메뉴 건너뛰기




Volumn 256, Issue 2, 1998, Pages 287-296

Structural characteristics of bullfrog (Rana catesbeiana) transthyretin and its cDNA. Comparison of its pattern of expression during metamorphosis with that of lipocalin

Author keywords

Bullfrog (Rana catesbeiana); Lipocalin; Metamorphosis; Transthyretin

Indexed keywords

COMPLEMENTARY DNA; LIPOCALIN; MESSENGER RNA; PREALBUMIN;

EID: 0031671848     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2560287.x     Document Type: Article
Times cited : (43)

References (66)
  • 1
    • 0001044657 scopus 로고
    • Hormonal control of amphibian metamorphosis
    • (Gilbert, L. I. & Frieden, E., eds) 2nd edn. Plenum Press, New York
    • White, B. A. & Nicoll, C. S. (1981) Hormonal control of amphibian metamorphosis, in Metamorphosis (Gilbert, L. I. & Frieden, E., eds) 2nd edn. pp. 363-396, Plenum Press, New York.
    • (1981) Metamorphosis , pp. 363-396
    • White, B.A.1    Nicoll, C.S.2
  • 2
    • 0002564224 scopus 로고
    • Thyroid feedback to the hypothalamic neurosecretory system in frog larvae
    • Etkin, W., Kikuyama, S. & Rosenbluth, J. (1965) Thyroid feedback to the hypothalamic neurosecretory system in frog larvae, Neuroendocrinology 1, 45-64.
    • (1965) Neuroendocrinology , vol.1 , pp. 45-64
    • Etkin, W.1    Kikuyama, S.2    Rosenbluth, J.3
  • 3
    • 0018183357 scopus 로고
    • Plasma thyroxine and triiodothyronine levels in spontaneously metamorphosing Rana catesbeiana tadpoles and in adult anuran amphibia
    • Regard, E., Taurog, A. & Nakashima, T. (1978) Plasma thyroxine and triiodothyronine levels in spontaneously metamorphosing Rana catesbeiana tadpoles and in adult anuran amphibia, Endocrinology 102, 674-684.
    • (1978) Endocrinology , vol.102 , pp. 674-684
    • Regard, E.1    Taurog, A.2    Nakashima, T.3
  • 4
    • 0019610886 scopus 로고
    • Changes in thyroidal and plasma iodine compounds during and after metamorphosis of the bullfrog
    • Suzuki, S. & Suzuki, M. (1981) Changes in thyroidal and plasma iodine compounds during and after metamorphosis of the bullfrog, Rana catesbeiana, Gen. Comp. Endocrinol. 45, 74-81.
    • (1981) Rana Catesbeiana, Gen. Comp. Endocrinol. , vol.45 , pp. 74-81
    • Suzuki, S.1    Suzuki, M.2
  • 5
    • 0025260037 scopus 로고
    • A correlation of thyroid hormone receptor gene expression with amphibian metamorphosis
    • Yaoita, Y. & Brown, D. D. (1990) A correlation of thyroid hormone receptor gene expression with amphibian metamorphosis, Genes Der. 4, 1917-1924.
    • (1990) Genes Der. , vol.4 , pp. 1917-1924
    • Yaoita, Y.1    Brown, D.D.2
  • 6
    • 0025895973 scopus 로고
    • Developmental and regional expression of thyroid hormone receptor genes during Xenopus metamorphosis
    • Kawahara, A., Baker, B. S. & Tata, J. R. (1991) Developmental and regional expression of thyroid hormone receptor genes during Xenopus metamorphosis, Development 112, 933-943.
    • (1991) Development , vol.112 , pp. 933-943
    • Kawahara, A.1    Baker, B.S.2    Tata, J.R.3
  • 7
    • 0026709440 scopus 로고
    • Autoinduction of thyroid hormone receptor during metamorphosis is reproduced in Xenopus XTC-2 cells
    • Machuca, I. & Tata, J. R. (1992) Autoinduction of thyroid hormone receptor during metamorphosis is reproduced in Xenopus XTC-2 cells, Mol. Cell. Endocrinol. 87, 105-113.
