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Volumn 261, Issue 2, 1999, Pages 405-412

Human mitochondrial thioredoxin reductase. cDNA cloning, expression and genomic organization

Author keywords

CDNA cloning; Genomic organization; Mitochondria; Thioredoxin reductase

Indexed keywords

HYBRID PROTEIN; MESSENGER RNA; MITOCHONDRIAL ENZYME; THIOREDOXIN REDUCTASE;

EID: 0033561016     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00286.x     Document Type: Article
Times cited : (152)

References (49)
  • 2
    • 78651146370 scopus 로고
    • Enzymatic synthesis of deoxyribonucleotides. Isolation and characterization of thioredoxin, the hydrogen donor from E. coli
    • 2. Laurent, T.C., Moore, E.C. & Reichard, P. (1964) Enzymatic synthesis of deoxyribonucleotides. Isolation and characterization of thioredoxin, the hydrogen donor from E. coli. 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
  • 3
    • 0026715172 scopus 로고
    • Thioredoxin regulates the DNA binding activity of NF-kappa B by reduction of a disulphide bond involving cysteine 62
    • 3. Matthews, J.R., Wakasugi, N., Virelizier, J.L., Yodoi, J. & Hay, R.T. (1992) Thioredoxin regulates the DNA binding activity of NF-kappa B by reduction of a disulphide bond involving cysteine 62. Nucleic Acids Res. 20, 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
  • 4
    • 0031302910 scopus 로고    scopus 로고
    • Elevation of manganese superoxide dismutase gene expression by thioredoxin
    • 4. Das, K.C., Lewis-Molock, Y. & White, C.W. (1997) Elevation of manganese superoxide dismutase gene expression by thioredoxin. Am. J. Respir. Cell Mol. Biol. 17, 713-726.
    • (1997) Am. J. Respir. Cell Mol. Biol. , vol.17 , pp. 713-726
    • Das, K.C.1    Lewis-Molock, Y.2    White, C.W.3
  • 6
    • 0022457811 scopus 로고
    • The role of thioredoxin reductase in the reduction of free radicals at the surface of the epidermis
    • 6. Schallreuter, K.U. & Wood, J.M. (1986) The role of thioredoxin reductase in the reduction of free radicals at the surface of the epidermis. Biochem. Biophys. Res. Commun. 136, 630-637.
    • (1986) Biochem. Biophys. Res. Commun. , vol.136 , pp. 630-637
    • Schallreuter, K.U.1    Wood, J.M.2
  • 7
    • 0028106431 scopus 로고
    • Adult T cell leukemia-derived factor/human thioredoxin protects endothelial F-2 cell injury caused by activated neutrophils or hydrogen peroxide
    • 7. Nakamura, H., Matsuda, M., Furuke, K., Kitaoka, Y., Iwata, S., Toda, K., Tnamoto, T., Yamaoka, Y., Ozawa, K. & Yodoi, J. (1994) Adult T cell leukemia-derived factor/human thioredoxin protects endothelial F-2 cell injury caused by activated neutrophils or hydrogen peroxide. Immunol. Lett. 42, 75-80.
    • (1994) Immunol. Lett. , vol.42 , pp. 75-80
    • Nakamura, H.1    Matsuda, M.2    Furuke, K.3    Kitaoka, Y.4    Iwata, S.5    Toda, K.6    Tnamoto, T.7    Yamaoka, Y.8    Ozawa, K.9    Yodoi, J.10
  • 8
    • 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
    • 8. Wakasugi, N., Tagaya, Y., Wakasugi, H., Mitsui, A., Maeda, M., Yodoi, J. & Tursz, T. (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, 8282-8286.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 8282-8286
    • Wakasugi, N.1    Tagaya, Y.2    Wakasugi, H.3    Mitsui, A.4    Maeda, M.5    Yodoi, J.6    Tursz, T.7
  • 9
    • 0028818288 scopus 로고
    • Cell growth stimulation by the redox protein thioredoxin occurs by a novel helper mechanism
    • 9. Gasdaska, J.R., Berggren, M. & Powis, G. (1995) Cell growth stimulation by the redox protein thioredoxin occurs by a novel helper mechanism. Cell Growth Differ. 6, 1643-1650.
