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Volumn 51, Issue 11, 2008, Pages 3116-3123

A prodomain peptide of Plasmodium falciparum cysteine protease (falcipain-2) inhibits malaria parasite development

Author keywords

[No Author keywords available]

Indexed keywords

ANTENNAPEDIA PROTEIN; ANTIMALARIAL AGENT; CYSTEINE PROTEINASE; FALCIPAIN 2; HEMOGLOBIN; HYBRID PROTEIN; PEPTIDE DERIVATIVE;

EID: 44949174908     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm070735f     Document Type: Article
Times cited : (32)

References (50)
  • 1
    • 0242669367 scopus 로고    scopus 로고
    • Data-mining approaches reveal hidden families of proteases in the genome of malaria parasite
    • Wu, Y.; Wang, X.; Liu, X.; Wang, Y. Data-mining approaches reveal hidden families of proteases in the genome of malaria parasite. Genome Res. 2003, 4, 601-616.
    • (2003) Genome Res , vol.4 , pp. 601-616
    • Wu, Y.1    Wang, X.2    Liu, X.3    Wang, Y.4
  • 3
    • 0035986688 scopus 로고    scopus 로고
    • Cysteine proteases of malaria parasites: Targets for chemotherapy
    • Rosenthal, P. J.; Sijwali, P. S.; Singh, A.; Shenai, B. R. Cysteine proteases of malaria parasites: targets for chemotherapy. Curr. Pharm. Des. 2002, 8 (18), 1659-1672.
    • (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
  • 4
    • 33745041171 scopus 로고    scopus 로고
    • Plasmodium falciparum ensures its amino acid supply with multiple acquisition pathways and redundant proteolytic enzyme systems
    • Liu, J.; Istvan, E. S.; Gluzman, I. Y.; Gross, J.; Goldberg, D. E. Plasmodium falciparum ensures its amino acid supply with multiple acquisition pathways and redundant proteolytic enzyme systems. Proc. Natl. Acad. Sci. U.S.A. 2006, 103 (23), 8840-8845.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , Issue.23 , pp. 8840-8845
    • Liu, J.1    Istvan, E.S.2    Gluzman, I.Y.3    Gross, J.4    Goldberg, D.E.5
  • 5
    • 0035793051 scopus 로고    scopus 로고
    • Malaria parasite exit from the host erythrocyte: A two-step process requiring extraerythrocytic proteolysis
    • Salmon, A. L.; Oksman, A.; Goldberg, D. E. Malaria parasite exit from the host erythrocyte: A two-step process requiring extraerythrocytic proteolysis. Proc. Natl. Acad. Sci. U.S.A. 2001, 98, 271-276.
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 271-276
    • Salmon, A.L.1    Oksman, A.2    Goldberg, D.E.3
  • 6
    • 0141509925 scopus 로고    scopus 로고
    • Selective inhibition of a two-step egress of malaria parasites from the host erythrocyte
    • Wickham, M. E.; Culvenor, J. G.; Cowman, A. F. Selective inhibition of a two-step egress of malaria parasites from the host erythrocyte. J. Biol. Chem. 2003, 278 (39), 37658-37663.
    • (2003) J. Biol. Chem , vol.278 , Issue.39 , pp. 37658-37663
    • Wickham, M.E.1    Culvenor, J.G.2    Cowman, A.F.3
  • 9
    • 1842533231 scopus 로고    scopus 로고
    • Gene disruption confirms a critical role for the cysteine protease falcipain-2 in hemoglobin hydrolysis by Plasmodium falciparum
    • Sijwali, P. S.; Rosenthal, P. J. Gene disruption confirms a critical role for the cysteine protease falcipain-2 in hemoglobin hydrolysis by Plasmodium falciparum. Proc. Natl. Acad. Sci. U.S.A. 2004, 101 (13), 4384-4389.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , Issue.13 , pp. 4384-4389
    • Sijwali, P.S.1    Rosenthal, P.J.2
  • 10
    • 34147117996 scopus 로고    scopus 로고
    • Falcipain-1, a Plasmodium falciparum cysteine protease with vaccine potential
    • Kumar, A.; Kumar, K.; Korde, R.; Puri, S. K.; Malhotra, P.; Chauhan, V. S. Falcipain-1, a Plasmodium falciparum cysteine protease with vaccine potential. Infect. Immun. 2007, 75 (4), 2026-2034.
