메뉴 건너뛰기




Volumn 68, Issue 3, 2000, Pages 1202-1206

Metalloprotease activity in a small heat shock protein of the human malaria parasite Plasmodium vivax

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN; METALLOPROTEINASE; PROTOZOAL PROTEIN;

EID: 0033982190     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.68.3.1202-1206.2000     Document Type: Article
Times cited : (11)

References (42)
  • 2
    • 0027451943 scopus 로고
    • A conserved parasite serine protease processes the Plasmodium falciparum Merozoite Surface Protein-1
    • Blackman, M. J., J. A. Chappel, S. Shai, and A. A. Holder. 1993. A conserved parasite serine protease processes the Plasmodium falciparum Merozoite Surface Protein-1. Mol. Biochem. Parasitol. 62:103-114.
    • (1993) Mol. Biochem. Parasitol. , vol.62 , pp. 103-114
    • Blackman, M.J.1    Chappel, J.A.2    Shai, S.3    Holder, A.A.4
  • 4
    • 0027932992 scopus 로고
    • Molecular characterization of the heat shock protein 90 gene of the human malaria parasite Plasmodium falciparum
    • Bonnefoy, S., G. Attal, G. Langsley, F. Tekaia, and O. Mercereau-Puijalon. 1994. Molecular characterization of the heat shock protein 90 gene of the human malaria parasite Plasmodium falciparum. Mol. Biochem. Parasitol. 67:157-170.
    • (1994) Mol. Biochem. Parasitol. , vol.67 , pp. 157-170
    • Bonnefoy, S.1    Attal, G.2    Langsley, G.3    Tekaia, F.4    Mercereau-Puijalon, O.5
  • 7
    • 0032489016 scopus 로고    scopus 로고
    • The HSP70 and HSP60 chaperone machines
    • Bukau, B., and A. Horwich. 1998. The HSP70 and HSP60 chaperone machines. Cell 92:351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.2
  • 8
    • 0024509987 scopus 로고
    • Surface acid proteinase (gp63) of Leishmania maxicana. A metalloenzyme capable of protecting liposome encapsulated proteins from phagolysosomal degradation by macrophages
    • Chaudhuri, G., M. Chaudhuri, A. Pan, and K. P. Chang. 1989. Surface acid proteinase (gp63) of Leishmania maxicana. A metalloenzyme capable of protecting liposome encapsulated proteins from phagolysosomal degradation by macrophages. J. Biol. Chem. 264:7483-7489.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7483-7489
    • Chaudhuri, G.1    Chaudhuri, M.2    Pan, A.3    Chang, K.P.4
  • 9
    • 0022617296 scopus 로고
    • Purification and characterization of an extra cellular protease of Legionella pneumophila
    • Dreyfus, L. A., and B. H. Iglewski. 1986. Purification and characterization of an extra cellular protease of Legionella pneumophila. Infect. Immun. 51:736-743.
    • (1986) Infect. Immun. , vol.51 , pp. 736-743
    • Dreyfus, L.A.1    Iglewski, B.H.2
  • 10
    • 0023029999 scopus 로고
    • Plasmodium falciparum: Protease inhibitors and inhibition of erythrocyte invasion
    • Dulzewski, A. R., K. Rangachari, R. J. M. Wilson, and W. B. C. Gratzer. 1986. Plasmodium falciparum: protease inhibitors and inhibition of erythrocyte invasion. Exp. Parasitol. 62:416-422.
    • (1986) Exp. Parasitol. , vol.62 , pp. 416-422
    • Dulzewski, A.R.1    Rangachari, K.2    Wilson, R.J.M.3    Gratzer, W.B.C.4
  • 11
    • 0019430775 scopus 로고
    • In vitro susceptibility of erythrocytes of Presbytisentellus (Indian Langur) to Plasmodium knowlesi and blocking of merozoite invasion process by certain protease inhibitors
    • Dutta, G. P., and H. S. Banyal. 1981. In vitro susceptibility of erythrocytes of Presbytisentellus (Indian Langur) to Plasmodium knowlesi and blocking of merozoite invasion process by certain protease inhibitors. Indian J. Exp. Biol. 19:9-11.
