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Volumn 17, Issue 10, 1997, Pages 5987-5995

Leishmania major Hsp100 is required chiefly in the mammalian stage of the parasite

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN;

EID: 1842337450     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.17.10.5987     Document Type: Article
Times cited : (96)

References (48)
  • 1
    • 0027413933 scopus 로고
    • Axenic amastigote culture of Leishmania amastigotes
    • Bates, P. A. 1993. Axenic amastigote culture of Leishmania amastigotes. Parasitol. Today 9:143-146.
    • (1993) Parasitol. Today , vol.9 , pp. 143-146
    • Bates, P.A.1
  • 2
    • 0018648646 scopus 로고
    • Leishmania major: Pathogenicity and in vitro macrophage function in strains of inbred mice
    • Behin, R., J. Mauel, and B. Sordat. 1979. Leishmania major: pathogenicity and in vitro macrophage function in strains of inbred mice. Exp. Parasitol. 8:81-91.
    • (1979) Exp. Parasitol. , vol.8 , pp. 81-91
    • Behin, R.1    Mauel, J.2    Sordat, B.3
  • 3
    • 0029143254 scopus 로고
    • High constitutive levels of heat-shock proteins in human-pathogenic parasites of the genus Leishmania
    • Brandau, S., A. Dresel, and J. Clos. 1995. High constitutive levels of heat-shock proteins in human-pathogenic parasites of the genus Leishmania. Biochem. J. 310:225-232.
    • (1995) Biochem. J. , vol.310 , pp. 225-232
    • Brandau, S.1    Dresel, A.2    Clos, J.3
  • 4
    • 85036485081 scopus 로고    scopus 로고
    • Unpublished data
    • 3a. Brandau, S. Unpublished data.
    • Brandau, S.1
  • 5
    • 85036487923 scopus 로고    scopus 로고
    • Unpublished data
    • 3b. Clos, J. Unpublished data.
    • Clos, J.1
  • 6
    • 0025049856 scopus 로고
    • Gene replacement in parasitic protozoa
    • Cruz, A., and S. M. Beverley. 1990. Gene replacement in parasitic protozoa. Nature 348:171-173.
    • (1990) Nature , vol.348 , pp. 171-173
    • Cruz, A.1    Beverley, S.M.2
  • 8
    • 0027442471 scopus 로고
    • Two more independent selectable markers for stable transfection of Leishmania
    • Freedman, D. J., and S. M. Beverley. 1993. Two more independent selectable markers for stable transfection of Leishmania. Mol. Biochem. Parasitol. 62:37-44.
    • (1993) Mol. Biochem. Parasitol. , vol.62 , pp. 37-44
    • Freedman, D.J.1    Beverley, S.M.2
  • 10
  • 11
    • 0029050870 scopus 로고
    • Transfection and continuous expression of heterologous genes in the protozoan parasite Entamoeba histolytica
    • Hamann, L., R. Nickel, and E. Tannich. 1995. Transfection and continuous expression of heterologous genes in the protozoan parasite Entamoeba histolytica. Proc. Natl. Acad. Sci. USA 92:8975-8979.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8975-8979
    • Hamann, L.1    Nickel, R.2    Tannich, E.3
  • 12
    • 0018745090 scopus 로고
    • Murine cutaneous leishmaniasis: Disease patterns in intact and nude mice of various genotypes and examination of some differences between normal and infected macrophages
    • Handman, E., R. Ceredig, and G. F. Mitchell. 1979. Murine cutaneous leishmaniasis: disease patterns in intact and nude mice of various genotypes and examination of some differences between normal and infected macrophages. Aust. J. Exp. Biol. Med. Sci. 57:9-29.
