, B.1    Krause, G.2    Homoki, J.3    Debatin, K.M.4    de Roux, N.5    Karges, W.6
  • 49
    • 0033312613 scopus 로고    scopus 로고
    • A germline mutation of the thyrotropin receptor gene associated with thyrotoxicosis and mitral valve prolapse in a Chinese family
    • Khoo, D.H., J. Parma, C. Rajasoorya, S.C. Ho and G. Vassart, 1999. A germline mutation of the thyrotropin receptor gene associated with thyrotoxicosis and mitral valve prolapse in a Chinese family. J. Clin Endocrinol. Metab., 84: 1459-1462.
    • (1999) J. Clin Endocrinol. Metab , vol.84 , pp. 1459-1462
    • Khoo, D.H.1    Parma, J.2    Rajasoorya, C.3    Ho, S.C.4    Vassart, G.5
  • 50
    • 1842276431 scopus 로고    scopus 로고
    • A novel germline mutation in the TSH receptor gene causing nonautoimmune congenital hyperthyroidism
    • Kohler, B., H. Biebermann, H.P. Krohn, D. Dralle, R Finke and A. Gruters, 1996. A novel germline mutation in the TSH receptor gene causing nonautoimmune congenital hyperthyroidism. Int. Congress Endocrinol, 946: 641-641.
    • (1996) Int. Congress Endocrinol , vol.946 , pp. 641
    • Kohler, B.1    Biebermann, H.2    Krohn, H.P.3    Dralle, D.4    Finke, R.5    Gruters, A.6
  • 51
    • 0028891649 scopus 로고
    • Congenital non-autoimmune hyperthyroidism caused by a neomutation in the thyrotropin receptor gene
    • Kopp, P., J. van Sande, L. Parma, K. Duprez, J.L. Zuppinger and G. Vassart, 1995. Congenital non-autoimmune hyperthyroidism caused by a neomutation in the thyrotropin receptor gene. New Engl. J. Med., 332: 150-154.
    • (1995) New Engl. J. Med , vol.332 , pp. 150-154
    • Kopp, P.1    van Sande, J.2    Parma, L.3    Duprez, K.4    Zuppinger, J.L.5    Vassart, G.6
  • 52
    • 0031406420 scopus 로고    scopus 로고
    • Congenital nonautoimmune hyperthyroidism in a nonidentical twin caused by a sporadic germline mutation in the thyrotropin receptor gene
    • Kopp, P., J.L. Jameson and T.F. Roe, 1997a. Congenital nonautoimmune hyperthyroidism in a nonidentical twin caused by a sporadic germline mutation in the thyrotropin receptor gene. Thyroid., 7: 765-770.
    • (1997) Thyroid , vol.7 , pp. 765-770
    • Kopp, P.1    Jameson, J.L.2    Roe, T.F.3
  • 53
    • 0030830146 scopus 로고    scopus 로고
    • Congenital hyperthyroidism caused by a solitary toxic adenoma harboring a novel somatic mutation(serine281~>isoleucine) in the extracellular domain of the thyrotropin receptor
    • Kopp, P., S. Mmrhead, N. Jourdain, W.X. Gu, J.L. Jameson and C. Rodd, 1997b. Congenital hyperthyroidism caused by a solitary toxic adenoma harboring a novel somatic mutation(serine281~>isoleucine) in the extracellular domain of the thyrotropin receptor. J. Clin. Invest, 100: 1634-1639.
    • (1997) J. Clin. Invest , vol.100 , pp. 1634-1639
    • Kopp, P.1    Mmrhead, S.2    Jourdain, N.3    Gu, W.X.4    Jameson, J.L.5    Rodd, C.6
  • 54
    • 0028863032 scopus 로고
    • TSH receptor and LH receptor, 1995
    • Kosugi, S. and T. Mori, 1995. TSH receptor and LH receptor, 1995. Endocrine J., 42: 587-606.
    • (1995) Endocrine J , vol.42 , pp. 587-606
    • Kosugi, S.1    Mori, T.2
  • 55
    • 0030348037 scopus 로고    scopus 로고
    • TSH receptor andLH receptor
    • Kosugi, S., H. Sugawa and T. Mori, 1996. TSH receptor andLH receptor. Endocrine J., 43: 595-604.
    • (1996) Endocrine J , vol.43 , pp. 595-604
    • Kosugi, S.1    Sugawa, H.2    Mori, T.3
  • 56
    • 0036484957 scopus 로고    scopus 로고
    • Non-autoimmune hyperthyroidism and hyperfunctioning thyroid adenomas caused by activating mutation of the thyrotropin receptor
    • Kosugi, S., 2002. [Non-autoimmune hyperthyroidism and hyperfunctioning thyroid adenomas caused by activating mutation of the thyrotropin receptor] Nippon Rmsho, 60: 291-296.
    • (2002) Nippon Rmsho , vol.60 , pp. 291-296
    • Kosugi, S.1
  • 57
    • 65349158284 scopus 로고    scopus 로고
    • Activating TSH-receptor mutation (Met453Thr) as a cause of adenomatous non-autoimmune hyperthyroidism in a 3-year-old boy
    • Kraemer, S., K. Rothe, R. Pfaeffle, D. Fuehrer-Sakel, H. Till and O.J. Muensterer, 2009. Activating TSH-receptor mutation (Met453Thr) as a cause of adenomatous non-autoimmune hyperthyroidism in a 3-year-old boy. J. Pediatr. Endocrinol. Metab., 22: 269-274.
