메뉴 건너뛰기




Volumn 6, Issue 7, 2007, Pages 1130-1136

Use of recombinant Entamoeba histolytica cysteine proteinase 1 to identify a potent inhibitor of amebic invasion in a human colonic model

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE PROTEINASE; CYSTEINE PROTEINASE I; CYSTEINE PROTEINASE INHIBITOR; DIVINYL SULFONE; PROTOZOAL PROTEIN; RECOMBINANT PROTEIN; SULFONE; UNCLASSIFIED DRUG; VIRULENCE FACTOR;

EID: 34447576973     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.00094-07     Document Type: Article
Times cited : (68)

References (56)
  • 1
    • 33846697738 scopus 로고    scopus 로고
    • Schistosomiasis mansoni: Novel chemotherapy using a cysteine protease inhibitor
    • Abdulla, M. H., K.-C. Lim, M. Sajid, J. H. McKerrow, and C. R. Caffrey. 2007. Schistosomiasis mansoni: novel chemotherapy using a cysteine protease inhibitor. PLoS Med. 4:e14.
    • (2007) PLoS Med , vol.4
    • Abdulla, M.H.1    Lim, K.-C.2    Sajid, M.3    McKerrow, J.H.4    Caffrey, C.R.5
  • 2
    • 0032918535 scopus 로고    scopus 로고
    • Antisense inhibition of expression of cysteine proteinases affects Entamoeba histolytica-induced formation of liver abscess in hamsters
    • Ankri, S., T. Stolarsky, R. Bracha, F. Padilla-Vaca, and D. Mirelman. 1999. Antisense inhibition of expression of cysteine proteinases affects Entamoeba histolytica-induced formation of liver abscess in hamsters. Infect. Immun. 67:421-422.
    • (1999) Infect. Immun , vol.67 , pp. 421-422
    • Ankri, S.1    Stolarsky, T.2    Bracha, R.3    Padilla-Vaca, F.4    Mirelman, D.5
  • 3
    • 0032789940 scopus 로고    scopus 로고
    • A new protein folding screen: Application to the ligand binding domains of glutamate and kinate receptor and to lysozyme and carbonic anhydrase
    • Armstrong, N., A. De Lencastre, and E. Gouaux. 1999. A new protein folding screen: application to the ligand binding domains of glutamate and kinate receptor and to lysozyme and carbonic anhydrase. Protein Sci. 8:1475-1483.
    • (1999) Protein Sci , vol.8 , pp. 1475-1483
    • Armstrong, N.1    De Lencastre, A.2    Gouaux, E.3
  • 4
    • 0029003409 scopus 로고
    • Theoretical and practical aspects of proteinase inhibition kinetics
    • Bieth, J. G. 1995. Theoretical and practical aspects of proteinase inhibition kinetics. Methods Enzymol. 248:59-84.
    • (1995) Methods Enzymol , vol.248 , pp. 59-84
    • Bieth, J.G.1
  • 5
    • 0029802679 scopus 로고    scopus 로고
    • Entamoeba histolytica and Entamoeba dispar: Differences in numbers and expression of cysteine proteinase genes
    • Bruchhaus, I., T. Jacobs, M. Leippe, and E. Tannich. 1996. Entamoeba histolytica and Entamoeba dispar: differences in numbers and expression of cysteine proteinase genes. Mol. Microbiol. 22:255-263.
    • (1996) Mol. Microbiol , vol.22 , pp. 255-263
    • Bruchhaus, I.1    Jacobs, T.2    Leippe, M.3    Tannich, E.4
  • 6
    • 0038482128 scopus 로고    scopus 로고
    • The intestinal protozoan parasite Entamoeba histolytica contains 20 cysteine protease genes, of which only a small subset is expressed during in vitro cultivation
    • Bruchhaus, I., B. J. Loftus, N. Hall, and E. Tannich. 2003. The intestinal protozoan parasite Entamoeba histolytica contains 20 cysteine protease genes, of which only a small subset is expressed during in vitro cultivation. Eukaryot. Cell 2:501-509
    • (2003) Eukaryot. Cell , vol.2 , pp. 501-509
    • Bruchhaus, I.1    Loftus, B.J.2    Hall, N.3    Tannich, E.4
  • 8
    • 33845423619 scopus 로고    scopus 로고
    • Davis, P. H., J. Schulze, and S. L. Stanley, Jr. 2007. Transcriptomic comparison of two Entamoeba histolytica strains with defined virulence phenotypes identifies new virulence factor candidates and key differences in the expression patterns of cysteine proteases, lectin light chains, and calmodulin. Mol. Biochem. Parasitol. 151:118-128.
