메뉴 건너뛰기




Volumn 6, Issue 3, 1999, Pages 151-160

Selenocysteine-containing proteins in mammals

Author keywords

Codon UGA; Glutathione peroxidase; Iodothyronine deiodinase; Selenocysteine; Selenoenzymes; Selenoprotein P; Selenoproteins; Thioredoxin reductase

Indexed keywords

GLUTATHIONE PEROXIDASE; SELENOCYSTEINE; SELENOPROTEIN; THIOREDOXIN REDUCTASE; THYROXINE DEIODINASE; TRANSFER RNA;

EID: 0032935722     PISSN: 10217770     EISSN: 14230127     Source Type: Journal    
DOI: 10.1007/BF02255899     Document Type: Review
Times cited : (159)

References (104)
  • 1
    • 0028955626 scopus 로고
    • 1-Chloro-2,4-dinitrobenzene is an irreversible inhibitor of human thioredoxin reductase. Loss of thioredoxin disulfide reductase activity is accompanied by a large increase in NADPH oxidase activity
    • Arner ES, Bjornstedt M, Holmgren A. 1-Chloro-2,4-dinitrobenzene is an irreversible inhibitor of human thioredoxin reductase. Loss of thioredoxin disulfide reductase activity is accompanied by a large increase in NADPH oxidase activity. J Biol Chem 270:3479-3482; 1995.
    • (1995) J Biol Chem , vol.270 , pp. 3479-3482
    • Arner, E.S.1    Bjornstedt, M.2    Holmgren, A.3
  • 2
    • 0031227819 scopus 로고    scopus 로고
    • Glutathione peroxidase revisited - Simulation of the catalytic cycle by computer-assisted molecular modelling
    • Aumann KD, Bedorf N, Brigelius-Flohe R, Schomburg D, Flohe L. Glutathione peroxidase revisited - Simulation of the catalytic cycle by computer-assisted molecular modelling. Biomed Environ Sci 10:136-155;1997.
    • (1997) Biomed Environ Sci , vol.10 , pp. 136-155
    • Aumann, K.D.1    Bedorf, N.2    Brigelius-Flohe, R.3    Schomburg, D.4    Flohe, L.5
  • 3
    • 0030695172 scopus 로고    scopus 로고
    • Thioredoxin, a gene found overexpressed in human cancer, inhibits apoptosis in vitro and in vivo
    • Baker A, Payne CM, Briehl MM, Powis G. Thioredoxin, a gene found overexpressed in human cancer, inhibits apoptosis in vitro and in vivo. Cancer Res 57:5162-5167;1997.
    • (1997) Cancer Res , vol.57 , pp. 5162-5167
    • Baker, A.1    Payne, C.M.2    Briehl, M.M.3    Powis, G.4
  • 4
    • 0031656463 scopus 로고    scopus 로고
    • Glutathione peroxidase protects mice from viral-induced myocarditis
    • Beck MA, Esworthy RS, Ho YS, Chu FF. Glutathione peroxidase protects mice from viral-induced myocarditis. FASEB J 12:1143-1149; 1998.
    • (1998) FASEB J , vol.12 , pp. 1143-1149
    • Beck, M.A.1    Esworthy, R.S.2    Ho, Y.S.3    Chu, F.F.4
  • 5
    • 0031021132 scopus 로고    scopus 로고
    • Mouse models of human disease. Part I: Techniques and resources for genetic analysis in mice
    • Bedell MA, Jenkins NA, Copeland NG. Mouse models of human disease. Part I: Techniques and resources for genetic analysis in mice. Genes Dev 11:1-10;1997.
    • (1997) Genes Dev , vol.11 , pp. 1-10
    • Bedell, M.A.1    Jenkins, N.A.2    Copeland, N.G.3
  • 6
    • 0023886514 scopus 로고
    • Evidence for specific selenium target tissues and new biologically important selenoproteins
    • Behne D, Hilmert H, Scheid S, Gessner H, Elger W. Evidence for specific selenium target tissues and new biologically important selenoproteins. Biochim Biophys Acta 966:12-21;1988.
    • (1988) Biochim Biophys Acta , vol.966 , pp. 12-21
    • Behne, D.1    Hilmert, H.2    Scheid, S.3    Gessner, H.4    Elger, W.5
  • 8
  • 9
    • 0025743489 scopus 로고
    • Recognition of UGA as a selenocysteine codon in type I deiodinase requires sequences in the 3′ untranslated region
    • Berry MJ, Banu L, Chen YY, Mandel SJ, Kieffer JD, Harney JW, Larsen PR. Recognition of UGA as a selenocysteine codon in type I deiodinase requires sequences in the 3′ untranslated region. Nature 353:273-276;1991.
    • (1991) Nature , vol.353 , pp. 273-276
    • Berry, M.J.1    Banu, L.2    Chen, Y.Y.3    Mandel, S.J.4    Kieffer, J.D.5    Harney, J.W.6    Larsen, P.R.7
  • 10
    • 0027282772 scopus 로고
    • Functional characterization of the eukaryotic SECIS elements which direct selenocysteine insertion at UGA codons
    • Berry MJ, Banu L, Harney JW, Larsen PR. Functional characterization of the eukaryotic SECIS elements which direct selenocysteine insertion at UGA codons. EMBO J 12:3315-3322;1993.