    • (1992) Mol. Cell. Endocrinol. , vol.87 , pp. 105-113
    • Machuca, I.1    Tata, J.R.2
  • 8
    • 0027193739 scopus 로고
    • Cultured cells as a model for amphibian metamorphosis
    • Kanamori, A. & Brown D. D. (1993) Cultured cells as a model for amphibian metamorphosis, Proc. Natl Acad. Sci. USA 90, 6013-6017.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6013-6017
    • Kanamori, A.1    Brown, D.D.2
  • 9
    • 0002457501 scopus 로고    scopus 로고
    • Hormonal interplay and thyroid hormone receptor expression during amphibian metamorphosis
    • (Gilbert, L. I., Tata, J. R. & Atkinson, B. G., eds) 3rd edn, Academic Press, San Diego
    • Tata, J. R. (1996) Hormonal interplay and thyroid hormone receptor expression during amphibian metamorphosis, in Metamorphosis (Gilbert, L. I., Tata, J. R. & Atkinson, B. G., eds) 3rd edn, pp. 465-503, Academic Press, San Diego.
    • (1996) Metamorphosis , pp. 465-503
    • Tata, J.R.1
  • 10
    • 0002457502 scopus 로고    scopus 로고
    • Thyroid hormone-regulated early and late genes during amphibian metamorphosis
    • (Gilbert, L. I., Tata, J. R. & Atkinson, B. G., eds) 3rd edn, Academic Press, San Diego
    • Shi, Y. B. (1996) Thyroid hormone-regulated early and late genes during amphibian metamorphosis, in Metamorphosis (Gilbert, L. I., Tata, J. R. & Atkinson, B. G., eds) 3rd edn, pp. 505-538, Academic Press, San Diego.
    • (1996) Metamorphosis , pp. 505-538
    • Shi, Y.B.1
  • 11
    • 0013623326 scopus 로고    scopus 로고
    • Reprogramming of genes expressed in amphibian liver during metamorphosis
    • (Gilbert, L. I., Tata, J. R. & Atkinson, B. G., eds) 3rd edn, Academic Press, San Diego
    • Atkinson, B. G., Helbing, C. & Chen, T. Q. (1996) Reprogramming of genes expressed in amphibian liver during metamorphosis, in Metamorphosis (Gilbert, L. I., Tata, J. R. & Atkinson, B. G., eds) 3rd edn, pp. 539-566, Academic Press, San Diego.
    • (1996) Metamorphosis , pp. 539-566
    • Atkinson, B.G.1    Helbing, C.2    Chen, T.Q.3
  • 12
    • 0017751496 scopus 로고
    • Studies on thyroid hormones and their binding in bullfrog tadpole plasma during metamorphosis
    • Miyauchi, H., LaRochelle, F. T., Suzuki, M., Freeman, M. & Frieden, E. (1977) Studies on thyroid hormones and their binding in bullfrog tadpole plasma during metamorphosis, Gen. Comp. Endocrinol. 33, 254-266.
    • (1977) Gen. Comp. Endocrinol. , vol.33 , pp. 254-266
    • Miyauchi, H.1    LaRochelle, F.T.2    Suzuki, M.3    Freeman, M.4    Frieden, E.5
  • 13
    • 0027210340 scopus 로고
    • Purification and characterization of a 3,5,3′-L-triiodothyronine-specific binding protein from bullfrog tadpole plasma: A homolog of mammalian transthyretin
    • Yamauchi, K., Kasahara, T., Hayashi, H. & Horiuchi, R. (1993) Purification and characterization of a 3,5,3′-L-triiodothyronine-specific binding protein from bullfrog tadpole plasma: a homolog of mammalian transthyretin, Endocrinology 132, 2254-2261.
