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Volumn 159, Issue 1, 2011, Pages 1-9

A selenium-dependent glutathione peroxidase in the Japanese scallop, Mizuhopecten yessoensis: CDNA cloning, promoter sequence analysis and mRNA expression

Author keywords

Mizuhopecten yessoensis; MRNA expression; Promoter analysis; Selenium dependent glutathione peroxidase; SNP

Indexed keywords

GLUTATHIONE PEROXIDASE; MESSENGER RNA; SELENIUM;

EID: 79952699746     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpb.2011.01.003     Document Type: Article
Times cited : (19)

References (61)
  • 1
    • 0025077481 scopus 로고
    • Redox regulation of fos and jun DNA-binding activity in vitro
    • Abate C., Patel L., Rauscher F.J., Curan T. Redox regulation of fos and jun DNA-binding activity in vitro. Science 1990, 249:1157-1161.
    • (1990) Science , vol.249 , pp. 1157-1161
    • Abate, C.1    Patel, L.2    Rauscher, F.J.3    Curan, T.4
  • 3
    • 33645672106 scopus 로고    scopus 로고
    • Validation of the 2-DeltaDeltaCt calculation as an alternate method of data analysis for quantitative PCR of BCR-ABL P210 transcripts
    • Arocho A., Chen B., Ladanyi M., Pan Q. Validation of the 2-DeltaDeltaCt calculation as an alternate method of data analysis for quantitative PCR of BCR-ABL P210 transcripts. Diagn. Mol. Pathol. 2006, 15:56-61.
    • (2006) Diagn. Mol. Pathol. , vol.15 , pp. 56-61
    • Arocho, A.1    Chen, B.2    Ladanyi, M.3    Pan, Q.4
  • 4
    • 0031227819 scopus 로고    scopus 로고
    • Glutathione peroxidase revisited-simulation of the catalytic cycle by computer-assisted molecular modelling
    • Aumann K.D., Bedorf N., Brigelius-Flohé R., Schomburg D., Flohé L. Glutathione peroxidase revisited-simulation of the catalytic cycle by computer-assisted molecular modelling. Biomed. Environ. Sci. 1997, 10:136-155.
    • (1997) Biomed. Environ. Sci. , vol.10 , pp. 136-155
    • Aumann, K.D.1    Bedorf, N.2    Brigelius-Flohé, R.3    Schomburg, D.4    Flohé, L.5
  • 5
    • 34447345961 scopus 로고    scopus 로고
    • Characterization of chitinase-like proteins (Cg-Clp1 and Cg-Clp2) involved in immune defence of the mollusc Crassostrea gigas
    • Badariotti F., Lelong C., Dubos M.P., Favrel P. Characterization of chitinase-like proteins (Cg-Clp1 and Cg-Clp2) involved in immune defence of the mollusc Crassostrea gigas. FEBS J. 2007, 274:3646-3654.
    • (2007) FEBS J. , vol.274 , pp. 3646-3654
    • Badariotti, F.1    Lelong, C.2    Dubos, M.P.3    Favrel, P.4
  • 6
    • 51249098717 scopus 로고    scopus 로고
    • The manganese superoxide dismutase gene in bay scallop Argopecten irradians: cloning, 3D modelling and mRNA expression
    • Bao Y.B., Li L., Zhang G.F. The manganese superoxide dismutase gene in bay scallop Argopecten irradians: cloning, 3D modelling and mRNA expression. Fish Shellfish Immunol. 2008, 25:425-432.
    • (2008) Fish Shellfish Immunol. , vol.25 , pp. 425-432
    • Bao, Y.B.1    Li, L.2    Zhang, G.F.3
  • 7
    • 77953389358 scopus 로고    scopus 로고
    • Polymorphism of the superoxide dismutase gene family in the bay scallop (Argopecten irradians) and its association with resistance/susceptibility to Vibrio anguillarum
    • Bao Y.B., Li Li., Zhang G.F. Polymorphism of the superoxide dismutase gene family in the bay scallop (Argopecten irradians) and its association with resistance/susceptibility to Vibrio anguillarum. Dev. Comp. Immunol. 2010, 34:553-561.