    • (2009) J. Pediatr. Endocrinol. Metab , vol.22 , pp. 269-274
    • Kraemer, S.1    Rothe, K.2    Pfaeffle, R.3    Fuehrer-Sakel, D.4    Till, H.5    Muensterer, O.J.6
  • 58
    • 78049283290 scopus 로고    scopus 로고
    • Identification and evaluation of constitutively active thyroid stimulating hormone receptor mutations
    • Lado-Abeal, J., L.R. Quisenberry and I. Castro-Piedras, 2010. Identification and evaluation of constitutively active thyroid stimulating hormone receptor mutations. Methods Enzymol., 484: 375-395.
    • (2010) Methods Enzymol , vol.484 , pp. 375-395
    • Lado-Abeal, J.1    Quisenberry, L.R.2    Castro-Piedras, I.3
  • 59
    • 79953250109 scopus 로고    scopus 로고
    • A family with congenital hypothyroidism caused by a combination of loss-of-function mutations in the thyrotropin receptor and adenylate cyclase-stimulating G a-protein subunit genes
    • Lado-Abeal, J., I. Castro-Piedras, F. Palos-Paz, J.I. Labarta-Aizpun and R. Albero-Gamboa, 2011. A family with congenital hypothyroidism caused by a combination of loss-of-function mutations in the thyrotropin receptor and adenylate cyclase-stimulating G a-protein subunit genes. Thyroid, 21: 103-109.
    • (2011) Thyroid , vol.21 , pp. 103-109
    • Lado-Abeal, J.1    Castro-Piedras, I.2    Palos-Paz, F.3    Labarta-Aizpun, J.I.4    Albero-Gamboa, R.5
  • 60
    • 77949700065 scopus 로고    scopus 로고
    • A Tyrosine residue on the TSH receptor stabilizews multimer formation
    • Latif, R, K. Michalk, S.A. Morshed and T.F. Davis, 2010a. A Tyrosine residue on the TSH receptor stabilizews multimer formation. PloS One, 5: e9449-e9449.
    • (2010) PloS One , vol.5
    • Latif, R.1    Michalk, K.2    Morshed, S.A.3    Davis, T.F.4
  • 61
    • 77957373574 scopus 로고    scopus 로고
    • Subunit interactions influence TSHR multimerization
    • Latif, R., K. Michalek and T.F. Davies, 2010b. Subunit interactions influence TSHR multimerization. Mol. Endocrinol, 24: 2009-2018.
    • (2010) Mol. Endocrinol , vol.24 , pp. 2009-2018
    • Latif, R.1    Michalek, K.2    Davies, T.F.3
  • 62
    • 34347257788 scopus 로고    scopus 로고
    • Lipid rafts are triage centers for multimeric and monomeric thyrotropin receptor regulation
    • Latif, R., T. Ando and T.F. Davies, 2007. Lipid rafts are triage centers for multimeric and monomeric thyrotropin receptor regulation. Endocrinology, 148: 3164-3175.
    • (2007) Endocrinology , vol.148 , pp. 3164-3175
    • Latif, R.1    Ando, T.2    Davies, T.F.3
  • 63
    • 0036002619 scopus 로고    scopus 로고
    • An activating mutation of the thyrotropin receptor gene in hereditary non-autoimmune hyperthyroidism
    • Lee, Y.S., L. Poh and K.Y. Loke, 2002. An activating mutation of the thyrotropin receptor gene in hereditary non-autoimmune hyperthyroidism. J. Pediatr. Endocrinol. Metab., 15: 211-215.
    • (2002) J. Pediatr. Endocrinol. Metab , vol.15 , pp. 211-215
    • Lee, Y.S.1    Poh, L.2    Loke, K.Y.3
  • 64
    • 0034282881 scopus 로고    scopus 로고
    • Bioengineering of human thyrotropin superactive analogs by site-directed lysine-scanning mutagenesis: Cooperative effects between peripheral loops
    • Leitolf, H., K.P.T. Tong, M. Grossmann, B.D. Wemtraub and M.W. Szkudlinski, 2000. Bioengineering of human thyrotropin superactive analogs by site-directed lysine-scanning mutagenesis: Cooperative effects between peripheral loops. J. Biol. Chem., 275: 27457-27465.
    • (2000) J. Biol. Chem , vol.275 , pp. 27457-27465
    • Leitolf, H.1    Tong, K.P.T.2    Grossmann, M.3    Wemtraub, B.D.4    Szkudlinski, M.W.5
  • 65
    • 79955557364 scopus 로고    scopus 로고
    • Common genetic variation in the 3'-untranslated region of gonadotropin-re leasing hormone receptor regulates gene expression in cella and is associated with thyroid function, insulin secretion as well as insulin sensitivity in polycystic ovary syndrome patients
    • Li, Q., G. Yang, Y. Wang, X. Zhang and Q. Sang et ed., 2011. Common genetic variation in the 3'-untranslated region of gonadotropin-re leasing hormone receptor regulates gene expression in cella and is associated with thyroid function, insulin secretion as well as insulin sensitivity in polycystic ovary syndrome patients. Hum. Genet.
    • (2011) Hum. Genet
    • Li, Q.1    Yang, G.2    Wang, Y.3    Zhang, X.4    Sang, Q.5
  • 67
    • 0027136111 scopus 로고
    • Affinity maturation of human growth hormone by monovalent phage display
    • Lowman, H.B. and J. A. Wells, 1993. Affinity maturation of human growth hormone by monovalent phage display. J. Mol. Biol, 234: 564-578.