    • (1979) Aust. J. Exp. Biol. Med. Sci. , vol.57 , pp. 9-29
    • Handman, E.1    Ceredig, R.2    Mitchell, G.F.3
  • 13
    • 0022632963 scopus 로고
    • Pathophysiology of experimental leishmaniasis: Pattern of development of metastatic disease in the susceptible host
    • Hill, J. O. 1986. Pathophysiology of experimental leishmaniasis: pattern of development of metastatic disease in the susceptible host. Infect. Immun. 52:364-369.
    • (1986) Infect. Immun. , vol.52 , pp. 364-369
    • Hill, J.O.1
  • 14
    • 0009882674 scopus 로고
    • Host immunity to leishmaniasis
    • K.-P. Chang and R. S. Bray (ed.), Elsevier Science Publishers, Amsterdam, The Netherlands
    • Howard, J. G. 1985. Host immunity to leishmaniasis, p. 139-162. In K.-P. Chang and R. S. Bray (ed.), Leishmaniasis. Elsevier Science Publishers, Amsterdam, The Netherlands.
    • (1985) Leishmaniasis , pp. 139-162
    • Howard, J.G.1
  • 15
    • 0028958754 scopus 로고
    • A member of the ClpB family of stress proteins is expressed during heat shock in Leishmania spp
    • Hübel, A., S. Brandau, A. Dresel, and J. Clos. 1995. A member of the ClpB family of stress proteins is expressed during heat shock in Leishmania spp. Mol. Biochem. Parasitol. 70:107-118.
    • (1995) Mol. Biochem. Parasitol. , vol.70 , pp. 107-118
    • Hübel, A.1    Brandau, S.2    Dresel, A.3    Clos, J.4
  • 16
    • 0342398231 scopus 로고    scopus 로고
    • The genomic organization of the HSP83 gene locus is conserved in three Leishmania species
    • Hübel, A., and J. Clos. 1996. The genomic organization of the HSP83 gene locus is conserved in three Leishmania species. Exp. Parasitol. 82:225-228.
    • (1996) Exp. Parasitol. , vol.82 , pp. 225-228
    • Hübel, A.1    Clos, J.2
  • 17
    • 0021735783 scopus 로고
    • Leishmanial differentiation in vitro: Induction of heat shock proteins
    • Hunter, K. W., C. L. Cook, and E. G. Hayunga. 1984. Leishmanial differentiation in vitro: induction of heat shock proteins. Biochem. Biophys. Res. Commun. 125:755-760.
    • (1984) Biochem. Biophys. Res. Commun. , vol.125 , pp. 755-760
    • Hunter, K.W.1    Cook, C.L.2    Hayunga, E.G.3
  • 18
    • 0027461089 scopus 로고
    • Cloning and characterisation of differentially expressed genes from in vitro-grown 'amastigotes' of Leishmania donovani
    • Joshi, M., D. M. Dwyer, and H. L. Nakhasi. 1993. Cloning and characterisation of differentially expressed genes from in vitro-grown 'amastigotes' of Leishmania donovani. Mol. Biochem. Parasitol. 58:345-354.
    • (1993) Mol. Biochem. Parasitol. , vol.58 , pp. 345-354
    • Joshi, M.1    Dwyer, D.M.2    Nakhasi, H.L.3
  • 19
    • 0025122367 scopus 로고
    • Stable transfection of the human parasite Leishmania major delineates a 30-kilobase region sufficient for extrachromosomal replication and expression
    • Kapler, G. M., C. M. Coburn, and S. M. Beverley. 1990. Stable transfection of the human parasite Leishmania major delineates a 30-kilobase region sufficient for extrachromosomal replication and expression. Mol. Cell. Biol. 10:1084-1094.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 1084-1094
    • Kapler, G.M.1    Coburn, C.M.2    Beverley, S.M.3
  • 21
    • 85036484787 scopus 로고    scopus 로고
    • Unpublished data
    • 17b. Krobitsch, S., et al. Unpublished data.
