메뉴 건너뛰기




Volumn 22, Issue 2, 1996, Pages 95-119

Membrane iodothyronine transporters part II: Review of protein biochemistry

Author keywords

[No Author keywords available]

Indexed keywords

BENZODIAZEPINE; BINDING PROTEIN; IODOTHYRONINE; PLASMA PROTEIN; THYROXINE;

EID: 0029884539     PISSN: 07435800     EISSN: None     Source Type: Journal    
DOI: 10.1080/07435809609030500     Document Type: Review
Times cited : (16)

References (119)
  • 1
    • 0027971390 scopus 로고
    • Membrane iodothyronine transporters Part I: Review of physiology
    • Kragie L. 1994 Membrane iodothyronine transporters Part I: review of physiology. Endo Res ; 20(4):319-342.
    • (1994) Endo Res , vol.20 , Issue.4 , pp. 319-342
    • Kragie, L.1
  • 2
    • 0030071445 scopus 로고    scopus 로고
    • Tripartite steroid hormone receptor pharmacology: Interaction with multiple effector sites as a basis for the cell-and promoter-specific action of thse hormones
    • Katzenellenbogen JA, O'Malley BW, Katzenellenbogen BS. 1996 Tripartite steroid hormone receptor pharmacology: interaction with multiple effector sites as a basis for the cell-and promoter-specific action of thse hormones. Molecular Endocrinology ; 10(2):119-131.
    • (1996) Molecular Endocrinology , vol.10 , Issue.2 , pp. 119-131
    • Katzenellenbogen, J.A.1    O'Malley, B.W.2    Katzenellenbogen, B.S.3
  • 3
    • 0026724592 scopus 로고
    • Triiodothyronine binding sites in the rat erythrocyte membrane: Involvement in triiodothyronine transport and relation to the tryptophan transport System T
    • Samson M, Osty J, Francon J, Blondear J-P. 1992 Triiodothyronine binding sites in the rat erythrocyte membrane: involvement in triiodothyronine transport and relation to the tryptophan transport System T. Biochim Biophys Acta ; 1108:91-98.
    • (1992) Biochim Biophys Acta , vol.1108 , pp. 91-98
    • Samson, M.1    Osty, J.2    Francon, J.3    Blondear, J.-P.4
  • 4
    • 0027316038 scopus 로고
    • Identification by photoaffinity labeling of a membrane thyroid hormone-binding protein associated with the triiodothyronine transport system in rat erythrocytes
    • Samson M, Osty J, Blondeau JP. 1993 Identification by photoaffinity labeling of a membrane thyroid hormone-binding protein associated with the triiodothyronine transport system in rat erythrocytes. Endocrinology ; 132(6):2470-6.
    • (1993) Endocrinology , vol.132 , Issue.6 , pp. 2470-2476
    • Samson, M.1    Osty, J.2    Blondeau, J.P.3
  • 5
    • 0025347918 scopus 로고
    • The transport of thyroxine into mouse neuroblastoma cells, NB41A3: The effect of L-system amino acids
    • Lakshmanan M, Goncalves E, Lessly G, Foti D, Robbins J. 1990 The transport of thyroxine into mouse neuroblastoma cells, NB41A3: the effect of L-system amino acids. Endocrinology ; 126:3245-3250.
    • (1990) Endocrinology , vol.126 , pp. 3245-3250
    • Lakshmanan, M.1    Goncalves, E.2    Lessly, G.3    Foti, D.4    Robbins, J.5
  • 6
    • 85035163160 scopus 로고
    • Desmethylimipramine, a potent blocker of synaptosomal norepinephrine transport, also blocks triiodothyronine transport into rat brain synaptosomes
    • Abstr #816
    • Tomlinson EE, Dratman MB. 1993 Desmethylimipramine, a potent blocker of synaptosomal norepinephrine transport, also blocks triiodothyronine transport into rat brain synaptosomes. 75th Annual Meeting of The Endocrine Society . Abstr #816.
    • (1993) 75th Annual Meeting of the Endocrine Society
    • Tomlinson, E.E.1    Dratman, M.B.2
  • 10
    • 0027162723 scopus 로고
    • L-triiodothyronine: Is this peripheral hormone a central neurotransmitter?
    • Mason GA, Walker CH, Prange Jr AJ. 1993 L-triiodothyronine: is this peripheral hormone a central neurotransmitter? Neuropsychopharmacology ; 8(3):253-8.
    • (1993) Neuropsychopharmacology , vol.8 , Issue.3 , pp. 253-258
    • Mason, G.A.1    Walker, C.H.2    Prange Jr., A.J.3
  • 11
    • 0027258087 scopus 로고
    • Effect of L-thyroxine and carbimazole on brain biogenic amines and amino acids in rats
    • Upadhyaya L, Agrawal JK. 1993 Effect of L-thyroxine and carbimazole on brain biogenic amines and amino acids in rats. Endocr Res ; 19:87-99.
    • (1993) Endocr Res , vol.19 , pp. 87-99
    • Upadhyaya, L.1    Agrawal, J.K.2
  • 12
    • 0023845218 scopus 로고
    • Characterization and localization of glutathione-S-transferases in rat brain and binding of hormones, neurotransmitters, and drugs
    • Abramovitz M, Homma H, Ishigaki S, Tansey F, Cammer W, Listowsky I. 1988 Characterization and localization of glutathione-S-transferases in rat brain and binding of hormones, neurotransmitters, and drugs. J Neurochem; 50(1):50-7.
    • (1988) J Neurochem , vol.50 , Issue.1 , pp. 50-57
    • Abramovitz, M.1    Homma, H.2    Ishigaki, S.3    Tansey, F.4    Cammer, W.5    Listowsky, I.6
  • 13
    • 0024473664 scopus 로고
    • Glutathione-S-transferases are major cytosolic thyroid hormone binding proteins
    • Ishigaki S, Abramovitz M, Listowsky I. 1989 Glutathione-S-transferases are major cytosolic thyroid hormone binding proteins. Arch Biochem Biophys ; 273(2):265-72.
    • (1989) Arch Biochem Biophys , vol.273 , Issue.2 , pp. 265-272
    • Ishigaki, S.1    Abramovitz, M.2    Listowsky, I.3
  • 14
    • 0018697743 scopus 로고
    • Uptake of L-tri-iodothyronine by isolated rat liver cells
    • Eckel J, Rao GS, Rao ML, Breuer H. 1979 Uptake of L-tri-iodothyronine by isolated rat liver cells. Biochem J ; 182:473-491.
