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Volumn 14, Issue 3, 2007, Pages 320-322

Characterization of Plasmodium vivax heat shock protein 70 and evaluation of its value for serodiagnosis of tertian malaria

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN 70; IMMUNOGLOBULIN G; IMMUNOGLOBULIN G1; IMMUNOGLOBULIN G3; IMMUNOGLOBULIN G4; PROTOZOAL PROTEIN; RECOMBINANT PROTEIN;

EID: 34147140822     PISSN: 15566811     EISSN: None     Source Type: Journal    
DOI: 10.1128/CVI.00424-06     Document Type: Article
Times cited : (11)

References (11)
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    • (1992) J. Immunol , vol.149 , pp. 3321-3330
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  • 2
    • 0029806414 scopus 로고    scopus 로고
    • Molecular cloning and antigenic mapping of heat-shock protein 70 from the malaria species Plasmodium berghei
    • Fan, J. Y., and E. A. Davidson. 1996. Molecular cloning and antigenic mapping of heat-shock protein 70 from the malaria species Plasmodium berghei. Am. J. Trop. Med. Hyg. 55:570-576.
    • (1996) Am. J. Trop. Med. Hyg , vol.55 , pp. 570-576
    • Fan, J.Y.1    Davidson, E.A.2
  • 4
    • 0026685816 scopus 로고
    • Nucleotide sequence of a Plasmodium falciparum stress protein with similarity to mammalian 78 kDa glucose-regulated protein
    • Kumar, N., and H. Zheng. 1992. Nucleotide sequence of a Plasmodium falciparum stress protein with similarity to mammalian 78 kDa glucose-regulated protein. Mol. Biochem. Parasitol. 56:353-356.
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    • Kumar, N.1    Zheng, H.2
  • 5
    • 0031687287 scopus 로고    scopus 로고
    • Evidence for epitope-specific thymus-independent response against a repeat sequence in a protein antigen
    • Kumar, N., and H. Zheng. 1998. Evidence for epitope-specific thymus-independent response against a repeat sequence in a protein antigen. Immunology 94:28-34.
    • (1998) Immunology , vol.94 , pp. 28-34
    • Kumar, N.1    Zheng, H.2
  • 6
    • 0842267072 scopus 로고    scopus 로고
    • Overproduction, purification, and characterization of the Plasmodium falciparum heat shock protein 70
    • Matambo, T. S., O. O. Odunuga, A. Boshoff, and G. L. Blatch. 2004. Overproduction, purification, and characterization of the Plasmodium falciparum heat shock protein 70. Protein Expr. Purif. 33:214-222.
    • (2004) Protein Expr. Purif , vol.33 , pp. 214-222
    • Matambo, T.S.1    Odunuga, O.O.2    Boshoff, A.3    Blatch, G.L.4
  • 7
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: Cellular functions and molecular mechanism
    • Mayer, M. P., and B. Bukau. 2005. Hsp70 chaperones: cellular functions and molecular mechanism. Cell. Mol. Life Sci. 62:670-684.
    • (2005) Cell. Mol. Life Sci , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 8
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    • Na, B. K., H. W. Lee, S. U. Moon, T. S. In, K. Lin, M. Maung, G. T. Chung, J. K. Lee, T. S. Kim, and Y. Kong. 2005. Genetic variations of the dihydrofolate reductase gene of Plasmodium vivax in Mandalay Division, Myanmar. Parasitol. Res. 96:321-325.
    • Na, B. K., H. W. Lee, S. U. Moon, T. S. In, K. Lin, M. Maung, G. T. Chung, J. K. Lee, T. S. Kim, and Y. Kong. 2005. Genetic variations of the dihydrofolate reductase gene of Plasmodium vivax in Mandalay Division, Myanmar. Parasitol. Res. 96:321-325.
  • 9
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    • Threonine 204 of the chaperone protein Hsc70 influences the structure of the active sites, but is not essential for ATP hydrolysis
    • O'Brien, M. C., and D. B. McKay. 1993. Threonine 204 of the chaperone protein Hsc70 influences the structure of the active sites, but is not essential for ATP hydrolysis. J. Biol. Chem. 268:24323-24329.
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  • 11
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    • Recurrent fever promotes Plasmodium falciparum development in human erythrocytes
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.