    • (1995) Cell Growth Differ , vol.6 , pp. 1643-1650
    • Gasdaska, J.R.1    Berggren, M.2    Powis, G.3
  • 10
    • 0020488534 scopus 로고
    • Rat liver thioredoxin and thioredoxin reductase: Purification and characterization
    • 10. Luthman, M. & Holmgren, A. (1982) Rat liver thioredoxin and thioredoxin reductase: purification and characterization. Biochemistry 21, 6628-6633.
    • (1982) Biochemistry , vol.21 , pp. 6628-6633
    • Luthman, M.1    Holmgren, A.2
  • 11
    • 0025331418 scopus 로고
    • Protein disulfide-isomerase is a substrate for thioredoxin reductase and has thioredoxin-like activity
    • 11. 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
  • 12
    • 0029876379 scopus 로고    scopus 로고
    • NK-lysin, a disulfide-containing effector peptide of T-lymphocytes, is reduced and inactivated by human thioredoxin reductase
    • 12. Andersson, M., Holmgren, A. & Spyrou, G. (1996) NK-lysin, a disulfide-containing effector peptide of T-lymphocytes, is reduced and inactivated by human thioredoxin reductase. J. Biol. Chem. 271, 10116-10120.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10116-10120
    • Andersson, M.1    Holmgren, A.2    Spyrou, G.3
  • 13
    • 0029187491 scopus 로고
    • Thioredoxin and thioredoxin reductase
    • 13. Holmgren, A. & Björnstedt, M. (1995) Thioredoxin and thioredoxin reductase. Methods Enzymol. 252, 199-208.
    • (1995) Methods Enzymol. , vol.252 , pp. 199-208
    • Holmgren, A.1    Björnstedt, M.2
  • 14
    • 0030570764 scopus 로고    scopus 로고
    • Efficient reduction of lipoamide and lipoic acid by mammalian thioredoxin reductase
    • 14. Arnér, E.S.J., Nordberg, J. & Holmgren, A. (1997) Efficient reduction of lipoamide and lipoic acid by mammalian thioredoxin reductase. Biochem. Biophys. Res. Commun. 225, 268-274.
    • (1997) Biochem. Biophys. Res. Commun. , vol.225 , pp. 268-274
    • Arnér, E.S.J.1    Nordberg, J.2    Holmgren, A.3
  • 15
    • 0029031370 scopus 로고
    • Human thioredoxin reductase directly reduces lipid hydroperoxydes by NADPH and selenocystine strongly stimulates the reaction via catalytically generated selenols
    • 15. Björnstedt, M., Hamberg, M., Kumar, S., Xue, J. & Holmgren, A. (1995) Human thioredoxin reductase directly reduces lipid hydroperoxydes by NADPH and selenocystine strongly stimulates the reaction via catalytically generated selenols. J. Biol. Chem. 270, 11761-11764.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11761-11764
    • Björnstedt, M.1    Hamberg, M.2    Kumar, S.3    Xue, J.4    Holmgren, A.5
  • 16
    • 0028139014 scopus 로고
    • The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase
    • 16. Björnstedt, M., Xue, J., Huang, W., Åkesson, B. & Holmgren, A. (1994) The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase. J. Biol. Chem. 269, 29382-29384.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29382-29384
    • Björnstedt, M.1    Xue, J.2    Huang, W.3    Åkesson, B.4    Holmgren, A.5
  • 17
    • 0029142578 scopus 로고
    • Cloning and sequencing of a human thioredoxin reductase
    • 17. Gasdaska, P.Y., Gasdaska, J.R., Cochran, S. & Powis, G. (1995) Cloning and sequencing of a human thioredoxin reductase. FEBS Lett. 373, 5-9.
