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Volumn , Issue , 2014, Pages 159-189

Thyroid Toxicogenomics: A Multi-Organ Paradigm

Author keywords

Endocrine disruption; HPT axis; Thyroid hormones; Toxicogenomics

Indexed keywords


EID: 84903402205     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978012397862200009-7     Document Type: Chapter
Times cited : (3)

References (190)
  • 3
    • 84903399524 scopus 로고    scopus 로고
    • Encyclopedia Britannica Online. Paracelsus
    • Encyclopedia Britannica Online. Paracelsus,<>; 2013. http://www.britannica.com/EBchecked/topic/442424/Paracelsus.
    • (2013)
  • 4
    • 0346818668 scopus 로고
    • Iodine in medicine and pharmacy since its discovery: 1811-1961
    • Kelly FC Iodine in medicine and pharmacy since its discovery: 1811-1961. Proc R Soc Med 1961, 54:831-836.
    • (1961) Proc R Soc Med , vol.54 , pp. 831-836
    • Kelly, F.C.1
  • 5
    • 84943211433 scopus 로고
    • The isolation in crystalline form of the compound containing iodin, which occurs in the thyroid
    • Kendall EC The isolation in crystalline form of the compound containing iodin, which occurs in the thyroid. JAMA 1915, 64:2042-2043.
    • (1915) JAMA , vol.64 , pp. 2042-2043
    • Kendall, E.C.1
  • 6
    • 0000076344 scopus 로고
    • The identification of 3:5:3'-L-triiodothyronine in human plasma
    • Gross J, Pitt-Rivers R The identification of 3:5:3'-L-triiodothyronine in human plasma. Lancet 1952, 1:439-441.
    • (1952) Lancet , vol.1 , pp. 439-441
    • Gross, J.1    Pitt-Rivers, R.2
  • 9
    • 0028120357 scopus 로고
    • Neoplastic lesions of questionable significance to humans
    • Alison RH, Capen CC, Prentice DE Neoplastic lesions of questionable significance to humans. Toxicol Pathol 1994, 22:179-186.
    • (1994) Toxicol Pathol , vol.22 , pp. 179-186
    • Alison, R.H.1    Capen, C.C.2    Prentice, D.E.3
  • 10
    • 84903399510 scopus 로고    scopus 로고
    • US Environmental Protection Agency, Office of Prevention, Pesticides and Toxic Substances, Washington DC USEPA
    • USEPA RED facts amitrole 1996, US Environmental Protection Agency, Office of Prevention, Pesticides and Toxic Substances, Washington DC.
    • (1996) RED facts amitrole
  • 11
    • 84859373425 scopus 로고    scopus 로고
    • Hormones and endocrine-disrupting chemicals: low-dose effects and nonmonotonic dose responses
    • Vandenberg LN, Colborn T, Hayes TB, Heindel JJ, Jacobs DR, Lee D-H, et al. Hormones and endocrine-disrupting chemicals: low-dose effects and nonmonotonic dose responses. Endocr Rev 2012, 33:378-455.
    • (2012) Endocr Rev , vol.33 , pp. 378-455
    • Vandenberg, L.N.1    Colborn, T.2    Hayes, T.B.3    Heindel, J.J.4    Jacobs, D.R.5    Lee, D.-H.6
  • 12
    • 0017337163 scopus 로고
    • Effects of total energy withdrawal (fasting) on the levels of growth hormone, thyrotropin, cortisol, adrenaline, noradrenaline, T4, T3, and rT3 in healthy males
    • Palmblad J, Levi L, Burger A, Melander A, Westgren U, von Schenck H, et al. Effects of total energy withdrawal (fasting) on the levels of growth hormone, thyrotropin, cortisol, adrenaline, noradrenaline, T4, T3, and rT3 in healthy males. Acta Med Scand 1977, 201:15-22.
    • (1977) Acta Med Scand , vol.201 , pp. 15-22
    • Palmblad, J.1    Levi, L.2    Burger, A.3    Melander, A.4    Westgren, U.5    von Schenck, H.6
  • 13
    • 0028918870 scopus 로고
    • Effects of high altitude and cold exposure on resting thyroid hormone concentrations
    • Hackney AC, Feith S, Pozos R, Seale J Effects of high altitude and cold exposure on resting thyroid hormone concentrations. Aviat Space Environ Med 1995, 66:325-329.
    • (1995) Aviat Space Environ Med , vol.66 , pp. 325-329
    • Hackney, A.C.1    Feith, S.2    Pozos, R.3    Seale, J.4
  • 14
    • 0014576567 scopus 로고
    • Effect of light and darkness upon thyroid secretion rate and on the endocrine glands of female rats
    • Singh DV, Turner CW Effect of light and darkness upon thyroid secretion rate and on the endocrine glands of female rats. Proc Soc Exp Biol Med 1969, 131:1296-1299.
    • (1969) Proc Soc Exp Biol Med , vol.131 , pp. 1296-1299
    • Singh, D.V.1    Turner, C.W.2
  • 17
    • 0018144614 scopus 로고
    • Pituitary-thyroid responses to surgical stress
    • Chan V, Wang C, Yeung RT Pituitary-thyroid responses to surgical stress. Acta Endocrinol 1978, 88:490-498.
    • (1978) Acta Endocrinol , vol.88 , pp. 490-498
    • Chan, V.1    Wang, C.2    Yeung, R.T.3
  • 18
    • 0024443946 scopus 로고
    • The effects of xenobiotics on the structure and function of thyroid follicular and C-cells
    • Capen CC, Martin SL The effects of xenobiotics on the structure and function of thyroid follicular and C-cells. Toxicol Pathol 1989, 17:266-293.
    • (1989) Toxicol Pathol , vol.17 , pp. 266-293
    • Capen, C.C.1    Martin, S.L.2
  • 19
    • 0022341972 scopus 로고
    • The influence of age and sex on tests of thyroid function
    • Franklyn JA, Ramsden DB, Sheppard MC The influence of age and sex on tests of thyroid function. Ann Clin Biochem 1985, 22(5):502-505.
    • (1985) Ann Clin Biochem , vol.22 , Issue.5 , pp. 502-505
    • Franklyn, J.A.1    Ramsden, D.B.2    Sheppard, M.C.3
  • 20
    • 0036959745 scopus 로고    scopus 로고
    • Narrow individual variations in serum T(4) and T(3) in normal subjects: a clue to the understanding of subclinical thyroid disease
    • Andersen S, Pedersen KM, Bruun NH, Laurberg P Narrow individual variations in serum T(4) and T(3) in normal subjects: a clue to the understanding of subclinical thyroid disease. J Clin Endocrinol Metab 2002, 87:1068-1072.
    • (2002) J Clin Endocrinol Metab , vol.87 , pp. 1068-1072
    • Andersen, S.1    Pedersen, K.M.2    Bruun, N.H.3    Laurberg, P.4
  • 21
    • 1642323634 scopus 로고    scopus 로고
    • Major genetic influence on the regulation of the pituitary-thyroid axis: a study of healthy Danish twins
    • Hansen PS, Brix TH, Sørensen TIA, Kyvik KO, Hegedüs L Major genetic influence on the regulation of the pituitary-thyroid axis: a study of healthy Danish twins. J Clin Endocrinol Metab 2004, 89:1181-1187.
    • (2004) J Clin Endocrinol Metab , vol.89 , pp. 1181-1187
    • Hansen, P.S.1    Brix, T.H.2    Sørensen, T.I.A.3    Kyvik, K.O.4    Hegedüs, L.5
  • 22
    • 1642434177 scopus 로고    scopus 로고
    • Application of toxicogenomics to the endocrine disruption issue
    • Shirai T, Asamoto M Application of toxicogenomics to the endocrine disruption issue. Pure Appl Chem 2003, 75:2419-2422.
    • (2003) Pure Appl Chem , vol.75 , pp. 2419-2422
    • Shirai, T.1    Asamoto, M.2
  • 23
    • 84860914331 scopus 로고    scopus 로고
    • Persistent cAMP signaling by internalized TSH receptors occurs in thyroid but not in HEK293 cells
    • Werthmann RC, Volpe S, Lohse MJ, Calebiro D Persistent cAMP signaling by internalized TSH receptors occurs in thyroid but not in HEK293 cells. FASEB J 2012, 26:2043-2048.
    • (2012) FASEB J , vol.26 , pp. 2043-2048
    • Werthmann, R.C.1    Volpe, S.2    Lohse, M.J.3    Calebiro, D.4
  • 24
    • 0033790195 scopus 로고    scopus 로고
    • Functional characterization of five constitutively activating thyrotrophin receptor mutations
    • Wonerow P, Chey S, Führer D, Holzapfel HP, Paschke R Functional characterization of five constitutively activating thyrotrophin receptor mutations. Clin Endocrinol 2000, 53:461-468.
    • (2000) Clin Endocrinol , vol.53 , pp. 461-468
    • Wonerow, P.1    Chey, S.2    Führer, D.3    Holzapfel, H.P.4    Paschke, R.5
  • 25
    • 41949114737 scopus 로고    scopus 로고
    • Epac, in synergy with cAMP-dependent protein kinase (PKA), is required for cAMP-mediated mitogenesis
    • Hochbaum D, Hong K, Barila G, Ribeiro-Neto F, Altschuler DL Epac, in synergy with cAMP-dependent protein kinase (PKA), is required for cAMP-mediated mitogenesis. J Biol Chem 2008, 283:4464-4468.
    • (2008) J Biol Chem , vol.283 , pp. 4464-4468
    • Hochbaum, D.1    Hong, K.2    Barila, G.3    Ribeiro-Neto, F.4    Altschuler, D.L.5
  • 26
    • 0842312972 scopus 로고    scopus 로고
    • A coated tube assay for the detection of blocking thyrotropin receptor autoantibodies
    • Minich WB, Lenzner C, Bergmann A, Morgenthaler NG A coated tube assay for the detection of blocking thyrotropin receptor autoantibodies. J Clin Endocrinol Metab 2004, 89:352-356.
    • (2004) J Clin Endocrinol Metab , vol.89 , pp. 352-356
    • Minich, W.B.1    Lenzner, C.2    Bergmann, A.3    Morgenthaler, N.G.4
  • 27
    • 39049154305 scopus 로고    scopus 로고
    • Quantitative high throughput screening using a live cell cAMP assay identifies small molecule agonists of the TSH receptor
    • Titus S, Neumann S, Zheng W, Southall N, Michael S, Klumpp C, et al. Quantitative high throughput screening using a live cell cAMP assay identifies small molecule agonists of the TSH receptor. J Biomol Screen 2008, 13:120-127.
