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Volumn 14, Issue 9, 2008, Pages 889-900

Drugs targeting parasite lysosomes

Author keywords

[No Author keywords available]

Indexed keywords

AMPHOTERICIN B DEOXYCHOLATE; ARTEMISIA ANNUA EXTRACT; ARTEMISININ; BENZNIDAZOLE; CATHEPSIN B INHIBITOR; CHLOROQUINE; CLINDAMYCIN; CYSTEINE PROTEINASE INHIBITOR; EFLORNITHINE; FOLINIC ACID; K 11777; K 777; MEGLUMINE ANTIMONATE; MELARSOPROL; METRONIDAZOLE; NIFURTIMOX; NITRILE INHIBITOR; NITROIMIDAZOLE DERIVATIVE; PAROMOMYCIN; PENTAMIDINE; PENTAMIDINE MESYLATE; PYRIMETHAMINE; QUININE; STIBOGLUCONATE SODIUM; SULFADIAZINE; SULFANILAMIDE DERIVATIVE; SURAMIN; THIOSEMICARBAZONE DERIVATIVE; TINIDAZOLE; TRIMETHOPRIM; UNINDEXED DRUG;

EID: 44349190903     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/138161208784041060     Document Type: Review
Times cited : (17)

References (191)
  • 1
    • 33751080094 scopus 로고    scopus 로고
    • Drug discovery and development for neglected parasitic diseases
    • Renslo AR, McKerrow JH. Drug discovery and development for neglected parasitic diseases. Nat Chem Biol 2006; 2: 701-10.
    • (2006) Nat Chem Biol , vol.2 , pp. 701-710
    • Renslo, A.R.1    McKerrow, J.H.2
  • 2
    • 34249019920 scopus 로고    scopus 로고
    • Intracellular protein degradation: From the vague idea thru the lysosome and ubiquitin-proteasome system and onto human disease and drug targeting
    • Ciechanover A. Intracellular protein degradation: From the vague idea thru the lysosome and ubiquitin-proteasome system and onto human disease and drug targeting. Hematology 2006; 1: 1-12.
    • (2006) Hematology , vol.1 , pp. 1-12
    • Ciechanover, A.1
  • 3
    • 0343067073 scopus 로고    scopus 로고
    • Lysosome membrane permeability: Implications for drug delivery
    • Lloyd JB. Lysosome membrane permeability: Implications for drug delivery. Adv. Drug Deliv Rev 2000; 41: 189-200.
    • (2000) Adv. Drug Deliv Rev , vol.41 , pp. 189-200
    • Lloyd, J.B.1
  • 5
    • 0032542285 scopus 로고    scopus 로고
    • An asparaginyl endopeptidase processes a microbial antigen for class II MHC presentation
    • Manoury B, Hewitt EW, Morrice N, Dando PM, Barret AJ, Watts C. An asparaginyl endopeptidase processes a microbial antigen for class II MHC presentation. Nature 1998; 396: 625-7.
    • (1998) Nature , vol.396 , pp. 625-627
    • Manoury, B.1    Hewitt, E.W.2    Morrice, N.3    Dando, P.M.4    Barret, A.J.5    Watts, C.6
  • 6
    • 33947367425 scopus 로고    scopus 로고
    • Abnormal expressions of the subunits of the UDP-N-acetylglucosamine: Lysosomal enzyme, N-acetylglucosamine-1-phosphotransferase, result in the formation of cytoplasmic vacuoles resembling those of the I-cells
    • Ho CY, Tang NL, Yeung AK, Lau AK, Hui J, Lo AW. Abnormal expressions of the subunits of the UDP-N-acetylglucosamine: Lysosomal enzyme, N-acetylglucosamine-1-phosphotransferase, result in the formation of cytoplasmic vacuoles resembling those of the I-cells. J Mol Med 2007; 85: 351-60.
    • (2007) J Mol Med , vol.85 , pp. 351-360
    • Ho, C.Y.1    Tang, N.L.2    Yeung, A.K.3    Lau, A.K.4    Hui, J.5    Lo, A.W.6
  • 7
    • 34548513526 scopus 로고    scopus 로고
    • The N-acylethanolamine-hydrolyzing acid amidase (NAAA)
    • Tsuboi K, Takezaki N, Ueda N. The N-acylethanolamine-hydrolyzing acid amidase (NAAA). Chem Biodivers 2007; 4: 1914-25.
    • (2007) Chem Biodivers , vol.4 , pp. 1914-1925
    • Tsuboi, K.1    Takezaki, N.2    Ueda, N.3
  • 8
    • 33947395690 scopus 로고    scopus 로고
    • Legumain/asparaginyl endopeptidase controls extracellular matrix remodeling through the degradation of fibronectin in mouse renal proximmal tubular cells
    • Morita Y, Araki H, Sugimoto T, Takeuchi K, Yamane T, Maeda T, et al. Legumain/asparaginyl endopeptidase controls extracellular matrix remodeling through the degradation of fibronectin in mouse renal proximmal tubular cells. FEBS Lett 2007; 581: 1417-24.
    • (2007) FEBS Lett , vol.581 , pp. 1417-1424
    • Morita, Y.1    Araki, H.2    Sugimoto, T.3    Takeuchi, K.4    Yamane, T.5    Maeda, T.6
  • 9
    • 33846517681 scopus 로고    scopus 로고
    • Chloride and the endosomal-lysosomal pathway: Emerging roles of CLC chloride transporters
    • Jentsch TJ. Chloride and the endosomal-lysosomal pathway: Emerging roles of CLC chloride transporters. J Physiol 2007; 578: 663-70.
    • (2007) J Physiol , vol.578 , pp. 663-670
    • Jentsch, T.J.1
  • 10
  • 11
    • 0037459016 scopus 로고    scopus 로고
    • Two lysosomal membrane proteins, LGP85 and LGP107, are delivered to late endosomes/lysosomes through different intracellular routes after exiting from the trans-Golgi network
    • Niwa K, Tanaka R, Murase H, Ishikawa T, Fujita H, Himeno M, et al. Two lysosomal membrane proteins, LGP85 and LGP107, are delivered to late endosomes/lysosomes through different intracellular routes after exiting from the trans-Golgi network. Biochem Biophys Res Commun 2003; 301: 833-40.
    • (2003) Biochem Biophys Res Commun , vol.301 , pp. 833-840
    • Niwa, K.1    Tanaka, R.2    Murase, H.3    Ishikawa, T.4    Fujita, H.5    Himeno, M.6
  • 12
    • 44349191860 scopus 로고    scopus 로고
    • Ubiquitin trafficking to the lysosome: Keeping the house tidy and getting rid of unwanted guests
    • Purdy GE, Russell DG. Ubiquitin trafficking to the lysosome: Keeping the house tidy and getting rid of unwanted guests. Proc Natl Acad Sci TNA 2007; 104: 6031-6.
    • (2007) Proc Natl Acad Sci TNA , vol.104 , pp. 6031-6036
    • Purdy, G.E.1    Russell, D.G.2
  • 13
    • 35748970461 scopus 로고    scopus 로고
    • Hepatocyte growth factor-regulated tyrosine kinase substrate (HRS) mediates post-endocytic trafficking of protease-activated receptor 2 and calcitonin receptor-like receptor
    • Hasdemir B, Bunnett NW, Conttrell GS. Hepatocyte growth factor-regulated tyrosine kinase substrate (HRS) mediates post-endocytic trafficking of protease-activated receptor 2 and calcitonin receptor-like receptor. J Biol Chem 2007; 282(40): 29646-57.
    • (2007) J Biol Chem , vol.282 , Issue.40 , pp. 29646-29657
    • Hasdemir, B.1    Bunnett, N.W.2    Conttrell, G.S.3
  • 14
    • 33846821720 scopus 로고    scopus 로고
    • Sorting of Fas ligand to secretory lysosomes is regulated by mono-ubiquitylation and phosphorylation
    • Zuccato E, Blott EJ, Holt O, Sigismund S, Shaw M, Bossi G, et al. Sorting of Fas ligand to secretory lysosomes is regulated by mono-ubiquitylation and phosphorylation. J Cell Sci 2007; 120: 191-9
    • (2007) J Cell Sci , vol.120 , pp. 191-199
    • Zuccato, E.1    Blott, E.J.2    Holt, O.3    Sigismund, S.4    Shaw, M.5    Bossi, G.6
  • 15
    • 34447629523 scopus 로고    scopus 로고
    • Innate and adaptive immunity through autophagy
    • Schmid D, Munz C. Innate and adaptive immunity through autophagy. Immmunity 2007; 27: 11-21.
    • (2007) Immmunity , vol.27 , pp. 11-21
    • Schmid, D.1    Munz, C.2
  • 16
    • 34547111522 scopus 로고    scopus 로고
    • Enhancement of lysosomal glycohydrolase activity in human primary B-lymphocytes during spontaneous apoptosis
    • Rosati E, Mencarelli S, Magini A, Sabatini R, Tassi C, Orlacchio A, et al. Enhancement of lysosomal glycohydrolase activity in human primary B-lymphocytes during spontaneous apoptosis. Int J Immunopathol Pharmacol 2007; 20: 279-87.
    • (2007) Int J Immunopathol Pharmacol , vol.20 , pp. 279-287
    • Rosati, E.1    Mencarelli, S.2    Magini, A.3    Sabatini, R.4    Tassi, C.5    Orlacchio, A.6
  • 17
    • 34250020188 scopus 로고    scopus 로고
    • Lysosomal cysteine cathepsins: Signaling pathways in apoptosis
    • Stoka V, Turk V, Turk B. Lysosomal cysteine cathepsins: Signaling pathways in apoptosis. Biol Chem 2007; 388: 555-60.
    • (2007) Biol Chem , vol.388 , pp. 555-560
    • Stoka, V.1    Turk, V.2    Turk, B.3
  • 18
    • 27244448634 scopus 로고    scopus 로고
    • The Trypanosoma cruzi-host interplay: Location, invasion, retention
    • Andrade LO, Andrews NA. The Trypanosoma cruzi-host interplay: location, invasion, retention. Nat Rev Microbiol 2005; 3: 819-23.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 819-823
    • Andrade, L.O.1    Andrews, N.A.2
  • 22
    • 0025719869 scopus 로고
    • Antimalarial effects of peptide inhibitors of a Plasmodium falciparum cysteine proteinase
    • Rosenthal PJ, Wollish WS, Palmer JT, Rasnick D. Antimalarial effects of peptide inhibitors of a Plasmodium falciparum cysteine proteinase. J Clin Invest 1991; 88: 1467-72.
    • (1991) J Clin Invest , vol.88 , pp. 1467-1472
    • Rosenthal, P.J.1    Wollish, W.S.2    Palmer, J.T.3    Rasnick, D.4
  • 23
    • 0035986688 scopus 로고    scopus 로고
    • Cysteine proteases of malaria parasites: Targets for chemotherapy
    • Rosenthal PJ, Sijwali PS, Singh A, Shenai BR. Cysteine proteases of malaria parasites: Targets for chemotherapy. Curr Pharm Des 2002; 8(18): 1659-72.