    • (1979) Biochem J , vol.182 , pp. 473-491
    • Eckel, J.1    Rao, G.S.2    Rao, M.L.3    Breuer, H.4
  • 15
    • 0020562171 scopus 로고
    • A rapid filtration assay for soluble receptors using polyethylenimine-treated filters
    • Bruns RF, Lawson, Wendung K, Pugsley TA. 1983 A rapid filtration assay for soluble receptors using polyethylenimine-treated filters. Anal Biochem ; 132(1):74-81.
    • (1983) Anal Biochem , vol.132 , Issue.1 , pp. 74-81
    • Bruns, R.F.1    Lawson2    Wendung, K.3    Pugsley, T.A.4
  • 16
    • 0026446221 scopus 로고
    • Purification and characterization of rat brain cytosolic 3,5,3′- Triiodo-L-thyronine-binding protein. Evidence for binding activity dependent on NADPH, NADP and thioredoxin
    • Lennon AM. 1992 Purification and characterization of rat brain cytosolic 3,5,3′- triiodo-L-thyronine-binding protein. Evidence for binding activity dependent on NADPH, NADP and thioredoxin. Eur J Biochem ; 210(1):79-85.
    • (1992) Eur J Biochem , vol.210 , Issue.1 , pp. 79-85
    • Lennon, A.M.1
  • 17
    • 0027205409 scopus 로고
    • Structure of the hormone binding domain of human beta 1 thyroid hormone nuclear receptor: Is it an alpha/beta barrel?
    • McPhie P, Parkison C, Lee BK, Cheng SY. 1993 Structure of the hormone binding domain of human beta 1 thyroid hormone nuclear receptor: is it an alpha/beta barrel? Biochemistry ; 32(29):7460-5.
    • (1993) Biochemistry , vol.32 , Issue.29 , pp. 7460-7465
    • McPhie, P.1    Parkison, C.2    Lee, B.K.3    Cheng, S.Y.4
  • 19
    • 0027414076 scopus 로고
    • Thyroxine targets different pathways of internalization of type II iodothyronine 5′-deiodinase in astrocytes
    • Farwell AP, DiBenedetto DJ, Leonard JL. 1993 Thyroxine targets different pathways of internalization of type II iodothyronine 5′-deiodinase in astrocytes. J Biol Chem ; 268(7):5055-62.
    • (1993) J Biol Chem , vol.268 , Issue.7 , pp. 5055-5062
    • Farwell, A.P.1    DiBenedetto, D.J.2    Leonard, J.L.3
  • 21
    • 0024357458 scopus 로고
    • Thyroid hormone effect on rat heart mitochondrial proteins and affinity labeling with N-bromoacetyl-3,3′,5-triiodothyronine. Lack of direct effect on the adenine nucleotide translocase
    • Rasmussen UB, Kohrle J, Rokos H, Hesch R-D. 1989 Thyroid hormone effect on rat heart mitochondrial proteins and affinity labeling with N-bromoacetyl-3,3′,5-triiodothyronine. Lack of direct effect on the adenine nucleotide translocase. FEBS Letters ; 255:385-390.
    • (1989) FEBS Letters , vol.255 , pp. 385-390
    • Rasmussen, U.B.1    Kohrle, J.2    Rokos, H.3    Hesch, R.-D.4
  • 23
    • 0027255880 scopus 로고
    • Selective labelling and inactivation of creatine kinase isoenzymes by the thyroid hormone derivative N-bromoacetyl-3,3′,5-tri-iodo-L-thyronine
    • Wyss M, Wallimann T, Kohrle J. 1993 Selective labelling and inactivation of creatine kinase isoenzymes by the thyroid hormone derivative N-bromoacetyl-3,3′,5-tri-iodo-L-thyronine. Biochem J; 291:463-72.
    • (1993) Biochem J , vol.291 , pp. 463-472
    • Wyss, M.1    Wallimann, T.2    Kohrle, J.3
  • 24
    • 0024077212 scopus 로고
    • Inhibition of uptake of thyroid hormone into rat hepatocytes by preincubation with N-bromoacetyl-3,3′,5-triiodothyronine
    • Docter R, Krenning EP, Bernard HF, Visser TJ, Hennemann G. 1988 Inhibition of uptake of thyroid hormone into rat hepatocytes by preincubation with N-bromoacetyl-3,3′,5-triiodothyronine. Endocrinology; 123:1520-1525.
    • (1988) Endocrinology , vol.123 , pp. 1520-1525
    • Docter, R.1    Krenning, E.P.2    Bernard, H.F.3    Visser, T.J.4    Hennemann, G.5
  • 25
    • 0025979337 scopus 로고
    • Type I iodothyronine deiodinase is a selenocysteine-containing enzyme
    • Berry MJ, Banu L, Larsen PR. 1991 Type I iodothyronine deiodinase is a selenocysteine-containing enzyme. Nature ; 349:438-440.
    • (1991) Nature , vol.349 , pp. 438-440
    • Berry, M.J.1    Banu, L.2    Larsen, P.R.3
  • 27
    • 15844417640 scopus 로고
    • Expression of the transmembrane thyroid hormone transport protein from rat liver in Xenopus Laevis oocytes
    • Toronto Canada, September 1995
    • Docter R, Friesema ECH, van Stralen PGJ, Hennemann G. 1995 Expression of the transmembrane thyroid hormone transport protein from rat liver in Xenopus Laevis oocytes. 11th International Thyroid Conference. Toronto Canada, September 1995.
    • (1995) 11th International Thyroid Conference
    • Docter, R.1    Friesema, E.C.H.2    Van Stralen, P.G.J.3    Hennemann, G.4
  • 28
    • 0026702592 scopus 로고
    • Regulation of thyroid hormone receptor-mediated transcription by a cytosol protein
    • Ashizawa K, Cheng SY. 1992 Regulation of thyroid hormone receptor-mediated transcription by a cytosol protein. Proc Natl Acad Sci USA ; 89(19):9277-81.
    • (1992) Proc Natl Acad Sci USA , vol.89 , Issue.19 , pp. 9277-9281
    • Ashizawa, K.1    Cheng, S.Y.2
  • 29
    • 0027326488 scopus 로고
    • Thyroid hormone transport proteins
    • Bartalena L, Robbins J. 1993 Thyroid hormone transport proteins. Clin Lab Med ; 13(3):583-98.
    • (1993) Clin Lab Med , vol.13 , Issue.3 , pp. 583-598
    • Bartalena, L.1    Robbins, J.2
  • 30
    • 0027723298 scopus 로고
    • Transthyretin expression in the rat brain: Effect of thyroid functional state and role in thyroxine transport
    • Blay P, Nilsson C, Owman C, Aldred A, Schreiber G. 1993 Transthyretin expression in the rat brain: effect of thyroid functional state and role in thyroxine transport. Brain Res ; 632:114-120.
