메뉴 건너뛰기




Volumn 127, Issue 21, 2014, Pages 4762-4773

A small heat shock protein is essential for thermotolerance and intracellular survival of Leishmania donovani

Author keywords

Alphacrystallin; HSP23; Infectivity; Leishmania; Small heat shock protein; Stress tolerance

Indexed keywords

HEAT SHOCK PROTEIN 23; HEAT SHOCK PROTEIN 70; SMALL HEAT SHOCK PROTEIN; UNCLASSIFIED DRUG; PROTOZOAL PROTEIN;

EID: 84913582079     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.157297     Document Type: Article
Times cited : (59)

References (74)
  • 1
    • 84864492897 scopus 로고    scopus 로고
    • Small heat shock proteins HSP27 (HspB1), aB-crystallin (HspB5) and HSP22 (HspB8) as regulators of cell death
    • Acunzo, J., Katsogiannou, M. and Rocchi, P. (2012). Small heat shock proteins HSP27 (HspB1), aB-crystallin (HspB5) and HSP22 (HspB8) as regulators of cell death. Int. J. Biochem. Cell Biol. 44, 1622-1631.
    • (2012) Int. J. Biochem. Cell Biol. , vol.44 , pp. 1622-1631
    • Acunzo, J.1    Katsogiannou, M.2    Rocchi, P.3
  • 2
    • 84878397984 scopus 로고    scopus 로고
    • The loss of virulence of histone H1 overexpressing Leishmania donovani parasites is directly associated with a reduction of HSP83 rate of translation
    • Alexandratos, A., Clos, J., Samiotaki, M., Efstathiou, A., Panayotou, G., Soteriadou, K. and Smirlis, D. (2013). The loss of virulence of histone H1 overexpressing Leishmania donovani parasites is directly associated with a reduction of HSP83 rate of translation. Mol. Microbiol. 88, 1015-1031.
    • (2013) Mol. Microbiol. , vol.88 , pp. 1015-1031
    • Alexandratos, A.1    Clos, J.2    Samiotaki, M.3    Efstathiou, A.4    Panayotou, G.5    Soteriadou, K.6    Smirlis, D.7
  • 4
    • 0000694228 scopus 로고
    • Molecular weight estimations of proteins by electrophoresis in polyacrylamide gels of graded porosity
    • Andersson, L., Borg, H. and Mikaelsson, M. (1972). Molecular weight estimations of proteins by electrophoresis in polyacrylamide gels of graded porosity. FEBS Lett. 20, 199-202.
    • (1972) FEBS Lett. , vol.20 , pp. 199-202
    • Andersson, L.1    Borg, H.2    Mikaelsson, M.3
  • 5
    • 0023697402 scopus 로고
    • Dynamic changes in the structure and intracellular locale of the mammalian low-molecular-weight heat shock protein
    • Arrigo, A. P., Suhan, J. P. and Welch, W. J. (1988). Dynamic changes in the structure and intracellular locale of the mammalian low-molecular-weight heat shock protein. Mol. Cell. Biol. 8, 5059-5071.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 5059-5071
    • Arrigo, A.P.1    Suhan, J.P.2    Welch, W.J.3
  • 6
    • 0038381514 scopus 로고    scopus 로고
    • Heat shock protein 90 function is essential for Plasmodium falciparum growth in human erythrocytes
    • Banumathy, G., Singh, V., Pavithra, S. R. and Tatu, U. (2003). Heat shock protein 90 function is essential for Plasmodium falciparum growth in human erythrocytes. J. Biol. Chem. 278, 18336-18345.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18336-18345
    • Banumathy, G.1    Singh, V.2    Pavithra, S.R.3    Tatu, U.4
  • 8
    • 0026674542 scopus 로고
    • Axenic cultivation and characterization of Leishmania mexicana amastigote-like forms
    • Bates, P. A., Robertson, C. D., Tetley, L. and Coombs, G. H. (1992). Axenic cultivation and characterization of Leishmania mexicana amastigote-like forms. Parasitology 105, 193-202.
