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Volumn 1, Issue , 2006, Pages 497-536

Proteases in parasitic diseases

Author keywords

Host; Immune response; Invasion; Parasite; Protease inhibitor

Indexed keywords

CRUZIPAIN; CYSTATIN; CYSTEINE PROTEINASE; HEMOGLOBIN; PROTEINASE; PROTEINASE INHIBITOR; SERINE PROTEINASE INHIBITOR;

EID: 33645744855     PISSN: 15534006     EISSN: 15534014     Source Type: Book Series    
DOI: 10.1146/annurev.pathol.1.110304.100151     Document Type: Review
Times cited : (341)

References (208)
  • 2
    • 4043122563 scopus 로고    scopus 로고
    • Bioinformatics of proteases in the MEROPS database
    • Barrett AJ. 2004. Bioinformatics of proteases in the MEROPS database. Curr. Opin. Drug Discov. Dev. 7:334-41
    • (2004) Curr. Opin. Drug Discov. Dev. , vol.7 , pp. 334-341
    • Barrett, A.J.1
  • 3
    • 0024986279 scopus 로고
    • Anisakis-from the platter to the microfuge
    • Sakanari JA. 1990. Anisakis-from the platter to the microfuge. Parasitol. Today 6:323-27
    • (1990) Parasitol. Today , vol.6 , pp. 323-327
    • Sakanari, J.A.1
  • 5
    • 0036186584 scopus 로고    scopus 로고
    • One confirmed and six suspected cases of cutaneous larva migrans caused by overseas infection with dog hookworm larvae
    • Nakamura-Uchiyama F, Yamasaki E, Nawa Y. 2002. One confirmed and six suspected cases of cutaneous larva migrans caused by overseas infection with dog hookworm larvae. J. Dermatol. 29:104-11
    • (2002) J. Dermatol. , vol.29 , pp. 104-111
    • Nakamura-Uchiyama, F.1    Yamasaki, E.2    Nawa, Y.3
  • 9
    • 0025305238 scopus 로고
    • Strongyloides stercoralis: Identification of a protease that facilitates penetration of skin by the infective larvae
    • McKerrow JH, Brindley P, Brown M, Gam AA, Staunton C, Neva FA. 1990. Strongyloides stercoralis: identification of a protease that facilitates penetration of skin by the infective larvae. Exp. Parasitol. 70:134-43
    • (1990) Exp. Parasitol. , vol.70 , pp. 134-143
    • McKerrow, J.H.1    Brindley, P.2    Brown, M.3    Gam, A.A.4    Staunton, C.5    Neva, F.A.6
  • 11
    • 0345283097 scopus 로고    scopus 로고
    • Cloning and expression of the major secreted cathepsin B-like protein from juvenile Fasciola hepatica and analysis of immunogenicity following liver fluke infection
    • Law RH, Smooker PM, Irving JA, Piedrafita D, Ponting R, et al. 2003. Cloning and expression of the major secreted cathepsin B-like protein from juvenile Fasciola hepatica and analysis of immunogenicity following liver fluke infection. Infect. Immun. 71:6921-32
    • (2003) Infect. Immun. , vol.71 , pp. 6921-6932
    • Law, R.H.1    Smooker, P.M.2    Irving, J.A.3    Piedrafita, D.4    Ponting, R.5
  • 12
    • 0033776405 scopus 로고    scopus 로고
    • Proteolytic activity of cysteine protease in excretory-secretory product of Paragonimus westermani newly excysted metacercariae pivotally regulates IL-8 production of human eosinophils
    • Shin MH, Lee SY. 2000. Proteolytic activity of cysteine protease in excretory-secretory product of Paragonimus westermani newly excysted metacercariae pivotally regulates IL-8 production of human eosinophils. Parasite Immunol. 22:529-33
    • (2000) Parasite Immunol. , vol.22 , pp. 529-533
    • Shin, M.H.1    Lee, S.Y.2
  • 13
    • 0038392947 scopus 로고    scopus 로고
    • Characterization and classification of five cysteine proteinases expressed by Paragonimus westermani adult worm
    • Park H, Kim SI, Hong KM, Kim MJ, Shin CH, et al. 2002. Characterization and classification of five cysteine proteinases expressed by Paragonimus westermani adult worm. Exp. Parasitol. 102:143-49
    • (2002) Exp. Parasitol. , vol.102 , pp. 143-149
    • Park, H.1    Kim, S.I.2    Hong, K.M.3    Kim, M.J.4    Shin, C.H.5
  • 14
    • 0036802282 scopus 로고    scopus 로고
    • Expression of cysteine proteinase of Clonorchis sinensis and its use in serodiagnosis of clonorchiasis
    • Na BK, Lee HJ, Cho SH, Lee HW, Cho JH, et al. 2002. Expression of cysteine proteinase of Clonorchis sinensis and its use in serodiagnosis of clonorchiasis. J. Parasitol. 88:1000-6
    • (2002) J. Parasitol. , vol.88 , pp. 1000-1006
    • Na, B.K.1    Lee, H.J.2    Cho, S.H.3    Lee, H.W.4    Cho, J.H.5
  • 15
    • 0028879166 scopus 로고
    • Purification and characterization of acid cysteine protease from metacercariae of the mammalian trematode parasite Paragonimus westermani
    • Yamakami K, Hamajima F, Akao S, Tadakuma T. 1995. Purification and characterization of acid cysteine protease from metacercariae of the mammalian trematode parasite Paragonimus westermani. Eur. J. Biochem. 233:490-97
    • (1995) Eur. J. Biochem. , vol.233 , pp. 490-497
    • Yamakami, K.1    Hamajima, F.2    Akao, S.3    Tadakuma, T.4
  • 16
    • 0033776405 scopus 로고    scopus 로고
    • Proteolytic activity of cysteine protease in excretory-secretory product of Paragonimus westermani newly excysted metacercariae pivotally regulate IL-8 production of human eosinophils
    • Shin MH, Lee SY. 2000. Proteolytic activity of cysteine protease in excretory-secretory product of Paragonimus westermani newly excysted metacercariae pivotally regulate IL-8 production of human eosinophils. Parasite Immunol. 22:529-33
    • (2000) Parasite Immunol. , vol.22 , pp. 529-533
    • Shin, M.H.1    Lee, S.Y.2
  • 17
    • 0022916238 scopus 로고
    • Cysteinyl proteinases of Schistosoma mansoni eggs: Purification and partial characterization
    • Sung CK, Dresden MH. 1986. Cysteinyl proteinases of Schistosoma mansoni eggs: purification and partial characterization. J. Parasitol. 72:891-900
    • (1986) J. Parasitol. , vol.72 , pp. 891-900
    • Sung, C.K.1    Dresden, M.H.2
  • 19
    • 0023201292 scopus 로고
    • Sera of Schistosoma japonicum-infected patients cross-react with diagnostic 31/32 kD proteins of S. mansoni
    • Ruppel A, Shi YE, Wei DX, Diesfeld HJ. 1987. Sera of Schistosoma japonicum-infected patients cross-react with diagnostic 31/32 kD proteins of S. mansoni. Clin. Exp. Immunol. 69:291-98
    • (1987) Clin. Exp. Immunol. , vol.69 , pp. 291-298
    • Ruppel, A.1    Shi, Y.E.2    Wei, D.X.3    Diesfeld, H.J.4
  • 20
    • 0029655973 scopus 로고    scopus 로고
    • Circulating antigens in schistosomiasis: Detection of 31/32-kDa proteins in sera from patients infected with Schistosoma japonicum, S. mansoni, S. haematobium, or S. intercalatum
    • Li YL, Idris MA, Corachan M, HanJJ, Kirschfink M, Ruppel A. 1996. Circulating antigens in schistosomiasis: detection of 31/32-kDa proteins in sera from patients infected with Schistosoma japonicum, S. mansoni, S. haematobium, or S. intercalatum. Parasitol. Res. 82:14-18
    • (1996) Parasitol. Res. , vol.82 , pp. 14-18
    • Li, Y.L.1    Idris, M.A.2    Corachan, M.3    Han, J.J.4    Kirschfink, M.5    Ruppel, A.6
  • 21
    • 0034458991 scopus 로고    scopus 로고
    • Structural and immunological characteristics of a 28-kilodalton cruzipain-like cysteine protease of Paragonimus westermani expressed in the definitive host stage
    • Yun DH, Chung JY, Chung YB, Bahk YY, Kang SY, et al. 2000. Structural and immunological characteristics of a 28-kilodalton cruzipain-like cysteine protease of Paragonimus westermani expressed in the definitive host stage. Clin. Diagn. Lab. Immunol. 7:932-39
    • (2000) Clin. Diagn. Lab. Immunol. , vol.7 , pp. 932-939
    • Yun, D.H.1    Chung, J.Y.2    Chung, Y.B.3    Bahk, Y.Y.4    Kang, S.Y.5
  • 22
    • 0024519061 scopus 로고
    • Effect of OPC-12759, a novel antiulcer agent, on chronic and acute experimental gastric ulcer, and gastric secretion in rats
    • Yamasaki K, Ishiyama H, Imaizumi T, Kanbe T, Yabuuchi Y. 1989. Effect of OPC-12759, a novel antiulcer agent, on chronic and acute experimental gastric ulcer, and gastric secretion in rats. Jpn. J. Pharmacol. 49:441-48
    • (1989) Jpn. J. Pharmacol. , vol.49 , pp. 441-448
    • Yamasaki, K.1    Ishiyama, H.2    Imaizumi, T.3    Kanbe, T.4    Yabuuchi, Y.5
  • 24
    • 33645736390 scopus 로고    scopus 로고
    • Intravascular schistosomes and complement
    • In press
    • Skelly PJ. 2005. Intravascular schistosomes and complement. Trends Parasitol. In press
    • (2005) Trends Parasitol.
