메뉴 건너뛰기




Volumn 242, Issue 1-2, 2000, Pages 321-330

Molecular cloning of mouse thioredoxin reductases

Author keywords

Mapping; Mitochondria; Redox; Selenocysteine; Selenoprotein

Indexed keywords

COMPLEMENTARY DNA; HYBRID PROTEIN; SELENOCYSTEINE; SELENOPROTEIN; THIOREDOXIN REDUCTASE;

EID: 0033969003     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(99)00498-9     Document Type: Article
Times cited : (21)

References (31)
  • 1
    • 0025887817 scopus 로고
    • In vitro DNA binding activity of Fos/Jun and BZLF1 but not C/EBP is affected by redox changes
    • Bannister A.J., Cook A., Kouzarides T. In vitro DNA binding activity of Fos/Jun and BZLF1 but not C/EBP is affected by redox changes. Oncogene. 6:1991;1243-1250.
    • (1991) Oncogene , vol.6 , pp. 1243-1250
    • Bannister, A.J.1    Cook, A.2    Kouzarides, T.3
  • 2
    • 0028226006 scopus 로고
    • Cloning and sequencing of thiol-specific antioxidant from mammalian brain: Alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes
    • Chae H.Z., Robison K., Poole L.B., Church G., Storz G., Rhee S.G. Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes. Proc. Natl. Acad. Sci. USA. 91:1994;7017-7021.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7017-7021
    • Chae, H.Z.1    Robison, K.2    Poole, L.B.3    Church, G.4    Storz, G.5    Rhee, S.G.6
  • 3
    • 0024421652 scopus 로고
    • Human transcription factor IIIC (TFIIIC). Purification, polypeptide structure, and the involvement of thiol groups in specific DNA binding
    • 100-18 109
    • Cromlish J.A., Roeder R.G. Human transcription factor IIIC (TFIIIC). Purification, polypeptide structure, and the involvement of thiol groups in specific DNA binding. J. Biol. Chem. 264:1989;18 100-18 109.
    • (1989) J. Biol. Chem. , vol.264 , pp. 18
    • Cromlish, J.A.1    Roeder, R.G.2
  • 4
    • 0029156177 scopus 로고
    • DiGeorge syndrome and related syndromes associated with 22q11.2 deletions
    • Demczuk S., Aurias A. DiGeorge syndrome and related syndromes associated with 22q11.2 deletions. Ann. Genet. 38:1995;59-76.
    • (1995) Ann. Genet. , vol.38 , pp. 59-76
    • Demczuk, S.1    Aurias, A.2
  • 5
    • 0029778527 scopus 로고
    • Transfection with human thioredoxin increases cell proliferation and a dominant-negative mutant thioredoxin reverses the transformed phenotype of human breast cancer cells
    • Gallegos A., Gasdaska J.R., Taylor C.W., Paine-Murrieta G.D., Goodman D., Gasdaska P.Y., Berggren M., Briehl M.M., Powis G. Transfection with human thioredoxin increases cell proliferation and a dominant-negative mutant thioredoxin reverses the transformed phenotype of human breast cancer cells. Cancer Res. 56:1995;5765-5770.
    • (1995) Cancer Res. , vol.56 , pp. 5765-5770
    • Gallegos, A.1    Gasdaska, J.R.2    Taylor, C.W.3    Paine-Murrieta, G.D.4    Goodman, D.5    Gasdaska, P.Y.6    Berggren, M.7    Briehl, M.M.8    Powis, G.9
  • 7
    • 0032898734 scopus 로고    scopus 로고
    • Cloning, sequencing and functional expression of a novel human thioredoxin reductase
    • Gasdaska P.Y., Berggren M.M., Berry M.J., Powis G. Cloning, sequencing and functional expression of a novel human thioredoxin reductase. FEBS Lett. 442:1999;105-111.
    • (1999) FEBS Lett. , vol.442 , pp. 105-111
    • Gasdaska, P.Y.1    Berggren, M.M.2    Berry, M.J.3    Powis, G.4
  • 8
    • 0029973142 scopus 로고    scopus 로고
    • Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene
