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Volumn 384, Issue 3, 2003, Pages 463-472

A putative gluatathione peroxidase of Drosophila encodes a thioredoxin peroxidase that provides resistance against oxidative stress but fails to complement a lack of catalase activity

Author keywords

Aging; Antioxidant; Hydrogen peroxide; Oenocytes; ROS

Indexed keywords

ANTIOXIDANT; CATALASE; GLUTATHIONE PEROXIDASE; HYDROGEN PEROXIDE; REACTIVE OXYGEN METABOLITE; THIOL DERIVATIVE; THIOREDOXIN PEROXIDASE; PARAQUAT; PEROXIDASE; PEROXIREDOXIN; TUMOR PROTEIN;

EID: 0037729054     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2003.052     Document Type: Review
Times cited : (66)

References (65)
  • 2
    • 0023897899 scopus 로고
    • Antioxidant enzymes of larvae of the cabbage looper moth, Trichoplusia ni: Subcellular distribution and activities of superoxide dismutase, catalase and glutathione reductase
    • Ahmad, S., Pritsos, C. A., Bowen, S. M., Heisler, C. R., Blomquist, G. J., and Pardini, R. S. (1988). Antioxidant enzymes of larvae of the cabbage looper moth, Trichoplusia ni: subcellular distribution and activities of superoxide dismutase, catalase and glutathione reductase. Free Radic. Res. Commun. 4, 403-408.
    • (1988) Free Radic. Res. Commun. , vol.4 , pp. 403-408
    • Ahmad, S.1    Pritsos, C.A.2    Bowen, S.M.3    Heisler, C.R.4    Blomquist, G.J.5    Pardini, R.S.6
  • 3
    • 0021105370 scopus 로고
    • Effect of catalase inactivation on levels of inorganic peroxides, superoxide dismutase, glutathione, oxygen consumption and life span in adult houseflies (Musca domestica)
    • Allen, R. G., Farmer, K. J., and Sohal, R. S. (1983). Effect of catalase inactivation on levels of inorganic peroxides, superoxide dismutase, glutathione, oxygen consumption and life span in adult houseflies (Musca domestica). Biochem. J. 216, 503-506.
    • (1983) Biochem. J. , vol.216 , pp. 503-506
    • Allen, R.G.1    Farmer, K.J.2    Sohal, R.S.3
  • 4
    • 0032841705 scopus 로고    scopus 로고
    • Disruption of selenoprotein biosynthesis affects cell proliferation in the imaginal discs and brain of Drosophila melanogaster
    • Alsina, B., Corominas, M., Berry, M. J., Baguna, J., and Serras, F. (1999). Disruption of selenoprotein biosynthesis affects cell proliferation in the imaginal discs and brain of Drosophila melanogaster. J. Cell Sci. 112, 2875-2884.
    • (1999) J. Cell Sci. , vol.112 , pp. 2875-2884
    • Alsina, B.1    Corominas, M.2    Berry, M.J.3    Baguna, J.4    Serras, F.5
  • 5
    • 0035823498 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae expresses three phospholipid hydroperoxide glutathione peroxidases
    • Avery, A. M. and Avery, S. V. (2001). Saccharomyces cerevisiae expresses three phospholipid hydroperoxide glutathione peroxidases. J. Biol. Chem. 276, 33730-33735.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33730-33735
    • Avery, A.M.1    Avery, S.V.2
  • 6
    • 0035188896 scopus 로고    scopus 로고
    • Overexpression of wild type and Secys/Cys mutant of human thioredoxin reductase in E. coli: The role of selenocysteine in the catalytic activity
    • Bar-Noy, S., Gorlatov, S. N., and Stadtman, T. C. (2001) Overexpression of wild type and Secys/Cys mutant of human thioredoxin reductase in E. coli: the role of selenocysteine in the catalytic activity. Free Radic. Biol. Med. 30, 51-61.