    • (1981) Indian J. Exp. Biol. , vol.19 , pp. 9-11
    • Dutta, G.P.1    Banyal, H.S.2
  • 12
    • 0026781519 scopus 로고
    • The sequence, organization, and expression of the major cysteine protease (cruzain) from Trypanosoma cruzi
    • Eakin, A. E., A. A. Mills, G. Harth, J. H. McKerrow, and C. S. Craik. 1992. The sequence, organization, and expression of the major cysteine protease (cruzain) from Trypanosoma cruzi. J. Biol. Chem. 267:7411-7420.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7411-7420
    • Eakin, A.E.1    Mills, A.A.2    Harth, G.3    McKerrow, J.H.4    Craik, C.S.5
  • 13
    • 0031452808 scopus 로고    scopus 로고
    • Identification of Plasmodium vivax heat shock protein which contains a metalloprotease sequence motif
    • Fakruddin, J. M., S. Biswas, and Y. D. Sharma. 1997. Identification of Plasmodium vivax heat shock protein which contains a metalloprotease sequence motif. Mol. Biochem. Parasitol. 90:387-390.
    • (1997) Mol. Biochem. Parasitol. , vol.90 , pp. 387-390
    • Fakruddin, J.M.1    Biswas, S.2    Sharma, Y.D.3
  • 14
    • 0032583101 scopus 로고    scopus 로고
    • A Plasmodium falciparum aminopeptidase gene belonging to the M1 family of zinc-metallopeptidases is expressed in erythrocytic stages
    • Florent, I., Z. Derhy, M. Allary, M. Monsigny, R. Mayer, and J. Schrevel. 1998. A Plasmodium falciparum aminopeptidase gene belonging to the M1 family of zinc-metallopeptidases is expressed in erythrocytic stages. Mol. Biochem. Parasitol. 97:149-160.
    • (1998) Mol. Biochem. Parasitol. , vol.97 , pp. 149-160
    • Florent, I.1    Derhy, Z.2    Allary, M.3    Monsigny, M.4    Mayer, R.5    Schrevel, J.6
  • 16
    • 0031048991 scopus 로고    scopus 로고
    • A novel membrane-associated metalloprotease, Ste 24P, is required for the first step of NH2-terminal processing of the yeast alpha factor precursor
    • Fujimura-Kamada, K., F. J. Nouvet, and S. Michaelis. 1997. A novel membrane-associated metalloprotease, Ste 24P, is required for the first step of NH2-terminal processing of the yeast alpha factor precursor. J. Cell Biol. 136:271-285.
    • (1997) J. Cell Biol. , vol.136 , pp. 271-285
    • Fujimura-Kamada, K.1    Nouvet, F.J.2    Michaelis, S.3
  • 19
    • 0019505043 scopus 로고
    • Purification and characterization of a transformation-dependent protein secreted by cultured murine fibroblasts
    • Gottesman, M. M., and F. Cabral. 1981. Purification and characterization of a transformation-dependent protein secreted by cultured murine fibroblasts. Biochemistry 20:1659-1665.
    • (1981) Biochemistry , vol.20 , pp. 1659-1665
    • Gottesman, M.M.1    Cabral, F.2
  • 20
    • 0030444320 scopus 로고    scopus 로고
    • Proteases and their targets in Escherichia coli
    • Gottesman, S. 1996. Proteases and their targets in Escherichia coli. Annu. Rev. Genet. 30:465-506.
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 465-506
    • Gottesman, S.1
  • 21
    • 0025878480 scopus 로고
    • Cloning and nucleotide sequence of the Vibrio cholerae hemagglutinin/protease (HA/protease) gene and construction of an HA/protease-negative strain
    • Hase, C. C., and R. A. Finkelstein. 1991. Cloning and nucleotide sequence of the Vibrio cholerae hemagglutinin/protease (HA/protease) gene and construction of an HA/protease-negative strain. J. Bacteriol. 173:3311-3317.
    • (1991) J. Bacteriol. , vol.173 , pp. 3311-3317
    • Hase, C.C.1    Finkelstein, R.A.2
  • 22
    • 0018854046 scopus 로고
    • Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates
    • Heussen, C., and E. B. Dowdle. 1980. Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates. Anal. Biochem. 102:196-202.
    • (1980) Anal. Biochem. , vol.102 , pp. 196-202
    • Heussen, C.1    Dowdle, E.B.2
  • 23
    • 0028354782 scopus 로고
    • Isolation and characterization of a chaperonin-60 gene of the human malaria parasite Plasmodium falciparum
    • Holloway, S. P., W. Min, and J. S. Inselburg. 1994. Isolation and characterization of a chaperonin-60 gene of the human malaria parasite Plasmodium falciparum. Mol. Biochem. Parasitol. 64:25-32.
    • (1994) Mol. Biochem. Parasitol. , vol.64 , pp. 25-32
    • Holloway, S.P.1    Min, W.2    Inselburg, J.S.3
  • 24
    • 0024559146 scopus 로고
    • A unique signature identifies a family of zinc-dependent metallopeptidases
    • Jongeneel, C. V., J. Bouvier, and A. Bairoch. 1989. A unique signature identifies a family of zinc-dependent metallopeptidases. FEBS Lett. 242:211-214.
