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Volumn 94, Issue 3 SPEC. ISS., 2005, Pages 191-206

Exploring the folate pathway in Plasmodium falciparum

Author keywords

Antifolate drugs; Drug resistance; Folate metabolism; Folate salvage; Gene disruption; Metabolic labelling

Indexed keywords

DIHYDROFOLATE REDUCTASE; DIHYDROPTEROATE SYNTHASE; FOLIC ACID;

EID: 19344363773     PISSN: 0001706X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.actatropica.2005.04.002     Document Type: Article
Times cited : (109)

References (99)
  • 1
    • 0033737481 scopus 로고    scopus 로고
    • Gene organization of a Plasmodium falciparum serine hydroxymethyltransferase and its functional expression in Escherichia coli
    • S. Alfadhli, and P.K. Rathod Gene organization of a Plasmodium falciparum serine hydroxymethyltransferase and its functional expression in Escherichia coli Mol. Biochem. Parasitol. 110 2000 283 291
    • (2000) Mol. Biochem. Parasitol. , vol.110 , pp. 283-291
    • Alfadhli, S.1    Rathod, P.K.2
  • 2
    • 0016709592 scopus 로고
    • Purification and properties of Escherichia coli dihydrofolate reductase
    • D. Baccanari, A. Phillips, S. Smith, D. Sinski, and J. Burchall Purification and properties of Escherichia coli dihydrofolate reductase Biochemistry 14 1975 5267 5273
    • (1975) Biochemistry , vol.14 , pp. 5267-5273
    • Baccanari, D.1    Phillips, A.2    Smith, S.3    Sinski, D.4    Burchall, J.5
  • 3
    • 0028080576 scopus 로고
    • Vitamin activities in human portal, hepatic and femoral blood after vitamin ingestion
    • H. Baker, W. Tenhove, E. Baker, and O. Frank Vitamin activities in human portal, hepatic and femoral blood after vitamin ingestion Int. J. Vitam. Nutr. Res. 64 1994 60 67
    • (1994) Int. J. Vitam. Nutr. Res. , vol.64 , pp. 60-67
    • Baker, H.1    Tenhove, W.2    Baker, E.3    Frank, O.4
  • 4
    • 0033587690 scopus 로고    scopus 로고
    • A set of independent selectable markers for transfection of the human malaria parasite Plasmodium falciparum
    • C. Ben Mamoun, I.Y. Gluzman, S. Goyard, S.M. Beverley, and D.E. Goldberg A set of independent selectable markers for transfection of the human malaria parasite Plasmodium falciparum Proc. Natl. Acad. Sci. U.S.A. 96 1999 8716 8720
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 8716-8720
    • Ben Mamoun, C.1    Gluzman, I.Y.2    Goyard, S.3    Beverley, S.M.4    Goldberg, D.E.5
  • 5
    • 0028021624 scopus 로고
    • Sequence variation of the hydroxymethyldihydropterin pyrophosphokinase - Dihydropteroate synthase gene in lines of the human malaria parasite, Plasmodium falciparum, with differing resistance to sulfadoxine
    • D.R. Brooks, P. Wang, M. Read, W.M. Watkins, P.F.G. Sims, and J.E. Hyde Sequence variation of the hydroxymethyldihydropterin pyrophosphokinase - dihydropteroate synthase gene in lines of the human malaria parasite, Plasmodium falciparum, with differing resistance to sulfadoxine Eur. J. Biochem. 224 1994 397 405
    • (1994) Eur. J. Biochem. , vol.224 , pp. 397-405
    • Brooks, D.R.1    Wang, P.2    Read, M.3    Watkins, W.M.4    Sims, P.F.G.5    Hyde, J.E.6
  • 6
    • 0017394111 scopus 로고
    • Synergism between trimethoprim and sulfamethoxazole
    • J.J. Burchall Synergism between trimethoprim and sulfamethoxazole Science 197 1977 1300 1301
    • (1977) Science , vol.197 , pp. 1300-1301
    • Burchall, J.J.1
  • 7
    • 0001651897 scopus 로고
    • Molecular cloning and sequence analysis of the Plasmodium falciparum dihydrofolate reductase-thymidylate synthase gene
    • D.J. Bzik, W.B. Li, T. Horii, and J. Inselburg Molecular cloning and sequence analysis of the Plasmodium falciparum dihydrofolate reductase-thymidylate synthase gene Proc. Natl. Acad. Sci. U.S.A. 84 1987 8360 8364
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 8360-8364
    • Bzik, D.J.1    Li, W.B.2    Horii, T.3    Inselburg, J.4
  • 8
    • 0023176096 scopus 로고
    • Kinetic and molecular properties of the dihydrofolate reductase from pyrimethamine-sensitive and pyrimethamine-resistant clones of the human malaria parasite Plasmodium falciparum
    • G.X. Chen, C. Mueller, M. Wendlinger, and J.W. Zolg Kinetic and molecular properties of the dihydrofolate reductase from pyrimethamine-sensitive and pyrimethamine-resistant clones of the human malaria parasite Plasmodium falciparum Mol. Pharmacol. 31 1987 430 437
    • (1987) Mol. Pharmacol. , vol.31 , pp. 430-437
    • Chen, G.X.1    Mueller, C.2    Wendlinger, M.3    Zolg, J.W.4
  • 9
    • 0021249879 scopus 로고
    • Synergistic antimalarial activity of pyrimethamine and sulfadoxine against Plasmodium falciparum in vitro
    • J.D. Chulay, W.M. Watkins, and D.G. Sixsmith Synergistic antimalarial activity of pyrimethamine and sulfadoxine against Plasmodium falciparum in vitro Am. J. Trop. Med. Hyg. 33 1984 325 330