    • (1993) Brain Res , vol.632 , pp. 114-120
    • Blay, P.1    Nilsson, C.2    Owman, C.3    Aldred, A.4    Schreiber, G.5
  • 32
    • 0021142842 scopus 로고
    • Comparison of binding of thyroid hormone analogues to hepatic organic anion binding proteins
    • Sugiyama Y, Stolz A, Hershman JM, Kaplowitz N. 1984 Comparison of binding of thyroid hormone analogues to hepatic organic anion binding proteins. Biochim Biophys Acta ; 801(2):184-8.
    • (1984) Biochim Biophys Acta , vol.801 , Issue.2 , pp. 184-188
    • Sugiyama, Y.1    Stolz, A.2    Hershman, J.M.3    Kaplowitz, N.4
  • 34
    • 0026079434 scopus 로고
    • The monomer of pyruvate kinase subtype Ml, is both a kinase and cytosolic thyroid hormone binding protein
    • Parkison C, Ashizawa K, McPhie P, Lin K-h, Cheng S-y. 1991 The monomer of pyruvate kinase subtype Ml, is both a kinase and cytosolic thyroid hormone binding protein. Biochem Biophys Res Comm ; 179:668-674.
    • (1991) Biochem Biophys Res Comm , vol.179 , pp. 668-674
    • Parkison, C.1    Ashizawa, K.2    McPhie, P.3    Lin, K.-H.4    Cheng, S.-Y.5
  • 35
    • 0025337997 scopus 로고
    • Regulation of thyroid hormone binding to its cytosolic binding protein by L-α-alanine
    • Ashizawa K, Kato H, McPhie P, Cheng S-Y. 1990 Regulation of thyroid hormone binding to its cytosolic binding protein by L-α-alanine. Biochem Biophys Res Comm ; 167:587-592.
    • (1990) Biochem Biophys Res Comm , vol.167 , pp. 587-592
    • Ashizawa, K.1    Kato, H.2    McPhie, P.3    Cheng, S.-Y.4
  • 36
    • 0027530612 scopus 로고
    • Cold-sensitive cytosolic 3,5,3′-triiodo-L-thyronine-binding protein and pyruvate kinase from human erythrocytes share similar regulatory properties of hormone binding by glycolytic intermediates
    • Fanjul AN, Farias RN. 1993 Cold-sensitive cytosolic 3,5,3′-triiodo-L-thyronine-binding protein and pyruvate kinase from human erythrocytes share similar regulatory properties of hormone binding by glycolytic intermediates. J Biol Chem ; 268(1):175-9.
    • (1993) J Biol Chem , vol.268 , Issue.1 , pp. 175-179
    • Fanjul, A.N.1    Farias, R.N.2
  • 38
    • 0026043928 scopus 로고
    • Cellular binding proteins of thyroid hormones
    • Ichikawa K, Hashizume K. 1991 Cellular binding proteins of thyroid hormones. Life Sciences ; 49:1513-1522.
    • (1991) Life Sciences , vol.49 , pp. 1513-1522
    • Ichikawa, K.1    Hashizume, K.2
  • 40
    • 0027441739 scopus 로고
    • Reaction of the type III iodothyronine deiodinase with the affinity label N-bromoacetyl-triiodothyronine
    • Schoenmakers CH, Pigmans IG, Kaptein E, Darras VM, Visser TJ. 1993 Reaction of the type III iodothyronine deiodinase with the affinity label N-bromoacetyl-triiodothyronine. FEBS Lett ; 335(1):104-8.
    • (1993) FEBS Lett , vol.335 , Issue.1 , pp. 104-108
    • Schoenmakers, C.H.1    Pigmans, I.G.2    Kaptein, E.3    Darras, V.M.4    Visser, T.J.5
  • 41
    • 0025875494 scopus 로고
    • Localization of type I iodothyronine 5′-deiodinase to the basolateral plasma membrane in renal cortical epithelial cells
    • Leonard JL, Ekenbarger DM, Frank SJ, Farwell A, Koehrle J. 1991 Localization of type I iodothyronine 5′-deiodinase to the basolateral plasma membrane in renal cortical epithelial cells. J Biol Chem ; 266:11262-11269.
    • (1991) J Biol Chem , vol.266 , pp. 11262-11269
    • Leonard, J.L.1    Ekenbarger, D.M.2    Frank, S.J.3    Farwell, A.4    Koehrle, J.5
  • 43
    • 0027414076 scopus 로고
    • Thyroxine targets different pathways of internalization of type II iodothyronine 5′-deiodinase in astrocytes
    • Farwell AP, DiBenedetto DJ, Leonard JL. 1993 Thyroxine targets different pathways of internalization of type II iodothyronine 5′-deiodinase in astrocytes. J Biol Chem ; 268:5055-5062.
    • (1993) J Biol Chem , vol.268 , pp. 5055-5062
    • Farwell, A.P.1    DiBenedetto, D.J.2    Leonard, J.L.3
  • 44
    • 0027322428 scopus 로고
    • Structural requirements of iodothyronines for the rapid inactivation and internalization of type II iodothyronine 5′-deiodinase in glial cells
    • Safran M, Farwell AP, Rokos H, Leonard JL. 1993 Structural requirements of iodothyronines for the rapid inactivation and internalization of type II iodothyronine 5′-deiodinase in glial cells. J Biol Chem ; 268(19):14224-9.
    • (1993) J Biol Chem , vol.268 , Issue.19 , pp. 14224-14229
    • Safran, M.1    Farwell, A.P.2    Rokos, H.3    Leonard, J.L.4
  • 46
    • 0025102476 scopus 로고
    • Molecular cloning of cDNA encoding a 55-kDa multifunctional thyroid hormone binding protein of skeletal muscle sarcoplasmic reticulum
    • Fliegel L, Newton E, Burns K, Michalak M. 1990 Molecular cloning of cDNA encoding a 55-kDa multifunctional thyroid hormone binding protein of skeletal muscle sarcoplasmic reticulum. J Biol Chem ; 265(26):15496-502.
    • (1990) J Biol Chem , vol.265 , Issue.26 , pp. 15496-15502
    • Fliegel, L.1    Newton, E.2    Burns, K.3    Michalak, M.4
  • 47
    • 0023865390 scopus 로고
    • Thyroid hormone down-regulates p55, a thyroid hormone-binding protein that is homologous to protein disulfide isomerase and the β-subunit of propyl-4-hydroxylase
    • Obata T, Kitagawa S, Gong Q-H, Pastan I, Cheng S-Y. 1988 Thyroid hormone down-regulates p55, a thyroid hormone-binding protein that is homologous to protein disulfide isomerase and the β-subunit of propyl-4-hydroxylase. J Biol Chem ; 263:782-785.
