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Volumn 58, Issue 3, 2009, Pages 311-313

Oxidative folding and reductive activities of EhPDI, a protein disulfide isomerase from Entamoeba histolytica

Author keywords

Entamoeba histolytica; Functional complementation; Mutagenic analysis; Protein disulfide isomerase

Indexed keywords

OXIDOREDUCTASE; PROTEIN DISULFIDE ISOMERASE;

EID: 67650397865     PISSN: 13835769     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.parint.2009.04.001     Document Type: Article
Times cited : (7)

References (26)
  • 1
    • 0034194815 scopus 로고    scopus 로고
    • Pathways for protein disulphide bond formation
    • Frand A.R., Cuozzo J.W., and Kaiser C.A. Pathways for protein disulphide bond formation. Trends Cell Biol 10 (2000) 203-210
    • (2000) Trends Cell Biol , vol.10 , pp. 203-210
    • Frand, A.R.1    Cuozzo, J.W.2    Kaiser, C.A.3
  • 2
    • 0030724094 scopus 로고    scopus 로고
    • Protein disulfide isomerase and assisted protein folding
    • Gilbert H.F. Protein disulfide isomerase and assisted protein folding. J Biol Chem 272 (1997) 29,399-29,402
    • (1997) J Biol Chem , vol.272
    • Gilbert, H.F.1
  • 3
    • 0033210414 scopus 로고
    • Protein disulfide isomerase: the multifunctional redox chaperone of the endoplasmic reticulum
    • Noiva R. Protein disulfide isomerase: the multifunctional redox chaperone of the endoplasmic reticulum. Semin Cell Dev Biol 10 (1990) 481-493
    • (1990) Semin Cell Dev Biol , vol.10 , pp. 481-493
    • Noiva, R.1
  • 4
    • 0025801897 scopus 로고
    • The reactivities and ionization properties of the active-site dithiol groups of mammalian protein disulphide-isomerase
    • Hawkins H.C., and Freedman R.B. The reactivities and ionization properties of the active-site dithiol groups of mammalian protein disulphide-isomerase. Biochem J 275 (1991) 335-339
    • (1991) Biochem J , vol.275 , pp. 335-339
    • Hawkins, H.C.1    Freedman, R.B.2
  • 5
    • 0026705344 scopus 로고
    • Expression and site-directed mutagenesis of human protein disulfide isomerase in Escherichia coli. This multifunctional polypeptide has two independently acting catalytic sites for the isomerase activity
    • Vuori K., Myllylä R., Pihlajaniemi T., and Kivirikko K.I. Expression and site-directed mutagenesis of human protein disulfide isomerase in Escherichia coli. This multifunctional polypeptide has two independently acting catalytic sites for the isomerase activity. J Biol Chem 267 (1992) 7211-7214
    • (1992) J Biol Chem , vol.267 , pp. 7211-7214
    • Vuori, K.1    Myllylä, R.2    Pihlajaniemi, T.3    Kivirikko, K.I.4
  • 6
    • 0030061006 scopus 로고    scopus 로고
    • Catalysis of oxidative protein folding by mutants of protein disulfide isomerase with a single active-site cysteine
    • Walker K.W., Lyles M.M., and Gilbert H.F. Catalysis of oxidative protein folding by mutants of protein disulfide isomerase with a single active-site cysteine. Biochemistry 35 (1996) 1972-1980
    • (1996) Biochemistry , vol.35 , pp. 1972-1980
    • Walker, K.W.1    Lyles, M.M.2    Gilbert, H.F.3
  • 7
    • 0028885790 scopus 로고
    • The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds
    • Laboissiere M.C., Sturley S.L., and Raines R.T. The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds. J Biol Chem 270 (1995) 28,006-28,009
    • (1995) J Biol Chem , vol.270
    • Laboissiere, M.C.1    Sturley, S.L.2    Raines, R.T.3
  • 8
    • 0028850389 scopus 로고
    • Human protein disulfide isomerase functionally complements a dsbA mutation and enhances the yield of pectate lyase C in Escherichia coli
    • Humphreys D.P., Weir N., Mountain A., and Lund P.A. Human protein disulfide isomerase functionally complements a dsbA mutation and enhances the yield of pectate lyase C in Escherichia coli. J Biol Chem 270 (1995) 28,210-28,215
    • (1995) J Biol Chem , vol.270
    • Humphreys, D.P.1    Weir, N.2    Mountain, A.3    Lund, P.A.4
  • 9
    • 0029822654 scopus 로고    scopus 로고
    • An in vivo pathway for disulfide bond isomerization in Escherichia coli
    • Rietsch A., Belin D., Martin N., and Beckwith J. An in vivo pathway for disulfide bond isomerization in Escherichia coli. Proc Natl Acad Sci USA 93 (1996) 13,048-13,053
    • (1996) Proc Natl Acad Sci USA , vol.93
    • Rietsch, A.1    Belin, D.2    Martin, N.3    Beckwith, J.4
  • 10
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • Bardwell J.C., McGovern K., and Beckwith J. Identification of a protein required for disulfide bond formation in vivo. Cell 67 (1991) 581-589
    • (1991) Cell , vol.67 , pp. 581-589
    • Bardwell, J.C.1    McGovern, K.2    Beckwith, J.3
  • 11
    • 0028222390 scopus 로고
    • Effects of DsbA on the disulfide folding of bovine pancreatic trypsin inhibitor and alpha-lactalbumin
    • Zapun A., and Creighton T.E. Effects of DsbA on the disulfide folding of bovine pancreatic trypsin inhibitor and alpha-lactalbumin. Biochemistry 33 (1994) 5202-5211
    • (1994) Biochemistry , vol.33 , pp. 5202-5211
    • Zapun, A.1    Creighton, T.E.2
  • 12