    • (1984) Am. J. Trop. Med. Hyg. , vol.33 , pp. 325-330
    • Chulay, J.D.1    Watkins, W.M.2    Sixsmith, D.G.3
  • 10
    • 0016174444 scopus 로고
    • 7,8-Dihydropteroyl oligo-gamma-l-glutamates: Synthesis and kinetic studies with purified dihydrofolate reductase from mammalian sources
    • J.K. Coward, K.N. Parameswaran, A.R. Cashmore, and J.R. Bertino 7,8-Dihydropteroyl oligo-gamma-l-glutamates: synthesis and kinetic studies with purified dihydrofolate reductase from mammalian sources Biochemistry 13 1974 3899 3903
    • (1974) Biochemistry , vol.13 , pp. 3899-3903
    • Coward, J.K.1    Parameswaran, K.N.2    Cashmore, A.R.3    Bertino, J.R.4
  • 11
    • 0000854414 scopus 로고
    • Amino-acid changes linked to pyrimethamine resistance in the dihydrofolate reductase-thymidylate synthase gene of Plasmodium falciparum
    • A.F. Cowman, M.J. Morry, B.A. Biggs, G.A.M. Cross, and S.J. Foote Amino-acid changes linked to pyrimethamine resistance in the dihydrofolate reductase-thymidylate synthase gene of Plasmodium falciparum Proc. Natl. Acad. Sci. U.S.A. 85 1988 9109 9113
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 9109-9113
    • Cowman, A.F.1    Morry, M.J.2    Biggs, B.A.3    Cross, G.A.M.4    Foote, S.J.5
  • 14
    • 0034655980 scopus 로고    scopus 로고
    • Disruption of cytoplasmic and mitochondrial folylpolyglutamate synthetase activity in Saccharomyces cerevisiae
    • L. DeSouza, Y. Shen, and A.L. Bognar Disruption of cytoplasmic and mitochondrial folylpolyglutamate synthetase activity in Saccharomyces cerevisiae Arch. Biochem. Biophys. 376 2000 299 312
    • (2000) Arch. Biochem. Biophys. , vol.376 , pp. 299-312
    • Desouza, L.1    Shen, Y.2    Bognar, A.L.3
  • 16
    • 0036162628 scopus 로고    scopus 로고
    • Negative selection of Plasmodium falciparum reveals targeted gene deletion by double crossover recombination
    • M.T. Duraisingh, T. Triglia, and A.F. Cowman Negative selection of Plasmodium falciparum reveals targeted gene deletion by double crossover recombination Int. J. Parasit. 32 2002 81 89
    • (2002) Int. J. Parasit. , vol.32 , pp. 81-89
    • Duraisingh, M.T.1    Triglia, T.2    Cowman, A.F.3
  • 17
    • 0032407858 scopus 로고    scopus 로고
    • Cycloguanil and its parent compound proguanil demonstrate distinct activities against Plasmodium falciparum malaria parasites transformed with human dihydrofolate reductase
    • D.A. Fidock, T. Nomura, and T.E. Wellems Cycloguanil and its parent compound proguanil demonstrate distinct activities against Plasmodium falciparum malaria parasites transformed with human dihydrofolate reductase Mol. Pharmacol. 54 1998 1140 1147
    • (1998) Mol. Pharmacol. , vol.54 , pp. 1140-1147
    • Fidock, D.A.1    Nomura, T.2    Wellems, T.E.3
  • 18
    • 0030885188 scopus 로고    scopus 로고
    • Transformation with human dihydrofolate reductase renders malaria parasites insensitive to WR99210 but does not affect the intrinsic activity of proguanil
    • D.A. Fidock, and T.E. Wellems Transformation with human dihydrofolate reductase renders malaria parasites insensitive to WR99210 but does not affect the intrinsic activity of proguanil Proc. Natl. Acad. Sci. U.S.A. 94 1997 10931 10936
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 10931-10936
    • Fidock, D.A.1    Wellems, T.E.2
  • 19
    • 0035053015 scopus 로고    scopus 로고
    • Subcellular localization and characterization of chorismate synthase in the apicomplexan Plasmodium falciparum
    • T. Fitzpatrick, S. Ricken, M. Lanzer, N. Amrhein, P. Macheroux, and B. Kappes Subcellular localization and characterization of chorismate synthase in the apicomplexan Plasmodium falciparum Mol. Microbiol. 40 2001 65 75
    • (2001) Mol. Microbiol. , vol.40 , pp. 65-75
    • Fitzpatrick, T.1    Ricken, S.2    Lanzer, M.3    Amrhein, N.4    MacHeroux, P.5    Kappes, B.6
  • 21
    • 0040668894 scopus 로고
    • The "inactivation" of folic acid by liver
    • S. Futterman, and M. Silverman The "inactivation" of folic acid by liver J. Biol. Chem. 224 1957 31 40
    • (1957) J. Biol. Chem. , vol.224 , pp. 31-40
    • Futterman, S.1    Silverman, M.2
  • 24
    • 0000481934 scopus 로고    scopus 로고
    • Folate biosynthesis, reduction, and polyglutamation
    • F.C. Neidhardt ASM Press Washington, DC
    • J.M. Green, B.P. Nichols, and R.G. Matthews Folate biosynthesis, reduction, and polyglutamation F.C. Neidhardt Escherichia coli and Salmonella 1996 ASM Press Washington, DC 665 673
    • (1996) Escherichia Coli and Salmonella , pp. 665-673
    • Green, J.M.1    Nichols, B.P.2    Matthews, R.G.3
  • 27
    • 0026066990 scopus 로고
    • Functional expression of the dihydrofolate reductase and thymidylate synthetase activities of the human malaria parasite Plasmodium falciparum in Escherichia coli