    • (1988) J Biol Chem , vol.263 , pp. 782-785
    • Obata, T.1    Kitagawa, S.2    Gong, Q.-H.3    Pastan, I.4    Cheng, S.-Y.5
  • 48
    • 0022539137 scopus 로고
    • Purification and characterization of a membrane-associated 3,3′,5-triiodo-L-thyronine binding protein from a human carcinoma cell line
    • Cheng S-Y, Hasumura S, Willingham M, Pastan I. 1986 Purification and characterization of a membrane-associated 3,3′,5-triiodo-L-thyronine binding protein from a human carcinoma cell line. Proc Natl Acad Sci USA; 83:947-951.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 947-951
    • Cheng, S.-Y.1    Hasumura, S.2    Willingham, M.3    Pastan, I.4
  • 49
    • 0023182842 scopus 로고
    • The nucleotide sequence of a human cellular thyroid hormone binding protein present in endoplasmic reticulum
    • Cheng S-Y, Gong Q, Parkison C, Robinson E, Appella E, Merlino G, Pastan I. 1987 The nucleotide sequence of a human cellular thyroid hormone binding protein present in endoplasmic reticulum. J Biol Chem ; 262:11221-11227.
    • (1987) J Biol Chem , vol.262 , pp. 11221-11227
    • Cheng, S.-Y.1    Gong, Q.2    Parkison, C.3    Robinson, E.4    Appella, E.5    Merlino, G.6    Pastan, I.7
  • 50
    • 0025331418 scopus 로고
    • Protein disulfide-isomerase is a substrate for thioredoxin reductase and has thioredoxin-like activity
    • Lundstrom J, Holmgren A. 1990 Protein disulfide-isomerase is a substrate for thioredoxin reductase and has thioredoxin-like activity. J Biol Chem ; 265:9114-9120.
    • (1990) J Biol Chem , vol.265 , pp. 9114-9120
    • Lundstrom, J.1    Holmgren, A.2
  • 51
    • 0026731788 scopus 로고
    • Protein disulfide isomerase. A mutifunctional protein resident in the lumen of the endoplasmic reticulum
    • Noiva R, Lennarz WJ. 1992 Protein disulfide isomerase. A mutifunctional protein resident in the lumen of the endoplasmic reticulum. J Biol Chem ; 267:3553-3556.
    • (1992) J Biol Chem , vol.267 , pp. 3553-3556
    • Noiva, R.1    Lennarz, W.J.2
  • 52
    • 0023654667 scopus 로고
    • A single polypeptide acts both as the β subunit of prolyl-4-hydroxylyase and as a protein disulfide isomerase
    • Koivu J, Myllyla R, Helaakkoski T, Pihlajaniemi T, Tasanen K, Kivirikko K. 1987 A single polypeptide acts both as the β subunit of prolyl-4-hydroxylyase and as a protein disulfide isomerase. J Biol Chem ; 262:6447-6449.
    • (1987) J Biol Chem , vol.262 , pp. 6447-6449
    • Koivu, J.1    Myllyla, R.2    Helaakkoski, T.3    Pihlajaniemi, T.4    Tasanen, K.5    Kivirikko, K.6
  • 53
    • 0024295428 scopus 로고
    • Glycosylation site binding protein, a component of oligosaccharyl transferase, is highly similar to three other 57 kDa lumenal proteins of the ER
    • Geetha-Habib M, Noiva R, Kaplan HA, Lennarz WJ. 1988 Glycosylation site binding protein, a component of oligosaccharyl transferase, is highly similar to three other 57 kDa lumenal proteins of the ER. Cell ; 54:1053-1060.
    • (1988) Cell , vol.54 , pp. 1053-1060
    • Geetha-Habib, M.1    Noiva, R.2    Kaplan, H.A.3    Lennarz, W.J.4
  • 54
    • 0028036401 scopus 로고
    • The interaction of human estrogen receptor with DNA is modulated by receptor-associated proteins
    • Landel CC, Kushner PJ, Greene GL. 1994 The interaction of human estrogen receptor with DNA is modulated by receptor-associated proteins. Mol Endocrinology ; 8:1407-1419.
    • (1994) Mol Endocrinology , vol.8 , pp. 1407-1419
    • Landel, C.C.1    Kushner, P.J.2    Greene, G.L.3
  • 55
    • 0027518745 scopus 로고
    • cDNA for R-cognin: Homology with a multifunctional protein
    • Rao ASMK, Hausman RE. 1993 cDNA for R-cognin: homology with a multifunctional protein. Proc Natl Acad Sci USA ; 90:2950-2954.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 2950-2954
    • Rao, A.S.M.K.1    Hausman, R.E.2
  • 57
    • 0023432663 scopus 로고
    • Immunohistochemical localization of a thyroid hormone-binding protein (p55) in human tissues
    • Willingham MC, Rutherford AV, Cheng S-Y. 1987 Immunohistochemical localization of a thyroid hormone-binding protein (p55) in human tissues. J Histochem Cytochem ; 35:1043-46.
    • (1987) J Histochem Cytochem , vol.35 , pp. 1043-1046
    • Willingham, M.C.1    Rutherford, A.V.2    Cheng, S.-Y.3
  • 58
    • 0024456399 scopus 로고
    • Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cells
    • Rothman JE. 1989 Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells. Cell ; 59:591-601.
    • (1989) Cell , vol.59 , pp. 591-601
    • Rothman, J.E.1
  • 59
    • 0027366385 scopus 로고
    • The hsp56 immunophilin component of steroid receptor heterocomplexes: Could this be the elusive nuclear localization signal-binding protein?
    • Pratt WB, Czar MJ, Stancato L, Owens JK. 1993 The hsp56 immunophilin component of steroid receptor heterocomplexes: could this be the elusive nuclear localization signal-binding protein? J Steroid Biochem ; 46(3):269-279.
    • (1993) J Steroid Biochem , vol.46 , Issue.3 , pp. 269-279
    • Pratt, W.B.1    Czar, M.J.2    Stancato, L.3    Owens, J.K.4
  • 60
    • 0027451956 scopus 로고
    • The role of heat shock proteins in regulating the function, folding and trafficking of the glucocorticoid receptor
    • Pratt WB. 1993 The role of heat shock proteins in regulating the function, folding and trafficking of the glucocorticoid receptor. J Biol Chem ; 268:21455-21458.