    • (1992) Parasitology , vol.105 , pp. 193-202
    • Bates, P.A.1    Robertson, C.D.2    Tetley, L.3    Coombs, G.H.4
  • 9
    • 0024500879 scopus 로고
    • Interaction of Drosophila 27,000 Mr heat-shock protein with the nucleus of heat-shocked and ecdysonestimulated culture cells
    • Beaulieu, J. F., Arrigo, A. P. and Tanguay, R. M. (1989). Interaction of Drosophila 27,000 Mr heat-shock protein with the nucleus of heat-shocked and ecdysonestimulated culture cells. J. Cell Sci. 92, 29-36.
    • (1989) J. Cell Sci. , vol.92 , pp. 29-36
    • Beaulieu, J.F.1    Arrigo, A.P.2    Tanguay, R.M.3
  • 10
    • 0032078233 scopus 로고    scopus 로고
    • Targeted disruption of the bradyzoite-specific gene BAG1 does not prevent tissue cyst formation in Toxoplasma gondii
    • Bohne, W., Hunter, C. A., White, M. W., Ferguson, D. J., Gross, U. and Roos, D. S. (1998). Targeted disruption of the bradyzoite-specific gene BAG1 does not prevent tissue cyst formation in Toxoplasma gondii. Mol. Biochem. Parasitol. 92, 291-301.
    • (1998) Mol. Biochem. Parasitol. , vol.92 , pp. 291-301
    • Bohne, W.1    Hunter, C.A.2    White, M.W.3    Ferguson, D.J.4    Gross, U.5    Roos, D.S.6
  • 11
    • 0029143254 scopus 로고
    • High constitutive levels of heatshock proteins in human-pathogenic parasites of the genus Leishmania
    • Brandau, S., Dresel, A. and Clos, J. (1995). High constitutive levels of heatshock 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
  • 12
    • 0032924953 scopus 로고    scopus 로고
    • Hsp90 & Co.-a holding for folding
    • Buchner, J. (1999). Hsp90 & Co.-a holding for folding. Trends Biochem. Sci. 24, 136-141.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 136-141
    • Buchner, J.1
  • 13
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau, B., Weissman, J. and Horwich, A. (2006). Molecular chaperones and protein quality control. Cell 125, 443-451.
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 14
    • 51249103203 scopus 로고    scopus 로고
    • Identification of a Leishmania infantum gene mediating resistance to miltefosine and SbIII
    • Choudhury, K., Zander, D., Kube, M., Reinhardt, R. and Clos, J. (2008). Identification of a Leishmania infantum gene mediating resistance to miltefosine and SbIII. Int. J. Parasitol. 38, 1411-1423.
    • (2008) Int. J. Parasitol. , vol.38 , pp. 1411-1423
    • Choudhury, K.1    Zander, D.2    Kube, M.3    Reinhardt, R.4    Clos, J.5
  • 16
    • 0027995077 scopus 로고
    • pJC20 and pJC40 -two high-copy-number vectors for T7 RNA polymerase-dependent expression of recombinant genes in Escherichia coli
    • Clos, J. and Brandau, S. (1994). pJC20 and pJC40 -two high-copy-number vectors for T7 RNA polymerase-dependent expression of recombinant genes in Escherichia coli. Protein Expr. Purif. 5, 133-137.
    • (1994) Protein Expr. Purif. , vol.5 , pp. 133-137
    • Clos, J.1    Brandau, S.2
  • 17
    • 0025606431 scopus 로고
    • Molecular cloning and expression of a hexameric Drosophila heat shock factor subject to negative regulation
    • Clos, J., Westwood, J. T., Becker, P. B., Wilson, S., Lambert, K. and Wu, C. (1990). Molecular cloning and expression of a hexameric Drosophila heat shock factor subject to negative regulation. Cell 63, 1085-1097.
    • (1990) Cell , vol.63 , pp. 1085-1097
    • Clos, J.1    Westwood, J.T.2    Becker, P.B.3    Wilson, S.4    Lambert, K.5    Wu, C.6
  • 19
    • 13244255415 scopus 로고    scopus 로고
    • MUSCLE: a multiple sequence alignment method with reduced time and space complexity
    • Edgar, R. C. (2004a). MUSCLE: a multiple sequence alignment method with reduced time and space complexity. BMC Bioinformatics 5, 113.