    • (2010) Dev. Comp. Immunol. , vol.34 , pp. 553-561
    • Bao, Y.B.1    Li, L.2    Zhang, G.F.3
  • 8
    • 17544404224 scopus 로고    scopus 로고
    • Reactive oxygen and reactive nitrogen intermediates in innate and specific immunity
    • Bogdan C., Röllinghoff M., Diefenbach A. Reactive oxygen and reactive nitrogen intermediates in innate and specific immunity. Curr. Opin. Immunol. 2000, 12:64-76.
    • (2000) Curr. Opin. Immunol. , vol.12 , pp. 64-76
    • Bogdan, C.1    Röllinghoff, M.2    Diefenbach, A.3
  • 10
    • 0030978102 scopus 로고    scopus 로고
    • Early embryonic lethality caused by targeted disruption of the mouse selenocysteine tRNA gene (Trsp)
    • Bösl M.R., Takaku K., Oshima M., Nishimura S., Taketo M.M. Early embryonic lethality caused by targeted disruption of the mouse selenocysteine tRNA gene (Trsp). Proc. Natl Acad. Sci. USA 1997, 94:5531-5534.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 5531-5534
    • Bösl, M.R.1    Takaku, K.2    Oshima, M.3    Nishimura, S.4    Taketo, M.M.5
  • 12
    • 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 P.R. The structure of the mouse glutathione peroxidase gene: the selenocysteine in the active site is encoded by the 'termination' codon, TGA. EMBO J. 1986, 5:1221-1227.
    • (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
  • 13
    • 0027536023 scopus 로고
    • Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI
    • Chu F.F., Doroshow J.H., Esworthy R.S. Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI. Biochem. J. 1993, 268:2571-2576.
    • (1993) Biochem. J. , vol.268 , pp. 2571-2576
    • Chu, F.F.1    Doroshow, J.H.2    Esworthy, R.S.3
  • 14
    • 0016291721 scopus 로고
    • Larval development of the giant scallop Placopecten Magellanicus (Gmelin)
    • Culliney J.L. Larval development of the giant scallop Placopecten Magellanicus (Gmelin). Biol. Bull. 1974, 147:321-332.
    • (1974) Biol. Bull. , vol.147 , pp. 321-332
    • Culliney, J.L.1
  • 16
    • 33750159082 scopus 로고    scopus 로고
    • Identification, sequencing and expression of selenium-dependent glutathione peroxidase transcript in the freshwater bivalve Unio tumidus exposed to Aroclor 1254
    • Doyen P., Vasseur P., Rodius F. Identification, sequencing and expression of selenium-dependent glutathione peroxidase transcript in the freshwater bivalve Unio tumidus exposed to Aroclor 1254. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 2006, 144:122-129.
    • (2006) Comp. Biochem. Physiol. C Toxicol. Pharmacol. , vol.144 , pp. 122-129
    • Doyen, P.1    Vasseur, P.2    Rodius, F.3
  • 17
    • 36749002700 scopus 로고    scopus 로고
    • Molecular cloning and expression study of pi-class glutathione S-transferase (pi-GST) and selenium-dependent glutathione peroxidase (Se-GPx) transcripts in the freshwater bivalve Dreissena polymorpha
    • Doyen P., Bigot A., Vasseur P., Rodius F. Molecular cloning and expression study of pi-class glutathione S-transferase (pi-GST) and selenium-dependent glutathione peroxidase (Se-GPx) transcripts in the freshwater bivalve Dreissena polymorpha. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 2008, 147:69-77.
    • (2008) Comp. Biochem. Physiol. C Toxicol. Pharmacol. , vol.147 , pp. 69-77
    • Doyen, P.1    Bigot, A.2    Vasseur, P.3    Rodius, F.4
  • 18
    • 33646193400 scopus 로고    scopus 로고
    • The antioxidant glutathione peroxidase family and spermatozoa: a complex story
    • Drevet J.R. The antioxidant glutathione peroxidase family and spermatozoa: a complex story. Mol. Cell. Endocrinol. 2006, 250:70-79.