    • Skelly, P.J.1
  • 25
    • 0037025351 scopus 로고    scopus 로고
    • Cercarial elastase is encoded by a functionally conserved gene family across multiple species of schistosomes
    • Salter JP, Choe Y, Albrecht H, Franklin C, Lim KC, et al. 2002. Cercarial elastase is encoded by a functionally conserved gene family across multiple species of schistosomes. J. Biol. Chem. 277:24618-24
    • (2002) J. Biol. Chem. , vol.277 , pp. 24618-24624
    • Salter, J.P.1    Choe, Y.2    Albrecht, H.3    Franklin, C.4    Lim, K.C.5
  • 26
    • 1942487645 scopus 로고    scopus 로고
    • Schistosomes in the skin: A balance between immune priming and regulation
    • Mountford AP, Trottein F. 2004. Schistosomes in the skin: a balance between immune priming and regulation. Trends Parasitol. 20:221-26
    • (2004) Trends Parasitol. , vol.20 , pp. 221-226
    • Mountford, A.P.1    Trottein, F.2
  • 27
    • 0037316979 scopus 로고    scopus 로고
    • Invasion of skin by schistosome cercariae: Some neglected facts
    • Curwen RS, Wilson RA. 2003. Invasion of skin by schistosome cercariae: some neglected facts. Trends Parasitol. 19:63-66
    • (2003) Trends Parasitol. , vol.19 , pp. 63-66
    • Curwen, R.S.1    Wilson, R.A.2
  • 28
    • 0029258345 scopus 로고
    • Novel mechanisms of immune evasion by Schistosoma mansoni
    • Fishelson Z. 1995. Novel mechanisms of immune evasion by Schistosoma mansoni. Mem. Inst. Orwaldo Cruz 90:289-92
    • (1995) Mem. Inst. Orwaldo Cruz , vol.90 , pp. 289-292
    • Fishelson, Z.1
  • 30
    • 0022571570 scopus 로고
    • Monoclonal antibody affinity purification of a Leishmania membrane glycoprotein and its inhibition of leishmania-macrophage binding
    • Chang CS, Chang KP. 1986. Monoclonal antibody affinity purification of a Leishmania membrane glycoprotein and its inhibition of leishmania-macrophage binding. Proc. Natl. Acad. Sci. USA 83:100-4
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 100-104
    • Chang, C.S.1    Chang, K.P.2
  • 32
    • 0033966027 scopus 로고    scopus 로고
    • Episomal expression of specific sense and antisense mRNAs in Leishmania amazonensis: Modulation of gp63 level in promastigotes and their infection of macrophages in vitro
    • Chen DQ, Kolli BK, Yadava N, Lu HG, Gilman-Sachs A, et al. 2000. Episomal expression of specific sense and antisense mRNAs in Leishmania amazonensis: modulation of gp63 level in promastigotes and their infection of macrophages in vitro. Infect. Immun. 68:80-86
    • (2000) Infect. Immun. , vol.68 , pp. 80-86
    • Chen, D.Q.1    Kolli, B.K.2    Yadava, N.3    Lu, H.G.4    Gilman-Sachs, A.5
  • 33
    • 0036178528 scopus 로고    scopus 로고
    • Targeted gene deletion in Leishmania major identifies leishmanolysin (GP63) as a virulence factor
    • Joshi PB, Kelly BL, Kamhawi S, Sacks DL, McMaster WR. 2002. Targeted gene deletion in Leishmania major identifies leishmanolysin (GP63) as a virulence factor. Mol. Biochem. Parasitol. 120:33-40
    • (2002) Mol. Biochem. Parasitol. , vol.120 , pp. 33-40
    • Joshi, P.B.1    Kelly, B.L.2    Kamhawi, S.3    Sacks, D.L.4    McMaster, W.R.5
  • 34
    • 0030296985 scopus 로고    scopus 로고
    • Exploitation of the complement system by Leishmania promastigotes
    • Brittingham A, Mosser DM. 1996. Exploitation of the complement system by Leishmania promastigotes. Parasitol. Today 12:444-47
    • (1996) Parasitol. Today , vol.12 , pp. 444-447
    • Brittingham, A.1    Mosser, D.M.2
  • 35
    • 0037128162 scopus 로고    scopus 로고
    • Complement interaction with trypanosomatid promastigotes in normal human serum
    • Dominguez M, Moreno I, Lopez-Trascasa M, Torano A. 2002. Complement interaction with trypanosomatid promastigotes in normal human serum. J. Exp. Med. 195:451-59
    • (2002) J. Exp. Med. , vol.195 , pp. 451-459
    • Dominguez, M.1    Moreno, I.2    Lopez-Trascasa, M.3    Torano, A.4
  • 36
    • 0037305054 scopus 로고    scopus 로고
    • Migration through the extracellular matrix by the parasitic protozoan Leishmania is enhanced by surface metalloprotease gp63
    • McGwire BS, Chang KP, Engman DM. 2003. Migration through the extracellular matrix by the parasitic protozoan Leishmania is enhanced by surface metalloprotease gp63. Infect. Immun. 71:1008-10
    • (2003) Infect. Immun. , vol.71 , pp. 1008-1010
    • McGwire, B.S.1    Chang, K.P.2    Engman, D.M.3
  • 37
    • 0034044991 scopus 로고    scopus 로고
    • Leishmania mexicana mutants lacking glycosylphosphatidylinositol (GPI):protein transamidase provide insights into the biosynthesis and functions of GPI-anchored proteins
    • Hilley JD, Zawadzki JL, McConville MJ, Coombs GH, Mottram JC. 2000. Leishmania mexicana mutants lacking glycosylphosphatidylinositol (GPI):protein transamidase provide insights into the biosynthesis and functions of GPI-anchored proteins. Mol. Biol. Cell 11:1183-95
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1183-1195
    • Hilley, J.D.1    Zawadzki, J.L.2    McConville, M.J.3    Coombs, G.H.4    Mottram, J.C.5
  • 38
    • 0032523872 scopus 로고    scopus 로고
    • Differentially expressed Leishmania major gp63 genes encode cell surface leishmanolysin with distinct signals for glycosylphosphatidylinositol attachment
    • Voth BR, Kelly BL, Joshi PB, Ivens AC, McMaster WR. 1998. Differentially expressed Leishmania major gp63 genes encode cell surface leishmanolysin with distinct signals for glycosylphosphatidylinositol attachment. Mol. Biochem. Parasitol. 93:31-41
    • (1998) Mol. Biochem. Parasitol. , vol.93 , pp. 31-41
    • Voth, B.R.1    Kelly, B.L.2    Joshi, P.B.3    Ivens, A.C.4    McMaster, W.R.5
  • 39
    • 0029143811 scopus 로고
    • Plasticity of gp63 gene organization in Leishmania (Viannia) braziliensis and Leishmania (Viannia) peruviana
    • Victoir K, Dujardin JC, de Doncker S, Barker DC, Arevalo J, et al. 1995. Plasticity of gp63 gene organization in Leishmania (Viannia) braziliensis and Leishmania (Viannia) peruviana. Parasitology 111(Pt. 3):265-73
    • (1995) Parasitology , vol.111 , Issue.PART 3 , pp. 265-273
    • Victoir, K.1    Dujardin, J.C.2    De Doncker, S.3    Barker, D.C.4    Arevalo, J.5
  • 40
    • 1942542161 scopus 로고    scopus 로고
    • Multiple products of the Leishmania chagasi major surface protease (MSP or GP63) gene family
    • Yao C, Luo J, Storlie P, Donelson JE, Wilson ME. 2004. Multiple products of the Leishmania chagasi major surface protease (MSP or GP63) gene family. Mol. Biochem. Parasitol. 135:171-83
    • (2004) Mol. Biochem. Parasitol. , vol.135 , pp. 171-183
    • Yao, C.1    Luo, J.2    Storlie, P.3    Donelson, J.E.4    Wilson, M.E.5
  • 41
    • 0029118175 scopus 로고
    • Structure of Leishmania lipophosphoglycan: Inter- and intra-specific polymorphism in Old World species
    • McConville MJ, Schnur LF, Jaffe C, Schneider P. 1995. Structure of Leishmania lipophosphoglycan: inter- and intra-specific polymorphism in Old World species. Biochem J. 310(Pt. 3):807-18
    • (1995) Biochem J. , vol.310 , Issue.PART 3 , pp. 807-818
    • McConville, M.J.1    Schnur, L.F.2    Jaffe, C.3    Schneider, P.4
  • 42
    • 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. 1992. Developmental modification of lipophosphoglycan during the differentiation of Leishmania major promastigotes to an infectious stage. EMBO J. 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
  • 43
    • 0026911141 scopus 로고
    • The structure and function of the surface lipophosphoglycan on different developmental stages of Leishmania promastigotes
    • Sacks DL. 1992. The structure and function of the surface lipophosphoglycan on different developmental stages of Leishmania promastigotes. Infect Agents Dis. 1:200-6
    • (1992) Infect Agents Dis. , vol.1 , pp. 200-206
    • Sacks, D.L.1
  • 44
    • 3343010589 scopus 로고    scopus 로고
    • Genetic complementation of Leishmania deficient in PSA (GP46) restores their resistance to lysis by complement
    • Lincoln LM, Ozaki M, Donelson JE, Beetham JK. 2004. Genetic complementation of Leishmania deficient in PSA (GP46) restores their resistance to lysis by complement. Mol. Biochem. Parasitol. 137:185-89
    • (2004) Mol. Biochem. Parasitol. , vol.137 , pp. 185-189
    • Lincoln, L.M.1    Ozaki, M.2    Donelson, J.E.3    Beetham, J.K.4
  • 45
    • 0037226127 scopus 로고    scopus 로고
    • Protozomics: Trypanosomatid parasite genetics comes of age
    • Beverley SM. 2003. Protozomics: trypanosomatid parasite genetics comes of age. Nat. Rev. Genet. 4:11-19
    • (2003) Nat. Rev. Genet. , vol.4 , pp. 11-19
    • Beverley, S.M.1
  • 49
    • 0029898541 scopus 로고    scopus 로고
    • Evidence from disruption of the lmcpb gene array of Leishmania mexicana that cysteine proteinases are virulence factors
    • Mottram JC, Souza AE, Hutchison JE, Carter R, Frame MJ, Coombs GH. 1996. Evidence from disruption of the lmcpb gene array of Leishmania mexicana that cysteine proteinases are virulence factors. Proc. Natl. Acad. Sci. USA 93:6008-13
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6008-6013
    • Mottram, J.C.1    Souza, A.E.2    Hutchison, J.E.3    Carter, R.4    Frame, M.J.5    Coombs, G.H.6
  • 50
    • 0030970429 scopus 로고    scopus 로고
    • The multiple cpb cysteine proteinase genes of Leishmania mexicana encode isoenzymes that differ in their stage regulation and substrate preferences
    • Mottram JC, Frame MJ, Brooks DR, Tetley L, Hutchison JE, et al. 1997. The multiple cpb cysteine proteinase genes of Leishmania mexicana encode isoenzymes that differ in their stage regulation and substrate preferences. J. Biol. Chem. 272:14285-93
    • (1997) J. Biol. Chem. , vol.272 , pp. 14285-14293
    • Mottram, J.C.1    Frame, M.J.2    Brooks, D.R.3    Tetley, L.4    Hutchison, J.E.5
  • 51
    • 0033820138 scopus 로고    scopus 로고
    • Analysis of the roles of cysteine proteinases of Leishmania mexicana in the host-parasite interaction
    • Frame MJ, Mottram JC, Coombs GH. 2000. Analysis of the roles of cysteine proteinases of Leishmania mexicana in the host-parasite interaction. Parasitology 121(Pt. 4):367-77
    • (2000) Parasitology , vol.121 , Issue.PART 4 , pp. 367-377
    • Frame, M.J.1    Mottram, J.C.2    Coombs, G.H.3
  • 52
    • 0032534577 scopus 로고    scopus 로고
    • Leishmania mexicana cysteine proteinase-deficient mutants have attenuated virulence for mice and potentiate a Th1 response
    • Alexander J, Coombs GH, Mottram JC. 1998. Leishmania mexicana cysteine proteinase-deficient mutants have attenuated virulence for mice and potentiate a Th1 response. J. Immunol. 161:6794-801
    • (1998) J. Immunol. , vol.161 , pp. 6794-6801
    • Alexander, J.1    Coombs, G.H.2    Mottram, J.C.3
  • 53
    • 4344613395 scopus 로고    scopus 로고
