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Volumn 61, Issue 2, 2012, Pages 324-332

Cloning and heterologous expression of Plasmodium ovale dihydrofolate reductase-thymidylate synthase gene

Author keywords

Antifolates; Dihydrofolate reductase thymidylate synthase; Plasmodium ovale

Indexed keywords

CYCLOGUANIL; DIHYDROFOLATE REDUCTASE; ESCHERICHIA COLI PROTEIN; METHOTREXATE; PYRIMETHAMINE; SEPHAROSE; THYMIDYLATE SYNTHASE;

EID: 84857799150     PISSN: 13835769     EISSN: 18730329     Source Type: Journal    
DOI: 10.1016/j.parint.2011.12.004     Document Type: Article
Times cited : (11)

References (31)
  • 5
    • 34248993025 scopus 로고    scopus 로고
    • Plasmodium malariae and Plasmodium ovale - the "bashful" malaria parasites
    • Mueller I., Zimmerman P.A., Reeder J.C. Plasmodium malariae and Plasmodium ovale - the "bashful" malaria parasites. Trends in Parasitology 2007, 23:278-283.
    • (2007) Trends in Parasitology , vol.23 , pp. 278-283
    • Mueller, I.1    Zimmerman, P.A.2    Reeder, J.C.3
  • 6
    • 0033211486 scopus 로고    scopus 로고
    • How prevalent are Plasmodium ovale and P. malariae in East Asia?
    • Kawamoto F., Liu Q., Ferreira M.U., Tantular I.S. How prevalent are Plasmodium ovale and P. malariae in East Asia?. Parasitology Today 1999, 15:422-426.
    • (1999) Parasitology Today , vol.15 , pp. 422-426
    • Kawamoto, F.1    Liu, Q.2    Ferreira, M.U.3    Tantular, I.S.4
  • 7
    • 53149105904 scopus 로고    scopus 로고
    • PCR-based detection of Plasmodium in Anopheles mosquitoes: a comparison of a new high-throughput assay with existing methods
    • Bass C., Nikou D., Blagborough A.M., Vontas J., Sinden R.E., Williamson M.S., et al. PCR-based detection of Plasmodium in Anopheles mosquitoes: a comparison of a new high-throughput assay with existing methods. Malaria Journal 2008, 7:177-185.
    • (2008) Malaria Journal , vol.7 , pp. 177-185
    • Bass, C.1    Nikou, D.2    Blagborough, A.M.3    Vontas, J.4    Sinden, R.E.5    Williamson, M.S.6
  • 10
    • 0035815313 scopus 로고    scopus 로고
    • Kinetic properties of dihydrofolate reductase from wild-type and mutant Plasmodium vivax expressed in Escherichia coli
    • Tahar R., de Pecoulas P.E., Basco L.K., Chiadmi M., Mazabraud A. Kinetic properties of dihydrofolate reductase from wild-type and mutant Plasmodium vivax expressed in Escherichia coli. Molecular and Biochemical Parasitology 2001, 113:241-249.
    • (2001) Molecular and Biochemical Parasitology , vol.113 , pp. 241-249
    • Tahar, R.1    de Pecoulas, P.E.2    Basco, L.K.3    Chiadmi, M.4    Mazabraud, A.5
  • 11
    • 0020634821 scopus 로고
    • Plasmodium falciparum: drug sensitivity in vitro of isolates before and after adaptation to continuous culture
    • Le Bras J., Deloron P., Ricour A., Andrieu B., Savel J., Coulaud J.P. Plasmodium falciparum: drug sensitivity in vitro of isolates before and after adaptation to continuous culture. Experimental Parasitology 1983, 56:9-14.
    • (1983) Experimental Parasitology , vol.56 , pp. 9-14
    • Le Bras, J.1    Deloron, P.2    Ricour, A.3    Andrieu, B.4    Savel, J.5    Coulaud, J.P.6
  • 13
    • 0036044961 scopus 로고    scopus 로고
    • Nested PCR analysis of Plasmodium parasites
    • Snounou G., Singh B. Nested PCR analysis of Plasmodium parasites. Methods in Molecular Medicine 2002, 72:189-203.
    • (2002) Methods in Molecular Medicine , vol.72 , pp. 189-203
    • Snounou, G.1    Singh, B.2
  • 14
    • 77957810996 scopus 로고    scopus 로고
    • Accurate and sensitive detection of Plasmodium species in humans by use of the dihydrofolate reductase-thymidylate synthase linker region