    • (1993) Endocrinology , vol.132 , pp. 2254-2261
    • Yamauchi, K.1    Kasahara, T.2    Hayashi, H.3    Horiuchi, R.4
  • 14
    • 0025735197 scopus 로고
    • Transthyretin (prealbumin) gene expression in choroid plexus is strongly conserved during evolution of vertebrates
    • Harms, P. J., Tu, G.-F., Richardson, S. J., Aldred, A. R., Jaworowski, A. & Schreiber, G. (1991) Transthyretin (prealbumin) gene expression in choroid plexus is strongly conserved during evolution of vertebrates, Comp. Biochem. Physiol. 99B, 239-249.
    • (1991) Comp. Biochem. Physiol. , vol.99 B , pp. 239-249
    • Harms, P.J.1    Tu, G.-F.2    Richardson, S.J.3    Aldred, A.R.4    Jaworowski, A.5    Schreiber, G.6
  • 18
    • 0026475385 scopus 로고
    • Protein synthesis at the blood-brain barrier: The major protein secreted by amphibian choroid plexux is a lipocalin
    • Achen, M. G., Harms, P. J., Thomas, T., Richardson, S. J., Wettenhall, R. E. H. & Schreiber, G. (1992) Protein synthesis at the blood-brain barrier: the major protein secreted by amphibian choroid plexux is a lipocalin, J. Biol. Chem. 267, 23 170-23 174.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23170-23174
    • Achen, M.G.1    Harms, P.J.2    Thomas, T.3    Richardson, S.J.4    Wettenhall, R.E.H.5    Schreiber, G.6
  • 19
    • 0030945339 scopus 로고    scopus 로고
    • The evolution of gene expression, structure and function of transthyretin
    • Schreiber, G. & Richardson, S. J. (1997) The evolution of gene expression, structure and function of transthyretin, Comp. Biochem. Physiol. 116B, 137-160.
    • (1997) Comp. Biochem. Physiol. , vol.116 B , pp. 137-160
    • Schreiber, G.1    Richardson, S.J.2
  • 20
    • 0024513250 scopus 로고
    • The mRNA encoding elongation facyor 1-α (EF-1α) is a major transcript at the midblastula transition in Xenopus
    • Krieg, P. A., Varnum, S. M., Wormington, W. M. & Melton, D. A. (1989) The mRNA encoding elongation facyor 1-α (EF-1α) is a major transcript at the midblastula transition in Xenopus, Dev. Biol. 133, 93-100.
    • (1989) Dev. Biol. , vol.133 , pp. 93-100
    • Krieg, P.A.1    Varnum, S.M.2    Wormington, W.M.3    Melton, D.A.4
  • 21
    • 33847025596 scopus 로고
    • Stages in the normal development of Rana pipiens
    • Taylor, A. C. & Kollros, J. J. (1946) Stages in the normal development of Rana pipiens, Anat. Rec. 94, 7-23.
    • (1946) Anat. Rec. , vol.94 , pp. 7-23
    • Taylor, A.C.1    Kollros, J.J.2
  • 22
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P. & Sacchi, N. (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction, Anal. Biochem. 162, 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 23
    • 0015356037 scopus 로고
    • Purification of biologically active globin messenger RNA by chromatography on oligothymidylic acid-cellulose
    • Aviv, H. & Leder, P. (1972) Purification of biologically active globin messenger RNA by chromatography on oligothymidylic acid-cellulose, Proc. Natl Acad. Sci. USA 69, 1408-1412.
    • (1972) Proc. Natl Acad. Sci. USA , vol.69 , pp. 1408-1412
    • Aviv, H.1    Leder, P.2
  • 24
    • 0028928861 scopus 로고
    • Cloning of cDNA encoding argininosuccinate lyase and arginase from Rana catesbeiana liver and regulation of their mRNAs during spontaneous and thyroid hormone-induced metamorphosis
    • Iwase, K., Yamauchi, K. & Ishikawa, K. (1995) Cloning of cDNA encoding argininosuccinate lyase and arginase from Rana catesbeiana liver and regulation of their mRNAs during spontaneous and thyroid hormone-induced metamorphosis. Biochim. Biophys. Acta 1260, 139-146.