    • Davis, P. H., J. Schulze, and S. L. Stanley, Jr. 2007. Transcriptomic comparison of two Entamoeba histolytica strains with defined virulence phenotypes identifies new virulence factor candidates and key differences in the expression patterns of cysteine proteases, lectin light chains, and calmodulin. Mol. Biochem. Parasitol. 151:118-128.
  • 9
    • 0017846267 scopus 로고
    • A new medium for the axenic cultivation of Entamoeba histolytica and other Entamoeba
    • Diamond, L. S., D. R. Harlow, and C. C. Cunnick. 1978. A new medium for the axenic cultivation of Entamoeba histolytica and other Entamoeba. Trans. R. Soc. Trop. Med. Hyg. 72:431-432.
    • (1978) Trans. R. Soc. Trop. Med. Hyg , vol.72 , pp. 431-432
    • Diamond, L.S.1    Harlow, D.R.2    Cunnick, C.C.3
  • 10
    • 0032541311 scopus 로고    scopus 로고
    • Cysteine proteinase inhibitors cure an experimental Trypanosoma cruzi infection
    • Engel, J. C., P. S. Doyle, I. Hsieh, and J. H. McKerrow. 1998. Cysteine proteinase inhibitors cure an experimental Trypanosoma cruzi infection. J. Exp. Med. 188:725-734.
    • (1998) J. Exp. Med , vol.188 , pp. 725-734
    • Engel, J.C.1    Doyle, P.S.2    Hsieh, I.3    McKerrow, J.H.4
  • 11
    • 33646529123 scopus 로고    scopus 로고
    • Gilchrist, C. A., E. Houpt, N. Trapaidze, Z. Fei, O. Crasta, A. Asgharpour, C. Evans, S. Martino-Catt, D. J. Baba, S. Stroup, S. Hamano, G. Ehrenkaufer, M. Okada, U. Singh, T. Nozaki, B. J. Mann, and W. A. Petri, Jr. 2006. Impact of intestinal colonization and invasion on the Entamoeba histolytica transcriptome. Mol. Biochem. Parasitol. 147:163-176.
    • Gilchrist, C. A., E. Houpt, N. Trapaidze, Z. Fei, O. Crasta, A. Asgharpour, C. Evans, S. Martino-Catt, D. J. Baba, S. Stroup, S. Hamano, G. Ehrenkaufer, M. Okada, U. Singh, T. Nozaki, B. J. Mann, and W. A. Petri, Jr. 2006. Impact of intestinal colonization and invasion on the Entamoeba histolytica transcriptome. Mol. Biochem. Parasitol. 147:163-176.
  • 12
    • 0035877015 scopus 로고    scopus 로고
    • Amebiasis and mucosal IgA antibody against the Entamoeba histolytica adherence lectin in Bangladeshi children
    • Haque, R., I. M. Ali, R. B. Sack, B. M. Farr, G. Ramakrishnan, and W. A. Petri. 2001. Amebiasis and mucosal IgA antibody against the Entamoeba histolytica adherence lectin in Bangladeshi children. J. Infect. Dis. 183:1787-1793.
