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Volumn 71, Issue 6, 2009, Pages 1386-1401

Methylene tetrahydrofolate dehydrogenase/cyclohydrolase and the synthesis of 10-CHO-THF are essential in Leishmania major

Author keywords

[No Author keywords available]

Indexed keywords

10 FORMYLTETRAHYDROFOLIC ACID; 5,10 METHYLENETETRAHYDROFOLATE REDUCTASE (FADH2); FOLIC ACID DERIVATIVE; FORMATE TETRAHYDROFOLATE LIGASE; METHYLENETETRAHYDROFOLIC ACID; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; RECOMBINANT ENZYME; UNCLASSIFIED DRUG;

EID: 62449213529     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2009.06610.x     Document Type: Article
Times cited : (49)

References (79)
  • 1
    • 0032520234 scopus 로고    scopus 로고
    • The 3-D structure of a folate-dependent dehydrogenase/cyclohydrolase bifunctional enzyme at 1.5 A resolution
    • Allaire, M., Li, Y., MacKenzie, R.E. Cygler, M. (1998) The 3-D structure of a folate-dependent dehydrogenase/cyclohydrolase bifunctional enzyme at 1.5 A resolution. Structure 6 : 173 182.
    • (1998) Structure , vol.6 , pp. 173-182
    • Allaire, M.1    Li, Y.2    MacKenzie, R.E.3    Cygler, M.4
  • 2
    • 0025954883 scopus 로고
    • Compartmentation of folate-mediated one-carbon metabolism in eukaryotes
    • Appling, D.R. (1991) Compartmentation of folate-mediated one-carbon metabolism in eukaryotes. FASEB J 5 : 2645 2651.
    • (1991) FASEB J , vol.5 , pp. 2645-2651
    • Appling, D.R.1
  • 3
    • 48749096392 scopus 로고    scopus 로고
    • Gene disruption of the DNA topoisomerase IB small subunit induces a non-viable phenotype in the hemoflagellate Leishmania major
    • Balana-Fouce, R., Garcia-Estrada, C., Perez-Pertejo, Y. Reguera, R.M. (2008) Gene disruption of the DNA topoisomerase IB small subunit induces a non-viable phenotype in the hemoflagellate Leishmania major. BMC Microbiol 8 : 113.
    • (2008) BMC Microbiol , vol.8 , pp. 113
    • Balana-Fouce, R.1    Garcia-Estrada, C.2    Perez-Pertejo, Y.3    Reguera, R.M.4
  • 4
    • 0033083293 scopus 로고    scopus 로고
    • Recent advances in identifying and validating drug targets in trypanosomes and leishmanias
    • Barrett, M.P., Mottram, J.C. Coombs, G.H. (1999) Recent advances in identifying and validating drug targets in trypanosomes and leishmanias. Trends Microbiol 7 : 82 88.
    • (1999) Trends Microbiol , vol.7 , pp. 82-88
    • Barrett, M.P.1    Mottram, J.C.2    Coombs, G.H.3
  • 5
    • 0027996240 scopus 로고
    • PTR1: A reductase mediating salvage of oxidized pteridines and methotrexate resistance in the protozoan parasite Leishmania major
    • Bello, A.R., Nare, B., Freedman, D., Hardy, L. Beverley, S.M. (1994) PTR1: a reductase mediating salvage of oxidized pteridines and methotrexate resistance in the protozoan parasite Leishmania major. Proc Natl Acad Sci USA 91 : 11442 11446.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11442-11446
    • Bello, A.R.1    Nare, B.2    Freedman, D.3    Hardy, L.4    Beverley, S.M.5
  • 7
    • 0037226127 scopus 로고    scopus 로고
    • Protozomics: Trypanosomatid parasite genetics comes of age
    • Beverley, S.M. (2003) Protozomics: trypanosomatid parasite genetics comes of age. Nat Rev Genet 4 : 11 19.