    • (2008) J Biomol Screen , vol.13 , pp. 120-127
    • Titus, S.1    Neumann, S.2    Zheng, W.3    Southall, N.4    Michael, S.5    Klumpp, C.6
  • 29
    • 84883885853 scopus 로고    scopus 로고
    • In vitro pituitary and thyroid cell proliferation assays and their relevance as alternatives to animal testing
    • Jomaa B, Aarts JMMJG, de Haan LHJ, Peijnenburg AACM, Bovee TFH, Murk AJ, et al. In vitro pituitary and thyroid cell proliferation assays and their relevance as alternatives to animal testing. ALTEX 2013, 30:293-307.
    • (2013) ALTEX , vol.30 , pp. 293-307
    • Jomaa, B.1    Aarts, J.M.M.J.G.2    de Haan, L.H.J.3    Peijnenburg, A.A.C.M.4    Bovee, T.F.H.5    Murk, A.J.6
  • 30
    • 57349176149 scopus 로고    scopus 로고
    • Transient congenital hypothyroidism caused by biallelic mutations of the dual oxidase 2 gene in Japanese patients detected by a neonatal screening program, J
    • Maruo Y, Takahashi H, Soeda I, Nishikura N, Matsui K, Ota Y, et al. Transient congenital hypothyroidism caused by biallelic mutations of the dual oxidase 2 gene in Japanese patients detected by a neonatal screening program, J. Clin Endocrinol Metab 2008, 93:4261-4267.
    • (2008) Clin Endocrinol Metab , vol.93 , pp. 4261-4267
    • Maruo, Y.1    Takahashi, H.2    Soeda, I.3    Nishikura, N.4    Matsui, K.5    Ota, Y.6
  • 31
    • 39049092782 scopus 로고    scopus 로고
    • Biallelic inactivation of the dual oxidase maturation factor 2 (DUOXA2) gene as a novel cause of congenital hypothyroidism
    • Zamproni I, Grasberger H, Cortinovis F, Vigone MC, Chiumello G, Mora S, et al. Biallelic inactivation of the dual oxidase maturation factor 2 (DUOXA2) gene as a novel cause of congenital hypothyroidism. J Clin Endocrinol Metab 2008, 93:605-610.
    • (2008) J Clin Endocrinol Metab , vol.93 , pp. 605-610
    • Zamproni, I.1    Grasberger, H.2    Cortinovis, F.3    Vigone, M.C.4    Chiumello, G.5    Mora, S.6
  • 32
    • 65449180375 scopus 로고    scopus 로고
    • Activation of dual oxidases Duox1 and Duox2 differential regulation mediated by cAMP-dependent protein kinase and protein kinase C-dependent phosphorylation
    • Rigutto S, Hoste C, Grasberger H, Milenkovic M, Communi D, Dumont JE, et al. Activation of dual oxidases Duox1 and Duox2 differential regulation mediated by cAMP-dependent protein kinase and protein kinase C-dependent phosphorylation. J Biol Chem 2009, 284:6725-6734.
    • (2009) J Biol Chem , vol.284 , pp. 6725-6734
    • Rigutto, S.1    Hoste, C.2    Grasberger, H.3    Milenkovic, M.4    Communi, D.5    Dumont, J.E.6
  • 33
    • 33947423432 scopus 로고    scopus 로고
    • Duox expression and related H2O2 measurement in mouse thyroid: onset in embryonic development and regulation by TSH in adult
    • Milenkovic M, De Deken X, Jin L, De Felice M, Di Lauro R, Dumont JE, et al. Duox expression and related H2O2 measurement in mouse thyroid: onset in embryonic development and regulation by TSH in adult. J Endocrinol 2007, 192:615-626.
    • (2007) J Endocrinol , vol.192 , pp. 615-626
    • Milenkovic, M.1    De Deken, X.2    Jin, L.3    De Felice, M.4    Di Lauro, R.5    Dumont, J.E.6
  • 34
    • 0034464770 scopus 로고    scopus 로고
    • Atypical protein kinase C-zeta stimulates thyrotropin-independent proliferation in rat thyroid cells
    • Fernandez N, Caloca MJ, Prendergast GV, Meinkoth JL, Kazanietz MG Atypical protein kinase C-zeta stimulates thyrotropin-independent proliferation in rat thyroid cells. Endocrinology 2000, 141:146-152.
    • (2000) Endocrinology , vol.141 , pp. 146-152
    • Fernandez, N.1    Caloca, M.J.2    Prendergast, G.V.3    Meinkoth, J.L.4    Kazanietz, M.G.5
  • 36
    • 27144452891 scopus 로고    scopus 로고
    • Systems toxicology: applications of toxicogenomics, transcriptomics, proteomics and metabolomics in toxicology
    • Heijne WHM, Kienhuis AS, van Ommen B, Stierum RH, Groten JP Systems toxicology: applications of toxicogenomics, transcriptomics, proteomics and metabolomics in toxicology. Expert Rev Proteomics 2005, 2:767-780.
    • (2005) Expert Rev Proteomics , vol.2 , pp. 767-780
    • Heijne, W.H.M.1    Kienhuis, A.S.2    van Ommen, B.3    Stierum, R.H.4    Groten, J.P.5
  • 37
    • 0021675425 scopus 로고
    • Compartmental models for human iodine metabolism
    • Hays MT Compartmental models for human iodine metabolism. Math Biosci 1984, 72:317-335.
    • (1984) Math Biosci , vol.72 , pp. 317-335
    • Hays, M.T.1
  • 40
    • 0037326161 scopus 로고    scopus 로고
    • The sodium/iodide symporter (NIS): characterization, regulation, and medical significance
    • Dohán O, la Vieja AD, Paroder V, Riedel C, Artani M, Reed M, et al. The sodium/iodide symporter (NIS): characterization, regulation, and medical significance. Endocr Rev 2003, 24:48-77.
    • (2003) Endocr Rev , vol.24 , pp. 48-77
    • Dohán, O.1    la Vieja, A.D.2    Paroder, V.3    Riedel, C.4    Artani, M.5    Reed, M.6
  • 43
    • 16944366606 scopus 로고    scopus 로고
    • Pendred syndrome is caused by mutations in a putative sulphate transporter gene (PDS)
    • Everett LA, Glaser B, Beck JC, Idol JR, Buchs A, Heyman M, et al. Pendred syndrome is caused by mutations in a putative sulphate transporter gene (PDS). Nat Genet 1997, 17:411-422.
    • (1997) Nat Genet , vol.17 , pp. 411-422
    • Everett, L.A.1    Glaser, B.2    Beck, J.C.3    Idol, J.R.4    Buchs, A.5    Heyman, M.6
  • 46
    • 2542553486 scopus 로고
    • Permeability of red corpuscles of the dog to sodium ion
    • Cohn WE, Cohn ET Permeability of red corpuscles of the dog to sodium ion. Proc Soc Exp Biol Med 1939, 41:445-449.
    • (1939) Proc Soc Exp Biol Med , vol.41 , pp. 445-449
    • Cohn, W.E.1    Cohn, E.T.2
  • 47
    • 0036828505 scopus 로고    scopus 로고
    • From overshoot to voltage clamp
    • Huxley A From overshoot to voltage clamp. Trends Neurosci 2002, 25:553-558.
    • (2002) Trends Neurosci , vol.25 , pp. 553-558
    • Huxley, A.1
  • 48
    • 0019441262 scopus 로고
    • Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches
    • Hamill OP, Marty A, Neher E, Sakmann B, Sigworth FJ Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches. Pflugers Arch 1981, 391:85-100.
    • (1981) Pflugers Arch , vol.391 , pp. 85-100
    • Hamill, O.P.1    Marty, A.2    Neher, E.3    Sakmann, B.4    Sigworth, F.J.5
  • 49
    • 79957787271 scopus 로고    scopus 로고
    • Intracellular anion fluorescence assay for sodium/iodide symporter substrates
    • Di Bernardo J, Iosco C, Rhoden KJ Intracellular anion fluorescence assay for sodium/iodide symporter substrates. Anal Biochem 2011, 415:32-38.
    • (2011) Anal Biochem , vol.415 , pp. 32-38
    • Di Bernardo, J.1    Iosco, C.2    Rhoden, K.J.3
  • 51
    • 1842581804 scopus 로고    scopus 로고
    • Functional characterization of pendrin in a polarized cell system: evidence for pendrin-mediated apical iodide efflux
    • Gillam MP, Sidhaye AR, Lee EJ, Rutishauser J, Stephan CW, Kopp P Functional characterization of pendrin in a polarized cell system: evidence for pendrin-mediated apical iodide efflux. J Biol Chem 2004, 279:13004-13010.
    • (2004) J Biol Chem , vol.279 , pp. 13004-13010
    • Gillam, M.P.1    Sidhaye, A.R.2    Lee, E.J.3    Rutishauser, J.4    Stephan, C.W.5    Kopp, P.6
  • 52
    • 33646811842 scopus 로고    scopus 로고
    • Differential regulation of apical and basal iodide transporters in the thyroid by thyroglobulin
    • Suzuki K, Kohn LD Differential regulation of apical and basal iodide transporters in the thyroid by thyroglobulin. J Endocrinol 2006, 189:247-255.
    • (2006) J Endocrinol , vol.189 , pp. 247-255
    • Suzuki, K.1    Kohn, L.D.2
  • 53
    • 46449089073 scopus 로고    scopus 로고
    • Peroxides and peroxide-degrading enzymes in the thyroid
    • Schweizer U, Chiu J, Köhrle J Peroxides and peroxide-degrading enzymes in the thyroid. Antioxid Redox Signal 2008, 10:1577-1592.
    • (2008) Antioxid Redox Signal , vol.10 , pp. 1577-1592
    • Schweizer, U.1    Chiu, J.2    Köhrle, J.3
  • 54
    • 81955164230 scopus 로고    scopus 로고
    • Thyroid adverse effects of psychotropic drugs: a review
    • Bou Khalil R, Richa S Thyroid adverse effects of psychotropic drugs: a review. Clin Neuropharmacol 2011, 34:248-255.
    • (2011) Clin Neuropharmacol , vol.34 , pp. 248-255
    • Bou Khalil, R.1    Richa, S.2
  • 55
    • 34250811630 scopus 로고    scopus 로고
    • The ultraviolet filter benzophenone 2 interferes with the thyroid hormone axis in rats and is a potent in vitro inhibitor of human recombinant thyroid peroxidase
    • Schmutzler C, Bacinski A, Gotthardt I, Huhne K, Ambrugger P, Klammer H, et al. The ultraviolet filter benzophenone 2 interferes with the thyroid hormone axis in rats and is a potent in vitro inhibitor of human recombinant thyroid peroxidase. Endocrinology 2007, 148:2835-2844.
