메뉴 건너뛰기




Volumn 123, Issue 2, 2009, Pages 182-189

Trypanosoma cruzi SHSP16: Characterization of an α-crystallin small heat shock protein

Author keywords

Crystallin small heat shock protein; Heat shock; SHSP16; Trypanosoma cruzi

Indexed keywords

HEAT SHOCK PROTEIN; MALATE DEHYDROGENASE; SMALL HEAT SHOCK PROTEIN 16; UNCLASSIFIED DRUG;

EID: 68949169092     PISSN: 00144894     EISSN: 10902449     Source Type: Journal    
DOI: 10.1016/j.exppara.2009.06.019     Document Type: Article
Times cited : (25)

References (52)
  • 2
    • 2142768810 scopus 로고    scopus 로고
    • Chaperone activity of cytosolic small heat shock proteins from wheat
    • Basha E., Lee G.J., Demeler B., and Vierling E. Chaperone activity of cytosolic small heat shock proteins from wheat. Eur. J. Biochem. 271 (2004) 1426-1436
    • (2004) Eur. J. Biochem. , vol.271 , pp. 1426-1436
    • Basha, E.1    Lee, G.J.2    Demeler, B.3    Vierling, E.4
  • 3
    • 22244441812 scopus 로고    scopus 로고
    • The genome of the African trypanosome Trypanosoma brucei
    • Berriman M., Ghedin E., Hertz-Fowler C., et al. The genome of the African trypanosome Trypanosoma brucei. Science 309 (2005) 416-422
    • (2005) Science , vol.309 , pp. 416-422
    • Berriman, M.1    Ghedin, E.2    Hertz-Fowler, C.3
  • 5
    • 19444377616 scopus 로고    scopus 로고
    • The stabilization of housekeeping transcripts in Trypanosoma cruzi epimastigotes evidences a global regulation of RNA decay during stationary phase
    • Cevallos A.M., Pérez-Escobar M., Espinosa N., Herrera J., López-Villaseñor I., and Hernández R. The stabilization of housekeeping transcripts in Trypanosoma cruzi epimastigotes evidences a global regulation of RNA decay during stationary phase. FEMS Microbiol. Lett. 246 (2005) 259-264
    • (2005) FEMS Microbiol. Lett. , vol.246 , pp. 259-264
    • Cevallos, A.M.1    Pérez-Escobar, M.2    Espinosa, N.3    Herrera, J.4    López-Villaseñor, I.5    Hernández, R.6
  • 6
    • 0032583153 scopus 로고    scopus 로고
    • Genetic nomenclature for Trypanosoma and Leishmania
    • Clayton C., Adams M., Almeida R., et al. Genetic nomenclature for Trypanosoma and Leishmania. Mol. Biochem. Parasitol. 97 (1998) 221-224
    • (1998) Mol. Biochem. Parasitol. , vol.97 , pp. 221-224
    • Clayton, C.1    Adams, M.2    Almeida, R.3
  • 7
    • 0032077156 scopus 로고    scopus 로고
    • Genealogy of the alpha-crystallin-small heat-shock protein superfamily
    • de Jong W.W., Caspers G.J., and Leunissen J.A.M. Genealogy of the alpha-crystallin-small heat-shock protein superfamily. Int. J. Biol. Macromol. 22 (1998) 151-162
    • (1998) Int. J. Biol. Macromol. , vol.22 , pp. 151-162
    • de Jong, W.W.1    Caspers, G.J.2    Leunissen, J.A.M.3
  • 8
    • 29144515438 scopus 로고    scopus 로고
    • Differential subcellular localization of members of the Toxoplasma gondii small heat shock protein family
    • de Miguel N., Echeverria P.C., and Angel S.O. Differential subcellular localization of members of the Toxoplasma gondii small heat shock protein family. Eukaryot. Cell 4 (2005) 1990-1997
    • (2005) Eukaryot. Cell , vol.4 , pp. 1990-1997
    • de Miguel, N.1    Echeverria, P.C.2    Angel, S.O.3
  • 9
    • 0036242661 scopus 로고    scopus 로고
    • Basic cell biology of Trypanosoma cruzi