    • Gladyshev V.N., Jeang K.T., Stadtman T.C. Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene. Proc. Natl. Acad. Sci. USA. 93:1996;6146-6151.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6146-6151
    • Gladyshev, V.N.1    Jeang, K.T.2    Stadtman, T.C.3
  • 9
    • 0032544012 scopus 로고    scopus 로고
    • Catechol-O-methyltransferase-deficient mice exhibit sexually dimorphic changes in catecholamine levels and behavior
    • Gogos J.A., Morgan M., Luine V., Santha M., Ogawa S., Pfaff D., Karayiogou M. Catechol-O-methyltransferase-deficient mice exhibit sexually dimorphic changes in catecholamine levels and behavior. Proc. Natl. Acad. Sci. USA. 95:1998;9991-9996.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9991-9996
    • Gogos, J.A.1    Morgan, M.2    Luine, V.3    Santha, M.4    Ogawa, S.5    Pfaff, D.6    Karayiogou, M.7
  • 11
    • 0032509431 scopus 로고    scopus 로고
    • Human AIM-1: CDNA cloning and reduced expression during endomitosis in megakaryocyte-lineage cells
    • Katayama H., Ota T., Morita K., Terada Y., Suzuki F., Katoh O., Tatsuka M. Human AIM-1: cDNA cloning and reduced expression during endomitosis in megakaryocyte-lineage cells. Gene. 224:1998;1-7.
    • (1998) Gene , vol.224 , pp. 1-7
    • Katayama, H.1    Ota, T.2    Morita, K.3    Terada, Y.4    Suzuki, F.5    Katoh, O.6    Tatsuka, M.7
  • 12
    • 0032546955 scopus 로고    scopus 로고
    • Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor
    • 366-15 372
    • Lee S.R., Kwon K.S., Kim S.R., Rhee S.G. Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor. J. Biol. Chem. 273:1998;15 366-15 372.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15
    • Lee, S.R.1    Kwon, K.S.2    Kim, S.R.3    Rhee, S.G.4
  • 13
    • 0033582515 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a mitochondrial selenocysteine-containing thioredoxin reductase from rat liver
    • Lee S.R., Kim J.R., Kwon K.S., Yoon H.W., Levine R.L., Ginsburg A., Rhee S.G. Molecular cloning and characterization of a mitochondrial selenocysteine-containing thioredoxin reductase from rat liver. J. Biol. Chem. 274:1999;4722-4734.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4722-4734
    • Lee, S.R.1    Kim, J.R.2    Kwon, K.S.3    Yoon, H.W.4    Levine, R.L.5    Ginsburg, A.6    Rhee, S.G.7
  • 15
    • 0029894345 scopus 로고    scopus 로고
    • Knowing when not to stop: Selenocysteine incorporation in eukaryotes
    • Low S.C., Berry M.J. Knowing when not to stop: selenocysteine incorporation in eukaryotes. Trends Biochem. Sci. 21:1996;203-208.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 203-208
    • Low, S.C.1    Berry, M.J.2
  • 16
    • 0032809682 scopus 로고    scopus 로고
    • Sequence-ready physical map of the mouse chromosome 16 region with conserved synteny to the human velocardiofacial syndrome region on 22q11.2
    • Lund J., Roe B., Chen F., Budarf M., Galili N., Riblet R., Miller R.D., Emanuel B.S., Reeves R.H. Sequence-ready physical map of the mouse chromosome 16 region with conserved synteny to the human velocardiofacial syndrome region on 22q11.2. Mamm. Genome. 10:1999;438-443.
    • (1999) Mamm. Genome , vol.10 , pp. 438-443
    • Lund, J.1    Roe, B.2    Chen, F.3    Budarf, M.4    Galili, N.5    Riblet, R.6    Miller, R.D.7    Emanuel, B.S.8    Reeves, R.H.9
  • 17
    • 0025331418 scopus 로고
    • Protein disulfide-isomerase is a substrate for thioredoxin reductase and has thioredoxin-like activity