    • (1993) EMBO J , vol.12 , pp. 3315-3322
    • Berry, M.J.1    Banu, L.2    Harney, J.W.3    Larsen, P.R.4
  • 11
    • 0028139014 scopus 로고
    • The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase
    • Bjornstedt M, Xue J, Huang W, Akesson B, Holmgren A. The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase. J Biol Chem 269:29382-29384;1994.
    • (1994) J Biol Chem , vol.269 , pp. 29382-29384
    • Bjornstedt, M.1    Xue, J.2    Huang, W.3    Akesson, B.4    Holmgren, A.5
  • 12
    • 0029031370 scopus 로고
    • Human thioredoxin reductase directly reduces lipid hydroperoxides by NADPH and selenocystine strongly stimulates the reaction via catalytically generated selenols
    • Bjornstedt M, Hamberg M, Kumar S, Xue J, Holmgren A. Human thioredoxin reductase directly reduces lipid hydroperoxides by NADPH and selenocystine strongly stimulates the reaction via catalytically generated selenols. J Biol Chem 270:11761-11764;1995.
    • (1995) J Biol Chem , vol.270 , pp. 11761-11764
    • Bjornstedt, M.1    Hamberg, M.2    Kumar, S.3    Xue, J.4    Holmgren, A.5
  • 13
    • 0029187633 scopus 로고
    • Selenite and selenodiglutathione: Reactions with thioredoxin systems
    • Bjornstedt M, Kumar S, Holmgren A. Selenite and selenodiglutathione: Reactions with thioredoxin systems. Methods Enzymol 252:209-219;1995.
    • (1995) Methods Enzymol , vol.252 , pp. 209-219
    • Bjornstedt, M.1    Kumar, S.2    Holmgren, A.3
  • 14
    • 0002615176 scopus 로고
    • Incorporation of selenium into bacterial selenoprotein
    • (Burk RF, ed.) New York, Springer
    • Bock A. Incorporation of selenium into bacterial selenoprotein. In: (Burk RF, ed.) Selenium in Biology and Human Health. New York, Springer, 146-177;1994.
    • (1994) Selenium in Biology and Human Health , pp. 146-177
    • Bock, A.1
  • 15
    • 0030978102 scopus 로고    scopus 로고
    • Early embryonic lethality caused by targeted disruption of the mouse selenocysteine tRNA gene (Trsp)
    • Bosl MR, Takaku K, Oshima M, Nishimura S, Taketo MM. Early embryonic lethality caused by targeted disruption of the mouse selenocysteine tRNA gene (Trsp). Proc Natl Acad Sci USA 94:5531-5534;1997.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 5531-5534
    • Bosl, M.R.1    Takaku, K.2    Oshima, M.3    Nishimura, S.4    Taketo, M.M.5
  • 17
    • 0028901930 scopus 로고
    • Pathogenesis of diquat-induced liver necrosis in selenium-deficient rats: Assessment of the roles of lipid peroxidation and selenoprotein P
    • Burk RF, Hill KE, Awad JA, Morrow JD, Kato T, Cockell KA, Lyons PR. Pathogenesis of diquat-induced liver necrosis in selenium-deficient rats: Assessment of the roles of lipid peroxidation and selenoprotein P. Hepatology 21:561-569;1995.
    • (1995) Hepatology , vol.21 , pp. 561-569
    • Burk, R.F.1    Hill, K.E.2    Awad, J.A.3    Morrow, J.D.4    Kato, T.5    Cockell, K.A.6    Lyons, P.R.7
  • 18
    • 0022730806 scopus 로고
    • The structure of the mouse glutathione peroxidase gene: The selenocysteine in the active site is encoded by the 'termination' codon, TGA
    • Chambers I, Frampton J, Goldfarb P, Affara N, McBain W, Harrison PR. The structure of the mouse glutathione peroxidase gene: The selenocysteine in the active site is encoded by the 'termination' codon, TGA. EMBO J 5: 1221-1227;1986.
    • (1986) EMBO J , vol.5 , pp. 1221-1227
    • Chambers, I.1    Frampton, J.2    Goldfarb, P.3    Affara, N.4    McBain, W.5    Harrison, P.R.6
  • 19
    • 0021140102 scopus 로고
    • Occurrence of selenium-containing tRNAs in mouse leukemia cells
    • Ching WM. Occurrence of selenium-containing tRNAs in mouse leukemia cells. Proc Natl Acad Sci USA 81:3010-3013;1984.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 3010-3013
    • Ching, W.M.1
  • 22
    • 0031225669 scopus 로고    scopus 로고
    • Expression and chromosomal mapping of mouse Gpx2 gene encoding the gastrointestinal form of glutathione peroxidase, GPX-GI
    • Chu FF, Esworthy RS, Ho YS, Bermeister M, Swiderek K, Elliott RW. Expression and chromosomal mapping of mouse Gpx2 gene encoding the gastrointestinal form of glutathione peroxidase, GPX-GI. Biomed Environ Sci 10: 156-162;1997.
    • (1997) Biomed Environ Sci , vol.10 , pp. 156-162
    • Chu, F.F.1    Esworthy, R.S.2    Ho, Y.S.3    Bermeister, M.4    Swiderek, K.5    Elliott, R.W.6
  • 24
    • 0030035595 scopus 로고    scopus 로고
    • Cloning of the mammalian type II iodothyronine deiodinase. A selenoprotein differentially expressed and regulated in human and rat brain and other tissues
    • Croteau W, Davey JC, Galton VA, St Germain DL. Cloning of the mammalian type II iodothyronine deiodinase. A selenoprotein differentially expressed and regulated in human and rat brain and other tissues. J Clin Invest 98: 405-417;1996.