    • (1993) J Biol Chem , vol.268 , pp. 21455-21458
    • Pratt, W.B.1
  • 61
    • 0028596331 scopus 로고
    • The hsp56 immunophilin component of untransformed steroid receptor complexes is localized both to microtubules in the cytoplasm and to the same nonrandom regions within the nucleus as the steroid receptor
    • Czar MJ, Owens-Grillo JK, Yem AW, Leach KL, Deibel Jr MR, Welsh MJ, Pratt WB . 1993 The hsp56 immunophilin component of untransformed steroid receptor complexes is localized both to microtubules in the cytoplasm and to the same nonrandom regions within the nucleus as the steroid receptor. Mol Endocrinol ; 8:1731-1741.
    • (1993) Mol Endocrinol , vol.8 , pp. 1731-1741
    • Czar, M.J.1    Owens-Grillo, J.K.2    Yem, A.W.3    Leach, K.L.4    Deibel Jr., M.R.5    Welsh, M.J.6    Pratt, W.B.7
  • 62
    • 0025082330 scopus 로고
    • Mammalian thioltransferase and protein disulfide isomerase have dehydroascorbate reductase activity
    • Wells WW, Peng Xu D, Yang Y, Rocque PA. 1990 Mammalian thioltransferase and protein disulfide isomerase have dehydroascorbate reductase activity. J Biol Chem ; 265:15361-15364.
    • (1990) J Biol Chem , vol.265 , pp. 15361-15364
    • Wells, W.W.1    Peng Xu, D.2    Yang, Y.3    Rocque, P.A.4
  • 64
    • 0027203922 scopus 로고
    • The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity
    • LaMantia M, Lennarz W. 1993 The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity. Cell ; 74:899-908.
    • (1993) Cell , vol.74 , pp. 899-908
    • LaMantia, M.1    Lennarz, W.2
  • 65
    • 0027220866 scopus 로고
    • Peptide binding to protein disulfide isomerase occurs at a site distinct from the active sites
    • Noiva R, Freedman RB, Lennarz WJ. 1993 Peptide binding to protein disulfide isomerase occurs at a site distinct from the active sites. J Biol Chem ; 268:19210-19217.
    • (1993) J Biol Chem , vol.268 , pp. 19210-19217
    • Noiva, R.1    Freedman, R.B.2    Lennarz, W.J.3
  • 66
    • 0028321726 scopus 로고
    • Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme
    • Puig A, Gilbert H. 1994 Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme. J Biol Chem ; 269:7764-7771.
    • (1994) J Biol Chem , vol.269 , pp. 7764-7771
    • Puig, A.1    Gilbert, H.2
  • 67
    • 0027136018 scopus 로고
    • Protein disulfide isomerase is both an enzyme and a chaperone
    • Wang C-C, Tsou C-L. 1993 Protein disulfide isomerase is both an enzyme and a chaperone. FASEB J ; 7:1515-17.
    • (1993) FASEB J , vol.7 , pp. 1515-1517
    • Wang, C.-C.1    Tsou, C.-L.2
  • 70
    • 0021888554 scopus 로고
    • Purification and characterization of a cytosolic protein enhancing GSH-dependent microsomal iodothyronine 5′-monodeiodination
    • Goswami A, Rosenberg IN. 1985 Purification and characterization of a cytosolic protein enhancing GSH-dependent microsomal iodothyronine 5′-monodeiodination. J Biol Chem ; 260:6012-6019.
    • (1985) J Biol Chem , vol.260 , pp. 6012-6019
    • Goswami, A.1    Rosenberg, I.N.2
  • 72
    • 0019325646 scopus 로고
    • Role of cytoplasmic thioltransferase in cellular regulation by thiol-disulfide interchange
    • Mannervik B, Pitot HC. 1980 Role of cytoplasmic thioltransferase in cellular regulation by thiol-disulfide interchange. Biochem J ; 190:125-130.
    • (1980) Biochem J , vol.190 , pp. 125-130
    • Mannervik, B.1    Pitot, H.C.2
  • 74
    • 0017186047 scopus 로고
    • Effects of glutathione-oxidizing agents on microtubule assembly and microtubule-dependent surface properties of human neutrophils
    • Oliver JM, Albertinie DF, Berlin RD. 1976 Effects of glutathione-oxidizing agents on microtubule assembly and microtubule-dependent surface properties of human neutrophils. J Cell Biol ; 71:921-932.
    • (1976) J Cell Biol , vol.71 , pp. 921-932
    • Oliver, J.M.1    Albertinie, D.F.2    Berlin, R.D.3
  • 75
    • 15844365578 scopus 로고
    • Interactions of thyroid hormone and enzyme systems in vitro
    • Litwack G, Kritchevsky D, eds. NY: John Wiley & Sons
    • Litwack G. 1964 Interactions of thyroid hormone and enzyme systems in vitro. In: Litwack G, Kritchevsky D, eds. Actions of Hormones on Molecular Processes. NY: John Wiley & Sons. pp. 132-153.
    • (1964) Actions of Hormones on Molecular Processes , pp. 132-153
    • Litwack, G.1
  • 76
    • 0022597123 scopus 로고
    • Direct thyroid hormone activation of mitochondria: The role of adenine nucleotide translocase
    • Sterling K. 1986 Direct thyroid hormone activation of mitochondria: the role of adenine nucleotide translocase. Endocrinology ; 119:292-295.
    • (1986) Endocrinology , vol.119 , pp. 292-295
    • Sterling, K.1
  • 77
    • 15844386066 scopus 로고
    • The mitochondrial pathway of thyroid hormone action
    • Nagataki S, Torizuka K, eds. Elsevier Science Publishers. NY, NY
    • Sterling K. 1988 The mitochondrial pathway of thyroid hormone action. In: Nagataki S, Torizuka K, eds. The Thyroid. Elsevier Science Publishers. NY, NY pp.361-374.
    • (1988) The Thyroid , pp. 361-374
    • Sterling, K.1
  • 78
    • 0028329807 scopus 로고
    • Characterization and differentiation of peripheral-type benzodiazepine receptors in rat and human prostate
    • Camins A, Sureda FX, Pubill D, Camarasa J, Escubedo E. 1994 Characterization and differentiation of peripheral-type benzodiazepine receptors in rat and human prostate. Life Sciences ; 54:759-767.
    • (1994) Life Sciences , vol.54 , pp. 759-767
    • Camins, A.1    Sureda, F.X.2    Pubill, D.3    Camarasa, J.4    Escubedo, E.5
  • 79
    • 0026591024 scopus 로고
    • Isolation of the mitochondrial benzodiazepine receptor: Association with the voltage-dependent anion channel and the adenine nucleotide carrier
    • McEnery M, Snowman AM, Trifiletti RR, Snyder SH. 1992 Isolation of the mitochondrial benzodiazepine receptor: association with the voltage-dependent anion channel and the adenine nucleotide carrier. PNAS ; 89:3170-3174.