    • S.J. Hall, P.F.G. Sims, and J.E. Hyde Functional expression of the dihydrofolate reductase and thymidylate synthetase activities of the human malaria parasite Plasmodium falciparum in Escherichia coli Mol. Biochem. Parasitol. 45 1991 317 330
    • (1991) Mol. Biochem. Parasitol. , vol.45 , pp. 317-330
    • Hall, S.J.1    Sims, P.F.G.2    Hyde, J.E.3
  • 29
    • 0035991854 scopus 로고    scopus 로고
    • Sulfadoxine-pyrimethamine resistance in the rodent malaria parasite Plasmodium chabaudi
    • K. Hayton, L.C. Ranford-Cartwright, and D. Walliker Sulfadoxine- pyrimethamine resistance in the rodent malaria parasite Plasmodium chabaudi Antimicrob. Agents Chemother. 46 2002 2482 2489
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 2482-2489
    • Hayton, K.1    Ranford-Cartwright, L.C.2    Walliker, D.3
  • 30
    • 0024989797 scopus 로고
    • The dihydrofolate reductase-thymidylate synthetase gene in the drug resistance of malaria parasites
    • J.E. Hyde The dihydrofolate reductase-thymidylate synthetase gene in the drug resistance of malaria parasites Pharmacol. Therap. 48 1990 45 59
    • (1990) Pharmacol. Therap. , vol.48 , pp. 45-59
    • Hyde, J.E.1
  • 31
    • 0036188538 scopus 로고    scopus 로고
    • Mechanisms of resistance of Plasmodium falciparum to antimalarial drugs
    • J.E. Hyde Mechanisms of resistance of Plasmodium falciparum to antimalarial drugs Microbes Infect. 4 2002 165 174
    • (2002) Microbes Infect. , vol.4 , pp. 165-174
    • Hyde, J.E.1
  • 32
    • 0347517722 scopus 로고    scopus 로고
    • Effect of dietary p-aminobenzoic acid on murine Plasmodium yoelii infection
    • G.A. Kicska, L.M. Ting, V.L. Schramm, and K. Kim Effect of dietary p-aminobenzoic acid on murine Plasmodium yoelii infection J. Inf. Dis. 188 2003 1776 1781
    • (2003) J. Inf. Dis. , vol.188 , pp. 1776-1781
    • Kicska, G.A.1    Ting, L.M.2    Schramm, V.L.3    Kim, K.4
  • 33
    • 0033027433 scopus 로고    scopus 로고
    • The antimalarial triazine WR99210 and the prodrug PS-15: Folate reversal of in vitro activity against Plasmodium falciparum and a non-antifolate mode of action of the prodrug
    • S.M. Kinyanjui, E.K. Mberu, P.A. Winstanley, D.P. Jacobus, and W.M. Watkins The antimalarial triazine WR99210 and the prodrug PS-15: folate reversal of in vitro activity against Plasmodium falciparum and a non-antifolate mode of action of the prodrug Am. J. Trop. Med. Hyg. 60 1999 943 947
    • (1999) Am. J. Trop. Med. Hyg. , vol.60 , pp. 943-947
    • Kinyanjui, S.M.1    Mberu, E.K.2    Winstanley, P.A.3    Jacobus, D.P.4    Watkins, W.M.5
  • 34
    • 0348048784 scopus 로고    scopus 로고
    • Functional analysis of Plasmodium falciparum parasitophorous vacuole membrane protein (Pfs16) during gametocytogenesis and gametogenesis by targeted gene disruption
    • D. Kongkasuriyachai, H. Fujioka, and N. Kumar Functional analysis of Plasmodium falciparum parasitophorous vacuole membrane protein (Pfs16) during gametocytogenesis and gametogenesis by targeted gene disruption Mol. Biochem. Parasitol. 133 2004 275 285
    • (2004) Mol. Biochem. Parasitol. , vol.133 , pp. 275-285
    • Kongkasuriyachai, D.1    Fujioka, H.2    Kumar, N.3
  • 35
    • 0027074126 scopus 로고
    • Regulatory role of oxidized and reduced pteroylpolyglutamates
    • C.L. Krumdieck, I. Eto, and J.E. Baggott Regulatory role of oxidized and reduced pteroylpolyglutamates Ann. N.Y. Acad. Sci. 669 1992 44 58
    • (1992) Ann. N.Y. Acad. Sci. , vol.669 , pp. 44-58
    • Krumdieck, C.L.1    Eto, I.2    Baggott, J.E.3
  • 36
    • 0024465225 scopus 로고
    • De novo and salvage biosynthesis of pteroylpentaglutamates in the human malaria parasite, Plasmodium falciparum
    • J. Krungkrai, H.K. Webster, and Y. Yuthavong De novo and salvage biosynthesis of pteroylpentaglutamates in the human malaria parasite, Plasmodium falciparum Mol. Biochem. Parasitol. 32 1989 25 37
    • (1989) Mol. Biochem. Parasitol. , vol.32 , pp. 25-37
    • Krungkrai, J.1    Webster, H.K.2    Yuthavong, Y.3
  • 38
    • 0035135063 scopus 로고    scopus 로고
    • Characterization of three genes encoding enzymes of the folate biosynthetic pathway in Plasmodium falciparum
    • C.S. Lee, E. Salcedo, Q. Wang, P. Wang, P.F.G. Sims, and J.E. Hyde Characterization of three genes encoding enzymes of the folate biosynthetic pathway in Plasmodium falciparum Parasitology 122 2001 1 13
    • (2001) Parasitology , vol.122 , pp. 1-13
    • Lee, C.S.1    Salcedo, E.2    Wang, Q.3    Wang, P.4    Sims, P.F.G.5    Hyde, J.E.6
  • 39
    • 0000533384 scopus 로고    scopus 로고
    • Leishmania major pteridine reductase 1 belongs to the short chain dehydrogenase family: Stereochemical and kinetic evidence
    • J. Luba, B. Nare, P.H. Liang, K.S. Anderson, S.M. Beverley, and L.W. Hardy Leishmania major pteridine reductase 1 belongs to the short chain dehydrogenase family: stereochemical and kinetic evidence Biochemistry 37 1998 4093 4104
    • (1998) Biochemistry , vol.37 , pp. 4093-4104