    • (1996) J Clin Invest , vol.98 , pp. 405-417
    • Croteau, W.1    Davey, J.C.2    Galton, V.A.3    St Germain, D.L.4
  • 25
    • 0025736597 scopus 로고
    • A genetic tool used to identify thioredoxin as a mediator of a growth inhibitory signal
    • Deiss LP, Kimchi A. A genetic tool used to identify thioredoxin as a mediator of a growth inhibitory signal. Science 252:117-120;1991.
    • (1991) Science , vol.252 , pp. 117-120
    • Deiss, L.P.1    Kimchi, A.2
  • 26
    • 0020393233 scopus 로고
    • Properties of the selenium-containing moiety of nicotinic acid hydroxylase from Clostridium barkeri
    • Dilworth GL. Properties of the selenium-containing moiety of nicotinic acid hydroxylase from Clostridium barkeri. Arch Biochem Biophys 219:30-38;1982.
    • (1982) Arch Biochem Biophys , vol.219 , pp. 30-38
    • Dilworth, G.L.1
  • 27
    • 0020630570 scopus 로고
    • Occurrence of molybdenum in the nicotinic acid hydroxylase from Clostridium barkeri
    • Dilworth GL. Occurrence of molybdenum in the nicotinic acid hydroxylase from Clostridium barkeri. Arch Biochem Biophys 221:565-569;1983.
    • (1983) Arch Biochem Biophys , vol.221 , pp. 565-569
    • Dilworth, G.L.1
  • 28
    • 0031425497 scopus 로고    scopus 로고
    • Diaryl chalcogenides as selective inhibitors of thioredoxin reductase and potential antitumor agents
    • Engman L, Cotgreave I, Angulo M, Taylor CW, Paine-Murrieta GD, Powis G. Diaryl chalcogenides as selective inhibitors of thioredoxin reductase and potential antitumor agents. Anticancer Res 17:4599-4605;1997.
    • (1997) Anticancer Res , vol.17 , pp. 4599-4605
    • Engman, L.1    Cotgreave, I.2    Angulo, M.3    Taylor, C.W.4    Paine-Murrieta, G.D.5    Powis, G.6
  • 29
    • 0020775636 scopus 로고
    • The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution
    • Epp O, Ladenstein R, Wendel A. The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution. Eur J Biochem 133:51-69;1983.
    • (1983) Eur J Biochem , vol.133 , pp. 51-69
    • Epp, O.1    Ladenstein, R.2    Wendel, A.3
  • 30
    • 0028835297 scopus 로고
    • Expression of selenium-dependent glutathione peroxidase in human breast tumor cell lines
    • Esworthy RS, Baker MA, Chu FF. Expression of selenium-dependent glutathione peroxidase in human breast tumor cell lines. Cancer Res 55:957-962;1995.
    • (1995) Cancer Res , vol.55 , pp. 957-962
    • Esworthy, R.S.1    Baker, M.A.2    Chu, F.F.3
  • 31
    • 0031879339 scopus 로고    scopus 로고
    • Selenium-dependent glutathione peroxidaseGI is a major glutathione peroxidase activity in the mucosal epithelium of rodent intestine
    • Esworthy RS, Swiderek KM, Ho YS, Chu FF. Selenium-dependent glutathione peroxidaseGI is a major glutathione peroxidase activity in the mucosal epithelium of rodent intestine. Biochim Biophys Acta 1381:213-226;1998.
    • (1998) Biochim Biophys Acta , vol.1381 , pp. 213-226
    • Esworthy, R.S.1    Swiderek, K.M.2    Ho, Y.S.3    Chu, F.F.4
  • 32
    • 0032575705 scopus 로고    scopus 로고
    • A matter of life and cell death
    • Evan G, Littlewood T. A matter of life and cell death. Science 281:1317-1320;1998.
    • (1998) Science , vol.281 , pp. 1317-1320
    • Evan, G.1    Littlewood, T.2
  • 33
    • 0029778527 scopus 로고    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 JR, Taylor CW, Paine-Murrieta GD, Goodman D, Gasdaska PY, Berggren M, Briehl MM, 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 56:5765-5770;1996.
    • (1996) 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
  • 34
    • 0030731916 scopus 로고    scopus 로고
    • Mechanisms of the regulation of thioredoxin reductase activity in cancer cells by the chemopreventive agent selenium
    • Gallegos A, Berggren M, Gasdaska JR, Powis G. Mechanisms of the regulation of thioredoxin reductase activity in cancer cells by the chemopreventive agent selenium. Cancer Res 57: 4965-4970;1997.
    • (1997) Cancer Res , vol.57 , pp. 4965-4970
    • Gallegos, A.1    Berggren, M.2    Gasdaska, J.R.3    Powis, G.4
  • 36
    • 0027957511 scopus 로고
    • Nicotinic acid hydroxylase from Clostridium barkeri: Electron paramagnetic resonance studies show that selenium is coordinated with molybdenum in the catalytically active selenium-dependent enzyme
    • Gladyshev VN, Khangulov SV, Stadtman TC. Nicotinic acid hydroxylase from Clostridium barkeri: Electron paramagnetic resonance studies show that selenium is coordinated with molybdenum in the catalytically active selenium-dependent enzyme. Proc Natl Acad Sci USA 91:232-236;1994.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 232-236
    • Gladyshev, V.N.1    Khangulov, S.V.2    Stadtman, T.C.3
  • 37
    • 0030068830 scopus 로고    scopus 로고
    • Properties of the selenium- and molybdenumcontaining nicotinic acid hydroxylase from Clostridium barkeri
    • Gladyshev VN, Khangulov SV, Stadtman TC. Properties of the selenium- and molybdenumcontaining nicotinic acid hydroxylase from Clostridium barkeri. Biochemistry 35:212-223;1996.