    • (2007) Endocrinology , vol.148 , pp. 2835-2844
    • Schmutzler, C.1    Bacinski, A.2    Gotthardt, I.3    Huhne, K.4    Ambrugger, P.5    Klammer, H.6
  • 57
    • 77955344256 scopus 로고    scopus 로고
    • A coherent organization of differentiation proteins is required to maintain an appropriate thyroid function in the pendred thyroid
    • Senou M, Khalifa C, Thimmesch M, Jouret F, Devuyst O, Col V, et al. A coherent organization of differentiation proteins is required to maintain an appropriate thyroid function in the pendred thyroid. J Clin Endocrinol Metab 2010, 95:4021-4030.
    • (2010) J Clin Endocrinol Metab , vol.95 , pp. 4021-4030
    • Senou, M.1    Khalifa, C.2    Thimmesch, M.3    Jouret, F.4    Devuyst, O.5    Col, V.6
  • 58
    • 0030946117 scopus 로고    scopus 로고
    • Glutathione peroxidase degrades intracellular hydrogen peroxide and thereby inhibits intracellular protein iodination in thyroid epithelium
    • Ekholm R, Björkman U Glutathione peroxidase degrades intracellular hydrogen peroxide and thereby inhibits intracellular protein iodination in thyroid epithelium. Endocrinology 1997, 138:2871-2878.
    • (1997) Endocrinology , vol.138 , pp. 2871-2878
    • Ekholm, R.1    Björkman, U.2
  • 59
    • 1942453285 scopus 로고    scopus 로고
    • Ultrastructural localization of thyroid peroxidase, hydrogen peroxide-generating sites, and monoamine oxidase in benign and malignant thyroid diseases
    • Masini-Repiso AM, Bonaterra M, Spitale L, Di Fulvio M, Bonino MI, Coleoni AH, et al. Ultrastructural localization of thyroid peroxidase, hydrogen peroxide-generating sites, and monoamine oxidase in benign and malignant thyroid diseases. Hum Pathol 2004, 35:436-446.
    • (2004) Hum Pathol , vol.35 , pp. 436-446
    • Masini-Repiso, A.M.1    Bonaterra, M.2    Spitale, L.3    Di Fulvio, M.4    Bonino, M.I.5    Coleoni, A.H.6
  • 61
    • 84866982897 scopus 로고    scopus 로고
    • Regulation of dual oxidase (DUOX) expression and H2O2 production by thyroglobulin
    • 10.1089/thy.2012-0003
    • Yoshihara A, Hara T, Kawashima A, Akama T, Tanigawa K, Wu H, et al. Regulation of dual oxidase (DUOX) expression and H2O2 production by thyroglobulin. Thyroid 2012, 10.1089/thy.2012-0003.
    • (2012) Thyroid
    • Yoshihara, A.1    Hara, T.2    Kawashima, A.3    Akama, T.4    Tanigawa, K.5    Wu, H.6
  • 62
    • 0033060460 scopus 로고    scopus 로고
    • Methimazole and propylthiouracil increase cellular thyroid peroxidase activity and thyroid peroxidase mRNA in cultured porcine thyroid follicles
    • Sugawara M, Sugawara Y, Wen K Methimazole and propylthiouracil increase cellular thyroid peroxidase activity and thyroid peroxidase mRNA in cultured porcine thyroid follicles. Thyroid 1999, 9:513-518.
    • (1999) Thyroid , vol.9 , pp. 513-518
    • Sugawara, M.1    Sugawara, Y.2    Wen, K.3
  • 63
    • 80052728031 scopus 로고    scopus 로고
    • Identification of classifiers for increase or decrease of thyroid peroxidase activity in the FTC-238/hTPO recombinant cell line
    • Song M, Kim Y-J, Song M-K, Choi H-S, Park Y-K, Ryu J-C Identification of classifiers for increase or decrease of thyroid peroxidase activity in the FTC-238/hTPO recombinant cell line. Environ Sci Technol 2011, 45:7906-7914.
    • (2011) Environ Sci Technol , vol.45 , pp. 7906-7914
    • Song, M.1    Kim, Y.-J.2    Song, M.-K.3    Choi, H.-S.4    Park, Y.-K.5    Ryu, J.-C.6
  • 64
    • 79955036320 scopus 로고    scopus 로고
    • Dual oxidase 1 induced by Th2 cytokines promotes STAT6 phosphorylation via oxidative inactivation of protein tyrosine phosphatase 1B in human epidermal keratinocytes
    • Hirakawa S, Saito R, Ohara H, Okuyama R, Aiba S Dual oxidase 1 induced by Th2 cytokines promotes STAT6 phosphorylation via oxidative inactivation of protein tyrosine phosphatase 1B in human epidermal keratinocytes. J Immunol 2011, 186:4762-4770.
    • (2011) J Immunol , vol.186 , pp. 4762-4770
    • Hirakawa, S.1    Saito, R.2    Ohara, H.3    Okuyama, R.4    Aiba, S.5
  • 65
    • 0023784555 scopus 로고
    • Identification of two subpopulations of thyroid lysosomes: relation to the thyroglobulin proteolytic pathway
    • Selmi S, Rousset B Identification of two subpopulations of thyroid lysosomes: relation to the thyroglobulin proteolytic pathway. Biochem J 1988, 253:523-532.
    • (1988) Biochem J , vol.253 , pp. 523-532
    • Selmi, S.1    Rousset, B.2
  • 66
    • 0017263546 scopus 로고
    • Inhibition of thyroglobulin biosynthesis and degradation by excess iodide: synergism with lithium
    • Radvila A, Roost R, Bürgi H, Kohler H, Studer H Inhibition of thyroglobulin biosynthesis and degradation by excess iodide: synergism with lithium. Acta Endocrinol 1976, 81:495-506.
    • (1976) Acta Endocrinol , vol.81 , pp. 495-506
    • Radvila, A.1    Roost, R.2    Bürgi, H.3    Kohler, H.4    Studer, H.5
  • 67
    • 79955692998 scopus 로고    scopus 로고
    • Systems biology of the autophagy-lysosomal pathway
    • Jegga AG, Schneider L, Ouyang X, Zhang J Systems biology of the autophagy-lysosomal pathway. Autophagy 2011, 7:477-489.
    • (2011) Autophagy , vol.7 , pp. 477-489
    • Jegga, A.G.1    Schneider, L.2    Ouyang, X.3    Zhang, J.4
  • 69
    • 4344699813 scopus 로고    scopus 로고
    • Cathepsin L is involved in cathepsin D processing and regulation of apoptosis in A549 human lung epithelial cells
    • Wille A, Gerber A, Heimburg A, Reisenauer A, Peters C, Saftig P, et al. Cathepsin L is involved in cathepsin D processing and regulation of apoptosis in A549 human lung epithelial cells. Biol Chem 2004, 385:665-670.
    • (2004) Biol Chem , vol.385 , pp. 665-670
    • Wille, A.1    Gerber, A.2    Heimburg, A.3    Reisenauer, A.4    Peters, C.5    Saftig, P.6
  • 71
    • 0042151174 scopus 로고    scopus 로고
    • Cloning and characterization of a novel thyroidal gene encoding proteins with a conserved nitroreductase domain
    • Moreno JC, Keijser R, Aarraas S, De Vijlder JJM, Ris-Stalpers C Cloning and characterization of a novel thyroidal gene encoding proteins with a conserved nitroreductase domain. J Endocrinol Invest 2002, 25:40.
    • (2002) J Endocrinol Invest , vol.25 , pp. 40
    • Moreno, J.C.1    Keijser, R.2    Aarraas, S.3    De Vijlder, J.J.M.4    Ris-Stalpers, C.5
  • 74
    • 67749120727 scopus 로고    scopus 로고
    • Crystal structure of iodotyrosine deiodinase, a novel flavoprotein responsible for iodide salvage in thyroid glands
    • Thomas SR, McTamney PM, Adler JM, LaRonde-LeBlanc N, Rokita SE Crystal structure of iodotyrosine deiodinase, a novel flavoprotein responsible for iodide salvage in thyroid glands. J Biol Chem 2009, 284:19659-19667.
    • (2009) J Biol Chem , vol.284 , pp. 19659-19667
    • Thomas, S.R.1    McTamney, P.M.2    Adler, J.M.3    LaRonde-LeBlanc, N.4    Rokita, S.E.5
  • 75
    • 9444274840 scopus 로고    scopus 로고
    • Iodotyrosine dehalogenase 1 (DEHAL1) is a transmembrane protein involved in the recycling of iodide close to the thyroglobulin iodination site
    • Gnidehou S, Caillou B, Talbot M, Ohayon R, Kaniewski J, Noël-Hudson M-S, et al. Iodotyrosine dehalogenase 1 (DEHAL1) is a transmembrane protein involved in the recycling of iodide close to the thyroglobulin iodination site. FASEB J 2004, 18:1574-1576.
    • (2004) FASEB J , vol.18 , pp. 1574-1576
    • Gnidehou, S.1    Caillou, B.2    Talbot, M.3    Ohayon, R.4    Kaniewski, J.5    Noël-Hudson, M.-S.6
  • 77
    • 0036179611 scopus 로고    scopus 로고
    • Purification and characterization of the thyrotropin-releasing hormone (TRH)-degrading serum enzyme and its identification as a product of liver origin
    • Schmitmeier S, Thole H, Bader A, Bauer K Purification and characterization of the thyrotropin-releasing hormone (TRH)-degrading serum enzyme and its identification as a product of liver origin. Eur J Biochem 2002, 269:1278-1286.
    • (2002) Eur J Biochem , vol.269 , pp. 1278-1286
    • Schmitmeier, S.1    Thole, H.2    Bader, A.3    Bauer, K.4
  • 78
    • 69449092115 scopus 로고    scopus 로고
    • Subcellular trafficking of the TRH receptor: effect of phosphorylation
    • Jones BW, Hinkle PM Subcellular trafficking of the TRH receptor: effect of phosphorylation. Mol Endocrinol 2009, 23:1466-1478.
    • (2009) Mol Endocrinol , vol.23 , pp. 1466-1478
    • Jones, B.W.1    Hinkle, P.M.2
  • 79
    • 0021268637 scopus 로고
    • The effects of carbamazepine on the thyrotropin response to thyrotropin-releasing hormone
    • Joffe RT, Gold PW, Uhde TW, Post RM The effects of carbamazepine on the thyrotropin response to thyrotropin-releasing hormone. Psychiatry Res 1984, 12:161-166.