    • Inhibition of lipopolysaccharide-induced macrophage IL-12 production by Leishmania mexicana amastigotes: The role of cysteine peptidases and the NF-kappaB signaling pathway
    • Cameron P, McGachy A, Anderson M, Paul A, Coombs GH, et al. 2004. Inhibition of lipopolysaccharide-induced macrophage IL-12 production by Leishmania mexicana amastigotes: the role of cysteine peptidases and the NF-kappaB signaling pathway. J. Immunol. 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
  • 54
    • 0141955100 scopus 로고    scopus 로고
    • Cysteine protease B of Leishmania mexicana inhibits host Th1 responses and protective immunity
    • Buxbaum LU, Denise H, Coombs GH, Alexander J, Mottram JC, Scott P. 2003. Cysteine protease B of Leishmania mexicana inhibits host Th1 responses and protective immunity. J. Immunol. 171:3711-17
    • (2003) J. Immunol. , vol.171 , pp. 3711-3717
    • Buxbaum, L.U.1    Denise, H.2    Coombs, G.H.3    Alexander, J.4    Mottram, J.C.5    Scott, P.6
  • 55
    • 0033970867 scopus 로고    scopus 로고
    • Synergistic effects of IL-4 and IL-18 on IL-12-dependent IFN-gamma production by dendritic cells
    • Fukao T, Matsuda S, Koyasu S. 2000. Synergistic effects of IL-4 and IL-18 on IL-12-dependent IFN-gamma production by dendritic cells. J. Immunol. 164:64-71
    • (2000) J. Immunol. , vol.164 , pp. 64-71
    • Fukao, T.1    Matsuda, S.2    Koyasu, S.3
  • 56
    • 18344405138 scopus 로고    scopus 로고
    • Phagosomes are competent organelles for antigen cross-presentation
    • Houde M, Bertholet S, Gagnon E, Brunet S, Goyette G, et al. 2003. Phagosomes are competent organelles for antigen cross-presentation. Nature 425:402-6
    • (2003) Nature , vol.425 , pp. 402-406
    • Houde, M.1    Bertholet, S.2    Gagnon, E.3    Brunet, S.4    Goyette, G.5
  • 58
    • 0031883488 scopus 로고    scopus 로고
    • The neutral cysteine proteinase of Entamoeba histolytica degrades IgG and prevents its binding
    • Tran VQ, Herdman DS, Torian BE, Reed SL. 1998. The neutral cysteine proteinase of Entamoeba histolytica degrades IgG and prevents its binding. J. Infect. Dis. 177:508-11
    • (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
  • 59
    • 0027491336 scopus 로고
    • Degradation of human IgA by Entamoeba histolytica
    • Kelsall BL, Ravdin JI. 1993. Degradation of human IgA by Entamoeba histolytica. J. Infect. Dis. 168:1319-22
    • (1993) J. Infect. Dis. , vol.168 , pp. 1319-1322
    • Kelsall, B.L.1    Ravdin, J.I.2
  • 60
    • 3142547281 scopus 로고    scopus 로고
    • Cysteine proteinase activity is required for survival of the parasite in experimental acute amoebic liver abscesses in hamsters
    • Olivos-Garcia A, Tello E, Nequiz-Avendano M, Gonzalez-Canto A, Lopez-Vancell R, et al. 2004. Cysteine proteinase activity is required for survival of the parasite in experimental acute amoebic liver abscesses in hamsters. Parasitology 129:19-25
    • (2004) Parasitology , vol.129 , pp. 19-25
    • Olivos-Garcia, A.1    Tello, E.2    Nequiz-Avendano, M.3    Gonzalez-Canto, A.4    Lopez-Vancell, R.5
  • 61
    • 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, Loftus BJ, Hall N, Tannich E. 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 2:501-9
    • (2003) Eukaryot. Cell , vol.2 , pp. 501-509
    • Bruchhaus, I.1    Loftus, B.J.2    Hall, N.3    Tannich, E.4
  • 62
    • 0029802679 scopus 로고    scopus 로고
    • Entamoeba histolytica and Entamoeba dispar: Differences in numbers and expression of cysteine proteinase genes
    • Bruchhaus I, Jacobs T, Leippe M, Tannich E. 1996. Entamoeba histolytica and Entamoeba dispar: differences in numbers and expression of cysteine proteinase genes. Mol. Microbiol. 22:255-63
    • (1996) Mol. Microbiol. , vol.22 , pp. 255-263
    • Bruchhaus, I.1    Jacobs, T.2    Leippe, M.3    Tannich, E.4
  • 63
    • 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 U, Hamann E, Tannich E. 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. 67:5925-29
    • (1999) Infect. Immun. , vol.67 , pp. 5925-5929
    • Willhoeft, U.1    Hamann, E.2    Tannich, E.3
  • 64
    • 0035145266 scopus 로고    scopus 로고
    • Overexpression of cysteine proteinase 2 in Entamoeba histolytica or Entamoeba dispar increases amoeba-induced monolayer destruction in vitro but does not augment amoebic liver abscess formation in gerbils
    • Hellberg A, Nickel R, Lotter H, Tannich E, Bruchhaus I. 2001. Overexpression of cysteine proteinase 2 in Entamoeba histolytica or Entamoeba dispar increases amoeba-induced monolayer destruction in vitro but does not augment amoebic liver abscess formation in gerbils. Cell. Microbiol. 3:13-20
    • (2001) Cell. Microbiol. , vol.3 , pp. 13-20
    • Hellberg, A.1    Nickel, R.2    Lotter, H.3    Tannich, E.4    Bruchhaus, I.5
  • 66
    • 0031804283 scopus 로고    scopus 로고
    • Antisense inhibition of expression of cysteine proteinases does not affect Entamoeba histolytica cytopathic or haemolytic activity but inhibits phagocytosis
    • Ankri S, Stolarsky T, Mirelman D. 1998. Antisense inhibition of expression of cysteine proteinases does not affect Entamoeba histolytica cytopathic or haemolytic activity but inhibits phagocytosis. Mol. Microbiol. 28:777-85
    • (1998) Mol. Microbiol. , vol.28 , pp. 777-785
    • Ankri, S.1    Stolarsky, T.2    Mirelman, D.3
  • 67
    • 0032918535 scopus 로고    scopus 로고
    • Antisense inhibition of expression of cysteine proteinases affects Entamoeba histolytica-induced formation of liver abscess in hamsters
    • Ankri S, Stolarsky T, Bracha R, Padilla-Vaca F, Mirelman D. 1999. Antisense inhibition of expression of cysteine proteinases affects Entamoeba histolytica-induced formation of liver abscess in hamsters. Infect. Immun. 67:421-22
    • (1999) Infect. Immun. , vol.67 , pp. 421-422
    • Ankri, S.1    Stolarsky, T.2    Bracha, R.3    Padilla-Vaca, F.4    Mirelman, D.5
  • 68
    • 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, Wang E, Seydel KB, Li E, Ankri S, et al. 2000. Entamoeba histolytica cysteine proteinases with interleukin-1 beta converting enzyme (ICE) activity cause intestinal inflammation and tissue damage in amoebiasis. Mol. Microbiol. 37:542-48
    • (2000) Mol. Microbiol. , vol.37 , pp. 542-548
    • Zhang, Z.1    Wang, E.2    Seydel, K.B.3    Li, E.4    Ankri, S.5
  • 69
    • 0037371362 scopus 로고    scopus 로고
    • A surface amebic cysteine proteinase inactivates interleukin-18
    • Que X, Kim SH, Sajid M, Eckmann E, Dinarello CA, et al. 2003. A surface amebic cysteine proteinase inactivates interleukin-18. Infect. Immun. 71:1274-80
    • (2003) Infect. Immun. , vol.71 , pp. 1274-1280
    • Que, X.1    Kim, S.H.2    Sajid, M.3    Eckmann, E.4    Dinarello, C.A.5
  • 70
    • 3142784289 scopus 로고    scopus 로고
    • Inhibition of gene expression with double strand RNA interference in Entamoeba histolytica
    • Kaur G, Lohia A. 2004. Inhibition of gene expression with double strand RNA interference in Entamoeba histolytica. Biochem. Biophys. Res. Commun. 320:1118-22
    • (2004) Biochem. Biophys. Res. Commun. , vol.320 , pp. 1118-1122
    • Kaur, G.1    Lohia, A.2
  • 72
    • 0028356910 scopus 로고
    • Anti-immunoglobulin e treatment decreases worm burden and egg production in Schistosoma mansoni-infected normal and interferon gamma knockout mice
    • Amiri P, Haak-Frendscho M, Robbins K, McKerrow JH, Stewart T, Jardieu P. 1994. Anti-immunoglobulin E treatment decreases worm burden and egg production in Schistosoma mansoni-infected normal and interferon gamma knockout mice. J. Exp. Med. 180:43-51
    • (1994) J. Exp. Med. , vol.180 , pp. 43-51
    • Amiri, P.1    Haak-Frendscho, M.2    Robbins, K.3    McKerrow, J.H.4    Stewart, T.5    Jardieu, P.6
  • 73
    • 0030636793 scopus 로고    scopus 로고
    • Mice with a targeted deletion of the IgE gene have increased worm burdens and reduced granulomatous inflammation following primary infection with Schistosoma mansoni
    • King CL, Xianli J, Malhotra I, Liu S, Mahmoud AA, Oettgen HC. 1997. Mice with a targeted deletion of the IgE gene have increased worm burdens and reduced granulomatous inflammation following primary infection with Schistosoma mansoni. J. Immunol. 158:294-300
    • (1997) J. Immunol. , vol.158 , pp. 294-300
    • King, C.L.1    Xianli, J.2    Malhotra, I.3    Liu, S.4    Mahmoud, A.A.5    Oettgen, H.C.6
  • 74
    • 0037407843 scopus 로고    scopus 로고
    • Mice genetically deficient in immunoglobulin e are more permissive hosts than wild-type mice to a primary, but not secondary, infection with the filarial nematode Brugia malayi
    • Spencer LA, Porte P, Zetoff C, Rajan TV. 2003. Mice genetically deficient in immunoglobulin E are more permissive hosts than wild-type mice to a primary, but not secondary, infection with the filarial nematode Brugia malayi. Infect. Immun. 71:2462-67
    • (2003) Infect. Immun. , vol.71 , pp. 2462-2467
    • Spencer, L.A.1    Porte, P.2    Zetoff, C.3    Rajan, T.V.4
  • 75
    • 0030176392 scopus 로고    scopus 로고
    • Schistosoma mansoni: Evidence for a 28-kDa membrane-anchored protease on schistosomula
    • Ghendler Y, Parizade M, Arnon R, McKerrow JH, Fishelson Z. 1996. Schistosoma mansoni: evidence for a 28-kDa membrane-anchored protease on schistosomula. Exp. Parasitol. 83:73-82
    • (1996) Exp. Parasitol. , vol.83 , pp. 73-82
    • Ghendler, Y.1    Parizade, M.2    Arnon, R.3    McKerrow, J.H.4    Fishelson, Z.5
  • 76
    • 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. 1998. Cysteine protease inhibitors alter Golgi complex ultrastructure and function in Trypanosoma cruzi. J. Cell Sci. 111(Pt. 5):597-606
    • (1998) J. Cell Sci. , vol.111 , Issue.PART 5 , 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
  • 77
    • 0028866134 scopus 로고
    • The mechanisms of Trypanosoma cruzi invasion of mammalian cells
    • Burleigh BA, Andrews NW. 1995. The mechanisms of Trypanosoma cruzi invasion of mammalian cells. Annu. Rev. Microbiol. 49:175-200
    • (1995) Annu. Rev. Microbiol. , vol.49 , pp. 175-200
    • Burleigh, B.A.1    Andrews, N.W.2
  • 78
    • 4844220220 scopus 로고    scopus 로고
    • Generation, specificity, and function of CD8+ T cells in Trypanosoma cruzi infection
    • Martin D, Tarleton R. 2004. Generation, specificity, and function of CD8+ T cells in Trypanosoma cruzi infection. Immunol. Rev. 201:304-17
    • (2004) Immunol. Rev. , vol.201 , pp. 304-317
    • Martin, D.1    Tarleton, R.2
  • 79
    • 0036155657 scopus 로고    scopus 로고
    • Pathogenesis of Chagas heart disease: Role of autoimmunity
    • Engman DM, Leon JS. 2002. Pathogenesis of Chagas heart disease: role of autoimmunity. Acta Trop. 81:123-32
    • (2002) Acta Trop. , vol.81 , pp. 123-132
    • Engman, D.M.1    Leon, J.S.2
  • 80
    • 1142291085 scopus 로고    scopus 로고
    • Chagas disease: A role for autoimmunity?