    • De Souza W. Basic cell biology of Trypanosoma cruzi. Curr. Pharm. Des. 8 (2002) 269-285
    • (2002) Curr. Pharm. Des. , vol.8 , pp. 269-285
    • De Souza, W.1
  • 10
    • 0033057735 scopus 로고    scopus 로고
    • Polymorphisms at the topoisomerase II gene locus provide more evidence for the partition of Trypanosoma cruzi into two major groups
    • Dos Santos W.G., and Buck G.A. Polymorphisms at the topoisomerase II gene locus provide more evidence for the partition of Trypanosoma cruzi into two major groups. J. Eukaryot. Microbiol. 46 (1999) 17-23
    • (1999) J. Eukaryot. Microbiol. , vol.46 , pp. 17-23
    • Dos Santos, W.G.1    Buck, G.A.2
  • 11
    • 0023125790 scopus 로고
    • The genome of Trypanosoma cruzi contains a constitutively expressed, tandemly arranged multicopy gene homologous to a major heat shock protein
    • Dragon E.A., Sias S.R., Kato E.A., and Gabe J.D. The genome of Trypanosoma cruzi contains a constitutively expressed, tandemly arranged multicopy gene homologous to a major heat shock protein. Mol. Cell. Biol. 7 (1987) 1271-1275
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 1271-1275
    • Dragon, E.A.1    Sias, S.R.2    Kato, E.A.3    Gabe, J.D.4
  • 12
    • 22244453726 scopus 로고    scopus 로고
    • The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas disease
    • El-Sayed N.M., Myler P.J., Bartholomeu D.C., et al. The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas disease. Science 309 (2005) 409-415
    • (2005) Science , vol.309 , pp. 409-415
    • El-Sayed, N.M.1    Myler, P.J.2    Bartholomeu, D.C.3
  • 13
    • 17644442993 scopus 로고    scopus 로고
    • Genotype and virulence correlation within Mexican stocks of Trypanosoma cruzi isolated from patients
    • Espinoza B., Vera-Cruz J.M., González H., Ortega E., and Hernández R. Genotype and virulence correlation within Mexican stocks of Trypanosoma cruzi isolated from patients. Acta Trop. 15 (1998) 63-72
    • (1998) Acta Trop. , vol.15 , pp. 63-72
    • Espinoza, B.1    Vera-Cruz, J.M.2    González, H.3    Ortega, E.4    Hernández, R.5
  • 14
    • 17044373554 scopus 로고    scopus 로고
    • Gene characterization and predicted protein structure of the mitochondrial chaperonin HSP10 of Trypanosoma cruzi
    • Fernandes M., Silva R., Rössle S.C., Bisch P.M., Rondinelli E., and Ürményi T.P. Gene characterization and predicted protein structure of the mitochondrial chaperonin HSP10 of Trypanosoma cruzi. Gene 349 (2005) 135-142
    • (2005) Gene , vol.349 , pp. 135-142
    • Fernandes, M.1    Silva, R.2    Rössle, S.C.3    Bisch, P.M.4    Rondinelli, E.5    Ürményi, T.P.6
  • 16
    • 33646166507 scopus 로고    scopus 로고
    • Identification of a highly conserved Pro-Gly doublet in non-animal small heat shock proteins and characterization of its structural and functional roles in Mycobacterium tuberculosis Hsp16.3
    • Fu X., and Chang Z. Identification of a highly conserved Pro-Gly doublet in non-animal small heat shock proteins and characterization of its structural and functional roles in Mycobacterium tuberculosis Hsp16.3. Biochemistry (Moscow) 71 Suppl. 1 (2006) S83-S90
    • (2006) Biochemistry (Moscow) , vol.71 , Issue.SUPPL. 1
    • Fu, X.1    Chang, Z.2
  • 18
    • 0030218808 scopus 로고    scopus 로고
    • Characterization and cellular distribution of heat-shock proteins HSP70 and HSP60 in Trypanosoma cruzi