    • Krobitsch, S.1
  • 22
    • 0024331981 scopus 로고
    • Transfection of Leishmania enriettü and expression of chloramphenicol acetyltransferase gene
    • Laban, A., and D. F. Wirth. 1989. Transfection of Leishmania enriettü and expression of chloramphenicol acetyltransferase gene. Proc. Natl. Acad. Sci. USA 86:9119-9123.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9119-9123
    • Laban, A.1    Wirth, D.F.2
  • 23
    • 0024345716 scopus 로고
    • Heat shock resistance conferred by expression of the human HSP27 gene in rodent cells
    • Landry, J., P. Chretien, H. Lambert, E. Hickey, and L. A. Weber. 1989. Heat shock resistance conferred by expression of the human HSP27 gene in rodent cells. J. Cell Biol. 109:7-15.
    • (1989) J. Cell Biol. , vol.109 , pp. 7-15
    • Landry, J.1    Chretien, P.2    Lambert, H.3    Hickey, E.4    Weber, L.A.5
  • 24
    • 0027417852 scopus 로고
    • Induction of Chinese hamster HSP27 gene expression in mouse cells confers resistance to heat shock
    • Lavoie, J. N., G. Gingras-Breton, R. M. Tanguay, and J. Landry. 1993. Induction of Chinese hamster HSP27 gene expression in mouse cells confers resistance to heat shock. J. Biol. Chem. 268:3420-3429.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3420-3429
    • Lavoie, J.N.1    Gingras-Breton, G.2    Tanguay, R.M.3    Landry, J.4
  • 25
    • 0022392239 scopus 로고
    • Induction of heat shock and stress proteins in promastigotes of three Leishmania species
    • Lawrence, F., and M. Robert-Gero. 1985. Induction of heat shock and stress proteins in promastigotes of three Leishmania species. Proc. Natl. Acad. Sci. USA 82:4414-4417.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4414-4417
    • Lawrence, F.1    Robert-Gero, M.2
  • 27
    • 0026073457 scopus 로고
    • Thermal response of rat fibroblasts stably transfected with the human 70-kDa heat shock protein-encoding gene
    • Li, G. C., L. G. Li, Y. K. Liu, J. Y. Mak, L. L. Chen, and W. M. Lee. 1991. Thermal response of rat fibroblasts stably transfected with the human 70-kDa heat shock protein-encoding gene. Proc. Natl. Acad. Sci. USA 88:1681-1685.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1681-1685
    • Li, G.C.1    Li, L.G.2    Liu, Y.K.3    Mak, J.Y.4    Chen, L.L.5    Lee, W.M.6
  • 28
    • 0026935588 scopus 로고
    • Heat-shock proteins and stress tolerance in microorganisms
    • Lindquist, S. 1992. Heat-shock proteins and stress tolerance in microorganisms. Curr. Opin. Genet. Dev. 2:748-755.
    • (1992) Curr. Opin. Genet. Dev. , vol.2 , pp. 748-755
    • Lindquist, S.1
  • 29
    • 0002322469 scopus 로고
    • On a test of whether one of two random variables is stochastically larger than the other
    • Mann, H. B., and D. R. Whitney. 1947. On a test of whether one of two random variables is stochastically larger than the other. Ann. Math. Stat. 18:50-60.
    • (1947) Ann. Math. Stat. , vol.18 , pp. 50-60
    • Mann, H.B.1    Whitney, D.R.2
  • 30
    • 0000675009 scopus 로고
    • Heat shock proteins and stress tolerance
    • R. I. Morimoto. A. Tissières, and C. Georgopoulos (ed.), Cold Spring Harbor Laboratory Press, Plainview, N.Y.
    • Parsell, D. A., and S. Lindquist. 1994. Heat shock proteins and stress tolerance, p. 457-494. In R. I. Morimoto. A. Tissières, and C. Georgopoulos (ed.), The biology of heat shock proteins and molecular chaperones. Cold Spring Harbor Laboratory Press, Plainview, N.Y.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 457-494
    • Parsell, D.A.1    Lindquist, S.2
  • 31
    • 0025777272 scopus 로고
    • Hsp104 is a highly conserved protein with two essential nucleotide-binding sites
    • Parsell, D. A., Y. Sanchez, J. D. Stitzel, and S. Lindquist. 1991. Hsp104 is a highly conserved protein with two essential nucleotide-binding sites. Nature 353:270-273.