    • Tarleton RL. 2003. Chagas disease: a role for autoimmunity? Trends Parasitol. 19:447-51
    • (2003) Trends Parasitol. , vol.19 , pp. 447-451
    • Tarleton, R.L.1
  • 81
    • 0034613763 scopus 로고    scopus 로고
    • Host cell invasion by Trypanosoma cruzi is potentiated by activation of bradykinin B(2) receptors
    • Scharfstein J, Schmitz V, Morandi V, Capella MM, Lima AP, et al. 2000. Host cell invasion by Trypanosoma cruzi is potentiated by activation of bradykinin B(2) receptors. J. Exp. Med. 192:1289-300
    • (2000) J. Exp. Med. , vol.192 , pp. 1289-1300
    • Scharfstein, J.1    Schmitz, V.2    Morandi, V.3    Capella, M.M.4    Lima, A.P.5
  • 82
    • 4644357065 scopus 로고    scopus 로고
    • Anew cruzipain-mediated pathway of human cell invasion by Trypanosoma cruzi requires trypomastigote membranes
    • Aparicio LM, Scharfstein J, Lima AP. 2004. Anew cruzipain-mediated pathway of human cell invasion by Trypanosoma cruzi requires trypomastigote membranes. Infect. Immun. 72:5892-902
    • (2004) Infect. Immun. , vol.72 , pp. 5892-5902
    • Aparicio, L.M.1    Scharfstein, J.2    Lima, A.P.3
  • 83
    • 0027222077 scopus 로고
    • Analysis and partial epitope mapping of human T cell responses to Trypanosoma cruzi cysteinyl proteinase
    • Arnholdt AC, Piuvezam MR, Russo DM, Lima AP, Pedrosa RC, et al. 1993. Analysis and partial epitope mapping of human T cell responses to Trypanosoma cruzi cysteinyl proteinase. J. Immunol. 151:3171-79
    • (1993) J. Immunol. , vol.151 , pp. 3171-3179
    • Arnholdt, A.C.1    Piuvezam, M.R.2    Russo, D.M.3    Lima, A.P.4    Pedrosa, R.C.5
  • 84
    • 0032890779 scopus 로고    scopus 로고
    • Chagas' disease and the autoimmunity hypothesis
    • Kierszenbaum F. 1999. Chagas' disease and the autoimmunity hypothesis. Clin. Microbiol. Rev. 12:210-23
    • (1999) Clin. Microbiol. Rev. , vol.12 , pp. 210-223
    • Kierszenbaum, F.1
  • 85
    • 0025760661 scopus 로고
    • Coincidence of tissue antibody and cardiac pathology in mice infected with Trypanosoma cruzi
    • Lozykowski MG, McCormick TS, Rowland EC. 1991. Coincidence of tissue antibody and cardiac pathology in mice infected with Trypanosoma cruzi. Trans. R. Soc. Trop. Med. Hyg. 85:225-26
    • (1991) Trans. R. Soc. Trop. Med. Hyg. , vol.85 , pp. 225-226
    • Lozykowski, M.G.1    McCormick, T.S.2    Rowland, E.C.3
  • 86
    • 0023882215 scopus 로고
    • Antiheart antibody-dependent cytotoxicity in the sera of mice chronically infected with Trypanosoma cruzi
    • Laguens RP, Meckert PC, Chambo JG. 1988. Antiheart antibody-dependent cytotoxicity in the sera of mice chronically infected with Trypanosoma cruzi. Infect. Immun. 56:993-97
    • (1988) Infect. Immun. , vol.56 , pp. 993-997
    • Laguens, R.P.1    Meckert, P.C.2    Chambo, J.G.3
  • 87
    • 0033739239 scopus 로고    scopus 로고
    • Induction of antibodies reactive to cardiac myosin and development of heart alterations in cruzipain-immunized mice and their offspring
    • Giordanengo L, Maldonado C, Rivarola HW, Iosa D, Girones N, et al. 2000. Induction of antibodies reactive to cardiac myosin and development of heart alterations in cruzipain-immunized mice and their offspring. Eur. J. Immunol. 30:3181-89
    • (2000) Eur. J. Immunol. , vol.30 , pp. 3181-3189
    • Giordanengo, L.1    Maldonado, C.2    Rivarola, H.W.3    Iosa, D.4    Girones, N.5
  • 88
    • 0033817862 scopus 로고    scopus 로고
    • Cruzipain induces autoimmune response against skeletal muscle and tissue damage in mice
    • Giordanengo L, Fretes BL, Diaz H, Cano R, Bacile A, et al. 2000. Cruzipain induces autoimmune response against skeletal muscle and tissue damage in mice. Muscle Nerve 23:1407-13
    • (2000) Muscle Nerve , vol.23 , pp. 1407-1413
    • Giordanengo, L.1    Fretes, B.L.2    Diaz, H.3    Cano, R.4    Bacile, A.5
  • 89
    • 9144241840 scopus 로고    scopus 로고
    • Immune response to a major Trypanosoma cruzi antigen, cruzipain, is differentially modulated in C57BL/6 and BALB/c mice
    • Guinazu N, Pellegrini A, Giordanengo L, Aoki MP, Rivarola HW, et al. 2004. Immune response to a major Trypanosoma cruzi antigen, cruzipain, is differentially modulated in C57BL/6 and BALB/c mice. Microbes Infect. 6:1250-58
    • (2004) Microbes Infect. , vol.6 , pp. 1250-1258
    • Guinazu, N.1    Pellegrini, A.2    Giordanengo, L.3    Aoki, M.P.4    Rivarola, H.W.5
  • 90
    • 0036232437 scopus 로고    scopus 로고
    • Cruzipain, a major Trypanosoma cruzi antigen, conditions the host immune response in favor of parasite
    • Giordanengo L, Guinazu N, Stempin C, Fretes R, Cerban F, Gea S. 2002. Cruzipain, a major Trypanosoma cruzi antigen, conditions the host immune response in favor of parasite. Eur. J. Immunol. 32:1003-11
    • (2002) Eur. J. Immunol. , vol.32 , pp. 1003-1011
    • Giordanengo, L.1    Guinazu, N.2    Stempin, C.3    Fretes, R.4    Cerban, F.5    Gea, S.6
  • 91
    • 0037265240 scopus 로고    scopus 로고
    • Alternative activation of macrophages
    • Gordon S. 2003. Alternative activation of macrophages. Nat. Rev. Immunol. 3:23-35
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 23-35
    • Gordon, S.1
  • 92
    • 0033214545 scopus 로고    scopus 로고
    • Th1/Th2-regulated expression of arginase isoforms in murine macrophages and dendritic cells
    • Munder M, Eichmann K, Moran JM, Centeno F, Soler G, Modolell M. 1999. Th1/Th2-regulated expression of arginase isoforms in murine macrophages and dendritic cells. J. Immunol. 163:3771-77
    • (1999) J. Immunol. , vol.163 , pp. 3771-3777
    • Munder, M.1    Eichmann, K.2    Moran, J.M.3    Centeno, F.4    Soler, G.5    Modolell, M.6
  • 93
    • 0032102990 scopus 로고    scopus 로고
    • Alternative metabolic states in murine macrophages reflected by the nitric oxide synthase/arginase balance: Competitive regulation by CD4+ T cells correlates with Th1/Th2 phenotype
    • Munder M, Eichmann K, Modolell M. 1998. Alternative metabolic states in murine macrophages reflected by the nitric oxide synthase/arginase balance: competitive regulation by CD4+ T cells correlates with Th1/Th2 phenotype. J. Immunol. 160:5347-54
    • (1998) J. Immunol. , vol.160 , pp. 5347-5354
    • Munder, M.1    Eichmann, K.2    Modolell, M.3
  • 95
    • 0036826843 scopus 로고    scopus 로고
    • Alternative activation and increase of Trypanosoma cruzi survival in murine macrophages stimulated by cruzipain, a parasite antigen
    • Stempin C, Giordanengo L, Gea S, Cerban F. 2002. Alternative activation and increase of Trypanosoma cruzi survival in murine macrophages stimulated by cruzipain, a parasite antigen. J. Leukoc. Biol. 72:727-34
    • (2002) J. Leukoc. Biol. , vol.72 , pp. 727-734
    • Stempin, C.1    Giordanengo, L.2    Gea, S.3    Cerban, F.4
  • 96
    • 1642554787 scopus 로고    scopus 로고
    • Arginase induction promotes Trypanosoma cruzi intracellular replication in Cruzipain-treated J774 cells through the activation of multiple signaling pathways
    • Stempin CC, Tanos TB, Coso OA, Cerban FM. 2004. Arginase induction promotes Trypanosoma cruzi intracellular replication in Cruzipain-treated J774 cells through the activation of multiple signaling pathways. Eur. J. Immunol. 34:200-9
    • (2004) Eur. J. Immunol. , vol.34 , pp. 200-209
    • Stempin, C.C.1    Tanos, T.B.2    Coso, O.A.3    Cerban, F.M.4
  • 97
    • 0035912807 scopus 로고    scopus 로고
    • L-arginine-dependent suppression of apoptosis in Trypanosoma cruzi: Contribution of the nitric oxide and polyamine pathways
    • Piacenza L, Peluffo G, Radi R. 2001. L-arginine-dependent suppression of apoptosis in Trypanosoma cruzi: contribution of the nitric oxide and polyamine pathways. Prof. Natl. Acad. Sci. USA 98:7301-6
    • (2001) Prof. Natl. Acad. Sci. USA , vol.98 , pp. 7301-7306
    • Piacenza, L.1    Peluffo, G.2    Radi, R.3
  • 98
    • 0029045156 scopus 로고
    • The cysteine protease of Trypanosoma cruzi as a model for antiparasite drug design
    • McKerrow JH, McGrath ME, Engel JC. 1995. The cysteine protease of Trypanosoma cruzi as a model for antiparasite drug design. Parasitol. Today 11:279-82
    • (1995) Parasitol. Today , vol.11 , pp. 279-282
    • McKerrow, J.H.1    McGrath, M.E.2    Engel, J.C.3
  • 99
    • 0032541311 scopus 로고    scopus 로고
    • Cysteine protease inhibitors cure an experimental Trypanosoma cruzi infection
    • Engel JC, Doyle PS, Hsieh I, McKerrow JH. 1998. Cysteine protease inhibitors cure an experimental Trypanosoma cruzi infection. J. Exp. Med. 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
  • 100
    • 0034008682 scopus 로고    scopus 로고
    • Upregulation of the secretory pathway in cysteine protease inhibitor-resistant Trypanosoma cruzi
    • Engel JC, Torres C, Hsieh I, Doyle PS, McKerrow JH, Garcia CT. 2000. Upregulation of the secretory pathway in cysteine protease inhibitor-resistant Trypanosoma cruzi. J. Cell Sci. 113(Pt. 8):1345-S4
    • (2000) J. Cell Sci. , vol.113 , Issue.PART 8
    • Engel, J.C.1    Torres, C.2    Hsieh, I.3    Doyle, P.S.4    McKerrow, J.H.5    Garcia, C.T.6
  • 101
    • 0037016762 scopus 로고    scopus 로고
    • Immediate/early response to Trypanosoma cruzi infection involves minimal modulation of host cell transcription
    • Vaena de Avalos S, Blader IJ, Fisher M, Boothroyd JC, Burleigh BA. 2002. Immediate/early response to Trypanosoma cruzi infection involves minimal modulation of host cell transcription. J. Biol. Chem. 277:639-44
    • (2002) J. Biol. Chem. , vol.277 , pp. 639-644
    • Vaena De Avalos, S.1    Blader, I.J.2    Fisher, M.3    Boothroyd, J.C.4    Burleigh, B.A.5
  • 103
    • 4844229519 scopus 로고    scopus 로고
    • Th2 response polarization during infection with the helminth parasite Schistosoma mansoni
    • Pearce EJ, Kane CM, Sun J, Taylor JJ, McKee AS, Cervi L. 2004. Th2 response polarization during infection with the helminth parasite Schistosoma mansoni. Immunol. Rev. 201:117-26
    • (2004) Immunol. Rev. , vol.201 , pp. 117-126
    • Pearce, E.J.1    Kane, C.M.2    Sun, J.3    Taylor, J.J.4    McKee, A.S.5    Cervi, L.6
  • 104
    • 0035962925 scopus 로고    scopus 로고
    • Modulation of the host immune system by phosphorylcholine-containing glycoproteins secreted by parasitic filarial nematodes