    • (2006) Mol. Cell. Endocrinol. , vol.250 , pp. 70-79
    • Drevet, J.R.1
  • 19
    • 0028835297 scopus 로고
    • Expression of selenium-dependent glutathione peroxidase in human breast tumor cell lines
    • Esworthy R.S., Baker M.A., Chu F.F. Expression of selenium-dependent glutathione peroxidase in human breast tumor cell lines. Cancer Res. 1995, 55:957-962.
    • (1995) Cancer Res. , vol.55 , pp. 957-962
    • Esworthy, R.S.1    Baker, M.A.2    Chu, F.F.3
  • 20
    • 0015880169 scopus 로고
    • Glutathione peroxidase: a selenoenzyme
    • Flohé L., Gunzler W.A., Schock H.H. Glutathione peroxidase: a selenoenzyme. FEBS Lett. 1973, 32:132-134.
    • (1973) FEBS Lett. , vol.32 , pp. 132-134
    • Flohé, L.1    Gunzler, W.A.2    Schock, H.H.3
  • 21
    • 4344649455 scopus 로고    scopus 로고
    • Functional variants in the glutathione peroxidase-1 (GPx-1) gene are associated with increased intima-media thickness of carotid arteries and risk of macrovascular diseases in japanese type 2 diabetic patients
    • Hamanishi T., Furuta H., Kato H., Doi A., Tamai M., Shimomura H., Sakagashira S., Nishi M., Sasaki H., Sanke T., Nanjo K. Functional variants in the glutathione peroxidase-1 (GPx-1) gene are associated with increased intima-media thickness of carotid arteries and risk of macrovascular diseases in japanese type 2 diabetic patients. Diabetes 2004, 53:2455-2460.
    • (2004) Diabetes , vol.53 , pp. 2455-2460
    • Hamanishi, T.1    Furuta, H.2    Kato, H.3    Doi, A.4    Tamai, M.5    Shimomura, H.6    Sakagashira, S.7    Nishi, M.8    Sasaki, H.9    Sanke, T.10    Nanjo, K.11
  • 22
    • 0033025174 scopus 로고    scopus 로고
    • The CCAAT-box binding factor NF-Y is required for the expression of the phospholipid hydroperoxide glutathione peroxidase in human epidermoid carcinoma A431 cells
    • Huang H.S., Jiunn C., Chang W.C. The CCAAT-box binding factor NF-Y is required for the expression of the phospholipid hydroperoxide glutathione peroxidase in human epidermoid carcinoma A431 cells. FEBS Lett. 1999, 455:111-116.
    • (1999) FEBS Lett. , vol.455 , pp. 111-116
    • Huang, H.S.1    Jiunn, C.2    Chang, W.C.3
  • 23
    • 2542473274 scopus 로고    scopus 로고
    • Effects of 17-beta estradiol and 4-nonylphenol on phase II electrophilic detoxification pathways in largemouth bass (Micropterus salmoides) liver
    • Hughes E.M., Gallagher E.P. Effects of 17-beta estradiol and 4-nonylphenol on phase II electrophilic detoxification pathways in largemouth bass (Micropterus salmoides) liver. Comp. Biochem. Physiol. C 2004, 137:237-247.
    • (2004) Comp. Biochem. Physiol. C , vol.137 , pp. 237-247
    • Hughes, E.M.1    Gallagher, E.P.2
  • 24
    • 0034595241 scopus 로고    scopus 로고
    • Structural organization of the human gastrointestinal glutathione peroxidase (GPX2) promoter and 3'-nontranscribed region: transcriptional response to exogenous redox agents
    • Kelner M.J., Bagnell R.D., Montoya M.A., Lanham K.A. Structural organization of the human gastrointestinal glutathione peroxidase (GPX2) promoter and 3'-nontranscribed region: transcriptional response to exogenous redox agents. Gene 2000, 248:109-116.