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 51-61
    • Bar-Noy, S.1    Gorlatov, S.N.2    Stadtman, T.C.3
  • 7
    • 0037124040 scopus 로고    scopus 로고
    • Thioredoxin-2 but not thioredoxin-1 is a substrate of thioredoxin peroxidase-1 from Drosophila melanogaster: Isolation and characterization of a second thioredoxin in D. Melanogaster and evidence for distinct biological functions of Trx-1 and Trx-2
    • Bauer, H., S. M. Kanzok, and Schirmer, R. H. (2002). Thioredoxin-2 but not thioredoxin-1 is a substrate of thioredoxin peroxidase-1 from Drosophila melanogaster: isolation and characterization of a second thioredoxin in D. Melanogaster and evidence for distinct biological functions of Trx-1 and Trx-2. J. Biol. Chem. 277, 17457-17463.
    • (2002) J. Biol. Chem. , vol.277 , pp. 17457-17463
    • Bauer, H.1    Kanzok, S.M.2    Schirmer, R.H.3
  • 8
    • 0033775650 scopus 로고    scopus 로고
    • Thioredoxin reductase as a pathophysiological factor and drug target
    • Becker, K., Gromer, S., Schirmer, R. H., and Muller, S. (2000). Thioredoxin reductase as a pathophysiological factor and drug target. Eur. J. Biochem. 267, 6118-6125.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6118-6125
    • Becker, K.1    Gromer, S.2    Schirmer, R.H.3    Muller, S.4
  • 9
    • 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., and 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
    • Bjornstedt, M.1    Xue, J.2    Huang, W.3    Akesson, B.4    Holmgren, A.5
  • 10
    • 0027160708 scopus 로고
    • Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
    • Brand, A. H. and Perrimon, N. (1993). Targeted gene expression as a means of altering cell fates and generating dominant phenotypes. Development 118, 401-415.
    • (1993) Development , vol.118 , pp. 401-415
    • Brand, A.H.1    Perrimon, N.2
  • 11
    • 0033230807 scopus 로고    scopus 로고
    • Tissue-specific functions of individual glutathione peroxidases
    • Brigelius-Flohé, R. (1999). Tissue-specific functions of individual glutathione peroxidases. Free Radic. Biol. Med. 27, 951-965.
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 951-965
    • Brigelius-Flohé, R.1
  • 12
    • 0003517672 scopus 로고
    • The Embryonic Development of Drosophila melanogaster
    • (Heidelberg, Germany: Springer Verlag)
    • Campos-Ortega, J. A. and Hartenstein, V. (1985). The Embryonic Development of Drosophila melanogaster (Heidelberg, Germany: Springer Verlag).
    • (1985)
    • Campos-Ortega, J.A.1    Hartenstein, V.2
  • 13
    • 0033767925 scopus 로고    scopus 로고
    • Roles of the glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress
    • Carmel-Harel, O. and Storz, G. (2000). Roles of the glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress. Annu. Rev. Microbiol. 54, 439-461.
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 439-461
    • Carmel-Harel, O.1    Storz, G.2
  • 14
    • 0028072911 scopus 로고
    • Thioredoxin-dependent peroxide reductase from yeast
    • Chae, H. Z., Chung, S. J., and Rhee, S. G. (1994). Thioredoxin-dependent peroxide reductase from yeast. J. Biol. Chem. 269, 27670-27678.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27670-27678
    • Chae, H.Z.1    Chung, S.J.2    Rhee, S.G.3
  • 15
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance, B., Sies, H., and Boveris, A. (1979). Hydroperoxide metabolism in mammalian organs. Physiol. Rev. 59, 527-605.
    • (1979) Physiol. Rev. , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 17
    • 0030906652 scopus 로고    scopus 로고
    • Genetic feminization of pheromones and its behavioral consequences in Drosophila males
    • Ferveur, J. F., Savarit, F., O'Kane, C. J., Sureau, G., Greenspan, R. J., and Jallon, J. M. (1997). Genetic feminization of pheromones and its behavioral consequences in Drosophila males. Science 276, 1555-1558.