    • (1995) Biochim. Biophys. Acta , vol.1260 , pp. 139-146
    • Iwase, K.1    Yamauchi, K.2    Ishikawa, K.3
  • 27
    • 0031893395 scopus 로고    scopus 로고
    • Metamorphosis-associated and region-specific expression of calbindin gene in the posterior intestinal epithelium of Xenopus laevis larva
    • Amano, T., Noro, N., Kawabata, H., Kobayashi, Y. & Yoshizato, K. (1998) Metamorphosis-associated and region-specific expression of calbindin gene in the posterior intestinal epithelium of Xenopus laevis larva, Dev. Growth. Differ. 40, 177-188.
    • (1998) Dev. Growth. Differ. , vol.40 , pp. 177-188
    • Amano, T.1    Noro, N.2    Kawabata, H.3    Kobayashi, Y.4    Yoshizato, K.5
  • 28
    • 0030977515 scopus 로고    scopus 로고
    • Evolution of shorter and more hydrophilic transthyretin N-termini by stepwise conversion of exon 2 into intron 1 sequences (shifting the 3′ splice site of intron 1)
    • Aldred, A. R., Prapunpoj, P. & Schreiber, G. (1997) Evolution of shorter and more hydrophilic transthyretin N-termini by stepwise conversion of exon 2 into intron 1 sequences (shifting the 3′ splice site of intron 1), Eur. J. Biochem. 246, 401-409.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 401-409
    • Aldred, A.R.1    Prapunpoj, P.2    Schreiber, G.3
  • 30
    • 0027476367 scopus 로고
    • The X-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30-Met variant to 1.7-Å resolution
    • Hamilton, J. A., Steinrauf, L. K., Braden, B. C., Liepnieks, J., Benson, M. D., Holmgren, G., Sandgren, O. & Steen, L. (1993) The X-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30-Met variant to 1.7-Å resolution, J. Biol. Chem. 268, 2416-2424.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2416-2424
    • Hamilton, J.A.1    Steinrauf, L.K.2    Braden, B.C.3    Liepnieks, J.4    Benson, M.D.5    Holmgren, G.6    Sandgren, O.7    Steen, L.8
  • 31
    • 0017824077 scopus 로고
    • Structure of prealbumin secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 Å
    • Blake, C. C. F., Geisow, M. J. & Oatley, S. J. (1978) Structure of prealbumin secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 Å, J. Mol. Biol. 121, 339-356.
    • (1978) J. Mol. Biol. , vol.121 , pp. 339-356
    • Blake, C.C.F.1    Geisow, M.J.2    Oatley, S.J.3
  • 33
    • 0023155210 scopus 로고
    • Tertiary templates for proteins: Use of packing criteria in the enumeration of allowed sequences for different structural classes
    • Ponder, J. W. & Richards, F. M. (1987) Tertiary templates for proteins: use of packing criteria in the enumeration of allowed sequences for different structural classes, J. Mol. Biol. 193, 775-791.
    • (1987) J. Mol. Biol. , vol.193 , pp. 775-791
    • Ponder, J.W.1    Richards, F.M.2
  • 34
    • 0030039296 scopus 로고    scopus 로고
    • Promotif-A program to identify and analyze structural motifs in proteins
    • Hutchinson, E. G. & Thornton, J. M. (1996) Promotif-A program to identify and analyze structural motifs in proteins, Protein Sci. 5, 212-220.
    • (1996) Protein Sci. , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 35
    • 0021770224 scopus 로고
    • Compilation and analysis of sequences upstream from the translational start site in eukaryotic mRNAs
    • Kozak, M. (1984) Compilation and analysis of sequences upstream from the translational start site in eukaryotic mRNAs, Nucleic Acids Res. 12, 857-872.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 857-872
    • Kozak, M.1
  • 36
    • 0022366770 scopus 로고
    • Transcription termination and 3′ processing: The end is in site!
    • Bimstiel, M. L., Busslinger, M. & Strub, K. (1985) Transcription termination and 3′ processing: the end is in site! Cell 41, 349-359.
