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Volumn 16, Issue 1, 2005, Pages 41-49

Identification and characterization of novel variants of the thioredoxin reductase 3 new transcript 1 TXNRD3NT1

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BETA TUBULIN; COMPLEMENTARY DNA; MESSENGER RNA; NUCLEOTIDE; PRIMER DNA; THIOREDOXIN REDUCTASE; THIOREDOXIN REDUCTASE 3; THYMOCYTE ANTIBODY; UNCLASSIFIED DRUG;

EID: 13244273549     PISSN: 09388990     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00335-004-2416-y     Document Type: Article
Times cited : (7)

References (36)
  • 2
    • 0025887817 scopus 로고
    • In vitro DNA binding activity of Fos/Jun and BZLF1 but not C/EBP is affected by redox changes
    • Bannister AJ, Cook A, Kouzarides T (1991) In vitro DNA binding activity of Fos/Jun and BZLF1 but not C/EBP is affected by redox changes. Oncogene 6(7), 1243-1250
    • (1991) Oncogene , vol.6 , Issue.7 , pp. 1243-1250
    • Bannister, A.J.1    Cook, A.2    Kouzarides, T.3
  • 3
    • 0028152513 scopus 로고
    • Thioredoxin increases the proliferation of human B-cell lines through a protein kinase C-dependent mechanism
    • Biguet C, Wakasugi N, Mishal Z, Holmgren A, Chouaib S, et al. (1994) Thioredoxin increases the proliferation of human B-cell lines through a protein kinase C-dependent mechanism. J Biol Chem 269(46), 28865-28870
    • (1994) J Biol Chem , vol.269 , Issue.46 , pp. 28865-28870
    • Biguet, C.1    Wakasugi, N.2    Mishal, Z.3    Holmgren, A.4    Chouaib, S.5
  • 4
    • 0141887515 scopus 로고    scopus 로고
    • The expression of vitamin D-upregulated protein 1 in skin and its interaction with sciellin in cultured keratinocytes
    • Champliaud MF, Viel A, Baden HP (2003) The expression of vitamin D-upregulated protein 1 in skin and its interaction with sciellin in cultured keratinocytes. J Invest Dermatol 121(4), 781-785
    • (2003) J Invest Dermatol , vol.121 , Issue.4 , pp. 781-785
    • Champliaud, M.F.1    Viel, A.2    Baden, H.P.3
  • 5
    • 0024421652 scopus 로고
    • Human transcription factor IIIC (TFIIIC). Purification, polypeptide structure, and the involvement of thiol groups in specific DNA binding
    • Cromlish JA, Roeder RG (1989) Human transcription factor IIIC (TFIIIC). Purification, polypeptide structure, and the involvement of thiol groups in specific DNA binding. J Biol Chem 264(30), 18100-18109
    • (1989) J Biol Chem , vol.264 , Issue.30 , pp. 18100-18109
    • Cromlish, J.A.1    Roeder, R.G.2
  • 6
    • 0035451223 scopus 로고    scopus 로고
    • Induction of thioredoxin by ultraviolet-A radiation prevents oxidative-mediated cell death in human fibroblasts
    • Didier C, Kerblat I, Drouet C, Favier A, Beani J-C, et al. (2001) Induction of thioredoxin by ultraviolet-A radiation prevents oxidative-mediated cell death in human fibroblasts. Free Rad Biol Med 31, 585-598
    • (2001) Free Rad Biol Med , vol.31 , pp. 585-598
    • Didier, C.1    Kerblat, I.2    Drouet, C.3    Favier, A.4    Beani, J.-C.5
  • 7
    • 0032727075 scopus 로고    scopus 로고
    • Psoriasis susceptibility locus in chromosome region 3q21 identified in patients from southwest Sweden
    • Enlund F, Samuelsson L, Enerback C, Inerot A, Wahlstrom J, et al. (1999) Psoriasis susceptibility locus in chromosome region 3q21 identified in patients from southwest Sweden. Eur J Hum Genet 7, 783-790
    • (1999) Eur J Hum Genet , vol.7 , pp. 783-790
    • Enlund, F.1    Samuelsson, L.2    Enerback, C.3    Inerot, A.4    Wahlstrom, J.5
  • 9
    • 0029142578 scopus 로고
    • Cloning and sequencing of a human thioredoxin reductase
    • Gasdaska PY, Gasdaska JR, Cochran S, Powis G (1995) Cloning and sequencing of a human thioredoxin reductase. FEES Lett 373(1), 5-9