    • Luba, J.1    Nare, B.2    Liang, P.H.3    Anderson, K.S.4    Beverley, S.M.5    Hardy, L.W.6
  • 40
    • 0036628341 scopus 로고    scopus 로고
    • Plasmodium falciparum: In vitro activity of sulfadoxine and dapsone in field isolates from Kenya: Point mutations in dihydropteroate synthase may not be the only determinants in sulfa resistance
    • E.K. Mberu, A.M. Nzila, E. Nduati, A. Ross, S.M. Monks, G.O. Kokwaro, W.M. Watkins, and C.H. Sibley Plasmodium falciparum: in vitro activity of sulfadoxine and dapsone in field isolates from Kenya: point mutations in dihydropteroate synthase may not be the only determinants in sulfa resistance Exp. Parasitol. 101 2002 90 96
    • (2002) Exp. Parasitol. , vol.101 , pp. 90-96
    • Mberu, E.K.1    Nzila, A.M.2    Nduati, E.3    Ross, A.4    Monks, S.M.5    Kokwaro, G.O.6    Watkins, W.M.7    Sibley, C.H.8
  • 44
    • 0035856231 scopus 로고    scopus 로고
    • Chlorproguanil-dapsone for treatment of drug-resistant falciparum malaria in Tanzania
    • T. Mutabingwa, A. Nzila, E. Mberu, E. Nduati, P. Winstanley, E. Hills, and W. Watkins Chlorproguanil-dapsone for treatment of drug-resistant falciparum malaria in Tanzania Lancet 358 2001 1218 1223
    • (2001) Lancet , vol.358 , pp. 1218-1223
    • Mutabingwa, T.1    Nzila, A.2    Mberu, E.3    Nduati, E.4    Winstanley, P.5    Hills, E.6    Watkins, W.7
  • 45
    • 0037325815 scopus 로고    scopus 로고
    • Affinity extraction combined with stable isotope dilution LC/MS for the determination of 5-methyltetrahydrofolate in human plasma
    • B.C. Nelson, C.M. Pfeiffer, S.A. Margolis, and C.P. Nelson Affinity extraction combined with stable isotope dilution LC/MS for the determination of 5-methyltetrahydrofolate in human plasma Anal. Biochem. 313 2003 117 127
    • (2003) Anal. Biochem. , vol.313 , pp. 117-127
    • Nelson, B.C.1    Pfeiffer, C.M.2    Margolis, S.A.3    Nelson, C.P.4
  • 46
    • 3142671580 scopus 로고    scopus 로고
    • Quantitative proteomics of the human malaria parasite Plasmodium falciparum and its application to studies of development and inhibition
    • N. Nirmalan, P.F.G. Sims, and J.E. Hyde Quantitative proteomics of the human malaria parasite Plasmodium falciparum and its application to studies of development and inhibition Mol. Microbiol. 52 2004 1187 1199
    • (2004) Mol. Microbiol. , vol.52 , pp. 1187-1199
    • Nirmalan, N.1    Sims, P.F.G.2    Hyde, J.E.3
  • 47
    • 2342650008 scopus 로고    scopus 로고
    • Translational up-regulation of antifolate drug targets in the human malaria parasite Plasmodium falciparum upon challenge with inhibitors
    • N. Nirmalan, P.F.G. Sims, and J.E. Hyde Translational up-regulation of antifolate drug targets in the human malaria parasite Plasmodium falciparum upon challenge with inhibitors Mol. Biochem. Parasitol. 136 2004 63 70
    • (2004) Mol. Biochem. Parasitol. , vol.136 , pp. 63-70
    • Nirmalan, N.1    Sims, P.F.G.2    Hyde, J.E.3
  • 48
    • 0036034808 scopus 로고    scopus 로고
    • Transcriptional analysis of genes encoding enzymes of the folate pathway in the human malaria parasite Plasmodium falciparum
    • N. Nirmalan, P. Wang, P.F.G. Sims, and J.E. Hyde Transcriptional analysis of genes encoding enzymes of the folate pathway in the human malaria parasite Plasmodium falciparum Mol. Microbiol. 46 2002 179 190
    • (2002) Mol. Microbiol. , vol.46 , pp. 179-190
    • Nirmalan, N.1    Wang, P.2    Sims, P.F.G.3    Hyde, J.E.4
  • 50
    • 0034065697 scopus 로고    scopus 로고
    • Towards an understanding of the mechanism of pyrimethamine-sulfadoxine resistance in Plasmodium falciparum: Genotyping of dihydrofolate reductase and dihydropteroate synthase of Kenyan parasites
    • A.M. Nzila, E.K. Mberu, J. Sulo, H. Dayo, P.A. Winstanley, C.H. Sibley, and W.M. Watkins Towards an understanding of the mechanism of pyrimethamine-sulfadoxine resistance in Plasmodium falciparum: Genotyping of dihydrofolate reductase and dihydropteroate synthase of Kenyan parasites Antimicrob. Agents Chemother. 44 2000 991 996
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 991-996
    • Nzila, A.M.1    Mberu, E.K.2    Sulo, J.3    Dayo, H.4    Winstanley, P.A.5    Sibley, C.H.6    Watkins, W.M.7
  • 51
    • 0034125270 scopus 로고    scopus 로고
    • Molecular evidence of greater selective pressure for drug resistance exerted by the long-acting antifolate pyrimethamine/sulfadoxine compared with the shorter-acting chlorproguanil/dapsone on Kenyan Plasmodium falciparum
    • A.M. Nzila, E. Nduati, E.K. Mberu, C.H. Sibley, S.A. Monks, P.A. Winstanley, and W.M. Watkins Molecular evidence of greater selective pressure for drug resistance exerted by the long-acting antifolate pyrimethamine/ sulfadoxine compared with the shorter-acting chlorproguanil/dapsone on Kenyan Plasmodium falciparum J. Inf. Dis. 181 2000 2023 2028