    • (2003) Nat Rev Genet , vol.4 , pp. 11-19
    • Beverley, S.M.1
  • 8
    • 18644379774 scopus 로고    scopus 로고
    • A polymorphism, R653Q, in the trifunctional enzyme methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase/formyltetrahydrofolate synthetase is a maternal genetic risk factor for neural tube defects: Report of the Birth Defects Research Group
    • Brody, L.C., Conley, M., Cox, C., Kirke, P.N., McKeever, M.P., Mills, J.L., et al. (2002) A polymorphism, R653Q, in the trifunctional enzyme methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase/formyltetrahydrofolate synthetase is a maternal genetic risk factor for neural tube defects: report of the Birth Defects Research Group. Am J Hum Genet 71 : 1207 1215.
    • (2002) Am J Hum Genet , vol.71 , pp. 1207-1215
    • Brody, L.C.1    Conley, M.2    Cox, C.3    Kirke, P.N.4    McKeever, M.P.5    Mills, J.L.6
  • 9
    • 36148930957 scopus 로고    scopus 로고
    • PH stability of individual folates during critical sample preparation steps in prevision of the analysis of plant folates
    • Brouwer, V.D., Zhang, G.F., Storozhenko, S., Straeten, D.V. Lambert, W.E. (2007) pH stability of individual folates during critical sample preparation steps in prevision of the analysis of plant folates. Phytochem Anal 18 : 496 508.
    • (2007) Phytochem Anal , vol.18 , pp. 496-508
    • Brouwer, V.D.1    Zhang, G.F.2    Storozhenko, S.3    Straeten, D.V.4    Lambert, W.E.5
  • 11
    • 40349108458 scopus 로고    scopus 로고
    • Discovery of potent pteridine reductase inhibitors to guide antiparasite drug development
    • Cavazzuti, A., Paglietti, G., Hunter, W.N., Gamarro, F., Piras, S., Loriga, M., et al. (2008) Discovery of potent pteridine reductase inhibitors to guide antiparasite drug development. Proc Natl Acad Sci USA 105 : 1448 1453.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 1448-1453
    • Cavazzuti, A.1    Paglietti, G.2    Hunter, W.N.3    Gamarro, F.4    Piras, S.5    Loriga, M.6
  • 12
    • 18144381509 scopus 로고    scopus 로고
    • Mitochondrial initiation factor 2 of Trypanosoma brucei binds imported formylated elongator-type tRNA (Met)
    • Charriere, F., Tan, T.H. Schneider, A. (2005) Mitochondrial initiation factor 2 of Trypanosoma brucei binds imported formylated elongator-type tRNA (Met). J Biol Chem 280 : 15659 15665.
    • (2005) J Biol Chem , vol.280 , pp. 15659-15665
    • Charriere, F.1    Tan, T.H.2    Schneider, A.3
  • 13
    • 33745095012 scopus 로고    scopus 로고
    • Mitochondrial one-carbon metabolism is adapted to the specific needs of yeast, plants and mammals
    • Christensen, K.E. MacKenzie, R.E. (2006) Mitochondrial one-carbon metabolism is adapted to the specific needs of yeast, plants and mammals. Bioessays 28 : 595 605.
    • (2006) Bioessays , vol.28 , pp. 595-605
    • Christensen, K.E.1    MacKenzie, R.E.2
  • 14
    • 51849134892 scopus 로고    scopus 로고
    • Mitochondrial methylenetetrahydrofolate dehydrogenase, methenyltetrahydrofolate cyclohydrolase, and formyltetrahydrofolate synthetases
    • Christensen, K.E. MacKenzie, R.E. (2008) Mitochondrial methylenetetrahydrofolate dehydrogenase, methenyltetrahydrofolate cyclohydrolase, and formyltetrahydrofolate synthetases. Vitam Horm 79 : 393 410.
    • (2008) Vitam Horm , vol.79 , pp. 393-410
    • Christensen, K.E.1    MacKenzie, R.E.2
  • 15
    • 14844297720 scopus 로고    scopus 로고
    • Disruption of the mthfd1 gene reveals a monofunctional 10-formyltetrahydrofolate synthetase in mammalian mitochondria
    • Christensen, K.E., Patel, H., Kuzmanov, U., Mejia, N.R. MacKenzie, R.E. (2005a) Disruption of the mthfd1 gene reveals a monofunctional 10-formyltetrahydrofolate synthetase in mammalian mitochondria. J Biol Chem 280 : 7597 7602.