    • (1995) FEES Lett , vol.373 , Issue.1 , pp. 5-9
    • Gasdaska, P.Y.1    Gasdaska, J.R.2    Cochran, S.3    Powis, G.4
  • 10
    • 0030838711 scopus 로고    scopus 로고
    • Functional modulation of estrogen receptor by redox state with reference to thioredoxin as a mediator
    • Hayashi S, Hajiro-Nakanishi K, Makino Y, Eguchi H, Yodoi J, et al. (1997) Functional modulation of estrogen receptor by redox state with reference to thioredoxin as a mediator. Nucleic Acids Res 25(20), 4035-4040
    • (1997) Nucleic Acids Res , vol.25 , Issue.20 , pp. 4035-4040
    • Hayashi, S.1    Hajiro-Nakanishi, K.2    Makino, Y.3    Eguchi, H.4    Yodoi, J.5
  • 11
    • 0031668171 scopus 로고    scopus 로고
    • Genetics of psoriasis
    • Henseler T (1998) Genetics of psoriasis. Arch Dermatol Res 290, 4463-4476
    • (1998) Arch Dermatol Res , vol.290 , pp. 4463-4476
    • Henseler, T.1
  • 12
    • 18344392840 scopus 로고    scopus 로고
    • Identification of a psoriasis susceptibility candidate gene by linkage disequilibrium mapping with a localized single nucleotide polymorphism map
    • Hewett D, Samuelsson L, Folding J, Enlund F, Smart D, et al. (2002) Identification of a psoriasis susceptibility candidate gene by linkage disequilibrium mapping with a localized single nucleotide polymorphism map. Genomics 79(3), 305-314
    • (2002) Genomics , vol.79 , Issue.3 , pp. 305-314
    • Hewett, D.1    Samuelsson, L.2    Folding, J.3    Enlund, F.4    Smart, D.5
  • 13
    • 0030936568 scopus 로고    scopus 로고
    • AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1
    • Hirota K, Matsui M, Iwata S, Nishiyama A, Mori K, et al. (1997) AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1. Proc Natl Acad Sci USA 94(8), 3633-3638
    • (1997) Proc Natl Acad Sci USA , vol.94 , Issue.8 , pp. 3633-3638
    • Hirota, K.1    Matsui, M.2    Iwata, S.3    Nishiyama, A.4    Mori, K.5
  • 14
    • 0036290861 scopus 로고    scopus 로고
    • Thioredoxin superfamily and thioredoxin-inducing agents
    • Hirota K, Nakamura H, Masutani H, Yodoi J (2002) Thioredoxin superfamily and thioredoxin-inducing agents. Ann NY Acad Sci 957, 189-199
    • (2002) Ann NY Acad Sci , vol.957 , pp. 189-199
    • Hirota, K.1    Nakamura, H.2    Masutani, H.3    Yodoi, J.4
  • 16
    • 0034658976 scopus 로고    scopus 로고
    • Vitamin D3 up-regulated protein 1 mediates oxidative stress via suppressing the thioredoxin function
    • Junn E, Ran SH, Im JY, Yang Y, Cho EW, et al. (2000) Vitamin D3 up-regulated protein 1 mediates oxidative stress via suppressing the thioredoxin function. J Immunol 164, 6287-6295
    • (2000) J Immunol , vol.164 , pp. 6287-6295
    • Junn, E.1    Ran, S.H.2    Im, J.Y.3    Yang, Y.4    Cho, E.W.5
  • 17
    • 78651146370 scopus 로고
    • Enzymatic synthesis of deoxyribonucleotides. IV. Isolation and characterization of thioredoxin, the hydrogen donor from Escherichia coli B
    • Laurent TC, Moore EC, Reichard P (1964) Enzymatic synthesis of deoxyribonucleotides. IV. Isolation and characterization of thioredoxin, the hydrogen donor from Escherichia coli B. J Biol Chem 239, 3436-3444
    • (1964) J Biol Chem , vol.239 , pp. 3436-3444
    • Laurent, T.C.1    Moore, E.C.2    Reichard, P.3
  • 18
    • 0034527208 scopus 로고    scopus 로고
    • New polymorphic microsatellite markers in the human MHC class II region
    • Matsuzaka Y, Makino S, Nakajima K, Tomizawa M, Oka A, et al. (2000) New polymorphic microsatellite markers in the human MHC class II region. Tissue Antigens 56, 492-500
    • (2000) Tissue Antigens , vol.56 , pp. 492-500
    • Matsuzaka, Y.1    Makino, S.2    Nakajima, K.3    Tomizawa, M.4    Oka, A.5