    • (1995) FEBS Lett. , vol.373 , pp. 5-9
    • Gasdaska, P.Y.1    Gasdaska, J.R.2    Cochran, S.3    Powis, G.4
  • 18
    • 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
    • 18. Zhong, L., Arner, E.S.J., Ljung, J., Åslund, F. & Holmgren, A. (1998) 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) J. Biol. Chem. , vol.273 , pp. 8581-8591
    • Zhong, L.1    Arner, E.S.J.2    Ljung, J.3    Åslund, F.4    Holmgren, A.5
  • 19
    • 0030020576 scopus 로고    scopus 로고
    • A new sclenoprotein from human lung adenocarcinoma cell: Purification, properties and thioredoxin activity
    • 19. Tamura, T. & Stadtman, T.C. (1996) A new sclenoprotein from human lung adenocarcinoma cell: purification, properties and thioredoxin activity. Proc. Natl Acad. Sci. USA 93, 1006-1011.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 1006-1011
    • Tamura, T.1    Stadtman, T.C.2
  • 20
    • 0029973142 scopus 로고    scopus 로고
    • Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, correspond to TGA in the human placental gene
    • 20. Gladyshev, V.N., Jeang, K.-T. & Stadtman, T.C. (1996) Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, correspond to TGA in the human placental gene. Proc. Natl Acad. Sci. USA 93, 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
  • 22
    • 0031182337 scopus 로고    scopus 로고
    • The novel oxidoreductase KDRF (KM-102-derived reductase-like factor) is identical with human thioredoxin reductase
    • 22. Miranda-Vizuete, A. & Spyrou, G. (1997) The novel oxidoreductase KDRF (KM-102-derived reductase-like factor) is identical with human thioredoxin reductase. Biochem. J. 325, 287-288.
    • (1997) Biochem. J. , vol.325 , pp. 287-288
    • Miranda-Vizuete, A.1    Spyrou, G.2
  • 23
    • 0029894345 scopus 로고    scopus 로고
    • Knowing when not to stop: Selenocysteine incorporation in eukaryotes
    • 23. Low, S.C. & Berry, M.J. (1996) Knowing when not to stop: selenocysteine incorporation in eukaryotes. Trends Biochem. Sci. 21, 203-208.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 203-208
    • Low, S.C.1    Berry, M.J.2
  • 24
  • 25
    • 0032080238 scopus 로고    scopus 로고
    • Mammalian thioredoxin reductase is irreversibly inhibited by dinitrohalonenzenes by alkylation of both the redox active selenocysteine and its neighboring cysteine residue
    • 25. Nordberg, J., Zhong, L., Holmgren, A. & Arner, E.S.J. (1998) Mammalian thioredoxin reductase is irreversibly inhibited by dinitrohalonenzenes by alkylation of both the redox active selenocysteine and its neighboring cysteine residue. J. Biol. Chem. 273, 10835-10842.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10835-10842
    • Nordberg, J.1    Zhong, L.2    Holmgren, A.3    Arner, E.S.J.4
  • 26
    • 0032555276 scopus 로고    scopus 로고
    • Human thioredoxin reductase from HeLa cells: Selective alkylation of selenocysteine in the pretien inhibits enzyme activity and reduction with NADPH influences affinity to heparin
    • 26. Gorlatov, S.N. & Stadtman, T.C. (1998) Human thioredoxin reductase from HeLa cells: selective alkylation of selenocysteine in the pretien inhibits enzyme activity and reduction with NADPH influences affinity to heparin. Proc. Natl Acad. Sci. USA 95, 8520-8525.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 8520-8525
    • Gorlatov, S.N.1    Stadtman, T.C.2
  • 27
    • 0030887844 scopus 로고    scopus 로고
    • The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanis of thioredoxin reductase from Escherichia coli
    • 27. Arscott, L.D., Gromer, S., Schirmer, R.H., Becker, K. & Williams, C.H.J. (1997) The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanis of thioredoxin reductase from Escherichia coli. Proc. Natl Acad. Sci. USA 94, 3621-3626.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 3621-3626
    • Arscott, L.D.1    Gromer, S.2    Schirmer, R.H.3    Becker, K.4    Williams, C.H.J.5
  • 30
    • 0030213227 scopus 로고    scopus 로고
    • Interpreting cDNA sequences: Some insights from studies on translation
    • 30. Kozak, M. (1996) Interpreting cDNA sequences: some insights from studies on translation. Mamm. Genome 7, 563-574.
    • (1996) Mamm. Genome , vol.7 , pp. 563-574
    • Kozak, M.1
  • 31
    • 0028395670 scopus 로고
    • Transport of proteins across mitochondrial membranes
    • 31. Neupert, W. (1994) Transport of proteins across mitochondrial membranes. Clin. Invest. 72, 251-261.