    • (1984) Psychiatry Res , vol.12 , pp. 161-166
    • Joffe, R.T.1    Gold, P.W.2    Uhde, T.W.3    Post, R.M.4
  • 80
    • 0028240617 scopus 로고
    • Contingent tolerance to carbamazepine: alterations in TRH mRNA and TRH receptor binding in limbic structures
    • Rosen JB, Weiss SR, Post RM Contingent tolerance to carbamazepine: alterations in TRH mRNA and TRH receptor binding in limbic structures. Brain Res 1994, 651:252-260.
    • (1994) Brain Res , vol.651 , pp. 252-260
    • Rosen, J.B.1    Weiss, S.R.2    Post, R.M.3
  • 81
    • 0038025925 scopus 로고    scopus 로고
    • Thyrotropin-releasing hormone receptors: similarities and differences
    • Sun Y, Lu X, Gershengorn MC Thyrotropin-releasing hormone receptors: similarities and differences. J Mol Endocrinol 2003, 30:87-97.
    • (2003) J Mol Endocrinol , vol.30 , pp. 87-97
    • Sun, Y.1    Lu, X.2    Gershengorn, M.C.3
  • 82
    • 33744965195 scopus 로고    scopus 로고
    • Low affinity analogs of thyrotropin-releasing hormone are super-agonists
    • Engel S, Neumann S, Kaur N, Monga V, Jain R, Northup J, et al. Low affinity analogs of thyrotropin-releasing hormone are super-agonists. J Biol Chem 2006, 281:13103-13109.
    • (2006) J Biol Chem , vol.281 , pp. 13103-13109
    • Engel, S.1    Neumann, S.2    Kaur, N.3    Monga, V.4    Jain, R.5    Northup, J.6
  • 83
    • 0034463026 scopus 로고    scopus 로고
    • TRH-R2 exhibits similar binding and acute signaling but distinct regulation and anatomic distribution compared with TRH-R1
    • O'Dowd BF, Lee DK, Huang W, Nguyen T, Cheng R, Liu Y, et al. TRH-R2 exhibits similar binding and acute signaling but distinct regulation and anatomic distribution compared with TRH-R1. Mol Endocrinol 2000, 14:183-193.
    • (2000) Mol Endocrinol , vol.14 , pp. 183-193
    • O'Dowd, B.F.1    Lee, D.K.2    Huang, W.3    Nguyen, T.4    Cheng, R.5    Liu, Y.6
  • 84
    • 0033305235 scopus 로고    scopus 로고
    • Rat TRH receptor type 2 exhibits higher basal signaling activity than TRH receptor type 1
    • Wang W, Gershengorn MC Rat TRH receptor type 2 exhibits higher basal signaling activity than TRH receptor type 1. Endocrinology 1999, 140:4916-4919.
    • (1999) Endocrinology , vol.140 , pp. 4916-4919
    • Wang, W.1    Gershengorn, M.C.2
  • 85
    • 0027401882 scopus 로고
    • Effect of calcium channel blockers on serum levels of thyroid hormones
    • Mittal SR, Mathur AK, Prasad N Effect of calcium channel blockers on serum levels of thyroid hormones. Int J Cardiol 1993, 38:131-132.
    • (1993) Int J Cardiol , vol.38 , pp. 131-132
    • Mittal, S.R.1    Mathur, A.K.2    Prasad, N.3
  • 86
    • 0021989915 scopus 로고
    • Effect of nifedipine on TRH stimulation of TSH and PRL release by the pituitary gland
    • Teba L, Smailer S, Taylor HC Effect of nifedipine on TRH stimulation of TSH and PRL release by the pituitary gland. Metab Clin Exp 1985, 34:161-163.
    • (1985) Metab Clin Exp , vol.34 , pp. 161-163
    • Teba, L.1    Smailer, S.2    Taylor, H.C.3
  • 87
    • 0022527469 scopus 로고
    • Thyrotropin-releasing hormone stimulation of thyrotropin secretion is suppressed by calcium ion antagonists that block transmembrane influx and intracellular mobilization of calcium ion in human subjects
    • Yamada M, Mori M, Yamaguchi M, Akiyama H, Shiono S, Kobayashi I, et al. Thyrotropin-releasing hormone stimulation of thyrotropin secretion is suppressed by calcium ion antagonists that block transmembrane influx and intracellular mobilization of calcium ion in human subjects. J Endocrinol Invest 1986, 9:227-231.
    • (1986) J Endocrinol Invest , vol.9 , pp. 227-231
    • Yamada, M.1    Mori, M.2    Yamaguchi, M.3    Akiyama, H.4    Shiono, S.5    Kobayashi, I.6
  • 88
    • 0142012016 scopus 로고    scopus 로고
    • Molecular pathogenesis of thyroid cancer
    • Segev DL, Umbricht C, Zeiger MA Molecular pathogenesis of thyroid cancer. Surg Oncol 2003, 12:69-90.
    • (2003) Surg Oncol , vol.12 , pp. 69-90
    • Segev, D.L.1    Umbricht, C.2    Zeiger, M.A.3
  • 89
    • 84903410429 scopus 로고    scopus 로고
    • Pituitary thyroid hormone resistance (PTHR)
    • Ahmed E-L, Steve O Pituitary thyroid hormone resistance (PTHR). Endocr Abstr 2011, 25:P66.
    • (2011) Endocr Abstr , vol.25
    • Ahmed, E.-L.1    Steve, O.2
  • 90
    • 0029090697 scopus 로고
    • Vinblastine and nocodazole inhibit basal and thyrotropin-releasing hormone-stimulated prolactin secretion in GH(3) cells
    • Ravindra R, Forman LJ, Patel SA Vinblastine and nocodazole inhibit basal and thyrotropin-releasing hormone-stimulated prolactin secretion in GH(3) cells. Endocrine 1995, 3:591-596.
    • (1995) Endocrine , vol.3 , pp. 591-596
    • Ravindra, R.1    Forman, L.J.2    Patel, S.A.3
  • 91
    • 84865982169 scopus 로고    scopus 로고
    • JNK pathway decreases thyroid hormones via TRH receptor: a novel mechanism for disturbance of thyroid hormone homeostasis by PCB153
    • Liu C, Ha M, Cui Y, Wang C, Yan M, Fu W, et al. JNK pathway decreases thyroid hormones via TRH receptor: a novel mechanism for disturbance of thyroid hormone homeostasis by PCB153. Toxicology 2012, 302:68-76.
    • (2012) Toxicology , vol.302 , pp. 68-76
    • Liu, C.1    Ha, M.2    Cui, Y.3    Wang, C.4    Yan, M.5    Fu, W.6
  • 92
    • 84903399513 scopus 로고    scopus 로고
    • Millipore TRH receptor assay
    • Millipore, Millipore TRH receptor assay, 2012.
    • (2012)
    • Millipore1
  • 93
    • 84903399515 scopus 로고    scopus 로고
    • AequoScreen® GPCR Cell Line
    • PerklinElmer, AequoScreen® GPCR Cell Line, 2009.
    • (2009)
    • PerklinElmer1
  • 94
    • 34548576414 scopus 로고
    • Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea
    • Shimomura O, Johnson FH, Saiga Y Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea. J Cell Comp Physiol 1962, 59:223-239.
    • (1962) J Cell Comp Physiol , vol.59 , pp. 223-239
    • Shimomura, O.1    Johnson, F.H.2    Saiga, Y.3
  • 95
    • 0024273002 scopus 로고
    • Retention of cyclic AMP response to TSH in a cloned human thyrocyte/T cell hybridoma (HY2-15)
    • Martin A, Platzer M, Davies TF Retention of cyclic AMP response to TSH in a cloned human thyrocyte/T cell hybridoma (HY2-15). Mol Cell Endocrinol 1988, 60:233-238.
    • (1988) Mol Cell Endocrinol , vol.60 , pp. 233-238
    • Martin, A.1    Platzer, M.2    Davies, T.F.3
  • 96
    • 0031047393 scopus 로고    scopus 로고
    • Thyroid hormone-induced expression of specific somatostatin receptor subtypes correlates with involution of the TtT-97 murine thyrotrope tumor
    • James RA, Sarapura VD, Bruns C, Raulf F, Dowding JM, Gordon DF, et al. Thyroid hormone-induced expression of specific somatostatin receptor subtypes correlates with involution of the TtT-97 murine thyrotrope tumor. Endocrinology 1997, 138:719-724.
    • (1997) Endocrinology , vol.138 , pp. 719-724
    • James, R.A.1    Sarapura, V.D.2    Bruns, C.3    Raulf, F.4    Dowding, J.M.5    Gordon, D.F.6
  • 97
    • 0029846336 scopus 로고    scopus 로고
    • Immortalization of pituitary cells at discrete stages of development by directed oncogenesis in transgenic mice
    • Alarid ET, Windle JJ, Whyte DB, Mellon PL Immortalization of pituitary cells at discrete stages of development by directed oncogenesis in transgenic mice. Development 1996, 122:3319-3329.
    • (1996) Development , vol.122 , pp. 3319-3329
    • Alarid, E.T.1    Windle, J.J.2    Whyte, D.B.3    Mellon, P.L.4
  • 98
    • 84857815866 scopus 로고    scopus 로고
    • Glutamine and glutamic acid enhance thyroid-stimulating hormone β subunit mRNA expression in the rat pars tuberalis
    • Aizawa S, Sakai T, Sakata I Glutamine and glutamic acid enhance thyroid-stimulating hormone β subunit mRNA expression in the rat pars tuberalis. J Endocrinol 2012, 212:383-394.
    • (2012) J Endocrinol , vol.212 , pp. 383-394
    • Aizawa, S.1    Sakai, T.2    Sakata, I.3
  • 99
    • 0015258881 scopus 로고
    • Late thyrotoxicosis complicating autoimmune thyroiditis
    • Gavras I, Thomson JA Late thyrotoxicosis complicating autoimmune thyroiditis. Acta Endocrinol 1972, 69:41-46.
    • (1972) Acta Endocrinol , vol.69 , pp. 41-46
    • Gavras, I.1    Thomson, J.A.2
  • 100
    • 66449126267 scopus 로고    scopus 로고
    • Thyrotropin-releasing hormone (TRH) in the cerebellum
    • Shibusawa N, Hashimoto K, Yamada M Thyrotropin-releasing hormone (TRH) in the cerebellum. Cerebellum 2008, 7:84-95.