    • (1985) Cell , vol.41 , pp. 349-359
    • Bimstiel, M.L.1    Busslinger, M.2    Strub, K.3
  • 37
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • von Heijne, G. (1986) A new method for predicting signal sequence cleavage sites, Nucleic Acids Res. 14, 4683-4690.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 4683-4690
    • Von Heijne, G.1
  • 38
    • 0016238506 scopus 로고
    • The amino acid sequence of human plasma prealbumin
    • Kanda, Y., Goodman, D., Canfield, R. E. & Morgan, F. J. (1974) The amino acid sequence of human plasma prealbumin, J. Biol. Chem. 249, 6796-6805.
    • (1974) J. Biol. Chem. , vol.249 , pp. 6796-6805
    • Kanda, Y.1    Goodman, D.2    Canfield, R.E.3    Morgan, F.J.4
  • 40
    • 0024382449 scopus 로고
    • The nucleotide sequence of transthyretin cDNA isolated from a sheep choroid plexus cDNA library
    • Tu, G.-F., Cole, T., Duan, W. & Schreiber, G. (1989) The nucleotide sequence of transthyretin cDNA isolated from a sheep choroid plexus cDNA library, Nucleic Acids. Res. 17, 6384.
    • (1989) Nucleic Acids. Res. , vol.17 , pp. 6384
    • Tu, G.-F.1    Cole, T.2    Duan, W.3    Schreiber, G.4
  • 41
    • 0021996005 scopus 로고
    • Rat transthyretin (prealbumin): Molecular cloning, nucleotide sequence, and gene expression in liver and brain
    • Dickson, P. W., Howlett, G. J. & Schreiber, G. (1985) Rat transthyretin (prealbumin): molecular cloning, nucleotide sequence, and gene expression in liver and brain, J. Biol. Chem. 260, 8214-8219.
    • (1985) J. Biol. Chem. , vol.260 , pp. 8214-8219
    • Dickson, P.W.1    Howlett, G.J.2    Schreiber, G.3
  • 43
    • 0025896250 scopus 로고
    • Isolation, characterization, cDNA cloning and gene expression of an avian transthyretin: Implications for the evolution of structure and function of transthyretin in vertebrates
    • Duan, W., Achen, M. G., Richardson, S. J., Lawrence, M. C., Wettenhall, R. E. H., Jaworowski, A. & Schreiber, G. (1991) Isolation, characterization, cDNA cloning and gene expression of an avian transthyretin: implications for the evolution of structure and function of transthyretin in vertebrates, Eur. J. Biochem. 200, 679-687.
    • (1991) Eur. J. Biochem. , vol.200 , pp. 679-687
    • Duan, W.1    Achen, M.G.2    Richardson, S.J.3    Lawrence, M.C.4    Wettenhall, R.E.H.5    Jaworowski, A.6    Schreiber, G.7
  • 45
    • 0021821048 scopus 로고
    • The primary structure of rabbit and rat prealbumin and a comparison with the tertiary structure of human prealbumin
    • Sundelin, J., Melhus, H., Das, S., Eriksson, U., Link, P., Trågardh, L., Peterson, P. A. & Rask, L. (1985) The primary structure of rabbit and rat prealbumin and a comparison with the tertiary structure of human prealbumin, J. Biol. Chem. 260, 6481-6487.
    • (1985) J. Biol. Chem. , vol.260 , pp. 6481-6487
    • Sundelin, J.1    Melhus, H.2    Das, S.3    Eriksson, U.4    Link, P.5    Trågardh, L.6    Peterson, P.A.7    Rask, L.8
  • 48
    • 0029062667 scopus 로고
    • Structure of a complex of two plasm proteins: Transthyretin and retinol-binding protein
    • Monaco, H. L., Rizzi, M. & Coda, A. (1995) Structure of a complex of two plasm proteins: transthyretin and retinol-binding protein, Science 268, 1039-1041.