    • (1994) Clin. Invest. , vol.72 , pp. 251-261
    • Neupert, W.1
  • 32
    • 0024688488 scopus 로고
    • Survey of aminoterminal proteolytic cleavage sites in mitochondrial precursor proteins: Leader peptides cleaved by two matrix proteases share a three-amino acid motif
    • 32. Hendrick, J.P., Hodges, P.E. & Rosenberg, L.E. (1989) Survey of aminoterminal proteolytic cleavage sites in mitochondrial precursor proteins: leader peptides cleaved by two matrix proteases share a three-amino acid motif. Proc. Natl Acad. Sci. USA 86, 4056-4060.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 4056-4060
    • Hendrick, J.P.1    Hodges, P.E.2    Rosenberg, L.E.3
  • 33
    • 0019363396 scopus 로고
    • Organization and expression of eucaryotic split genes coding for proteins
    • 33. Breathnach, R. & Chambon, P. (1981) Organization and expression of eucaryotic split genes coding for proteins. Annu. Rev. Biochem. 50, 349-383.
    • (1981) Annu. Rev. Biochem. , vol.50 , pp. 349-383
    • Breathnach, R.1    Chambon, P.2
  • 34
    • 0025348834 scopus 로고
    • Evolutionary and biosynthetic aspects of aspartate aminotransferase isoenzymes and other aminotransferases
    • 34. Christen, P., Jaussi, R., Juretic, N., Mehta, P.K., Hale, T.I. & Ziak, M. (1990) Evolutionary and biosynthetic aspects of aspartate aminotransferase isoenzymes and other aminotransferases. Ann. NY Acad. Sci. 585, 331-338.
    • (1990) Ann. NY Acad. Sci. , vol.585 , pp. 331-338
    • Christen, P.1    Jaussi, R.2    Juretic, N.3    Mehta, P.K.4    Hale, T.I.5    Ziak, M.6
  • 35
    • 0039080152 scopus 로고
    • Do exons code for structural or functional units in proteins?
    • 35. Traut, T.W. (1988) Do exons code for structural or functional units in proteins? Proc. Natl Acad. Sci. USA 85, 2944-2948.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 2944-2948
    • Traut, T.W.1
  • 36
    • 0030588144 scopus 로고    scopus 로고
    • Human thioredoxin reductase gene localization to chromosomal position 12q23-q24.1 and mRNA distribution in human tissue
    • 36. Gasdaska, J.R., Gasdaska, P.Y., Gallegos, A. & Powis, G. (1996) Human thioredoxin reductase gene localization to chromosomal position 12q23-q24.1 and mRNA distribution in human tissue. Genomics 37, 257-259.
    • (1996) Genomics , vol.37 , pp. 257-259
    • Gasdaska, J.R.1    Gasdaska, P.Y.2    Gallegos, A.3    Powis, G.4
  • 37
    • 0031038104 scopus 로고    scopus 로고
    • Cloning and characterization of a novel oxidoreductase KDRF from a human bone marrow-derived stromal cell line KM-102
    • 37. Koishi, R., Kawashima, I., Yoshimura, C., Sugawara, M. & Serizawa, N. (1997) 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) J. Biol. Chem. , vol.272 , pp. 2570-2577
    • Koishi, R.1    Kawashima, I.2    Yoshimura, C.3    Sugawara, M.4    Serizawa, N.5
  • 38
    • 0029311281 scopus 로고
    • Chimeric green fluorescent protein as a tool for visualizing subcellular organelles in living cells
    • 38. Rizzuto, R., Brini, M., Pizzo, P., Murgia, M. & Pozzan, T. (1995) Chimeric green fluorescent protein as a tool for visualizing subcellular organelles in living cells. Curr. Biol. 5, 635-642.
    • (1995) Curr. Biol. , vol.5 , pp. 635-642
    • Rizzuto, R.1    Brini, M.2    Pizzo, P.3    Murgia, M.4    Pozzan, T.5
  • 40
    • 0031984162 scopus 로고    scopus 로고
    • Purification of mitochondrial thioredoxin reductase and its involvement in the redox regulation of membrane permeability
    • 40. Rigobello, M.P., Callegaro, M.T., Barzon, E., Benetti, M. & Bindoli, A. (1998) Purification of mitochondrial thioredoxin reductase and its involvement in the redox regulation of membrane permeability. Free Rad. Biol. Med. 24, 370-376.