    • Harnett W, Harnett MM. 2001. Modulation of the host immune system by phosphorylcholine-containing glycoproteins secreted by parasitic filarial nematodes. Biochim. Biophys. Acta 1539:7-15
    • (2001) Biochim. Biophys. Acta , vol.1539 , pp. 7-15
    • Harnett, W.1    Harnett, M.M.2
  • 105
    • 0031974840 scopus 로고    scopus 로고
    • The Xid defect imparts susceptibility to experimental murine filariosis-association with a lack of antibody and IL-10 production by B cells in response to phosphorylcholine
    • Al-Qaoud KM, Fleischer B, Hoerauf A. 1998. The Xid defect imparts susceptibility to experimental murine filariosis-association with a lack of antibody and IL-10 production by B cells in response to phosphorylcholine. Int. Immunol. 10:17-25
    • (1998) Int. Immunol. , vol.10 , pp. 17-25
    • Al-Qaoud, K.M.1    Fleischer, B.2    Hoerauf, A.3
  • 106
    • 0031741077 scopus 로고    scopus 로고
    • Filarial nematode parasites secrete a homologue of the human cytokine macrophage migration inhibitory factor
    • Pastrana DV, Raghavan N, FitzGerald P, Eisinger SW, Metz G, et al. 1998. Filarial nematode parasites secrete a homologue of the human cytokine macrophage migration inhibitory factor. Infect. Immun. 66:5955-63
    • (1998) Infect. Immun. , vol.66 , pp. 5955-5963
    • Pastrana, D.V.1    Raghavan, N.2    Fitzgerald, P.3    Eisinger, S.W.4    Metz, G.5
  • 107
    • 0042825912 scopus 로고    scopus 로고
    • Modulation of host immune response by nematode cystatins
    • Hartmann S, Lucias R. 2003. Modulation of host immune response by nematode cystatins. Int. J. Parasitol. 33:1291-302
    • (2003) Int. J. Parasitol. , vol.33 , pp. 1291-1302
    • Hartmann, S.1    Lucias, R.2
  • 108
    • 0030876166 scopus 로고    scopus 로고
    • A filarial cysteine protease inhibitor down regulates T cell proliferation and enhances interleukin 10 production
    • 107a. Hartmann S, Kyewski B, Sonnenburg B, Lucius R. 1997. A filarial cysteine protease inhibitor down regulates T cell proliferation and enhances interleukin 10 production. Eur. J. Immunol. 27:2253-60
    • (1997) Eur. J. Immunol. , vol.27 , pp. 2253-2260
    • Hartmann, S.1    Kyewski, B.2    Sonnenburg, B.3    Lucius, R.4
  • 109
    • 0035281750 scopus 로고    scopus 로고
    • Serine proteinase inhibitors from nematodes and the arms race between host and pathogen
    • Zang X, Maizels RM. 2001. Serine proteinase inhibitors from nematodes and the arms race between host and pathogen. Trends Biochem. Sci. 26:191-97
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 191-197
    • Zang, X.1    Maizels, R.M.2
  • 112
    • 0026804645 scopus 로고
    • Molecular cloning and characterization of onchocystatin, a cysteine proteinase inhibitor of Onchocerca volvulus
    • Lustigman S, Brotman B, Huima T, Prince AM, McKerrow JH. 1992. Molecular cloning and characterization of onchocystatin, a cysteine proteinase inhibitor of Onchocerca volvulus. J. Biol. Chem. 267:17339-46
    • (1992) J. Biol. Chem. , vol.267 , pp. 17339-17346
    • Lustigman, S.1    Brotman, B.2    Huima, T.3    Prince, A.M.4    McKerrow, J.H.5
  • 113
    • 0035916803 scopus 로고    scopus 로고
    • Bm-CPI-2, a cystatin homolog secreted by the filarial parasite Brugia malayi, inhibits class II MHC-restricted antigen processing
    • Manoury B, Gregory WF, Maizels RM, Watts C. 2001. Bm-CPI-2, a cystatin homolog secreted by the filarial parasite Brugia malayi, inhibits class II MHC-restricted antigen processing. Curr. Biol. 11:447-51
    • (2001) Curr. Biol. , vol.11 , pp. 447-451
    • Manoury, B.1    Gregory, W.F.2    Maizels, R.M.3    Watts, C.4
  • 115
    • 0035080521 scopus 로고    scopus 로고
    • Cloning and expression of cystatin, a potent cysteine protease inhibitor from the gut of Haemonchus contortus
    • Newlands GF, Skuce PJ, Knox DP, Smith WD. 2001. Cloning and expression of cystatin, a potent cysteine protease inhibitor from the gut of Haemonchus contortus. Parasitology 122:371-78
    • (2001) Parasitology , vol.122 , pp. 371-378
    • Newlands, G.F.1    Skuce, P.J.2    Knox, D.P.3    Smith, W.D.4
  • 116
    • 0035257859 scopus 로고    scopus 로고
    • Molecular cloning of a cystatin from parasitic intestinal nematode, Nippostrongylus brasiliensis
    • Dainichi T, Maekawa Y, Ishii K, Himeno K. 2001. Molecular cloning of a cystatin from parasitic intestinal nematode, Nippostrongylus brasiliensis. J. Med. Invest. 48:81-87
    • (2001) J. Med. Invest. , vol.48 , pp. 81-87
    • Dainichi, T.1    Maekawa, Y.2    Ishii, K.3    Himeno, K.4
  • 118
    • 0035884985 scopus 로고    scopus 로고
    • Modulation of human T cell responses and macrophage functions by onchocystatin, a secreted protein of the filarial nematode Onchocerca volvulus
    • Schonemeyer A, Lucius R, Sonnenburg B, Brattig N, Sabat R, et al. 2001. Modulation of human T cell responses and macrophage functions by onchocystatin, a secreted protein of the filarial nematode Onchocerca volvulus. J. Immunol. 167:3207-15
    • (2001) J. Immunol. , vol.167 , pp. 3207-3215
    • Schonemeyer, A.1    Lucius, R.2    Sonnenburg, B.3    Brattig, N.4    Sabat, R.5
  • 119
    • 12344299679 scopus 로고    scopus 로고
    • Bm-CPI-2, a cystatin from Brugia malayi nematode parasites, differs from Caenorhabditis elegans cystatins in a specific site mediating inhibition of the antigen-processing enzyme AEP
    • Murray J, Manoury B, Balic A, Watts C, Maizels RM. 2005. Bm-CPI-2, a cystatin from Brugia malayi nematode parasites, differs from Caenorhabditis elegans cystatins in a specific site mediating inhibition of the antigen-processing enzyme AEP. Mol. Biochem. Parasitol. 139:197-203
    • (2005) Mol. Biochem. Parasitol. , vol.139 , pp. 197-203
    • Murray, J.1    Manoury, B.2    Balic, A.3    Watts, C.4    Maizels, R.M.5
  • 120
    • 0033430264 scopus 로고    scopus 로고
    • The role of lysosomal proteinases in MHC class II-mediated antigen processing and presentation
    • Nakagawa TY, Rudensky AY. 1999. The role of lysosomal proteinases in MHC class II-mediated antigen processing and presentation. Immunol. Rev. 172:121-29
    • (1999) Immunol. Rev. , vol.172 , pp. 121-129
    • Nakagawa, T.Y.1    Rudensky, A.Y.2
  • 121
    • 0033696962 scopus 로고    scopus 로고
    • Control of antigen presentation by a single protease cleavage site
    • Antoniou AN, Blackwood SL, Mazzeo D, Watts C. 2000. Control of antigen presentation by a single protease cleavage site. Immunity 12:391-98
    • (2000) Immunity , vol.12 , pp. 391-398
    • Antoniou, A.N.1    Blackwood, S.L.2    Mazzeo, D.3    Watts, C.4
  • 122
    • 0032568806 scopus 로고    scopus 로고
    • Developmental regulation of invariant chain proteolysis controls MHC class II trafficking in mouse dendritic cells
    • Pierre P, Mellman I. 1998. Developmental regulation of invariant chain proteolysis controls MHC class II trafficking in mouse dendritic cells. Cell 93:1135-45
    • (1998) Cell , vol.93 , pp. 1135-1145
    • Pierre, P.1    Mellman, I.2
  • 124
    • 0030021935 scopus 로고    scopus 로고
    • High levels of spontaneous and parasite antigen-driven interleukin-10 production are associated with antigen-specific hyporesponsiveness in human lymphatic filariasis
    • Mahanty S, Mollis SN, Ravichandran M, Abrams JS, Kumaraswami V, et al. 1996. High levels of spontaneous and parasite antigen-driven interleukin-10 production are associated with antigen-specific hyporesponsiveness in human lymphatic filariasis. J. Infect. Dis. 173:769-73
    • (1996) J. Infect. Dis. , vol.173 , pp. 769-773
    • Mahanty, S.1    Mollis, S.N.2    Ravichandran, M.3    Abrams, J.S.4    Kumaraswami, V.5
  • 125
    • 0033051015 scopus 로고    scopus 로고
    • Interleukin-10 and antigen-presenting cells actively suppress Th1 cells in BALB/c mice infected with the filarial parasite Brugia pahangi
    • Osborne J, Devaney E. 1999. Interleukin-10 and antigen-presenting cells actively suppress Th1 cells in BALB/c mice infected with the filarial parasite Brugia pahangi. Infect. Immun. 67:1599-605
    • (1999) Infect. Immun. , vol.67 , pp. 1599-1605
    • Osborne, J.1    Devaney, E.2
  • 127
  • 128
    • 0035823595 scopus 로고    scopus 로고
    • The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature
    • Silverman GA, Bird PI, Carrell RW, Church FC, Coughlin PB, et al. 2001. The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature. J. Biol. Chem. 276:33293-96
    • (2001) J. Biol. Chem. , vol.276 , pp. 33293-33296
    • Silverman, G.A.1    Bird, P.I.2    Carrell, R.W.3    Church, F.C.4    Coughlin, P.B.5
  • 129
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-protease complex shows inhibition by deformation
    • Huntington JA, Read RJ, Carrell RW. 2000. Structure of a serpin-protease complex shows inhibition by deformation. Nature 407:923-26
    • (2000) Nature , vol.407 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 130
    • 0030866891 scopus 로고    scopus 로고
    • Identification of human neutrophil-derived cathepsin G and azurocidin/CAP37 as chemoattractants for mononuclear cells and neutrophils
    • Chertov O, Ueda H, Xu LL, Tani K, Murphy WJ, et al. 1997. Identification of human neutrophil-derived cathepsin G and azurocidin/CAP37 as chemoattractants for mononuclear cells and neutrophils. J. Exp. Med. 186:739-47
    • (1997) J. Exp. Med. , vol.186 , pp. 739-747
    • Chertov, O.1    Ueda, H.2    Xu, L.L.3    Tani, K.4    Murphy, W.J.5
  • 131
    • 0028136620 scopus 로고
    • Interleukin-8 processing by neutrophil elastase, cathepsin G and proteinase-3
    • Padrines M, Wolf M, Walz A, Baggiolini M. 1994. Interleukin-8 processing by neutrophil elastase, cathepsin G and proteinase-3. FEBS Lett. 352:231-35
    • (1994) FEBS Lett. , vol.352 , pp. 231-235
    • Padrines, M.1    Wolf, M.2    Walz, A.3    Baggiolini, M.4
  • 132
    • 0029048266 scopus 로고
    • Cardioprotection by a novel recombinant serine protease inhibitor in myocardial ischemia and reperfusion injury
    • Murohara T, Guo JP, Lefer AM. 1995. Cardioprotection by a novel recombinant serine protease inhibitor in myocardial ischemia and reperfusion injury. J. Pharmacol. Exp. Ther: 274:1246-53
    • (1995) J. Pharmacol. Exp. Ther , vol.274 , pp. 1246-1253
    • Murohara, T.1    Guo, J.P.2    Lefer, A.M.3