    • (2005) J Biol Chem , vol.280 , pp. 7597-7602
    • Christensen, K.E.1    Patel, H.2    Kuzmanov, U.3    Mejia, N.R.4    MacKenzie, R.E.5
  • 16
    • 26644472196 scopus 로고    scopus 로고
    • Magnesium and phosphate ions enable NAD binding to methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase
    • Christensen, K.E., Mirza, I.A., Berghuis, A.M. MacKenzie, R.E. (2005b) Magnesium and phosphate ions enable NAD binding to methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase. J Biol Chem 280 : 34316 34323.
    • (2005) J Biol Chem , vol.280 , pp. 34316-34323
    • Christensen, K.E.1    Mirza, I.A.2    Berghuis, A.M.3    MacKenzie, R.E.4
  • 17
    • 0033198238 scopus 로고    scopus 로고
    • Genetic manipulation of kinetoplastida
    • Clayton, C.E. (1999) Genetic manipulation of kinetoplastida. Parasitol Today 15 : 372 378.
    • (1999) Parasitol Today , vol.15 , pp. 372-378
    • Clayton, C.E.1
  • 18
    • 0008614282 scopus 로고
    • Overproduction of a bifunctional thymidylate synthetase-dihydrofolate reductase and DNA amplification in methotrexate-resistant Leishmania tropica
    • Coderre, J.A., Beverley, S.M., Schimke, R.T. Santi, D.V. (1983) Overproduction of a bifunctional thymidylate synthetase-dihydrofolate reductase and DNA amplification in methotrexate-resistant Leishmania tropica. Proc Natl Acad Sci USA 80 : 2132 2136.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 2132-2136
    • Coderre, J.A.1    Beverley, S.M.2    Schimke, R.T.3    Santi, D.V.4
  • 19
    • 0025049856 scopus 로고
    • Gene replacement in parasitic protozoa
    • Cruz, A. Beverley, S.M. (1990) Gene replacement in parasitic protozoa. Nature 348 : 171 173.
    • (1990) Nature , vol.348 , pp. 171-173
    • Cruz, A.1    Beverley, S.M.2
  • 20
    • 0025882658 scopus 로고
    • Double targeted gene replacement for creating null mutants
    • Cruz, A., Coburn, C. Beverley, S.M. (1991) Double targeted gene replacement for creating null mutants. Proc Natl Acad Sci USA 88 : 7170 7174.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7170-7174
    • Cruz, A.1    Coburn, C.2    Beverley, S.M.3
  • 21
    • 0027410144 scopus 로고
    • Plasticity in chromosome number and testing of essential genes in Leishmania by targeting
    • Cruz, A.K., Titus, R. Beverley, S.M. (1993) Plasticity in chromosome number and testing of essential genes in Leishmania by targeting. Proc Natl Acad Sci USA 90 : 1599 1603.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 1599-1603
    • Cruz, A.K.1    Titus, R.2    Beverley, S.M.3
  • 22
    • 0036261663 scopus 로고    scopus 로고
    • Mitochondrial NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase is essential for embryonic development
    • Di Pietro, E., Sirois, J., Tremblay, M.L. MacKenzie, R.E. (2002) Mitochondrial NAD-dependent methylenetetrahydrofolate dehydrogenase- methenyltetrahydrofolate cyclohydrolase is essential for embryonic development. Mol Cell Biol 22 : 4158 4166.
    • (2002) Mol Cell Biol , vol.22 , pp. 4158-4166
    • Di Pietro, E.1    Sirois, J.2    Tremblay, M.L.3    MacKenzie, R.E.4
  • 23
    • 0030926411 scopus 로고    scopus 로고
    • Disruption of the trypanothione reductase gene of Leishmania decreases its ability to survive oxidative stress in macrophages
    • Dumas, C., Ouellette, M., Tovar, J., Cunningham, M.L., Fairlamb, A.H., Tamar, S., et al. (1997) Disruption of the trypanothione reductase gene of Leishmania decreases its ability to survive oxidative stress in macrophages. EMBO J 16 : 2590 2598.