    • (1993) J. Mol. Biol , vol.234 , pp. 564-578
    • Lowman, H.B.1    Wells, J.A.2
  • 68
  • 69
    • 33745144355 scopus 로고    scopus 로고
    • Deoxyribonucleic acid damage and spontaneous mutagenesis in the thyroid gland of rats and mice
    • Maier, J., H. van Steeg, C. van Oostrom, S. Karger, R. Paschke and K. Krohn, 2006. Deoxyribonucleic acid damage and spontaneous mutagenesis in the thyroid gland of rats and mice. Endocrinology, 147: 3391-3397.
    • (2006) Endocrinology , vol.147 , pp. 3391-3397
    • Maier, J.1    van Steeg, H.2    van Oostrom, C.3    Karger, S.4    Paschke, R.5    Krohn, K.6
  • 70
    • 78650310186 scopus 로고    scopus 로고
    • Studies on stabilities of some human chorionic gonadotropin complexes with a-emitting radionuclides
    • Maiti, M., K. Sen, S. Sen and S. Lahiri, 2011. Studies on stabilities of some human chorionic gonadotropin complexes with a-emitting radionuclides. Applied Radiation Isotopes, 69: 316-319.
    • (2011) Applied Radiation Isotopes , vol.69 , pp. 316-319
    • Maiti, M.1    Sen, K.2    Sen, S.3    Lahiri, S.4
  • 74
    • 77954439713 scopus 로고    scopus 로고
    • Maternal thyroid stimulating hormone level during the first trimester of pregnancy at South East of Caspian sea in Iran
    • Mansourian, A.R., A.R. Ahmadi, H.R Mansourian, A. Sifi, A. Marjani and E. Ghaemi, 2010b. Maternal thyroid stimulating hormone level during the first trimester of pregnancy at South East of Caspian sea in Iran. J. Clin. Diagnostic Res., 4: 2472-2477.
    • (2010) J. Clin. Diagnostic Res , vol.4 , pp. 2472-2477
    • Mansourian, A.R.1    Ahmadi, A.R.2    Mansourian, H.R.3    Sifi, A.4    Marjani, A.5    Ghaemi, E.6
  • 75
    • 77957560325 scopus 로고    scopus 로고
    • A review on post-puberty hypothyroidism: Agalance at myxedema
    • Mansourian, A.R., 2010a. A review on post-puberty hypothyroidism: Agalance at myxedema. Pak. J. Biol. Sci., 13: 866-876.
    • (2010) Pak. J. Biol. Sci , vol.13 , pp. 866-876
    • Mansourian, A.R.1
  • 76
    • 79251485983 scopus 로고    scopus 로고
    • Metabolic pathways of tetraidothyronine(T4) and triidothyronin(T3) production by thyroid gland: A review of articles
    • Mansourian, A.R., 2010b. Metabolic pathways of tetraidothyronine(T4) and triidothyronin(T3) production by thyroid gland: A review of articles. Pak. J. Biol. Sci., 14: 1-12.
    • (2010) Pak. J. Biol. Sci , vol.14 , pp. 1-12
    • Mansourian, A.R.1
  • 77
    • 77957658549 scopus 로고    scopus 로고
    • Thyroid function tests during first-trimester of pregnancy: A reviewof Litrature
    • Mansourian, A.R., 2010c. Thyroid function tests during first-trimester of pregnancy: A reviewof Litrature. Pak. J. Biol. Sci., 13: 664-673.
    • (2010) Pak. J. Biol. Sci , vol.13 , pp. 664-673
    • Mansourian, A.R.1
  • 78
    • 77957586082 scopus 로고    scopus 로고
    • The immune system which adversely alter thyroid functions: A review on the concept of autoimmunity
    • Mansourian, A.R., 2010d. The immune system which adversely alter thyroid functions: A review on the concept of autoimmunity. Pak. J. Biol. Sci., 13: 765-774.
    • (2010) Pak. J. Biol. Sci , vol.13 , pp. 765-774
    • Mansourian, A.R.1
  • 79
    • 78249277434 scopus 로고    scopus 로고
    • A review on hyperthyroidism: Thyrotoxicosis under surveillance
    • Mansourian, A.R., 2010e. A review on hyperthyroidism: Thyrotoxicosis under surveillance. Pak. J. Biol. Sci., 13: 1066-1076.
    • (2010) Pak. J. Biol. Sci , vol.13 , pp. 1066-1076
    • Mansourian, A.R.1
  • 80
    • 78650260609 scopus 로고    scopus 로고
    • Correlation between inverse age and serum thyroxine level among children and adolescents
    • Mansourian, A.R. and A.R. Ahmadi, 2010. Correlation between inverse age and serum thyroxine level among children and adolescents. J. Clin. Diagnostic Res., 4: 3196-3200.
    • (2010) J. Clin. Diagnostic Res , vol.4 , pp. 3196-3200
    • Mansourian, A.R.1    Ahmadi, A.R.2
  • 81
    • 48249085386 scopus 로고    scopus 로고
    • Lipidperoxidation in serum ofhypothyroidpatients in Gorgan-South Eastof Caspian Sea
    • Marjani, A., A.R. Mansourian, E.O. Ghaemi, A. Aahmadi and V. Khori, 2008. Lipidperoxidation in serum ofhypothyroidpatients in Gorgan-South Eastof Caspian Sea. Asian J. Cell Biol, 3: 47-50.
    • (2008) Asian J. Cell Biol , vol.3 , pp. 47-50
    • Marjani, A.1    Mansourian, A.R.2    Ghaemi, E.O.3    Aahmadi, A.4    Khori, V.5
  • 82
    • 0028225588 scopus 로고
    • Processing of the precursors of the human thyroid-stimulating hormone receptor in various eukaryotic cells (human thyrocytes, transfected L cells and baculovirus-infected insect cells)
    • Misarhi, M., N. Ghinea, S. Sar, B. Saunier and A. Jolivete, 1994. Processing of the precursors of the human thyroid-stimulating hormone receptor in various eukaryotic cells (human thyrocytes, transfected L cells and baculovirus-infected insect cells). Eur. J. Biochem., 222: 711-719.