    • (2001) J. Infect. Dis , vol.183 , pp. 1787-1793
    • Haque, R.1    Ali, I.M.2    Sack, R.B.3    Farr, B.M.4    Ramakrishnan, G.5    Petri, W.A.6
  • 15
    • 0034608931 scopus 로고    scopus 로고
    • A rapid and general profiling of protease specificity by using combinational fluorogenic substrate libraries
    • Harris, J. L., B. J. Backes, F. Leonetti, S. Mahrus, J. A. Elfman, and C. S. Craik. 2000. A rapid and general profiling of protease specificity by using combinational fluorogenic substrate libraries. Proc. Natl. Acad. Sci. USA 97:7754-7759.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7754-7759
    • Harris, J.L.1    Backes, B.J.2    Leonetti, F.3    Mahrus, S.4    Elfman, J.A.5    Craik, C.S.6
  • 16
    • 0033967291 scopus 로고    scopus 로고
    • Two major 'higher molecular mass proteinases' of Entamoeba histolytica are identified as cysteine proteinases 1 and 2
    • Hellberg, A., M. Leippe, and I. Bruchhaus. 2000. Two major 'higher molecular mass proteinases' of Entamoeba histolytica are identified as cysteine proteinases 1 and 2. Mol. Biochem. Parasitol. 105:305-309.
    • (2000) Mol. Biochem. Parasitol , vol.105 , pp. 305-309
    • Hellberg, A.1    Leippe, M.2    Bruchhaus, I.3
  • 18
    • 0031962434 scopus 로고    scopus 로고
    • Isolation and molecular characterization of a surface-bound proteinase of Entamoeba histolytica
    • Jacobs, T., I. Bruchhaus, T. Dandekar, E. Tannich, and M. Leippe. 1998. Isolation and molecular characterization of a surface-bound proteinase of Entamoeba histolytica. Mol. Microbiol. 27:269-276.
    • (1998) Mol. Microbiol , vol.27 , pp. 269-276
    • Jacobs, T.1    Bruchhaus, I.2    Dandekar, T.3    Tannich, E.4    Leippe, M.5
  • 19
    • 0022607021 scopus 로고
    • The major neutral proteinase of Entamoeba histolytica
    • Keene, W. E., M. G. Pettit, S. Allen, and J. H. McKerrow. 1986. The major neutral proteinase of Entamoeba histolytica. J. Exp. Med. 163:536-549.
    • (1986) J. Exp. Med , vol.163 , pp. 536-549
    • Keene, W.E.1    Pettit, M.G.2    Allen, S.3    McKerrow, J.H.4
  • 20
    • 0025040467 scopus 로고
    • Entamoeba histolytica: Correlation of the cytopathic effect of virulent trophozoites with secretion of cysteine proteinase
    • Keene, W. E., M. E. Hidalgo, E. Orozco, and J. H. McKerrow. 1990. Entamoeba histolytica: correlation of the cytopathic effect of virulent trophozoites with secretion of cysteine proteinase. Exp. Parasitol. 71:199-206.
    • (1990) Exp. Parasitol , vol.71 , pp. 199-206
    • Keene, W.E.1    Hidalgo, M.E.2    Orozco, E.3    McKerrow, J.H.4
  • 21
    • 0027491336 scopus 로고
    • Degradation of human IgA by Entamoeba histolytica
    • Kelsall, B. L., and J. I. Ravdin. 1993. Degradation of human IgA by Entamoeba histolytica. J. Infect. Dis. 168:1319-1322.
    • (1993) J. Infect. Dis , vol.168 , pp. 1319-1322
    • Kelsall, B.L.1    Ravdin, J.I.2
  • 22
    • 0035853034 scopus 로고    scopus 로고
    • Site specific mutations in the mature form of human IL-18 with enhanced biological activity and decreased neutralization by IL-18 binding protein
    • Kim, S. H., T. Azam, D. Y. Yoon, L. L. Reznikov, D. Novick, M. Rubenstein, and C. A. Dinarello. 2001. Site specific mutations in the mature form of human IL-18 with enhanced biological activity and decreased neutralization by IL-18 binding protein. Proc. Natl. Acad. Sci. USA 98:3304-3309.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3304-3309
    • Kim, S.H.1    Azam, T.2    Yoon, D.Y.3    Reznikov, L.L.4    Novick, D.5    Rubenstein, M.6    Dinarello, C.A.7
  • 23
    • 2442462002 scopus 로고    scopus 로고
    • Proteinase inhibitors TPCK and TLCK prevent Entamoeba histolytica disturbance of tight junctions and microvilli in enteric cell layers in vitro
    • Lauwaet, T., M. J. Oliveira, B. Callewaert, G. De Bruyne, M. Mareel, and A. Leroy. 2004. Proteinase inhibitors TPCK and TLCK prevent Entamoeba histolytica disturbance of tight junctions and microvilli in enteric cell layers in vitro. Int. J. Parasitol. 34:785-794.
