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Volumn 127, Issue 3, 2011, Pages 693-701

Echinococcus multilocularis: Identification and functional characterization of cathepsin B-like peptidases from metacestode

Author keywords

Cathepsin B like peptidase; Cestode; Echinococcus multilocularis; Host proteins; Metacestode; Recombinant enzyme

Indexed keywords

ALBUMIN; CATHEPSIN B LIKE PEPTIDASE 1; CATHEPSIN B LIKE PEPTIDASE 2; COLLAGEN TYPE 1; COLLAGEN TYPE 4; FIBRONECTIN; IMMUNOGLOBULIN G; PEPTIDASE; RECOMBINANT ENZYME; UNCLASSIFIED DRUG;

EID: 79951723913     PISSN: 00144894     EISSN: 10902449     Source Type: Journal    
DOI: 10.1016/j.exppara.2010.11.005     Document Type: Article
Times cited : (15)

References (40)
  • 2
    • 33845805614 scopus 로고    scopus 로고
    • Effect of a cysteine protease inhibitor on Fasciola hepatica (liver fluke) fecundity, egg viability, parasite burden, and size in experimentally infected sheep
    • Alcala-Canto Y., Ibarra-Velarde F., Sumano-Lopez H., Gracia-Mora J., Alberti-Navarro A. Effect of a cysteine protease inhibitor on Fasciola hepatica (liver fluke) fecundity, egg viability, parasite burden, and size in experimentally infected sheep. Parasitology Research 2007, 100:461-465.
    • (2007) Parasitology Research , vol.100 , pp. 461-465
    • Alcala-Canto, Y.1    Ibarra-Velarde, F.2    Sumano-Lopez, H.3    Gracia-Mora, J.4    Alberti-Navarro, A.5
  • 4
    • 0032438791 scopus 로고    scopus 로고
    • The influence of Ala205 on the specificity of cathepsin L produced by dextran sulfate assisted activation of the recombinant proenzyme
    • Barlic-Maganja D., Dolinar M., Turk V. The influence of Ala205 on the specificity of cathepsin L produced by dextran sulfate assisted activation of the recombinant proenzyme. Biological Chemistry 1998, 379:1449-1452.
    • (1998) Biological Chemistry , vol.379 , pp. 1449-1452
    • Barlic-Maganja, D.1    Dolinar, M.2    Turk, V.3
  • 7
    • 0019765848 scopus 로고
    • Cathepsin B, Cathepsin H, and cathepsin L
    • Barrett A.J., Kirschke H. Cathepsin B, Cathepsin H, and cathepsin L. Methods in Enzymology 1981, 80:535-561.
    • (1981) Methods in Enzymology , vol.80 , pp. 535-561
    • Barrett, A.J.1    Kirschke, H.2
  • 12
    • 0026661928 scopus 로고
    • Characterization of recombinant rat cathepsin B and nonglycosylated mutants expressed in yeast. New insights into the pH dependence of cathepsin B-catalyzed hydrolyses
    • Hasnain S., Hirama T., Tam A., Mort J.S. Characterization of recombinant rat cathepsin B and nonglycosylated mutants expressed in yeast. New insights into the pH dependence of cathepsin B-catalyzed hydrolyses. The Journal of Biological Chemistry 1992, 267:4713-4721.
    • (1992) The Journal of Biological Chemistry , vol.267 , pp. 4713-4721
    • Hasnain, S.1    Hirama, T.2    Tam, A.3    Mort, J.S.4
  • 14
    • 7944232696 scopus 로고    scopus 로고
    • Science review: extracellular acidosis and the immune response: clinical and physiologic implications
    • Kellum J.A., Song M., Li J. Science review: extracellular acidosis and the immune response: clinical and physiologic implications. Critical Care 2004, 8:331-336.
    • (2004) Critical Care , vol.8 , pp. 331-336
    • Kellum, J.A.1    Song, M.2    Li, J.3
  • 15
    • 31944452249 scopus 로고    scopus 로고
    • Medical treatment of echinococcosis under the guidance of Good Clinical Practice (GCP/ICH)
    • Kern P. Medical treatment of echinococcosis under the guidance of Good Clinical Practice (GCP/ICH). Parasitology International 2006, 55 Suppl:S273-S282.
    • (2006) Parasitology International , vol.55 , Issue.SUPPL
    • Kern, P.1
  • 16
    • 0026075381 scopus 로고
    • Metalloproteinases in the larvae of Echinococcus granulosus
    • Marco M., Nieto A. Metalloproteinases in the larvae of Echinococcus granulosus. International Journal for Parasitology 1991, 21:743-746.