    • (1989) FEBS Lett. , vol.242 , pp. 211-214
    • Jongeneel, C.V.1    Bouvier, J.2    Bairoch, A.3
  • 25
    • 0343399662 scopus 로고
    • Plasmodium falciparum gene encoding a protein similar to the 78-kDa rat glucose-regulated stress protein
    • Kumar, N., C. A. Syin, R. Carter, I. Quakyi, and L. H. Miller. 1988. Plasmodium falciparum gene encoding a protein similar to the 78-kDa rat glucose-regulated stress protein. Proc. Natl. Acad. Sci. USA 85:6277-6281.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 6277-6281
    • Kumar, N.1    Syin, C.A.2    Carter, R.3    Quakyi, I.4    Miller, L.H.5
  • 27
    • 0024560589 scopus 로고
    • Purification and substrate specificity of a strongly hydrophobic extracellular metalloendopeptidase ("gelatinase") from Streptococcus faecalis (strain OGI-10)
    • Makinen, P. L., D. B. Clewell, F. An, and K. K. Makinen. 1989. Purification and substrate specificity of a strongly hydrophobic extracellular metalloendopeptidase ("gelatinase") from Streptococcus faecalis (strain OGI-10). J. Biol. Chem. 264:3325-3334.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3325-3334
    • Makinen, P.L.1    Clewell, D.B.2    An, F.3    Makinen, K.K.4
  • 28
    • 0029072044 scopus 로고
    • Pseudolysin and other pathogen endopeptidases of thermolysin family
    • Morihara, K. 1995. Pseudolysin and other pathogen endopeptidases of thermolysin family. Methods Enzymol. 248:242-253.
    • (1995) Methods Enzymol. , vol.248 , pp. 242-253
    • Morihara, K.1
  • 29
    • 0031878901 scopus 로고    scopus 로고
    • Plasmodium chabaudi chabaudi and P. falciparum: Inhibition of aminopeptidase and parasite growth by bestatin and nitrobestatin
    • Nankya-Kitaka, M. F., G. P. Curley, C. S. Gavigan, A. Bell, and J. P. Dalton. 1998. Plasmodium chabaudi chabaudi and P. falciparum: inhibition of aminopeptidase and parasite growth by bestatin and nitrobestatin. Parasitol. Res. 84:552-558.
    • (1998) Parasitol. Res. , vol.84 , pp. 552-558
    • Nankya-Kitaka, M.F.1    Curley, G.P.2    Gavigan, C.S.3    Bell, A.4    Dalton, J.P.5
  • 30
    • 0029828987 scopus 로고    scopus 로고
    • Plasmodium falciparum proteinases: Targeted drug development
    • Olliaro, P. L., M. Gottlieb, and D. F. Wirth. 1996. Plasmodium falciparum proteinases: targeted drug development. Parasitol. Today 12:413.
    • (1996) Parasitol. Today , vol.12 , pp. 413
    • Olliaro, P.L.1    Gottlieb, M.2    Wirth, D.F.3
  • 31
    • 0029036451 scopus 로고
    • Evolutionary families of metallopeptidases
    • Rawlings, N. D., and A. J. Barrett. 1995. Evolutionary families of metallopeptidases. Methods Enzymol. 248:183-228.
    • (1995) Methods Enzymol. , vol.248 , pp. 183-228
    • Rawlings, N.D.1    Barrett, A.J.2
  • 32
    • 0028134672 scopus 로고
    • Plasmodium vivax immune responses in a cross-section of the population in the Delhi area of India
    • Ray, P., M. A. Ansari, and Y. D. Sharma. 1994. Plasmodium vivax immune responses in a cross-section of the population in the Delhi area of India. Am. J. Trop. Med. Hyg. 51:436-443.
    • (1994) Am. J. Trop. Med. Hyg. , vol.51 , pp. 436-443
    • Ray, P.1    Ansari, M.A.2    Sharma, Y.D.3
  • 33
    • 0024208917 scopus 로고
    • A malarial cysteine proteinase is necessary for hemoglobin degradation by Plasmodium falciparum
    • Rosenthal, P. J., J. H. McKarrow, M. Aikawa, H. Nagasawa, and J. H. Leech. 1988. A malarial cysteine proteinase is necessary for hemoglobin degradation by Plasmodium falciparum. J. Clin. Investig. 82:1560-1566.