    • (1991) Nature , vol.353 , pp. 270-273
    • Parsell, D.A.1    Sanchez, Y.2    Stitzel, J.D.3    Lindquist, S.4
  • 32
    • 0027996115 scopus 로고
    • Protein disaggregation mediated by heat-shock protein Hsp104
    • Parsell, D. A., A. S. Kowal, M. A. Singer, and S. Lindquist. 1994. Protein disaggregation mediated by heat-shock protein Hsp104. Nature 372:475-478.
    • (1994) Nature , vol.372 , pp. 475-478
    • Parsell, D.A.1    Kowal, A.S.2    Singer, M.A.3    Lindquist, S.4
  • 33
    • 0027981247 scopus 로고
    • Saccharomyces cerevisiae Hsp104 protein
    • Parsell, D. A., A. S. Kowal, and S. Lindquist. 1994. Saccharomyces cerevisiae Hsp104 protein. J. Biol. Chem. 269:4480-4487.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4480-4487
    • Parsell, D.A.1    Kowal, A.S.2    Lindquist, S.3
  • 34
    • 0025854217 scopus 로고
    • Heat shock proteins in host-parasite interactions
    • Polla, B. S. 1991. Heat shock proteins in host-parasite interactions. Parasitol. Today 7:A38-A41.
    • (1991) Parasitol. Today , vol.7
    • Polla, B.S.1
  • 35
    • 84907110208 scopus 로고
    • Isolation of viral IgY antibodies from yolks of immunized hens
    • Poison, A., B. von Wechmar, and M. H. V. van Regenmortel. 1980. Isolation of viral IgY antibodies from yolks of immunized hens. Immunol. Commun. 9:475-493.
    • (1980) Immunol. Commun. , vol.9 , pp. 475-493
    • Poison, A.1    Von Wechmar, B.2    Van Regenmortel, M.H.V.3
  • 38
    • 0026523626 scopus 로고
    • Hsp104 is required for tolerance to many forms of stress
    • Sanchez, Y., J. Taulien, K. A. Borkovich, and S. Lindquist. 1992. Hsp104 is required for tolerance to many forms of stress. EMBO J. 11:2357-2364.
    • (1992) EMBO J. , vol.11 , pp. 2357-2364
    • Sanchez, Y.1    Taulien, J.2    Borkovich, K.A.3    Lindquist, S.4
  • 39
    • 0025193343 scopus 로고
    • Hsp104 required for induced thermotolerance
    • Sanchez, Y., and S. L. Lindquist. 1990. Hsp104 required for induced thermotolerance. Science 248:1112-1115.
    • (1990) Science , vol.248 , pp. 1112-1115
    • Sanchez, Y.1    Lindquist, S.L.2
  • 40
    • 0026761426 scopus 로고
    • Effects of long-term in vitro cultivation on the virulence of cloned lines of Leishmania major promastigotes
    • Segovia, M., J. M. Artero, E. Mellado, and M. L. Chance. 1992. Effects of long-term in vitro cultivation on the virulence of cloned lines of Leishmania major promastigotes. Ann. Trop. Med. Parasitol. 86:347-354.
    • (1992) Ann. Trop. Med. Parasitol. , vol.86 , pp. 347-354
    • Segovia, M.1    Artero, J.M.2    Mellado, E.3    Chance, M.L.4
  • 41
    • 0024448044 scopus 로고
    • Heat-shock protein 83 of Leishmania mexicana amazonensis is an abundant cytoplasmic protein with a tandemly repeated genomic arrangement
    • Shapira, M., and E. Pinelli. 1989. Heat-shock protein 83 of Leishmania mexicana amazonensis is an abundant cytoplasmic protein with a tandemly repeated genomic arrangement. Eur. J. Biochem. 185:231-236.