    • (2004) Int. J. Parasitol , vol.34 , pp. 785-794
    • Lauwaet, T.1    Oliveira, M.J.2    Callewaert, B.3    De Bruyne, G.4    Mareel, M.5    Leroy, A.6
  • 24
    • 0014106723 scopus 로고
    • Recent modifications of the glycol methacrylate embedding procedure
    • Leduc, E. H., and W. Bernhard. 1967. Recent modifications of the glycol methacrylate embedding procedure. J. Ultrastruct. Res. 19:196-199.
    • (1967) J. Ultrastruct. Res , vol.19 , pp. 196-199
    • Leduc, E.H.1    Bernhard, W.2
  • 25
    • 14544294428 scopus 로고    scopus 로고
    • Loftus, B., I. Anderson, R. Davies, U. C. M. Alsmark, J. Samuelson, P. Amedeo, P. Roncaglia, M. Berriman, R. P. Hirt, B. J. Mann, T. Nozaki, B. Suh, M. Pop, M. Duchene, J. Ackers, E. Tannich, M. Leippe, M. Hofer, I. Bruchhaus, U. Willhoeft, A. Bhattacharya, T. Chillingworth, C. Churcher, Z. Hance, B. Harris, D. Harris, K. Jagels, S. Moule, K. Mungall, D. Ormond, R. Squares, S. Whitehead, M. A. Quail, E. Rabbinowitsch, H. Norbertczak, C. Price, Z. Wang, N. Guillén, C. Gilchrist, S. E. Stroup, S. Bhattacharya, A. Lohia, P. G. Foster, T. Sicheritz-Ponten, C. Weber, U. Singh, C. Mukherjee, N. M. El-Sayed, W. A. Petri, Jr., C. G. Clark, T. M. Embley, B. Barrell, C. M. Fraser, and N. Hall. 2005. The genome of the protist parasite Entamoeba histolytica. Nature 433:865-868.
    • Loftus, B., I. Anderson, R. Davies, U. C. M. Alsmark, J. Samuelson, P. Amedeo, P. Roncaglia, M. Berriman, R. P. Hirt, B. J. Mann, T. Nozaki, B. Suh, M. Pop, M. Duchene, J. Ackers, E. Tannich, M. Leippe, M. Hofer, I. Bruchhaus, U. Willhoeft, A. Bhattacharya, T. Chillingworth, C. Churcher, Z. Hance, B. Harris, D. Harris, K. Jagels, S. Moule, K. Mungall, D. Ormond, R. Squares, S. Whitehead, M. A. Quail, E. Rabbinowitsch, H. Norbertczak, C. Price, Z. Wang, N. Guillén, C. Gilchrist, S. E. Stroup, S. Bhattacharya, A. Lohia, P. G. Foster, T. Sicheritz-Ponten, C. Weber, U. Singh, C. Mukherjee, N. M. El-Sayed, W. A. Petri, Jr., C. G. Clark, T. M. Embley, B. Barrell, C. M. Fraser, and N. Hall. 2005. The genome of the protist parasite Entamoeba histolytica. Nature 433:865-868.
  • 26
    • 2542465880 scopus 로고    scopus 로고
    • Leishmania tropica: Cysteine proteases are essential for growth and pathogenicity
    • Mahmoudzadeh-Niknam, H., and J. H. McKerrow. 2004. Leishmania tropica: cysteine proteases are essential for growth and pathogenicity. Exp. Parasitol. 106:158-163.