    • Giambiagi-de Marval M., Souto-Padrón T., and Rondinelli E. Characterization and cellular distribution of heat-shock proteins HSP70 and HSP60 in Trypanosoma cruzi. Exp. Parasitol. 83 (1996) 335-345
    • (1996) Exp. Parasitol. , vol.83 , pp. 335-345
    • Giambiagi-de Marval, M.1    Souto-Padrón, T.2    Rondinelli, E.3
  • 19
    • 1842375705 scopus 로고    scopus 로고
    • A 16 kDa protein family overexpressed by Streptococcus thermophilus PB18 in acid environments
    • González-Márquez H., Perrin C., Bracquart P., Guimont C., and Linden G. A 16 kDa protein family overexpressed by Streptococcus thermophilus PB18 in acid environments. Microbiology 143 (1997) 1587-1594
    • (1997) Microbiology , vol.143 , pp. 1587-1594
    • González-Márquez, H.1    Perrin, C.2    Bracquart, P.3    Guimont, C.4    Linden, G.5
  • 20
    • 0037657656 scopus 로고    scopus 로고
    • Inhibition of HSP90 in Trypanosoma cruzi induces a stress response but no stage differentiation
    • Graefe S.E.B., Wiesgigl M., Gaworski I., Macdonald A., and Clos J. Inhibition of HSP90 in Trypanosoma cruzi induces a stress response but no stage differentiation. Eukaryot. Cell 1 (2002) 936-943
    • (2002) Eukaryot. Cell , vol.1 , pp. 936-943
    • Graefe, S.E.B.1    Wiesgigl, M.2    Gaworski, I.3    Macdonald, A.4    Clos, J.5
  • 21
    • 0036809333 scopus 로고    scopus 로고
    • sHsps and their role in the chaperone network
    • Haslbeck M. sHsps and their role in the chaperone network. Cell. Mol. Life Sci. 59 (2002) 1649-1657
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1649-1657
    • Haslbeck, M.1
  • 22
    • 0026483279 scopus 로고
    • Α-crystallin can function as a molecular chaperone
    • Horwitz J. Α-crystallin can function as a molecular chaperone. Proc. Natl. Acad. Sci. USA 89 (1992) 10449-10453
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 23
    • 22244437571 scopus 로고    scopus 로고
    • The genome of the kinetoplastid parasite, Leishmania major
    • Ivens A.C., Peacock C.S., Worthey E.A., et al. The genome of the kinetoplastid parasite, Leishmania major. Science 309 (2005) 436-442
    • (2005) Science , vol.309 , pp. 436-442
    • Ivens, A.C.1    Peacock, C.S.2    Worthey, E.A.3
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0031024691 scopus 로고    scopus 로고
    • A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
    • Lee G.J., Roseman A.M., Saibil H.R., and Vierling E. A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. EMBO J. 16 (1997) 659-671
    • (1997) EMBO J. , vol.16 , pp. 659-671
    • Lee, G.J.1    Roseman, A.M.2    Saibil, H.R.3    Vierling, E.4
  • 28
    • 0026778954 scopus 로고
    • DNA fingerprinting of Trypanosoma cruzi: a new tool for characterization of strains and clones
    • Macedo A.M., Martins M.S., Chiari E., and Pena S.D. DNA fingerprinting of Trypanosoma cruzi: a new tool for characterization of strains and clones. Mol. Biochem. Parasitol. 55 (1992) 147-153
    • (1992) Mol. Biochem. Parasitol. , vol.55 , pp. 147-153
    • Macedo, A.M.1    Martins, M.S.2    Chiari, E.3    Pena, S.D.4
  • 29
    • 0037197747 scopus 로고    scopus 로고
    • Sequence variation in the dihydrofolate reductase-thymidylate synthase (DHFR-TS) and trypanothione reductase (TR) genes of Trypanosoma cruzi