    • (2000) J. Inf. Dis. , vol.181 , pp. 2023-2028
    • Nzila, A.M.1    Nduati, E.2    Mberu, E.K.3    Sibley, C.H.4    Monks, S.A.5    Winstanley, P.A.6    Watkins, W.M.7
  • 52
    • 0031963057 scopus 로고    scopus 로고
    • Kenyan Plasmodium falciparum field isolates: Correlation between pyrimethamine and chlorcycloguanil activity in vitro and point mutations in the dihydrofolate reductase domain
    • A. Nzila-Mounda, E.K. Mberu, C.H. Sibley, C.V. Plowe, P.A. Winstanley, and W.M. Watkins Kenyan Plasmodium falciparum field isolates: correlation between pyrimethamine and chlorcycloguanil activity in vitro and point mutations in the dihydrofolate reductase domain Antimicrob. Agents Chemother. 42 1998 164 169
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 164-169
    • Nzila-Mounda, A.1    Mberu, E.K.2    Sibley, C.H.3    Plowe, C.V.4    Winstanley, P.A.5    Watkins, W.M.6
  • 53
    • 0035253776 scopus 로고    scopus 로고
    • An alteration in concatameric structure is associated with efficient segregation of plasmids in transfected Plasmodium falciparum parasites
    • R.A. O'Donnell, P.R. Preiser, D.H. Williamson, P.W. Moore, A.F. Cowman, and B.S. Crabb An alteration in concatameric structure is associated with efficient segregation of plasmids in transfected Plasmodium falciparum parasites Nucleic Acids Res. 29 2001 716 724
    • (2001) Nucleic Acids Res. , vol.29 , pp. 716-724
    • O'Donnell, R.A.1    Preiser, P.R.2    Williamson, D.H.3    Moore, P.W.4    Cowman, A.F.5    Crabb, B.S.6
  • 54
    • 0030946240 scopus 로고    scopus 로고
    • Isolation and molecular characterization of the bifunctional hydroxymethyldihydropterin pyrophosphokinase-dihydropteroate synthase gene from Toxoplasma gondii
    • T.V. Pashley, F. Volpe, M. Pudney, J.E. Hyde, P.F.G. Sims, and C.J. Delves Isolation and molecular characterization of the bifunctional hydroxymethyldihydropterin pyrophosphokinase-dihydropteroate synthase gene from Toxoplasma gondii Mol. Biochem. Parasitol. 86 1997 37 47
    • (1997) Mol. Biochem. Parasitol. , vol.86 , pp. 37-47
    • Pashley, T.V.1    Volpe, F.2    Pudney, M.3    Hyde, J.E.4    Sims, P.F.G.5    Delves, C.J.6
  • 57
    • 0000841123 scopus 로고
    • Evidence that a point mutation in dihydrofolate reductase-thymidylate synthase confers resistance to pyrimethamine in falciparum malaria
    • D.S. Peterson, D. Walliker, and T.E. Wellems Evidence that a point mutation in dihydrofolate reductase-thymidylate synthase confers resistance to pyrimethamine in falciparum malaria Proc. Natl. Acad. Sci. U.S.A. 85 1988 9114 9118
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 9114-9118
    • Peterson, D.S.1    Walliker, D.2    Wellems, T.E.3
  • 59
    • 77949634490 scopus 로고    scopus 로고
    • P. falciparum dihydrofolate reductase and dihydropteroate synthase mutations: Epidemiology and role in clinical resistance to antifolates
    • C.V. Plowe, J.G. Kublin, and O.K. Doumbo P. falciparum dihydrofolate reductase and dihydropteroate synthase mutations: epidemiology and role in clinical resistance to antifolates Drug Resist. Update 1 1998 389 396
    • (1998) Drug Resist. Update , vol.1 , pp. 389-396
    • Plowe, C.V.1    Kublin, J.G.2    Doumbo, O.K.3
  • 60
    • 0035180748 scopus 로고    scopus 로고
    • Drug resistant falciparum malaria: Clinical consequences and strategies for prevention
    • R.N. Price, and F. Nosten Drug resistant falciparum malaria: clinical consequences and strategies for prevention Drug Resist. Update 4 2001 187 196
    • (2001) Drug Resist. Update , vol.4 , pp. 187-196
    • Price, R.N.1    Nosten, F.2
  • 61
    • 0037784010 scopus 로고    scopus 로고
    • Docking and database screening reveal new classes of Plasmodium falciparum dihydrofolate reductase inhibitors
    • G. Rastelli, S. Pacchioni, W. Sirawaraporn, R. Sirawaraporn, M.D. Parenti, and A.M. Ferrari Docking and database screening reveal new classes of Plasmodium falciparum dihydrofolate reductase inhibitors J. Med. Chem. 46 2003 2834 2845
    • (2003) J. Med. Chem. , vol.46 , pp. 2834-2845
    • Rastelli, G.1    Pacchioni, S.2    Sirawaraporn, W.3    Sirawaraporn, R.4    Parenti, M.D.5    Ferrari, A.M.6
  • 62
    • 0035910001 scopus 로고    scopus 로고
    • Tetrahydrofolate biosynthesis in plants: Molecular and functional characterization of dihydrofolate synthetase and three isoforms of folylpolyglutamate synthetase in Arabidopsis thaliana
    • S. Ravanel, H. Cherest, S. Jabrin, D. Grunwald, Y. Surdin-Kerjan, R. Douce, and F. Rebeille Tetrahydrofolate biosynthesis in plants: molecular and functional characterization of dihydrofolate synthetase and three isoforms of folylpolyglutamate synthetase in Arabidopsis thaliana Proc. Natl. Acad. Sci. U.S.A. 98 2001 15360 15365
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 15360-15365
    • Ravanel, S.1    Cherest, H.2    Jabrin, S.3    Grunwald, D.4    Surdin-Kerjan, Y.5    Douce, R.6    Rebeille, F.7