    • (2007) Infect. Immun , vol.75 , Issue.4 , pp. 2026-2034
    • Kumar, A.1    Kumar, K.2    Korde, R.3    Puri, S.K.4    Malhotra, P.5    Chauhan, V.S.6
  • 11
    • 12744262976 scopus 로고    scopus 로고
    • Cysteine proteases of malaria parasites
    • Rosenthal, P. J. Cysteine proteases of malaria parasites. Int. J. Parasitol. 2004, 34 (13-14), 1489-1499.
    • (2004) Int. J. Parasitol , vol.34 , Issue.13-14 , pp. 1489-1499
    • Rosenthal, P.J.1
  • 12
  • 13
    • 0036254611 scopus 로고    scopus 로고
    • Novel cysteine proteinase inhibitors homologous to the proregions of cysteine proteinases
    • Yamamoto, Y.; Kurata, M.; Watabe, S.; Murakami, R.; Takahashi, S. Y. Novel cysteine proteinase inhibitors homologous to the proregions of cysteine proteinases. Curr. Protein Pept. Sci. 2002, 3 (2), 231-238.
    • (2002) Curr. Protein Pept. Sci , vol.3 , Issue.2 , pp. 231-238
    • Yamamoto, Y.1    Kurata, M.2    Watabe, S.3    Murakami, R.4    Takahashi, S.Y.5
  • 14
    • 0036233856 scopus 로고    scopus 로고
    • The peptidase zymogen proregions: Nature's way of preventing undesired activation and proteolysis
    • Lazure, C. The peptidase zymogen proregions: nature's way of preventing undesired activation and proteolysis. Curr. Pharm. Des. 2002, 8 (7), 511-531.
    • (2002) Curr. Pharm. Des , vol.8 , Issue.7 , pp. 511-531
    • Lazure, C.1
  • 15
    • 0042208063 scopus 로고    scopus 로고
    • Functional characterization of the propeptide of Plasmodium falciparum subtilisin-like protease-1
    • Jean, L.; Hackett, F.; Martin, S. R.; Blackman, M. J. Functional characterization of the propeptide of Plasmodium falciparum subtilisin-like protease-1. J. Biol. Chem. 2003, 278 (31), 28572-28579.
    • (2003) J. Biol. Chem , vol.278 , Issue.31 , pp. 28572-28579
    • Jean, L.1    Hackett, F.2    Martin, S.R.3    Blackman, M.J.4
  • 18
    • 0036041210 scopus 로고    scopus 로고
    • The role of N-terminal propeptide of the pro-aminopeptidase processing protease: Refolding, processing, and enzyme inhibition
    • Tang, B.; Nirasawa, S.; Kitaoka, M.; Hayashi, K. The role of N-terminal propeptide of the pro-aminopeptidase processing protease: refolding, processing, and enzyme inhibition. Biochem. Biophys. Res. Commun. 2002, 296, 78-84.
    • (2002) Biochem. Biophys. Res. Commun , vol.296 , pp. 78-84
    • Tang, B.1    Nirasawa, S.2    Kitaoka, M.3    Hayashi, K.4
  • 19
    • 0037459069 scopus 로고    scopus 로고
    • General function of N-terminal propeptide on assisting protein folding and inhibiting catalytic activity based on observations with a chimeric thermolysin-like protease
    • Tang, B.; Nirasawa, S.; Kitaoka, M.; Marie-Claire, C.; Hayashi, K. General function of N-terminal propeptide on assisting protein folding and inhibiting catalytic activity based on observations with a chimeric thermolysin-like protease. Biochem. Biophys. Res. Commun. 2003, 301 (4), 1093-1098.
    • (2003) Biochem. Biophys. Res. Commun , vol.301 , Issue.4 , pp. 1093-1098
    • Tang, B.1    Nirasawa, S.2    Kitaoka, M.3    Marie-Claire, C.4    Hayashi, K.5
  • 20
    • 15744362474 scopus 로고    scopus 로고
    • Muntener, K.; Willimann, A.; Zwicky, R.; Svoboda, B.; Mach, L.; Baici, A. Folding competence of N-terminally truncated forms of human procathepsin B. J. Biol. Chem. 2005, 280 (12), 11973-11980.
    • Muntener, K.; Willimann, A.; Zwicky, R.; Svoboda, B.; Mach, L.; Baici, A. Folding competence of N-terminally truncated forms of human procathepsin B. J. Biol. Chem. 2005, 280 (12), 11973-11980.
  • 21
    • 0034666133 scopus 로고    scopus 로고
    • Characterization of native and recombinant falcipain-2, a principal trophozoite cysteine protease and essential hemoglobinase of Plasmodium falciparum
    • Shenai, B. R.; Sijwali, P. S.; Singh, A.; Rosenthal, P. J. Characterization of native and recombinant falcipain-2, a principal trophozoite cysteine protease and essential hemoglobinase of Plasmodium falciparum. J. Biol. Chem. 2000, 275 (37), 29000-29010.