    • (2002) Curr Pharm Des , vol.8 , Issue.18 , pp. 1659-1672
    • Rosenthal, P.J.1    Sijwali, P.S.2    Singh, A.3    Shenai, B.R.4
  • 24
    • 0036183460 scopus 로고    scopus 로고
    • Hydrolysis of erythrocyte proteins by proteases of malaria parasites
    • Rosenthal PJ. Hydrolysis of erythrocyte proteins by proteases of malaria parasites. Curr Opin Hematol 2002; 9: 140-5.
    • (2002) Curr Opin Hematol , vol.9 , pp. 140-145
    • Rosenthal, P.J.1
  • 26
    • 34247490248 scopus 로고    scopus 로고
    • Lysosomal sequestration of amine-containing drugs: Analysis and therapeutic implications
    • Kaufmann AM, Krise JP. Lysosomal sequestration of amine-containing drugs: Analysis and therapeutic implications J Pharm Sci 2007; 96: 729-46.
    • (2007) J Pharm Sci , vol.96 , pp. 729-746
    • Kaufmann, A.M.1    Krise, J.P.2
  • 27
    • 0141907718 scopus 로고    scopus 로고
    • Destination lysosome: A target organelle for tumor cell killing?
    • Castino R, Demos M, Isidoro C. Destination lysosome: A target organelle for tumor cell killing? J Mol Recog 2003; 16: 337-48.
    • (2003) J Mol Recog , vol.16 , pp. 337-348
    • Castino, R.1    Demos, M.2    Isidoro, C.3
  • 28
    • 33748126226 scopus 로고    scopus 로고
    • Recent approaches to intracellular delivery of drugs and DNA and organelle targeting
    • Torchilin VP. Recent approaches to intracellular delivery of drugs and DNA and organelle targeting. Ann Rev Biomed Eng 2006; 8: 343-75.
    • (2006) Ann Rev Biomed Eng , vol.8 , pp. 343-375
    • Torchilin, V.P.1
  • 29
    • 33847073097 scopus 로고    scopus 로고
    • Duncan R Designing polymer conjugates as lysosomotropic nanomedicines. Biochem Soc Trans 2007; 35: 56-60.
    • Duncan R Designing polymer conjugates as lysosomotropic nanomedicines. Biochem Soc Trans 2007; 35: 56-60.
  • 30
    • 0142258170 scopus 로고    scopus 로고
    • Chemotherapy of human African trypanosomiasis: Current and future prospects
    • Fairlamb A. Chemotherapy of human African trypanosomiasis: Current and future prospects. Trends Parasitol 2003; 19: 488-94.
    • (2003) Trends Parasitol , vol.19 , pp. 488-494
    • Fairlamb, A.1
  • 34
    • 27144462250 scopus 로고    scopus 로고
    • Protozoan genomics for drug discovery
    • Chaudhary K, Roos DS. Protozoan genomics for drug discovery. Nat Biotechnol 2005; 23: 1089-91.
    • (2005) Nat Biotechnol , vol.23 , pp. 1089-1091
    • Chaudhary, K.1    Roos, D.S.2
  • 35
    • 37849023306 scopus 로고    scopus 로고
    • Assessing performance of orthology detection strategies applied to eukaryotic genomes
    • Chen F, Mackey AJ, Vermunt JK, Roos DS. Assessing performance of orthology detection strategies applied to eukaryotic genomes. PLoS ONE 2007; 2(4): E383.
    • (2007) PLoS ONE , vol.2 , Issue.4
    • Chen, F.1    Mackey, A.J.2    Vermunt, J.K.3    Roos, D.S.4
  • 36
    • 39649085703 scopus 로고    scopus 로고
    • Mapping the antigenicity of the parasites in Leishmania donovani infection by proteome serology
    • Forgber M. Basu R. Roychoudhury K, Theinet S, Roy S, Sundar S, et al. Mapping the antigenicity of the parasites in Leishmania donovani infection by proteome serology. PLoS ONE 2006; 1: E40.
    • (2006) PLoS ONE , vol.1
    • Forgber, M.1    Basu, R.2    Roychoudhury, K.3    Theinet, S.4    Roy, S.5    Sundar, S.6
  • 37
    • 0141909066 scopus 로고    scopus 로고
    • Proteome mapping of the protozoan parasite Leishmania and application to the study of drug targets and resistance mechanisms
    • Drummelsmith J, Brochu V, Girard I, Messier N, Oullette M. Proteome mapping of the protozoan parasite Leishmania and application to the study of drug targets and resistance mechanisms. Mol Cell Proteomics 2003; 2: 145-55.
    • (2003) Mol Cell Proteomics , vol.2 , pp. 145-155
    • Drummelsmith, J.1    Brochu, V.2    Girard, I.3    Messier, N.4    Oullette, M.5
  • 38
    • 33745060757 scopus 로고    scopus 로고
    • Comparative proteomics of glycosomes from bloodstream form and procyclic culture form Trypanosoma brucei brucei
    • Colasante C, Ellis M, Ruppert T, Voncken F. Comparative proteomics of glycosomes from bloodstream form and procyclic culture form Trypanosoma brucei brucei. Proteomics 2006; 11: 3275-9.
    • (2006) Proteomics , vol.11 , pp. 3275-3279
    • Colasante, C.1    Ellis, M.2    Ruppert, T.3    Voncken, F.4
  • 39
    • 33845423619 scopus 로고    scopus 로고
    • Transcriptomic comparison of two Entamoeba histolytica strains with defined virulence phenotypes indentifies new virulence factor candidates and key differences in the expression patterns, lectin light chains and calmodulin
    • Davis PH, Schulze J, Stanley SL. Transcriptomic comparison of two Entamoeba histolytica strains with defined virulence phenotypes indentifies new virulence factor candidates and key differences in the expression patterns, lectin light chains and calmodulin. Mol Biochem Parasitol 2007; 115: 118-28.
    • (2007) Mol Biochem Parasitol , vol.115 , pp. 118-128
    • Davis, P.H.1    Schulze, J.2    Stanley, S.L.3
  • 40
    • 33748486043 scopus 로고    scopus 로고
    • Comparative proteomic analysis of two Entamoeba histolytica strains with different virulence Phenotypes identifies peroxiredoxin as an important component of amoebic virulence
    • Davis PH, Zhang X, Gui J, Townsend RR, Stanley SL. Comparative proteomic analysis of two Entamoeba histolytica strains with different virulence Phenotypes identifies peroxiredoxin as an important component of amoebic virulence. Mol Microbiol 2006; 61: 1523-32.
    • (2006) Mol Microbiol , vol.61 , pp. 1523-1532
    • Davis, P.H.1    Zhang, X.2    Gui, J.3    Townsend, R.R.4    Stanley, S.L.5
  • 41
    • 33745531689 scopus 로고    scopus 로고
    • Sims PF, Hyde JE. Proteomics of the human malaria parasite Plasmodium falciparum. Exp Rev Proteomics, 2006; 3: 87-95.
    • Sims PF, Hyde JE. Proteomics of the human malaria parasite Plasmodium falciparum. Exp Rev Proteomics, 2006; 3: 87-95.
  • 42
    • 26644451857 scopus 로고    scopus 로고
    • Proteomic analysis of rhoptry organelles reveals many novel constituents for host-parasite interactions in Toxoplasma gondii
    • Bradley PJ, Ward C, Cheng SJ, Alexander DL, Coller S, Coombs GH, et al. Proteomic analysis of rhoptry organelles reveals many novel constituents for host-parasite interactions in Toxoplasma gondii. J Biol Chem 2005; 280: 34245-58.
    • (2005) J Biol Chem , vol.280 , pp. 34245-34258
    • Bradley, P.J.1    Ward, C.2    Cheng, S.J.3    Alexander, D.L.4    Coller, S.5    Coombs, G.H.6
  • 43
    • 22044458052 scopus 로고    scopus 로고
    • Genomic and proteomic approaches for Chagas' disease: Critical analysis of diagnostic methods
    • Huete-Ferez JA, Flores-Obando RE, Ghedin E, Caffrey CR. Genomic and proteomic approaches for Chagas' disease: Critical analysis of diagnostic methods. Exp Rev Mol Diagn 2005; 5: 521-30.
    • (2005) Exp Rev Mol Diagn , vol.5 , pp. 521-530
    • Huete-Ferez, J.A.1    Flores-Obando, R.E.2    Ghedin, E.3    Caffrey, C.R.4
  • 44
    • 3242699070 scopus 로고    scopus 로고
    • Parasite genome databases and web-based resources
    • Heriz-Fowler C, Hall N. Parasite genome databases and web-based resources. Methods Mol Biol 2004; 270: 45-74.
    • (2004) Methods Mol Biol , vol.270 , pp. 45-74
    • Heriz-Fowler, C.1    Hall, N.2
  • 45
    • 0037192115 scopus 로고    scopus 로고
    • Metabolic pathway analysis in trypanosomes and malaria parasites
    • Fairlamb A. Metabolic pathway analysis in trypanosomes and malaria parasites. Phil Trans R Soc Lond B 2002; 357: 101-7.
    • (2002) Phil Trans R Soc Lond B , vol.357 , pp. 101-107
    • Fairlamb, A.1
  • 46
    • 0028949538 scopus 로고
    • Molecular mechanisms and therapeutic approaches to the treatment of African trypanosomiasis
    • Wang CC. Molecular mechanisms and therapeutic approaches to the treatment of African trypanosomiasis. Annu Rev Pharmacol Toxicol 1995; 35: 93-127.
    • (1995) Annu Rev Pharmacol Toxicol , vol.35 , pp. 93-127
    • Wang, C.C.1
  • 47
    • 33846466564 scopus 로고    scopus 로고
    • Two metallocarboxypeptidases from the protozoan Trypanosoma cruzi belong to the M32 family, found so far only in prokaryotes
    • Niemirowicz G, Parussini F, Aguero F, Cazzulo JJ. Two metallocarboxypeptidases from the protozoan Trypanosoma cruzi belong to the M32 family, found so far only in prokaryotes. Biochem J 2007; 401: 399-410.
    • (2007) Biochem J , vol.401 , pp. 399-410
    • Niemirowicz, G.1    Parussini, F.2    Aguero, F.3    Cazzulo, J.J.4
  • 48
    • 0036178381 scopus 로고    scopus 로고
    • Cysteine Droteases of parasitic organisms
    • Sajid M, McKerrow JH. Cysteine Droteases of parasitic organisms. Mol Biochem Parasitol 2002; 120: 1-21.
    • (2002) Mol Biochem Parasitol , vol.120 , pp. 1-21
    • Sajid, M.1    McKerrow, J.H.2
  • 50
    • 33644854957 scopus 로고    scopus 로고
    • Identification of novel parasitic cysteine protease inhibitors by use of virtual screening. 2. The available chemical directory
    • Desai PV, Patny A, Gut J, Rosenthal PJ, Tekwani B, Srivastava A, et al. Identification of novel parasitic cysteine protease inhibitors by use of virtual screening. 2. The available chemical directory. J Med Chem 2006; 49: 1576-84.