    • (1998) Free Rad. Biol. Med. , vol.24 , pp. 370-376
    • Rigobello, M.P.1    Callegaro, M.T.2    Barzon, E.3    Benetti, M.4    Bindoli, A.5
  • 41
    • 0018784261 scopus 로고
    • Keilin's respiratory chain concept and its chemiosmotic consequences
    • 41. Mitchell, P. (1979) Keilin's respiratory chain concept and its chemiosmotic consequences. Science 206, 1148-1159.
    • (1979) Science , vol.206 , pp. 1148-1159
    • Mitchell, P.1
  • 43
    • 0032493647 scopus 로고    scopus 로고
    • Human placenta thioredoxin reductase. Isolation of the selenoenzyme, steady state kinetics and inhibition by therapeutic gold compounds
    • 43. Gromer, S., Arscott, L.D., Williams, C.H.J., Schirmer, R.H. & Becker, K. (1998) Human placenta thioredoxin reductase. Isolation of the selenoenzyme, steady state kinetics and inhibition by therapeutic gold compounds. J. Biol. Chem. 273, 20096-20101.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20096-20101
    • Gromer, S.1    Arscott, L.D.2    Williams, C.H.J.3    Schirmer, R.H.4    Becker, K.5
  • 44
    • 0000301355 scopus 로고    scopus 로고
    • Fetal mouse selenophosphate synthetase 2 (SPS2): Characterization of the cysteine mutant form overproduced in a baulovirus-insect cell system
    • 44. Kim, I.Y., Guimaraes, M.J., Zlotnik, A., Bazan, J.F. & Stadtman, T.C. (1997) Fetal mouse selenophosphate synthetase 2 (SPS2): characterization of the cysteine mutant form overproduced in a baulovirus-insect cell system. Proc. Natl Acad. Sci. USA 94, 418-421.
    • (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
  • 45
    • 0029082801 scopus 로고
    • Possible function of SP-22, a substrate of mitochondrial ATP-dependent protease, as a radical scavenger
    • 45. Watabe, S., Hasegawa, H., Takimoto, K., Yamamoto, Y. & Takahashi, Y. (1995) Possible function of SP-22, a substrate of mitochondrial ATP-dependent protease, as a radical scavenger. Biochem. Biophys. Res. Commun. 213, 1010-1016.
    • (1995) Biochem. Biophys. Res. Commun. , vol.213 , pp. 1010-1016
    • Watabe, S.1    Hasegawa, H.2    Takimoto, K.3    Yamamoto, Y.4    Takahashi, Y.5
  • 46
    • 0028000994 scopus 로고
    • Coaxial stacking of helixes enhances binding of oligoribonucleotides and improves predictions of RNA folding
    • 46. Walter, A.E., Turner, D.H., Kim, J., Lyttle, M.H., Muller, P., Matthews, D.H. & Zuker, M. (1994) Coaxial stacking of helixes enhances binding of oligoribonucleotides and improves predictions of RNA folding. Proc. Natl Acad. Sci. USA 91, 9218-9222.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 9218-9222
    • Walter, A.E.1    Turner, D.H.2    Kim, J.3    Lyttle, M.H.4    Muller, P.5    Matthews, D.H.6    Zuker, M.7
  • 47
    • 0025361744 scopus 로고
    • Cloning and sequencing of mammalian glutathione reductase cDNA
    • 47. Tutic, M., Lu, X., Schirmer, R.H. & Werner, D. (1990) Cloning and sequencing of mammalian glutathione reductase cDNA. Eur. J. Biochem. 188, 523-528.
    • (1990) Eur. J. Biochem. , vol.188 , pp. 523-528
    • Tutic, M.1    Lu, X.2    Schirmer, R.H.3    Werner, D.4
  • 48
    • 0032898734 scopus 로고    scopus 로고
    • Cloning, sequencing and functional expression of a novel human thioredoxin reductase
    • 48. Gasdaska, P.Y., Berggren, M.M., Berry, M.J. & Powis, G. (1999) Cloning, sequencing and functional expression of a novel human thioredoxin reductase. FEBS Lett. 442, 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
  • 49
    • 0033582515 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a mitochondrial selenocysteine-containing thioredoxin reductase from rat liver
    • 49. Lee, S.-R., Kim, J.-R., Kwon, K.-S., Yoon, H.W., Levine, R.L., Ginsburg, A. & Rhee, S.G. (1999) Molecular cloning and characterization of a mitochondrial selenocysteine-containing thioredoxin reductase from rat liver. J. Biol. Chem. 274, 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


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