  • 63
    • 0034708162 scopus 로고    scopus 로고
    • Pgh1 modulates sensitivity and resistance to multiple antimalarials in Plasmodium falciparum
    • M.B. Reed, K.J. Saliba, S.R. Caruana, K. Kirk, and A.F. Cowman Pgh1 modulates sensitivity and resistance to multiple antimalarials in Plasmodium falciparum Nature 403 2000 906 909
    • (2000) Nature , vol.403 , pp. 906-909
    • Reed, M.B.1    Saliba, K.J.2    Caruana, S.R.3    Kirk, K.4    Cowman, A.F.5
  • 64
    • 0029775095 scopus 로고    scopus 로고
    • Point mutations in the dihydrofolate reductase and dihydropteroate synthetase genes and in vitro susceptibility to pyrimethamine and cycloguanil of Plasmodium falciparum isolates from Papua New Guinea
    • J.C. Reeder, K.H. Rieckmann, B. Genton, K. Lorry, B. Wines, and A.F. Cowman Point mutations in the dihydrofolate reductase and dihydropteroate synthetase genes and in vitro susceptibility to pyrimethamine and cycloguanil of Plasmodium falciparum isolates from Papua New Guinea Am. J. Trop. Med. Hyg. 55 1996 209 213
    • (1996) Am. J. Trop. Med. Hyg. , vol.55 , pp. 209-213
    • Reeder, J.C.1    Rieckmann, K.H.2    Genton, B.3    Lorry, K.4    Wines, B.5    Cowman, A.F.6
  • 65
    • 0031574462 scopus 로고    scopus 로고
    • A pteridine reductase gene ptr1 contiguous to a p-glycoprotein confers resistance to antifolates in Trypanosoma cruzi
    • C. Robello, P. Navarro, S. Castanys, and F. Gamarro A pteridine reductase gene ptr1 contiguous to a p-glycoprotein confers resistance to antifolates in Trypanosoma cruzi Mol. Biochem. Parasitol. 90 1997 525 535
    • (1997) Mol. Biochem. Parasitol. , vol.90 , pp. 525-535
    • Robello, C.1    Navarro, P.2    Castanys, S.3    Gamarro, F.4
  • 67
    • 0018567923 scopus 로고
    • The characteristics and significance of sulfonamides as substrates for Escherichia coli dihydropteroate synthase
    • S. Roland, R. Ferone, R.J. Harvey, V.L. Styles, and R.W. Morrison The characteristics and significance of sulfonamides as substrates for Escherichia coli dihydropteroate synthase J. Biol. Chem. 254 1979 10337 10345
    • (1979) J. Biol. Chem. , vol.254 , pp. 10337-10345
    • Roland, S.1    Ferone, R.2    Harvey, R.J.3    Styles, V.L.4    Morrison, R.W.5
  • 68
    • 0035112562 scopus 로고    scopus 로고
    • A bifunctional dihydrofolate synthetase-folylpolyglutamate synthetase in Plasmodium falciparum identified by functional complementation in yeast and bacteria
    • E. Salcedo, J.F. Cortese, C.V. Plowe, P.F.G. Sims, and J.E. Hyde A bifunctional dihydrofolate synthetase-folylpolyglutamate synthetase in Plasmodium falciparum identified by functional complementation in yeast and bacteria Mol. Biochem. Parasitol. 112 2001 241 254
    • (2001) Mol. Biochem. Parasitol. , vol.112 , pp. 241-254
    • Salcedo, E.1    Cortese, J.F.2    Plowe, C.V.3    Sims, P.F.G.4    Hyde, J.E.5
  • 70
    • 0022479388 scopus 로고
    • The susceptibility of Plasmodium falciparum to sulfadoxine and pyrimethamine - Correlation of in vivo and in vitro results
    • A. Schapira, I.C. Bygbjerg, S. Jepsen, H. Flachs, and M.W. Bentzon The susceptibility of Plasmodium falciparum to sulfadoxine and pyrimethamine - correlation of in vivo and in vitro results Am. J. Trop. Med. Hyg. 35 1986 239 245
    • (1986) Am. J. Trop. Med. Hyg. , vol.35 , pp. 239-245
    • Schapira, A.1    Bygbjerg, I.C.2    Jepsen, S.3    Flachs, H.4    Bentzon, M.W.5
  • 71
    • 0024433256 scopus 로고
    • Determination of tissue folate composition by affinity-chromatography followed by high-pressure ion-pair liquid-chromatography
    • J. Selhub Determination of tissue folate composition by affinity-chromatography followed by high-pressure ion-pair liquid-chromatography Anal. Biochem. 182 1989 84 93
    • (1989) Anal. Biochem. , vol.182 , pp. 84-93
    • Selhub, J.1
  • 72
    • 0033621358 scopus 로고    scopus 로고
    • Essential protein-protein interactions between Plasmodium falciparum thymidylate synthase and dihydrofolate reductase domains
    • S. Shallom, K. Zhang, L. Jiang, and P.K. Rathod Essential protein-protein interactions between Plasmodium falciparum thymidylate synthase and dihydrofolate reductase domains J. Biol. Chem. 274 1999 37781 37786
    • (1999) J. Biol. Chem. , vol.274 , pp. 37781-37786
    • Shallom, S.1    Zhang, K.2    Jiang, L.3    Rathod, P.K.4
  • 74
    • 0033119016 scopus 로고    scopus 로고
    • Selection and synergy in Plasmodium falciparum
    • P. Sims, P. Wang, and J.E. Hyde Selection and synergy in Plasmodium falciparum Parasitol. Today 15 1999 132 134
    • (1999) Parasitol. Today , vol.15 , pp. 132-134
    • Sims, P.1    Wang, P.2    Hyde, J.E.3
  • 76
    • 0025605441 scopus 로고
    • Heterologous expression of active thymidylate synthase dihydrofolate-reductase from Plasmodium falciparum