    • (2004) Exp. Parasitol , vol.106 , pp. 158-163
    • Mahmoudzadeh-Niknam, H.1    McKerrow, J.H.2
  • 27
    • 0037039894 scopus 로고    scopus 로고
    • Expedient solid phase synthesis of fluorogenic protease substrates using the 7-amino-4-carbamoylmethylcoumarin (ACC) fluorophore
    • Maly, D., F. Leonetti, B. J. Backes, D. S. Dauber, J. L. Harris, C. S. Craik, and J. A. Ellman. 2002. Expedient solid phase synthesis of fluorogenic protease substrates using the 7-amino-4-carbamoylmethylcoumarin (ACC) fluorophore. J. Org. Chem. 67:910-915.
    • (2002) J. Org. Chem , vol.67 , pp. 910-915
    • Maly, D.1    Leonetti, F.2    Backes, B.J.3    Dauber, D.S.4    Harris, J.L.5    Craik, C.S.6    Ellman, J.A.7
  • 28
    • 0036180196 scopus 로고    scopus 로고
    • Ubiquitous production of macrophage migration inhibitory factor by human gastric and intestinal epithelium
    • Masser, C., L. Eckmann, G. Paesold, H. S. Kim, and M. F. Kagnoff. 2002. Ubiquitous production of macrophage migration inhibitory factor by human gastric and intestinal epithelium. Gastroenterology 122:667-680.
    • (2002) Gastroenterology , vol.122 , pp. 667-680
    • Masser, C.1    Eckmann, L.2    Paesold, G.3    Kim, H.S.4    Kagnoff, M.F.5
  • 29
    • 0023219622 scopus 로고
    • Mucosal surface pH of the large intestine of the rat and of normal and inflamed large intestine in man
    • McNeil, N. I., K. L. Ling, and J. Wager. 1987. Mucosal surface pH of the large intestine of the rat and of normal and inflamed large intestine in man. Gut 28:707-713.
    • (1987) Gut , vol.28 , pp. 707-713
    • McNeil, N.I.1    Ling, K.L.2    Wager, J.3
  • 30
    • 34250776178 scopus 로고    scopus 로고
    • Mitra, B. N., Y. Saito-Nakano, K. Nakada-Tsukui, D. Sato, and T. Nozaki. 17 April 2007. RAB11B small GTPase regulates secretion of cysteine proteases in the enteric protozoan parasite Entamoeba histolytica. Cell. Microbiol. [Epub ahead of print.]
    • Mitra, B. N., Y. Saito-Nakano, K. Nakada-Tsukui, D. Sato, and T. Nozaki. 17 April 2007. RAB11B small GTPase regulates secretion of cysteine proteases in the enteric protozoan parasite Entamoeba histolytica. Cell. Microbiol. [Epub ahead of print.]
  • 31
    • 0037305905 scopus 로고    scopus 로고
    • Entamoeba histolytica cysteine proteinases disrupt the polymeric structure of colonic mucin and alter its protective function
    • Moncada, D., K. Keller, and K. Chadee. 2003. Entamoeba histolytica cysteine proteinases disrupt the polymeric structure of colonic mucin and alter its protective function. Infect. Immun. 71:838-844.
    • (2003) Infect. Immun , vol.71 , pp. 838-844
    • Moncada, D.1    Keller, K.2    Chadee, K.3
  • 32
    • 33644849683 scopus 로고    scopus 로고
    • Antisense inhibition of Entamoeba histolytica cysteine proteases inhibits colonic mucus degradation
    • Moncada, D., K. Keller, S. Ankir, D. Mirelman, and K. Chadee. 2006. Antisense inhibition of Entamoeba histolytica cysteine proteases inhibits colonic mucus degradation. Gastroenterology 130:721-730.