    • (1997) Science , vol.276 , pp. 1555-1558
    • Ferveur, J.F.1    Savarit, F.2    O'Kane, C.J.3    Sureau, G.4    Greenspan, R.J.5    Jallon, J.M.6
  • 18
    • 0030820697 scopus 로고    scopus 로고
    • Genetic analysis of stomatogastric nervous system development in Drosophila using enhancer trap lines
    • Forjanic, J. P., Chen, C. K., Jäckle, H., and Gonzalez Gaitan, M. (1997). Genetic analysis of stomatogastric nervous system development in Drosophila using enhancer trap lines. Dev. Biol. 186, 139-154.
    • (1997) Dev. Biol. , vol.186 , pp. 139-154
    • Forjanic, J.P.1    Chen, C.K.2    Jäckle, H.3    Gonzalez Gaitan, M.4
  • 19
    • 0029929731 scopus 로고    scopus 로고
    • Molecular characterization of the glutathione peroxidase gene of the human malaria parasite Plasmodium falciparum
    • Gamain, B., Langsley, G., Fourmaux, M. N., Touzel, J. P., Camus, D., Dive, D., and Slomianny, C. (1996). Molecular characterization of the glutathione peroxidase gene of the human malaria parasite Plasmodium falciparum. Mol. Biochem. Parasitol. 78, 237-248.
    • (1996) Mol. Biochem. Parasitol. , vol.78 , pp. 237-248
    • Gamain, B.1    Langsley, G.2    Fourmaux, M.N.3    Touzel, J.P.4    Camus, D.5    Dive, D.6    Slomianny, C.7
  • 20
    • 0031821531 scopus 로고    scopus 로고
    • Lipid hydroperoxide generation, turnover, and effector action in biological systems
    • Girotti, A. W. (1998). Lipid hydroperoxide generation, turnover, and effector action in biological systems. J. Lipid. Res. 39, 1529-1542.
    • (1998) J. Lipid. Res. , vol.39 , pp. 1529-1542
    • Girotti, A.W.1
  • 21
    • 0034304490 scopus 로고    scopus 로고
    • Tip cell-derived RTK signaling initiates cell movements in the Drosophila stomato-gastric nervous system anlage
    • Gonzalez-Gaitan, M. and Jäckle, H. (2000). Tip cell-derived RTK signaling initiates cell movements in the Drosophila stomato-gastric nervous system anlage. EMBO Rep. 1, 366-371.
    • (2000) EMBO Rep. , vol.1 , pp. 366-371
    • Gonzalez-Gaitan, M.1    Jäckle, H.2
  • 23
    • 0027284743 scopus 로고
    • Molecular characterization and rescue of acatalasemic mutants of Drosophila melanogaster
    • Griswold, C. M., Matthews, A. L., Bewley, K. E., and Mahaffey, J. W. (1993). Molecular characterization and rescue of acatalasemic mutants of Drosophila melanogaster. Genetics 134, 781-788.
    • (1993) Genetics , vol.134 , pp. 781-788
    • Griswold, C.M.1    Matthews, A.L.2    Bewley, K.E.3    Mahaffey, J.W.4
  • 25
    • 0021259320 scopus 로고
    • Transformation of white locus DNA in Drosophila: Dosage compensation, zeste interaction, and position effects
    • Hazelrigg, T., Levis, R., and Rubin, G. M. (1984). Transformation of white locus DNA in Drosophila: dosage compensation, zeste interaction, and position effects. Cell 36, 469-481.
    • (1984) Cell , vol.36 , pp. 469-481
    • Hazelrigg, T.1    Levis, R.2    Rubin, G.M.3
  • 26
    • 0034328891 scopus 로고    scopus 로고
    • The class 2 selenophosphate synthetase gene of Drosophila contains a functional mammalian-type SECIS
    • Hirosawa-Takamori, M., Jäckle, H., and Vorbruggen, G. (2000). The class 2 selenophosphate synthetase gene of Drosophila contains a functional mammalian-type SECIS. EMBO Rep. 1, 441-446.