    • (2000) J. Biol. Chem , vol.275 , Issue.37 , pp. 29000-29010
    • Shenai, B.R.1    Sijwali, P.S.2    Singh, A.3    Rosenthal, P.J.4
  • 22
    • 23244457789 scopus 로고    scopus 로고
    • Inhibition of a cathepsin L-like cysteine protease a chimeric propeptide-derived inhibitor
    • Godat, E.; Chowdhury, S.; Lecaille, F.; Belghazi, M.; Purisima, E. O.; Lalmanach, G. Inhibition of a cathepsin L-like cysteine protease a chimeric propeptide-derived inhibitor. Biochemistry 2005, 44 (31), 10486-10493.
    • (2005) Biochemistry , vol.44 , Issue.31 , pp. 10486-10493
    • Godat, E.1    Chowdhury, S.2    Lecaille, F.3    Belghazi, M.4    Purisima, E.O.5    Lalmanach, G.6
  • 23
    • 0032980694 scopus 로고    scopus 로고
    • The propeptide of Faciola hepatica Cathepsin L is a potent and selective inhibitor of mature enzyme
    • Roche, L.; Tort, J.; Dalton, J. P. The propeptide of Faciola hepatica Cathepsin L is a potent and selective inhibitor of mature enzyme. Mol. Biochem. Parasitol. 1999, 98, 271-277.
    • (1999) Mol. Biochem. Parasitol , vol.98 , pp. 271-277
    • Roche, L.1    Tort, J.2    Dalton, J.P.3
  • 24
    • 0030565487 scopus 로고    scopus 로고
    • Inhibition of cathepsin B by its propeptide: Use of overlapping peptides to identify a critical segment
    • Chagas, J. R.; Ferrer-Di Martino, M.; Gauthier, F.; Lalmanach, G. Inhibition of cathepsin B by its propeptide: use of overlapping peptides to identify a critical segment. FEBS Lett. 1996, 392 (3), 233-236.
    • (1996) FEBS Lett , vol.392 , Issue.3 , pp. 233-236
    • Chagas, J.R.1    Ferrer-Di Martino, M.2    Gauthier, F.3    Lalmanach, G.4
  • 26
    • 21544442303 scopus 로고    scopus 로고
    • The Plasmodium falciparum cysteine protease falcipain-2 captures its substrate, hemoglobin, via a unique motif
    • Pandey, K. C.; Wang, S. X.; Sijwali, P. S.; Lau, A. L.; McKerrow, J. H.; Rosenthal, P. J. The Plasmodium falciparum cysteine protease falcipain-2 captures its substrate, hemoglobin, via a unique motif. Proc. Natl. Acad. Sci U.S.A. 2005, 102 (26), 9138-9143.
    • (2005) Proc. Natl. Acad. Sci U.S.A , vol.102 , Issue.26 , pp. 9138-9143
    • Pandey, K.C.1    Wang, S.X.2    Sijwali, P.S.3    Lau, A.L.4    McKerrow, J.H.5    Rosenthal, P.J.6
  • 27
    • 33748741385 scopus 로고    scopus 로고
    • TIMP-3 inhibits the procollagen N-proteinase ADAMTS-2
    • Wang, W. M.; Ge, G.; Lim, N. H.; Nagase, H.; Greenspan, D. S. TIMP-3 inhibits the procollagen N-proteinase ADAMTS-2. Biochem. J. 2006, 398 (3), 515-519.
    • (2006) Biochem. J , vol.398 , Issue.3 , pp. 515-519
    • Wang, W.M.1    Ge, G.2    Lim, N.H.3    Nagase, H.4    Greenspan, D.S.5
  • 28
    • 1642422393 scopus 로고    scopus 로고
    • Exploring the role of putative active site amino acids and pro-region motif of recombinant falcipain-2, a principal hemoglobinase of Plasmodium falciparum
    • Kumar, A.; Dasaradhi, P. V. N.; Chauhan, V. S.; Malhotra, P. Exploring the role of putative active site amino acids and pro-region motif of recombinant falcipain-2, a principal hemoglobinase of Plasmodium falciparum. Biochem. Biophys. Res. Commun. 2004, 317 (1), 35-45.