    • (1995) Science , vol.268 , pp. 1039-1041
    • Monaco, H.L.1    Rizzi, M.2    Coda, A.3
  • 50
    • 1842589542 scopus 로고    scopus 로고
    • The 'edge-strand' hypothesis: Prediction and test of a mutational 'hot-spot' on the transthyretin molecule associated with FAP amyloidogenesis
    • Serpell, L. C., Goldsteins, G., Dacklin, I., Lundgren, E. & Blake, C. C. F. (1996) The 'edge-strand' hypothesis: prediction and test of a mutational 'hot-spot' on the transthyretin molecule associated with FAP amyloidogenesis, Amyloid, Int. J. Exp. Clin. Invest. 3, 75-85.
    • (1996) Amyloid, Int. J. Exp. Clin. Invest. , vol.3 , pp. 75-85
    • Serpell, L.C.1    Goldsteins, G.2    Dacklin, I.3    Lundgren, E.4    Blake, C.C.F.5
  • 51
    • 0027204024 scopus 로고
    • Helix stop signals in proteins and peptides: The capping box
    • Harper, E. T. & Rose, G. D. (1993) Helix stop signals in proteins and peptides: the capping box, Biochemistry 32, 7605-7609.
    • (1993) Biochemistry , vol.32 , pp. 7605-7609
    • Harper, E.T.1    Rose, G.D.2
  • 53
    • 0029020484 scopus 로고
    • N- and C-capping preferences for 20 amino acids in α-helical peptides
    • Doig, A. J. & Baldwin, R. L. (1995) N- and C-capping preferences for 20 amino acids in α-helical peptides. Protein Sci. 4, 1325-1336.
    • (1995) Protein Sci. , vol.4 , pp. 1325-1336
    • Doig, A.J.1    Baldwin, R.L.2
  • 54
    • 0013672147 scopus 로고
    • Thyroid hormone transport proteins: Their nature, biosynthesis, and metabolism
    • (Braverman, L. E. & Utiger, R. D., eds) 6th edn, Lippincott, Philadelphia
    • Robbins, J. & Edelhoch, H. (1991) Thyroid hormone transport proteins: their nature, biosynthesis, and metabolism, in Werner's the thyroid (Braverman, L. E. & Utiger, R. D., eds) 6th edn, pp. 116-127, Lippincott, Philadelphia.
    • (1991) Werner's the Thyroid , pp. 116-127
    • Robbins, J.1    Edelhoch, H.2
  • 55
    • 0002699669 scopus 로고
    • Multiple modes of binding of thyroid hormones and other iodothyronines to human plasma transthyretin
    • (Beddell, C. R., ed.) Wiley, Brisbane
    • De La Paz, P., Burridge, J. M., Oatley, S. J. & Blake, C. C. F. (1992) Multiple modes of binding of thyroid hormones and other iodothyronines to human plasma transthyretin, in The design of drugs to macromolecular targets (Beddell, C. R., ed.) pp. 119-172, Wiley, Brisbane.
    • (1992) The Design of Drugs to Macromolecular Targets , pp. 119-172
    • De La Paz, P.1    Burridge, J.M.2    Oatley, S.J.3    Blake, C.C.F.4
  • 56
    • 0026584392 scopus 로고
    • Mechanisms of molecular recognition: Structural aspects of 3,3′-diiodo-L-thyronine binding to human serum transthyretin
    • Wojtczak, A., Luft, J. & Cody, V. (1992) Mechanisms of molecular recognition: structural aspects of 3,3′-diiodo-L-thyronine binding to human serum transthyretin, J. Biol. Chem. 267, 353-357.
    • (1992) J. Biol. Chem. , vol.267 , pp. 353-357
    • Wojtczak, A.1    Luft, J.2    Cody, V.3
  • 57
    • 0030484635 scopus 로고    scopus 로고
    • Structures of human transthyretin complexed with thyroxine at 2.0 Å and 3′,5′-dinitro-N-acetyl-L-thyronine at 2.2 Å resolution
    • Wojtczak, A., Cody, V., Luft, J. & Pangburn, W. (1996) Structures of human transthyretin complexed with thyroxine at 2.0 Å and 3′,5′-dinitro-N-acetyl-L-thyronine at 2.2 Å resolution, Acta Crystallogr. Sect. D Biol. Crystallogr. 52, 758-765.