  • 19
    • 0036401503 scopus 로고    scopus 로고
    • Identification of the hRDH-E2 gene, a novel member of the SDR family, and its increased expression in psoriatic lesion
    • Matsuzaka Y, Okamoto K, Tsuji H, Mabuchi T, Ozawa A, et al. (2002) Identification of the hRDH-E2 gene, a novel member of the SDR family, and its increased expression in psoriatic lesion. Biochem Biophys Res Commun 297, 1171-1180
    • (2002) Biochem Biophys Res Commun , vol.297 , pp. 1171-1180
    • Matsuzaka, Y.1    Okamoto, K.2    Tsuji, H.3    Mabuchi, T.4    Ozawa, A.5
  • 20
    • 0026715172 scopus 로고
    • Thioredoxin regulates the DNA binding activity of NF-kappa B by reduction of a disulphide bond involving cysteine 62
    • Matthews JR, Wakasugi N, Virelizier JL, Yodoi J, Hay RT (1992) Thioredoxin regulates the DNA binding activity of NF-kappa B by reduction of a disulphide bond involving cysteine 62. Nucleic Acids Res 20(15), 3821-3830
    • (1992) Nucleic Acids Res , vol.20 , Issue.15 , pp. 3821-3830
    • Matthews, J.R.1    Wakasugi, N.2    Virelizier, J.L.3    Yodoi, J.4    Hay, R.T.5
  • 22
    • 0028298235 scopus 로고
    • Opposing regulatory effects of thioredoxin and eosinophil cytotoxicity-enhancing factor on the development of human immunodeficiency virus 1
    • Newman GW, Balcewicz-Sablinska MK, Guarnaccia JR, Remold HG, Silberstein DS (1994) Opposing regulatory effects of thioredoxin and eosinophil cytotoxicity-enhancing factor on the development of human immunodeficiency virus 1. J Exp Med 180(1), 359-363
    • (1994) J Exp Med , vol.180 , Issue.1 , pp. 359-363
    • Newman, G.W.1    Balcewicz-Sablinska, M.K.2    Guarnaccia, J.R.3    Remold, H.G.4    Silberstein, D.S.5
  • 23
    • 0033618398 scopus 로고    scopus 로고
    • Identification of thioredoxin-binding protein-2/vitamin D(3) up-regulated protein 1 as a negative regulator of thioredoxin function and expression
    • Nishiyama A, Matsui M, Iwata S, Hirota K, Masutani H, et al. (1999) Identification of thioredoxin-binding protein-2/vitamin D(3) up-regulated protein 1 as a negative regulator of thioredoxin function and expression. J Biol Chem 274, 21645-21650
    • (1999) J Biol Chem , vol.274 , pp. 21645-21650
    • Nishiyama, A.1    Matsui, M.2    Iwata, S.3    Hirota, K.4    Masutani, H.5
  • 24
    • 1042302126 scopus 로고    scopus 로고
    • Thioredoxin secreted upon ultraviolet A irradiation modulates activities of matrix metalloproteinase-2 and tissue inhibitor of metalloproteinase-2 in human dermal fibroblasts
    • Oh JH, Chung AS, Steinbrenner H, Sies H, Brenneisen P (2004) Thioredoxin secreted upon ultraviolet A irradiation modulates activities of matrix metalloproteinase-2 and tissue inhibitor of metalloproteinase-2 in human dermal fibroblasts. Arch Biochem Biophys 423(1), 218-226
    • (2004) Arch Biochem Biophys , vol.423 , Issue.1 , pp. 218-226
    • Oh, J.H.1    Chung, A.S.2    Steinbrenner, H.3    Sies, H.4    Brenneisen, P.5
  • 25
    • 0032697536 scopus 로고    scopus 로고
    • Association analysis using refined microsatellite markers localizes a susceptibility locus for psoriasis vulgaris within a 111kb segment telomeric to the HLA-C gene
    • Oka A, Tamiya G, Tomizawa M, Ota M, Katsuyama Y, et al. (1999) Association analysis using refined microsatellite markers localizes a susceptibility locus for psoriasis vulgaris within a 111kb segment telomeric to the HLA-C gene. Hum Mol Genet 8, 2165-2170
    • (1999) Hum Mol Genet , vol.8 , pp. 2165-2170
    • Oka, A.1    Tamiya, G.2    Tomizawa, M.3    Ota, M.4    Katsuyama, Y.5
  • 26
    • 0027177564 scopus 로고
    • From RNA to DNA, why so many ribonucleotide reductases?