    • (2004) BMC Bioinformatics , vol.5 , pp. 113
    • Edgar, R.C.1
  • 20
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar, R. C. (2004b). MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 32, 1792-1797.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 21
    • 0033057848 scopus 로고    scopus 로고
    • Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology
    • Feder, M. E. and Hofmann, G. E. (1999). Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology. Annu. Rev. Physiol. 61, 243-282.
    • (1999) Annu. Rev. Physiol. , vol.61 , pp. 243-282
    • Feder, M.E.1    Hofmann, G.E.2
  • 22
    • 43249105354 scopus 로고    scopus 로고
    • p23/Sba1p protects against Hsp90 inhibitors independently of its intrinsic chaperone activity
    • Forafonov, F., Toogun, O. A., Grad, I., Suslova, E, Freeman, B. C. and Picard, D. (2008). p23/Sba1p protects against Hsp90 inhibitors independently of its intrinsic chaperone activity. Mol. Cell. Biol. 28, 3446-56.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 3446-3456
    • Forafonov, F.1    Toogun, O.A.2    Grad, I.3    Suslova, E.4    Freeman, B.C.5    Picard, D.6
  • 24
    • 27144448839 scopus 로고    scopus 로고
    • Some like it hot: the structure and function of small heat-shock proteins
    • Haslbeck, M., Franzmann, T., Weinfurtner, D. and Buchner, J. (2005). Some like it hot: the structure and function of small heat-shock proteins. Nat. Struct. Mol. Biol. 12, 842-846.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 842-846
    • Haslbeck, M.1    Franzmann, T.2    Weinfurtner, D.3    Buchner, J.4
  • 25
    • 84904251225 scopus 로고    scopus 로고
    • No stress-Hsp90 and the signal transduction in Leishmania
    • Hombach, A. and Clos, J. (2014). No stress-Hsp90 and the signal transduction in Leishmania. Parasitol. 141, 1156-1166.
    • (2014) Parasitol. , vol.141 , pp. 1156-1166
    • Hombach, A.1    Clos, J.2
  • 26
    • 84874974453 scopus 로고    scopus 로고
    • The Hsp90-Sti1 interaction is critical for Leishmania donovani proliferation in both life cycle stages
    • Hombach, A., Ommen, G., Chrobak, M. and Clos, J. (2013). The Hsp90-Sti1 interaction is critical for Leishmania donovani proliferation in both life cycle stages. Cell. Microbiol. 15, 585-600.
    • (2013) Cell. Microbiol. , vol.15 , pp. 585-600
    • Hombach, A.1    Ommen, G.2    Chrobak, M.3    Clos, J.4
  • 27
    • 0037325497 scopus 로고    scopus 로고
    • Alpha-crystallin
    • Horwitz, J. (2003). Alpha-crystallin. Exp. Eye Res. 76, 145-153.
    • (2003) Exp. Eye Res. , vol.76 , pp. 145-153
    • Horwitz, J.1
  • 28
  • 29
    • 0028958754 scopus 로고
    • A member of the ClpB family of stress proteins is expressed during heat shock in Leishmania spp
    • Hübel, A., Brandau, S., Dresel, A. and Clos, J. (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
  • 30
    • 1842337450 scopus 로고    scopus 로고
    • Leishmania major Hsp100 is required chiefly in the mammalian stage of the parasite
    • Hübel, A., Krobitsch, S., Hörauf, A. and Clos, J. (1997). Leishmania major Hsp100 is required chiefly in the mammalian stage of the parasite. Mol. Cell. Biol. 17, 5987-5995.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5987-5995
    • Hübel, A.1    Krobitsch, S.2    Hörauf, A.3    Clos, J.4
  • 31
    • 0021735783 scopus 로고
    • Leishmanial differentiation in vitro: induction of heat shock proteins
    • Hunter, K. W., Cook, C. L. and Hayunga, E. G. (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
  • 32
    • 84857048585 scopus 로고    scopus 로고
    • Evolution and function of diverse Hsp90 homologs and cochaperone proteins
    • Johnson, J. L. (2012). Evolution and function of diverse Hsp90 homologs and cochaperone proteins. Biochim. Biophys. Acta 1823, 607-613.