    • Machado C.A., and Ayala F.J. Sequence variation in the dihydrofolate reductase-thymidylate synthase (DHFR-TS) and trypanothione reductase (TR) genes of Trypanosoma cruzi. Mol. Biochem. Parasitol. 121 (2002) 33-47
    • (2002) Mol. Biochem. Parasitol. , vol.121 , pp. 33-47
    • Machado, C.A.1    Ayala, F.J.2
  • 30
    • 0033927557 scopus 로고    scopus 로고
    • Structure and function of small heat shock/alpha-crystallin proteins: established concepts and emerging ideas
    • MacRae T.H. Structure and function of small heat shock/alpha-crystallin proteins: established concepts and emerging ideas. Cell. Mol. Life Sci. 57 (2000) 899-913
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 899-913
    • MacRae, T.H.1
  • 31
    • 3242887157 scopus 로고    scopus 로고
    • CD-Search: protein domain annotations on the fly
    • Marchler-Bauer A., and Bryant S.H. CD-Search: protein domain annotations on the fly. Nucleic Acids Res. 32 W (2004) 327-331
    • (2004) Nucleic Acids Res. , vol.32 , Issue.W , pp. 327-331
    • Marchler-Bauer, A.1    Bryant, S.H.2
  • 32
    • 42949124442 scopus 로고    scopus 로고
    • The Leishmania HSP20 is antigenic during natural infections, but, as DNA vaccine, it does protect BALB/c mice against experimental L. amazonensis infection
    • Montalvo-Álvarez, A.M., Folguiera, C., Carrión, J., Monzote-Fidalgo, L., Cañavate, C., Requena, J.M. 2008. The Leishmania HSP20 is antigenic during natural infections, but, as DNA vaccine, it does protect BALB/c mice against experimental L. amazonensis infection. J. Biomed. Biotechnol. 2008, 1-9.
    • (2008) J. Biomed. Biotechnol. 2008 , pp. 1-9
    • Montalvo-Álvarez, A.M.1    Folguiera, C.2    Carrión, J.3    Monzote-Fidalgo, L.4    Cañavate, C.5    Requena, J.M.6
  • 33
    • 0036195722 scopus 로고    scopus 로고
    • Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network
    • Narberhaus F. Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network. Microbiol. Mol. Biol. Rev. 66 (2002) 64-93
    • (2002) Microbiol. Mol. Biol. Rev. , vol.66 , pp. 64-93
    • Narberhaus, F.1
  • 35
    • 0033933636 scopus 로고    scopus 로고
    • Cascaded multiple classifiers for secondary structure prediction
    • Ovali M., and King R.D. Cascaded multiple classifiers for secondary structure prediction. Prot. Sci. 9 (2000) 1162-1176
    • (2000) Prot. Sci. , vol.9 , pp. 1162-1176
    • Ovali, M.1    King, R.D.2
  • 36
    • 34250833345 scopus 로고    scopus 로고
    • Trypanosoma cruzi ribosomal protein S4: characterization of its coding locus, analysis of transcripts, and antigenicity of the protein
    • Pérez-Escobar M., Cevallos A.M., Espinoza B., Espinosa N., Martínez I., and Hernández R. Trypanosoma cruzi ribosomal protein S4: characterization of its coding locus, analysis of transcripts, and antigenicity of the protein. Mem. Inst. Oswaldo Cruz 102 (2007) 473-479
    • (2007) Mem. Inst. Oswaldo Cruz , vol.102 , pp. 473-479
    • Pérez-Escobar, M.1    Cevallos, A.M.2    Espinoza, B.3    Espinosa, N.4    Martínez, I.5    Hernández, R.6
  • 37
    • 0041935939 scopus 로고    scopus 로고
    • US National Institutes of Health, Bethesda, Maryland, USA. Available from
    • Rasband, W.S., 1997-2008. ImageJ. US National Institutes of Health, Bethesda, Maryland, USA. Available from: .