    • (2006) J Med Chem , vol.49 , pp. 1576-1584
    • Desai, P.V.1    Patny, A.2    Gut, J.3    Rosenthal, P.J.4    Tekwani, B.5    Srivastava, A.6
  • 51
    • 33947517664 scopus 로고    scopus 로고
    • Cathepsin Cs are key for he intracellular survival of the protozoan parasite Toxoplasma gondii
    • Que X, Engel JC, Ferguson D, Wunderlich A, Tomavo S, Reed SL. Cathepsin Cs are key for he intracellular survival of the protozoan parasite Toxoplasma gondii. J Biol Chem 2007; 282(7): 4994-5003.
    • (2007) J Biol Chem , vol.282 , Issue.7 , pp. 4994-5003
    • Que, X.1    Engel, J.C.2    Ferguson, D.3    Wunderlich, A.4    Tomavo, S.5    Reed, S.L.6
  • 52
    • 33846561051 scopus 로고    scopus 로고
    • Cysteine protease inhibitors block Toxoplasma zondii microneme secretion and cell invasion
    • Teo CF, Zhou XW, Bogyo M, Carruthers VB. Cysteine protease inhibitors block Toxoplasma zondii microneme secretion and cell invasion. Antimicrob Agents Chemother 2007; 51(2): 679-88.
    • (2007) Antimicrob Agents Chemother , vol.51 , Issue.2 , pp. 679-688
    • Teo, C.F.1    Zhou, X.W.2    Bogyo, M.3    Carruthers, V.B.4
  • 53
    • 35848971033 scopus 로고    scopus 로고
    • A cysteine protease inhibitor cures Chagas' disease in an immunodeficient mouse model of infection
    • Doyle PS, Zhou YM, Engel JC, McKerrow JH. A cysteine protease inhibitor cures Chagas' disease in an immunodeficient mouse model of infection. Antimicrob Agents Chemother 2007; 51(11): 3932-9.
    • (2007) Antimicrob Agents Chemother , vol.51 , Issue.11 , pp. 3932-3939
    • Doyle, P.S.1    Zhou, Y.M.2    Engel, J.C.3    McKerrow, J.H.4
  • 54
    • 0027924584 scopus 로고
    • American Trypanosomiasis (Chagas' Disease)- a tropical disease now in the United States
    • Kirchhoff LV. American Trypanosomiasis (Chagas' Disease)- a tropical disease now in the United States. N Engl J Med 1993; 329: 639-44.
    • (1993) N Engl J Med , vol.329 , pp. 639-644
    • Kirchhoff, L.V.1
  • 55
    • 33847039866 scopus 로고    scopus 로고
    • Transfusion complications: Transfusion-acquired Trypanosoma cruzi infection
    • Young C, Losikoff P, Chawla A, Glasser L, Forman E. Transfusion complications: Transfusion-acquired Trypanosoma cruzi infection. Transfusion 2007; 47(3): 540-4.
    • (2007) Transfusion , vol.47 , Issue.3 , pp. 540-544
    • Young, C.1    Losikoff, P.2    Chawla, A.3    Glasser, L.4    Forman, E.5
  • 56
    • 44349087346 scopus 로고    scopus 로고
    • Chagas C. In: Carlos Chagas: Coletanea dee trabalhos cientificos. Editora Universidade de Brasilia 1981; 6: 247-58.
    • Chagas C. In: Carlos Chagas: Coletanea dee trabalhos cientificos. Editora Universidade de Brasilia 1981; 6: 247-58.
  • 57
    • 0030803050 scopus 로고    scopus 로고
    • Cardiac involvement is a constant finding in acute Chagas' disease: A clinical, parasitological, and histopathological study
    • Parada H, Carrasco HA, Anez N, Inglessis I. Cardiac involvement is a constant finding in acute Chagas' disease: A clinical, parasitological, and histopathological study. Int J Cardiol 1997; 60: 49-54.
    • (1997) Int J Cardiol , vol.60 , pp. 49-54
    • Parada, H.1    Carrasco, H.A.2    Anez, N.3    Inglessis, I.4
  • 58
    • 0033253538 scopus 로고    scopus 로고
    • Disease and Immunosuppression
    • Ferreira MS. Chagas' Disease and Immunosuppression. Mem Inst Oswaldo Cruz 1999; 94(I): 325-7.
    • (1999) Mem Inst Oswaldo Cruz , vol.94 , Issue.I , pp. 325-327
    • Chagas', F.M.S.1
  • 59
    • 0037088708 scopus 로고    scopus 로고
    • CDC. Chagas' disease after organ transplantation. United States, MMWR Morb Mortal Wkly Rep 2002; 51(10):210-2.
    • CDC. Chagas' disease after organ transplantation. United States, MMWR Morb Mortal Wkly Rep 2002; 51(10):210-2.
  • 61
    • 0037963656 scopus 로고    scopus 로고
    • Nitroheterocyclic drugs with broad-spectrum activity
    • Raether W, Hänel H. Nitroheterocyclic drugs with broad-spectrum activity. Parasitol Res 2003; 90: S19-39.
    • (2003) Parasitol Res , vol.90
    • Raether, W.1    Hänel, H.2
  • 62
    • 3543087283 scopus 로고    scopus 로고
    • Efficacy of chemotherapy with benznidazolee in children in the indeterminate phase of Chagas' disease
    • Estani SS, Segura EL, Ruiz AM, Velazquez E, Porcel BM, Yampotis C. Efficacy of chemotherapy with benznidazolee in children in the indeterminate phase of Chagas' disease. Am J Trop Med Hyg 1998; 59: 526-9.
    • (1998) Am J Trop Med Hyg , vol.59 , pp. 526-529
    • Estani, S.S.1    Segura, E.L.2    Ruiz, A.M.3    Velazquez, E.4    Porcel, B.M.5    Yampotis, C.6
  • 63
    • 0033252802 scopus 로고    scopus 로고
    • Treatment of Trypanosoma cruzi infection in the undetermined phase. Experience and current guidelines of treatment in Argentina
    • Estani SS, Segura EL. Treatment of Trypanosoma cruzi infection in the undetermined phase. Experience and current guidelines of treatment in Argentina. Mem Inst Oswaldo Cruz 1999; 94(1): 363-5.
    • (1999) Mem Inst Oswaldo Cruz , vol.94 , Issue.1 , pp. 363-365
    • Estani, S.S.1    Segura, E.L.2
  • 64
    • 0141557725 scopus 로고    scopus 로고
    • Interventional study in the natural evolution of Chagas' disease. Evaluation of specific antiparasitic trealment Retrospective-prospective study of antiparasitic therapy
    • Gallerano RR, Sosa RR. Interventional study in the natural evolution of Chagas' disease. Evaluation of specific antiparasitic trealment Retrospective-prospective study of antiparasitic therapy. Rev Fac Cien Med Univ Nac Cordoba 2005; 57(2): 135-62.
    • (2005) Rev Fac Cien Med Univ Nac Cordoba , vol.57 , Issue.2 , pp. 135-162
    • Gallerano, R.R.1    Sosa, R.R.2
  • 65
    • 0024559290 scopus 로고
    • Genotoxicity testing of antiparasitic nitrofurans in the Drosophila wing somatic mutation and recombination test
    • Moraga AA, Graf U. Genotoxicity testing of antiparasitic nitrofurans in the Drosophila wing somatic mutation and recombination test. Mutagenesis 1989; 4(2): 105-10.
    • (1989) Mutagenesis , vol.4 , Issue.2 , pp. 105-110
    • Moraga, A.A.1    Graf, U.2
  • 66
    • 0027362776 scopus 로고
    • Genetic differences between the standard Ames tester strains TA100 and TA98
    • Jurado J, Alejandre-Duran E, Pueyo C. Genetic differences between the standard Ames tester strains TA100 and TA98. Mutagenesis 1993; 8(6): 527-632.
    • (1993) Mutagenesis , vol.8 , Issue.6 , pp. 527-632
    • Jurado, J.1    Alejandre-Duran, E.2    Pueyo, C.3
  • 67
    • 0023609713 scopus 로고
    • Susceptibility and natural resistance of Trypanosoma cruzi strains to drugs used clinically in Chagas' disease
    • Filardi, LS, Brener Z. Susceptibility and natural resistance of Trypanosoma cruzi strains to drugs used clinically in Chagas' disease. Trans Royal Soc Trop Med Hyg 1987; 81: 755-9.
    • (1987) Trans Royal Soc Trop Med Hyg , vol.81 , pp. 755-759
    • Filardi, L.S.1    Brener, Z.2
  • 68
    • 33646847271 scopus 로고    scopus 로고
    • Long-term cardiac outcomes of treating chronic Chagas' disease with benznidazole versus no treatment: A nonrandomized trial
    • Viotti R, Vigliano C, Lococo B, Bertocchi G, Pett M, Alvarez MG, et al. Long-term cardiac outcomes of treating chronic Chagas' disease with benznidazole versus no treatment: A nonrandomized trial. Ann Intern Med 2006; 144(10): 724-34.
    • (2006) Ann Intern Med , vol.144 , Issue.10 , pp. 724-734
    • Viotti, R.1    Vigliano, C.2    Lococo, B.3    Bertocchi, G.4    Pett, M.5    Alvarez, M.G.6
  • 69
    • 0032541311 scopus 로고    scopus 로고
    • Cysteine protease inhibitors cure an experimental Trypanosoma cruzi infection
    • Engel JC, Doyle PS, Hsieh I, McKerrow JH. Cysteine protease inhibitors cure an experimental Trypanosoma cruzi infection. J Exp Med 1998; 188: 725-34.
    • (1998) J Exp Med , vol.188 , pp. 725-734
    • Engel, J.C.1    Doyle, P.S.2    Hsieh, I.3    McKerrow, J.H.4
  • 70
    • 44349164876 scopus 로고    scopus 로고
    • The major cysteine proteinase of Trypanosoma cruzi: A valid target for chemotherapy of Chagas' disease
    • Cazzulo JJ, Stoka V, Turk V. The major cysteine proteinase of Trypanosoma cruzi: A valid target for chemotherapy of Chagas' disease. Immunol Lett 2001; 78(3): 135-42.
    • (2001) Immunol Lett , vol.78 , Issue.3 , pp. 135-142
    • Cazzulo, J.J.1    Stoka, V.2    Turk, V.3
  • 73
    • 0031937742 scopus 로고    scopus 로고
    • Cysteine protease inhibitors alter Golgi complex ultrastructure and function in Trypanosoma cruzi
    • Engel JC, Doyle PS, Palmer J, Hsieh I, Bainton DF, McKerrow JH. Cysteine protease inhibitors alter Golgi complex ultrastructure and function in Trypanosoma cruzi. J Cell Sci 1998; 111: 597-606.