    • (1997) EMBO J , vol.16 , pp. 2590-2598
    • Dumas, C.1    Ouellette, M.2    Tovar, J.3    Cunningham, M.L.4    Fairlamb, A.H.5    Tamar, S.6
  • 24
    • 0037057092 scopus 로고    scopus 로고
    • Characterization of the folylpolyglutamate synthetase gene and polyglutamylation of folates in the protozoan parasite Leishmania
    • El Fadili, A., Kundig, C. Ouellette, M. (2002) Characterization of the folylpolyglutamate synthetase gene and polyglutamylation of folates in the protozoan parasite Leishmania. Mol Biochem Parasitol 124 : 63 71.
    • (2002) Mol Biochem Parasitol , vol.124 , pp. 63-71
    • El Fadili, A.1    Kundig, C.2    Ouellette, M.3
  • 26
    • 0037192115 scopus 로고    scopus 로고
    • Metabolic pathway analysis in trypanosomes and malaria parasites
    • Fairlamb, A.H. (2002) Metabolic pathway analysis in trypanosomes and malaria parasites. Philos Trans R Soc Lond B Biol Sci 357 : 101 107.
    • (2002) Philos Trans R Soc Lond B Biol Sci , vol.357 , pp. 101-107
    • Fairlamb, A.H.1
  • 27
    • 0035458366 scopus 로고    scopus 로고
    • The art and design of genetic screens: Yeast
    • Forsburg, S.L. (2001) The art and design of genetic screens: yeast. Nat Rev Genet 2 : 659 668.
    • (2001) Nat Rev Genet , vol.2 , pp. 659-668
    • Forsburg, S.L.1
  • 29
  • 30
    • 0031282556 scopus 로고    scopus 로고
    • Biochemical and genetic tests for inhibitors of Leishmania pteridine pathways
    • Hardy, L.W., Matthews, W., Nare, B. Beverley, S.M. (1997) Biochemical and genetic tests for inhibitors of Leishmania pteridine pathways. Exp Parasitol 87 : 157 169.
    • (1997) Exp Parasitol , vol.87 , pp. 157-169
    • Hardy, L.W.1    Matthews, W.2    Nare, B.3    Beverley, S.M.4
  • 32
    • 0033169025 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol biosynthetic enzymes are localized to a stable tubular subcompartment of the endoplasmic reticulum in Leishmania mexicana
    • Ilgoutz, S.C., Mullin, K.A., Southwell, B.R. McConville, M.J. (1999a) Glycosylphosphatidylinositol biosynthetic enzymes are localized to a stable tubular subcompartment of the endoplasmic reticulum in Leishmania mexicana. EMBO J 18 : 3643 3654.
    • (1999) EMBO J , vol.18 , pp. 3643-3654
    • Ilgoutz, S.C.1    Mullin, K.A.2    Southwell, B.R.3    McConville, M.J.4
  • 33
    • 0033577698 scopus 로고    scopus 로고
    • Evidence that free GPI glycolipids are essential for growth of Leishmania mexicana
    • Ilgoutz, S.C., Zawadzki, J.L., Ralton, J.E. McConville, M.J. (1999b) Evidence that free GPI glycolipids are essential for growth of Leishmania mexicana. EMBO J 18 : 2746 2755.
    • (1999) EMBO J , vol.18 , pp. 2746-2755
    • Ilgoutz, S.C.1    Zawadzki, J.L.2    Ralton, J.E.3    McConville, M.J.4
  • 35
    • 33846847777 scopus 로고    scopus 로고
    • Leishmania vaccines: Progress and problems
    • Suppl
    • Kedzierski, L., Zhu, Y. Handman, E. (2006) Leishmania vaccines: progress and problems. Parasitology 133 (Suppl S87 S112.