    • (1996) Biochemistry , vol.35 , pp. 212-223
    • Gladyshev, V.N.1    Khangulov, S.V.2    Stadtman, T.C.3
  • 38
    • 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 VN, Jeang KT, Stadtman TC. 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 93:6146-6151;1996.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6146-6151
    • Gladyshev, V.N.1    Jeang, K.T.2    Stadtman, T.C.3
  • 39
    • 0032502777 scopus 로고    scopus 로고
    • A new human selenium-containing protein. Purification, characterization, and cDNA sequence
    • Gladyshev VN, Jeang KT, Wootton JC, Hatfield DL. A new human selenium-containing protein. Purification, characterization, and cDNA sequence. J Biol Chem 273:8910-8915; 1998.
    • (1998) J Biol Chem , vol.273 , pp. 8910-8915
    • Gladyshev, V.N.1    Jeang, K.T.2    Wootton, J.C.3    Hatfield, D.L.4
  • 41
    • 0032552946 scopus 로고    scopus 로고
    • Contrasting patterns of regulation of the antioxidant selenoproteins, thioredoxin reductase and glutathione peroxidase, in cancer cells
    • Gladyshev VN, Factor VM, Housseau F, Hatfield DL. Contrasting patterns of regulation of the antioxidant selenoproteins, thioredoxin reductase and glutathione peroxidase, in cancer cells. Biochem Biophys Res Commun 251: 488-493;1998.
    • (1998) Biochem Biophys Res Commun , vol.251 , pp. 488-493
    • Gladyshev, V.N.1    Factor, V.M.2    Housseau, F.3    Hatfield, D.L.4
  • 42
    • 0032555276 scopus 로고    scopus 로고
    • Human thioredoxin reductase from HeLa cells: Selective alkylation of selenocysteine in the protein inhibits enzyme activity and reduction with NADPH influences affinity to heparin
    • Gorlatov SN, Stadtman TC. Human thioredoxin reductase from HeLa cells: Selective alkylation of selenocysteine in the protein inhibits enzyme activity and reduction with NADPH influences affinity to heparin. Proc Natl Acad Sci USA 95:8520-8525;1998.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 8520-8525
    • Gorlatov, S.N.1    Stadtman, T.C.2
  • 44
    • 0032493647 scopus 로고    scopus 로고
    • Human placenta thioredoxin reductase. Isolation of the selenoenzyme, steady state kinetics, and inhibition by therapeutic gold compounds
    • Gromer S, Arscott LD, Williams CH Jr, Schirmer RH, Becker K. Human placenta thioredoxin reductase. Isolation of the selenoenzyme, steady state kinetics, and inhibition by therapeutic gold compounds. J Biol Chem 273:20096-20101;1998.
    • (1998) J Biol Chem , vol.273 , pp. 20096-20101
    • Gromer, S.1    Arscott, L.D.2    Williams Jr., C.H.3    Schirmer, R.H.4    Becker, K.5
  • 46
    • 0027523260 scopus 로고
    • UGA: A split personality in the universal genetic code
    • Hatfield DL, Diamond AM. UGA: A split personality in the universal genetic code. Trends Genet 9:69-70;1993.
    • (1993) Trends Genet , vol.9 , pp. 69-70
    • Hatfield, D.L.1    Diamond, A.M.2
  • 49
    • 0027369153 scopus 로고
    • Selenium metabolism in microorganisms
    • Heider J, Böck A. Selenium metabolism in microorganisms. Adv Microb Physiol 35:71-109;1993.
    • (1993) Adv Microb Physiol , vol.35 , pp. 71-109
    • Heider, J.1    Böck, A.2
  • 50
    • 0027475803 scopus 로고
    • Conserved nucleotide sequences in the open reading frame and 3′ untranslated region of selenoprotein P mRNA
    • Hill KE, Lloyd RS, Burk RF. Conserved nucleotide sequences in the open reading frame and 3′ untranslated region of selenoprotein P mRNA. Proc Natl Acad Sci USA 90:537-541; 1993.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 537-541
    • Hill, K.E.1    Lloyd, R.S.2    Burk, R.F.3
  • 51
    • 0031230375 scopus 로고    scopus 로고
    • Selenoprotein P: Recent studies in rats and in humans
    • Hill KE, Burk RF. Selenoprotein P: Recent studies in rats and in humans. Biomed Environ Sci 10:198-208;1997.
    • (1997) Biomed Environ Sci , vol.10 , pp. 198-208
    • Hill, K.E.1    Burk, R.F.2
  • 53
    • 0030013634 scopus 로고    scopus 로고
    • Isoforms of Selenoprotein P in rat plasma. Evidence for a full-length form and another form that terminates at the second UGA in the open reading frame
    • Himeno S, Chittum HS, Burk RF. Isoforms of Selenoprotein P in rat plasma. Evidence for a full-length form and another form that terminates at the second UGA in the open reading frame. J Biol Chem 271:15769-15775;1996.