    • (1991) International Journal for Parasitology , vol.21 , pp. 743-746
    • Marco, M.1    Nieto, A.2
  • 19
    • 0021918507 scopus 로고
    • Isolation, fractionation and partial characterization of the tegumental surface from protoscoleces of the hydatid organism, Echinococcus granulosus
    • McManus D.P., Barrett N.J. Isolation, fractionation and partial characterization of the tegumental surface from protoscoleces of the hydatid organism, Echinococcus granulosus. Parasitology 1985, 90:111-129.
    • (1985) Parasitology , vol.90 , pp. 111-129
    • McManus, D.P.1    Barrett, N.J.2
  • 25
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H., Engelbrecht J., Brunak S., von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Engineering 1997, 10:1-6.
    • (1997) Protein Engineering , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    von Heijne, G.4
  • 28
    • 0031106627 scopus 로고    scopus 로고
    • Extracellular matrix: a tool for defining the extracorporeal function of parasite proteases
    • Rhoads M.L., Fetterer R.H. Extracellular matrix: a tool for defining the extracorporeal function of parasite proteases. Parasitology Today 1997, 13:119-122.
    • (1997) Parasitology Today , vol.13 , pp. 119-122
    • Rhoads, M.L.1    Fetterer, R.H.2
  • 33
    • 34447259277 scopus 로고    scopus 로고
    • Cloning and characterization of cathepsin L-like peptidases of Echinococcus multilocularis metacestodes
    • Sako Y., Yamasaki H., Nakaya K., Nakao M., Ito A. Cloning and characterization of cathepsin L-like peptidases of Echinococcus multilocularis metacestodes. Molecular and Biochemical Parasitology 2007, 154:181-189.
    • (2007) Molecular and Biochemical Parasitology , vol.154 , pp. 181-189
    • Sako, Y.1    Yamasaki, H.2    Nakaya, K.3    Nakao, M.4    Ito, A.5
  • 34
    • 17844382740 scopus 로고    scopus 로고
    • Degranulation of human eosinophils induced by Paragonimus westermani-secreted protease
    • Shin M.H., Chung Y.B., Kita H. Degranulation of human eosinophils induced by Paragonimus westermani-secreted protease. Korean Journal of Parasitology 2005, 43:33-37.
    • (2005) Korean Journal of Parasitology , vol.43 , pp. 33-37
    • Shin, M.H.1    Chung, Y.B.2    Kita, H.3
  • 35
    • 77956874519 scopus 로고    scopus 로고
    • Cathepsin B proteases of flukes: the key to facilitating parasite control?
    • Smooker P.M., Jayaraj R., Pike R.N., Spithill T.W. Cathepsin B proteases of flukes: the key to facilitating parasite control?. Trends in Parasitology 2010, 26:506-514.
    • (2010) Trends in Parasitology , vol.26 , pp. 506-514
    • Smooker, P.M.1    Jayaraj, R.2    Pike, R.N.3    Spithill, T.W.4
  • 37
    • 0001884468 scopus 로고
    • Biology and systematics of Echinococcus
    • CAB International, Wallingford, UK, R.C.A. Thompson, A.J. Lymbery (Eds.)
    • Thompson R.C.A. Biology and systematics of Echinococcus. Echinococcus and Hydatid Disease 1995, 1-50. CAB International, Wallingford, UK. R.C.A. Thompson, A.J. Lymbery (Eds.).
    • (1995) Echinococcus and Hydatid Disease , pp. 1-50
    • Thompson, R.C.A.1
  • 39
    • 0034615570 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: more than scavengers
    • Turk B., Turk D., Turk V. Lysosomal cysteine proteases: more than scavengers. Biochimica et Biophysica Acta 2000, 1477:98-111.
    • (2000) Biochimica et Biophysica Acta , vol.1477 , pp. 98-111
    • Turk, B.1    Turk, D.2    Turk, V.3
  • 40
    • 0033610817 scopus 로고    scopus 로고
    • Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization
    • Wang B., Shi G.P., Yao P.M., Li Z., Chapman H.A., Bromme D. Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization. The Journal of Biological Chemistry 1998, 273:32000-32008.
    • (1998) The Journal of Biological Chemistry , vol.273 , pp. 32000-32008
    • Wang, B.1    Shi, G.P.2    Yao, P.M.3    Li, Z.4    Chapman, H.A.5    Bromme, D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.