    • (2006) Parasitology , vol.133
    • Kedzierski, L.1    Zhu, Y.2    Handman, E.3
  • 36
    • 0020570527 scopus 로고
    • Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles
    • Kozak, M. (1983) Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles. Microbiol Rev 47 : 1 45.
    • (1983) Microbiol Rev , vol.47 , pp. 1-45
    • Kozak, M.1
  • 37
    • 0034015357 scopus 로고    scopus 로고
    • Initiation of protein synthesis in Saccharomyces cerevisiae mitochondria without formylation of the initiator tRNA
    • Li, Y., Holmes, W.B., Appling, D.R. RajBhandary, U.L. (2000) Initiation of protein synthesis in Saccharomyces cerevisiae mitochondria without formylation of the initiator tRNA. J Bacteriol 182 : 2886 2892.
    • (2000) J Bacteriol , vol.182 , pp. 2886-2892
    • Li, Y.1    Holmes, W.B.2    Appling, D.R.3    Rajbhandary, U.L.4
  • 39
    • 0027262263 scopus 로고
    • Rapid isolation of DNA from trypanosomatid protozoa using a simple 'mini-prep' procedure
    • Medina-Acosta, E. Cross, G.A. (1993) Rapid isolation of DNA from trypanosomatid protozoa using a simple 'mini-prep' procedure. Mol Biochem Parasitol 59 : 327 329.
    • (1993) Mol Biochem Parasitol , vol.59 , pp. 327-329
    • Medina-Acosta, E.1    Cross, G.A.2
  • 40
    • 0023695662 scopus 로고
    • NAD-dependent methylenetetrahydrofolate dehydrogenase- methenyltetrahydrofolate cyclohydrolase in transformed cells is a mitochondrial enzyme
    • Mejia, N.R. MacKenzie, R.E. (1988) NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase in transformed cells is a mitochondrial enzyme. Biochem Biophys Res Commun 155 : 1 6.
    • (1988) Biochem Biophys Res Commun , vol.155 , pp. 1-6
    • Mejia, N.R.1    MacKenzie, R.E.2
  • 41
    • 34247579197 scopus 로고    scopus 로고
    • Chemotherapy of leishmaniasis: Past, present and future
    • Mishra, J., Saxena, A. Singh, S. (2007) Chemotherapy of leishmaniasis: past, present and future. Curr Med Chem 14 : 1153 1169.
    • (2007) Curr Med Chem , vol.14 , pp. 1153-1169
    • Mishra, J.1    Saxena, A.2    Singh, S.3
  • 42
    • 0016285940 scopus 로고
    • Purification and characterization of nicotinamide adenine dinucleotide-dependent methylenetetrahydrofolate dehydrogenase from Clostridium formicoaceticum
    • Moore, M.R., O'Brien, W.E. Ljungdahl, L.G. (1974) Purification and characterization of nicotinamide adenine dinucleotide-dependent methylenetetrahydrofolate dehydrogenase from Clostridium formicoaceticum. J Biol Chem 249 : 5250 5253.
    • (1974) J Biol Chem , vol.249 , pp. 5250-5253
    • Moore, M.R.1    O'Brien, W.E.2    Ljungdahl, L.G.3
  • 43
    • 0030921824 scopus 로고    scopus 로고
    • New approaches to Leishmania chemotherapy: Pteridine reductase 1 (PTR1) as a target and modulator of antifolate sensitivity
    • Nare, B., Luba, J., Hardy, L.W. Beverley, S. (1997) New approaches to Leishmania chemotherapy: pteridine reductase 1 (PTR1) as a target and modulator of antifolate sensitivity. Parasitology 114 : S101 S110.
    • (1997) Parasitology , vol.114
    • Nare, B.1    Luba, J.2    Hardy, L.W.3    Beverley, S.4
  • 44
    • 0033529488 scopus 로고    scopus 로고
    • Formylation is not essential for initiation of protein synthesis in all eubacteria
    • Newton, D.T., Creuzenet, C. Mangroo, D. (1999) Formylation is not essential for initiation of protein synthesis in all eubacteria. J Biol Chem 274 : 22143 22146.