    • (1994) Eur. J. Biochem , vol.222 , pp. 711-719
    • Misarhi, M.1    Ghinea, N.2    Sar, S.3    Saunier, B.4    Jolivete, A.5
  • 83
    • 27944503012 scopus 로고    scopus 로고
    • Induction of GH, PRL and TSH beta mRNA by transfection of Pit-1 in a human pituitary adenoma-derived cell line
    • Miyai, S., S. Yoshimura, Y. Iwasaki, S. Takekoshi, R. V. Lloyd and R. Y. Osamura, 2005. Induction of GH, PRL and TSH beta mRNA by transfection of Pit-1 in a human pituitary adenoma-derived cell line. Cell Tissue Res., 322: 269-277.
    • (2005) Cell Tissue Res , vol.322 , pp. 269-277
    • Miyai, S.1    Yoshimura, S.2    Iwasaki, Y.3    Takekoshi, S.4    Lloyd, R.V.5    Osamura, R.Y.6
  • 84
    • 79951508420 scopus 로고    scopus 로고
    • Immuno-localisation of anti-thyroid antibodies in adult human cerebral cortex
    • 10.1016/j.jns.2010.11.027
    • Moodley, K., J. Botha, D.M. Raidoo and S. Naidoo, 2010. Immuno-localisation of anti-thyroid antibodies in adult human cerebral cortex. J. Neurol. Sci., 10.1016/j.jns.2010.11.027
    • (2010) J. Neurol. Sci
    • Moodley, K.1    Botha, J.2    Raidoo, D.M.3    Naidoo, S.4
  • 85
  • 86
    • 0027129826 scopus 로고
    • Characterization of human thyrotropin receptor-related peptide-like immunoreactivity in peripheral blood of Graves disease
    • Murakami, M., K. Miyashita, M. Yamada, T. Iriuchijima and M. Mori, 1992. Characterization of human thyrotropin receptor-related peptide-like immunoreactivity in peripheral blood of Graves disease. Biochem. Biophys. Res. Commun, 186: 1074-1080.
    • (1992) Biochem. Biophys. Res. Commun , vol.186 , pp. 1074-1080
    • Murakami, M.1    Miyashita, K.2    Yamada, M.3    Iriuchijima, T.4    Mori, M.5
  • 87
    • 0034730516 scopus 로고    scopus 로고
    • Activation of the luteinizing hormone receptor following substitution of Ser-277 with selective hydrophobic residues in the ectodomain hinge region
    • Nakabayashi, K., M. Kudo, B. Kobilka and A.J. Hsueh, 2000. Activation of the luteinizing hormone receptor following substitution of Ser-277 with selective hydrophobic residues in the ectodomain hinge region. J. Biol. Chem., 275: 30264-30271.
    • (2000) J. Biol. Chem , vol.275 , pp. 30264-30271
    • Nakabayashi, K.1    Kudo, M.2    Kobilka, B.3    Hsueh, A.J.4
  • 89
    • 78049513746 scopus 로고    scopus 로고
    • Contitutivity active thyrotropin and throtropin -releasing hormone receptors and their inverse agonists
    • Neumann, S., B.M. Raaka and M.C. Gershengorn, 2010. Contitutivity active thyrotropin and throtropin -releasing hormone receptors and their inverse agonists. Methods Enzymol., 485: 147-160.
    • (2010) Methods Enzymol , vol.485 , pp. 147-160
    • Neumann, S.1    Raaka, B.M.2    Gershengorn, M.C.3
  • 90
    • 67649361912 scopus 로고    scopus 로고
    • Thyroid stimulating autoantibody M22 mimics TSH binding to the TSH receptor leucine rich domain: A comparative structural study of protein-protein interactions
    • NunezMiguel, R, J. Sanders, D.Y. Chirgadze, J. Furmaniak and B.R. Smith, 2009. Thyroid stimulating autoantibody M22 mimics TSH binding to the TSH receptor leucine rich domain: A comparative structural study of protein-protein interactions. J. Mol. Endocrinol, 42: 381-395.
    • (2009) J. Mol. Endocrinol , vol.42 , pp. 381-395
    • Nunezmiguel, R.1    Sanders, J.2    Chirgadze, D.Y.3    Furmaniak, J.4    Smith, B.R.5
  • 92
    • 0034505940 scopus 로고    scopus 로고
    • Epitope analysis of the human thyrotropin (TSH) receptor using monoclonal antibodies
    • Oda, Y., J. Sanders, M. Evans, A. Kiddie and A. Munkley et al., 2000. Epitope analysis of the human thyrotropin (TSH) receptor using monoclonal antibodies. Thyroid., 10: 1051-1059.
    • (2000) Thyroid , vol.10 , pp. 1051-1059
    • Oda, Y.1    Sanders, J.2    Evans, M.3    Kiddie, A.4    Munkley, A.5
  • 93
    • 0030868842 scopus 로고    scopus 로고
    • Co-expression of defective luteinizing hormone receptor fragments partially reconstitutes ligand-induced signal generation
    • Osuga, Y., M. Hayashi, M. Kudo, M. Conti, B. Kobilka and A.J. Hsueh, 1997. Co-expression of defective luteinizing hormone receptor fragments partially reconstitutes ligand-induced signal generation. J. Biol Chem., 272: 25006-25012.