    • (1992) PNAS , vol.89 , pp. 3170-3174
    • McEnery, M.1    Snowman, A.M.2    Trifiletti, R.R.3    Snyder, S.H.4
  • 81
    • 0026517083 scopus 로고
    • 125I]triiodothyronine accumulation into human liver, human neuroblast, and rat pituitary cell lines
    • 125I]triiodothyronine accumulation into human liver, human neuroblast, and rat pituitary cell lines. Endocrinology ; 130:1211-1216.
    • (1992) Endocrinology , vol.130 , pp. 1211-1216
    • Kragie, L.1    Doyle, D.2
  • 82
    • 0026686102 scopus 로고
    • Requisite structural characteristics for benzodiazepine inhibition of triiodothyronine uptake into a human liver cell line
    • Kragie L. 1992 Requisite structural characteristics for benzodiazepine inhibition of triiodothyronine uptake into a human liver cell line. Life Sciences ; 51:PL83-PL88.
    • (1992) Life Sciences , vol.51
    • Kragie, L.1
  • 83
    • 0028300042 scopus 로고
    • Computer-assisted molecular modeling of benzodiazepine and thyromimetic inhibitors of the HepG2 iodothyronine transporter
    • Kragie L, Forrester ML, Cody V, McCourt M. 1994 Computer-assisted molecular modeling of benzodiazepine and thyromimetic inhibitors of the HepG2 iodothyronine transporter. Mol Endocrinol ; 8:382-391.
    • (1994) Mol Endocrinol , vol.8 , pp. 382-391
    • Kragie, L.1    Forrester, M.L.2    Cody, V.3    McCourt, M.4
  • 84
    • 0025123413 scopus 로고
    • Evidence for a close link between the thyroid hormone transport system and the aromatic amino acid transport system T in erythrocytes
    • Zhou Y, Samson M, Osty J, Francon J, Blondeau J-P. 1990 Evidence for a close link between the thyroid hormone transport system and the aromatic amino acid transport system T in erythrocytes. J Biol Chem ; 265:1700-4.
    • (1990) J Biol Chem , vol.265 , pp. 1700-1704
    • Zhou, Y.1    Samson, M.2    Osty, J.3    Francon, J.4    Blondeau, J.-P.5
  • 85
    • 0027260967 scopus 로고
    • Saturable, stereospecific transport of 3,5,3′-triiodo-L-thyronine and L-thyroxine into GH4C1 pituitary cells
    • Yan Z, Hinkle PM. 1993 Saturable, stereospecific transport of 3,5,3′-triiodo-L-thyronine and L-thyroxine into GH4C1 pituitary cells. J Biol Chem ; 268(27):20179-84.
    • (1993) J Biol Chem , vol.268 , Issue.27 , pp. 20179-20184
    • Yan, Z.1    Hinkle, P.M.2
  • 86
    • 0024467308 scopus 로고
    • Carrier-mediated transport of thyroid hormones into rat glial cells in primary culture
    • Francon J, Chantoux F, Blondeau JP. 1989 Carrier-mediated transport of thyroid hormones into rat glial cells in primary culture. J Neurochem ; 53(5):1456-63.
    • (1989) J Neurochem , vol.53 , Issue.5 , pp. 1456-1463
    • Francon, J.1    Chantoux, F.2    Blondeau, J.P.3
  • 87
    • 0025095302 scopus 로고
    • Role of amino acid transport and counter-transport in nutrition and metabolism
    • Christensen HN. 1990 Role of amino acid transport and counter-transport in nutrition and metabolism. Physiol Rev ;70:43-77.
    • (1990) Physiol Rev , vol.70 , pp. 43-77
    • Christensen, H.N.1
  • 88
    • 0027457516 scopus 로고
    • Triiodothyronine is a high-affinity inhibitor of amino acid transport system L in cultured astrocytes
    • Blondeau J-P, Beslin A, Chantoux F, Francon J. 1993 Triiodothyronine is a high-affinity inhibitor of amino acid transport system L in cultured astrocytes. J Neurochem ; 60:1407-1413.
    • (1993) J Neurochem , vol.60 , pp. 1407-1413
    • Blondeau, J.-P.1    Beslin, A.2    Chantoux, F.3    Francon, J.4
  • 89
    • 0028147406 scopus 로고
    • Relationship between thyroid hormone transport and neutral amino acid transport in JAR human choriocarcinoma cells
    • Prasad PD, Leibach FH, Mahesh VB, Ganapathy V. 1994 Relationship between thyroid hormone transport and neutral amino acid transport in JAR human choriocarcinoma cells. Endocrinology ; 134(2):574-81.
    • (1994) Endocrinology , vol.134 , Issue.2 , pp. 574-581
    • Prasad, P.D.1    Leibach, F.H.2    Mahesh, V.B.3    Ganapathy, V.4
  • 90
    • 85035170085 scopus 로고
    • Modeling the iodothyronine and amino acid transport sites in mouse neuroblastoma cells
    • Washington DC, Abstr #422
    • Kragie L, McCourt M, Lakshmanan M. Modeling the iodothyronine and amino acid transport sites in mouse neuroblastoma cells. The 77th Annual Meeting of The Endocrine Society. Washington DC, 1995. Abstr #422, p574.
    • (1995) The 77th Annual Meeting of the Endocrine Society , pp. 574
    • Kragie, L.1    McCourt, M.2    Lakshmanan, M.3
  • 91
    • 0024795243 scopus 로고
    • High affinity L-triiodothyronine binding to right-side-out and inside-out vesicles from rat and human erythrocyte membrane
    • Angel RC, Botta JA, Farias RN. 1989 High affinity L-triiodothyronine binding to right-side-out and inside-out vesicles from rat and human erythrocyte membrane. J Biol Chem ; 264(32):19143-6.
    • (1989) J Biol Chem , vol.264 , Issue.32 , pp. 19143-19146
    • Angel, R.C.1    Botta, J.A.2    Farias, R.N.3
  • 92
    • 0023156358 scopus 로고
    • Modification of L-triiodothyronine binding sites from rat erythrocyte membrane by heating and by proteinase treatments
    • Angel RC, Botta JA, Farias RN. 1987 Modification of L-triiodothyronine binding sites from rat erythrocyte membrane by heating and by proteinase treatments. Biochim Biophys Acta ; 897(3):488-94.