    • (1999) J Biol Chem , vol.274 , pp. 22143-22146
    • Newton, D.T.1    Creuzenet, C.2    Mangroo, D.3
  • 45
    • 0026062946 scopus 로고
    • Isolation, characterization, and structural organization of 10-formyltetrahydrofolate synthetase from spinach leaves
    • Nour, J.M. Rabinowitz, J.C. (1991) Isolation, characterization, and structural organization of 10-formyltetrahydrofolate synthetase from spinach leaves. J Biol Chem 266 : 18363 18369.
    • (1991) J Biol Chem , vol.266 , pp. 18363-18369
    • Nour, J.M.1    Rabinowitz, J.C.2
  • 46
    • 19444371029 scopus 로고    scopus 로고
    • Comparative folate metabolism in humans and malaria parasites (part I): Pointers for malaria treatment from cancer chemotherapy
    • Nzila, A., Ward, S.A., Marsh, K., Sims, P.F. Hyde, J.E. (2005) Comparative folate metabolism in humans and malaria parasites (part I): pointers for malaria treatment from cancer chemotherapy. Trends Parasitol 21 : 292 298.
    • (2005) Trends Parasitol , vol.21 , pp. 292-298
    • Nzila, A.1    Ward, S.A.2    Marsh, K.3    Sims, P.F.4    Hyde, J.E.5
  • 47
    • 33947221526 scopus 로고    scopus 로고
    • Metabolism of Leishmania: Proven and predicted
    • Opperdoes, F.R. Coombs, G.H. (2007) Metabolism of Leishmania: proven and predicted. Trends Parasitol 23 : 149 158.
    • (2007) Trends Parasitol , vol.23 , pp. 149-158
    • Opperdoes, F.R.1    Coombs, G.H.2
  • 49
    • 0030665360 scopus 로고    scopus 로고
    • Parameters controlling the rate of gene targeting frequency in the protozoan parasite Leishmania
    • Papadopoulou, B. Dumas, C. (1997) Parameters controlling the rate of gene targeting frequency in the protozoan parasite Leishmania. Nucleic Acids Res 25 : 4278 4286.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4278-4286
    • Papadopoulou, B.1    Dumas, C.2
  • 50
    • 24344491209 scopus 로고    scopus 로고
    • A polymorphism in the MTHFD1 gene increases a mother's risk of having an unexplained second trimester pregnancy loss
    • Parle-McDermott, A., Pangilinan, F., Mills, J.L., Signore, C.C., Molloy, A.M., Cotter, A., et al. (2005) A polymorphism in the MTHFD1 gene increases a mother's risk of having an unexplained second trimester pregnancy loss. Mol Hum Reprod 11 : 477 480.
    • (2005) Mol Hum Reprod , vol.11 , pp. 477-480
    • Parle-Mcdermott, A.1    Pangilinan, F.2    Mills, J.L.3    Signore, C.C.4    Molloy, A.M.5    Cotter, A.6
  • 51
    • 0038819954 scopus 로고    scopus 로고
    • Mammalian fibroblasts lacking mitochondrial NAD+-dependent methylenetetrahydrofolate dehydrogenase-cyclohydrolase are glycine auxotrophs
    • Patel, H., Pietro, E.D. MacKenzie, R.E. (2003) Mammalian fibroblasts lacking mitochondrial NAD+-dependent methylenetetrahydrofolate dehydrogenase-cyclohydrolase are glycine auxotrophs. J Biol Chem 278 : 19436 19441.
    • (2003) J Biol Chem , vol.278 , pp. 19436-19441
    • Patel, H.1    Pietro, E.D.2    MacKenzie, R.E.3
  • 52
    • 0032570311 scopus 로고    scopus 로고
    • Methenyltetrahydrofolate cyclohydrolase is rate limiting for the enzymatic conversion of 10-formyltetrahydrofolate to 5,10- methylenetetrahydrofolate in bifunctional dehydrogenase-cyclohydrolase enzymes
    • Pawelek, P.D. MacKenzie, R.E. (1998) Methenyltetrahydrofolate cyclohydrolase is rate limiting for the enzymatic conversion of 10-formyltetrahydrofolate to 5,10-methylenetetrahydrofolate in bifunctional dehydrogenase-cyclohydrolase enzymes. Biochemistry 37 : 1109 1115.