    • (2000) Gene , vol.248 , pp. 109-116
    • Kelner, M.J.1    Bagnell, R.D.2    Montoya, M.A.3    Lanham, K.A.4
  • 25
    • 0038792250 scopus 로고    scopus 로고
    • Evidence of two clock control of endogenous rhythm in the Washington clam, Saxidomus purpuratus
    • Kim W.S., Huh H.T., Je J.G., Han K.N. Evidence of two clock control of endogenous rhythm in the Washington clam, Saxidomus purpuratus. Mar. Biol. 2003, 142:305-309.
    • (2003) Mar. Biol. , vol.142 , pp. 305-309
    • Kim, W.S.1    Huh, H.T.2    Je, J.G.3    Han, K.N.4
  • 27
    • 4644293545 scopus 로고    scopus 로고
    • Biochemical properties of glutathione peroxidase in Gammarus pulex
    • Kutlu M., Susuz F. Biochemical properties of glutathione peroxidase in Gammarus pulex. Bull. Environ. Contam. Toxicol. 2004, 73:432-436.
    • (2004) Bull. Environ. Contam. Toxicol. , vol.73 , pp. 432-436
    • Kutlu, M.1    Susuz, F.2
  • 28
    • 0034752752 scopus 로고    scopus 로고
    • Noradrenaline and alpha-adrenergic signaling induce the hsp70 gene promoter in mollusc immune cells
    • Lacoste A., De Cian M.C., Cueff A., Poulet S.A. Noradrenaline and alpha-adrenergic signaling induce the hsp70 gene promoter in mollusc immune cells. J. Cell Sci. 2001, 114:3557-3564.
    • (2001) J. Cell Sci. , vol.114 , pp. 3557-3564
    • Lacoste, A.1    De Cian, M.C.2    Cueff, A.3    Poulet, S.A.4
  • 29
    • 0037084394 scopus 로고    scopus 로고
    • P35-sensitive caspases, MAP kinases and Rho modulate beta-adrenergic induction of apoptosis in mollusc immune cells
    • Lacoste A., Cueff A., Poulet S.A. P35-sensitive caspases, MAP kinases and Rho modulate beta-adrenergic induction of apoptosis in mollusc immune cells. J. Cell Sci. 2002, 115:761-768.
    • (2002) J. Cell Sci. , vol.115 , pp. 761-768
    • Lacoste, A.1    Cueff, A.2    Poulet, S.A.3
  • 30
    • 34447327783 scopus 로고    scopus 로고
    • Genetic variation in Chinese hatchery populations of the Japanese scallop (Patinopecten yessoensis) inferred from microsatellite data
    • Li Q., Xu K.F., Yu R.H. Genetic variation in Chinese hatchery populations of the Japanese scallop (Patinopecten yessoensis) inferred from microsatellite data. Aquaculture 2007, 269:211-219.
    • (2007) Aquaculture , vol.269 , pp. 211-219
    • Li, Q.1    Xu, K.F.2    Yu, R.H.3
  • 31
    • 79952694597 scopus 로고    scopus 로고
    • The polymorphism of lysozyme gene in Zhikong scallop (Chlamys farreri) and its association with susceptibility/resistance to Listonella anguillarum
    • Li M., Zhao J.M., Wang L.L., Qiu L.M., Zhang H., Dong C.H., Cong M., Song L.S. The polymorphism of lysozyme gene in Zhikong scallop (Chlamys farreri) and its association with susceptibility/resistance to Listonella anguillarum. Fish Shellfish Immunol. 2009, 13:1-7.
    • (2009) Fish Shellfish Immunol. , vol.13 , pp. 1-7
    • Li, M.1    Zhao, J.M.2    Wang, L.L.3    Qiu, L.M.4    Zhang, H.5    Dong, C.H.6    Cong, M.7    Song, L.S.8
  • 32
    • 34247378650 scopus 로고    scopus 로고
    • Identification and cloning of the antioxidant enzyme, glutathione peroxidase, of white shrimp, Litopenaeus vannamei, and its expression following Vibrio alginolyticus infection
    • Liu C.H., Tseng M.C., Cheng W. Identification and cloning of the antioxidant enzyme, glutathione peroxidase, of white shrimp, Litopenaeus vannamei, and its expression following Vibrio alginolyticus infection. Fish Shellfish Immunol. 2007, 23:34-45.