    • (1997) J. Biol Chem , vol.272 , pp. 25006-25012
    • Osuga, Y.1    Hayashi, M.2    Kudo, M.3    Conti, M.4    Kobilka, B.5    Hsueh, A.J.6
  • 95
    • 0034604451 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: A G protein-coupled receptor
    • Palczewski, K., T. Kumasaka, T. Hori, C.A. Behnke and H. Motoshima et al., 2000. Crystal structure of rhodopsin: A G protein-coupled receptor. Sci., 289: 739-745.
    • (2000) Sci , vol.289 , pp. 739-745
    • Palczewski, K.1    Kumasaka, T.2    Hori, T.3    Behnke, C.A.4    Motoshima, H.5
  • 96
    • 56749156643 scopus 로고    scopus 로고
    • Prevalence of mutations in TSHR, GNAS, PRKARIA and RAS genes in a large series of toxic thyroid adenomas from Galicia, an iodine-deficient area in NW Spam
    • Palos-Paz, F., O. Perez-Guerra, J. Cameselle-Teijeiro, C. Rueda-Chimeno and F. Barreiro-Morandeira et al., 2008. Prevalence of mutations in TSHR, GNAS, PRKARIA and RAS genes in a large series of toxic thyroid adenomas from Galicia, an iodine-deficient area in NW Spam. Eur. J. Endocrinol, 159: 623-631.
    • (2008) Eur. J. Endocrinol , vol.159 , pp. 623-631
    • Palos-Paz, F.1    Perez-Guerra, O.2    Cameselle-Teijeiro, J.3    Rueda-Chimeno, C.4    Barreiro-Morandeira, F.5
  • 98
    • 8544221172 scopus 로고    scopus 로고
    • Diversity and prevalence of somatic mutations adenomas in the TSH receptor and Gs a genes as a cause of toxic thyroid Adenomas
    • Parma, J., L. Duprez, J. van Sande, G. Hermans and G. van Vlietx, 1997. Diversity and prevalence of somatic mutations adenomas in the TSH receptor and Gs a genes as a cause of toxic thyroid Adenomas. J. Clin. Endocrinol. Metab., 82: 2695-2701.
    • (1997) J. Clin. Endocrinol. Metab , vol.82 , pp. 2695-2701
    • Parma, J.1    Duprez, L.2    van Sande, J.3    Hermans, G.4    van Vlietx, G.5
  • 100
    • 79957506246 scopus 로고    scopus 로고
    • Thyroid disruptor l,l,l-trichloro-2,2-bis(p-chlorophenyl)ethane (DDT) prevents internalization of TSH receptor
    • Picchietti, S., M. Belardinelli, A.R. Taddei, A.M. Fausto and M. Pellegrino et al., 2009. Thyroid disruptor l,l,l-trichloro-2,2-bis(p-chlorophenyl)ethane (DDT) prevents internalization of TSH receptor. Cell. Tissue Res., 336: 31-40.
    • (2009) Cell. Tissue Res , vol.336 , pp. 31-40
    • Picchietti, S.1    Belardinelli, M.2    Taddei, A.R.3    Fausto, A.M.4    Pellegrino, M.5
  • 101
    • 0043017261 scopus 로고    scopus 로고
    • Proteolytic enzyme activation of rat ovarian adenylate cyclase
    • Richert, N.D. and R.J. Ryan, 1997. Proteolytic enzyme activation of rat ovarian adenylate cyclase. Proc. Natl. Acad. Sci. USA., 74: 4857-4861.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 4857-4861
    • Richert, N.D.1    Ryan, R.J.2
  • 102
    • 0032542355 scopus 로고    scopus 로고
    • Familial gestational hyperthyroidism caused by a mutant thyrotropin receptor hypersensitive to human chorionic gonadotropin
    • Rodien, P., C. Bremont, M.L. Sanson, J. Parma and J. van Sande et al., 1998. Familial gestational hyperthyroidism caused by a mutant thyrotropin receptor hypersensitive to human chorionic gonadotropin. N. Engl. J. Med., 339: 1823-1826.
    • (1998) N. Engl. J. Med , vol.339 , pp. 1823-1826
    • Rodien, P.1    Bremont, C.2    Sanson, M.L.3    Parma, J.4    van Sande, J.5
  • 103
    • 24644504859 scopus 로고    scopus 로고
    • Dominant portion of thyrotropin-releasing hormone receptor is excluded from lipid domains. Detergent-resistant and detergent-sensitive pools of TRH receptor and Gqalpha/Gl 1 alpha protein
    • Rudajev, V., J. Novotny, L. Hejnova, G. Milligan and P. Svoboda, 2005. Dominant portion of thyrotropin-releasing hormone receptor is excluded from lipid domains. Detergent-resistant and detergent-sensitive pools of TRH receptor and Gqalpha/Gl 1 alpha protein. J. Biochem., 138: 111-125.
    • (2005) J. Biochem , vol.138 , pp. 111-125
    • Rudajev, V.1    Novotny, J.2    Hejnova, L.3    Milligan, G.4    Svoboda, P.5
  • 104
    • 0025719831 scopus 로고
    • A new structural model for the thyrotropin (TSH) receptor as determined by covalent crosslinking of TSH to the recombinant receptor in intact cells: Evidence for a single polypeptide chain
    • Russo, D., G.D. Chazenbalk, Y. Nagayama, H.L. Wadsworth, P. Seto and B. Rapoport, 1991. A new structural model for the thyrotropin (TSH) receptor as determined by covalent crosslinking of TSH to the recombinant receptor in intact cells: Evidence for a single polypeptide chain. Mol. Endocrinol, 5: 1607-1612.