    • (1996) J Biol Chem , vol.271 , pp. 15769-15775
    • Himeno, S.1    Chittum, H.S.2    Burk, R.F.3
  • 54
    • 0030971057 scopus 로고    scopus 로고
    • Mice deficient in cellular glutathione peroxidase develop normally and show no increased sensitivity to hyperoxia
    • Ho YS, Magnenat JL, Bronson RT, Cao J, Gargano M, Sugawara M, Funk CD. Mice deficient in cellular glutathione peroxidase develop normally and show no increased sensitivity to hyperoxia. J Biol Chem 272:16644-16651; 1997.
    • (1997) J Biol Chem , vol.272 , pp. 16644-16651
    • Ho, Y.S.1    Magnenat, J.L.2    Bronson, R.T.3    Cao, J.4    Gargano, M.5    Sugawara, M.6    Funk, C.D.7
  • 56
    • 0017653811 scopus 로고
    • Bovine thioredoxin system. Purification of thioredoxin reductase from calf liver and thymus and studies of its function in disulfide reduction
    • Holmgren A. Bovine thioredoxin system. Purification of thioredoxin reductase from calf liver and thymus and studies of its function in disulfide reduction. J Biol Chem 252:4600-4606; 1977.
    • (1977) J Biol Chem , vol.252 , pp. 4600-4606
    • Holmgren, A.1
  • 58
    • 0000301355 scopus 로고    scopus 로고
    • Fetal mouse selenophosphate synthetase 2 (SPS2): Characterization of the cysteine mutant form overproduced in a baculovirus-insect cell system
    • Kim IY, Guimaraes MJ, Zlotnik A, Bazan JF, Stadtman TC. Fetal mouse selenophosphate synthetase 2 (SPS2): Characterization of the cysteine mutant form overproduced in a baculovirus-insect cell system. Proc Natl Acad Sci USA 94:418-421;1997.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 418-421
    • Kim, I.Y.1    Guimaraes, M.J.2    Zlotnik, A.3    Bazan, J.F.4    Stadtman, T.C.5
  • 59
    • 0031038104 scopus 로고    scopus 로고
    • Cloning and characterization of a novel oxidoreductase KDRF from a human bone marrow-derived stromal cell line KM-102
    • Koishi R, Kawashima I, Yoshimura C, Sugawara M, Serizawa N. Cloning and characterization of a novel oxidoreductase KDRF from a human bone marrow-derived stromal cell line KM-102. J Biol Chem 272:2570-2577;1997.
    • (1997) J Biol Chem , vol.272 , pp. 2570-2577
    • Koishi, R.1    Kawashima, I.2    Yoshimura, C.3    Sugawara, M.4    Serizawa, N.5
  • 60
    • 0031466528 scopus 로고    scopus 로고
    • Cell line-directed screening assay for inhibitors of thioredoxin reductase signaling as potential anti-cancer drugs
    • Kunkel MW, Kirkpatrick DL, Johnson JI, Powis G. Cell line-directed screening assay for inhibitors of thioredoxin reductase signaling as potential anti-cancer drugs. Anticancer Drug Des 12:659-670; 1997.
    • (1997) Anticancer Drug des , vol.12 , pp. 659-670
    • Kunkel, M.W.1    Kirkpatrick, D.L.2    Johnson, J.I.3    Powis, G.4
  • 61
    • 0030610239 scopus 로고    scopus 로고
    • Heparin-binding properties of selenium-containing thioredoxin reductase from HeLa cells and human lung adenocarcinoma cells
    • Liu SY, Stadtman TC. Heparin-binding properties of selenium-containing thioredoxin reductase from HeLa cells and human lung adenocarcinoma cells. Proc Natl Acad Sci USA 94: 6138-6141;1997.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6138-6141
    • Liu, S.Y.1    Stadtman, T.C.2
  • 62
    • 0030975820 scopus 로고    scopus 로고
    • Update on the human iodothyronine selenodeiodinases, the enzymes regulating the activation and inactivation of thyroid hormone
    • Larsen PR. Update on the human iodothyronine selenodeiodinases, the enzymes regulating the activation and inactivation of thyroid hormone. Biochem Soc Trans 25:588-592;1997.
    • (1997) Biochem Soc Trans , vol.25 , pp. 588-592
    • Larsen, P.R.1
  • 64
    • 0023907071 scopus 로고
    • Gene for a novel tRNA species that accepts L-serine and cotranslationally inserts selenocysteine
    • Leinfelder W, Zehelein E, Mandrand-Berthelot MA, Bock A. Gene for a novel tRNA species that accepts L-serine and cotranslationally inserts selenocysteine. Nature 331:723-725; 1988.
    • (1988) Nature , vol.331 , pp. 723-725
    • Leinfelder, W.1    Zehelein, E.2    Mandrand-Berthelot, M.A.3    Bock, A.4
  • 65
    • 0029097629 scopus 로고
    • Cloning and functional characterization of human selenophosphate synthetase, an essential component of selenoprotein synthesis
    • Low SC, Harney JW, Berry MJ. Cloning and functional characterization of human selenophosphate synthetase, an essential component of selenoprotein synthesis. J Biol Chem 270: 21659-21664;1995.