    • (2000) EMBO Rep. , vol.1 , pp. 441-446
    • Hirosawa-Takamori, M.1    Jäckle, H.2    Vorbruggen, G.3
  • 27
    • 0033578750 scopus 로고    scopus 로고
    • Genetic analysis of glutathione peroxidase in oxidative stress response of Saccharomyces cerevisiae
    • Inoue, Y., Matsuda, T., Sugiyama, K., Izawa, S., and Kimura, A. (1999). Genetic analysis of glutathione peroxidase in oxidative stress response of Saccharomyces cerevisiae. J. Biol. Chem. 274, 27002-27009.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27002-27009
    • Inoue, Y.1    Matsuda, T.2    Sugiyama, K.3    Izawa, S.4    Kimura, A.5
  • 28
    • 0037066696 scopus 로고    scopus 로고
    • A Chinese cabbage cDNA with high sequence identity to phospholipid hydroperoxide glutathione peroxidases encodes a novel isoform of thioredoxin-dependent peroxidase
    • Jung, B. G., Lee, K. O., Lee, S. S., Chi, Y. H., Jang, H. H., Kang, S. S., Lee, K., Lim, D., Yoon, S. C., Yun, D. J., et al. (2002). A Chinese cabbage cDNA with high sequence identity to phospholipid hydroperoxide glutathione peroxidases encodes a novel isoform of thioredoxin-dependent peroxidase. J. Biol. Chem. 277, 12572-12578.
    • (2002) J. Biol. Chem. , vol.277 , pp. 12572-12578
    • Jung, B.G.1    Lee, K.O.2    Lee, S.S.3    Chi, Y.H.4    Jang, H.H.5    Kang, S.S.6    Lee, K.7    Lim, D.8    Yoon, S.C.9    Yun, D.J.10
  • 29
    • 0034704081 scopus 로고    scopus 로고
    • The thioredoxin system of the malaria parasite Plasmodium falciparum. Glutathione reduction revisited
    • Kanzok, S. M., Schirmer, R. H., Turbachova, I., Iozef, R., and Becker, K. (2000). The thioredoxin system of the malaria parasite Plasmodium falciparum. Glutathione reduction revisited. J. Biol. Chem. 275, 40180-40186.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40180-40186
    • Kanzok, S.M.1    Schirmer, R.H.2    Turbachova, I.3    Iozef, R.4    Becker, K.5
  • 31
    • 0034669473 scopus 로고    scopus 로고
    • Decreased mitochondrial hydrogen peroxide release in transgenic Drosophila melanogaster expressing intramitochondrial catalase
    • Kwong, L.K., Mockett, R.J., Bayne, A.V., Orr, W.C., and Sohal, R.S. (2000). Decreased mitochondrial hydrogen peroxide release in transgenic Drosophila melanogaster expressing intramitochondrial catalase. Archiv. Biochem. Biophys. 383, 303-308.
    • (2000) Archiv. Biochem. Biophys. , vol.383 , pp. 303-308
    • Kwong, L.K.1    Mockett, R.J.2    Bayne, A.V.3    Orr, W.C.4    Sohal, R.S.5
  • 33
    • 0028170326 scopus 로고
    • Importance of Se-glutathione peroxidase, catalase, and Cu/Zn-SOD for cell survival against oxidative stress
    • Michiels, C., Raes, M., Toussaint, O., and Remacle, J. (1994). Importance of Se-glutathione peroxidase, catalase, and Cu/Zn-SOD for cell survival against oxidative stress. Free Radic. Biol. Med. 17, 235-248.
    • (1994) Free Radic. Biol. Med. , vol.17 , pp. 235-248
    • Michiels, C.1    Raes, M.2    Toussaint, O.3    Remacle, J.4
  • 34
    • 0014565549 scopus 로고
    • The physiologic regulation of erythrocyte metabolism
    • Mills, G. C. (1969). The physiologic regulation of erythrocyte metabolism. Tex. Rep. Biol. Med. 27, 773-786.