    • (1991) Mol. Endocrinol , vol.5 , pp. 1607-1612
    • Russo, D.1    Chazenbalk, G.D.2    Nagayama, Y.3    Wadsworth, H.L.4    Seto, P.5    Rapoport, B.6
  • 105
    • 0026518857 scopus 로고
    • Role of amino acids 261-418 in proteolytic cleavage of the extracellular region of the human thyrotropin receptor
    • Russo, D., Y. Nagayama, G.D. Chazenbalk, H.L. Wadsworth and B. Rapoport, 1992. Role of amino acids 261-418 in proteolytic cleavage of the extracellular region of the human thyrotropin receptor. Endocrinology, 130: 2135-2138.
    • (1992) Endocrinology , vol.130 , pp. 2135-2138
    • Russo, D.1    Nagayama, Y.2    Chazenbalk, G.D.3    Wadsworth, H.L.4    Rapoport, B.5
  • 107
    • 0030998004 scopus 로고    scopus 로고
    • Molecular insights into TSH receptor abnormality and thyroid disease
    • Russo, D., F. Arturi, E. Chiefari and S. Filetti, 1997. Molecular insights into TSH receptor abnormality and thyroid disease. J. Endocrinol. Invest., 20: 36-47.
    • (1997) J. Endocrinol. Invest , vol.20 , pp. 36-47
    • Russo, D.1    Arturi, F.2    Chiefari, E.3    Filetti, S.4
  • 108
    • 0034527615 scopus 로고    scopus 로고
    • A novel mutation in the thyrotropin (TSH) receptor gene causing loss of TSH binding but constitutive receptor activation in a family with resistance to TSH
    • Russo, D., C. Betterle, F. Arturi, E. Chiefari, M.E. Girelh and S. Filetti, 2000. A novel mutation in the thyrotropin (TSH) receptor gene causing loss of TSH binding but constitutive receptor activation in a family with resistance to TSH. J. Clin. Endocrinol. Metab., 85: 4238-4242.
    • (2000) J. Clin. Endocrinol. Metab , vol.85 , pp. 4238-4242
    • Russo, D.1    Betterle, C.2    Arturi, F.3    Chiefari, E.4    Girelh, M.E.5    Filetti, S.6
  • 109
    • 58549118946 scopus 로고    scopus 로고
    • The effect of ambient temperature on thyroid hormones concentration and histopathologic al changes of thyroid gland in cattle in Tabriz, Iran
    • Saber, A.P.R., M.T. Jalali, D. Mohjen, A.A. Akhoole, H.Z.N. Teymourluei, M. Nouri and S. Garachorlo, 2009. The effect of ambient temperature on thyroid hormones concentration and histopathologic al changes of thyroid gland in cattle in Tabriz, Iran. Asian J. Anim. Vet. Adv., 4: 28-33.
    • (2009) Asian J. Anim. Vet. Adv , vol.4 , pp. 28-33
    • Saber, A.P.R.1    Jalali, M.T.2    Mohjen, D.3    Akhoole, A.A.4    Teymourluei, H.Z.N.5    Nouri, M.6    Garachorlo, S.7
  • 110
    • 34249941108 scopus 로고    scopus 로고
    • Crystal structure of the TSH receptor in complex with a thyroid-stimulating autoantibody
    • Sanders, J., D.Y. Chirgadze, P. Sanders, S. Baker and A. Sullivanx 2007. Crystal structure of the TSH receptor in complex with a thyroid-stimulating autoantibody. Thyroid, 17: 395-410.
    • (2007) Thyroid , vol.17 , pp. 395-410
    • Sanders, J.1    Chirgadze, D.Y.2    Sanders, P.3    Baker, S.4    Sullivanx, A.5
  • 111
    • 78049488270 scopus 로고    scopus 로고
    • TSH receptor monoclonal antibodies with agonist, antagonist and inverse agonist activities
    • Sanders, J., R.N. Miguel, J. Furmaniak and B.R. Smith, 2010. TSH receptor monoclonal antibodies with agonist, antagonist and inverse agonist activities. Methods Enzymol, 485: 393-420.
    • (2010) Methods Enzymol , vol.485 , pp. 393-420
    • Sanders, J.1    Miguel, R.N.2    Furmaniak, J.3    Smith, B.R.4
  • 112
    • 79953675359 scopus 로고    scopus 로고
    • Crystal structure of the TSH receptor bound to a blocking type TSHR autoantibody
    • 10.1530/JME-10-0127
    • Sanders, P., S. Young, J. Sanders, K. Kabelis and S. Baker et al, 2011. Crystal structure of the TSH receptor bound to a blocking type TSHR autoantibody. J. Mol. Endocrinol., 10.1530/JME-10-0127
    • (2011) J. Mol. Endocrinol
    • Sanders, P.1    Young, S.2    Sanders, J.3    Kabelis, K.4    Baker, S.5
  • 113
    • 0027177102 scopus 로고
    • Interaction of barnase with its polypeptide inhibitor barstar studied by protein engineering
    • Schreiber, G. and A.R. Fersht, 1993. Interaction of barnase with its polypeptide inhibitor barstar studied by protein engineering. Biochemistry, 32: 5145-5150.
    • (1993) Biochemistry , vol.32 , pp. 5145-5150
    • Schreiber, G.1    Fersht, A.R.2
  • 114
    • 0028157562 scopus 로고
    • A recombinant extracellular domain of the thyrotropin (TSH) receptor binds TSH in the absence of membranes
    • Seetharamaiah, G.S., A. Kurosky, R.K. Desai, J.S. Dallas and B.S. Prabhakar, 1994. A recombinant extracellular domain of the thyrotropin (TSH) receptor binds TSH in the absence of membranes. Endocrinology, 134: 549-554.