    • (1987) Biochim Biophys Acta , vol.897 , Issue.3 , pp. 488-494
    • Angel, R.C.1    Botta, J.A.2    Farias, R.N.3
  • 93
    • 85035164807 scopus 로고
    • Putative iodothyronine transporter membrane proteins from liver and brain as identified with antibodies and ligand affinity chromatography
    • Las Vegas, June Abstr #818
    • Kragie L, Smiehorowski R, Goonawardena D. Putative iodothyronine transporter membrane proteins from liver and brain as identified with antibodies and ligand affinity chromatography. 75th Annual Meeting of The Endocrine Society. Las Vegas, June 1993, Abstr #818.
    • (1993) 75th Annual Meeting of the Endocrine Society
    • Kragie, L.1    Smiehorowski, R.2    Goonawardena, D.3
  • 96
    • 0021926903 scopus 로고
    • Comparative characterization of thyroid hormone receptors and binding proteins in rat liver nucleus, plasma membrane, and cytosol by photoaffinity labeling with L-thyroxine
    • Dozin B, Cahnmann H, Nikodem V. 1985 Comparative characterization of thyroid hormone receptors and binding proteins in rat liver nucleus, plasma membrane, and cytosol by photoaffinity labeling with L-thyroxine. Biochemistry ; 24:5203-5208.
    • (1985) Biochemistry , vol.24 , pp. 5203-5208
    • Dozin, B.1    Cahnmann, H.2    Nikodem, V.3
  • 97
    • 0018763061 scopus 로고
    • High affinity thyroxine binding to purified rat liver plasma membranes
    • Gharby J, Torresani J. 1979 High affinity thyroxine binding to purified rat liver plasma membranes. Biochim Biophys Res Commun ; 88:170.
    • (1979) Biochim Biophys Res Commun , vol.88 , pp. 170
    • Gharby, J.1    Torresani, J.2
  • 98
    • 0019793781 scopus 로고
    • Thyroid hormone binding to plasma membrane preparations: Studies in different thyroid states and tissues
    • Gharby-Chihi J, Torresani J. 1981 Thyroid hormone binding to plasma membrane preparations: studies in different thyroid states and tissues. J Endocrinol Invest ; 4:177.
    • (1981) J Endocrinol Invest , vol.4 , pp. 177
    • Gharby-Chihi, J.1    Torresani, J.2
  • 99
    • 0022483755 scopus 로고
    • Saturable binding of thyroid hormone to isolated rat hepatocytes
    • Blondeau J-P. 1986 Saturable binding of thyroid hormone to isolated rat hepatocytes. FEBS Letters ; 204:41-46.
    • (1986) FEBS Letters , vol.204 , pp. 41-46
    • Blondeau, J.-P.1
  • 100
    • 0022844496 scopus 로고
    • Inhibition of iodothyronine transport into rat liver cells by a monoclonal antibody
    • Mol JA, Krenning EP, Docter R, Rozing J, Hennemann G. 1986 Inhibition of iodothyronine transport into rat liver cells by a monoclonal antibody. J Biol Chem ; 261:7640-7643.
    • (1986) J Biol Chem , vol.261 , pp. 7640-7643
    • Mol, J.A.1    Krenning, E.P.2    Docter, R.3    Rozing, J.4    Hennemann, G.5
  • 101
    • 0017282512 scopus 로고
    • Specific binding sites for L-triiodothyronine in rat liver and kidney cytosol
    • Visser TJ, Bernard HF, Docter R, Hennemann G. 1976 Specific binding sites for L-triiodothyronine in rat liver and kidney cytosol. Acta Endocrinologica ; 82:98-104.
    • (1976) Acta Endocrinologica , vol.82 , pp. 98-104
    • Visser, T.J.1    Bernard, H.F.2    Docter, R.3    Hennemann, G.4
  • 102
    • 0028080178 scopus 로고
    • In vitro binding of 3,5-di-iodo-L-thyronine to rat liver mitochondria
    • Goglia F, Lanni A, Horst C, Moreno M, Thoma R. 1994 In vitro binding of 3,5-di-iodo-L-thyronine to rat liver mitochondria. J Mol Endocrinol ; 13:275-282.
    • (1994) J Mol Endocrinol , vol.13 , pp. 275-282
    • Goglia, F.1    Lanni, A.2    Horst, C.3    Moreno, M.4    Thoma, R.5
  • 103
    • 0026025982 scopus 로고
    • The thyroxine-binding site of human apolipoprotein-A-1: Location in the N-terminal domain
    • Benvenga B, Cahnman H, Robbins J. 1991 The thyroxine-binding site of human apolipoprotein-A-1: location in the N-terminal domain. Endocrinology ; 128:547-552.
    • (1991) Endocrinology , vol.128 , pp. 547-552
    • Benvenga, B.1    Cahnman, H.2    Robbins, J.3
  • 104
    • 0027524990 scopus 로고
    • A naturally occurring furan fatty acid enhances drug inhibition of thyroxine binding in serum
    • Lim CF, Stockigt JR, Curtis AJ, Wynne KN, Barlow JW, Topliss DJ. 1993 A naturally occurring furan fatty acid enhances drug inhibition of thyroxine binding in serum. Metabolism ; 42(11):1468-74.
    • (1993) Metabolism , vol.42 , Issue.11 , pp. 1468-1474
    • Lim, C.F.1    Stockigt, J.R.2    Curtis, A.J.3    Wynne, K.N.4    Barlow, J.W.5    Topliss, D.J.6
  • 105
    • 0027550197 scopus 로고
    • Stimulating and inhibiting effect of individual blood serum transport proteins on thyroid hormone binding with human placental cell membrane
    • Karpyza EI, Kiklevich IE, Ermolenko MN, Sviridov OV. 1993 Stimulating and inhibiting effect of individual blood serum transport proteins on thyroid hormone binding with human placental cell membrane. Biokhimiia ; 58(2):285-94.
    • (1993) Biokhimiia , vol.58 , Issue.2 , pp. 285-294
    • Karpyza, E.I.1    Kiklevich, I.E.2    Ermolenko, M.N.3    Sviridov, O.V.4
  • 106
    • 0020119687 scopus 로고
    • High-affinity 3,5,3′-L-triiodothyronine binding to synaptosomes in rat cerebral cortex
    • Mashio Y, Inada M, Tanaka K, Nishikawa M, Takahashi K, Imura H. 1982 High-affinity 3,5,3′-L-triiodothyronine binding to synaptosomes in rat cerebral cortex. Endocrinology ; 110:1257-1261.