    • W. Sirawaraporn, R. Sirawaraporn, A.F. Cowman, Y. Yuthavong, and D.V. Santi Heterologous expression of active thymidylate synthase dihydrofolate-reductase from Plasmodium falciparum Biochemistry 29 1990 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
  • 77
    • 0031282471 scopus 로고    scopus 로고
    • Plasmodium falciparum: Asparagine mutant at residue 108 of dihydrofolate reductase is an optimal antifolate-resistant single mutant
    • W. Sirawaraporn, S. Yongkiettrakul, R. Sirawaraporn, Y. Yuthavong, and D.V. Santi Plasmodium falciparum: asparagine mutant at residue 108 of dihydrofolate reductase is an optimal antifolate-resistant single mutant Exp. Parasitol. 87 1997 245 252
    • (1997) Exp. Parasitol. , vol.87 , pp. 245-252
    • Sirawaraporn, W.1    Yongkiettrakul, S.2    Sirawaraporn, R.3    Yuthavong, Y.4    Santi, D.V.5
  • 78
    • 0024584012 scopus 로고
    • Characterization of the dihydrofolate reductase-thymidylate synthetase gene from human malaria parasites highly resistant to pyrimethamine
    • V.A. Snewin, S.M. England, P.F.G. Sims, and J.E. Hyde Characterization of the dihydrofolate reductase-thymidylate synthetase gene from human malaria parasites highly resistant to pyrimethamine Gene 76 1989 41 52
    • (1989) Gene , vol.76 , pp. 41-52
    • Snewin, V.A.1    England, S.M.2    Sims, P.F.G.3    Hyde, J.E.4
  • 79
    • 0032698219 scopus 로고    scopus 로고
    • A genetic map and recombination parameters of the human malaria parasite Plasmodium falciparum
    • X. Su, M. Ferdig, Y. Huang, C.Q. Huynh, A. Liu, J. You, J.C. Wootton, and T.E. Wellems A genetic map and recombination parameters of the human malaria parasite Plasmodium falciparum Science 286 1999 1351 1353
    • (1999) Science , vol.286 , pp. 1351-1353
    • Su, X.1    Ferdig, M.2    Huang, Y.3    Huynh, C.Q.4    Liu, A.5    You, J.6    Wootton, J.C.7    Wellems, T.E.8
  • 80
    • 0037068963 scopus 로고    scopus 로고
    • Chlorproguanil-dapsone versus sulfadoxine-pyrimethamine for sequential episodes of uncomplicated falciparum malaria in Kenya and Malawi: A randomised clinical trial
    • J. Sulo, P. Chimpeni, J. Hatcher, J.G. Kublin, C.V. Plowe, M.E. Molyneux, K. Marsh, T.E. Taylor, W.M. Watkins, and P.A. Winstanley Chlorproguanil-dapsone versus sulfadoxine-pyrimethamine for sequential episodes of uncomplicated falciparum malaria in Kenya and Malawi: a randomised clinical trial Lancet 360 2002 1136 1143
    • (2002) Lancet , vol.360 , pp. 1136-1143
    • Sulo, J.1    Chimpeni, P.2    Hatcher, J.3    Kublin, J.G.4    Plowe, C.V.5    Molyneux, M.E.6    Marsh, K.7    Taylor, T.E.8    Watkins, W.M.9    Winstanley, P.A.10
  • 81
    • 0028291789 scopus 로고
    • Primary structure and expression of the dihydropteroate synthetase gene of Plasmodium falciparum
    • T. Triglia, and A.F. Cowman Primary structure and expression of the dihydropteroate synthetase gene of Plasmodium falciparum Proc. Natl. Acad. Sci. U.S.A. 91 1994 7149 7153
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 7149-7153
    • Triglia, T.1    Cowman, A.F.2
  • 82
    • 0032777096 scopus 로고    scopus 로고
    • Plasmodium falciparum: A homologue of p-aminobenzoic acid synthetase
    • T. Triglia, and A.F. Cowman Plasmodium falciparum: a homologue of p-aminobenzoic acid synthetase Exp. Parasitol. 92 1999 154 158
    • (1999) Exp. Parasitol. , vol.92 , pp. 154-158
    • Triglia, T.1    Cowman, A.F.2
  • 84
    • 0031444278 scopus 로고    scopus 로고
    • Mutations in dihydropteroate synthase are responsible for sulfone and sulfonamide resistance in Plasmodium falciparum
    • T. Triglia, J.G.T. Menting, C. Wilson, and A.F. Cowman Mutations in dihydropteroate synthase are responsible for sulfone and sulfonamide resistance in Plasmodium falciparum Proc. Natl. Acad. Sci. U.S.A. 94 1997 13944 13949
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 13944-13949
    • Triglia, T.1    Menting, J.G.T.2    Wilson, C.3    Cowman, A.F.4
  • 87
    • 0033022037 scopus 로고    scopus 로고
    • Utilization of exogenous folate in the human malaria parasite Plasmodium falciparum and its critical role in antifolate drug synergy
    • P. Wang, R.K.B. Brobey, T. Horii, P.F.G. Sims, and J.E. Hyde Utilization of exogenous folate in the human malaria parasite Plasmodium falciparum and its critical role in antifolate drug synergy Mol. Microbiol. 32 1999 1254 1262
    • (1999) Mol. Microbiol. , vol.32 , pp. 1254-1262
    • Wang, P.1    Brobey, R.K.B.2    Horii, T.3    Sims, P.F.G.4    Hyde, J.E.5
  • 88
    • 0030801206 scopus 로고    scopus 로고
    • Resistance to antifolates in Plasmodium falciparum monitored by sequence analysis of dihydropteroate synthetase and dihydrofolate reductase alleles in a large number of field samples of diverse origins