    • (1997) ImageJ
    • Rasband, W.S.1
  • 38
    • 20444423237 scopus 로고    scopus 로고
    • Identification and expression of a small heat shock protein in two lines of the endoparasitic wasp Venturia canescens
    • Reineke A. Identification and expression of a small heat shock protein in two lines of the endoparasitic wasp Venturia canescens. Comp. Biochem. Physiol. A Mol. Integr. Physiol. 141 (2005) 60-69
    • (2005) Comp. Biochem. Physiol. A Mol. Integr. Physiol. , vol.141 , pp. 60-69
    • Reineke, A.1
  • 44
    • 14644386908 scopus 로고    scopus 로고
    • Cloning and characterization of the hsp 18.55 gene, a new member of the small heat shock gene family isolated from wine Lactobacillus plantarum
    • Spano G., Beneduce L., Perrota C., and Massa S. Cloning and characterization of the hsp 18.55 gene, a new member of the small heat shock gene family isolated from wine Lactobacillus plantarum. Res. Microbiol. 156 (2005) 219-224
    • (2005) Res. Microbiol. , vol.156 , pp. 219-224
    • Spano, G.1    Beneduce, L.2    Perrota, C.3    Massa, S.4
  • 45
    • 0036375506 scopus 로고    scopus 로고
    • A critical motif for oligomerization and chaperone activity of bacterial alpha-heat shock proteins
    • Studer S., Obrist M., Lentze N., and Narberhaus F. A critical motif for oligomerization and chaperone activity of bacterial alpha-heat shock proteins. Eur. J. Biochem. 269 (2002) 3578-3586
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3578-3586
    • Studer, S.1    Obrist, M.2    Lentze, N.3    Narberhaus, F.4
  • 47
    • 0029098368 scopus 로고
    • Population genetics of parasitic protozoa and other microorganisms
    • Tibayrenc M. Population genetics of parasitic protozoa and other microorganisms. Adv. Parasitol. 36 (1995) 47-115
    • (1995) Adv. Parasitol. , vol.36 , pp. 47-115
    • Tibayrenc, M.1
  • 50
    • 31544467265 scopus 로고    scopus 로고
    • Two hybridization events define the population structure of Trypanosoma cruzi
    • Westenberger S.J., Barnabé C., Campbell D.A., and Sturm N.R. Two hybridization events define the population structure of Trypanosoma cruzi. Genetics 171 (2005) 527-543
    • (2005) Genetics , vol.171 , pp. 527-543
    • Westenberger, S.J.1    Barnabé, C.2    Campbell, D.A.3    Sturm, N.R.4
  • 51
    • 0036294520 scopus 로고    scopus 로고
    • Control of Chagas Disease
    • WHO, World Health Organization
    • WHO - World Health Organization, 2002. Control of Chagas Disease. WHO Technical Report Series, vol. 905, pp. 82-83.
    • (2002) WHO Technical Report Series , vol.905 , pp. 82-83
  • 52
    • 34247559233 scopus 로고    scopus 로고
    • Thermally induced and developmentally regulated expression of a small heat shock protein in Trichinella spiralis
    • Wu Z., Nagano I., Boonmars T., and Takahashi Y. Thermally induced and developmentally regulated expression of a small heat shock protein in Trichinella spiralis. Parasitol. Res. 101 (2007) 201-212
    • (2007) Parasitol. Res. , vol.101 , pp. 201-212
    • Wu, Z.1    Nagano, I.2    Boonmars, T.3    Takahashi, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.