    • Tanomsing N., Imwong M., Theppabutr S., Pukrittayakamee S., Day N.P., White N.J., et al. Accurate and sensitive detection of Plasmodium species in humans by use of the dihydrofolate reductase-thymidylate synthase linker region. Journal of Clinical Microbiology 2010, 48:3735-3737.
    • (2010) Journal of Clinical Microbiology , vol.48 , pp. 3735-3737
    • Tanomsing, N.1    Imwong, M.2    Theppabutr, S.3    Pukrittayakamee, S.4    Day, N.P.5    White, N.J.6
  • 15
    • 0023684064 scopus 로고
    • A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions
    • Higuchi R., Krummel B., Saiki R.K. A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions. Nucleic Acids Research 1988, 16:7351-7367.
    • (1988) Nucleic Acids Research , vol.16 , pp. 7351-7367
    • Higuchi, R.1    Krummel, B.2    Saiki, R.K.3
  • 16
    • 11144309676 scopus 로고    scopus 로고
    • Subunit complementation of thymidylate synthase in Plasmodium falciparum bifunctional dihydrofolate reductase-thymidylate synthase
    • Chanama M., Chitnumsub P., Yuthavong Y. Subunit complementation of thymidylate synthase in Plasmodium falciparum bifunctional dihydrofolate reductase-thymidylate synthase. Molecular and Biochemical Parasitology 2005, 139:83-90.
    • (2005) Molecular and Biochemical Parasitology , vol.139 , pp. 83-90
    • Chanama, M.1    Chitnumsub, P.2    Yuthavong, Y.3
  • 17
    • 0021912893 scopus 로고
    • Purification and characterization of the bifunctional thymidylate synthetase-dihydrofolate reductase from methotrexate-resistant Leishmania tropica
    • Meek T.D., Garvey E.P., Santi D.V. Purification and characterization of the bifunctional thymidylate synthetase-dihydrofolate reductase from methotrexate-resistant Leishmania tropica. Biochemistry 1985, 24:678-686.
    • (1985) Biochemistry , vol.24 , pp. 678-686
    • Meek, T.D.1    Garvey, E.P.2    Santi, D.V.3
  • 18
    • 0014151463 scopus 로고
    • Effect of substrate decomposition on the spectrophotometric assay of dihydrofolate reductase
    • Hillcoat B.L., Nixon P.F., Blakley R.L. Effect of substrate decomposition on the spectrophotometric assay of dihydrofolate reductase. Analytical Biochemistry 1967, 21:178-189.
    • (1967) Analytical Biochemistry , vol.21 , pp. 178-189
    • Hillcoat, B.L.1    Nixon, P.F.2    Blakley, R.L.3
  • 19
    • 0002242695 scopus 로고
    • Direct spectrophotometric evidence for the oxidation of tetrahydrofolate during the enzymatic synthesis of thymidylate
    • Wahba A.J., Friedkin M. Direct spectrophotometric evidence for the oxidation of tetrahydrofolate during the enzymatic synthesis of thymidylate. Journal of Biological Chemistry 1961, 236:PC11-PC12.
    • (1961) Journal of Biological Chemistry , vol.236
    • Wahba, A.J.1    Friedkin, M.2
  • 20
    • 0013965282 scopus 로고
    • An isotopic assay for thymidylate synthetase
    • Roberts D. An isotopic assay for thymidylate synthetase. Biochemistry 1966, 5:3546-3548.
    • (1966) Biochemistry , vol.5 , pp. 3546-3548
    • Roberts, D.1
  • 21
    • 0025605441 scopus 로고
    • Heterologous expression of active thymidylate synthase-dihydrofolate reductase from Plasmodium falciparum
    • Sirawaraporn W., Sirawaraporn R., Cowman A.F., Yuthavong Y., Santi D.V. Heterologous expression of active thymidylate synthase-dihydrofolate reductase from Plasmodium falciparum. Biochemistry 1990, 29:10779-10785.
    • (1990) Biochemistry , vol.29 , pp. 10779-10785
    • Sirawaraporn, W.1    Sirawaraporn, R.2    Cowman, A.F.3    Yuthavong, Y.4    Santi, D.V.5
  • 25
    • 0024282746 scopus 로고
    • Fidelity of DNA synthesis by the Thermus aquaticus DNA polymerase