    • P. Wang, C.S. Lee, R. Bayoumi, A. Djimde, O. Doumbo, G. Swedberg, L.D. Dao, H. Mshinda, and M. Tanner Resistance to antifolates in Plasmodium falciparum monitored by sequence analysis of dihydropteroate synthetase and dihydrofolate reductase alleles in a large number of field samples of diverse origins Mol. Biochem. Parasitol. 89 1997 161 177
    • (1997) Mol. Biochem. Parasitol. , vol.89 , pp. 161-177
    • Wang, P.1    Lee, C.S.2    Bayoumi, R.3    Djimde, A.4    Doumbo, O.5    Swedberg, G.6    Dao, L.D.7    Mshinda, H.8    Tanner, M.9
  • 89
    • 1842713046 scopus 로고    scopus 로고
    • Genetic and metabolic analysis of folate salvage in the human malaria parasite Plasmodium falciparum
    • P. Wang, N. Nirmalan, Q. Wang, P.F.G. Sims, and J.E. Hyde Genetic and metabolic analysis of folate salvage in the human malaria parasite Plasmodium falciparum Mol. Biochem. Parasitol. 135 2004 77 87
    • (2004) Mol. Biochem. Parasitol. , vol.135 , pp. 77-87
    • Wang, P.1    Nirmalan, N.2    Wang, Q.3    Sims, P.F.G.4    Hyde, J.E.5
  • 90
    • 0031029877 scopus 로고    scopus 로고
    • Sulfadoxine resistance in the human malaria parasite Plasmodium falciparum is determined by mutations in dihydropteroate synthetase and an additional factor associated with folate utilization
    • P. Wang, M. Read, P.F.G. Sims, and J.E. Hyde Sulfadoxine resistance in the human malaria parasite Plasmodium falciparum is determined by mutations in dihydropteroate synthetase and an additional factor associated with folate utilization Mol. Microbiol. 23 1997 979 986
    • (1997) Mol. Microbiol. , vol.23 , pp. 979-986
    • Wang, P.1    Read, M.2    Sims, P.F.G.3    Hyde, J.E.4
  • 91
    • 0030868588 scopus 로고    scopus 로고
    • A modified in vitro sulfadoxine susceptibility assay for Plasmodium falciparum suitable for investigating Fansidar resistance
    • P. Wang, P.F.G. Sims, and J.E. Hyde A modified in vitro sulfadoxine susceptibility assay for Plasmodium falciparum suitable for investigating Fansidar resistance Parasitology 115 1997 223 230
    • (1997) Parasitology , vol.115 , pp. 223-230
    • Wang, P.1    Sims, P.F.G.2    Hyde, J.E.3
  • 92
    • 1542721577 scopus 로고    scopus 로고
    • Transfection studies to explore essential folate metabolism and antifolate drug synergy in the human malaria parasite Plasmodium falciparum
    • P. Wang, Q. Wang, T.V. Aspinall, P.F.G. Sims, and J.E. Hyde Transfection studies to explore essential folate metabolism and antifolate drug synergy in the human malaria parasite Plasmodium falciparum Mol. Microbiol. 51 2004 1425 1438
    • (2004) Mol. Microbiol. , vol.51 , pp. 1425-1438
    • Wang, P.1    Wang, Q.2    Aspinall, T.V.3    Sims, P.F.G.4    Hyde, J.E.5
  • 93
    • 0037036625 scopus 로고    scopus 로고
    • Rapid positive selection of stable integrants following transfection of Plasmodium falciparum
    • P. Wang, Q. Wang, P.F.G. Sims, and J.E. Hyde Rapid positive selection of stable integrants following transfection of Plasmodium falciparum Mol. Biochem. Parasitol. 123 2002 1 10
    • (2002) Mol. Biochem. Parasitol. , vol.123 , pp. 1-10
    • Wang, P.1    Wang, Q.2    Sims, P.F.G.3    Hyde, J.E.4
  • 94
    • 0030813699 scopus 로고    scopus 로고
    • The efficacy of antifolate antimalarial combinations in Africa: A predictive model based on pharmacodynamic and pharmacokinetic analyses
    • W.M. Watkins, E.K. Mberu, P.A. Winstanley, and C.V. Plowe The efficacy of antifolate antimalarial combinations in Africa: a predictive model based on pharmacodynamic and pharmacokinetic analyses Parasitol. Today 13 1997 459 464
    • (1997) Parasitol. Today , vol.13 , pp. 459-464
    • Watkins, W.M.1    Mberu, E.K.2    Winstanley, P.A.3    Plowe, C.V.4
  • 96
    • 0036188537 scopus 로고    scopus 로고
    • Clinical status and implications of antimalarial drug resistance
    • P.A. Winstanley, S.A. Ward, and R.W. Snow Clinical status and implications of antimalarial drug resistance Microbes Infect. 4 2002 157 164
    • (2002) Microbes Infect. , vol.4 , pp. 157-164
    • Winstanley, P.A.1    Ward, S.A.2    Snow, R.W.3
  • 97
    • 0031002773 scopus 로고    scopus 로고
    • Analysis in yeast of antimalaria drugs that target the dihydrofolate reductase of Plasmodium falciparum
    • J.M. Wooden, L.H. Hartwell, B. Vasquez, and C.H. Sibley Analysis in yeast of antimalaria drugs that target the dihydrofolate reductase of Plasmodium falciparum Mol. Biochem. Parasitol. 85 1997 25 40
    • (1997) Mol. Biochem. Parasitol. , vol.85 , pp. 25-40
    • Wooden, J.M.1    Hartwell, L.H.2    Vasquez, B.3    Sibley, C.H.4
  • 99
    • 0037134042 scopus 로고    scopus 로고
    • Divergent regulation of dihydrofolate reductase between malaria parasite and human host
    • K. Zhang, and P.K. Rathod Divergent regulation of dihydrofolate reductase between malaria parasite and human host Science 296 2002 545 547
    • (2002) Science , vol.296 , pp. 545-547
    • Zhang, K.1    Rathod, P.K.2


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