메뉴 건너뛰기




Volumn 88, Issue 1, 1998, Pages 43-50

Dirofilaria immitis: Molecular cloning and expression of a cDNA encoding a selenium-independent secreted glutathione peroxidase

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; GLUTATHIONE PEROXIDASE; RECOMBINANT PROTEIN;

EID: 0031903982     PISSN: 00144894     EISSN: None     Source Type: Journal    
DOI: 10.1006/expr.1998.4217     Document Type: Article
Times cited : (20)

References (36)
  • 2
    • 0028139014 scopus 로고
    • The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase
    • Björnstedt M., Xue J., Huang W., Åkesson B., Holmgren A. The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase. The Journal of Biological Chemistry. 269:1994;29382-29384.
    • (1994) The Journal of Biological Chemistry , vol.269 , pp. 29382-29384
    • Björnstedt, M.1    Xue, J.2    Huang, W.3    Åkesson, B.4    Holmgren, A.5
  • 3
    • 0024574320 scopus 로고
    • Biochemical and immunochemical characterisation of a 20-kilodalton complex of surface-associated antigens from adultOnchocerca gutturosa
    • Bradley J. E., Gregory W. F., Bianco A. E., Maizels R. M. Biochemical and immunochemical characterisation of a 20-kilodalton complex of surface-associated antigens from adultOnchocerca gutturosa. Molecular and Biochemical Parasitology. 34:1989;197-208.
    • (1989) Molecular and Biochemical Parasitology , vol.34 , pp. 197-208
    • Bradley, J.E.1    Gregory, W.F.2    Bianco, A.E.3    Maizels, R.M.4
  • 5
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Analytical Biochemistry. 162:1987;156-159.
    • (1987) Analytical Biochemistry , vol.162 , pp. 156-159
    • ChoMcZynski, P.1    Sacchi, N.2
  • 6
    • 0026686203 scopus 로고
    • Identification of the major cuticular glycoprotein of lymphatic filarial nematode parasites (gp29) as a secretory homolog of glutathione peroxidase
    • Cookson E., Blaxter M. L., Selkirk M. E. Identification of the major cuticular glycoprotein of lymphatic filarial nematode parasites (gp29) as a secretory homolog of glutathione peroxidase. Proceedings of the National Academy of Sciences of the USA. 89:1992;5837-5841.
    • (1992) Proceedings of the National Academy of Sciences of the USA , vol.89 , pp. 5837-5841
    • Cookson, E.1    Blaxter, M.L.2    Selkirk, M.E.3
  • 7
    • 0027398735 scopus 로고
    • Conservation of primary sequence of gp29, the major soluble cuticular glycoprotein, in three species of lymphatic filariae
    • Cookson E., Tang L., Selkirk M. E. Conservation of primary sequence of gp29, the major soluble cuticular glycoprotein, in three species of lymphatic filariae. Molecular and Biochemical Parasitology. 58:1993;155-160.
    • (1993) Molecular and Biochemical Parasitology , vol.58 , pp. 155-160
    • Cookson, E.1    Tang, L.2    Selkirk, M.E.3
  • 8
    • 0028670641 scopus 로고
    • Stage specific differences in steady state levels of mRNA encoding the major surface glycoprotein ofBrugia pahangi
    • Cox-Singh J., Paine M. J. I., Martin S. A. M., Devaney E. Stage specific differences in steady state levels of mRNA encoding the major surface glycoprotein ofBrugia pahangi. Tropical Medicine and Parasitology. 45:1994;352-354.
    • (1994) Tropical Medicine and Parasitology , vol.45 , pp. 352-354
    • Cox-Singh, J.1    Paine, M.J.I.2    Martin, S.A.M.3    Devaney, E.4
  • 9
    • 0026816078 scopus 로고
    • Isolation and characterization of a plant cDNA showing homology to animal glutathione peroxidases
    • Criqui M. C., Jamet E., Parmentier Y., Marbach J., Durr A., Fleck J. Isolation and characterization of a plant cDNA showing homology to animal glutathione peroxidases. Plant Molecular Biology. 18:1992;623-627.
    • (1992) Plant Molecular Biology , vol.18 , pp. 623-627
    • Criqui, M.C.1    Jamet, E.2    Parmentier, Y.3    Marbach, J.4    Durr, A.5    Fleck, J.6
  • 10
    • 0025924349 scopus 로고
    • The expression of the Mr 30,000 antigen in the third stage larvae ofBrugia pahangi
    • Devaney E., Jecock R. M. The expression of the Mr 30,000 antigen in the third stage larvae ofBrugia pahangi. Parasite Immunology. 13:1991;75-87.
    • (1991) Parasite Immunology , vol.13 , pp. 75-87
    • Devaney, E.1    Jecock, R.M.2
  • 11
    • 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. European Journal of Biochemistry. 133:1983;51-69.
    • (1983) European Journal of Biochemistry , vol.133 , pp. 51-69
    • Epp, O.1    Ladenstein, R.2    Wendel, A.3
  • 12
    • 0022456422 scopus 로고
    • Nucleotide sequence of the btuCED genes involved in vitamin B12 transport inEscherichia coli
    • Friedrich M. J., Deveaux L. C., Kadner R. J. Nucleotide sequence of the btuCED genes involved in vitamin B12 transport inEscherichia coli. Journal of Bacteriology. 167:1986;928-934.
    • (1986) Journal of Bacteriology , vol.167 , pp. 928-934
    • Friedrich, M.J.1    Deveaux, L.C.2    Kadner, R.J.3
  • 13
    • 0025602326 scopus 로고
    • A mouse cDNA sequence for epididymal androgen-regulated proteins related to glutathione peroxidase
    • Ghyselinck N. B., Dufaure J. P. A mouse cDNA sequence for epididymal androgen-regulated proteins related to glutathione peroxidase. Nucleic Acids Research. 18:1990;7144.