    • (1996) Acta Crystallogr. Sect. D Biol. Crystallogr. , vol.52 , pp. 758-765
    • Wojtczak, A.1    Cody, V.2    Luft, J.3    Pangburn, W.4
  • 59
    • 0342412870 scopus 로고
    • Two transthyretin mutations associated with euthyroid hyperthyroxinemia
    • Izumoto, S., Kornberg, J. & Herbert, J. (1993) Two transthyretin mutations associated with euthyroid hyperthyroxinemia, J. Rheumatol. 20, 186.
    • (1993) J. Rheumatol. , vol.20 , pp. 186
    • Izumoto, S.1    Kornberg, J.2    Herbert, J.3
  • 60
    • 0027459456 scopus 로고
    • X-ray crystal structure of the Ala-109-Thr variant of human transthyretin which produces euthyroid hyperthyroxinemia
    • Steinrauf, L. K., Hamilton, J. A., Braden, B. C., Murrell, J. R. & Benson, M. D. (1993) X-ray crystal structure of the Ala-109-Thr variant of human transthyretin which produces euthyroid hyperthyroxinemia, J. Biol. Chem. 268, 2425-2430.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2425-2430
    • Steinrauf, L.K.1    Hamilton, J.A.2    Braden, B.C.3    Murrell, J.R.4    Benson, M.D.5
  • 62
    • 0023811701 scopus 로고
    • The expression of transthyretin mRNA in the developing rat brain
    • Thomas, T., Power, B., Hudson, P., Schreiber, G. & Dziadek, M. (1988) The expression of transthyretin mRNA in the developing rat brain, Dev. Biol. 128, 415-427.
    • (1988) Dev. Biol. , vol.128 , pp. 415-427
    • Thomas, T.1    Power, B.2    Hudson, P.3    Schreiber, G.4    Dziadek, M.5
  • 63
    • 0025992065 scopus 로고
    • Ontogenesis of transthyretin gene expression in chicken choroid plexus and liver, Comp
    • Southwell, B. R., Duan, W., Tu, G.-F. & Schreiber, G. (1991) Ontogenesis of transthyretin gene expression in chicken choroid plexus and liver, Comp. Biochem. Physiol. 100B, 329-338.
    • (1991) Biochem. Physiol. , vol.100 B , pp. 329-338
    • Southwell, B.R.1    Duan, W.2    Tu, G.-F.3    Schreiber, G.4
  • 64
    • 0025125103 scopus 로고
    • Expression of the genes for transthyretin, cystatin C and beta-A4 amyloid precursor protein in sheep choroid plexus during development
    • Tu, G.-F., Cole, T., Southwell, B. R. & Schreiber, G. (1990) Expression of the genes for transthyretin, cystatin C and beta-A4 amyloid precursor protein in sheep choroid plexus during development, Dev. Brain Res. 55, 203-208.
    • (1990) Dev. Brain Res. , vol.55 , pp. 203-208
    • Tu, G.-F.1    Cole, T.2    Southwell, B.R.3    Schreiber, G.4
  • 65
    • 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
  • 66
    • 0027946187 scopus 로고
    • An in vivo study of the effect of 5-HT and sympathetic nerves on transferrin and transthyretin mRNA expression in rat choroid plexus and meninges
    • Blay, P., Nilsson, C., Hansson, S., Owman, C., Aldred, A. R. & Schreiber, G. (1994) An in vivo study of the effect of 5-HT and sympathetic nerves on transferrin and transthyretin mRNA expression in rat choroid plexus and meninges, Brain Res. 662, 148-154.
    • (1994) Brain Res. , vol.662 , pp. 148-154
    • Blay, P.1    Nilsson, C.2    Hansson, S.3    Owman, C.4    Aldred, A.R.5    Schreiber, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.