    • (1969) Tex. Rep. Biol. Med. , vol.27 , pp. 773-786
    • Mills, G.C.1
  • 36
    • 0035928823 scopus 로고    scopus 로고
    • Cooperative action of antioxidant defense systems in Drosophila
    • Missirlis, F., Phillips, J. P., and Jäckle, H. (2001). Cooperative action of antioxidant defense systems in Drosophila. Curr. Biol. 11, 1272-1277.
    • (2001) Curr. Biol. , vol.11 , pp. 1272-1277
    • Missirlis, F.1    Phillips, J.P.2    Jäckle, H.3
  • 37
    • 0037192766 scopus 로고    scopus 로고
    • Mitochondrial and cytoplasmic thioredoxin reductase variants encoded by a single Drosophila gene are both essential for viability
    • Missirlis, F., J. K. Ulschmid, Hirosawa-Takamori, M., Gronke, S., Schäfer, U., Becker, K., Phillips, J. P., Jäckle, H. (2002). Mitochondrial and cytoplasmic thioredoxin reductase variants encoded by a single Drosophila gene are both essential for viability. J. Biol. Chem. 277, 11521-11526.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11521-11526
    • Missirlis, F.1    Ulschmid, J.K.2    Hirosawa-Takamori, M.3    Gronke, S.4    Schäfer, U.5    Becker, K.6    Phillips, J.P.7    Jäckle, H.8
  • 38
    • 0035476441 scopus 로고    scopus 로고
    • Modulation of the Ras/MAPK signalling pathway by the redox function of selenoproteins in Drosophila melanogaster
    • Morey, M., Serras, F., Baguñà, J., Hafen, E., and Corominas, M. (2001). Modulation of the Ras/MAPK signalling pathway by the redox function of selenoproteins in Drosophila melanogaster. Dev. Biol. 238, 145-156.
    • (2001) Dev. Biol. , vol.238 , pp. 145-156
    • Morey, M.1    Serras, F.2    Baguñà, J.3    Hafen, E.4    Corominas, M.5
  • 39
    • 0034652113 scopus 로고    scopus 로고
    • Thioredoxin reductase
    • Mustacich, D. and Powis, G. (2000). Thioredoxin reductase. Biochem. J. 346, 1-8.
    • (2000) Biochem. J. , vol.346 , pp. 1-8
    • Mustacich, D.1    Powis, G.2
  • 40
    • 0026783733 scopus 로고
    • The effects of catalase gene overexpression on life span and resistance to oxidative stress in transgenic Drosophila melanogaster
    • Orr, W. C., and Sohal, R. S. (1992). The effects of catalase gene overexpression on life span and resistance to oxidative stress in transgenic Drosophila melanogaster. Arch. Biochem. Biophys. 297, 35-41.
    • (1992) Arch. Biochem. Biophys. , vol.297 , pp. 35-41
    • Orr, W.C.1    Sohal, R.S.2
  • 41
    • 0028220114 scopus 로고
    • Extension of life-span by overexpression of superoxide dismutase and catalase in Drosophila melanogaster
    • Orr, W. C. and Sohal, R. S. (1994). Extension of life-span by overexpression of superoxide dismutase and catalase in Drosophila melanogaster. Science 263, 1128-1130.
    • (1994) Science , vol.263 , pp. 1128-1130
    • Orr, W.C.1    Sohal, R.S.2
  • 42
    • 0027739252 scopus 로고
    • Genetic and biochemical analysis of glutathione-S-transferase in the oxygen defense system of Drosophila melanogaster
    • Parkes, T. L., Hilliker, A. J., and Phillips, J. P. (1993). Genetic and biochemical analysis of glutathione-S-transferase in the oxygen defense system of Drosophila melanogaster. Genome 36, 1007-1014.