    • (1990) Nucleic Acids Research , vol.18 , pp. 7144
    • Ghyselinck, N.B.1    Dufaure, J.P.2
  • 15
    • 0002508819 scopus 로고
    • Protection against oxidants in biological systems: The superoxide theory of oxygen toxicity
    • Oxford: Clarendon. p. 86-187
    • Halliwell B., Gutteridge J. M. C. Protection against oxidants in biological systems: the superoxide theory of oxygen toxicity. Free Radicals in Biology and Medicine. 1989;Clarendon, Oxford. p. 86-187.
    • (1989) Free Radicals in Biology and Medicine
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 17
    • 0027562881 scopus 로고
    • Molecular characterization of salt-stress-associated protein in citrus: Protein and cDNA sequence homology to mammalian glutathione peroxidases
    • Holland D., Ben-Hayyim G., Flatin Z., Camoin L., Strosberg A. D., Eshdat Y. Molecular characterization of salt-stress-associated protein in citrus: Protein and cDNA sequence homology to mammalian glutathione peroxidases. Plant Molecular Biology. 21:1993;923-927.
    • (1993) Plant Molecular Biology , vol.21 , pp. 923-927
    • Holland, D.1    Ben-Hayyim, G.2    Flatin, Z.3    Camoin, L.4    Strosberg, A.D.5    Eshdat, Y.6
  • 23
    • 0029816278 scopus 로고    scopus 로고
    • Expression and characterization of glutathione peroxidase activity in the human blood flukeSchistosoma mansoni
    • Mei H., Thakur A., Schwartz J., LoVerde P. T. Expression and characterization of glutathione peroxidase activity in the human blood flukeSchistosoma mansoni. Infection and Immunity. 64:1996;4299-4306.
    • (1996) Infection and Immunity , vol.64 , pp. 4299-4306
    • Mei, H.1    Thakur, A.2    Schwartz, J.3    Loverde, P.T.4
  • 24
    • 0001537409 scopus 로고
    • Characterization of a selenium-independent glutathione peroxidase fromEuglena gracilis
    • Overbaugh J. M., Fall R. Characterization of a selenium-independent glutathione peroxidase fromEuglena gracilis. Plant Physiology. 77:1985;437-442.
    • (1985) Plant Physiology , vol.77 , pp. 437-442
    • Overbaugh, J.M.1    Fall, R.2
  • 25
    • 0026714544 scopus 로고
    • Genetic evidence for an androgen-regulated epididymal secretory glutathione peroxidase whose transcript does not contain a selenocysteine codon
    • Perry A. C. F., Jones R., Niang L. S. P., Jackson R. M., Hall L. Genetic evidence for an androgen-regulated epididymal secretory glutathione peroxidase whose transcript does not contain a selenocysteine codon. Journal of Biochemistry. 285:1992;863-870.
    • (1992) Journal of Biochemistry , vol.285 , pp. 863-870
    • Perry, A.C.F.1    Jones, R.2    Niang, L.S.P.3    Jackson, R.M.4    Hall, L.5
  • 26
    • 0026587399 scopus 로고
    • Purification and properties of a recombinant sulfur analog of murine selenium-glutathione peroxidase
    • Rocher C., Lalanne J. L., Chaudière J. Purification and properties of a recombinant sulfur analog of murine selenium-glutathione peroxidase. European Journal of Biochemistry. 205:1992;955-960.
    • (1992) European Journal of Biochemistry , vol.205 , pp. 955-960
    • Rocher, C.1    Lalanne, J.L.2    Chaudière, J.3
  • 27
    • 0021151656 scopus 로고
    • Immunological and ultrastructural aspects of the cell-mediated killing ofDirofilaria immitis
    • Rzepczyk C., Bishop C. J. Immunological and ultrastructural aspects of the cell-mediated killing ofDirofilaria immitis. Parasite Immunology. 6:1984;443-457.
    • (1984) Parasite Immunology , vol.6 , pp. 443-457
    • Rzepczyk, C.1    Bishop, C.J.2
  • 30
    • 0029100111 scopus 로고
    • Heterologous expression and enzymatic properties of a selenium-independent glutathione peroxidase from the parasitic nematodeBrugia pahangi
    • Tang L., Gounaris K., Griffiths C., Selkirk M. E. Heterologous expression and enzymatic properties of a selenium-independent glutathione peroxidase from the parasitic nematodeBrugia pahangi. The Journal of Biological Chemistry. 270:1995;18313-18318.
    • (1995) The Journal of Biological Chemistry , vol.270 , pp. 18313-18318
    • Tang, L.1    Gounaris, K.2    Griffiths, C.3    Selkirk, M.E.4
  • 32
    • 0026636510 scopus 로고
    • Construction of Cu-Zn superoxide dismutase deletion mutants ofBrucella abortus:in vitroin vivo
    • Tatum F. M., Detilleux P. G., Sacks J. M., Halling S. M. Construction of Cu-Zn superoxide dismutase deletion mutants ofBrucella abortus:in vitroin vivo. Infection and Immunity. 60:1992;2863-2869.
    • (1992) Infection and Immunity , vol.60 , pp. 2863-2869
    • Tatum, F.M.1    Detilleux, P.G.2    Sacks, J.M.3    Halling, S.M.4
  • 33
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proceedings of the National Academy of Sciences of the USA. 76:1979;4350-4354.
    • (1979) Proceedings of the National Academy of Sciences of the USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 35
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • Von Heijne G. A new method for predicting signal sequence cleavage sites. Nucleic Acids Research. 14:1986;4683-4690.
    • (1986) Nucleic Acids Research , vol.14 , pp. 4683-4690
    • Von Heijne, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.