    • (2006) Gastroenterology , vol.130 , pp. 721-730
    • Moncada, D.1    Keller, K.2    Ankir, S.3    Mirelman, D.4    Chadee, K.5
  • 33
    • 1642292453 scopus 로고    scopus 로고
    • Identification and biochemical characterization of vivapains, cysteine proteases of the malaria parasite Plasmodium vivax
    • Na, B. K., B. R. Shenai, P. S. Sijwali, Y. Choe, K. C. Pandey, A. Singh, C. S. Craik, and P. J. Rosenthal. 2004. Identification and biochemical characterization of vivapains, cysteine proteases of the malaria parasite Plasmodium vivax. Biochem. J. 378:529-538.
    • (2004) Biochem. J , vol.378 , pp. 529-538
    • Na, B.K.1    Shenai, B.R.2    Sijwali, P.S.3    Choe, Y.4    Pandey, K.C.5    Singh, A.6    Craik, C.S.7    Rosenthal, P.J.8
  • 35
    • 18044389332 scopus 로고    scopus 로고
    • Proteomic analysis of phagocytosis of the protozoan parasite Entamoeba histolytica
    • Okada, M., C. D. Huston, B. J. Mann, W. A. Petri, K. Kita, and T. Nozaki. 2005. Proteomic analysis of phagocytosis of the protozoan parasite Entamoeba histolytica. Eukaryot. Cell 4:827-831.
    • (2005) Eukaryot. Cell , vol.4 , pp. 827-831
    • Okada, M.1    Huston, C.D.2    Mann, B.J.3    Petri, W.A.4    Kita, K.5    Nozaki, T.6
  • 38
    • 0037067759 scopus 로고    scopus 로고
    • The cathepsin B of Toxoplasma gondii, toxopain-1, is critical for parasite invasion and rhoptry protein processing
    • Que, X., H. Ngo, J. Lawton, M. Gray, Q. Liu, J. Engel, L. Brinen, P. Ghosh, K. Joiner, and S. L. Reed. 2002. The cathepsin B of Toxoplasma gondii, toxopain-1, is critical for parasite invasion and rhoptry protein processing. J. Biol. Chem. 277:25791-25797.
    • (2002) J. Biol. Chem , vol.277 , pp. 25791-25797
    • Que, X.1    Ngo, H.2    Lawton, J.3    Gray, M.4    Liu, Q.5    Engel, J.6    Brinen, L.7    Ghosh, P.8    Joiner, K.9    Reed, S.L.10
  • 39
    • 0034041714 scopus 로고    scopus 로고
    • Cysteine proteinases and the pathogenesis of amebiasis
    • Que, X., and S. L. Reed. 2000. Cysteine proteinases and the pathogenesis of amebiasis. Clin. Microbiol. Rev. 13:196-206.
    • (2000) Clin. Microbiol. Rev , vol.13 , pp. 196-206
    • Que, X.1    Reed, S.L.2
  • 40
    • 2142647845 scopus 로고    scopus 로고
    • Toxopain-1 is critical for infection in a novel chicken embryo model of congenital toxoplasmosis
    • Que, X., A. Wunderlich, K. A. Joiner, and S. L. Reed. 2004. Toxopain-1 is critical for infection in a novel chicken embryo model of congenital toxoplasmosis. Infect. Immun. 72:2915-2921.
    • (2004) Infect. Immun , vol.72 , pp. 2915-2921
    • Que, X.1    Wunderlich, A.2    Joiner, K.A.3    Reed, S.L.4
  • 41
    • 0029018428 scopus 로고
    • The extracellular neutral cysteine proteinase of Entamoeba histolytica degrades anaphylatoxins C3a and C5a
    • Reed, S. L., J. A. Ember, D. S. Herdman, R. G. DiScipio, T. E. Hugli, and I. Gigli. 1995. The extracellular neutral cysteine proteinase of Entamoeba histolytica degrades anaphylatoxins C3a and C5a. J. Immunol. 155:266-274.
    • (1995) J. Immunol , vol.155 , pp. 266-274
    • Reed, S.L.1    Ember, J.A.2    Herdman, D.S.3    DiScipio, R.G.4    Hugli, T.E.5    Gigli, I.6
  • 42
    • 0024306669 scopus 로고
    • Thiol proteinase expression and pathogenicity of Entamoeba histolytica
    • Reed, S. L., W. E. Keene, and J. H. McKerrow. 1989. Thiol proteinase expression and pathogenicity of Entamoeba histolytica. J. Clin. Microbiol. 27:2772-2777.