    • (1998) Biochemistry , vol.37 , pp. 1109-1115
    • Pawelek, P.D.1    MacKenzie, R.E.2
  • 53
    • 34347339518 scopus 로고    scopus 로고
    • Comparative genomic analysis of three Leishmania species that cause diverse human disease
    • Peacock, C.S., Seeger, K., Harris, D., Murphy, L., Ruiz, J.C., Quail, M.A., et al. (2007) Comparative genomic analysis of three Leishmania species that cause diverse human disease. Nat Genet 39 : 839 847.
    • (2007) Nat Genet , vol.39 , pp. 839-847
    • Peacock, C.S.1    Seeger, K.2    Harris, D.3    Murphy, L.4    Ruiz, J.C.5    Quail, M.A.6
  • 54
    • 3643128069 scopus 로고    scopus 로고
    • Effects of sulfanilamide and methotrexate on 13C fluxes through the glycine decarboxylase/serine hydroxymethyltransferase enzyme system in arabidopsis
    • Prabhu, V., Chatson, K.B., Lui, H., Abrams, G.D. King, J. (1998) Effects of sulfanilamide and methotrexate on 13C fluxes through the glycine decarboxylase/serine hydroxymethyltransferase enzyme system in arabidopsis. Plant Physiol 116 : 137 144.
    • (1998) Plant Physiol , vol.116 , pp. 137-144
    • Prabhu, V.1    Chatson, K.B.2    Lui, H.3    Abrams, G.D.4    King, J.5
  • 55
    • 77952306859 scopus 로고
    • Preparation and properties of 5,10-methenyltetrahydrofolic acid and 10-formyltetrahydrofolic acid
    • Rabinowitz, J.C. (1963) Preparation and properties of 5,10-methenyltetrahydrofolic acid and 10-formyltetrahydrofolic acid. Methods Enzymol 6 : 814 815.
    • (1963) Methods Enzymol , vol.6 , pp. 814-815
    • Rabinowitz, J.C.1
  • 56
    • 0001360467 scopus 로고
    • Formyltetrahydrofolate synthetase. I. Isolation and crystallization of the enzyme
    • Jr
    • Rabinowitz, J.C. Pricer, W.E., Jr (1962) Formyltetrahydrofolate synthetase. I. Isolation and crystallization of the enzyme. J Biol Chem 237 : 2898 2902.
    • (1962) J Biol Chem , vol.237 , pp. 2898-2902
    • Rabinowitz, J.C.1    Pricer, W.E.2
  • 57
    • 0028125575 scopus 로고
    • Initiator transfer RNAs
    • RajBhandary, U.L. (1994) Initiator transfer RNAs. J Bacteriol 176 : 547 552.
    • (1994) J Bacteriol , vol.176 , pp. 547-552
    • Rajbhandary, U.L.1
  • 58
    • 0034652330 scopus 로고    scopus 로고
    • More surprises in translation: Initiation without the initiator tRNA
    • RajBhandary, U.L. (2000) More surprises in translation: initiation without the initiator tRNA. Proc Natl Acad Sci USA 97 : 1325 1327.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 1325-1327
    • Rajbhandary, U.L.1
  • 59
    • 0037884861 scopus 로고    scopus 로고
    • Improvements in transfection efficiency and tests of RNA interference (RNAi) approaches in the protozoan parasite Leishmania
    • Robinson, K.A. Beverley, S.M. (2003) Improvements in transfection efficiency and tests of RNA interference (RNAi) approaches in the protozoan parasite Leishmania. Mol Biochem Parasitol 128 : 217 228.