    • (1995) J Biol Chem , vol.270 , pp. 21659-21664
    • Low, S.C.1    Harney, J.W.2    Berry, M.J.3
  • 66
    • 0029894345 scopus 로고    scopus 로고
    • Knowing when not to stop: Selenocysteine incorporation in eukaryotes
    • Low SC, Berry MJ. Knowing when not to stop: Selenocysteine incorporation in eukaryotes. Trends Biochem Sci 21:203-208;1996.
    • (1996) Trends Biochem Sci , vol.21 , pp. 203-208
    • Low, S.C.1    Berry, M.J.2
  • 67
    • 0025331418 scopus 로고
    • Protein disulfideisomerase is a substrate for thioredoxin reductase and has thioredoxin-like activity
    • Lundstrom J, Holmgren A. Protein disulfideisomerase is a substrate for thioredoxin reductase and has thioredoxin-like activity. J Biol Chem 265:9114-9120;1990.
    • (1990) J Biol Chem , vol.265 , pp. 9114-9120
    • Lundstrom, J.1    Holmgren, A.2
  • 68
    • 0028795422 scopus 로고
    • Two resident ER-proteins, CaBP1 and CaBP2, with thioredoxin domains, are substrates for thioredoxin reductase: Comparison with protein disulfide isomerase
    • Lundstrom-Ljung J, Birnbach U, Rupp K, Soling HD, Holmgren A. Two resident ER-proteins, CaBP1 and CaBP2, with thioredoxin domains, are substrates for thioredoxin reductase: Comparison with protein disulfide isomerase. FEBS Lett 357:305-308;1995.
    • (1995) FEBS Lett , vol.357 , pp. 305-308
    • Lundstrom-Ljung, J.1    Birnbach, U.2    Rupp, K.3    Soling, H.D.4    Holmgren, A.5
  • 69
    • 0031689441 scopus 로고    scopus 로고
    • Testosterone mediates expression of the selenoprotein PHGPx by induction of spermatogenesis and not by direct transcriptional gene activation
    • Maiorino M, Wissing JB, Brigelius-Flohe R, Calabrese F, Roveri A, Steinert P, Ursini F, Flohe L. Testosterone mediates expression of the selenoprotein PHGPx by induction of spermatogenesis and not by direct transcriptional gene activation. FASEB J 12:1359-1370;1998.
    • (1998) FASEB J , vol.12 , pp. 1359-1370
    • Maiorino, M.1    Wissing, J.B.2    Brigelius-Flohe, R.3    Calabrese, F.4    Roveri, A.5    Steinert, P.6    Ursini, F.7    Flohe, L.8
  • 70
    • 0014209150 scopus 로고
    • Fine structure of RNA codewords recognized by bacterial, amphibian, and mammalian transfer RNA
    • Marshall RE, Caskey CT, Nirenberg M. Fine structure of RNA codewords recognized by bacterial, amphibian, and mammalian transfer RNA. Science 155:820-826;1967.
    • (1967) Science , vol.155 , pp. 820-826
    • Marshall, R.E.1    Caskey, C.T.2    Nirenberg, M.3
  • 71
    • 0025082801 scopus 로고
    • Inhibition of thioredoxin reductase (E.C. 1.6.4.5.) by antitumor quinones
    • Mau BL, Powis G. Inhibition of thioredoxin reductase (E.C. 1.6.4.5.) by antitumor quinones. Free Radic Res Commun 8:365-372; 1990.
    • (1990) Free Radic Res Commun , vol.8 , pp. 365-372
    • Mau, B.L.1    Powis, G.2
  • 72
    • 0026505778 scopus 로고
    • Inhibition of cellular thioredoxin reductase by diaziquone and doxorubicin. Relationship to the inhibition of cell proliferation and decreased ribonucleotide reductase activity
    • Mau BL, Powis G. Inhibition of cellular thioredoxin reductase by diaziquone and doxorubicin. Relationship to the inhibition of cell proliferation and decreased ribonucleotide reductase activity. Biochem Pharmacol 43:1621-1627; 1992.
    • (1992) Biochem Pharmacol , vol.43 , pp. 1621-1627
    • Mau, B.L.1    Powis, G.2
  • 73
    • 0030611083 scopus 로고    scopus 로고
    • Reduction of dehydroascorbate to ascorbate by the selenoenzyme thioredoxin reductase
    • May JM, Mendiratta S, Hill KE, Burk RF. Reduction of dehydroascorbate to ascorbate by the selenoenzyme thioredoxin reductase. J Biol Chem 272:22607-22610;1997.
    • (1997) J Biol Chem , vol.272 , pp. 22607-22610
    • May, J.M.1    Mendiratta, S.2    Hill, K.E.3    Burk, R.F.4
  • 74
    • 0032483382 scopus 로고    scopus 로고
    • Reduction of the ascorbyl free radical to ascorbate by thioredoxin reductase
    • May JM, Cobb CE, Mendiratta S, Hill KE, Burk RF. Reduction of the ascorbyl free radical to ascorbate by thioredoxin reductase. J Biol Chem 273:23039-23045;1998.
    • (1998) J Biol Chem , vol.273 , pp. 23039-23045
    • May, J.M.1    Cobb, C.E.2    Mendiratta, S.3    Hill, K.E.4    Burk, R.F.5
  • 76
    • 0032080238 scopus 로고    scopus 로고
    • Mammalian thioredoxin reductase is irreversibly inhibited by dinitrohalobenzenes by alkylation of both the redox active selenocysteine and its neighboring cysteine residue
    • Nordberg J, Zhong L, Holmgren A, Arner ES. Mammalian thioredoxin reductase is irreversibly inhibited by dinitrohalobenzenes by alkylation of both the redox active selenocysteine and its neighboring cysteine residue. J Biol Chem 273:10835-10842;1998.