    • (1989) J. Clin. Microbiol , vol.27 , pp. 2772-2777
    • Reed, S.L.1    Keene, W.E.2    McKerrow, J.H.3
  • 43
    • 0024363666 scopus 로고
    • Cleavage of C3 by a neutral cysteine proteinase of Entamoeba histolytica
    • Reed, S. L., W. E. Keene, J. H. McKerrow, and I. Gigli. 1989. Cleavage of C3 by a neutral cysteine proteinase of Entamoeba histolytica. J. Immunol. 143: 189-195.
    • (1989) J. Immunol , vol.143 , pp. 189-195
    • Reed, S.L.1    Keene, W.E.2    McKerrow, J.H.3    Gigli, I.4
  • 44
    • 0036178381 scopus 로고    scopus 로고
    • Cysteine proteases of parasitic organisms
    • Sajid, M., and J. H. McKerrow. 2002. Cysteine proteases of parasitic organisms. Mol. Biochem. Parasitol. 120:1-21.
    • (2002) Mol. Biochem. Parasitol , vol.120 , pp. 1-21
    • Sajid, M.1    McKerrow, J.H.2
  • 46
    • 0031760740 scopus 로고    scopus 로고
    • Epithelial cell-initiated inflammation plays a crucial role in early tissue damage in amebic infection of human intestine
    • Seydel, K. B., E. Li, Z. Zhang, and S. L. Stanley. 1998. Epithelial cell-initiated inflammation plays a crucial role in early tissue damage in amebic infection of human intestine. Gastroenterology 115:1446-1453.
    • (1998) Gastroenterology , vol.115 , pp. 1446-1453
    • Seydel, K.B.1    Li, E.2    Zhang, Z.3    Stanley, S.L.4
  • 47
    • 0034966663 scopus 로고    scopus 로고
    • Systematic optimization of expression and refolding of the Plasmodium falciparum cysteine protease falcipain-2
    • Sijwali, P. S., L. S. Brinen, and P. J. Rosenthal. 2001. Systematic optimization of expression and refolding of the Plasmodium falciparum cysteine protease falcipain-2. Protein Expr. Purif. 22:128-134.
    • (2001) Protein Expr. Purif , vol.22 , pp. 128-134
    • Sijwali, P.S.1    Brinen, L.S.2    Rosenthal, P.J.3
  • 48
    • 0035644195 scopus 로고    scopus 로고
    • Expression and characterization of the Plasmodium falciparum haemoglobinase falcipain-3
    • Sijwali, P. S., B. R. Shenai, J. Gut, A. Singh, and P. J. Rosenthal. 2001. Expression and characterization of the Plasmodium falciparum haemoglobinase falcipain-3. Biochem. J. 360:481-489.
    • (2001) Biochem. J , vol.360 , pp. 481-489
    • Sijwali, P.S.1    Shenai, B.R.2    Gut, J.3    Singh, A.4    Rosenthal, P.J.5
  • 49
    • 0037460789 scopus 로고    scopus 로고
    • Amoebiasis
    • Stanley, S. L. 2003. Amoebiasis. Lancet 361:1025-1034.
    • (2003) Lancet , vol.361 , pp. 1025-1034
    • Stanley, S.L.1
  • 50
    • 0028902211 scopus 로고
    • Role of the Entamoeba histolytica cysteine proteinase in amebic liver abscess formation in severe combined immunodeficient mice
    • Stanley, S. L., T. Zhang, D. Rubin, and E. Li. 1995. Role of the Entamoeba histolytica cysteine proteinase in amebic liver abscess formation in severe combined immunodeficient mice. Infect. Immun. 63:1587-1589.