    • (2008) Cerebellum , vol.7 , pp. 84-95
    • Shibusawa, N.1    Hashimoto, K.2    Yamada, M.3
  • 101
    • 33845984884 scopus 로고    scopus 로고
    • An analog of thyrotropin-releasing hormone (TRH) is neuroprotective against glutamate-induced toxicity in fetal rat hippocampal neurons in vitro
    • Veronesi MC, Yard M, Jackson J, Lahiri DK, Kubek MJ An analog of thyrotropin-releasing hormone (TRH) is neuroprotective against glutamate-induced toxicity in fetal rat hippocampal neurons in vitro. Brain Res 2007, 1128:79-85.
    • (2007) Brain Res , vol.1128 , pp. 79-85
    • Veronesi, M.C.1    Yard, M.2    Jackson, J.3    Lahiri, D.K.4    Kubek, M.J.5
  • 102
    • 18844374837 scopus 로고    scopus 로고
    • Inverse shift in circulating corticosterone and leptin levels elevates hypothalamic deiodinase type 2 in fasted rats
    • Coppola A, Meli R, Diano S Inverse shift in circulating corticosterone and leptin levels elevates hypothalamic deiodinase type 2 in fasted rats. Endocrinology 2005, 146:2827-2833.
    • (2005) Endocrinology , vol.146 , pp. 2827-2833
    • Coppola, A.1    Meli, R.2    Diano, S.3
  • 103
    • 77950860422 scopus 로고    scopus 로고
    • Regulation of the hypothalamic thyrotropin releasing hormone (TRH) neuron by neuronal and peripheral inputs
    • Nillni EA Regulation of the hypothalamic thyrotropin releasing hormone (TRH) neuron by neuronal and peripheral inputs. Front Neuroendocrinol 2010, 31:134-156.
    • (2010) Front Neuroendocrinol , vol.31 , pp. 134-156
    • Nillni, E.A.1
  • 105
    • 0024790712 scopus 로고
    • Thyrotropin-releasing hormone gene expression in normal thyroid parafollicular cells
    • Gkonos PJ, Tavianini MA, Liu CC, Roos BA Thyrotropin-releasing hormone gene expression in normal thyroid parafollicular cells. Mol Endocrinol 1989, 3:2101-2109.
    • (1989) Mol Endocrinol , vol.3 , pp. 2101-2109
    • Gkonos, P.J.1    Tavianini, M.A.2    Liu, C.C.3    Roos, B.A.4
  • 107
    • 0026653478 scopus 로고
    • Interaction between thyrotrophin-releasing hormone and the muscarinic cholinergic system in rat brain
    • Garcia SI, Dabsys SM, Santajuliana D, Delorenzi A, Finkielman S, Nahmod VE, et al. Interaction between thyrotrophin-releasing hormone and the muscarinic cholinergic system in rat brain. J Endocrinol 1992, 134:215-219.
    • (1992) J Endocrinol , vol.134 , pp. 215-219
    • Garcia, S.I.1    Dabsys, S.M.2    Santajuliana, D.3    Delorenzi, A.4    Finkielman, S.5    Nahmod, V.E.6
  • 108
    • 84859498749 scopus 로고    scopus 로고
    • Molecular network profiling of U373MG human glioblastoma cells following induction of apoptosis by novel marine-derived anti-cancer 1,2,3,4-tetrahydroisoquinoline alkaloids
    • Tabunoki H, Saito N, Suwanborirux K, Charupant K, Satoh J Molecular network profiling of U373MG human glioblastoma cells following induction of apoptosis by novel marine-derived anti-cancer 1,2,3,4-tetrahydroisoquinoline alkaloids. Cancer Cell Int 2012, 12:14.
    • (2012) Cancer Cell Int , vol.12 , pp. 14
    • Tabunoki, H.1    Saito, N.2    Suwanborirux, K.3    Charupant, K.4    Satoh, J.5
  • 110
    • 0035048283 scopus 로고    scopus 로고
    • Critical role for thyroid hormone receptor beta2 in the regulation of paraventricular thyrotropin-releasing hormone neurons
    • Abel ED, Ahima RS, Boers ME, Elmquist JK, Wondisford FE Critical role for thyroid hormone receptor beta2 in the regulation of paraventricular thyrotropin-releasing hormone neurons. J Clin Invest 2001, 107:1017-1023.
    • (2001) J Clin Invest , vol.107 , pp. 1017-1023
    • Abel, E.D.1    Ahima, R.S.2    Boers, M.E.3    Elmquist, J.K.4    Wondisford, F.E.5
  • 111
    • 0028900123 scopus 로고
    • Functional regulation of thyroid hormone receptor variant TR alpha 2 by phosphorylation
    • Katz D, Reginato MJ, Lazar MA Functional regulation of thyroid hormone receptor variant TR alpha 2 by phosphorylation. Mol Cell Biol 1995, 15:2341-2348.
    • (1995) Mol Cell Biol , vol.15 , pp. 2341-2348
    • Katz, D.1    Reginato, M.J.2    Lazar, M.A.3
  • 112
    • 0034964207 scopus 로고    scopus 로고
    • Physiological and molecular basis of thyroid hormone action
    • Yen PM Physiological and molecular basis of thyroid hormone action. Physiol Rev 2001, 81:1097-1142.
    • (2001) Physiol Rev , vol.81 , pp. 1097-1142
    • Yen, P.M.1
  • 113
    • 0028025348 scopus 로고
    • Characteristics of a negative thyroid hormone response element
    • Carr FE, Wong NC Characteristics of a negative thyroid hormone response element. J Biol Chem 1994, 269:4175-4179.
    • (1994) J Biol Chem , vol.269 , pp. 4175-4179
    • Carr, F.E.1    Wong, N.C.2
  • 114
    • 0033118328 scopus 로고    scopus 로고
    • Mice deficient in the steroid receptor co-activator 1 (SRC-1) are resistant to thyroid hormone
    • Weiss RE, Xu J, Ning G, Pohlenz J, O'Malley BW, Refetoff S Mice deficient in the steroid receptor co-activator 1 (SRC-1) are resistant to thyroid hormone. EMBO J 1999, 18:1900-1904.
    • (1999) EMBO J , vol.18 , pp. 1900-1904
    • Weiss, R.E.1    Xu, J.2    Ning, G.3    Pohlenz, J.4    O'Malley, B.W.5    Refetoff, S.6
  • 115
    • 78650522817 scopus 로고    scopus 로고
    • Detection of thyroid hormone receptor disruptors by a novel stable in vitro reporter gene assay
    • Freitas J, Cano P, Craig-Veit C, Goodson ML, Furlow JD, Murk AJ Detection of thyroid hormone receptor disruptors by a novel stable in vitro reporter gene assay. Toxicol In Vitro 2011, 25:257-266.
    • (2011) Toxicol In Vitro , vol.25 , pp. 257-266
    • Freitas, J.1    Cano, P.2    Craig-Veit, C.3    Goodson, M.L.4    Furlow, J.D.5    Murk, A.J.6
  • 117
    • 84855168678 scopus 로고    scopus 로고
    • Thyroid hormone-regulated gene expression in juvenile mouse liver: identification of thyroid response elements using microarray profiling and in silico analyses
    • Paquette MA, Dong H, Gagné R, Williams A, Malowany M, Wade MG, et al. Thyroid hormone-regulated gene expression in juvenile mouse liver: identification of thyroid response elements using microarray profiling and in silico analyses. BMC Genomics 2011, 12:634.
    • (2011) BMC Genomics , vol.12 , pp. 634
    • Paquette, M.A.1    Dong, H.2    Gagné, R.3    Williams, A.4    Malowany, M.5    Wade, M.G.6
  • 118
    • 0034464045 scopus 로고    scopus 로고
    • Thyroid hormone regulation of hepatic genes in vivo detected by complementary DNA microarray
    • Feng X, Jiang Y, Meltzer P, Yen PM Thyroid hormone regulation of hepatic genes in vivo detected by complementary DNA microarray. Mol Endocrinol 2000, 14:947-955.
    • (2000) Mol Endocrinol , vol.14 , pp. 947-955
    • Feng, X.1    Jiang, Y.2    Meltzer, P.3    Yen, P.M.4
  • 119
    • 79953065771 scopus 로고    scopus 로고
    • Genome-wide expression profiling of carbaryl and vinclozolin in human thyroid follicular carcinoma (FTC-238) cells
    • Song M, Kim YJ, Lee J-N, Ryu JC Genome-wide expression profiling of carbaryl and vinclozolin in human thyroid follicular carcinoma (FTC-238) cells. BioChip J 2010, 4:89-98.
    • (2010) BioChip J , vol.4 , pp. 89-98
    • Song, M.1    Kim, Y.J.2    Lee, J.-N.3    Ryu, J.C.4
  • 120
    • 58849113213 scopus 로고    scopus 로고
    • Pharmacological manipulation of the RAR/RXR signaling pathway maintains the repopulating capacity of hematopoietic stem cells in culture
    • Safi R, Muramoto GG, Salter AB, Meadows S, Himburg H, Russell L, et al. Pharmacological manipulation of the RAR/RXR signaling pathway maintains the repopulating capacity of hematopoietic stem cells in culture. Mol Endocrinol 2009, 23:188-201.
    • (2009) Mol Endocrinol , vol.23 , pp. 188-201
    • Safi, R.1    Muramoto, G.G.2    Salter, A.B.3    Meadows, S.4    Himburg, H.5    Russell, L.6
  • 121
    • 0029132202 scopus 로고
    • Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor
    • Hörlein AJ, Näär AM, Heinzel T, Torchia J, Gloss B, Kurokawa R, et al. Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor. Nature 1995, 377:397-404.
    • (1995) Nature , vol.377 , pp. 397-404
    • Hörlein, A.J.1    Näär, A.M.2    Heinzel, T.3    Torchia, J.4    Gloss, B.5    Kurokawa, R.6
  • 122
    • 0029097233 scopus 로고
    • A transcriptional co-repressor that interacts with nuclear hormone receptors
    • Chen JD, Evans RM A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature 1995, 377:454-457.
    • (1995) Nature , vol.377 , pp. 454-457
    • Chen, J.D.1    Evans, R.M.2
  • 124
    • 79960549182 scopus 로고    scopus 로고
    • A quantitative high throughput screen identifies novel inhibitors of the interaction of thyroid receptor beta with a peptide of steroid receptor coactivator 2
    • Johnson RL, Hwang JY, Arnold LA, Huang R, Wichterman J, Augustinaite I, et al. A quantitative high throughput screen identifies novel inhibitors of the interaction of thyroid receptor beta with a peptide of steroid receptor coactivator 2. J Biomol Screen 2011, 16:618-627.