    • (1982) Endocrinology , vol.110 , pp. 1257-1261
    • Mashio, Y.1    Inada, M.2    Tanaka, K.3    Nishikawa, M.4    Takahashi, K.5    Imura, H.6
  • 108
    • 0025169516 scopus 로고
    • High-affinity binding of thyroid hormones to neuroblastoma plasma membranes
    • Goncalves E, Lakshmanan M, Cahnmann HJ, Robbins J. 1990 High-affinity binding of thyroid hormones to neuroblastoma plasma membranes. Biochim Biopys Acta ; 1055:151-156.
    • (1990) Biochim Biopys Acta , vol.1055 , pp. 151-156
    • Goncalves, E.1    Lakshmanan, M.2    Cahnmann, H.J.3    Robbins, J.4
  • 109
    • 0027518965 scopus 로고
    • Molecular interconversion of cold-sensitive cytosolic 3,3′,5-tri-iodo- L-thyronine-binding proteins from human erythrocytes: Effect of cold, heat and pH treatments
    • Fanjul AN, Farias RN. 1993 Molecular interconversion of cold-sensitive cytosolic 3,3′,5-tri-iodo- L-thyronine-binding proteins from human erythrocytes: effect of cold, heat and pH treatments. Biochem J :579-82.
    • (1993) Biochem J , pp. 579-582
    • Fanjul, A.N.1    Farias, R.N.2
  • 110
    • 0028136191 scopus 로고
    • Retinoids stimulate type I iodothyronine 5′-deiodinase activity in human follicular thyroid carcinoma cell lines
    • Schreck R, Schnieders F, Schmutzler C, Kohrle J. 1994 Retinoids stimulate type I iodothyronine 5′-deiodinase activity in human follicular thyroid carcinoma cell lines. J Clin Endocrinol Metab ; 79(3):791-8.
    • (1994) J Clin Endocrinol Metab , vol.79 , Issue.3 , pp. 791-798
    • Schreck, R.1    Schnieders, F.2    Schmutzler, C.3    Kohrle, J.4
  • 111
    • 0020555749 scopus 로고
    • Characterization of binding and uptake of 3,3′,5-triiodo-L-thyronine in cultured mouse fibroblasts
    • Cheng S-Y. 1983 Characterization of binding and uptake of 3,3′,5-triiodo-L-thyronine in cultured mouse fibroblasts. Endocrinology ; 112:1754-1762.
    • (1983) Endocrinology , vol.112 , pp. 1754-1762
    • Cheng, S.-Y.1
  • 112
    • 0024552154 scopus 로고
    • Antagonism of thyroid hormone action by amiodarone in rat pituitary tumor cells
    • Norman MP, Lavin TN. 1989 Antagonism of thyroid hormone action by amiodarone in rat pituitary tumor cells. J Clin Invest ; 83:306-313.
    • (1989) J Clin Invest , vol.83 , pp. 306-313
    • Norman, M.P.1    Lavin, T.N.2
  • 113
    • 0026514152 scopus 로고
    • Differential effect of a new thyromimetic on triiodothyronine transport into myoblast and hepatoma and neuroblastoma cells
    • Lakshmanan M, Goncalves E, Pontecorvi A, Robbins J. 1992 Differential effect of a new thyromimetic on triiodothyronine transport into myoblast and hepatoma and neuroblastoma cells. Biochim Biophys Acta ; 1133:213-217.
    • (1992) Biochim Biophys Acta , vol.1133 , pp. 213-217
    • Lakshmanan, M.1    Goncalves, E.2    Pontecorvi, A.3    Robbins, J.4
  • 114
    • 0025605918 scopus 로고
    • Transport of thyroid hormones by human erythrocytes: Kinetic characterization in adults and newborns
    • Osty J, Valensi P, Samsom M, Francon J, Blondeau J-P. 1990 Transport of thyroid hormones by human erythrocytes: kinetic characterization in adults and newborns. J Clin Endocrinol Metab ; 71:1589-1595.
    • (1990) J Clin Endocrinol Metab , vol.71 , pp. 1589-1595
    • Osty, J.1    Valensi, P.2    Samsom, M.3    Francon, J.4    Blondeau, J.-P.5
  • 115
    • 0023848356 scopus 로고
    • Characterization of the thyroid hormone transport system of isolated hepatocytes
    • Blondeau J-P, Osty J, Francon J. 1988 Characterization of the thyroid hormone transport system of isolated hepatocytes. J Biol Chem ; 263:2685-2692.
    • (1988) J Biol Chem , vol.263 , pp. 2685-2692
    • Blondeau, J.-P.1    Osty, J.2    Francon, J.3
  • 116
    • 0024533218 scopus 로고
    • Uptake of 3,5,3′-triiodothyronine by cultured rat hepatoma cells is inhibitable by nonbile acid cholephils, diphenylhydantoin, and nonsteroidal antiinflammatory drugs
    • Topliss DJ, Kolliniatis E, Barlow JW, Lim C-F, Stockigt JR. 1989 Uptake of 3,5,3′-triiodothyronine by cultured rat hepatoma cells is inhibitable by nonbile acid cholephils, diphenylhydantoin, and nonsteroidal antiinflammatory drugs. Endocrinology; 124:980-987.
    • (1989) Endocrinology , vol.124 , pp. 980-987
    • Topliss, D.J.1    Kolliniatis, E.2    Barlow, J.W.3    Lim, C.-F.4    Stockigt, J.R.5
  • 117
    • 0024498675 scopus 로고
    • Phloretin inhibits cellular uptake and nuclear receptor binding of triiodothyronine in human HepG2 hepatocarcinoma cells
    • Movius EG, Phyillaier MM, Robbins J. 1989 Phloretin inhibits cellular uptake and nuclear receptor binding of triiodothyronine in human HepG2 hepatocarcinoma cells. Endocrinology ; 124:1988-1997.
    • (1989) Endocrinology , vol.124 , pp. 1988-1997
    • Movius, E.G.1    Phyillaier, M.M.2    Robbins, J.3
  • 118
    • 0023865047 scopus 로고
    • 5,5′-diphenylhydantoin decreases the entry of 3,5,3′-triiodo-L-thyronine but not L-thyroxine in cultured GH-producing cells
    • Zemel LR, Biezunski DR, Shapiro LE, Surks MI. 1988 5,5′-diphenylhydantoin decreases the entry of 3,5,3′-triiodo-L-thyronine but not L-thyroxine in cultured GH-producing cells. Acta Endocrinologica ; 117:392-398.
    • (1988) Acta Endocrinologica , vol.117 , pp. 392-398
    • Zemel, L.R.1    Biezunski, D.R.2    Shapiro, L.E.3    Surks, M.I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.