    • (1994) Endocrinology , vol.134 , pp. 549-554
    • Seetharamaiah, G.S.1    Kurosky, A.2    Desai, R.K.3    Dallas, J.S.4    Prabhakar, B.S.5
  • 115
    • 73349133317 scopus 로고    scopus 로고
    • Serum thyroid hormone level in women with nausea and vomiting in early pregnancy
    • Shahmohammdi, F., A.R. Mansourian and H.R Mansourian, 2008. Serum thyroid hormone level in women with nausea and vomiting in early pregnancy. J. Med. Sci., 8: 507-510.
    • (2008) J. Med. Sci , vol.8 , pp. 507-510
    • Shahmohammdi, F.1    Mansourian, A.R.2    Mansourian, H.R.3
  • 116
    • 35948945305 scopus 로고    scopus 로고
    • Review TSH receptor antibodies
    • Smith, B.R., J. Sanders and J. Furmaniak, 2007. Review TSH receptor antibodies. Thyroid, 17: 923-938.
    • (2007) Thyroid , vol.17 , pp. 923-938
    • Smith, B.R.1    Sanders, J.2    Furmaniak, J.3
  • 119
    • 0029093051 scopus 로고
    • Rarity of oncogenic mutations in the thyrotropin receptor of autonomously functioning thyroid nodules in Japan
    • Takeshita, A., Y. Nagayama, N. Yokoyama, K. Ishikawa and K. Ito et al., 1995. Rarity of oncogenic mutations in the thyrotropin receptor of autonomously functioning thyroid nodules in Japan. J. Clin. Endocrinol. Metab., 80: 2607-2611.
    • (1995) J. Clin. Endocrinol. Metab , vol.80 , pp. 2607-2611
    • Takeshita, A.1    Nagayama, Y.2    Yokoyama, N.3    Ishikawa, K.4    Ito, K.5
  • 121
    • 78349272440 scopus 로고    scopus 로고
    • Genetic susceptibility to autoimmune thyroid disease: Past, present and future
    • Tomer, Y., 2010. Genetic susceptibility to autoimmune thyroid disease: Past, present and future. Thyroid, 20: 715-725.
    • (2010) Thyroid , vol.20 , pp. 715-725
    • Tomer, Y.1
  • 122
    • 9044240477 scopus 로고    scopus 로고
    • Functional characteristics of three new germline mutations of the thyrotropin receptor gene causing autosomal dominant toxic thyroid hyperplasia
    • Tonacchera, M., J. Van Sande, F. Cetani, S. Swillens and C. Schvartz et al., 1996. Functional characteristics of three new germline mutations of the thyrotropin receptor gene causing autosomal dominant toxic thyroid hyperplasia. J. Clin. Endocrinol. Metab., 81: 547-554.
    • (1996) J. Clin. Endocrinol. Metab , vol.81 , pp. 547-554
    • Tonacchera, M.1    van Sande, J.2    Cetani, F.3    Swillens, S.4    Schvartz, C.5
  • 123
    • 13144255717 scopus 로고    scopus 로고
    • Activating thyrotropin receptor mutations in histologically heterogeneous hyperfunctioning nodules of multinodular goiter
    • Tonacchera, M., P. V itti, P. Agretti, B. Giulianetti and B. Mazzi etal., 1998a. Activating thyrotropin receptor mutations in histologically heterogeneous hyperfunctioning nodules of multinodular goiter. Thyroid., 8: 559-564.
    • (1998) Thyroid , vol.8 , pp. 559-564
    • Tonacchera, M.1    Itti, P.V.2    Agretti, P.3    Giulianetti, B.4    Mazzi, B.5
  • 124
    • 15144351998 scopus 로고    scopus 로고
    • Hyperfunctioning thyroid nodules in toxic multinodular goiter share activating thyrotropin receptor mutations with solitary toxic adenoma
    • Tonacchera, M., L. Chiovato, A. Pinchera, P. Agretti and E. Fiore et al, 1998b. Hyperfunctioning thyroid nodules in toxic multinodular goiter share activating thyrotropin receptor mutations with solitary toxic adenoma. J. Clin. Endocrinol. Meta., 83: 492-498.
    • (1998) J. Clin. Endocrinol. Meta , vol.83 , pp. 492-498
    • Tonacchera, M.1    Chiovato, L.2    Pinchera, A.3    Agretti, P.4    Fiore, E.5
  • 125
    • 17744383626 scopus 로고    scopus 로고
    • Activating thyrotropin receptor mutations are present in nonadenomatous hyperfunctioning nodules of toxic or autonomous multinodular goiter
    • Tonacchera, M., P. Agretti, L. Chiovato, V. Rosellini and G. Ceccarini et al, 2000. Activating thyrotropin receptor mutations are present in nonadenomatous hyperfunctioning nodules of toxic or autonomous multinodular goiter. J. Clin. Endocrinol. Metab., 85: 2270-2274.
    • (2000) J. Clin. Endocrinol. Metab , vol.85 , pp. 2270-2274
    • Tonacchera, M.1    Agretti, P.2    Chiovato, L.3    Rosellini, V.4    Ceccarini, G.5
  • 127
    • 0028916473 scopus 로고
    • In Chinese hamster ovary Kl cells dog and human thyrotropin receptors activate both the cyclic AMP and the phosphatidylinositol 4,5-bis phosphate cascades in the presence of thyrotropin and the cyclic AMP cascade in its absence
    • Van Sande, J., S. Swillens, C. Gerard, A. Allgeier, C. Massart, G. Vassart and J. Dumont, 1995b. In Chinese hamster ovary Kl cells dog and human thyrotropin receptors activate both the cyclic AMP and the phosphatidylinositol 4,5-bis phosphate cascades in the presence of thyrotropin and the cyclic AMP cascade in its absence. Eur. J. Biochem., 229: 338-343.