    • (2011) J Biomol Screen , vol.16 , pp. 618-627
    • Johnson, R.L.1    Hwang, J.Y.2    Arnold, L.A.3    Huang, R.4    Wichterman, J.5    Augustinaite, I.6
  • 125
    • 80054988658 scopus 로고    scopus 로고
    • Similarities and differences between two modes of antagonism of the thyroid hormone receptor
    • Sadana P, Hwang JY, Attia RR, Arnold LA, Neale G, Guy RK Similarities and differences between two modes of antagonism of the thyroid hormone receptor. ACS Chem Biol 2011, 6:1096-1106.
    • (2011) ACS Chem Biol , vol.6 , pp. 1096-1106
    • Sadana, P.1    Hwang, J.Y.2    Attia, R.R.3    Arnold, L.A.4    Neale, G.5    Guy, R.K.6
  • 126
    • 0033997885 scopus 로고    scopus 로고
    • The thyroxine-binding proteins
    • Schussler GC The thyroxine-binding proteins. Thyroid 2000, 10:141-149.
    • (2000) Thyroid , vol.10 , pp. 141-149
    • Schussler, G.C.1
  • 128
    • 28044432318 scopus 로고    scopus 로고
    • Transthyretin is not necessary for thyroid hormone metabolism in conditions of increased hormone demand
    • Sousa JC, de Escobar GM, Oliveira P, Saraiva MJ, Palha JA Transthyretin is not necessary for thyroid hormone metabolism in conditions of increased hormone demand. J Endocrinol 2005, 187:257-266.
    • (2005) J Endocrinol , vol.187 , pp. 257-266
    • Sousa, J.C.1    de Escobar, G.M.2    Oliveira, P.3    Saraiva, M.J.4    Palha, J.A.5
  • 129
    • 0031773503 scopus 로고    scopus 로고
    • Complete thyroxine-binding globulin (TBG) deficiency produced by a mutation in acceptor splice site causing frameshift and early termination of translation (TBG-Kankakee)
    • Carvalho GA, Weiss RE, Refetoff S Complete thyroxine-binding globulin (TBG) deficiency produced by a mutation in acceptor splice site causing frameshift and early termination of translation (TBG-Kankakee). J Clin Endocrinol Metab 1998, 83:3604-3608.
    • (1998) J Clin Endocrinol Metab , vol.83 , pp. 3604-3608
    • Carvalho, G.A.1    Weiss, R.E.2    Refetoff, S.3
  • 130
    • 0034046012 scopus 로고    scopus 로고
    • Concordant decreases of thyroxine and thyroxine binding protein concentrations during sepsis
    • Afandi B, Vera R, Schussler GC, Yap MG Concordant decreases of thyroxine and thyroxine binding protein concentrations during sepsis. Metabolism 2000, 49:753-754.
    • (2000) Metabolism , vol.49 , pp. 753-754
    • Afandi, B.1    Vera, R.2    Schussler, G.C.3    Yap, M.G.4
  • 131
    • 84867765495 scopus 로고    scopus 로고
    • New approaches to assess the transthyretin binding capacity of bioactivated thyroid hormone disruptors
    • Montaño M, Cocco E, Guignard C, Marsh G, Hoffmann L, Bergman A, et al. New approaches to assess the transthyretin binding capacity of bioactivated thyroid hormone disruptors. Toxicol Sci 2012, 130:94-105.
    • (2012) Toxicol Sci , vol.130 , pp. 94-105
    • Montaño, M.1    Cocco, E.2    Guignard, C.3    Marsh, G.4    Hoffmann, L.5    Bergman, A.6
  • 132
    • 0026763858 scopus 로고
    • Effects of interleukin-6 on the expression of thyroid hormone-binding protein genes in cultured human hepatoblastoma-derived (Hep G2) cells
    • Bartalena L, Farsetti A, Flink IL, Robbins J Effects of interleukin-6 on the expression of thyroid hormone-binding protein genes in cultured human hepatoblastoma-derived (Hep G2) cells. Mol Endocrinol 1992, 6:935-942.
    • (1992) Mol Endocrinol , vol.6 , pp. 935-942
    • Bartalena, L.1    Farsetti, A.2    Flink, I.L.3    Robbins, J.4
  • 135
    • 0036793106 scopus 로고    scopus 로고
    • Identification of a novel human organic anion transporting polypeptide as a high affinity thyroxine transporter
    • Pizzagalli F, Hagenbuch B, Stieger B, Klenk U, Folkers G, Meier PJ Identification of a novel human organic anion transporting polypeptide as a high affinity thyroxine transporter. Mol Endocrinol 2002, 16:2283-2296.
    • (2002) Mol Endocrinol , vol.16 , pp. 2283-2296
    • Pizzagalli, F.1    Hagenbuch, B.2    Stieger, B.3    Klenk, U.4    Folkers, G.5    Meier, P.J.6
  • 136
    • 42249084123 scopus 로고    scopus 로고
    • Tissue-specific mRNA expression profiles of human solute carrier transporter superfamilies
    • Nishimura M, Naito S Tissue-specific mRNA expression profiles of human solute carrier transporter superfamilies. Drug Metab Pharmacokinet 2008, 23:22-44.
    • (2008) Drug Metab Pharmacokinet , vol.23 , pp. 22-44
    • Nishimura, M.1    Naito, S.2
  • 137
    • 74749085075 scopus 로고    scopus 로고
    • Molecular aspects of thyroid hormone transporters, including MCT8, MCT10, and OATPs, and the effects of genetic variation in these transporters
    • van der Deure WM, Peeters RP, Visser TJ Molecular aspects of thyroid hormone transporters, including MCT8, MCT10, and OATPs, and the effects of genetic variation in these transporters. J Mol Endocrinol 2010, 44:1-11.
    • (2010) J Mol Endocrinol , vol.44 , pp. 1-11
    • van der Deure, W.M.1    Peeters, R.P.2    Visser, T.J.3
  • 138
    • 84857433358 scopus 로고    scopus 로고
    • Impact of Oatp1c1 deficiency on thyroid hormone metabolism and action in the mouse brain
    • Mayerl S, Visser TJ, Darras VM, Horn S, Heuer H Impact of Oatp1c1 deficiency on thyroid hormone metabolism and action in the mouse brain. Endocrinology 2012, 153:1528-1537.
    • (2012) Endocrinology , vol.153 , pp. 1528-1537
    • Mayerl, S.1    Visser, T.J.2    Darras, V.M.3    Horn, S.4    Heuer, H.5
  • 140
    • 0025294669 scopus 로고
    • Calcium is the first messenger for the action of thyroid hormone at the level of the plasma membrane: first evidence for an acute effect of thyroid hormone on calcium uptake in the heart
    • Segal J Calcium is the first messenger for the action of thyroid hormone at the level of the plasma membrane: first evidence for an acute effect of thyroid hormone on calcium uptake in the heart. Endocrinology 1990, 126:2693-2702.
    • (1990) Endocrinology , vol.126 , pp. 2693-2702
    • Segal, J.1
  • 141
    • 71649109028 scopus 로고    scopus 로고
    • Surface translocation and tri-iodothyronine uptake of mutant MCT8 proteins are cell type-dependent
    • Kinne A, Roth S, Biebermann H, Köhrle J, Grüters A, Schweizer U Surface translocation and tri-iodothyronine uptake of mutant MCT8 proteins are cell type-dependent. J Mol Endocrinol 2009, 43:263-271.
    • (2009) J Mol Endocrinol , vol.43 , pp. 263-271
    • Kinne, A.1    Roth, S.2    Biebermann, H.3    Köhrle, J.4    Grüters, A.5    Schweizer, U.6
  • 142
    • 70350279309 scopus 로고    scopus 로고
    • The blood-brain barrier thyroxine transporter organic anion-transporting polypeptide 1c1 displays atypical transport kinetics
    • Westholm DE, Salo DR, Viken KJ, Rumbley JN, Anderson GW The blood-brain barrier thyroxine transporter organic anion-transporting polypeptide 1c1 displays atypical transport kinetics. Endocrinology 2009, 150:5153-5162.
    • (2009) Endocrinology , vol.150 , pp. 5153-5162
    • Westholm, D.E.1    Salo, D.R.2    Viken, K.J.3    Rumbley, J.N.4    Anderson, G.W.5
  • 143
    • 77956236827 scopus 로고    scopus 로고
    • Retinoic acid induces expression of the thyroid hormone transporter, monocarboxylate transporter 8 (Mct8)
    • Kogai T, Liu Y-Y, Richter LL, Mody K, Kagechika H, Brent GA Retinoic acid induces expression of the thyroid hormone transporter, monocarboxylate transporter 8 (Mct8). J Biol Chem 2010, 285:27279-27288.
    • (2010) J Biol Chem , vol.285 , pp. 27279-27288
    • Kogai, T.1    Liu, Y.-Y.2    Richter, L.L.3    Mody, K.4    Kagechika, H.5    Brent, G.A.6
  • 144
    • 59649091925 scopus 로고    scopus 로고
    • The monocarboxylate transporter 8 and L-type amino acid transporters 1 and 2 are expressed in mouse skeletons and in osteoblastic MC3T3-E1 cells
    • Capelo LP, Beber EH, Fonseca TL, Gouveia CHA The monocarboxylate transporter 8 and L-type amino acid transporters 1 and 2 are expressed in mouse skeletons and in osteoblastic MC3T3-E1 cells. Thyroid 2009, 19:171-180.
    • (2009) Thyroid , vol.19 , pp. 171-180
    • Capelo, L.P.1    Beber, E.H.2    Fonseca, T.L.3    Gouveia, C.H.A.4
  • 146
    • 0242384851 scopus 로고    scopus 로고
    • Functional characterization of rat brain-specific organic anion transporter (Oatp14) at the blood-brain barrier: high affinity transporter for thyroxine
    • Sugiyama D, Kusuhara H, Taniguchi H, Ishikawa S, Nozaki Y, Aburatani H, et al. Functional characterization of rat brain-specific organic anion transporter (Oatp14) at the blood-brain barrier: high affinity transporter for thyroxine. J Biol Chem 2003, 278:43489-43495.
    • (2003) J Biol Chem , vol.278 , pp. 43489-43495
    • Sugiyama, D.1    Kusuhara, H.2    Taniguchi, H.3    Ishikawa, S.4    Nozaki, Y.5    Aburatani, H.6
  • 147
    • 29144438784 scopus 로고    scopus 로고
    • Alteration of thyroid hormone homeostasis by antiepileptic drugs in humans: involvement of glucuronosyltransferase induction
    • Benedetti MS, Whomsley R, Baltes E, Tonner F Alteration of thyroid hormone homeostasis by antiepileptic drugs in humans: involvement of glucuronosyltransferase induction. Eur J Clin Pharmacol 2005, 61:863-872.