    • Tindall K.R., Kunkel T.A. Fidelity of DNA synthesis by the Thermus aquaticus DNA polymerase. Biochemistry 1988, 27:6008-6013.
    • (1988) Biochemistry , vol.27 , pp. 6008-6013
    • Tindall, K.R.1    Kunkel, T.A.2
  • 26
    • 33750596700 scopus 로고    scopus 로고
    • Evaluation of the activities of pyrimethamine analogs against Plasmodium vivax and Plasmodium falciparum dihydrofolate reductase-thymidylate synthase using in vitro enzyme inhibition and bacterial complementation assays
    • Bunyarataphan S., Leartsakulpanich U., Taweechai S., Tarnchompoo B., Kamchonwongpaisan S., Yuthavong Y. Evaluation of the activities of pyrimethamine analogs against Plasmodium vivax and Plasmodium falciparum dihydrofolate reductase-thymidylate synthase using in vitro enzyme inhibition and bacterial complementation assays. Antimicrobial Agents and Chemotherapy 2006, 50:3631-3637.
    • (2006) Antimicrobial Agents and Chemotherapy , vol.50 , pp. 3631-3637
    • Bunyarataphan, S.1    Leartsakulpanich, U.2    Taweechai, S.3    Tarnchompoo, B.4    Kamchonwongpaisan, S.5    Yuthavong, Y.6
  • 27
    • 0346096856 scopus 로고    scopus 로고
    • Evolution of enzymatic activity in the enolase superfamily: functional studies of the promiscuous o-succinylbenzoate synthase from Amycolatopsis
    • Taylor Ringia E.A., Garrett J.B., Thoden J.B., Holden H.M., Rayment I., Gerlt J.A. Evolution of enzymatic activity in the enolase superfamily: functional studies of the promiscuous o-succinylbenzoate synthase from Amycolatopsis. Biochemistry 2004, 43:224-229.
    • (2004) Biochemistry , vol.43 , pp. 224-229
    • Taylor Ringia, E.A.1    Garrett, J.B.2    Thoden, J.B.3    Holden, H.M.4    Rayment, I.5    Gerlt, J.A.6
  • 28
    • 0027445257 scopus 로고
    • The dihydrofolate reductase domain of Plasmodium falciparum thymidylate synthase-dihydrofolate reductase. Gene synthesis, expression, and anti-folate-resistant mutants
    • Sirawaraporn W., Prapunwattana P., Sirawaraporn R., Yuthavong Y., Santi D.V. The dihydrofolate reductase domain of Plasmodium falciparum thymidylate synthase-dihydrofolate reductase. Gene synthesis, expression, and anti-folate-resistant mutants. Journal of Biological Chemistry 1993, 268:21637-21644.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 21637-21644
    • Sirawaraporn, W.1    Prapunwattana, P.2    Sirawaraporn, R.3    Yuthavong, Y.4    Santi, D.V.5
  • 29
    • 0024402297 scopus 로고
    • Hydride transfer by dihydrofolate reductase. Causes and consequences of the wide range of rates exhibited by bacterial and vertebrate enzymes
    • Beard W.A., Appleman J.R., Delcamp T.J., Freisheim J.H., Blakley R.L. Hydride transfer by dihydrofolate reductase. Causes and consequences of the wide range of rates exhibited by bacterial and vertebrate enzymes. Journal of Biological Chemistry 1989, 264:9391-9399.
    • (1989) Journal of Biological Chemistry , vol.264 , pp. 9391-9399
    • Beard, W.A.1    Appleman, J.R.2    Delcamp, T.J.3    Freisheim, J.H.4    Blakley, R.L.5
  • 31
    • 79951578070 scopus 로고    scopus 로고
    • Formation of catalytically active cross-species heterodimers of thymidylate synthase from Plasmodium falciparum and Plasmodium vivax
    • Chanama M., Chanama S., Shaw P.J., Chitnumsub P., Leartsakulpanich U., Yuthavong Y. Formation of catalytically active cross-species heterodimers of thymidylate synthase from Plasmodium falciparum and Plasmodium vivax. Molecular Biology Reports 2011, 38:1029-1037.
    • (2011) Molecular Biology Reports , vol.38 , pp. 1029-1037
    • Chanama, M.1    Chanama, S.2    Shaw, P.J.3    Chitnumsub, P.4    Leartsakulpanich, U.5    Yuthavong, Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.