    • (1993) Genome , vol.36 , pp. 1007-1014
    • Parkes, T.L.1    Hilliker, A.J.2    Phillips, J.P.3
  • 43
    • 0028915976 scopus 로고
    • Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: Studies in yeast and neural cells
    • Rabizadeh, S., Gralla, E. B., Borchelt, D. R., Gwinn, R., Valentine, J. S., Sisodia, S., Wong, P., Lee, M., Hahn, H., and Bredesen, D. E. (1995). Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: studies in yeast and neural cells. Proc. Natl. Acad. Sci. USA 92, 3024-3028.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3024-3028
    • Rabizadeh, S.1    Gralla, E.B.2    Borchelt, D.R.3    Gwinn, R.4    Valentine, J.S.5    Sisodia, S.6    Wong, P.7    Lee, M.8    Hahn, H.9    Bredesen, D.E.10
  • 45
    • 0034662094 scopus 로고    scopus 로고
    • The importance of selenium to human health
    • Rayman, M. P. (2000). The importance of selenium to human health. Lancet 356, 233-241.
    • (2000) Lancet , vol.356 , pp. 233-241
    • Rayman, M.P.1
  • 46
    • 0029015420 scopus 로고
    • Activation of posterior gap gene expression in the Drosophila blastoderm
    • Rivera-Pomar, R., Lu, X., Perrimon, N., Taubert, H., and Jäckle, H. (1995). Activation of posterior gap gene expression in the Drosophila blastoderm. Nature 376, 253-256.
    • (1995) Nature , vol.376 , pp. 253-256
    • Rivera-Pomar, R.1    Lu, X.2    Perrimon, N.3    Taubert, H.4    Jäckle, H.5
  • 47
    • 0026587399 scopus 로고
    • Purification and properties of a recombinant sulfur analog of murine selenium-glutathione peroxidase
    • Rocher, C., Lalanne, J. L., and Chaudiere, J. (1992). Purification and properties of a recombinant sulfur analog of murine selenium-glutathione peroxidase. Eur. J. Biochem. 205, 955-960.
    • (1992) Eur. J. Biochem. , vol.205 , pp. 955-960
    • Rocher, C.1    Lalanne, J.L.2    Chaudiere, J.3
  • 48
    • 0019945644 scopus 로고
    • Genetic transformation of Drosophila with transposable element vectors
    • Rubin, G. M. and Spradling, A. C. (1982). Genetic transformation of Drosophila with transposable element vectors. Science 218, 348-353.
    • (1982) Science , vol.218 , pp. 348-353
    • Rubin, G.M.1    Spradling, A.C.2
  • 50
    • 0039844391 scopus 로고    scopus 로고
    • Structure and regulated expression of the δ-aminolevulinate synthase gene from Drosophila melanogaster
    • Ruiz de Mena, I., Fernandez-Moreno, M.A., Bornstein, B., Kaguni, L.S., and Garesse, R. (1999) Structure and regulated expression of the δ-aminolevulinate synthase gene from Drosophila melanogaster. J. Biol. Chem. 274, 37321-37328.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37321-37328
    • Ruiz de Mena, I.1    Fernandez-Moreno, M.A.2    Bornstein, B.3    Kaguni, L.S.4    Garesse, R.5
  • 51
    • 0028353337 scopus 로고
    • The Drosophila maternal effect locus deadhead encodes a thioredoxin homolog required for female meiosis and early embryonic development
    • Salz, H. K., Flickinger, T. W., Mittendorf, E., Pellicena-Palle, A., Petschek, J. P., and Albrecht, E. B. (1994). The Drosophila maternal effect locus deadhead encodes a thioredoxin homolog required for female meiosis and early embryonic development. Genetics 136, 1075-1086.
    • (1994) Genetics , vol.136 , pp. 1075-1086
    • Salz, H.K.1    Flickinger, T.W.2    Mittendorf, E.3    Pellicena-Palle, A.4    Petschek, J.P.5    Albrecht, E.B.6
  • 53
    • 0027155884 scopus 로고
    • Autocrine production of extracellular catalase prevents apoptosis of the human CEM T-cell line in serum-free medium
    • Sandstrom, P. A. and Buttke, T. M. (1993). Autocrine production of extracellular catalase prevents apoptosis of the human CEM T-cell line in serum-free medium. Proc. Natl. Acad. Sci. USA 90, 4708-4712.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4708-4712
    • Sandstrom, P.A.1    Buttke, T.M.2
  • 54
    • 33746017613 scopus 로고    scopus 로고
    • Sites of synthesis and transport pathways of insect hydrocarbons - Cuticle and ovary as target tissues
    • Schal, C., Sevala, V. L., Young, H. P., and Bachmann, J. A. S. (1998). Sites of synthesis and transport pathways of insect hydrocarbons - cuticle and ovary as target tissues. Am. Zoologist 38, 382-393.