    • (1998) J Cell Sci , vol.111 , pp. 597-606
    • Engel, J.C.1    Doyle, P.S.2    Palmer, J.3    Hsieh, I.4    Bainton, D.F.5    McKerrow, J.H.6
  • 75
    • 0025095388 scopus 로고
    • Aminoacid and carbohydrate composition of a lysosomal cysteine proteinase from Trypanosoma cruzi. Absence of phosphorylated mannose residues
    • Cazzullo JJ, Hellman U, Cousos R, Parodi AJ. Aminoacid and carbohydrate composition of a lysosomal cysteine proteinase from Trypanosoma cruzi. Absence of phosphorylated mannose residues. Mol Biochem Parasitol 1990; 38: 41-8.
    • (1990) Mol Biochem Parasitol , vol.38 , pp. 41-48
    • Cazzullo, J.J.1    Hellman, U.2    Cousos, R.3    Parodi, A.J.4
  • 76
    • 0022474117 scopus 로고
    • Trypanosoma cruzi: Characterization and isolation of a 57/51 1000 m.w. surface glycoprotein (GP57/51) expressed by epimastiogtes and blood-stream trypomastigotes
    • Scharfstein J, Schechter M, Senna M, Peralta JM, Mendoca-Previato L, Miles MA. Trypanosoma cruzi: Characterization and isolation of a 57/51 1000 m.w. surface glycoprotein (GP57/51) expressed by epimastiogtes and blood-stream trypomastigotes. J Immunol 1986; 137: 1336-41.
    • (1986) J Immunol , vol.137 , pp. 1336-1341
    • Scharfstein, J.1    Schechter, M.2    Senna, M.3    Peralta, J.M.4    Mendoca-Previato, L.5    Miles, M.A.6
  • 77
    • 0024558590 scopus 로고
    • Subcellular localization of a cysteine proteinase from Trypanosoma cruzi
    • Bontempi E., Martinez J, Cazzulo JJ. Subcellular localization of a cysteine proteinase from Trypanosoma cruzi. Mol Biochem Parasitol 1989; 33: 43-8.
    • (1989) Mol Biochem Parasitol , vol.33 , pp. 43-48
    • Bontempi, E.1    Martinez, J.2    Cazzulo, J.J.3
  • 78
    • 0026781519 scopus 로고
    • The sequence, organization, and expression of the major cysteine protease (cruzi-pain) from Trypanosoma cruzi
    • Eakin AE, McGrath ME, McKerrow JH, Craig CS. The sequence, organization, and expression of the major cysteine protease (cruzi-pain) from Trypanosoma cruzi: J Biol Chem 1992; 267: 7411-20.
    • (1992) J Biol Chem , vol.267 , pp. 7411-7420
    • Eakin, A.E.1    McGrath, M.E.2    McKerrow, J.H.3    Craig, C.S.4
  • 79
    • 0028789754 scopus 로고
    • A cysteine protease is a target for the enzyme structure-based design of antiparasitic drugs
    • Eakin EA, McKerrow JH, Craig CS. A cysteine protease is a target for the enzyme structure-based design of antiparasitic drugs. Drug Inf J 1995; 29: 1501-17.
    • (1995) Drug Inf J , vol.29 , pp. 1501-1517
    • Eakin, E.A.1    McKerrow, J.H.2    Craig, C.S.3
  • 80
    • 0027537709 scopus 로고
    • Production of crystallizable cruzain, the major cysteine protease from Trypanosomas cruzi
    • Eakin AE, McGrath ME, McKerrow JH, Fletterick RJ, Craig CS. Production of crystallizable cruzain, the major cysteine protease from Trypanosomas cruzi. J Biol Chem 1993; 268: 6115-8.
    • (1993) J Biol Chem , vol.268 , pp. 6115-6118
    • Eakin, A.E.1    McGrath, M.E.2    McKerrow, J.H.3    Fletterick, R.J.4    Craig, C.S.5
  • 82
    • 0027508262 scopus 로고
    • Use of Trypanosoma cruzi purified glycoprotein (GP57/51) or trypomastigote-shed antigens to assess cure for human Chagas' disease
    • Gazzinelli RT, Galvao LMC, Krautz G, Lima AP, Ganzado JR, Scharfstein J, et al. Use of Trypanosoma cruzi purified glycoprotein (GP57/51) or trypomastigote-shed antigens to assess cure for human Chagas' disease. Am J Trop Med Hyg 1993; 49: 625-35.
    • (1993) Am J Trop Med Hyg , vol.49 , pp. 625-635
    • Gazzinelli, R.T.1    Galvao, L.M.C.2    Krautz, G.3    Lima, A.P.4    Ganzado, J.R.5    Scharfstein, J.6
  • 83
    • 0029045156 scopus 로고
    • The cysteine protease of Trypanosoma cruzi as a model for antiparasitic drug design
    • McKerrow JH, McGrath ME, Engel JC. The cysteine protease of Trypanosoma cruzi as a model for antiparasitic drug design. Parasitol Today 1995; 11: 279-82.
    • (1995) Parasitol Today , vol.11 , pp. 279-282
    • McKerrow, J.H.1    McGrath, M.E.2    Engel, J.C.3
  • 84
    • 0029978872 scopus 로고    scopus 로고
    • Stage-regulated expression of cruzipain, the major cystein protease of Trypanosoma cruzi us independent of the level of RNA
    • Tomas A, Kelly JM. Stage-regulated expression of cruzipain, the major cystein protease of Trypanosoma cruzi us independent of the level of RNA. Mol Biochem Parasitol 1996; 76: 91-103.
    • (1996) Mol Biochem Parasitol , vol.76 , pp. 91-103
    • Tomas, A.1    Kelly, J.M.2
  • 85
    • 0026691797 scopus 로고
    • Identification of a large pre-lysosomal compartment in the pathogenic protozoan Trypanosoma cruzi
    • Soares MG, Souto-Padron T, De Souza W. Identification of a large pre-lysosomal compartment in the pathogenic protozoan Trypanosoma cruzi. J Cell Sci 1992; 102: 157-67
    • (1992) J Cell Sci , vol.102 , pp. 157-167
    • Soares, M.G.1    Souto-Padron, T.2    De Souza, W.3
  • 86
    • 0028919880 scopus 로고
    • The presence of complex type oligosaccharides at the C-terminal domain glycosylation site of some molecules if cruzipain
    • Parodi AJ, Labriola C, Cazzulo J.J. The presence of complex type oligosaccharides at the C-terminal domain glycosylation site of some molecules if cruzipain. Mol Biochem Parasitol 1995; 69: 247-55.
    • (1995) Mol Biochem Parasitol , vol.69 , pp. 247-255
    • Parodi, A.J.1    Labriola, C.2    Cazzulo, J.J.3
  • 87
    • 0029085605 scopus 로고
    • Retention of glucose units added by the UDP-G-LC: Glycoprotein glucosyltransfera delays exit of glycoproteins from the ER
    • Labriola C, Cazzulo JJ, Parodi AJ. Retention of glucose units added by the UDP-G-LC: Glycoprotein glucosyltransfera delays exit of glycoproteins from the ER. J Cell Biol 1995; 130: 771-9.
    • (1995) J Cell Biol , vol.130 , pp. 771-779
    • Labriola, C.1    Cazzulo, J.J.2    Parodi, A.J.3
  • 88
    • 16844365217 scopus 로고    scopus 로고
    • de A Lima AP. Chagasin, the endogenous cysteine-protease inhibitor of Trypanosoma cruzi, modulates parasite differentiation and invasion of mammalian cells
    • Santos CC, Sant'anna C, Terres A, Cunha-e-Silva NL, Scharfstein J, de A Lima AP. Chagasin, the endogenous cysteine-protease inhibitor of Trypanosoma cruzi, modulates parasite differentiation and invasion of mammalian cells. J Cell Sci 2005; 118: 901-5.
    • (2005) J Cell Sci , vol.118 , pp. 901-905
    • Santos, C.C.1    Sant'anna, C.2    Terres, A.3    Cunha-e-Silva, N.L.4    Scharfstein, J.5
  • 89
    • 0025040524 scopus 로고
    • Lysis of trypanosomes by peptidyl fluoromethyl ketones
    • Ashall F, Angliker H, Shaw E. Lysis of trypanosomes by peptidyl fluoromethyl ketones. Biochem Biophy Res Commun 1990; 170: 923-9.
    • (1990) Biochem Biophy Res Commun , vol.170 , pp. 923-929
    • Ashall, F.1    Angliker, H.2    Shaw, E.3
  • 90
    • 0027398184 scopus 로고
    • Peptide-fluoromethylketones arrest intracellular replication and intercellular transmission of Trypanosoma czuzi
    • Harth G, Andrews N, Mills AA, Engel JC, Smith R, McKerrow JH. Peptide-fluoromethylketones arrest intracellular replication and intercellular transmission of Trypanosoma czuzi. Mol Biochem Parasitol 1993; 58:175-84.
    • (1993) Mol Biochem Parasitol , vol.58 , pp. 175-184
    • Harth, G.1    Andrews, N.2    Mills, A.A.3    Engel, J.C.4    Smith, R.5    McKerrow, J.H.6
  • 91
    • 0029099619 scopus 로고
    • Vinyl sulfones as mechanism-based cysteine protease inhibitors
    • Palmer JT, Rasnick D, Klaus, JL, Bromme D. Vinyl sulfones as mechanism-based cysteine protease inhibitors. J Med Chem 1995; 38: 3193-6.
    • (1995) J Med Chem , vol.38 , pp. 3193-3196
    • Palmer, J.T.1    Rasnick, D.2    Klaus, J.L.3    Bromme, D.4
  • 92
    • 0036679896 scopus 로고    scopus 로고
    • Recent advances in the synthesis design and selection of cysteine protease inhibitors
    • Alvarez Hernandez A, Roush WR. Recent advances in the synthesis design and selection of cysteine protease inhibitors. Curr Opin Chem Biol 2002; 6: 459-65.
    • (2002) Curr Opin Chem Biol , vol.6 , pp. 459-465
    • Alvarez Hernandez, A.1    Roush, W.R.2
  • 93
    • 44349158155 scopus 로고    scopus 로고
    • Emal CD, Alvarez-Hernandez A, Truong Y. Hansel E, Doyle PS, McKerrow JH, et al. Effect of hydrophobicity on trypanocidal activity of Peptidyl Vinyl Sulfonyl inhibitors. Chem Biol Drug Des 2008; (manuscript submitted).
    • Emal CD, Alvarez-Hernandez A, Truong Y. Hansel E, Doyle PS, McKerrow JH, et al. Effect of hydrophobicity on trypanocidal activity of Peptidyl Vinyl Sulfonyl inhibitors. Chem Biol Drug Des 2008; (manuscript submitted).
  • 95
    • 0026606269 scopus 로고
    • Inhibitors of the major cysteinyl proteinase GP57/51 impair host cell invasion and arrest the intracellular development of Trypanosoma cruzi
    • Meirelles MN, Juiliano L, Carmona L, Silva SG, Costa EM, Murta ACM, et al. Inhibitors of the major cysteinyl proteinase GP57/51 impair host cell invasion and arrest the intracellular development of Trypanosoma cruzi. Mol Biochem Parasitol 1992; 52: 175-84.