    • (2007) Fish Shellfish Immunol. , vol.23 , pp. 34-45
    • Liu, C.H.1    Tseng, M.C.2    Cheng, W.3
  • 33
    • 79952701316 scopus 로고    scopus 로고
    • Discovery of host defence genes in the Japanese scallop Mizuhopecten yessoensis Jay by expressed sequence tag analysis of kidney tissue
    • Liu W.D., He C.B., Li W.J., Zhou Z.C., Gao X.G., Fu L.Y. Discovery of host defence genes in the Japanese scallop Mizuhopecten yessoensis Jay by expressed sequence tag analysis of kidney tissue. Aqua. Res. 2010, 41:1602-1613.
    • (2010) Aqua. Res. , vol.41 , pp. 1602-1613
    • Liu, W.D.1    He, C.B.2    Li, W.J.3    Zhou, Z.C.4    Gao, X.G.5    Fu, L.Y.6
  • 34
    • 1642545529 scopus 로고    scopus 로고
    • Invertebrate immune systems-not homogeneous, not simple, not well understood
    • Loker E.S., Adema C.M., Zhang S.M., Kepler T.B. Invertebrate immune systems-not homogeneous, not simple, not well understood. Immunol. Rev. 2004, 198:10-24.
    • (2004) Immunol. Rev. , vol.198 , pp. 10-24
    • Loker, E.S.1    Adema, C.M.2    Zhang, S.M.3    Kepler, T.B.4
  • 35
    • 0037443421 scopus 로고    scopus 로고
    • Cu/Zn superoxide dismutase plays important role in immune response
    • Marikovsky M., Ziv V., Nevo N., Harris-Cerruti C., Mahler O. Cu/Zn superoxide dismutase plays important role in immune response. J. Immunol. 2003, 170:2993-3001.
    • (2003) J. Immunol. , vol.170 , pp. 2993-3001
    • Marikovsky, M.1    Ziv, V.2    Nevo, N.3    Harris-Cerruti, C.4    Mahler, O.5
  • 37
    • 0037066502 scopus 로고    scopus 로고
    • Decoding the patterns of self and nonself by the innate immune system
    • Medzhitov R., Janeway C.A. Decoding the patterns of self and nonself by the innate immune system. Science 2002, 296:298-300.
    • (2002) Science , vol.296 , pp. 298-300
    • Medzhitov, R.1    Janeway, C.A.2
  • 38
    • 0033198299 scopus 로고    scopus 로고
    • Relationships between antioxidants, antioxidant enzyme activities and lipid peroxidation products during early development in Dentex dentex eggs and larvae
    • Mourente G., Tocher D.R., Diaz E., Grau A., Pastor E. Relationships between antioxidants, antioxidant enzyme activities and lipid peroxidation products during early development in Dentex dentex eggs and larvae. Aquaculture 1999, 179:309-324.
    • (1999) Aquaculture , vol.179 , pp. 309-324
    • Mourente, G.1    Tocher, D.R.2    Diaz, E.3    Grau, A.4    Pastor, E.5
  • 40
    • 21644435110 scopus 로고    scopus 로고
    • Genetic structure of Japanese scallop population in Hokkaido, analyzed by mitochondrial haplotype distribution
    • Nagashima K., Sato M., Kawamata K., Nakamura A., Ohta T. Genetic structure of Japanese scallop population in Hokkaido, analyzed by mitochondrial haplotype distribution. Mar. Biotechnol. 2005, 7:1-10.
    • (2005) Mar. Biotechnol. , vol.7 , pp. 1-10
    • Nagashima, K.1    Sato, M.2    Kawamata, K.3    Nakamura, A.4    Ohta, T.5
  • 41
    • 0026714544 scopus 로고
    • Genetic evidence for an androgen-regulated epididymal secretory glutathione peroxidase whose transcript does not contain a selenocysteine codon
    • Perry A.C., Jones R., Niang L.S., Jackson R.M., Hall L. Genetic evidence for an androgen-regulated epididymal secretory glutathione peroxidase whose transcript does not contain a selenocysteine codon. Biochem. J. 1992, 285:863-870.