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 607-613
    • Johnson, J.L.1
  • 33
    • 58149271606 scopus 로고    scopus 로고
    • Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms
    • Johnson, J. L. and Brown, C. (2009). Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms. Cell Stress Chaperones 14, 83-94.
    • (2009) Cell Stress Chaperones , vol.14 , pp. 83-94
    • Johnson, J.L.1    Brown, C.2
  • 34
    • 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., Coburn, C. M. and Beverley, S. M. (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
  • 35
    • 84913547300 scopus 로고    scopus 로고
    • Untersuchungen zur rolle des Hitzeschock-Proteins HSP100 während der stadienentwicklung von Leishmania-parasiten
    • Hamburg: University of Hamburg
    • Krobitsch, S. (1998). Untersuchungen zur rolle des Hitzeschock-Proteins HSP100 während der stadienentwicklung von Leishmania-parasiten. In Faculty of Biology. Hamburg: University of Hamburg.
    • (1998) Faculty of Biology
    • Krobitsch, S.1
  • 36
    • 0032852245 scopus 로고    scopus 로고
    • A novel role for 100 kD heat shock proteins in the parasite Leishmania donovani
    • Krobitsch, S. and Clos, J. (1999). A novel role for 100 kD heat shock proteins in the parasite Leishmania donovani. Cell Stress Chaperones 4, 191-198.
    • (1999) Cell Stress Chaperones , vol.4 , pp. 191-198
    • Krobitsch, S.1    Clos, J.2
  • 37
    • 0034653307 scopus 로고    scopus 로고
    • Cross-species homologous recombination in Leishmania donovani reveals the sites of integration
    • Krobitsch, S. and Clos, J. (2000). Cross-species homologous recombination in Leishmania donovani reveals the sites of integration. Mol. Biochem. Parasitol. 107, 123-128.
    • (2000) Mol. Biochem. Parasitol. , vol.107 , pp. 123-128
    • Krobitsch, S.1    Clos, J.2
  • 38
    • 0032513205 scopus 로고    scopus 로고
    • Leishmania donovani heat shock protein 100. Characterization and function in amastigote stage differentiation
    • Krobitsch, S., Brandau, S., Hoyer, C., Schmetz, C., Hübel, A. and Clos, J. (1998). Leishmania donovani heat shock protein 100. Characterization and function in amastigote stage differentiation. J. Biol. Chem. 273, 6488-6494.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6488-6494
    • Krobitsch, S.1    Brandau, S.2    Hoyer, C.3    Schmetz, C.4    Hübel, A.5    Clos, J.6
  • 39
    • 0024331981 scopus 로고
    • Transfection of Leishmania enriettii and expression of chloramphenicol acetyltransferase gene
    • Laban, A. and Wirth, D. F. (1989). Transfection of Leishmania enriettii 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
  • 40
    • 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
  • 41
    • 0033529033 scopus 로고    scopus 로고
    • Molecular chaperones: the busy life of Hsp90
    • Mayer, M. P. and Bukau, B. (1999). Molecular chaperones: the busy life of Hsp90. Curr. Biol. 9, R322-R325.
    • (1999) Curr. Biol. , vol.9 , pp. R322-R325
    • Mayer, M.P.1    Bukau, B.2
  • 42
    • 84862015365 scopus 로고    scopus 로고
    • Small but crucial: the novel small heat shock protein Hsp21 mediates stress adaptation and virulence in Candida albicans
    • Mayer, F. L., Wilson, D., Jacobsen, I. D., Miramón, P., Slesiona, S., Bohovych, I. M., Brown, A. J. and Hube, B. (2012). Small but crucial: the novel small heat shock protein Hsp21 mediates stress adaptation and virulence in Candida albicans. PLoS ONE 7, e38584.