    • (1992) Mol Biochem Parasitol , vol.52 , pp. 175-184
    • Meirelles, M.N.1    Juiliano, L.2    Carmona, L.3    Silva, S.G.4    Costa, E.M.5    Murta, A.C.M.6
  • 96
    • 34250162859 scopus 로고    scopus 로고
    • Bis-acridines as lead anti-parasitic, agent: Structure activity analysis of a discrete compound library in vitro. Antimicrob
    • Caffrey C, Steverding D, Swenerton RK, Kelly B, Walshe D, Debnath A, et al. Bis-acridines as lead anti-parasitic, agent: Structure activity analysis of a discrete compound library in vitro. Antimicrob Agents Chemother 2007; 51(6): 2164-72.
    • (2007) Agents Chemother , vol.51 , Issue.6 , pp. 2164-2172
    • Caffrey, C.1    Steverding, D.2    Swenerton, R.K.3    Kelly, B.4    Walshe, D.5    Debnath, A.6
  • 98
    • 0037142343 scopus 로고    scopus 로고
    • Synthesis and structure-activity relationship study of potent trypanocidal thio semicarbazone inhibitors ofthe trypanosomal cysteine protease cruzain
    • Du X, Guo, C, Hansel E, Doyle PS, Caffrey CR, Holler TP, et al. Synthesis and structure-activity relationship study of potent trypanocidal thio semicarbazone inhibitors ofthe trypanosomal cysteine protease cruzain. J Med Chem. 2002; 45(13): 2695-707.
    • (2002) J Med Chem , vol.45 , Issue.13 , pp. 2695-2707
    • Du, X.1    Guo, C.2    Hansel, E.3    Doyle, P.S.4    Caffrey, C.R.5    Holler, T.P.6
  • 100
    • 0034662749 scopus 로고    scopus 로고
    • A target within a target: Probing cruzain's P1 site to define structural determinants for the Chagas' dr sease protease
    • Brinen LS, Hansell E, Cheng J, Roush WR, McKerrow JH, Fletterick RJ. A target within a target: Probing cruzain's P1 site to define structural determinants for the Chagas' dr sease protease. Structure 2000; 15: 831-40.
    • (2000) Structure , vol.15 , pp. 831-840
    • Brinen, L.S.1    Hansell, E.2    Cheng, J.3    Roush, W.R.4    McKerrow, J.H.5    Fletterick, R.J.6
  • 101
    • 6444244485 scopus 로고    scopus 로고
    • Crystal structure of reversible ketone-based inhibitors of the cysteine protease cruzain
    • Huang L, Brinen LS, Ellman JA. Crystal structure of reversible ketone-based inhibitors of the cysteine protease cruzain. Bioorg Med Chem 2003; 11: 21-9.
    • (2003) Bioorg Med Chem , vol.11 , pp. 21-29
    • Huang, L.1    Brinen, L.S.2    Ellman, J.A.3
  • 102
    • 0033791657 scopus 로고    scopus 로고
    • In vitro evaluation of the disposition of a novel cysteine protease inhibitor
    • Jacobsen W, Christians U, Benet LZ. In vitro evaluation of the disposition of a novel cysteine protease inhibitor. Drug Metab Dispos 2000; 28: 1343-51.
    • (2000) Drug Metab Dispos , vol.28 , pp. 1343-1351
    • Jacobsen, W.1    Christians, U.2    Benet, L.Z.3
  • 103
    • 33846697738 scopus 로고    scopus 로고
    • Schistosomiasis mansoni: Novel chemotherapy using a cysteine protease inhibitor
    • Abdulla MH, Lim KC, Sajid M, McKerrow JH, Caffrey CR. Schistosomiasis mansoni: Novel chemotherapy using a cysteine protease inhibitor. PLoS Med 2007; 4(1): E14.
    • (2007) PLoS Med , vol.4 , Issue.1
    • Abdulla, M.H.1    Lim, K.C.2    Sajid, M.3    McKerrow, J.H.4    Caffrey, C.R.5
  • 104
    • 33748890278 scopus 로고    scopus 로고
    • Cunha e Silva N, Sant'Anna C, Gomez Pereira M, Porto-Carreiro I, Jeovanio AL, De Souza W. Reservosomes; multipurpose organelles? Parasitol Res 2006; 99: 325-7.
    • Cunha e Silva N, Sant'Anna C, Gomez Pereira M, Porto-Carreiro I, Jeovanio AL, De Souza W. Reservosomes; multipurpose organelles? Parasitol Res 2006; 99: 325-7.
  • 105
    • 0025292469 scopus 로고
    • Cysteine proteinase in Trypanosoma czuzi: Immunochemical localization and involvement in parasite-host cell interaction
    • Souto-Padron T, Completella O, Cazzulo JJ, De Souza W. Cysteine proteinase in Trypanosoma czuzi: Immunochemical localization and involvement in parasite-host cell interaction. J Cell Sci 1990; 96: 485-90.
    • (1990) J Cell Sci , vol.96 , pp. 485-490
    • Souto-Padron, T.1    Completella, O.2    Cazzulo, J.J.3    De Souza, W.4
  • 106
    • 0039702904 scopus 로고    scopus 로고
    • Protease trafficking in two primitive eukaryotes is mediated by a prodomain protein motif
    • Huete-Perez JA, Engel JC, Brinen LS, Mottram JC, McKerrow JH. Protease trafficking in two primitive eukaryotes is mediated by a prodomain protein motif. J Biol Chem 1999; 274: 16249-56.
    • (1999) J Biol Chem , vol.274 , pp. 16249-16256
    • Huete-Perez, J.A.1    Engel, J.C.2    Brinen, L.S.3    Mottram, J.C.4    McKerrow, J.H.5
  • 107
    • 0029166451 scopus 로고
    • Protein trafficking in kinetoplastid protozoa
    • Clayton C, Hausler T, Blattner J. Protein trafficking in kinetoplastid protozoa. Microb Rev 1995; 59: 325-44.
    • (1995) Microb Rev , vol.59 , pp. 325-344
    • Clayton, C.1    Hausler, T.2    Blattner, J.3
  • 108
    • 0026084062 scopus 로고
    • Self-proteolysis of the cysteine proteinase cruzipain from Trypanosoma cruzi gives a major fragment corresponding to its carboxy-terminal domain
    • Hellmann U, Wernstedt C, Cazzulo JJ. Self-proteolysis of the cysteine proteinase cruzipain from Trypanosoma cruzi gives a major fragment corresponding to its carboxy-terminal domain. Mol Biochem Parasitol 1991; 44: 15-22.
    • (1991) Mol Biochem Parasitol , vol.44 , pp. 15-22
    • Hellmann, U.1    Wernstedt, C.2    Cazzulo, J.J.3
  • 109
    • 38649111363 scopus 로고    scopus 로고
    • Cysteine cathepsins: Cellular roadmap to different functions
    • Brix K, Dunkhorst A, Mayer K, Jordans S. Cysteine cathepsins: Cellular roadmap to different functions. Biochimie 2007; 90(2): 194-207.
    • (2007) Biochimie , vol.90 , Issue.2 , pp. 194-207
    • Brix, K.1    Dunkhorst, A.2    Mayer, K.3    Jordans, S.4
  • 111
    • 0037155252 scopus 로고    scopus 로고
    • Heparan sulfate modulates kinin release by trypanosoma cruzi through the activity of cruzipain
    • Lima AP, Almeida PC, Tersario IL, Schmitz V, Schmaier AH, Juliano I, et al. Heparan sulfate modulates kinin release by trypanosoma cruzi through the activity of cruzipain. J Biol Chem 2002; 277(8): 5875-81.
    • (2002) J Biol Chem , vol.277 , Issue.8 , pp. 5875-5881
    • Lima, A.P.1    Almeida, P.C.2    Tersario, I.L.3    Schmitz, V.4    Schmaier, A.H.5    Juliano, I.6
  • 113
    • 33847769168 scopus 로고    scopus 로고
    • The cysteine proteinase inhibitor Z-Phe-Ala-CHN2 alters cell morphology and cell division activity of Trypanosoma brucei bloodstream forms in vivo
    • Scory S, Stierhof YD, Caffrey CR, Steverding D. The cysteine proteinase inhibitor Z-Phe-Ala-CHN2 alters cell morphology and cell division activity of Trypanosoma brucei bloodstream forms in vivo. Kintoplastid Biol Dis 2007; 6: 2.
    • (2007) Kintoplastid Biol Dis , vol.6 , pp. 2
    • Scory, S.1    Stierhof, Y.D.2    Caffrey, C.R.3    Steverding, D.4
  • 114
    • 0023850604 scopus 로고    scopus 로고
    • Peptidyl sulfonium salts. A new class of protease inhibitors
    • Shaw E. Peptidyl sulfonium salts. A new class of protease inhibitors J Biol Chem 1998; 263(6): 2768-2.
    • (1998) J Biol Chem , vol.263 , Issue.6 , pp. 2768-2772
    • Shaw, E.1
  • 115
    • 9144235678 scopus 로고    scopus 로고
    • A cathepsin B-like protease is required for host protein degradation in Trypanosoma brucei
    • Mackey ZB, O'Brien TC, Greenbaum DC, Blank RB, McKerrow JH. A cathepsin B-like protease is required for host protein degradation in Trypanosoma brucei. J Biol Chem 2004; 279(46): 48426-33.
    • (2004) J Biol Chem , vol.279 , Issue.46 , pp. 48426-48433
    • Mackey, Z.B.1    O'Brien, T.C.2    Greenbaum, D.C.3    Blank, R.B.4    McKerrow, J.H.5
  • 116
    • 0023443661 scopus 로고
    • Receptor-mediated endocytosis in the bloodstream form of Trypanosoma brucei
    • Coppens I, Opperdoes FR, Courtoy PJ, Baudhuin P. Receptor-mediated endocytosis in the bloodstream form of Trypanosoma brucei. J Protozool 1987; 34(4): 465-73.
    • (1987) J Protozool , vol.34 , Issue.4 , pp. 465-473
    • Coppens, I.1    Opperdoes, F.R.2    Courtoy, P.J.3    Baudhuin, P.4
  • 117
    • 0030605020 scopus 로고    scopus 로고
    • Low affinity of Trypanosoma brucei transferrin receptor to apotransferrin at pH 5 explains the fate of the ligand during endocytosis
    • Maier A, Steverding D. Low affinity of Trypanosoma brucei transferrin receptor to apotransferrin at pH 5 explains the fate of the ligand during endocytosis. FEBS Lett 1996;396(1): 87-9.