    • (1992) Biochem. J. , vol.285 , pp. 863-870
    • Perry, A.C.1    Jones, R.2    Niang, L.S.3    Jackson, R.M.4    Hall, L.5
  • 42
    • 0035348255 scopus 로고    scopus 로고
    • Identification of a specific sperm nuclei selenoenzyme necessary for protamine thiol cross-linking during sperm maturation
    • Pfeifer H., Conrad M., Roethlein D., Kyriakopoulos A., Brielmeier M., Bornkamm G.W., Behne D. Identification of a specific sperm nuclei selenoenzyme necessary for protamine thiol cross-linking during sperm maturation. FASEB J. 2001, 15:1236-1238.
    • (2001) FASEB J. , vol.15 , pp. 1236-1238
    • Pfeifer, H.1    Conrad, M.2    Roethlein, D.3    Kyriakopoulos, A.4    Brielmeier, M.5    Bornkamm, G.W.6    Behne, D.7
  • 43
    • 0000911250 scopus 로고
    • Environmental contaminants influencing immunefunction in marine bivalve molluscs
    • Pipe R.K., Coles J.A. Environmental contaminants influencing immunefunction in marine bivalve molluscs. Fish Shellfish Immunol. 1995, 5:581-595.
    • (1995) Fish Shellfish Immunol. , vol.5 , pp. 581-595
    • Pipe, R.K.1    Coles, J.A.2
  • 44
    • 0026473086 scopus 로고
    • The helix-loop-helix/leucine repeat transcription factor USF can be functionally regulated in a redox-dependent manner
    • Pognonec P., Kato H., Roeder R.G. The helix-loop-helix/leucine repeat transcription factor USF can be functionally regulated in a redox-dependent manner. J. Biol. Chem. 1993, 267:24563-24567.
    • (1993) J. Biol. Chem. , vol.267 , pp. 24563-24567
    • Pognonec, P.1    Kato, H.2    Roeder, R.G.3
  • 45
    • 63449093689 scopus 로고    scopus 로고
    • A selenium-dependent glutathione peroxidase (Se-GPx) and two glutathione S-transferases (GSTs) from Chinese shrimp (Fenneropenaeus chinensis)
    • Ren Q., Sun R.R., Zhao X.F., Wang J.X. A selenium-dependent glutathione peroxidase (Se-GPx) and two glutathione S-transferases (GSTs) from Chinese shrimp (Fenneropenaeus chinensis). Comp. Biochem. Physiol. C Toxicol. Pharmacol. 2009, 149:613-623.
    • (2009) Comp. Biochem. Physiol. C Toxicol. Pharmacol. , vol.149 , pp. 613-623
    • Ren, Q.1    Sun, R.R.2    Zhao, X.F.3    Wang, J.X.4
  • 46
    • 33747077499 scopus 로고    scopus 로고
    • A clockwork mollusc: ultradian rhythms in bivalve activity revealed by digital photography
    • Rodland D.L., Schöne B.R., Helama S., Nielsen J.K., Baier S. A clockwork mollusc: ultradian rhythms in bivalve activity revealed by digital photography. J. Exp. Mar. Biol. Ecol. 2006, 334:316-323.
    • (2006) J. Exp. Mar. Biol. Ecol. , vol.334 , pp. 316-323
    • Rodland, D.L.1    Schöne, B.R.2    Helama, S.3    Nielsen, J.K.4    Baier, S.5
  • 49
    • 0025739254 scopus 로고
    • Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kappa B transcription factor and HIV-1
    • Schreck R., Rieber P., Baeuerle P.A. Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kappa B transcription factor and HIV-1. EMBO J. 1991, 10:2247-2258.