    • (1998) J Biol Chem , vol.273 , pp. 10835-10842
    • Nordberg, J.1    Zhong, L.2    Holmgren, A.3    Arner, E.S.4
  • 77
    • 0032005378 scopus 로고    scopus 로고
    • Controlling your losses: Conditional gene silencing in mammals
    • Porter A. Controlling your losses: Conditional gene silencing in mammals. Trends Genet 14: 73-79;1998.
    • (1998) Trends Genet , vol.14 , pp. 73-79
    • Porter, A.1
  • 78
    • 0028825467 scopus 로고
    • Rat phospholipidhydroperoxide glutathione peroxidase. cDNA cloning and identification of multiple transcription and translation start sites
    • Pushpa-Rekha TR, Burdsall AL, Oleksa LM, Chisolm GM, Driscoll DM. Rat phospholipidhydroperoxide glutathione peroxidase. cDNA cloning and identification of multiple transcription and translation start sites. J Biol Chem 270:26993-26999;1995.
    • (1995) J Biol Chem , vol.270 , pp. 26993-26999
    • Pushpa-Rekha, T.R.1    Burdsall, A.L.2    Oleksa, L.M.3    Chisolm, G.M.4    Driscoll, D.M.5
  • 80
    • 0025049330 scopus 로고
    • Selenium and amino acid composition of selenoprotein P, the major selenoprotein in rat serum
    • Read R, Bellew T, Yang JG, Hill KE, Palmer IS, Burk RF. Selenium and amino acid composition of selenoprotein P, the major selenoprotein in rat serum. J Biol Chem 265:17899-17905;1990.
    • (1990) J Biol Chem , vol.265 , pp. 17899-17905
    • Read, R.1    Bellew, T.2    Yang, J.G.3    Hill, K.E.4    Palmer, I.S.5    Burk, R.F.6
  • 81
    • 0031584269 scopus 로고    scopus 로고
    • The crystal structure of selenoglutathione peroxidase from human plasma at 2.9 A resolution
    • Ren B, Huang W, Akesson B, Ladenstein R. The crystal structure of selenoglutathione peroxidase from human plasma at 2.9 A resolution. J Mol Biol 268:869-885;1997.
    • (1997) J Mol Biol , vol.268 , pp. 869-885
    • Ren, B.1    Huang, W.2    Akesson, B.3    Ladenstein, R.4
  • 82
    • 0031984162 scopus 로고    scopus 로고
    • Purification of mitochondrial thioredoxin reductase and its involvement in the redox regulation of membrane permeability
    • Rigobello MP, Callegaro MT, Barzon E, Benetti M, Bindoli A. Purification of mitochondrial thioredoxin reductase and its involvement in the redox regulation of membrane permeability. Free Radie Biol Med 24:370-376;1998.
    • (1998) Free Radie Biol Med , vol.24 , pp. 370-376
    • Rigobello, M.P.1    Callegaro, M.T.2    Barzon, E.3    Benetti, M.4    Bindoli, A.5
  • 83
    • 0021810653 scopus 로고
    • Immunohistochemical localization of thioredoxin and thioredoxin reductase in adult rats
    • Rozell B, Hansson HA, Luthman M, Holmgren A. Immunohistochemical localization of thioredoxin and thioredoxin reductase in adult rats. Eur J Cell Biol 38:79-86;1985.
    • (1985) Eur J Cell Biol , vol.38 , pp. 79-86
    • Rozell, B.1    Hansson, H.A.2    Luthman, M.3    Holmgren, A.4
  • 84
    • 0028967352 scopus 로고
    • High rates of thioredoxin secretion correlate with growth arrest in hepatoma cells
    • Rubartelli A, Bonifaci N, Sitia R. High rates of thioredoxin secretion correlate with growth arrest in hepatoma cells. Cancer Res 55:675-680; 1995.
    • (1995) Cancer Res , vol.55 , pp. 675-680
    • Rubartelli, A.1    Bonifaci, N.2    Sitia, R.3
  • 85
    • 0029938790 scopus 로고    scopus 로고
    • Molecular biological and biochemical characterization of the human type 2 selenodeiodinase
    • Salvatore D, Bartha T, Harney JW, Larsen PR. Molecular biological and biochemical characterization of the human type 2 selenodeiodinase. Endocrinology 137:3308-3315;1996.
    • (1996) Endocrinology , vol.137 , pp. 3308-3315
    • Salvatore, D.1    Bartha, T.2    Harney, J.W.3    Larsen, P.R.4
  • 88
    • 0001900935 scopus 로고
    • Intracellular glutathione peroxidases - Structure, regulation, and function
    • (Burk RF, ed.) New York, Springer
    • Sunde RA. Intracellular glutathione peroxidases - Structure, regulation, and function. In: (Burk RF, ed.) Selenium in Biology and Human Health. New York, Springer, 146-177; 1994.
    • (1994) Selenium in Biology and Human Health , pp. 146-177
    • Sunde, R.A.1
  • 90
    • 0024461420 scopus 로고
    • ATL-derived factor (ADF), an IL-2 receptor/Tac inducer homologous to thioredoxin; possible involvement of dithiol-reduction in the IL-2 receptor induction
    • Tagaya Y, Maeda Y, Mitsui A, Kondo N, Matsui H, Hamuro J, Brown N, Akai K, Yokota T, Wakasugi H, et al. ATL-derived factor (ADF), an IL-2 receptor/Tac inducer homologous to thioredoxin; possible involvement of dithiol-reduction in the IL-2 receptor induction. EMBO J 8:757-764;1989.