    • (1996) FEBS Lett , vol.396 , Issue.1 , pp. 87-89
    • Maier, A.1    Steverding, D.2
  • 118
    • 2542533103 scopus 로고    scopus 로고
    • Synthesis and structure-activity relationship of parasiticidal thiosemicarbazone cysteine protease inhibitors against Plasmodium falciparum, Trypanosoma brucei, and Trypanosoma cruzi
    • Greenbaum DC, Mackey Z, Hansell E, Doyle PS, Gut J, Caffrey CR, et al. Synthesis and structure-activity relationship of parasiticidal thiosemicarbazone cysteine protease inhibitors against Plasmodium falciparum, Trypanosoma brucei, and Trypanosoma cruzi, J Med Chem 2004; 47(12): 3212-9.
    • (2004) J Med Chem , vol.47 , Issue.12 , pp. 3212-3219
    • Greenbaum, D.C.1    Mackey, Z.2    Hansell, E.3    Doyle, P.S.4    Gut, J.5    Caffrey, C.R.6
  • 120
    • 39149083105 scopus 로고    scopus 로고
    • Development of potent purine-derived nitrile inhibitor of the trypanosomal protease TbcatB
    • Mallari JP, Shelat AA, O'Brien TC, Caffrey CR, Kosinski A, Connelly MC, et al. Development of potent purine-derived nitrile inhibitor of the trypanosomal protease TbcatB. J Med Chem 2008; 51(3): 545-52.
    • (2008) J Med Chem , vol.51 , Issue.3 , pp. 545-552
    • Mallari, J.P.1    Shelat, A.A.2    O'Brien, T.C.3    Caffrey, C.R.4    Kosinski, A.5    Connelly, M.C.6
  • 121
    • 33749330723 scopus 로고    scopus 로고
    • Miltefosine-discovery of the antileishmnial activity of phospholipid derivatives
    • Croft SL, Engel J. Miltefosine-discovery of the antileishmnial activity of phospholipid derivatives. Trans R Soc Trop Med Hyg 2006; 100: 4-8
    • (2006) Trans R Soc Trop Med Hyg , vol.100 , pp. 4-8
    • Croft, S.L.1    Engel, J.2
  • 122
    • 0026744781 scopus 로고
    • Developmental modification of lipophosphoglycan during the differentiation of Leishmania major promastigotes to an infectious stage
    • McConville MJ, Turco SJ, Ferguson MA, Sacks DL. Developmental modification of lipophosphoglycan during the differentiation of Leishmania major promastigotes to an infectious stage. EMBO J 1992; 11: 3593-600.
    • (1992) EMBO J , vol.11 , pp. 3593-3600
    • McConville, M.J.1    Turco, S.J.2    Ferguson, M.A.3    Sacks, D.L.4
  • 123
    • 0035012676 scopus 로고    scopus 로고
    • Secretory and endocytic pathways converge in a dynamic endosomal system in a primitive protozoan
    • Ghedin E, Debrabant A, Engel JC, Dwyer DM. Secretory and endocytic pathways converge in a dynamic endosomal system in a primitive protozoan. Traffic 2001; 2: 175-88.
    • (2001) Traffic , vol.2 , pp. 175-188
    • Ghedin, E.1    Debrabant, A.2    Engel, J.C.3    Dwyer, D.M.4
  • 125
    • 0035094602 scopus 로고    scopus 로고
    • Megasome biogenensis in Leishmania amazonensis: A morphometric and cytometric study
    • Ueda-Nakamura T, Attias M, De Souza W. Megasome biogenensis in Leishmania amazonensis: A morphometric and cytometric study Parasitol Res 2001; 87: 89-97.
    • (2001) Parasitol Res , vol.87 , pp. 89-97
    • Ueda-Nakamura, T.1    Attias, M.2    De Souza, W.3
  • 126
    • 0035861634 scopus 로고    scopus 로고
    • The stage-regulated expression of Leishmania mexicana CPB cysteine proteases is mediated by an intercistronic sequence element
    • Brooks DR, Westrop DH, Coombs GH, Mottram JC. The stage-regulated expression of Leishmania mexicana CPB cysteine proteases is mediated by an intercistronic sequence element. J Biol Chem 2001; 276(50): 47061-9.
    • (2001) J Biol Chem , vol.276 , Issue.50 , pp. 47061-47069
    • Brooks, D.R.1    Westrop, D.H.2    Coombs, G.H.3    Mottram, J.C.4
  • 128
    • 4344613395 scopus 로고    scopus 로고
    • Inhibition or lipopolysaccharide-induced macrophage TL-12 production by Leishmania mexicana amastigotes: The role of cysteine peptidases and the NF-B signaling pathway
    • Cameron P, McGachy A, Anderson M, Paul A, Coombs GH, Mottram JC, et al. Inhibition or lipopolysaccharide-induced macrophage TL-12 production by Leishmania mexicana amastigotes: The role of cysteine peptidases and the NF-B signaling pathway. J Immunol 2004; 173: 3297-304.
    • (2004) J Immunol , vol.173 , pp. 3297-3304
    • Cameron, P.1    McGachy, A.2    Anderson, M.3    Paul, A.4    Coombs, G.H.5    Mottram, J.C.6
  • 129
    • 0033820138 scopus 로고    scopus 로고
    • Analysis of the roies of cysteine proteinases of Leishmania mexicana in the host-parasite interaction
    • Frame MJ, Mottram JC, Coombs GH. Analysis of the roies of cysteine proteinases of Leishmania mexicana in the host-parasite interaction. Parasitology 2000; 121: 367-77.
    • (2000) Parasitology , vol.121 , pp. 367-377
    • Frame, M.J.1    Mottram, J.C.2    Coombs, G.H.3
  • 130
    • 0141991014 scopus 로고    scopus 로고
    • Extracellular release of the surface nictalloprotease, gp63, from Leishmania and insect trypanosomatids
    • Jaffe CL, Dwyer DM. Extracellular release of the surface nictalloprotease, gp63, from Leishmania and insect trypanosomatids. Parasitol Res 2003; 91: 229-37.
    • (2003) Parasitol Res , vol.91 , pp. 229-237
    • Jaffe, C.L.1    Dwyer, D.M.2
  • 131
    • 33947221526 scopus 로고    scopus 로고
    • Metabolism of Leishmania: Proven and predicted
    • Opperdoes FR, Coombs GH. Metabolism of Leishmania: Proven and predicted. Trends Parasitol 2007; 4: 149-58.
    • (2007) Trends Parasitol , vol.4 , pp. 149-158
    • Opperdoes, F.R.1    Coombs, G.H.2
  • 132
    • 33748300634 scopus 로고    scopus 로고
    • Cysteine peptidases CPA and CPB are vital for auiopbagy and differenhahon in Leishmania mexicana
    • Williams RA, Tetley L, Mottram JC, Coombs GH. Cysteine peptidases CPA and CPB are vital for auiopbagy and differenhahon in Leishmania mexicana. Mol Microbiol 2006; 61: 655-74.
    • (2006) Mol Microbiol , vol.61 , pp. 655-674
    • Williams, R.A.1    Tetley, L.2    Mottram, J.C.3    Coombs, G.H.4
  • 133
    • 34248141875 scopus 로고    scopus 로고
    • Molecular and functional analyses of a novel class I secretory nuclease from the human pathogen, Leishmania donovani
    • Joshi MB, Dwyer DM. Molecular and functional analyses of a novel class I secretory nuclease from the human pathogen, Leishmania donovani. J Biol Chem 2007; 282: 10079-95.
    • (2007) J Biol Chem , vol.282 , pp. 10079-10095
    • Joshi, M.B.1    Dwyer, D.M.2
  • 134
    • 0027332807 scopus 로고
    • Leishmania: Immunochemical comparison of the extracellular acid phosphatases from various species
    • Doyle P S, Dwyer DM. Leishmania: Immunochemical comparison of the extracellular acid phosphatases from various species. Exp Parasitol 1993; 7: 435-8.
    • (1993) Exp Parasitol , vol.7 , pp. 435-438
    • Doyle, P.S.1    Dwyer, D.M.2
  • 135
    • 33846672925 scopus 로고    scopus 로고
    • Effect of l-leucine methyl ester on growth and ultrastructure of Trypanosoma cruzi
    • Adade CM, Figueiredo RCBQ, De Castro SL, Soares MJ. Effect of l-leucine methyl ester on growth and ultrastructure of Trypanosoma cruzi. Acta Tropica 2007; 101: 69-79.
    • (2007) Acta Tropica , vol.101 , pp. 69-79
    • Adade, C.M.1    Figueiredo, R.C.B.Q.2    De Castro, S.L.3    Soares, M.J.4
  • 136
    • 34247486135 scopus 로고    scopus 로고
    • TOR-induced resistance to toxic adenosine analogs in Leishmania brought about by the internalization and degradation of me adenosine permease
    • Detke S. TOR-induced resistance to toxic adenosine analogs in Leishmania brought about by the internalization and degradation of me adenosine permease. Exp Cell Res 2007; 313: 1963-78.
    • (2007) Exp Cell Res , vol.313 , pp. 1963-1978
    • Detke, S.1
  • 139
    • 0032773796 scopus 로고    scopus 로고
    • Trypanosoma brucei: Killing of bloodstream forms in vitro and in vivo by the cysteine proteinase inhibitor Z-phe-ala-CHN2
    • Scory S, Caffrey CR, Stierhof YD, Ruppel A, Steverding D. Trypanosoma brucei: Killing of bloodstream forms in vitro and in vivo by the cysteine proteinase inhibitor Z-phe-ala-CHN2. Exp Parasitol 1999; 91(4): 327-33.
    • (1999) Exp Parasitol , vol.91 , Issue.4 , pp. 327-333
    • Scory, S.1    Caffrey, C.R.2    Stierhof, Y.D.3    Ruppel, A.4    Steverding, D.5
  • 140
    • 0026901767 scopus 로고
    • Toxoplasmic encephalitis in AIDS
    • Luft BJ, Remington JS. Toxoplasmic encephalitis in AIDS. Clin Infect Dis 1992; 15: 211-22
    • (1992) Clin Infect Dis , vol.15 , pp. 211-222
    • Luft, B.J.1    Remington, J.S.2
  • 142
    • 0028013088 scopus 로고
    • Early and longitudinal evaluations of treated infants and children and untreated historical patients with congenital toxoplasmosis: The Chicago Collaborative Treatment Trial
    • McAuley J, Boyer KM, Patel D, Mets M, Swisher C, Roizen N, et al. Early and longitudinal evaluations of treated infants and children and untreated historical patients with congenital toxoplasmosis: The Chicago Collaborative Treatment Trial. Clin infect Dis 1994; 18: 38-72.
    • (1994) Clin infect Dis , vol.18 , pp. 38-72
    • McAuley, J.1    Boyer, K.M.2    Patel, D.3    Mets, M.4    Swisher, C.5    Roizen, N.6
  • 143
    • 0029151285 scopus 로고
    • Preventing toxoplasmic encephalitis in persons infected with human immunodeficiency virus
    • Richards FO, Kovacs JA, Luft BJ. Preventing toxoplasmic encephalitis in persons infected with human immunodeficiency virus. Clin infect Dis 1995; 21: 49-56.