    • (1991) EMBO J. , vol.10 , pp. 2247-2258
    • Schreck, R.1    Rieber, P.2    Baeuerle, P.A.3
  • 50
    • 0030834975 scopus 로고    scopus 로고
    • Briviba, K. Glutathione peroxidase protects against peroxynitrite-mediated oxidation. A new function for selenoproteins as peroxynitrite reductase
    • Sies H., Sharov V.S., Klotz L.O. Briviba, K. Glutathione peroxidase protects against peroxynitrite-mediated oxidation. A new function for selenoproteins as peroxynitrite reductase. J. Biol. Chem. 1997, 272:27812-27817.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27812-27817
    • Sies, H.1    Sharov, V.S.2    Klotz, L.O.3
  • 51
    • 0022471869 scopus 로고
    • Selenium-dependent glutathione peroxidase protein and activity: immunological investigations on cellular and plasma enzymes
    • Takahashi K., Cohen H.J. Selenium-dependent glutathione peroxidase protein and activity: immunological investigations on cellular and plasma enzymes. Blood 1986, 68:640-645.
    • (1986) Blood , vol.68 , pp. 640-645
    • Takahashi, K.1    Cohen, H.J.2
  • 53
    • 0031574072 scopus 로고    scopus 로고
    • The Clustal_X Windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., Higgins D.G. The Clustal_X Windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 1997, 25:4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 54
    • 0025852479 scopus 로고
    • Modulation of transcription factor NF-kappa B binding activity by oxidation-reduction in vitro
    • Toledano M.B., Leonard W.J. Modulation of transcription factor NF-kappa B binding activity by oxidation-reduction in vitro. Proc. Natl Acad. Sci. USA 1991, 88:4328-4332.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 4328-4332
    • Toledano, M.B.1    Leonard, W.J.2
  • 55
    • 0043163817 scopus 로고    scopus 로고
    • Functional characterization of cis-and transregulatory elements involved in expression of phospholipid hydroperoxide glutathione peroxidase
    • Ufer C., Borchert A., Kuhn H. Functional characterization of cis-and transregulatory elements involved in expression of phospholipid hydroperoxide glutathione peroxidase. Nucleic Acids Res. 2003, 31:4293-4303.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 4293-4303
    • Ufer, C.1    Borchert, A.2    Kuhn, H.3
  • 56
    • 0021803196 scopus 로고
    • The selenoenzyme phospholipid hydroperoxide glutathione peroxidase
    • Ursini F., Maiorino M., Gregolin C. The selenoenzyme phospholipid hydroperoxide glutathione peroxidase. Biochim. Biophys. Acta 1985, 839:62-70.
    • (1985) Biochim. Biophys. Acta , vol.839 , pp. 62-70
    • Ursini, F.1    Maiorino, M.2    Gregolin, C.3
  • 58
    • 0032729659 scopus 로고    scopus 로고
    • Selenium-independent epididymis-restricted glutathione peroxidase 5 protein (GPX5) can back up failing Se-dependent GPXs in mice subjected to selenium deficiency
    • Vernet P., Rock E., Mazur A., Rayssiguier Y., Dufaure J.P., Drevet J.R. Selenium-independent epididymis-restricted glutathione peroxidase 5 protein (GPX5) can back up failing Se-dependent GPXs in mice subjected to selenium deficiency. Mol. Reprod. Dev. 1999, 54:362-370.
    • (1999) Mol. Reprod. Dev. , vol.54 , pp. 362-370
    • Vernet, P.1    Rock, E.2    Mazur, A.3    Rayssiguier, Y.4    Dufaure, J.P.5    Drevet, J.R.6
  • 61
    • 1842840037 scopus 로고    scopus 로고
    • Effects of watersoluble fractions of diesel oil on the antioxidant defenses of the goldfish, Carassius auratus
    • Zhang J.F., Wang X.R., Guo H.Y., Wu J.C., Xue Y.Q. Effects of watersoluble fractions of diesel oil on the antioxidant defenses of the goldfish, Carassius auratus. Ecotoxicol. Environ. Saf. 2004, 58:110-116.
    • (2004) Ecotoxicol. Environ. Saf. , vol.58 , pp. 110-116
    • Zhang, J.F.1    Wang, X.R.2    Guo, H.Y.3    Wu, J.C.4    Xue, Y.Q.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.