    • (2005) Eur J Clin Pharmacol , vol.61 , pp. 863-872
    • Benedetti, M.S.1    Whomsley, R.2    Baltes, E.3    Tonner, F.4
  • 148
    • 39749153526 scopus 로고    scopus 로고
    • Reawakened interest in type III iodothyronine deiodinase in critical illness and injury
    • Huang SA, Bianco AC Reawakened interest in type III iodothyronine deiodinase in critical illness and injury. Nat Clin Pract Endocrinol Metab 2008, 4:148-155.
    • (2008) Nat Clin Pract Endocrinol Metab , vol.4 , pp. 148-155
    • Huang, S.A.1    Bianco, A.C.2
  • 150
    • 23344450788 scopus 로고    scopus 로고
    • Induction of phase I, II and III drug metabolism/transport by xenobiotics
    • Xu C, Li CY-T, Kong A-NT Induction of phase I, II and III drug metabolism/transport by xenobiotics. Arch Pharm Res 2005, 28:249-268.
    • (2005) Arch Pharm Res , vol.28 , pp. 249-268
    • Xu, C.1    Li, C.Y.-T.2    Kong, A.-N.T.3
  • 151
    • 0027235464 scopus 로고
    • Glucuronidation of thyroid hormone by human bilirubin and phenol UDP-glucuronyltransferase isoenzymes
    • Visser TJ, Kaptein E, Gijzel AL, de Herder WW, Ebner T, Burchell B Glucuronidation of thyroid hormone by human bilirubin and phenol UDP-glucuronyltransferase isoenzymes. FEBS Lett 1993, 324:358-360.
    • (1993) FEBS Lett , vol.324 , pp. 358-360
    • Visser, T.J.1    Kaptein, E.2    Gijzel, A.L.3    de Herder, W.W.4    Ebner, T.5    Burchell, B.6
  • 152
    • 0034458006 scopus 로고    scopus 로고
    • Characterization of the uridine diphosphate-glucuronosyltransferase-catalyzing thyroid hormone glucuronidation in man
    • Findlay KA, Kaptein E, Visser TJ, Burchell B Characterization of the uridine diphosphate-glucuronosyltransferase-catalyzing thyroid hormone glucuronidation in man. J Clin Endocrinol Metab 2000, 85:2879-2883.
    • (2000) J Clin Endocrinol Metab , vol.85 , pp. 2879-2883
    • Findlay, K.A.1    Kaptein, E.2    Visser, T.J.3    Burchell, B.4
  • 153
    • 69749109088 scopus 로고    scopus 로고
    • Synergistic acceleration of thyroid hormone degradation by phenobarbital and the PPAR alpha agonist WY14643 in rat hepatocytes
    • Wieneke N, Neuschäfer-Rube F, Bode LM, Kuna M, Andres J, Carnevali LC, et al. Synergistic acceleration of thyroid hormone degradation by phenobarbital and the PPAR alpha agonist WY14643 in rat hepatocytes. Toxicol Appl Pharmacol 2009, 240:99-107.
    • (2009) Toxicol Appl Pharmacol , vol.240 , pp. 99-107
    • Wieneke, N.1    Neuschäfer-Rube, F.2    Bode, L.M.3    Kuna, M.4    Andres, J.5    Carnevali, L.C.6
  • 154
    • 14244251989 scopus 로고    scopus 로고
    • CARs and drugs: a risky combination
    • Zavacki AM, Larsen PR CARs and drugs: a risky combination. Endocrinology 2005, 146:992-994.
    • (2005) Endocrinology , vol.146 , pp. 992-994
    • Zavacki, A.M.1    Larsen, P.R.2
  • 155
    • 0027943720 scopus 로고
    • Uptake of triiodothyroacetic acid and its effect on thyrotropin secretion in cultured anterior pituitary cells
    • Everts ME, Visser TJ, Moerings EP, Docter R, van Toor H, Tempelaars AM, et al. Uptake of triiodothyroacetic acid and its effect on thyrotropin secretion in cultured anterior pituitary cells. Endocrinology 1994, 135:2700-2707.
    • (1994) Endocrinology , vol.135 , pp. 2700-2707
    • Everts, M.E.1    Visser, T.J.2    Moerings, E.P.3    Docter, R.4    van Toor, H.5    Tempelaars, A.M.6
  • 156
    • 0028990141 scopus 로고
    • Long-lasting effects of Triac and thyroxine on the control of thyrotropin and hepatic deiodinase type I
    • Juge-Aubry CE, Morin O, Pernin AT, Liang H, Philippe J, Burger AG Long-lasting effects of Triac and thyroxine on the control of thyrotropin and hepatic deiodinase type I. Eur J Endocrinol 1995, 132:751-758.
    • (1995) Eur J Endocrinol , vol.132 , pp. 751-758
    • Juge-Aubry, C.E.1    Morin, O.2    Pernin, A.T.3    Liang, H.4    Philippe, J.5    Burger, A.G.6
  • 157
    • 0035118770 scopus 로고    scopus 로고
    • Differences between the effects of thyroxine and tetraiodothyroacetic acid on TSH suppression and cardiac hypertrophy
    • Lameloise N, Siegrist-Kaiser C, O'Connell M, Burger A Differences between the effects of thyroxine and tetraiodothyroacetic acid on TSH suppression and cardiac hypertrophy. Eur J Endocrinol 2001, 144:145-154.
    • (2001) Eur J Endocrinol , vol.144 , pp. 145-154
    • Lameloise, N.1    Siegrist-Kaiser, C.2    O'Connell, M.3    Burger, A.4
  • 158
    • 0018967637 scopus 로고
    • Serum concentration, metabolic clearance, and production rates of 3,5,3'triiodothyroacetic acid in normal and athyreotic man
    • Gavin LA, Livermore BM, Cavalieri RR, Hammond ME, Castle JN Serum concentration, metabolic clearance, and production rates of 3,5,3'triiodothyroacetic acid in normal and athyreotic man. J Clin Endocrinol Metab 1980, 51:529-534.
    • (1980) J Clin Endocrinol Metab , vol.51 , pp. 529-534
    • Gavin, L.A.1    Livermore, B.M.2    Cavalieri, R.R.3    Hammond, M.E.4    Castle, J.N.5
  • 159
    • 84903399517 scopus 로고    scopus 로고
    • FDA, FDA and the U.S. Attorney for the Western District of Texas Announce Guilty Plea in Drug Counterfeiting Case, Press release accessed on.
    • FDA, FDA and the U.S. Attorney for the Western District of Texas Announce Guilty Plea in Drug Counterfeiting Case, 2004 Press release accessed on . http://www.fda.gov/NewsEvents/Newsroom/PressAnnouncements/2004/ucm108266.htm.
    • (2004)
  • 160
    • 84903399502 scopus 로고    scopus 로고
    • FDA, Tiratricol (triiodothyroacetic acid). Safety Alerts for Human Medical Products
    • FDA, Tiratricol (triiodothyroacetic acid). Safety Alerts for Human Medical Products 2009.
    • (2009)
  • 161
  • 162
    • 84876733947 scopus 로고    scopus 로고
    • Mechanism-based testing strategy using in vitro approaches for identification of thyroid hormone disrupting chemicals
    • 10.1016/j.tiv.2013.02.012
    • Murk AJ, Rijntjes E, Blaauboer BJ, Clewell R, Crofton KM, Dingemans MML, et al. Mechanism-based testing strategy using in vitro approaches for identification of thyroid hormone disrupting chemicals. Toxicol In Vitro 2013, 10.1016/j.tiv.2013.02.012.
    • (2013) Toxicol In Vitro
    • Murk, A.J.1    Rijntjes, E.2    Blaauboer, B.J.3    Clewell, R.4    Crofton, K.M.5    Dingemans, M.M.L.6
  • 163
    • 47249109317 scopus 로고    scopus 로고
    • Stability indicating validated HPLC method for quantification of levothyroxine with eight degradation peaks in the presence of excipients
    • Shah RB, Bryant A, Collier J, Habib MJ, Khan MA Stability indicating validated HPLC method for quantification of levothyroxine with eight degradation peaks in the presence of excipients. Int J Pharm 2008, 360:77-82.
    • (2008) Int J Pharm , vol.360 , pp. 77-82
    • Shah, R.B.1    Bryant, A.2    Collier, J.3    Habib, M.J.4    Khan, M.A.5
  • 164
    • 40249113342 scopus 로고    scopus 로고
    • The Sterolgene v0 cDNA microarray: a systemic approach to studies of cholesterol homeostasis and drug metabolism
    • Režen T, Juvan P, Tacer KF, Kuzman D, Roth A, Pompon D, et al. The Sterolgene v0 cDNA microarray: a systemic approach to studies of cholesterol homeostasis and drug metabolism. BMC Genomics 2008, 9:76.
    • (2008) BMC Genomics , vol.9 , pp. 76
    • Režen, T.1    Juvan, P.2    Tacer, K.F.3    Kuzman, D.4    Roth, A.5    Pompon, D.6
  • 165
    • 10344230404 scopus 로고    scopus 로고
    • Molecular genetic defects in congenital hypothyroidism
    • Gruters A Molecular genetic defects in congenital hypothyroidism. Eur J Endocrinol 2004, 151:U39-U44.
    • (2004) Eur J Endocrinol , vol.151
    • Gruters, A.1
  • 166
    • 58549107573 scopus 로고    scopus 로고
    • Two puzzling cases of thyroid dysgenesis
    • Kuehnen P, Grueters A, Krude H Two puzzling cases of thyroid dysgenesis. Horm Res 2009, 71:93-97.
    • (2009) Horm Res , vol.71 , pp. 93-97
    • Kuehnen, P.1    Grueters, A.2    Krude, H.3
  • 167
    • 13544273520 scopus 로고    scopus 로고
    • Linkage and mutational analysis of familial thyroid dysgenesis demonstrate genetic heterogeneity implicating novel genes
    • Castanet M, Sura-Trueba S, Chauty A, Carré A, de Roux N, Heath S, et al. Linkage and mutational analysis of familial thyroid dysgenesis demonstrate genetic heterogeneity implicating novel genes. Eur J Hum Genet 2005, 13:232-239.