    • (1989) EMBO J , vol.8 , pp. 757-764
    • Tagaya, Y.1    Maeda, Y.2    Mitsui, A.3    Kondo, N.4    Matsui, H.5    Hamuro, J.6    Brown, N.7    Akai, K.8    Yokota, T.9    Wakasugi, H.10
  • 91
    • 0030020576 scopus 로고    scopus 로고
    • A new selenoprotein from human lung adenocarcinoma cells: Purification, properties, and thioredoxin reductase activity
    • Tamura T, Stadtman TC. A new selenoprotein from human lung adenocarcinoma cells: Purification, properties, and thioredoxin reductase activity. Proc Natl Acad Sci USA 93:1006-1011;1996.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1006-1011
    • Tamura, T.1    Stadtman, T.C.2
  • 92
    • 0027933605 scopus 로고
    • A basis for new approaches to the chemotherapy of AIDS: Novel genes in HIV-1 potentially encode selenoproteins expressed by ribosomal frameshifting and termination suppression
    • Taylor EW, Ramanathan CS, Jalluri RK, Nadimpalli RG. A basis for new approaches to the chemotherapy of AIDS: Novel genes in HIV-1 potentially encode selenoproteins expressed by ribosomal frameshifting and termination suppression. J Med Chem 37:2637-2654;1994.
    • (1994) J Med Chem , vol.37 , pp. 2637-2654
    • Taylor, E.W.1    Ramanathan, C.S.2    Jalluri, R.K.3    Nadimpalli, R.G.4
  • 93
    • 0031225515 scopus 로고    scopus 로고
    • Phospholipid hydroperoxide glutathione peroxidase (PHGPx): More than an antioxidant enzyme?
    • Ursini F, Maiorino M, Roveri A. Phospholipid hydroperoxide glutathione peroxidase (PHGPx): More than an antioxidant enzyme? Biomed Environ Sci 10:327-332;1997.
    • (1997) Biomed Environ Sci , vol.10 , pp. 327-332
    • Ursini, F.1    Maiorino, M.2    Roveri, A.3
  • 95
    • 0029112942 scopus 로고
    • Cell cycle inhibition of HTLV-I transformed T cell lines by retinoic acid: The possible therapeutic use of thioredoxin reductase inhibitors
    • U-Taniguchi Y, Furuke K, Masutani H, Nakamura H, Yodoi J. Cell cycle inhibition of HTLV-I transformed T cell lines by retinoic acid: The possible therapeutic use of thioredoxin reductase inhibitors. Oncol Res 7:183-189; 1995.
    • (1995) Oncol Res , vol.7 , pp. 183-189
    • U-Taniguchi, Y.1    Furuke, K.2    Masutani, H.3    Nakamura, H.4    Yodoi, J.5
  • 98
    • 0028144791 scopus 로고
    • A purified selenophosphate-dependent enzyme from Salmonella typhimurium catalyzes the replacement of sulfur in 2-thiouridine residues in tRNAs with selenium
    • Veres Z, Stadtman TC. A purified selenophosphate-dependent enzyme from Salmonella typhimurium catalyzes the replacement of sulfur in 2-thiouridine residues in tRNAs with selenium. Proc Natl Acad Sci USA 91: 8092-8096;1994.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8092-8096
    • Veres, Z.1    Stadtman, T.C.2
  • 99
    • 0029805895 scopus 로고    scopus 로고
    • A novel RNA structural motif in the selenocysteine insertion element of eukaryotic selenoprotein mRNAs
    • Walczak R, Hubert N, Carbon P, Krol A. A novel RNA structural motif in the selenocysteine insertion element of eukaryotic selenoprotein mRNAs. RNA 2:367-379;1996.
    • (1996) RNA , vol.2 , pp. 367-379
    • Walczak, R.1    Hubert, N.2    Carbon, P.3    Krol, A.4
  • 100
    • 0032475832 scopus 로고    scopus 로고
    • The Human Genome Project: Reaching the finish line
    • Waterston R, Sulston JE. The Human Genome Project: Reaching the finish line. Science 282:53-54;1998.
    • (1998) Science , vol.282 , pp. 53-54
    • Waterston, R.1    Sulston, J.E.2
  • 102
    • 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, Arner ES, 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 273:8581-8591;1998.
    • (1998) J Biol Chem , vol.273 , pp. 8581-8591
    • Zhong, L.1    Arner, E.S.2    Ljung, J.3    Aslund, F.4    Holmgren, A.5
  • 103
    • 0001256080 scopus 로고
    • Nucleolide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogenlyase-linked) from Escherichia coli
    • Zinoni F, Birkmann A, Stadtman TC, Böck A. Nucleolide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogenlyase-linked) from Escherichia coli. Proc Natl Acad Sci USA 83:4650-4654;1986.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 4650-4654
    • Zinoni, F.1    Birkmann, A.2    Stadtman, T.C.3    Böck, A.4
  • 104
    • 84878720782 scopus 로고    scopus 로고
    • http://www.ncbi.nlm.nih.gov/ncicgap/expression_tech_info.html, 11/06/98.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.