    • (1995) Infect. Immun , vol.63 , pp. 1587-1589
    • Stanley, S.L.1    Zhang, T.2    Rubin, D.3    Li, E.4
  • 51
    • 0016442534 scopus 로고
    • Electron microscope studies of experimental Entamoeba histolytica infections in the guinea pig. I. Penetration of the intestinal epithelium by trophozoites
    • Takeuchi, A., and B. P. Phillips. 1975. Electron microscope studies of experimental Entamoeba histolytica infections in the guinea pig. I. Penetration of the intestinal epithelium by trophozoites. Am. J. Trop. Med. Hyg. 24:34-48.
    • (1975) Am. J. Trop. Med. Hyg , vol.24 , pp. 34-48
    • Takeuchi, A.1    Phillips, B.P.2
  • 52
    • 0020473244 scopus 로고
    • Determination of the rate constant of enzyme by measuring the substrate reaction in the presence of modifier
    • Tian, W.-X., and C.-L. Tsou. 1982. Determination of the rate constant of enzyme by measuring the substrate reaction in the presence of modifier. Biochemistry 21:1028-1032.
    • (1982) Biochemistry , vol.21 , pp. 1028-1032
    • Tian, W.-X.1    Tsou, C.-L.2
  • 53
    • 0031883488 scopus 로고    scopus 로고
    • The neutral cysteine proteinase of Entamoeba histolytica degrades IgG and prevents its binding
    • Tran, V. Q., D. S. Herdman, B. E. Torian, and S. L. Reed. 1998. The neutral cysteine proteinase of Entamoeba histolytica degrades IgG and prevents its binding. J. Infect. Dis. 177:508-511.
    • (1998) J. Infect. Dis , vol.177 , pp. 508-511
    • Tran, V.Q.1    Herdman, D.S.2    Torian, B.E.3    Reed, S.L.4
  • 54
    • 0032705737 scopus 로고    scopus 로고
    • A DNA sequence corresponding to the gene encoding cysteine proteinase 5 in Entamoeba histolytica is present and positionally conserved but highly degenerated in Entamoeba dispar
    • Willhoeft, V., L. Hamann, and E. Tannich. 1999. A DNA sequence corresponding to the gene encoding cysteine proteinase 5 in Entamoeba histolytica is present and positionally conserved but highly degenerated in Entamoeba dispar. Infect. Immun. 67:5925-5929.
    • (1999) Infect. Immun , vol.67 , pp. 5925-5929
    • Willhoeft, V.1    Hamann, L.2    Tannich, E.3
  • 55
    • 0034243942 scopus 로고    scopus 로고
    • Entamoeba histolytica cysteine proteinases with interleukin-1 beta converting enzyme (ICE) activity cause intestinal inflammation and tissue damage in amoebiasis
    • Zhang, Z., L. Yan, L. Wang, K. B. Seydel, E. Li, S. Ankri, D. Mirelman, and S. L. Stanley. 2000. Entamoeba histolytica cysteine proteinases with interleukin-1 beta converting enzyme (ICE) activity cause intestinal inflammation and tissue damage in amoebiasis. Mol. Microbiol. 37:542-548.
    • (2000) Mol. Microbiol , vol.37 , pp. 542-548
    • Zhang, Z.1    Yan, L.2    Wang, L.3    Seydel, K.B.4    Li, E.5    Ankri, S.6    Mirelman, D.7    Stanley, S.L.8
  • 56
    • 0036894603 scopus 로고    scopus 로고
    • A quantitative analysis of rate-limiting steps in the metastatic cascade using human-specific real-time polymerase chain reaction
    • Zijlstra, A., R. Mellor, G. Panzarella, R. T. Aimes, J. D. Hooper, N. D. Marchenko, and J. P. Quigley. 2002. A quantitative analysis of rate-limiting steps in the metastatic cascade using human-specific real-time polymerase chain reaction. Cancer Res. 62:7083-7092.
    • (2002) Cancer Res , vol.62 , pp. 7083-7092
    • Zijlstra, A.1    Mellor, R.2    Panzarella, G.3    Aimes, R.T.4    Hooper, J.D.5    Marchenko, N.D.6    Quigley, J.P.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.