    • (1988) J. Clin. Investig. , vol.82 , pp. 1560-1566
    • Rosenthal, P.J.1    McKarrow, J.H.2    Aikawa, M.3    Nagasawa, H.4    Leech, J.H.5
  • 34
    • 0026586422 scopus 로고
    • Isolation and characterization of a cysteine protease gene of Plasmodium falciparum
    • Rosenthal, P. J., and R. G. Nelson. 1992. Isolation and characterization of a cysteine protease gene of Plasmodium falciparum. Mol. Biochem. Parasitol. 51:143-152.
    • (1992) Mol. Biochem. Parasitol. , vol.51 , pp. 143-152
    • Rosenthal, P.J.1    Nelson, R.G.2
  • 35
    • 0029057887 scopus 로고
    • Functional expression of falcipain, a Plasmodium falciparum cysteine proteinase, supports its role as a malarial hemoglobinase
    • Salas, F., J. Fichmann, G. K. Lee, M. D. Scott, and P. J. Rosenthal. 1995. Functional expression of falcipain, a Plasmodium falciparum cysteine proteinase, supports its role as a malarial hemoglobinase. Infect. Immun. 63:2120-2125.
    • (1995) Infect. Immun. , vol.63 , pp. 2120-2125
    • Salas, F.1    Fichmann, J.2    Lee, G.K.3    Scott, M.D.4    Rosenthal, P.J.5
  • 36
    • 0025872835 scopus 로고
    • Isolation and serological characterization of a Plasmodium vivax recombinant antigen
    • Sharma, Y. D., V. P. Sharma, P. Ray, S. Laal, S. D. Sawant, and S. Verma. 1991. Isolation and serological characterization of a Plasmodium vivax recombinant antigen. Infect. Immun. 59:1922-1926.
    • (1991) Infect. Immun. , vol.59 , pp. 1922-1926
    • Sharma, Y.D.1    Sharma, V.P.2    Ray, P.3    Laal, S.4    Sawant, S.D.5    Verma, S.6
  • 37
    • 0033617146 scopus 로고    scopus 로고
    • A temperature-dependent switch from chaperone to protease in a widely conserved heat-shock protein
    • Spiess, C., A. Beil, and M. Ehrmann. 1999. A temperature-dependent switch from chaperone to protease in a widely conserved heat-shock protein. Cell 97:339-347.
    • (1999) Cell , vol.97 , pp. 339-347
    • Spiess, C.1    Beil, A.2    Ehrmann, M.3
  • 38
    • 17144438526 scopus 로고    scopus 로고
    • Actin-binding proteins of invasive malaria parasites and the regulation of actin polymerization by a complex of 32/34-kDa proteins associated with heat-shock protein 70kDa
    • Tardieux, I., I. Baines, M. Mossakowska, and G. E. Ward. 1998. Actin-binding proteins of invasive malaria parasites and the regulation of actin polymerization by a complex of 32/34-kDa proteins associated with heat-shock protein 70kDa. Mol. Biochem. Parasitol. 93:295-308.
    • (1998) Mol. Biochem. Parasitol. , vol.93 , pp. 295-308
    • Tardieux, I.1    Baines, I.2    Mossakowska, M.3    Ward, G.E.4
  • 39
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 40
    • 0024954937 scopus 로고
    • Disease problem in the Third World
    • Walsh, J. A. 1989. Disease problem in the Third World. Ann. N.Y. Acad. Sci. 569:1-16.
    • (1989) Ann. N.Y. Acad. Sci. , vol.569 , pp. 1-16
    • Walsh, J.A.1
  • 41
    • 0030871598 scopus 로고    scopus 로고
    • Cloning and characterization of heat-shock protein Dnaj homologues from Plasmodium falciparum and comparison with ring infected erythrocyte surface antigen
    • Watanabe, J. 1997. Cloning and characterization of heat-shock protein Dnaj homologues from Plasmodium falciparum and comparison with ring infected erythrocyte surface antigen. Mol. Biochem. Parasitol. 88:253-258.
    • (1997) Mol. Biochem. Parasitol. , vol.88 , pp. 253-258
    • Watanabe, J.1
  • 42
    • 0023449350 scopus 로고
    • The primary structure of a Plasmodium falciparum polypeptide related to heat shock proteins
    • Yang, Y. F., P. Tan-ariya, Y. D. Sharma, and A. Kilejian. 1987. The primary structure of a Plasmodium falciparum polypeptide related to heat shock proteins. Mol. Biochem. Parasitol. 26:61-67.
    • (1987) Mol. Biochem. Parasitol. , vol.26 , pp. 61-67
    • Yang, Y.F.1    Tan-Ariya, P.2    Sharma, Y.D.3    Kilejian, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.