  • 134
    • 0026728952 scopus 로고
    • Viral inhibition of inflammation: Cowpox virus encodes an inhibitor of the interleukin-1 beta converting enzyme
    • Ray CA, Black RA, Kronheim SR, Greenstreet TA, Sleath PR, et al. 1992. Viral inhibition of inflammation: cowpox virus encodes an inhibitor of the interleukin-1 beta converting enzyme. Cell 69:597-604
    • (1992) Cell , vol.69 , pp. 597-604
    • Ray, C.A.1    Black, R.A.2    Kronheim, S.R.3    Greenstreet, T.A.4    Sleath, P.R.5
  • 135
    • 0033763829 scopus 로고    scopus 로고
    • Transplant vasculopathy: Viral anti-inflammatory serpin regulation of atherogenesis
    • Lucas A, Dai E, Liu L, Guan H, Nash P, et al. 2000. Transplant vasculopathy: viral anti-inflammatory serpin regulation of atherogenesis. J. Heart Lung Transpl. 19:1029-38
    • (2000) J. Heart Lung Transpl. , vol.19 , pp. 1029-1038
    • Lucas, A.1    Dai, E.2    Liu, L.3    Guan, H.4    Nash, P.5
  • 136
    • 0028948124 scopus 로고
    • Molecular cloning of a serine proteinase inhibitor from Brugia malayi
    • Yenbutr P, Scott AL. 1995. Molecular cloning of a serine proteinase inhibitor from Brugia malayi. Infect. Immun. 63:1745-53
    • (1995) Infect. Immun. , vol.63 , pp. 1745-1753
    • Yenbutr, P.1    Scott, A.L.2
  • 137
    • 0033567081 scopus 로고    scopus 로고
    • A novel serpin expressed by blood-borne microfilariae of the parasitic nematode Brugia malayi inhibits human neutrophil serine proteinases
    • Zang X, Yazdanbakhsh M, Jiang H, Kanost MR, Maizels RM. 1999. A novel serpin expressed by blood-borne microfilariae of the parasitic nematode Brugia malayi inhibits human neutrophil serine proteinases. Blood 94:1418-28
    • (1999) Blood , vol.94 , pp. 1418-1428
    • Zang, X.1    Yazdanbakhsh, M.2    Jiang, H.3    Kanost, M.R.4    Maizels, R.M.5
  • 138
    • 0037845183 scopus 로고    scopus 로고
    • BmSPN2, a serpin secreted by the filarial nematode Brugia malayi, does not inhibit human neutrophil proteinases but plays a noninhibitory role
    • Stanley P, Stein PE. 2003. BmSPN2, a serpin secreted by the filarial nematode Brugia malayi, does not inhibit human neutrophil proteinases but plays a noninhibitory role. Biochemistry 42:6241-48
    • (2003) Biochemistry , vol.42 , pp. 6241-6248
    • Stanley, P.1    Stein, P.E.2
  • 139
    • 0024430428 scopus 로고
    • Ovalbumin and angiotensinogen lack serpin S-R conformational change
    • Stein PE, Tewkesbury DA, Carrell RW. 1989. Ovalbumin and angiotensinogen lack serpin S-R conformational change. Biochem. J. 262:103-7
    • (1989) Biochem. J. , vol.262 , pp. 103-107
    • Stein, P.E.1    Tewkesbury, D.A.2    Carrell, R.W.3
  • 140
    • 0035966068 scopus 로고    scopus 로고
    • The molecular interactions of heat shock protein 47 (Hsp47) and their implications for collagen biosynthesis
    • Dafforn TR, Della M, Miller AD. 2001. The molecular interactions of heat shock protein 47 (Hsp47) and their implications for collagen biosynthesis. J. Biol. Chem. 276:49310-19
    • (2001) J. Biol. Chem. , vol.276 , pp. 49310-49319
    • Dafforn, T.R.1    Della, M.2    Miller, A.D.3
  • 141
    • 0028241404 scopus 로고
    • Schistosoma mansoni: Isolation and characterization of Smpi56, a novel serine protease inhibitor
    • Ghendler Y, Arnon R, Fishelson Z. 1994. Schistosoma mansoni: isolation and characterization of Smpi56, a novel serine protease inhibitor. Exp. Parasitol. 78:121-31
    • (1994) Exp. Parasitol. , vol.78 , pp. 121-131
    • Ghendler, Y.1    Arnon, R.2    Fishelson, Z.3
  • 142
  • 143
    • 0028089035 scopus 로고
    • Characterization of a native and recombinant Schistosoma haematobium serine protease inhibitor gene product
    • Blanton RE, Licate LS, Aman RA. 1994. Characterization of a native and recombinant Schistosoma haematobium serine protease inhibitor gene product. Mol. Biochem. Parasitol. 63:1-11
    • (1994) Mol. Biochem. Parasitol. , vol.63 , pp. 1-11
    • Blanton, R.E.1    Licate, L.S.2    Aman, R.A.3
  • 144
    • 13044256381 scopus 로고    scopus 로고
    • Purification and crystallization of a novel membrane-anchored protein: The Schistosoma haematobium serpin
    • Huang W, Haas TA, Biesterfeldt J, Mankawsky L, Blanton RE, Lee X. 1999. Purification and crystallization of a novel membrane-anchored protein: the Schistosoma haematobium serpin. Acta Crystallogr. D 55(Pt. 1):350-52
    • (1999) Acta Crystallogr. D , vol.55 , Issue.PART 1 , pp. 350-352
    • Huang, W.1    Haas, T.A.2    Biesterfeldt, J.3    Mankawsky, L.4    Blanton, R.E.5    Lee, X.6
  • 145
    • 0345737016 scopus 로고    scopus 로고
    • Killing of schistosomes by elastase and hydrogen peroxide: Implications for leukocyte-mediated schistosome killing
    • Freudenstein-Dan A, Gold D, Fishelson Z. 2003. Killing of schistosomes by elastase and hydrogen peroxide: implications for leukocyte-mediated schistosome killing. J. Parasitol. 89:1129-35
    • (2003) J. Parasitol. , vol.89 , pp. 1129-1135
    • Freudenstein-Dan, A.1    Gold, D.2    Fishelson, Z.3
  • 146
    • 0014407496 scopus 로고
    • The amino acid sequence of a trypsin inhibitor isolated from ascaris (Ascaris lumbricoides var. suum)
    • Fraefel W, Acher R. 1968. The amino acid sequence of a trypsin inhibitor isolated from ascaris (Ascaris lumbricoides var. suum). Biochim. Biophys. Acta 154:615-17
    • (1968) Biochim. Biophys. Acta , vol.154 , pp. 615-617
    • Fraefel, W.1    Acher, R.2
  • 147
    • 0021453880 scopus 로고
    • The isoinhibitors of chymotrypsin/elastase from Ascaris lumbricoides: The primary structure
    • Babin DR, Peanasky RJ, Goos SM. 1984. The isoinhibitors of chymotrypsin/elastase from Ascaris lumbricoides: the primary structure. Arch. Biochem. Biophys. 232:143-61
    • (1984) Arch. Biochem. Biophys. , vol.232 , pp. 143-161
    • Babin, D.R.1    Peanasky, R.J.2    Goos, S.M.3
  • 148
    • 0021459593 scopus 로고
    • The isoinhibitors of chymotrypsin/elastase from Ascaris lumbricoides: Isolation by affinity chromatography and association with the enzymes
    • Peanasky RJ, Bentz Y, Paulson B, Graham DL, Babin DR. 1984. The isoinhibitors of chymotrypsin/elastase from Ascaris lumbricoides: isolation by affinity chromatography and association with the enzymes. Arch. Biochem. Biophys. 232:127-34
    • (1984) Arch. Biochem. Biophys. , vol.232 , pp. 127-134
    • Peanasky, R.J.1    Bentz, Y.2    Paulson, B.3    Graham, D.L.4    Babin, D.R.5
  • 149
    • 0028773904 scopus 로고
    • High-resolution structure of Ascaris trypsin inhibitor in solution: Direct evidence for a pH-induced conformational transition in the reactive site
    • Grasberger BL, Clore GM, Gronenborn AM. 1994. High-resolution structure of Ascaris trypsin inhibitor in solution: direct evidence for a pH-induced conformational transition in the reactive site. Structure 2:669-78
    • (1994) Structure , vol.2 , pp. 669-678
    • Grasberger, B.L.1    Clore, G.M.2    Gronenborn, A.M.3
  • 150
    • 0028773905 scopus 로고
    • The molecular structure of the complex Ascaris chymotrypsin/elastase inhibitor with porcine elastase
    • Huang K, Streynadka NC, Bernard VD, Peanasky RJ, James MN. 1994. The molecular structure of the complex Ascaris chymotrypsin/elastase inhibitor with porcine elastase. Structure 2:679-89
    • (1994) Structure , vol.2 , pp. 679-689
    • Huang, K.1    Streynadka, N.C.2    Bernard, V.D.3    Peanasky, R.J.4    James, M.N.5
  • 151
    • 0033569932 scopus 로고    scopus 로고
    • Inherent flexibility in a potent inhibitor of blood coagulation, recombinant nematode anticoagulant protein c2
    • Duggan BM, Dyson HJ, Wright PE. 1999. Inherent flexibility in a potent inhibitor of blood coagulation, recombinant nematode anticoagulant protein c2. Eur. J. Biochem. 265:539-48
    • (1999) Eur. J. Biochem. , vol.265 , pp. 539-548
    • Duggan, B.M.1    Dyson, H.J.2    Wright, P.E.3
  • 152
    • 0021930005 scopus 로고
    • Ascaris suum: Localization by immunochemical and fluorescent probes of host proteases and parasite proteinase inhibitors in cross-sections
    • Martzen MR, Geise GL, Hogan BJ, Peanasky RJ. 1985. Ascaris suum: localization by immunochemical and fluorescent probes of host proteases and parasite proteinase inhibitors in cross-sections. Exp. Parasitol. 60:139-49
    • (1985) Exp. Parasitol. , vol.60 , pp. 139-149
    • Martzen, M.R.1    Geise, G.L.2    Hogan, B.J.3    Peanasky, R.J.4
  • 153
    • 0031849122 scopus 로고    scopus 로고
    • Anisakis simplex: Mutational bursts in the reactive site centers of serine protease inhibitors from an ascarid nematode
    • Lu CC, Nguyen T, Morris S, Hill D, Sakanari JA. 1998. Anisakis simplex: mutational bursts in the reactive site centers of serine protease inhibitors from an ascarid nematode. Exp. Parasitol. 89:257-61
    • (1998) Exp. Parasitol. , vol.89 , pp. 257-261
    • Lu, C.C.1    Nguyen, T.2    Morris, S.3    Hill, D.4    Sakanari, J.A.5
  • 154
    • 0034088301 scopus 로고    scopus 로고
    • Trichuris suis: A secretory chymotrypsin/elastase inhibitor with potential as an immunomodulator
    • Rhoads ML, Fetterer RH, Hill DE, Urban JF Jr. 2000. Trichuris suis: a secretory chymotrypsin/elastase inhibitor with potential as an immunomodulator. Exp. Parasitol. 95:36-44
    • (2000) Exp. Parasitol. , vol.95 , pp. 36-44
    • Rhoads, M.L.1    Fetterer, R.H.2    Hill, D.E.3    Urban Jr., J.F.4
  • 155
    • 0005945807 scopus 로고    scopus 로고
    • Primary structure and properties of the cathepsin G/chymotrypsin inhibitor from the larval hemolymph of Apis mellifera
    • Bania J, Stachowiak D, Polanowski A. 1999. Primary structure and properties of the cathepsin G/chymotrypsin inhibitor from the larval hemolymph of Apis mellifera. Eur. J. Biochem. 262:680-87
    • (1999) Eur. J. Biochem. , vol.262 , pp. 680-687
    • Bania, J.1    Stachowiak, D.2    Polanowski, A.3
  • 156
    • 0030063710 scopus 로고    scopus 로고
    • BSTI, a trypsin inhibitor from skin secretions of Bombina bombina related to protease inhibitors of nematodes
    • Mignogna G, Pascarella S, Wechselberger C, Hinterleitner C, Mollay C, et al. 1996. BSTI, a trypsin inhibitor from skin secretions of Bombina bombina related to protease inhibitors of nematodes. Protein Sci. 5:357-62