    • (1995) Eur. J. Biochem , vol.229 , pp. 338-343
    • van Sande, J.1    Swillens, S.2    Gerard, C.3    Allgeier, A.4    Massart, C.5    Vassart, G.6    Dumont, J.7
  • 128
    • 0036740782 scopus 로고    scopus 로고
    • Oncogenic mutations in the thyrotropin receptor of autonomously functioning thyroid nodules in the Japanese population
    • Vanvooren, V., S. Uchino, L. Duprez, M.J. Costa and J. Vandekerckhove etal., 2002. Oncogenic mutations in the thyrotropin receptor of autonomously functioning thyroid nodules in the Japanese population. Eur. J. Endocrinol, 147: 287-291.
    • (2002) Eur. J. Endocrinol , vol.147 , pp. 287-291
    • Vanvooren, V.1    Uchino, S.2    Duprez, L.3    Costa, M.J.4    Vandekerckhove, J.5
  • 129
    • 0026743033 scopus 로고
    • The thyrotropin receptor and the regulation of thyrocyte function and growth
    • Vassart, G. and J.E. Dumont, 1992. The thyrotropin receptor and the regulation of thyrocyte function and growth. Endocr. Rev., 13: 596-611.
    • (1992) Endocr. Rev , vol.13 , pp. 596-611
    • Vassart, G.1    Dumont, J.E.2
  • 130
    • 33646565826 scopus 로고    scopus 로고
    • Physiological factors associated with weak neonatal poults (Meleagris gallopavo)
    • Vern, L.C., D.T. Ort and J.L. Grimes, 2003. Physiological factors associated with weak neonatal poults (Meleagris gallopavo). Int. J. Poult. Sci., 2: 7-14.
    • (2003) Int. J. Poult. Sci , vol.2 , pp. 7-14
    • Vern, L.C.1    Ort, D.T.2    Grimes, J.L.3
  • 131
    • 0025096140 scopus 로고
    • An insertion in the human thyrotropin receptor critical for high affinity hormone binding
    • Wadsworth, H.L., G.D. Chazenbalk, Y. Nagayama, D. Russo and B. Rapoport, 1990. An insertion in the human thyrotropin receptor critical for high affinity hormone binding. Science, 249: 1423-1425.
    • (1990) Science , vol.249 , pp. 1423-1425
    • Wadsworth, H.L.1    Chazenbalk, G.D.2    Nagayama, Y.3    Russo, D.4    Rapoport, B.5
  • 132
    • 0031048778 scopus 로고    scopus 로고
    • A mixed-charge pair in human interleukin 4 dominates high-affinity interaction with the receptor alpha chain
    • Wang, Y., B.J. Shen and W. Sebald, 1997. A mixed-charge pair in human interleukin 4 dominates high-affinity interaction with the receptor alpha chain. Proc. Natl. Acad. Sci. USA., 94: 1657-1662.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1657-1662
    • Wang, Y.1    Shen, B.J.2    Sebald, W.3
  • 133
    • 9844223914 scopus 로고    scopus 로고
    • Resistance to thyrotropin (TSH) in three families is not associated with mutations in the TSH receptor or TSH
    • Xie, J., S. Pannain, J. Pohlenz, R.E. Weiss and K. Moltz et al, 1997. Resistance to thyrotropin (TSH) in three families is not associated with mutations in the TSH receptor or TSH. J. Clin. Endocrinol. Metab., 82: 3933-3940.
    • (1997) J. Clin. Endocrinol. Metab , vol.82 , pp. 3933-3940
    • Xie, J.1    Pannain, S.2    Pohlenz, J.3    Weiss, R.E.4    Moltz, K.5
  • 134
    • 72249123195 scopus 로고    scopus 로고
    • Variation in thyroidal activity during estrous cycle and natural breeding season in markhos goat breeds
    • Zarei, M.A., A. Farshad and S. Akhondzadeh, 2009. Variation in thyroidal activity during estrous cycle and natural breeding season in markhos goat breeds. Pak. J. Biol. Sci., 12: 1420-1424.
    • (2009) Pak. J. Biol. Sci , vol.12 , pp. 1420-1424
    • Zarei, M.A.1    Farshad, A.2    Akhondzadeh, S.3
  • 135
    • 0023840141 scopus 로고
    • Regulation of follicle-stimulating hormone binding to receptors on bovine calf testis membranes by cholera toxin-sensitive guanine nucleotide binding protein
    • Zhang, S.B., B. Dattatreyamurty and L.E. Jr. Reichert, 1988. Regulation of follicle-stimulating hormone binding to receptors on bovine calf testis membranes by cholera toxin-sensitive guanine nucleotide binding protein. Mol. Endocrinol., 2: 148-158.
    • (1988) Mol. Endocrinol , vol.2 , pp. 148-158
    • Zhang, S.B.1    Dattatreyamurty, B.2    Reichert Jr., L.E.3
  • 136
    • 0029056743 scopus 로고
    • Constitutive activation of the thyrotropin receptor by deletion of a portion of the extracellular domain
    • Zhang, M.L., H. Sugawa, S. Kosugi and T. Mori, 1995. Constitutive activation of the thyrotropin receptor by deletion of a portion of the extracellular domain. Biochem. Biophys. Res. Commun, 211: 205-210.
    • (1995) Biochem. Biophys. Res. Commun , vol.211 , pp. 205-210
    • Zhang, M.L.1    Sugawa, H.2    Kosugi, S.3    Mori, T.4


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