    • (1989) Eur. J. Biochem. , vol.185 , pp. 231-236
    • Shapira, M.1    Pinelli, E.2
  • 42
    • 0023848229 scopus 로고
    • Leishmania braziliensis panamensis: Increased infectivity resulting from heat shock
    • Smejkal, R. M., R. Wolff, and J. G. Olenick. 1988. Leishmania braziliensis panamensis: increased infectivity resulting from heat shock. Exp. Parasitol. 65:1-9.
    • (1988) Exp. Parasitol. , vol.65 , pp. 1-9
    • Smejkal, R.M.1    Wolff, R.2    Olenick, J.G.3
  • 43
    • 0025787706 scopus 로고
    • Changes in Hsp70 alter thermotolerance and heat-shock regulation in Drosophila
    • Solomon, J. M., J. M. Rossi, K. Golic, T. McGarry, and S. Lindquist. 1991. Changes in Hsp70 alter thermotolerance and heat-shock regulation in Drosophila. New Biol. 3:1106-1120.
    • (1991) New Biol. , vol.3 , pp. 1106-1120
    • Solomon, J.M.1    Rossi, J.M.2    Golic, K.3    McGarry, T.4    Lindquist, S.5
  • 44
    • 0026571094 scopus 로고
    • The CIp proteins: Proteolysis regulators or molecular chaperones?
    • Squires, C., and C. L. Squires. 1992. The CIp proteins: proteolysis regulators or molecular chaperones? J. Bacteriol. 174:1081-1085.
    • (1992) J. Bacteriol. , vol.174 , pp. 1081-1085
    • Squires, C.1    Squires, C.L.2
  • 45
    • 0021866913 scopus 로고
    • Heat shock genes: Regulatory role for differentiation in parasitic protozoa
    • van der Ploeg, L. H. T., S. H. Giannini, and C. R. Cantor. 1985. Heat shock genes: regulatory role for differentiation in parasitic protozoa. Science 228: 1443-1446.
    • (1985) Science , vol.228 , pp. 1443-1446
    • Van Der Ploeg, L.H.T.1    Giannini, S.H.2    Cantor, C.R.3
  • 46
    • 0029257254 scopus 로고
    • Heat-shock proteins Hsp104 and Hsp70 reactivate mRNA splicing after heat inactivation
    • Vogel, J. L., D. A. Parsell, and S. Lindquist. 1995. Heat-shock proteins Hsp104 and Hsp70 reactivate mRNA splicing after heat inactivation. Curr. Biol. 5:306-317.
    • (1995) Curr. Biol. , vol.5 , pp. 306-317
    • Vogel, J.L.1    Parsell, D.A.2    Lindquist, S.3
  • 47
    • 0002176468 scopus 로고
    • Stress proteins and infectious diseases
    • R. I. Morimoto. A. Tissières, and C. Georgopoulos (ed.), Cold Spring Harbor Laboratory Press, Plainview, N.Y.
    • Young, D. B., A. Mehlert, and D. F. Smith. 1990. Stress proteins and infectious diseases, p. 131-166. In R. I. Morimoto. A. Tissières, and C. Georgopoulos (ed.), Stress proteins in biology and medicine. Cold Spring Harbor Laboratory Press, Plainview, N.Y.
    • (1990) Stress Proteins in Biology and Medicine , pp. 131-166
    • Young, D.B.1    Mehlert, A.2    Smith, D.F.3
  • 48
    • 0028061958 scopus 로고
    • The role of pH and temperature in the development of Leishmania parasites
    • Zilberstein, D., and M. Shapira. 1994. The role of pH and temperature in the development of Leishmania parasites. Annu. Rev. Microbiol. 48:449-470.
    • (1994) Annu. Rev. Microbiol. , vol.48 , pp. 449-470
    • Zilberstein, D.1    Shapira, M.2


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