    • (1996) Protein Sci. , vol.5 , pp. 357-362
    • Mignogna, G.1    Pascarella, S.2    Wechselberger, C.3    Hinterleitner, C.4    Mollay, C.5
  • 157
    • 0036873001 scopus 로고    scopus 로고
    • Inhibition of factor VIIa/tissue factor with nematode anticoagulant protein c2: From unique mechanism to a promising new clinical anticoagulant
    • Vlasuk GP, Rote WE. 2002. Inhibition of factor VIIa/tissue factor with nematode anticoagulant protein c2: from unique mechanism to a promising new clinical anticoagulant. Trends Cardiovasc. Med. 12:325-31
    • (2002) Trends Cardiovasc. Med. , vol.12 , pp. 325-331
    • Vlasuk, G.P.1    Rote, W.E.2
  • 158
    • 0000386699 scopus 로고
    • The presence of a substance inhibiting the coagulation of blood in anchylostoma
    • Loeb L, Smith AJ. 1904. The presence of a substance inhibiting the coagulation of blood in anchylostoma. Proc. Natl. Acad. Sci. USA 7:173-78
    • (1904) Proc. Natl. Acad. Sci. USA , vol.7 , pp. 173-178
    • Loeb, L.1    Smith, A.J.2
  • 159
    • 0027155257 scopus 로고
    • Ancylostoma factor Xa inhibitor: Partial purification and its identification as a major hookworm-derived anticoagulant in vitro
    • Cappello M, Clyne LP, McPhedran P, Hotez PJ. 1993. Ancylostoma factor Xa inhibitor: partial purification and its identification as a major hookworm-derived anticoagulant in vitro. J. Infect. Dis. 167:1474-77
    • (1993) J. Infect. Dis. , vol.167 , pp. 1474-1477
    • Cappello, M.1    Clyne, L.P.2    McPhedran, P.3    Hotez, P.J.4
  • 160
    • 0029014045 scopus 로고
    • Ancylostoma caninum anticoagulant peptide: A hookworm-derived inhibitor of human coagulation factor Xa
    • Cappello M, Vlasuk GP, Bergum PW, Huang S, Hotez PJ. 1995. Ancylostoma caninum anticoagulant peptide: a hookworm-derived inhibitor of human coagulation factor Xa. Proc. Natl. Acad. Sci. USA 92:6152-56
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6152-6156
    • Cappello, M.1    Vlasuk, G.P.2    Bergum, P.W.3    Huang, S.4    Hotez, P.J.5
  • 162
    • 0032549024 scopus 로고    scopus 로고
    • Regulation of extrinsic pathway factor Xa formation by tissue factor pathway inhibitor
    • Baugh RJ, Broze GJ Jr, Krishnaswamy S. 1998. Regulation of extrinsic pathway factor Xa formation by tissue factor pathway inhibitor. J. Biol. Chem. 273:4378-86
    • (1998) J. Biol. Chem. , vol.273 , pp. 4378-4386
    • Baugh, R.J.1    Broze Jr., G.J.2    Krishnaswamy, S.3
  • 163
    • 0348048783 scopus 로고    scopus 로고
    • Anticoagulant peptides from Ancylostoma caninum are immunologically distinct and localize to separate structures within the adult hookworm
    • Mieszczanek J, Harrison LM, Vlasuk GP, Cappello M. 2004. Anticoagulant peptides from Ancylostoma caninum are immunologically distinct and localize to separate structures within the adult hookworm. Mol. Biochem. Parasitol. 133:319-23
    • (2004) Mol. Biochem. Parasitol. , vol.133 , pp. 319-323
    • Mieszczanek, J.1    Harrison, L.M.2    Vlasuk, G.P.3    Cappello, M.4
  • 164
    • 3342988385 scopus 로고    scopus 로고
    • Ancylostoma ceylanicum anticoagulant peptide-1: Role of the predicted reactive site amino acid in mediating inhibition of coagulation factors Xa and VIIa
    • Mieszczanek J, Harrison LM, Cappello M. 2004. Ancylostoma ceylanicum anticoagulant peptide-1: role of the predicted reactive site amino acid in mediating inhibition of coagulation factors Xa and VIIa. Mol. Biochem. Parasitol. 137:151-59
    • (2004) Mol. Biochem. Parasitol. , vol.137 , pp. 151-159
    • Mieszczanek, J.1    Harrison, L.M.2    Cappello, M.3
  • 165
    • 0037155248 scopus 로고    scopus 로고
    • Molecular characterization of Ancylostoma inhibitors of coagulation factor Xa. Hookworm anticoagulant activity in vitro predicts parasite bloodfeeding in vivo
    • Harrison LM, Nerlinger A, Bungiro RD, Cordova JL, Kuzmic P, Cappello M. 2002. Molecular characterization of Ancylostoma inhibitors of coagulation factor Xa. Hookworm anticoagulant activity in vitro predicts parasite bloodfeeding in vivo. J. Biol. Chem. 277:6223-39
    • (2002) J. Biol. Chem. , vol.277 , pp. 6223-6239
    • Harrison, L.M.1    Nerlinger, A.2    Bungiro, R.D.3    Cordova, J.L.4    Kuzmic, P.5    Cappello, M.6
  • 166
    • 0019156482 scopus 로고
    • Pathogenicity of hookworms. The significance of population regression for the pathogenicity of hookworms
    • Rep BH. 1980. Pathogenicity of hookworms. The significance of population regression for the pathogenicity of hookworms. Trop. Geogr. Med. 32:251-55
    • (1980) Trop. Geogr. Med. , vol.32 , pp. 251-255
    • Rep, B.H.1
  • 167
    • 0242438144 scopus 로고    scopus 로고
    • Pharmacokinetics and anticoagulant properties of the factor VIIa-tissue factor inhibitor recombinant Nematode Anticoagulant Protein c2 following subcutaneous administration in man. Dependence on the stoichiometric binding to circulating factor X
    • Vlasuk GP, Bradbury A, Lopez-Kinninger L, Colon S, Bergum PW, et al. 2003. Pharmacokinetics and anticoagulant properties of the factor VIIa-tissue factor inhibitor recombinant Nematode Anticoagulant Protein c2 following subcutaneous administration in man. Dependence on the stoichiometric binding to circulating factor X. Thromb. Haemost. 90:803-12
    • (2003) Thromb. Haemost. , vol.90 , pp. 803-812
    • Vlasuk, G.P.1    Bradbury, A.2    Lopez-Kinninger, L.3    Colon, S.4    Bergum, P.W.5
  • 168
    • 0035800075 scopus 로고    scopus 로고
    • Dose-response study of recombinant factor VIIa/tissue factor inhibitor recombinant nematode anticoagulant protein c2 in prevention of postoperative venous thromboembolism in patients undergoing total knee replacement
    • Lee A, Agnelli G, Buller H, Ginsberg J, Heit J, et al. 2001. Dose-response study of recombinant factor VIIa/tissue factor inhibitor recombinant nematode anticoagulant protein c2 in prevention of postoperative venous thromboembolism in patients undergoing total knee replacement. Circulation 104:74-78
    • (2001) Circulation , vol.104 , pp. 74-78
    • Lee, A.1    Agnelli, G.2    Buller, H.3    Ginsberg, J.4    Heit, J.5
  • 170
    • 0037215047 scopus 로고    scopus 로고
    • Phylogeny of gregarines (Apicomplexa) as inferred from small-subunit rDNA and beta-tubulin
    • Leander BS, Clopton RE, Keeling PJ. 2003. Phylogeny of gregarines (Apicomplexa) as inferred from small-subunit rDNA and beta-tubulin. Int. J. Syst. Evol. Microbiol. 53:345-54
    • (2003) Int. J. Syst. Evol. Microbiol. , vol.53 , pp. 345-354
    • Leander, B.S.1    Clopton, R.E.2    Keeling, P.J.3
  • 171
    • 1842482437 scopus 로고    scopus 로고
    • Intracellular parasite invasion strategies
    • Sibley LD. 2004. Intracellular parasite invasion strategies. Science 304:248-53
    • (2004) Science , vol.304 , pp. 248-253
    • Sibley, L.D.1
  • 172
    • 1642396715 scopus 로고    scopus 로고
    • Toxoplasma as a novel system for motility
    • Soldati D, Meissner M. 2004. Toxoplasma as a novel system for motility. Curr. Opin. Cell Biol. 16:32-40
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 32-40
    • Soldati, D.1    Meissner, M.2
  • 173
    • 8844228268 scopus 로고    scopus 로고
    • Location, location, location: Trafficking and function of secreted proteases of toxoplasma and Plasmodium
    • Binder EM, Kim K. 2004. Location, location, location: trafficking and function of secreted proteases of toxoplasma and Plasmodium. Traffic 5:914-24
    • (2004) Traffic , vol.5 , pp. 914-924
    • Binder, E.M.1    Kim, K.2
  • 174
    • 1542285447 scopus 로고    scopus 로고
    • Toxoplasma gondii: The model apicomplexan
    • Kim K, Weiss LM. 2004. Toxoplasma gondii: the model apicomplexan. Int. J. Parasitol. 34:423-32
    • (2004) Int. J. Parasitol. , vol.34 , pp. 423-432
    • Kim, K.1    Weiss, L.M.2
  • 175
    • 4544238896 scopus 로고    scopus 로고
    • Proteases in host cell invasion by the malaria parasite
    • Blackman MJ. 2004. Proteases in host cell invasion by the malaria parasite. Cell. Microbiol. 6:893-903
    • (2004) Cell. Microbiol. , vol.6 , pp. 893-903
    • Blackman, M.J.1
  • 176
    • 0037007235 scopus 로고    scopus 로고
    • Intramembrane cleavage of microneme proteins at the surface of the apicomplexan parasite Toxoplasma gondii
    • Opitz C, Di Cristina M, Reiss M, Ruppert T, Crisanti A, Soldati D. 2002. Intramembrane cleavage of microneme proteins at the surface of the apicomplexan parasite Toxoplasma gondii. EMBO J. 21:1577-85
    • (2002) EMBO J. , vol.21 , pp. 1577-1585
    • Opitz, C.1    Di Cristina, M.2    Reiss, M.3    Ruppert, T.4    Crisanti, A.5    Soldati, D.6
  • 177
    • 0034640516 scopus 로고    scopus 로고
    • The Toxoplasma adhesive protein MIC2 is proteolytically processed at multiple sites by two parasite-derived proteases
    • Carruthers VB, Sherman GD, Sibley LD. 2000. The Toxoplasma adhesive protein MIC2 is proteolytically processed at multiple sites by two parasite-derived proteases. J. Biol. Chem. 275:14346-53
    • (2000) J. Biol. Chem. , vol.275 , pp. 14346-14353
    • Carruthers, V.B.1    Sherman, G.D.2    Sibley, L.D.3
  • 178
    • 0035976961 scopus 로고    scopus 로고
    • A conserved subtilisin-like protein TgSUB1 in microneme organelles of Toxoplasma gondii
    • Miller SA, Binder EM, Blackman MJ, Carruthers VB, Kim K. 2001. A conserved subtilisin-like protein TgSUB1 in microneme organelles of Toxoplasma gondii. J. Biol. Chem. 276:45341-48
    • (2001) J. Biol. Chem. , vol.276 , pp. 45341-45348
    • Miller, S.A.1    Binder, E.M.2    Blackman, M.J.3    Carruthers, V.B.4    Kim, K.5
  • 180
    • 1642513730 scopus 로고    scopus 로고
    • Gene targeting demonstrates that the Plasmodium berghei subtilisin PbSUB2 is essential for red cell invasion and reveals spontaneous genetic recombination events
    • Uzureau P, Barale JC, Janse CJ, Waters AP, Breton CB. 2004. Gene targeting demonstrates that the Plasmodium berghei subtilisin PbSUB2 is essential for red cell invasion and reveals spontaneous genetic recombination events. Cell. Microbiol. 6:65-78
    • (2004) Cell. Microbiol. , vol.6 , pp. 65-78
    • Uzureau, P.1    Barale, J.C.2    Janse, C.J.3    Waters, A.P.4    Breton, C.B.5
  • 181
    • 0028281596 scopus 로고
    • What is the function of MSP-1 on the malaria merzoite?