    • (2012) PLoS ONE , vol.7
    • Mayer, F.L.1    Wilson, D.2    Jacobsen, I.D.3    Miramón, P.4    Slesiona, S.5    Bohovych, I.M.6    Brown, A.J.7    Hube, B.8
  • 45
    • 0001806571 scopus 로고
    • The stress response, function of the proteins, and perspectives
    • (ed. R. I. Morimoto, A. Tissières and C. Georgopoulos), Plainview, NY: Cold Spring Harbor Laboratory Press
    • Morimoto, R. I., Tissieres, A. and Georgopoulos, C. (1990). The stress response, function of the proteins, and perspectives. In Stress Proteins in Biology and Medicine (ed. R. I. Morimoto, A. Tissières and C. Georgopoulos), pp. 1-36. Plainview, NY: Cold Spring Harbor Laboratory Press.
    • (1990) Stress Proteins in Biology and Medicine , pp. 1-36
    • Morimoto, R.I.1    Tissieres, A.2    Georgopoulos, C.3
  • 46
    • 0029037110 scopus 로고
    • Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase
    • Nathan, D. F. and Lindquist, S. (1995). Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase. Mol. Cell. Biol. 15, 3917-3925.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3917-3925
    • Nathan, D.F.1    Lindquist, S.2
  • 47
    • 0034983973 scopus 로고    scopus 로고
    • Geldanamycin: the prototype of a class of antitumor drugs targeting the heat shock protein 90 family of molecular chaperones
    • Ochel, H. J., Eichhorn, K. and Gademann, G. (2001). Geldanamycin: the prototype of a class of antitumor drugs targeting the heat shock protein 90 family of molecular chaperones. Cell Stress Chaperones 6, 105-112.
    • (2001) Cell Stress Chaperones , vol.6 , pp. 105-112
    • Ochel, H.J.1    Eichhorn, K.2    Gademann, G.3
  • 48
    • 84859652629 scopus 로고    scopus 로고
    • Heat shock proteins in protozoan parasites -Leishmania spp
    • (ed. S. Calderwood, G. Santoro and G. Pockley), Berlin: Springer
    • Ommen, G. and Clos, J. (2009). Heat shock proteins in protozoan parasites -Leishmania spp. In Prokaryotic and Eukaryotic Heat Shock Proteins in Infectious Disease (ed. S. Calderwood, G. Santoro and G. Pockley), pp. 135-151. Berlin: Springer.
    • (2009) Prokaryotic and Eukaryotic Heat Shock Proteins in Infectious Disease , pp. 135-151
    • Ommen, G.1    Clos, J.2
  • 49
    • 59749090972 scopus 로고    scopus 로고
    • One-step generation of double-allele gene replacement mutants in Leishmania donovani
    • Ommen, G., Lorenz, S. and Clos, J. (2009). One-step generation of double-allele gene replacement mutants in Leishmania donovani. Int. J. Parasitol. 39, 541-546.
    • (2009) Int. J. Parasitol. , vol.39 , pp. 541-546
    • Ommen, G.1    Lorenz, S.2    Clos, J.3
  • 50
    • 77955653279 scopus 로고    scopus 로고
    • The co-chaperone SGT of Leishmania donovani is essential for the parasite's viability
    • Ommen, G., Chrobak, M. and Clos, J. (2010). The co-chaperone SGT of Leishmania donovani is essential for the parasite's viability. Cell Stress Chaperones 15, 443-455.
    • (2010) Cell Stress Chaperones , vol.15 , pp. 443-455
    • Ommen, G.1    Chrobak, M.2    Clos, J.3
  • 51
    • 78649667345 scopus 로고    scopus 로고
    • Heat shock protein 90 as a drug target against protozoan infections: biochemical characterization of HSP90 from Plasmodium falciparum and Trypanosoma evansi and evaluation of its inhibitor as a candidate drug
    • Pallavi, R., Roy, N., Nageshan, R. K., Talukdar, P., Pavithra, S. R., Reddy, R., Venketesh, S., Kumar, R., Gupta, A. K., Singh, R. K. et al. (2010). Heat shock protein 90 as a drug target against protozoan infections: biochemical characterization of HSP90 from Plasmodium falciparum and Trypanosoma evansi and evaluation of its inhibitor as a candidate drug. J. Biol. Chem. 285, 37964-37975.