    • Reichard P (1993) From RNA to DNA, why so many ribonucleotide reductases? Science 260, 1773-1777
    • (1993) Science , vol.260 , pp. 1773-1777
    • Reichard, P.1
  • 27
    • 0026443077 scopus 로고
    • Secretion of thioredoxin by normal and neoplastic cells through a leaderless secretory pathway
    • Rubartelli A, Bajetto A, Allavena G, Wollman E, Sitia (1992) Secretion of thioredoxin by normal and neoplastic cells through a leaderless secretory pathway. J Biol Chem 267(34), 24161-24164
    • (1992) J Biol Chem , vol.267 , Issue.34 , pp. 24161-24164
    • Rubartelli, A.1    Bajetto, A.2    Allavena, G.3    Wollman, E.4    Sitia5
  • 28
    • 0032080283 scopus 로고    scopus 로고
    • Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1
    • Saitoh M, Nishitoh H, Fujii M, Takeda K, Tobiume K, et al. (1998) Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1. EMBO J 17(9), 2596-2606
    • (1998) EMBO J , vol.17 , Issue.9 , pp. 2596-2606
    • Saitoh, M.1    Nishitoh, H.2    Fujii, M.3    Takeda, K.4    Tobiume, K.5
  • 29
    • 0035891543 scopus 로고    scopus 로고
    • Thioredoxin reductaser - Its role in epidermal redox status
    • Schallreuter KU, Wood JM (2001) Thioredoxin reductaser - its role in epidermal redox status. J Photochem Photobiol B 64, 179-184
    • (2001) J Photochem Photobiol B , vol.64 , pp. 179-184
    • Schallreuter, K.U.1    Wood, J.M.2
  • 30
    • 0033609827 scopus 로고    scopus 로고
    • Redox regulation of cell signaling by selenocysteine in mammalian thioredoxin reductases
    • Sun Q-A, Wu Y, Zappacosta F, Jeang K-T, Lee BJ, et al. (1999) Redox regulation of cell signaling by selenocysteine in mammalian thioredoxin reductases. J Biol Chem 247, 24522-24530
    • (1999) J Biol Chem , vol.247 , pp. 24522-24530
    • Sun, Q.-A.1    Wu, Y.2    Zappacosta, F.3    Jeang, K.-T.4    Lee, B.J.5
  • 31
    • 0030020576 scopus 로고    scopus 로고
    • A new selenoprotein from human lung adenocarcinoma cells: Purification, properties, and thioredoxin reductase activity
    • Tamura T, Stadtman TC (1996) A new selenoprotein from human lung adenocarcinoma cells: purification, properties, and thioredoxin reductase activity. Proc Natl Acad Sci USA 93(3), 1006-1011
    • (1996) Proc Natl Acad Sci USA , vol.93 , Issue.3 , pp. 1006-1011
    • Tamura, T.1    Stadtman, T.C.2
  • 33
    • 0025852479 scopus 로고
    • Modulation of transcription factor NF-kappa B binding activity by oxidation-reduction in vitro
    • Toledano MB, Leonard WJ (1991) Modulation of transcription factor NF-kappa B binding activity by oxidation-reduction in vitro. Proc Natl Acad Sci USA. 88(10), 4328-4332
    • (1991) Proc Natl Acad Sci USA , vol.88 , Issue.10 , pp. 4328-4332
    • Toledano, M.B.1    Leonard, W.J.2
  • 34
    • 0037288999 scopus 로고    scopus 로고
    • SLURP-2, a novel member of the human Ly-6 superfamily that is up-regulated in psoriasis vulgaris
    • Tsuji H, Okamoto K, Matsuzaka Y, Iizuka H, Tamiya G, et al. (2003) SLURP-2, a novel member of the human Ly-6 superfamily that is up-regulated in psoriasis vulgaris. Genomics 81, 26-33
    • (2003) Genomics , vol.81 , pp. 26-33
    • Tsuji, H.1    Okamoto, K.2    Matsuzaka, Y.3    Iizuka, H.4    Tamiya, G.5
  • 35
    • 0025066731 scopus 로고
    • Adult T-cell leukemia-derived factor/thioredoxin, produced by both human T-lymphotropic virus type I- and Epstein-Barr virus-transformed lymphocytes, acts as an autocrine growth factor and synergizes with interleukin 1 and interleukin 2
    • Wakasugi N, Tagaya Y, Wakasugi H, Mitsui A, Maeda M, et al. (1990) Adult T-cell leukemia-derived factor/thioredoxin, produced by both human T-lymphotropic virus type I- and Epstein-Barr virus-transformed lymphocytes, acts as an autocrine growth factor and synergizes with interleukin 1 and interleukin 2. Proc Natl Acad Sci USA 87(21), 8282-8286
    • (1990) Proc Natl Acad Sci USA , vol.87 , Issue.21 , pp. 8282-8286
    • Wakasugi, N.1    Tagaya, Y.2    Wakasugi, H.3    Mitsui, A.4    Maeda, M.5
  • 36
    • 0024291284 scopus 로고
    • Autoregulated instability of beta-tubulin mRNAs by recognition of the nascent amino terminus of beta-tubulin
    • Yen TJ, Machlin PS, Cleveland DW (1988) Autoregulated instability of beta-tubulin mRNAs by recognition of the nascent amino terminus of beta-tubulin. Nature 334, 580-585
    • (1988) Nature , vol.334 , pp. 580-585
    • Yen, T.J.1    Machlin, P.S.2    Cleveland, D.W.3


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