    • Holder AA, Blackman MJ. 1994. What is the function of MSP-1 on the malaria merzoite? Parasitol. Today 10:182-84
    • (1994) Parasitol. Today , vol.10 , pp. 182-184
    • Holder, A.A.1    Blackman, M.J.2
  • 183
    • 0033186127 scopus 로고    scopus 로고
    • Molecular mechanisms of malaria sporozoite motility and invasion of host cells
    • Sultan AA. 1999. Molecular mechanisms of malaria sporozoite motility and invasion of host cells. Int. Microbiol. 2:155-60
    • (1999) Int. Microbiol. , vol.2 , pp. 155-160
    • Sultan, A.A.1
  • 185
    • 4143127652 scopus 로고    scopus 로고
    • Host cell invasion by the apicomplexans: The significance of microneme protein proteolysis
    • Dowse T, Soldati D. 2004. Host cell invasion by the apicomplexans: the significance of microneme protein proteolysis. Curr. Opin. Microbiol. 7:388-96
    • (2004) Curr. Opin. Microbiol. , vol.7 , pp. 388-396
    • Dowse, T.1    Soldati, D.2
  • 186
    • 0036935112 scopus 로고    scopus 로고
    • Characterization of Neospora caninum protease, NcSUB1 (NC-p65), with rabbit anti-N54
    • Louie K, Nordhausen R, Robinson TW, Barr BC, Conrad PA. 2002. Characterization of Neospora caninum protease, NcSUB1 (NC-p65), with rabbit anti-N54. J. Parasitol. 88:1113-19
    • (2002) J. Parasitol. , vol.88 , pp. 1113-1119
    • Louie, K.1    Nordhausen, R.2    Robinson, T.W.3    Barr, B.C.4    Conrad, P.A.5
  • 187
    • 0025182460 scopus 로고
    • Reduction in cell entry of Eimeria tenella (Coccidia) sporozoites by protease inhibitors, and partial characterization of proteolytic activity associated with intact sporozoites and merozoites
    • Fuller AL, McDougald LR. 1990. Reduction in cell entry of Eimeria tenella (Coccidia) sporozoites by protease inhibitors, and partial characterization of proteolytic activity associated with intact sporozoites and merozoites. J. Parasitol. 76:464-67
    • (1990) J. Parasitol. , vol.76 , pp. 464-467
    • Fuller, A.L.1    McDougald, L.R.2
  • 188
    • 2242432614 scopus 로고    scopus 로고
    • A role for the protease falcipain 1 in host cell invasion by the human malaria parasite
    • Greenbaum DC, Baruch A, Grainger M, Bozdech Z, Medzihradszky KF, et al. 2002. A role for the protease falcipain 1 in host cell invasion by the human malaria parasite. Science 298:2002-6
    • (2002) Science , vol.298 , pp. 2002-2006
    • Greenbaum, D.C.1    Baruch, A.2    Grainger, M.3    Bozdech, Z.4    Medzihradszky, K.F.5
  • 189
    • 3142626622 scopus 로고    scopus 로고
    • Plasmodium falciparum cysteine protease, falcipain 1, reduces oocyst production, not erythrocytic stage growth
    • Eski S, Czesny B, Greenbaum DC, Boygo M, Williamson KC. 2004. argeted disruption of Plasmodium falciparum cysteine protease, falcipain 1, reduces oocyst production, not erythrocytic stage growth. Mol. Microbiol. 53:243-50
    • (2004) Mol. Microbiol. , vol.53 , pp. 243-250
    • Eski, S.1    Czesny, B.2    Greenbaum, D.C.3    Boygo, M.4    Williamson, K.C.5
  • 190
    • 0024315151 scopus 로고
    • Purification and identification of a neutral endopeptidase in Plasmodium falciparum schizonts and merozoites
    • Grellier P, Picard I, Bernard F, Mayer R, Heidrich HG, et al. 1989. Purification and identification of a neutral endopeptidase in Plasmodium falciparum schizonts and merozoites. Parasitol. Res. 75:455-60
    • (1989) Parasitol. Res. , vol.75 , pp. 455-460
    • Grellier, P.1    Picard, I.2    Bernard, F.3    Mayer, R.4    Heidrich, H.G.5
  • 191
    • 0038267453 scopus 로고    scopus 로고
    • A single malaria merozoite serine protease mediates shedding of multiple surface proteins by juxtamembrane cleavage
    • Howell SA, Well I, Fleck SL, Kettleborough C, Collins CR, Blackman MJ. 2003. A single malaria merozoite serine protease mediates shedding of multiple surface proteins by juxtamembrane cleavage. J. Biol. Chem. 278:23890-98
    • (2003) J. Biol. Chem. , vol.278 , pp. 23890-23898
    • Howell, S.A.1    Well, I.2    Fleck, S.L.3    Kettleborough, C.4    Collins, C.R.5    Blackman, M.J.6
  • 193
    • 0025882218 scopus 로고
    • The entry of Theileria parva sporozoites into bovine lymphocytes: Evidence for MHC class I involvement
    • Shaw MK, Tilney LG, Musoke AJ. 1991. The entry of Theileria parva sporozoites into bovine lymphocytes: evidence for MHC class I involvement. J. CellBiol. 113:87-101
    • (1991) J. CellBiol. , vol.113 , pp. 87-101
    • Shaw, M.K.1    Tilney, L.G.2    Musoke, A.J.3
  • 194
    • 0027933912 scopus 로고
    • Cytolysins from intracellular pathogens
    • Andrews NW, Portnoy DA. 1994. Cytolysins from intracellular pathogens. Trends Microbiol. 2:261-63
    • (1994) Trends Microbiol. , vol.2 , pp. 261-263
    • Andrews, N.W.1    Portnoy, D.A.2
  • 195
    • 33645740667 scopus 로고    scopus 로고
    • note
    • Deleted in proof
  • 196
    • 0036851878 scopus 로고    scopus 로고
    • Migration through host cells activates Plasmodium sporozoites for infection
    • Mota MM, Hafalla JC, Rodriguez A. 2002. Migration through host cells activates Plasmodium sporozoites for infection. Nat. Med. 8:1318-22
    • (2002) Nat. Med. , vol.8 , pp. 1318-1322
    • Mota, M.M.1    Hafalla, J.C.2    Rodriguez, A.3
  • 197
    • 12344299732 scopus 로고    scopus 로고
    • The Plasmodium circumsporozoite protein is proteolytically processed during cell invasion
    • Coppi A, Pinzon-Ortiz C, Hutter C, Sinnis P. 2005. The Plasmodium circumsporozoite protein is proteolytically processed during cell invasion. J. Exp. Med. 201:27-33
    • (2005) J. Exp. Med. , vol.201 , pp. 27-33
    • Coppi, A.1    Pinzon-Ortiz, C.2    Hutter, C.3    Sinnis, P.4
  • 198
    • 0020568103 scopus 로고
    • Plasmodium knowlesi: Studies on invasion of rhesus erythrocytes by merozoites in the presence of protease inhibitors
    • Hadley T, Aikawa M, Miller LH. 1983. Plasmodium knowlesi: studies on invasion of rhesus erythrocytes by merozoites in the presence of protease inhibitors. Exp. Parasitol. 55:306-11
    • (1983) Exp. Parasitol. , vol.55 , pp. 306-311
    • Hadley, T.1    Aikawa, M.2    Miller, L.H.3
  • 199
    • 0022613309 scopus 로고
    • Plasmodium falciparum antigens synthesized by schizonts and stabilized at the merozoite surface by antibodies when schizonts mature in the presence of growth inhibitory immune serum
    • Lyon JA, Haynes JD, Diggs CL, Chulay JD, Pratt-Rossiter JM. 1986. Plasmodium falciparum antigens synthesized by schizonts and stabilized at the merozoite surface by antibodies when schizonts mature in the presence of growth inhibitory immune serum. J. Immunol. 136:2252-58
    • (1986) J. Immunol. , vol.136 , pp. 2252-2258
    • Lyon, J.A.1    Haynes, J.D.2    Diggs, C.L.3    Chulay, J.D.4    Pratt-Rossiter, J.M.5
  • 200
    • 0035793051 scopus 로고    scopus 로고
    • Malaria parasite exit from the host erythrocyte: A two-step process requiring extraerythrocytic proteolysis
    • Salmon BL, Oksman A, Goldberg DE. 2001. Malaria parasite exit from the host erythrocyte: a two-step process requiring extraerythrocytic proteolysis. Proc. Natl. Acad. Sci. USA 98:271-76
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 271-276
    • Salmon, B.L.1    Oksman, A.2    Goldberg, D.E.3
  • 201
    • 0141509925 scopus 로고    scopus 로고
    • Selective inhibition of a two-step egress of malaria parasites from the host erythrocyte
    • Wickham ME, Culvenor JG, Cowman AF. 2003. Selective inhibition of a two-step egress of malaria parasites from the host erythrocyte. J. Biol. Chem. 278:37658-63
    • (2003) J. Biol. Chem. , vol.278 , pp. 37658-37663
    • Wickham, M.E.1    Culvenor, J.G.2    Cowman, A.F.3
  • 202
    • 6344225452 scopus 로고    scopus 로고
    • The serine repeat antigen (SERA) gene family phylogeny in Plasmodium: The impact of GC content and reconciliation of gene and species trees
    • Bourgon R, Delorenzi M, Sargeant T, Hodder AN, Crabb BS, Speed TP. 2004. The serine repeat antigen (SERA) gene family phylogeny in Plasmodium: the impact of GC content and reconciliation of gene and species trees. Mol. Biol. Evol. 21:2161-71
    • (2004) Mol. Biol. Evol. , vol.21 , pp. 2161-2171
    • Bourgon, R.1    Delorenzi, M.2    Sargeant, T.3    Hodder, A.N.4    Crabb, B.S.5    Speed, T.P.6
  • 203
    • 0037033116 scopus 로고    scopus 로고
    • A subset of Plasmodium falciparum SERA genes are expressed and appear to play an important role in the erythrocytic cycle
    • Miller SK, Good RT, Drew DR, Delorenzi M, Sanders PR, et al. 2002. A subset of Plasmodium falciparum SERA genes are expressed and appear to play an important role in the erythrocytic cycle. J. Biol. Chem. 277:47524-32
    • (2002) J. Biol. Chem. , vol.277 , pp. 47524-47532
    • Miller, S.K.1    Good, R.T.2    Drew, D.R.3    Delorenzi, M.4    Sanders, P.R.5
  • 204
    • 0036682503 scopus 로고    scopus 로고
    • Plasmodium falciparum cysteine protease falcipain-2 cleaves erythrocyte membrane skeletal proteins at late stages of parasite development
    • Hanspal M, Dua M, Takakuwa Y, Chishti AH, Mizuno A. 2002. Plasmodium falciparum cysteine protease falcipain-2 cleaves erythrocyte membrane skeletal proteins at late stages of parasite development. Blood 100:1048-54
    • (2002) Blood , vol.100 , pp. 1048-1054
    • Hanspal, M.1    Dua, M.2    Takakuwa, Y.3    Chishti, A.H.4    Mizuno, A.5
  • 205
    • 0043031443 scopus 로고    scopus 로고
    • Ankyrin peptide blocks falcipain-2-mediated malaria parasite release from red blood cells
    • Dhawan S, Dua M, Chishti AH, Hanspal M. 2003. Ankyrin peptide blocks falcipain-2-mediated malaria parasite release from red blood cells. J. Biol. Chem. 278:30180-86
    • (2003) J. Biol. Chem. , vol.278 , pp. 30180-30186
    • Dhawan, S.1    Dua, M.2    Chishti, A.H.3    Hanspal, M.4
  • 207
    • 10744231797 scopus 로고    scopus 로고
    • Enzymic, phylogenetic, and structural characterization of the unusual papain-like protease domain of Plasmodium falciparum SERA5 J
    • Hodder AN, Drew DR, Epa VC, Delorenzi M, Bourgon R, et al. 2003. Enzymic, phylogenetic, and structural characterization of the unusual papain-like protease domain of Plasmodium falciparum SERA5 J. Biol. Chem. 278:48169-77
    • (2003) Biol. Chem. , vol.278 , pp. 48169-48177
    • Hodder, A.N.1    Drew, D.R.2    Epa, V.C.3    Delorenzi, M.4    Bourgon, R.5
  • 208
    • 0033553410 scopus 로고    scopus 로고
    • Plasmepsin II, an acidic hemoglobinase from the Plasmodium falciparum food vacuole, is active at neutral pH on the host erythrocyte membrane skeleton
    • Le Bonniec S, Deregnaucourt C, Redeker V, Banerjee R, Grellier P, et al. 1999. Plasmepsin II, an acidic hemoglobinase from the Plasmodium falciparum food vacuole, is active at neutral pH on the host erythrocyte membrane skeleton. J. Biol. Chem. 274:14218-23
    • (1999) J. Biol. Chem. , vol.274 , pp. 14218-14223
    • Le Bonniec, S.1    Deregnaucourt, C.2    Redeker, V.3    Banerjee, R.4    Grellier, P.5


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