    • 0028296940 scopus 로고
    • The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation
    • Missiakas D., Georgopoulos C., and Raina S. The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation. EMBO J 13 (1994) 2013-2020
    • (1994) EMBO J , vol.13 , pp. 2013-2020
    • Missiakas, D.1    Georgopoulos, C.2    Raina, S.3
  • 13
    • 0028215226 scopus 로고
    • Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity
    • Shevchik V.E., Condemine G., and Robert-Baudouy J. Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity. EMBO J 13 (1994) 2007-2012
    • (1994) EMBO J , vol.13 , pp. 2007-2012
    • Shevchik, V.E.1    Condemine, G.2    Robert-Baudouy, J.3
  • 14
    • 0028949156 scopus 로고
    • Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli
    • Zapun A., Missiakas D., Raina S., and Creighton T.E. Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli. Biochemistry 34 (1995) 5075-5089
    • (1995) Biochemistry , vol.34 , pp. 5075-5089
    • Zapun, A.1    Missiakas, D.2    Raina, S.3    Creighton, T.E.4
  • 16
    • 0036000594 scopus 로고    scopus 로고
    • Structure and function of the Entamoeba histolytica Gal/GalNAc lectin
    • Mann B.J. Structure and function of the Entamoeba histolytica Gal/GalNAc lectin. Int Rev Cytol 216 (2002) 59-80
    • (2002) Int Rev Cytol , vol.216 , pp. 59-80
    • Mann, B.J.1
  • 17
    • 37549067349 scopus 로고    scopus 로고
    • In silico identification of the protein disulfide isomerase family from a protozoan parasite
    • Ramos M.A., Mares R.E., Magaña P.D., Ortega J.E., and Cornejo-Bravo J.M. In silico identification of the protein disulfide isomerase family from a protozoan parasite. Comput Biol Chem 32 (2008) 66-70
    • (2008) Comput Biol Chem , vol.32 , pp. 66-70
    • Ramos, M.A.1    Mares, R.E.2    Magaña, P.D.3    Ortega, J.E.4    Cornejo-Bravo, J.M.5
  • 18
    • 23944476801 scopus 로고    scopus 로고
    • Identification of an Entamoeba histolytica gene encoding a protein disulfide isomerase that functionally complements the dsbA mutation in Escherichia coli
    • Ramos M.A., Sánchez-López R., Mares R.E., Olvera F., and Alagón A. Identification of an Entamoeba histolytica gene encoding a protein disulfide isomerase that functionally complements the dsbA mutation in Escherichia coli. Mol Biochem Parasitol 143 (2005) 236-240
    • (2005) Mol Biochem Parasitol , vol.143 , pp. 236-240
    • Ramos, M.A.1    Sánchez-López, R.2    Mares, R.E.3    Olvera, F.4    Alagón, A.5
  • 19
    • 0025914068 scopus 로고
    • A general method for introducing a series of mutations into cloned DNA using the polymerase chain reaction
    • Ito W., Ishiguro H., and Kurosawa Y. A general method for introducing a series of mutations into cloned DNA using the polymerase chain reaction. Gene 102 (1991) 67-70
    • (1991) Gene , vol.102 , pp. 67-70
    • Ito, W.1    Ishiguro, H.2    Kurosawa, Y.3
  • 20
    • 0026062381 scopus 로고
    • Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer
    • Lyles M.M., and Gilbert H.F. Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer. Biochemistry 30 3 (1991) 613-619
    • (1991) Biochemistry , vol.30 , Issue.3 , pp. 613-619
    • Lyles, M.M.1    Gilbert, H.F.2
  • 21
    • 0018723651 scopus 로고
    • Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide
    • Holmgren A. Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide. J Biol Chem 254 (1979) 9627-9632
    • (1979) J Biol Chem , vol.254 , pp. 9627-9632
    • Holmgren, A.1
  • 22
    • 0036087747 scopus 로고    scopus 로고
    • Identification of a disulfide isomerase protein of Leishmania major as a putative virulence factor
    • Ben Achour Y., Chenik M., Louzir H., and Dellagi K. Identification of a disulfide isomerase protein of Leishmania major as a putative virulence factor. Infect Immun 70 (2002) 3576-3585
    • (2002) Infect Immun , vol.70 , pp. 3576-3585
    • Ben Achour, Y.1    Chenik, M.2    Louzir, H.3    Dellagi, K.4
  • 23
    • 33947367471 scopus 로고    scopus 로고
    • Biochemical properties and cellular localization of Plasmodium falciparum protein disulfide isomerase
    • Mouray E., Moutiez M., Girault S., Sergheraert C., Florent I., and Grellier P. Biochemical properties and cellular localization of Plasmodium falciparum protein disulfide isomerase. Biochimie 89 3 (2007) 337-346
    • (2007) Biochimie , vol.89 , Issue.3 , pp. 337-346
    • Mouray, E.1    Moutiez, M.2    Girault, S.3    Sergheraert, C.4    Florent, I.5    Grellier, P.6
  • 24
    • 37349023592 scopus 로고    scopus 로고
    • Neospora caninum: functional inhibition of protein disulfide isomerase by the broad-spectrum anti-parasitic drug nitazoxanide and other thiazolides
    • Müller J., Naguleswaran A., Müller N., and Hemphill A. Neospora caninum: functional inhibition of protein disulfide isomerase by the broad-spectrum anti-parasitic drug nitazoxanide and other thiazolides. Exp Parasitol 118 (2008) 80-88
    • (2008) Exp Parasitol , vol.118 , pp. 80-88
    • Müller, J.1    Naguleswaran, A.2    Müller, N.3    Hemphill, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.