    • (1995) Clin infect Dis , vol.21 , pp. 49-56
    • Richards, F.O.1    Kovacs, J.A.2    Luft, B.J.3
  • 144
    • 0036138684 scopus 로고    scopus 로고
    • Cysteine proteinases from distinct cellular compartments are recruited to phagocytic vesicles by Entamoeba histolytica
    • Que X, Brinen LS, Perkins P, Herdman S. Hirata K, Torian BE, et al. Cysteine proteinases from distinct cellular compartments are recruited to phagocytic vesicles by Entamoeba histolytica. Mol Biochem Parasitol 2002; 119: 23-32.
    • (2002) Mol Biochem Parasitol , vol.119 , pp. 23-32
    • Que, X.1    Brinen, L.S.2    Perkins, P.3    Herdman, S.4    Hirata, K.5    Torian, B.E.6
  • 145
    • 33947109437 scopus 로고    scopus 로고
    • Rhoptries are major players in Toxoplasma gondii invasion and host cell interaction
    • Dubremetz JF. Rhoptries are major players in Toxoplasma gondii invasion and host cell interaction. Cell Microbiol 2007; 9: 841-8.
    • (2007) Cell Microbiol , vol.9 , pp. 841-848
    • Dubremetz, J.F.1
  • 146
    • 2142647845 scopus 로고    scopus 로고
    • Toxopain-1 is critical for infection in a novel chicken embryo model of congenital toxoplasmosis
    • Que X, Wunderlich A, Joiner, KA, Reed SL. Toxopain-1 is critical for infection in a novel chicken embryo model of congenital toxoplasmosis. Infect Immun 2004; 72: 2915-21.
    • (2004) Infect Immun , vol.72 , pp. 2915-2921
    • Que, X.1    Wunderlich, A.2    Joiner, K.A.3    Reed, S.L.4
  • 147
    • 12544251879 scopus 로고    scopus 로고
    • The role of Plasmodium falciparum food vacuole plasmepsins
    • Liu J, Gluzman IY, Drew ME, Goldberg DE. The role of Plasmodium falciparum food vacuole plasmepsins. J Biol Chem 2005; 280: 1432-7
    • (2005) J Biol Chem , vol.280 , pp. 1432-1437
    • Liu, J.1    Gluzman, I.Y.2    Drew, M.E.3    Goldberg, D.E.4
  • 148
    • 0037836069 scopus 로고    scopus 로고
    • Plasmodium falciparum falcilysin: An unprocessed food vacuole enzyme
    • Murata CE, Goldberg DE. Plasmodium falciparum falcilysin: An unprocessed food vacuole enzyme. Mol Biochem Parasitol 2003; 129(1): 123-6.
    • (2003) Mol Biochem Parasitol , vol.129 , Issue.1 , pp. 123-126
    • Murata, C.E.1    Goldberg, D.E.2
  • 149
    • 5644247394 scopus 로고    scopus 로고
    • A Plasmodium falciparum dipeptidyl aminopeptidase I participates in vacuolar hemoglobin degradation
    • Klemba M, Gluzman I, Goldberg DE. A Plasmodium falciparum dipeptidyl aminopeptidase I participates in vacuolar hemoglobin degradation. J Biol Chem 2004; 279(41): 43000-7.
    • (2004) J Biol Chem , vol.279 , Issue.41 , pp. 43000-43007
    • Klemba, M.1    Gluzman, I.2    Goldberg, D.E.3
  • 150
    • 0034844897 scopus 로고    scopus 로고
    • The role of aminopeptidases in haemoglobin degradation in Plasmodium falciparum-infected erythrocytes
    • Gavigan CS, Dalton JP, Bell A. The role of aminopeptidases in haemoglobin degradation in Plasmodium falciparum-infected erythrocytes. Mol Biochem Parasitol 2001; 117(1):37-48
    • (2001) Mol Biochem Parasitol , vol.117 , Issue.1 , pp. 37-48
    • Gavigan, C.S.1    Dalton, J.P.2    Bell, A.3
  • 151
    • 0042329312 scopus 로고    scopus 로고
    • The formation of haemozoin-further intrigue
    • Trager W. The formation of haemozoin-further intrigue. Trends Parasitol 2003; 19(9): 399-92.
    • (2003) Trends Parasitol , vol.19 , Issue.9 , pp. 399-492
    • Trager, W.1
  • 152
    • 36749000794 scopus 로고    scopus 로고
    • Malaria chemotherapeutics part I: History of antimalarial drug development, currently used therapeutics, and drugs in clinical development
    • Schlitzer M. Malaria chemotherapeutics part I: History of antimalarial drug development, currently used therapeutics, and drugs in clinical development. Chem Med Chem 2007; 2(7): 944-56.
    • (2007) Chem Med Chem , vol.2 , Issue.7 , pp. 944-956
    • Schlitzer, M.1
  • 153
    • 0033286295 scopus 로고    scopus 로고
    • Chloroquine uptake and activity is determined by binding to ferriprotoporphyrin IX in Plasmodium falciparum
    • Bray PG, Janneh O, Ward SA. Chloroquine uptake and activity is determined by binding to ferriprotoporphyrin IX in Plasmodium falciparum. Novartis Found Symp 1999; 226: 252-60.
    • (1999) Novartis Found Symp , vol.226 , pp. 252-260
    • Bray, P.G.1    Janneh, O.2    Ward, S.A.3
  • 154
    • 0035884456 scopus 로고    scopus 로고
    • Chloroquine-resistant malaria
    • Wellems TE, Plowe CV. Chloroquine-resistant malaria. J Infect Dis 2001; 184(6): 770-6.
    • (2001) J Infect Dis , vol.184 , Issue.6 , pp. 770-776
    • Wellems, T.E.1    Plowe, C.V.2
  • 156
    • 0002295721 scopus 로고    scopus 로고
    • Use of Artemisinin (Qinghaosu) derivatives in the treatment of malaria
    • Kokwaro GO. Use of Artemisinin (Qinghaosu) derivatives in the treatment of malaria. African J Health Sci 1998; 5(1): 8-11
    • (1998) African J Health Sci , vol.5 , Issue.1 , pp. 8-11
    • Kokwaro, G.O.1
  • 157
    • 33645870422 scopus 로고    scopus 로고
    • Production of the antimalarial drug precursor artemisinic acid in engineered yeast
    • Ro DK, Paradise EM, Ouellet M, Fisher KJ, Newman KL, Ndungu JM, et al. Production of the antimalarial drug precursor artemisinic acid in engineered yeast. Nature 2006; 440: 940-3.
    • (2006) Nature , vol.440 , pp. 940-943
    • Ro, D.K.1    Paradise, E.M.2    Ouellet, M.3    Fisher, K.J.4    Newman, K.L.5    Ndungu, J.M.6
  • 159
    • 33748328016 scopus 로고    scopus 로고
    • Gene disruptions demonstrate independent roles for the four falcipain cysteine proteases of Plasmodium falciparum
    • Sijwali PS, Koo J, Singh N, Rosenthal PJ. Gene disruptions demonstrate independent roles for the four falcipain cysteine proteases of Plasmodium falciparum. Mol Biochem Parasitol 2006; 150(1): 96-106.
    • (2006) Mol Biochem Parasitol , vol.150 , Issue.1 , pp. 96-106
    • Sijwali, P.S.1    Koo, J.2    Singh, N.3    Rosenthal, P.J.4
  • 160
    • 0031691453 scopus 로고    scopus 로고
    • Antimalarial synergy of cysteine and aspartic protease inhibitors
    • Semenov A, Olson JE, Rosenthal PJ. Antimalarial synergy of cysteine and aspartic protease inhibitors. Antimicrob Agents Chemother 1998; 42(9): 2254-8.
    • (1998) Antimicrob Agents Chemother , vol.42 , Issue.9 , pp. 2254-2258
    • Semenov, A.1    Olson, J.E.2    Rosenthal, P.J.3
  • 161
    • 33746791205 scopus 로고    scopus 로고
    • Structural basis for unique mechanisms of folding and hemoglobin binding by a malarial protease
    • Wang SX, Pandey KC, Somoza JR, Sijwali PS, Kortemme T, Brinen LS, et al. Structural basis for unique mechanisms of folding and hemoglobin binding by a malarial protease. Proc. Natl Acad Sci USA 2006; 103(31):11503-8.
    • (2006) Proc. Natl Acad Sci USA , vol.103 , Issue.31 , pp. 11503-11508
    • Wang, S.X.1    Pandey, K.C.2    Somoza, J.R.3    Sijwali, P.S.4    Kortemme, T.5    Brinen, L.S.6
  • 162
    • 0037175033 scopus 로고    scopus 로고
    • Active site contribution to specificity of the aspartic proteases plasmepsins I and II
    • Siripurkpong P, Yuvaniyama J, Wilairat P, Goldberg DE. Active site contribution to specificity of the aspartic proteases plasmepsins I and II. J Biol Chem 2002; 277: 41009-13.
    • (2002) J Biol Chem , vol.277 , pp. 41009-41013
    • Siripurkpong, P.1    Yuvaniyama, J.2    Wilairat, P.3    Goldberg, D.E.4
  • 163
    • 0035138734 scopus 로고    scopus 로고
    • Drug targets and mechanisms of resistance in anaerobic protozoa
    • Upcroft P, Upcroft JA. Drug targets and mechanisms of resistance in anaerobic protozoa. Clin Microb Rev 2001; 14: 150-4.
    • (2001) Clin Microb Rev , vol.14 , pp. 150-154
    • Upcroft, P.1    Upcroft, J.A.2
  • 165
    • 0037460789 scopus 로고    scopus 로고
    • Amoebiasis
    • Stanley SL. Amoebiasis. Lancet 2003; 361: 1025-34.
    • (2003) Lancet , vol.361 , pp. 1025-1034
    • Stanley, S.L.1
  • 167
    • 0034821972 scopus 로고    scopus 로고
    • Parasitic infections of the gastrointestinal tract
    • Katz DE, Taylor DN. Parasitic infections of the gastrointestinal tract. Gastroenterol Clin 2001; 30: 1-9.
    • (2001) Gastroenterol Clin , vol.30 , pp. 1-9
    • Katz, D.E.1    Taylor, D.N.2
  • 168
    • 34848872528 scopus 로고    scopus 로고
    • Experience with intravenous metronidazole to treat moderate to severe amebiasisi in Japan
    • Kimura M, Nakamura T, Nawa Y. Experience with intravenous metronidazole to treat moderate to severe amebiasisi in Japan. Am J Trop Med Hyg 2007; 77: 381-5.
    • (2007) Am J Trop Med Hyg , vol.77 , pp. 381-385
    • Kimura, M.1    Nakamura, T.2    Nawa, Y.3
  • 169
    • 0031465651 scopus 로고    scopus 로고
    • Samarawickerma NA, Brown DM, Upcroft iA, Thammapalerd N, Upcroft P. Involvement of superoxide dismutase and pyruvate-ferredoxin oxidoreductase in mechanisms of metronidazole resistance in Entamoeba histolytica. J. Antimicrob Ther 1997; 40: 833-40.