    • Lundstrom J., Holmgren A. Protein disulfide-isomerase is a substrate for thioredoxin reductase and has thioredoxin-like activity. J. Biol. Chem. 265:1990;9114-9120.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9114-9120
    • Lundstrom, J.1    Holmgren, A.2
  • 18
    • 0020488534 scopus 로고
    • Rat liver thioredoxin and thioredoxin reductase: Purification and characterization
    • Luthman M., Holmgren A. Rat liver thioredoxin and thioredoxin reductase: purification and characterization. Biochemistry. 21:1982;6628-6633.
    • (1982) Biochemistry , vol.21 , pp. 6628-6633
    • Luthman, M.1    Holmgren, A.2
  • 19
    • 0026715172 scopus 로고
    • Thioredoxin regulates the DNA binding activity of NF-kappa B by reduction of a disulphide bond involving cysteine 62
    • Matthews J.R., Wakasugi N., Virelizier J.L., Yodoi J., Hay R.T. Thioredoxin regulates the DNA binding activity of NF-kappa B by reduction of a disulphide bond involving cysteine 62. Nucleic Acids Res. 20:1992;3821-3830.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 3821-3830
    • Matthews, J.R.1    Wakasugi, N.2    Virelizier, J.L.3    Yodoi, J.4    Hay, R.T.5
  • 22
    • 0028395670 scopus 로고
    • Transport of proteins across mitochondrial membranes
    • Neupert W. Transport of proteins across mitochondrial membranes. Clin. Investig. 72:1994;251-261.
    • (1994) Clin. Investig. , vol.72 , pp. 251-261
    • Neupert, W.1
  • 24
    • 0022457811 scopus 로고
    • The role of thioredoxin reductase in the reduction of free radicals at the surface of the epidermis
    • Schallreuter K.U., Wood J.M. The role of thioredoxin reductase in the reduction of free radicals at the surface of the epidermis. Biochem. Biophys. Res. Commun. 136:1986;630-637.
    • (1986) Biochem. Biophys. Res. Commun. , vol.136 , pp. 630-637
    • Schallreuter, K.U.1    Wood, J.M.2
  • 27
    • 0030020576 scopus 로고    scopus 로고
    • A new selenoprotein from human lung adenocarcinoma cells: Purification, properties, and thioredoxin reductase activity
    • Tamura T., Stadtman T.C. A new selenoprotein from human lung adenocarcinoma cells: purification, properties, and thioredoxin reductase activity. Proc. Natl. Acad. Sci. USA. 93:1996;1006-1011.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1006-1011
    • Tamura, T.1    Stadtman, T.C.2
  • 30
    • 0026714672 scopus 로고
    • Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme
    • Xanthoudakis S., Miao G., Wang F., Pan Y.C., Curran T. Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme. EMBO J. 11:1992;3323-3335.
    • (1992) EMBO J. , vol.11 , pp. 3323-3335
    • Xanthoudakis, S.1    Miao, G.2    Wang, F.3    Pan, Y.C.4    Curran, T.5
  • 31
    • 0032502720 scopus 로고    scopus 로고
    • Rat and calf thioredoxin reductase are homologous to glutathione reductase with a carboxyl-terminal elongation containing a conserved catalytically active penultimate selenocysteine residue
    • Zhong L., Arn-er E.S., Ljung J., Aslund F., Holmgren A. Rat and calf thioredoxin reductase are homologous to glutathione reductase with a carboxyl-terminal elongation containing a conserved catalytically active penultimate selenocysteine residue. J. Biol. Chem. 273:1998;8581-8591.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8581-8591
    • Zhong, L.1    Arn-Er, E.S.2    Ljung, J.3    Aslund, F.4    Holmgren, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.