    • (2004) Biochem. Biophys. Res. Commun , vol.317 , Issue.1 , pp. 35-45
    • Kumar, A.1    Dasaradhi, P.V.N.2    Chauhan, V.S.3    Malhotra, P.4
  • 29
    • 0037177832 scopus 로고    scopus 로고
    • Folding of the Plasmodium falciparum cysteine protease falcipain-2 is mediated by a chaperone-like peptide and not the prodomain
    • Sijwali, P. S.; Shenai, B. R.; Rosenthal, P. J. Folding of the Plasmodium falciparum cysteine protease falcipain-2 is mediated by a chaperone-like peptide and not the prodomain. J. Biol. Chem. 2002, 277 (17), 14910-14915.
    • (2002) J. Biol. Chem , vol.277 , Issue.17 , pp. 14910-14915
    • Sijwali, P.S.1    Shenai, B.R.2    Rosenthal, P.J.3
  • 30
    • 0027394245 scopus 로고
    • Two Distinct Gene Subfamilies within the Family of Cysteine Protease Genes
    • Karrer, K. M.; Peiffer, S. L.; DiTomas, M. E. Two Distinct Gene Subfamilies within the Family of Cysteine Protease Genes. Proc. Natl. Acad. Sci. U.S.A. 1993, 90, 3063-3067.
    • (1993) Proc. Natl. Acad. Sci. U.S.A , vol.90 , pp. 3063-3067
    • Karrer, K.M.1    Peiffer, S.L.2    DiTomas, M.E.3
  • 32
    • 0043031443 scopus 로고    scopus 로고
    • Ankyrin peptide blocks falcipain-2-mediated malaria parasite release from red blood cells
    • Dhawan, S.; Dua, M.; Chishti, A. H.; Hanspal, M. Ankyrin peptide blocks falcipain-2-mediated malaria parasite release from red blood cells. J. Biol. Chem. 2003, 278 (32), 30180-30186.
    • (2003) J. Biol. Chem , vol.278 , Issue.32 , pp. 30180-30186
    • Dhawan, S.1    Dua, M.2    Chishti, A.H.3    Hanspal, M.4
  • 33
    • 23344444863 scopus 로고    scopus 로고
    • Tudor domains bind symmetrical dimethylated arginines
    • Cote, J.; Richard, S. Tudor domains bind symmetrical dimethylated arginines. J. Biol. Chem. 2005, 280, 28476-28483.
    • (2005) J. Biol. Chem , vol.280 , pp. 28476-28483
    • Cote, J.1    Richard, S.2
  • 34
    • 0028948564 scopus 로고
    • Plasmodium falciparum: Effects of Proteinase inhibitors on Globin Hydrolysis by cultured malaria parasites
    • Rosenthal, P. J. Plasmodium falciparum: Effects of Proteinase inhibitors on Globin Hydrolysis by cultured malaria parasites. Exp. Parasitol. 1995, 80, 272-281.
    • (1995) Exp. Parasitol , vol.80 , pp. 272-281
    • Rosenthal, P.J.1
  • 36
    • 0029045156 scopus 로고
    • The cysteine protease of Trypanosoma cruzi as a model for antiparasite drug design
    • McKerrow, J. H.; McGrath, M. E.; Engel, J. C. The cysteine protease of Trypanosoma cruzi as a model for antiparasite drug design. Parasitology Today 1995, 11, 279-282.
    • (1995) Parasitology Today , vol.11 , pp. 279-282
    • McKerrow, J.H.1    McGrath, M.E.2    Engel, J.C.3
  • 37
    • 0033057631 scopus 로고    scopus 로고
    • Antimalarial effects in mice of orally administered peptidyl cysteine protease inhibitors
    • Olson, J. E.; Lee, G. K.; Semenov, A.; Rosenthal, P. J. Antimalarial effects in mice of orally administered peptidyl cysteine protease inhibitors. Bioorg. Med. Chem. 1999, 7, 633-638.
    • (1999) Bioorg. Med. Chem , vol.7 , pp. 633-638
    • Olson, J.E.1    Lee, G.K.2    Semenov, A.3    Rosenthal, P.J.4
  • 39
    • 1642292453 scopus 로고    scopus 로고
    • Identification and biochemical characterization of vivapains, cysteine proteases of the malaria parasite Plasmodium vivax
    • Na, B. K.; Shenai, B. R.; Sijwali, P. S.; Choe, Y.; Pandey, K. C.; Singh, A.; Craik, C. S.; Rosenthal, P. J. Identification and biochemical characterization of vivapains, cysteine proteases of the malaria parasite Plasmodium vivax. Biochem. J. 2004, 378 (2), 529-538.