    • (1998) Am. Zoologist , vol.38 , pp. 382-393
    • Schal, C.1    Sevala, V.L.2    Young, H.P.3    Bachmann, J.A.S.4
  • 55
    • 0018398183 scopus 로고
    • Phylogenetic distribution of glutathione peroxidase
    • Smith, J. and Shrift, A. (1979). Phylogenetic distribution of glutathione peroxidase. Comp. Biochem. Physiol. B 63, 39-44.
    • (1979) Comp. Biochem. Physiol. B , vol.63 , pp. 39-44
    • Smith, J.1    Shrift, A.2
  • 56
  • 57
    • 0030020576 scopus 로고    scopus 로고
    • A new selenoprotein from human lung adenocarcinoma cells: Purification, properties, and thioredoxin reductase activity
    • Tamura, T. and Stadtman, T. C. (1996). A new selenoprotein from human lung adenocarcinoma cells: purification, properties, and thioredoxin reductase 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
  • 58
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G., and Gibson, T. J. (1994). CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 61
    • 0037053395 scopus 로고    scopus 로고
    • The Trypanosoma cruzi enzyme TcGPXI is a glycosomal peroxidase and can be linked to trypanothione reduction by glutathione or tryparedoxin
    • Wilkinson, S. R., Meyer, D. J., Taylor, M. C., Bromley, E. V., Miles, M. A., and Kelly, J. M. (2002). The Trypanosoma cruzi enzyme TcGPXI is a glycosomal peroxidase and can be linked to trypanothione reduction by glutathione or tryparedoxin. J. Biol. Chem. 277, 17062-17071.
    • (2002) J. Biol. Chem. , vol.277 , pp. 17062-17071
    • Wilkinson, S.R.1    Meyer, D.J.2    Taylor, M.C.3    Bromley, E.V.4    Miles, M.A.5    Kelly, J.M.6
  • 63
    • 0032767979 scopus 로고    scopus 로고
    • Schizosaccharomyces pombe homologue of glutathione peroxidase, which does not contain selenocysteine, is induced by several stresses and works as an antioxidant
    • Yamada, K., Nakagawa, C. W., and Mutoh, N. (1999). Schizosaccharomyces pombe homologue of glutathione peroxidase, which does not contain selenocysteine, is induced by several stresses and works as an antioxidant. Yeast 15, 1125-1132.
    • (1999) Yeast , vol.15 , pp. 1125-1132
    • Yamada, K.1    Nakagawa, C.W.2    Mutoh, N.3
  • 64
    • 0030692005 scopus 로고    scopus 로고
    • Thioredoxin peroxidase is a novel inhibitor of apoptosis with a mechanism distinct from that of Bcl-2
    • Zhang, P., Liu, B., Kang, S. W., Seo, M. S., Rhee, S. G., and Obeid, L. M. (1997). Thioredoxin peroxidase is a novel inhibitor of apoptosis with a mechanism distinct from that of Bcl-2. J. Biol. Chem. 272, 30615-30618.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30615-30618
    • Zhang, P.1    Liu, B.2    Kang, S.W.3    Seo, M.S.4    Rhee, S.G.5    Obeid, L.M.6
  • 65
    • 0034674566 scopus 로고    scopus 로고
    • Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations
    • Zhong, L. and Holmgren, A. (2000). Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations. J. Biol. Chem. 275, 18121-18128.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18121-18128
    • Zhong, L.1    Holmgren, A.2


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