    • Samarawickerma NA, Brown DM, Upcroft iA, Thammapalerd N, Upcroft P. Involvement of superoxide dismutase and pyruvate-ferredoxin oxidoreductase in mechanisms of metronidazole resistance in Entamoeba histolytica. J. Antimicrob Ther 1997; 40: 833-40.
  • 170
    • 0036324358 scopus 로고    scopus 로고
    • Letter to Editor
    • Harder A. Letter to Editor. Parasitol Res 2002; 88: 1
    • (2002) Parasitol Res , vol.88 , pp. 1
    • Harder, A.1
  • 172
    • 0025040467 scopus 로고
    • Entamoeba histolytica: Correlation of the cytopathic effect of virulent trophozoites with secretion of cysteine proteinase
    • Keene WM, Hidalgo ME, Orozco E, McKerrow JH. Entamoeba histolytica: Correlation of the cytopathic effect of virulent trophozoites with secretion of cysteine proteinase. Exp Parasitol 1990; 71: 199-206.
    • (1990) Exp Parasitol , vol.71 , pp. 199-206
    • Keene, W.M.1    Hidalgo, M.E.2    Orozco, E.3    McKerrow, J.H.4
  • 173
    • 2442462002 scopus 로고    scopus 로고
    • Proteinase inhibitors TPCK and TCLK prevent Entamoeba histolytica disturbance of tight junctions and microvilli in enteric layers in vitro
    • Lauwact T, Oliveira MJ, Callewaert B, de Bruyne G, Marcel M, Leroy A. Proteinase inhibitors TPCK and TCLK prevent Entamoeba histolytica disturbance of tight junctions and microvilli in enteric layers in vitro. Int J Parasitol 2004; 34: 785-94.
    • (2004) Int J Parasitol , vol.34 , pp. 785-794
    • Lauwact, T.1    Oliveira, M.J.2    Callewaert, B.3    de Bruyne, G.4    Marcel, M.5    Leroy, A.6
  • 175
    • 0027245498 scopus 로고
    • Cloning a virulence factor of Entamoeba histolytica: Pathogenic strains posses a unique cysteine proteinase gene
    • Reed S, Bouvier J, Pollack AS, Engel JC, Brown M, Hirata K, et al. Cloning a virulence factor of Entamoeba histolytica: Pathogenic strains posses a unique cysteine proteinase gene. J Clin Invest 1993; 91: 1532-40.
    • (1993) J Clin Invest , vol.91 , pp. 1532-1540
    • Reed, S.1    Bouvier, J.2    Pollack, A.S.3    Engel, J.C.4    Brown, M.5    Hirata, K.6
  • 176
    • 0038482128 scopus 로고    scopus 로고
    • The intestinal protozoan parasite Entamoeha histolytica contains 20 cysteine protease genes, of which only a small subset is expressed during in vitro cultivation
    • Bruchhaus I, Loftus BJ, Hall N, Tannich E. The intestinal protozoan parasite Entamoeha histolytica contains 20 cysteine protease genes, of which only a small subset is expressed during in vitro cultivation. Eukaryot Cell 2003; 2: 501-9.
    • (2003) Eukaryot Cell , vol.2 , pp. 501-509
    • Bruchhaus, I.1    Loftus, B.J.2    Hall, N.3    Tannich, E.4
  • 177
    • 33748792562 scopus 로고    scopus 로고
    • Two cysteine protease inbibitors, EhICP1 and 2, localized in distinct compartments, negatively regulate secretion in Entamoeba hystolytica
    • Sato D, Nakada-Tsukui K, Okada M, Nozaki T. Two cysteine protease inbibitors, EhICP1 and 2, localized in distinct compartments, negatively regulate secretion in Entamoeba hystolytica. FEBS Lett 2006; 580: 5306-12.
    • (2006) FEBS Lett , vol.580 , pp. 5306-5312
    • Sato, D.1    Nakada-Tsukui, K.2    Okada, M.3    Nozaki, T.4
  • 178
    • 33751397621 scopus 로고    scopus 로고
    • A phagocytosis mutant of Entamoeaba histolytica is less virulent due to deficient proteinase expression and release
    • Hirata K, Que X, Melendez-Lopez SG, Debnath A, Myers S, Herdman S, et al. A phagocytosis mutant of Entamoeaba histolytica is less virulent due to deficient proteinase expression and release. Exp Parasitol 2007; 115: 192-9.
    • (2007) Exp Parasitol , vol.115 , pp. 192-199
    • Hirata, K.1    Que, X.2    Melendez-Lopez, S.G.3    Debnath, A.4    Myers, S.5    Herdman, S.6
  • 179
    • 34447576973 scopus 로고    scopus 로고
    • Use of recombinant Entamoeba histolytica cysteine proteinase 1 to identify a potent inhibitor of amebic invasion in a human colonic model
    • Melendez-Lopez SG, Herdman S, Hirata K, Choi M, Choe Y, Craik C, et al. Use of recombinant Entamoeba histolytica cysteine proteinase 1 to identify a potent inhibitor of amebic invasion in a human colonic model. Eukaryot Cell 2007; 6: 1130-6.
    • (2007) Eukaryot Cell , vol.6 , pp. 1130-1136
    • Melendez-Lopez, S.G.1    Herdman, S.2    Hirata, K.3    Choi, M.4    Choe, Y.5    Craik, C.6
  • 180
    • 18044389332 scopus 로고    scopus 로고
    • Okada M, Huston CD, Mann BJ, Petri WA, Kita k, Nozaki T. Proteomic analysis of phagocytosis of the protozoan parasite Entamoeba histolytica. Eukaryot Cell 2005; 4: 827-1.
    • Okada M, Huston CD, Mann BJ, Petri WA, Kita k, Nozaki T. Proteomic analysis of phagocytosis of the protozoan parasite Entamoeba histolytica. Eukaryot Cell 2005; 4: 827-1.
  • 181
    • 34249941288 scopus 로고    scopus 로고
    • Transcriptional and secretory responses of Entamoeba histolytica to mucins, epithelial cells and bacteria
    • Debnath A, Tashker JS, Sajid M, McKerrow JH. Transcriptional and secretory responses of Entamoeba histolytica to mucins, epithelial cells and bacteria. Int J Parasitol 2007; 37: 897-906.
    • (2007) Int J Parasitol , vol.37 , pp. 897-906
    • Debnath, A.1    Tashker, J.S.2    Sajid, M.3    McKerrow, J.H.4
  • 182
    • 4243178226 scopus 로고    scopus 로고
    • Free-living amobeae as opportunistic and non-opportunistic pathogens of humans and animals
    • Schuster FL, Visvesvara GS. Free-living amobeae as opportunistic and non-opportunistic pathogens of humans and animals. Int J Parasitol 2004; 34: 1001-7.
    • (2004) Int J Parasitol , vol.34 , pp. 1001-1007
    • Schuster, F.L.1    Visvesvara, G.S.2
  • 183
    • 3042699709 scopus 로고    scopus 로고
    • Treatment of Acanthamoeba keratitis
    • Seal D. Treatment of Acanthamoeba keratitis. Expert Rev Anti Infect Ther 2003; 1: 205-8.
    • (2003) Expert Rev Anti Infect Ther , vol.1 , pp. 205-208
    • Seal, D.1
  • 184
    • 30944453886 scopus 로고    scopus 로고
    • Intracellular localization and trafficking of serine proteinase AhSub and cysteine proteinase AhCP of Acanthamoeba healyi
    • Moon EK, Lee ST, Chung DI, Kong IIII. Intracellular localization and trafficking of serine proteinase AhSub and cysteine proteinase AhCP of Acanthamoeba healyi. Eukaryot Cell 2006; 5: 125-31.
    • (2006) Eukaryot Cell , vol.5 , pp. 125-131
    • Moon, E.K.1    Lee, S.T.2    Chung, D.I.3    IIII, K.4
  • 185
    • 0031962434 scopus 로고    scopus 로고
    • Isolation and molecular characterization of a surface-bound proteinase of Entamoeba histolytica
    • Jacobs T, Bruchhaus I, Dandekar T, Tannich E, Leippe M. Isolation and molecular characterization of a surface-bound proteinase of Entamoeba histolytica. Mol Microbiol 1998; 27: 269-76.
    • (1998) Mol Microbiol , vol.27 , pp. 269-276
    • Jacobs, T.1    Bruchhaus, I.2    Dandekar, T.3    Tannich, E.4    Leippe, M.5
  • 186
  • 187
    • 19744380878 scopus 로고    scopus 로고
    • Therapy for common parasitic diseases in pregnancy in the United States: A review and a survey of obstetrician/ gynecologists' level of knowledge about theses diseases
    • Jones JL, Schulkin J, Maguire JH. Therapy for common parasitic diseases in pregnancy in the United States: A review and a survey of obstetrician/ gynecologists' level of knowledge about theses diseases. Obstet Gynecol Surv 2005; 60: 386-93.
    • (2005) Obstet Gynecol Surv , vol.60 , pp. 386-393
    • Jones, J.L.1    Schulkin, J.2    Maguire, J.H.3
  • 189
    • 0037096981 scopus 로고    scopus 로고
    • Membrane-associated dipeptidyl peptidase IV is involved in encystation-specific gene expression during Giardia differentiation
    • Touz MC, Nores MJ, Slavin I, Piacenza L, Acosta D, Carmona C, et al. Membrane-associated dipeptidyl peptidase IV is involved in encystation-specific gene expression during Giardia differentiation. Biochem J 2002; 364: 703-810.
    • (2002) Biochem J , vol.364 , pp. 703-810
    • Touz, M.C.1    Nores, M.J.2    Slavin, I.3    Piacenza, L.4    Acosta, D.5    Carmona, C.6
  • 190
    • 0037040969 scopus 로고    scopus 로고
    • The activity of a developmentally regulated cysteine proteinase is required for cyst wall formation in the primitive eukaryote Giardia lamblia
    • Touz MC, Nores MJ, Slavin I, Carmona C, Conrad JT, Mowatt MR, et al. The activity of a developmentally regulated cysteine proteinase is required for cyst wall formation in the primitive eukaryote Giardia lamblia. J Biol Chem 2002; 277(10):847-81.
    • (2002) J Biol Chem , vol.277 , Issue.10 , pp. 847-881
    • Touz, M.C.1    Nores, M.J.2    Slavin, I.3    Carmona, C.4    Conrad, J.T.5    Mowatt, M.R.6
  • 191
    • 0030952807 scopus 로고    scopus 로고
    • A primitive enzyme for a primitive cell: The protease required for excystation of Giardia
    • Ward W, Alvarado L, Rawlings ND, Engel JC, Franklin C, McKerrow JH. A primitive enzyme for a primitive cell: The protease required for excystation of Giardia. Cell 1997; 89: 437-44.
    • (1997) Cell , vol.89 , pp. 437-444
    • Ward, W.1    Alvarado, L.2    Rawlings, N.D.3    Engel, J.C.4    Franklin, C.5    McKerrow, J.H.6


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