    • (2004) Biochem. J , vol.378 , Issue.2 , pp. 529-538
    • Na, B.K.1    Shenai, B.R.2    Sijwali, P.S.3    Choe, Y.4    Pandey, K.C.5    Singh, A.6    Craik, C.S.7    Rosenthal, P.J.8
  • 40
    • 0037226491 scopus 로고    scopus 로고
    • Structure-activity relationships for inhibition of cysteine protease activity and development of Plasmodium falciparum by peptidyl vinyl sulfones
    • Shenai, B. R.; Lee, B. J.; Alvarez-Hernandez, A.; Chong, P. Y.; Emal, C. D.; Neitz, R. J.; Roush, W. R.; Rosenthal, P. J. Structure-activity relationships for inhibition of cysteine protease activity and development of Plasmodium falciparum by peptidyl vinyl sulfones. Antimicrob. Agents Chemother. 2003, 47 (1), 154-160.
    • (2003) Antimicrob. Agents Chemother , vol.47 , Issue.1 , pp. 154-160
    • Shenai, B.R.1    Lee, B.J.2    Alvarez-Hernandez, A.3    Chong, P.Y.4    Emal, C.D.5    Neitz, R.J.6    Roush, W.R.7    Rosenthal, P.J.8
  • 43
    • 3042549368 scopus 로고    scopus 로고
    • Uptake of proteins and degradation of human serum albumin by Plasmodium falciparum-infected human erythrocytes
    • Tahir, A. E. L.; Malhotra, P.; Chauhan, V. S. Uptake of proteins and degradation of human serum albumin by Plasmodium falciparum-infected human erythrocytes. Malaria J. 2003, 2, 11.
    • (2003) Malaria J , vol.2 , pp. 11
    • Tahir, A.E.L.1    Malhotra, P.2    Chauhan, V.S.3
  • 46
    • 0031691453 scopus 로고    scopus 로고
    • Antimalarial synergy of cysteine and aspartic protease inhibitors
    • Semenov, A.; Olson, J. E.; Rosenthal, P. J. Antimalarial synergy of cysteine and aspartic protease inhibitors. Antimicrob. Agents. Chemother. 1998, 48, 2254-2258.
    • (1998) Antimicrob. Agents. Chemother , vol.48 , pp. 2254-2258
    • Semenov, A.1    Olson, J.E.2    Rosenthal, P.J.3
  • 47
    • 0017311840 scopus 로고
    • Human malaria parasites in continuous culture
    • Trager, W.; Jensen, J. B. Human malaria parasites in continuous culture. Science 1976, 193 (4254), 673-675.
    • (1976) Science , vol.193 , Issue.4254 , pp. 673-675
    • Trager, W.1    Jensen, J.B.2
  • 48
    • 0035886970 scopus 로고    scopus 로고
    • Trafficking and assembly of cytoadherence complex in Plasmodium falciparum-infected human erythrocytes
    • Wickham, M. E.; Rug, M.; Ralph, S. A.; Klonis, N.; McFadden, G. I.; Tilley, L.; Cowman, A. F. Trafficking and assembly of cytoadherence complex in Plasmodium falciparum-infected human erythrocytes. Embo. J. 2001, 20, 5636-5649.
    • (2001) Embo. J , vol.20 , pp. 5636-5649
    • Wickham, M.E.1    Rug, M.2    Ralph, S.A.3    Klonis, N.4    McFadden, G.I.5    Tilley, L.6    Cowman, A.F.7
  • 49
    • 0018704491 scopus 로고
    • Synchronization of Plasmodium falciparum erythrocytic stages in culture
    • Lambros, C.; Vanderberg, J. P. Synchronization of Plasmodium falciparum erythrocytic stages in culture. J. Parasitol. 1979, 65 (3), 418-420.
    • (1979) J. Parasitol , vol.65 , Issue.3 , pp. 418-420
    • Lambros, C.1    Vanderberg, J.P.2
  • 50
    • 0036049784 scopus 로고    scopus 로고
    • Double-stranded RNA-mediated gene silencing of cysteine proteases (falcipain-1 and -2) of Plasmodium falciparum
    • Malhotra, P.; Dasaradhi, P. V.; Kumar, A.; Mohmmed, A.; Agrawal, N.; Bhatnagar, R. K.; Chauhan, V. S. Double-stranded RNA-mediated gene silencing of cysteine proteases (falcipain-1 and -2) of Plasmodium falciparum. Mol. Microbiol. 2002, 45 (5), 1245-1254.
    • (2002) Mol. Microbiol , vol.45 , Issue.5 , pp. 1245-1254
    • Malhotra, P.1    Dasaradhi, P.V.2    Kumar, A.3    Mohmmed, A.4    Agrawal, N.5    Bhatnagar, R.K.6    Chauhan, V.S.7


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