    • (2005) Eur J Hum Genet , vol.13 , pp. 232-239
    • Castanet, M.1    Sura-Trueba, S.2    Chauty, A.3    Carré, A.4    de Roux, N.5    Heath, S.6
  • 168
    • 5444271023 scopus 로고    scopus 로고
    • Thyroid development and its disorders: genetics and molecular mechanisms
    • Felice MD, Lauro RD Thyroid development and its disorders: genetics and molecular mechanisms. Endocr Rev 2004, 25:722-746.
    • (2004) Endocr Rev , vol.25 , pp. 722-746
    • Felice, M.D.1    Lauro, R.D.2
  • 169
    • 27844552888 scopus 로고    scopus 로고
    • Thyroid dysgenesis: multigenic or epigenetic .. or both?
    • Vassart G, Dumont JE Thyroid dysgenesis: multigenic or epigenetic .. or both?. Endocrinology 2005, 146:5035-5037.
    • (2005) Endocrinology , vol.146 , pp. 5035-5037
    • Vassart, G.1    Dumont, J.E.2
  • 170
    • 0033812161 scopus 로고    scopus 로고
    • Drug therapy for hyperthyroidism in pregnancy: safety issues for mother and fetus
    • Atkins P, Cohen SB, Phillips BJ Drug therapy for hyperthyroidism in pregnancy: safety issues for mother and fetus. Drug Saf 2000, 23:229-244.
    • (2000) Drug Saf , vol.23 , pp. 229-244
    • Atkins, P.1    Cohen, S.B.2    Phillips, B.J.3
  • 171
    • 0032770523 scopus 로고    scopus 로고
    • Radioiodine and pregnancy
    • Gorman CA Radioiodine and pregnancy. Thyroid 1999, 9:721-726.
    • (1999) Thyroid , vol.9 , pp. 721-726
    • Gorman, C.A.1
  • 172
    • 18244368524 scopus 로고    scopus 로고
    • A population-based study on the frequency of additional congenital malformations in infants with congenital hypothyroidism: data from the Italian Registry for Congenital Hypothyroidism (1991-1998)
    • Olivieri A, Stazi MA, Mastroiacovo P, Fazzini C, Medda E, Spagnolo A, et al. A population-based study on the frequency of additional congenital malformations in infants with congenital hypothyroidism: data from the Italian Registry for Congenital Hypothyroidism (1991-1998). J Clin Endocrinol Metab 2002, 87:557-562.
    • (2002) J Clin Endocrinol Metab , vol.87 , pp. 557-562
    • Olivieri, A.1    Stazi, M.A.2    Mastroiacovo, P.3    Fazzini, C.4    Medda, E.5    Spagnolo, A.6
  • 173
    • 84855522667 scopus 로고    scopus 로고
    • Genetics of thyroid function and disease
    • Panicker V Genetics of thyroid function and disease. Clin Biochem Rev 2011, 32:165-175.
    • (2011) Clin Biochem Rev , vol.32 , pp. 165-175
    • Panicker, V.1
  • 174
    • 0035095887 scopus 로고    scopus 로고
    • Evidence for a major role of heredity in Graves' disease: a population-based study of two Danish twin cohorts
    • Brix TH, Kyvik KO, Christensen K, Hegedüs L Evidence for a major role of heredity in Graves' disease: a population-based study of two Danish twin cohorts. J Clin Endocrinol Metab 2001, 86:930-934.
    • (2001) J Clin Endocrinol Metab , vol.86 , pp. 930-934
    • Brix, T.H.1    Kyvik, K.O.2    Christensen, K.3    Hegedüs, L.4
  • 175
    • 84867403047 scopus 로고    scopus 로고
    • The incidence and prevalence of thyroid autoimmunity
    • McLeod DSA, Cooper DS The incidence and prevalence of thyroid autoimmunity. Endocrine 2012, 42:252-265.
    • (2012) Endocrine , vol.42 , pp. 252-265
    • McLeod, D.S.A.1    Cooper, D.S.2
  • 177
    • 0036072337 scopus 로고    scopus 로고
    • Goitrogenic and estrogenic activity of soy isoflavones
    • Doerge DR, Sheehan DM Goitrogenic and estrogenic activity of soy isoflavones. Environ Health Perspect 2002, 110:349-353.
    • (2002) Environ Health Perspect , vol.110 , pp. 349-353
    • Doerge, D.R.1    Sheehan, D.M.2
  • 178
    • 22144494707 scopus 로고    scopus 로고
    • Integrin αVβ3 contains a cell surface receptor site for thyroid hormone that is linked to activation of mitogen-activated protein kinase and induction of angiogenesis
    • Bergh JJ, Lin H-Y, Lansing L, Mohamed SN, Davis FB, Mousa S, et al. Integrin αVβ3 contains a cell surface receptor site for thyroid hormone that is linked to activation of mitogen-activated protein kinase and induction of angiogenesis. Endocrinology 2005, 146:2864-2871.
    • (2005) Endocrinology , vol.146 , pp. 2864-2871
    • Bergh, J.J.1    Lin, H.-Y.2    Lansing, L.3    Mohamed, S.N.4    Davis, F.B.5    Mousa, S.6
  • 179
    • 0017884170 scopus 로고
    • Lithium treatment for psychiatric disorders
    • Maletzky BM, Shore JH Lithium treatment for psychiatric disorders. West J Med 1978, 128:488-498.
    • (1978) West J Med , vol.128 , pp. 488-498
    • Maletzky, B.M.1    Shore, J.H.2
  • 181
    • 84873623726 scopus 로고    scopus 로고
    • Thyroid functions and bipolar affective disorder
    • Chakrabarti S Thyroid functions and bipolar affective disorder. J Thyroid Res 2011, 2011:1-13.
    • (2011) J Thyroid Res , vol.2011 , pp. 1-13
    • Chakrabarti, S.1
  • 182
    • 0031764843 scopus 로고    scopus 로고
    • The effects of lithium therapy on thyroid and thyrotropin-releasing hormone
    • Lazarus JH The effects of lithium therapy on thyroid and thyrotropin-releasing hormone. Thyroid 1998, 8:909-913.
    • (1998) Thyroid , vol.8 , pp. 909-913
    • Lazarus, J.H.1
  • 183
    • 0033964118 scopus 로고    scopus 로고
    • High-throughput and ultra-high-throughput screening: solution- and cell-based approaches
    • Sundberg SA High-throughput and ultra-high-throughput screening: solution- and cell-based approaches. Curr Opin Biotechnol 2000, 11:47-53.
    • (2000) Curr Opin Biotechnol , vol.11 , pp. 47-53
    • Sundberg, S.A.1
  • 185
    • 0030753429 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha (TNF-alpha) and transforming growth factor-beta 1 (TGF-beta 1) inhibit the expression and activity of Na+/K(+)-ATPase in FRTL-5 rat thyroid cells
    • Pekary AE, Levin SR, Johnson DG, Berg L, Hershman JM Tumor necrosis factor-alpha (TNF-alpha) and transforming growth factor-beta 1 (TGF-beta 1) inhibit the expression and activity of Na+/K(+)-ATPase in FRTL-5 rat thyroid cells. J Interferon Cytokine Res 1997, 17:185-195.
    • (1997) J Interferon Cytokine Res , vol.17 , pp. 185-195
    • Pekary, A.E.1    Levin, S.R.2    Johnson, D.G.3    Berg, L.4    Hershman, J.M.5
  • 186
    • 69549122856 scopus 로고    scopus 로고
    • Simple, rapid zebrafish larva bioassay for assessing the potential of chemical pollutants and drugs to disrupt thyroid gland function
    • Ralduúa D, Babin PJ Simple, rapid zebrafish larva bioassay for assessing the potential of chemical pollutants and drugs to disrupt thyroid gland function. Environ Sci Technol 2009, 43:6844-6850.
    • (2009) Environ Sci Technol , vol.43 , pp. 6844-6850
    • Ralduúa, D.1    Babin, P.J.2
  • 187
    • 77954463079 scopus 로고    scopus 로고
    • Therapeutic concentrations of mitotane (o,p-DDD) inhibit thyrotroph cell viability and TSH expression and secretion in a mouse cell line model
    • Zatelli MC, Gentilin E, Daffara F, Tagliati F, Reimondo G, Carandina G, et al. Therapeutic concentrations of mitotane (o,p-DDD) inhibit thyrotroph cell viability and TSH expression and secretion in a mouse cell line model. Endocrinology 2010, 151:2453-2461.
    • (2010) Endocrinology , vol.151 , pp. 2453-2461
    • Zatelli, M.C.1    Gentilin, E.2    Daffara, F.3    Tagliati, F.4    Reimondo, G.5    Carandina, G.6
  • 188
    • 21344441049 scopus 로고    scopus 로고
    • Expression of recombinant membrane-bound type I iodothyronine deiodinase in yeast
    • Kuiper GGJM, Klootwijk W, Visser TJ Expression of recombinant membrane-bound type I iodothyronine deiodinase in yeast. J Mol Endocrinol 2005, 34:865-878.
    • (2005) J Mol Endocrinol , vol.34 , pp. 865-878
    • Kuiper, G.G.J.M.1    Klootwijk, W.2    Visser, T.J.3
  • 189
    • 80054762464 scopus 로고    scopus 로고
    • Structure-activity relationships for hydroxylated polychlorinated biphenyls as inhibitors of the sulfation of dehydroepiandrosterone catalyzed by human hydroxysteroid sulfotransferase SULT2A1
    • Ekuase EJ, Liu Y, Lehmler H-J, Robertson LW, Duffel MW Structure-activity relationships for hydroxylated polychlorinated biphenyls as inhibitors of the sulfation of dehydroepiandrosterone catalyzed by human hydroxysteroid sulfotransferase SULT2A1. Chem Res Toxicol 2011, 24:1720-1728.
    • (2011) Chem Res Toxicol , vol.24 , pp. 1720-1728
    • Ekuase, E.J.1    Liu, Y.2    Lehmler, H.-J.3    Robertson, L.W.4    Duffel, M.W.5
  • 190
    • 84857377134 scopus 로고    scopus 로고
    • Polychlorinated biphenyl congeners that increase the glucuronidation and biliary excretion of thyroxine are distinct from the congeners that enhance the serum disappearance of thyroxine
    • Martin LA, Wilson DT, Reuhl KR, Gallo MA, Klaassen CD Polychlorinated biphenyl congeners that increase the glucuronidation and biliary excretion of thyroxine are distinct from the congeners that enhance the serum disappearance of thyroxine. Drug Metab Dispos 2012, 40:588-595.
    • (2012) Drug Metab Dispos , vol.40 , pp. 588-595
    • Martin, L.A.1    Wilson, D.T.2    Reuhl, K.R.3    Gallo, M.A.4    Klaassen, C.D.5


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