    • (2010) J. Biol. Chem. , vol.285 , pp. 37964-37975
    • Pallavi, R.1    Roy, N.2    Nageshan, R.K.3    Talukdar, P.4    Pavithra, S.R.5    Reddy, R.6    Venketesh, S.7    Kumar, R.8    Gupta, A.K.9    Singh, R.K.10
  • 52
    • 0000675009 scopus 로고
    • Heat shock proteins and stress tolerance
    • (ed. R. I. Morimoto, A. Tissières and C. Georgopoulos), Plainview, NY: Cold Spring Harbor Laboratory Press
    • Parsell, D. A. and Lindquist, S. (1994). Heat shock proteins and stress tolerance. In The Biology of Heat Shock Proteins and Molecular Chaperones (ed. R. I. Morimoto, A. Tissières and C. Georgopoulos), pp. 457-494. Plainview, NY: Cold Spring Harbor Laboratory Press.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 457-494
    • Parsell, D.A.1    Lindquist, S.2
  • 53
    • 0027981247 scopus 로고
    • Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes
    • Parsell, D. A., Kowal, A. S. and Lindquist, S. (1994). Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes. 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
  • 54
    • 0036810352 scopus 로고    scopus 로고
    • Heat-shock protein 90, a chaperone for folding and regulation
    • Picard, D. (2002). Heat-shock protein 90, a chaperone for folding and regulation. Cell. Mol. Life Sci. 59, 1640-1648.
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1640-1648
    • Picard, D.1
  • 55
    • 84907110208 scopus 로고
    • Isolation of viral IgY antibodies from yolks of immunized hens
    • Polson, A., von Wechmar, M. B. and van Regenmortel, M. H. V. (1980). Isolation of viral IgY antibodies from yolks of immunized hens. Immunol. Commun. 9, 475-493.
    • (1980) Immunol. Commun. , vol.9 , pp. 475-493
    • Polson, A.1    von Wechmar, M.B.2    van Regenmortel, M.H.V.3
  • 56
  • 57
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt, W. B. and Toft, D. O. (2003). Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp. Biol. Med. (Maywood) 228, 111-133.
    • (2003) Exp. Biol. Med. (Maywood) , vol.228 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 58
    • 84857051938 scopus 로고    scopus 로고
    • The 'active life' of Hsp90 complexes
    • Prodromou, C. (2012). The 'active life' of Hsp90 complexes. Biochim. Biophys. Acta 1823, 614-623.
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 614-623
    • Prodromou, C.1
  • 59
    • 77952828769 scopus 로고    scopus 로고
    • Overexpression of a single Leishmania major gene enhances parasite infectivity in vivo and in vitro
    • Reiling, L., Chrobak, M., Schmetz, C. and Clos, J. (2010). Overexpression of a single Leishmania major gene enhances parasite infectivity in vivo and in vitro. Mol. Microbiol. 76, 1175-1190.
    • (2010) Mol. Microbiol. , vol.76 , pp. 1175-1190
    • Reiling, L.1    Chrobak, M.2    Schmetz, C.3    Clos, J.4
  • 61
    • 0004262043 scopus 로고    scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Sambrook, J. and Russell, D. W. (2001). Molecular Cloning. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
    • (2001) Molecular Cloning
    • Sambrook, J.1    Russell, D.W.2
  • 62
    • 0025193343 scopus 로고
    • HSP104 required for induced thermotolerance
    • Sanchez, Y. and Lindquist, S. L. (1990). HSP104 required for induced thermotolerance. Science 248, 1112-1115.
    • (1990) Science , vol.248 , pp. 1112-1115
    • Sanchez, Y.1    Lindquist, S.L.2
  • 63
    • 0026523626 scopus 로고
    • Hsp104 is required for tolerance to many forms of stress
    • Sanchez, Y., Taulien, J., Borkovich, K. A. and Lindquist, S. (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
  • 64
    • 0030219939 scopus 로고    scopus 로고
    • HSP100/ Clp proteins: a common mechanism explains diverse functions
    • Schirmer, E. C., Glover, J. R., Singer, M. A. and Lindquist, S. (1996). HSP100/ Clp proteins: a common mechanism explains diverse functions. Trends Biochem. Sci. 21, 289-296.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 289-296
    • Schirmer, E.C.1    Glover, J.R.2    Singer, M.A.3    Lindquist, S.4
  • 67
    • 0032416104 scopus 로고    scopus 로고
    • Molecular chaperones: biology and prospects for pharmacological intervention
    • Smith, D. F., Whitesell, L. and Katsanis, E. (1998). Molecular chaperones: biology and prospects for pharmacological intervention. Pharmacol. Rev. 50, 493-514.
    • (1998) Pharmacol. Rev. , vol.50 , pp. 493-514
    • Smith, D.F.1    Whitesell, L.2    Katsanis, E.3
  • 68
    • 33846554383 scopus 로고    scopus 로고
    • A proteomics screen implicates HSP83 and a small kinetoplastid calpain-related protein in drug resistance in Leishmania donovani clinical field isolates by modulating drug-induced programmed cell death
    • Vergnes, B., Gourbal, B., Girard, I., Sundar, S., Drummelsmith, J. and Ouellette, M. (2007). A proteomics screen implicates HSP83 and a small kinetoplastid calpain-related protein in drug resistance in Leishmania donovani clinical field isolates by modulating drug-induced programmed cell death. Mol. Cell. Proteomics 6, 88-101.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 88-101
    • Vergnes, B.1    Gourbal, B.2    Girard, I.3    Sundar, S.4    Drummelsmith, J.5    Ouellette, M.6
  • 70
    • 0025955517 scopus 로고
    • Stress-induced oligomerization and chromosomal relocalization of heat-shock factor
    • Westwood, J. T., Clos, J. and Wu, C. (1991). Stress-induced oligomerization and chromosomal relocalization of heat-shock factor. Nature 353, 822-827.
    • (1991) Nature , vol.353 , pp. 822-827
    • Westwood, J.T.1    Clos, J.2    Wu, C.3
  • 71
    • 84864488251 scopus 로고    scopus 로고
    • Small heat shock proteins and the cytoskeleton: an essential interplay for cell integrity?
    • Wettstein, G., Bellaye, P. S., Micheau, O. and Bonniaud, P. (2012). Small heat shock proteins and the cytoskeleton: an essential interplay for cell integrity? Int. J. Biochem. Cell Biol. 44, 1680-1686.
    • (2012) Int. J. Biochem. Cell Biol. , vol.44 , pp. 1680-1686
    • Wettstein, G.1    Bellaye, P.S.2    Micheau, O.3    Bonniaud, P.4
  • 72
    • 0035203992 scopus 로고    scopus 로고
    • Heat shock protein 90 homeostasis controls stage differentiation in Leishmania donovani
    • Wiesgigl, M. and Clos, J. (2001). Heat shock protein 90 homeostasis controls stage differentiation in Leishmania donovani. Mol. Biol. Cell 12, 3307-3316.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3307-3316
    • Wiesgigl, M.1    Clos, J.2
  • 73
    • 0035698491 scopus 로고    scopus 로고
    • Small heat shock protein p26 associates with nuclear lamins and HSP70 in nuclei and nuclear matrix fractions from stressed cells
    • Willsie, J. K. and Clegg, J. S. (2002). Small heat shock protein p26 associates with nuclear lamins and HSP70 in nuclei and nuclear matrix fractions from stressed cells. J. Cell. Biochem. 84, 601-614.
    • (2002) J. Cell. Biochem. , vol.84 , pp. 601-614
    • Willsie, J.K.1    Clegg, J.S.2
  • 74
    • 26844478297 scopus 로고    scopus 로고
    • Stage-specific expression of the mitochondrial co-chaperonin of Leishmania donovani, CPN10
    • Zamora-Veyl, F. B., Kroemer, M., Zander, D. and Clos, J. (2005). Stage-specific expression of the mitochondrial co-chaperonin of Leishmania donovani, CPN10. Kinetoplastid Biol. Dis. 4, 3.
    • (2005) Kinetoplastid Biol. Dis. , vol.4 , pp. 3
    • Zamora-Veyl, F.B.1    Kroemer, M.2    Zander, D.3    Clos, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.