    • (2003) Mol Biochem Parasitol , vol.128 , pp. 217-228
    • Robinson, K.A.1    Beverley, S.M.2
  • 60
    • 0034732937 scopus 로고    scopus 로고
    • Structures of three inhibitor complexes provide insight into the reaction mechanism of the human methylenetetrahydrofolate dehydrogenase/cyclohydrolase
    • Schmidt, A., Wu, H., MacKenzie, R.E., Chen, V.J., Bewly, J.R., Ray, J.E., et al. (2000) Structures of three inhibitor complexes provide insight into the reaction mechanism of the human methylenetetrahydrofolate dehydrogenase/ cyclohydrolase. Biochemistry 39 : 6325 6335.
    • (2000) Biochemistry , vol.39 , pp. 6325-6335
    • Schmidt, A.1    Wu, H.2    MacKenzie, R.E.3    Chen, V.J.4    Bewly, J.R.5    Ray, J.E.6
  • 61
    • 0025361947 scopus 로고
    • Dihydrofolate reductase as a therapeutic target
    • Schweitzer, B.I., Dicker, A.P. Bertino, J.R. (1990) Dihydrofolate reductase as a therapeutic target. FASEB J 4 : 2441 2452.
    • (1990) FASEB J , vol.4 , pp. 2441-2452
    • Schweitzer, B.I.1    Dicker, A.P.2    Bertino, J.R.3
  • 62
    • 0023141861 scopus 로고
    • Folate utilization by Leishmania species and the identification of intracellular derivatives and folate-metabolizing enzymes
    • Scott, D.A., Coombs, G.H. Sanderson, B.E. (1987) Folate utilization by Leishmania species and the identification of intracellular derivatives and folate-metabolizing enzymes. Mol Biochem Parasitol 23 : 139 149.
    • (1987) Mol Biochem Parasitol , vol.23 , pp. 139-149
    • Scott, D.A.1    Coombs, G.H.2    Sanderson, B.E.3
  • 63
    • 38049148752 scopus 로고    scopus 로고
    • The role of the mitochondrial glycine cleavage complex in the metabolism and virulence of the protozoan parasite Leishmania major
    • Scott, D.A., Hickerson, S.M., Vickers, T.J. Beverley, S.M. (2008) The role of the mitochondrial glycine cleavage complex in the metabolism and virulence of the protozoan parasite Leishmania major. J Biol Chem 283 : 155 165.
    • (2008) J Biol Chem , vol.283 , pp. 155-165
    • Scott, D.A.1    Hickerson, S.M.2    Vickers, T.J.3    Beverley, S.M.4
  • 64
    • 33751404556 scopus 로고    scopus 로고
    • Leishmania donovani: Dyskinetoplastid cells survive and proliferate in the presence of pyruvate and uridine but do not undergo apoptosis after treatment with camptothecin
    • Sen, N., Banerjee, B., Gupta, S.S., Das, B.B., Ganguly, A. Majumder, H.K. (2007) Leishmania donovani: dyskinetoplastid cells survive and proliferate in the presence of pyruvate and uridine but do not undergo apoptosis after treatment with camptothecin. Exp Parasitol 115 : 215 219.
    • (2007) Exp Parasitol , vol.115 , pp. 215-219
    • Sen, N.1    Banerjee, B.2    Gupta, S.S.3    Das, B.B.4    Ganguly, A.5    Majumder, H.K.6
  • 65
    • 6044234880 scopus 로고    scopus 로고
    • Interaction of mitochondrial initiation factor 2 with mitochondrial fMet-tRNA
    • Spencer, A.C. Spremulli, L.L. (2004) Interaction of mitochondrial initiation factor 2 with mitochondrial fMet-tRNA. Nucleic Acids Res 32 : 5464 5470.
    • (2004) Nucleic Acids Res , vol.32 , pp. 5464-5470
    • Spencer, A.C.1    Spremulli, L.L.2
  • 66
    • 0036229177 scopus 로고    scopus 로고
    • Physiology of folic acid in health and disease
    • Stanger, O. (2002) Physiology of folic acid in health and disease. Curr Drug Metab 3 : 211 223.
    • (2002) Curr Drug Metab , vol.3 , pp. 211-223
    • Stanger, O.1
  • 68
    • 0017576548 scopus 로고
    • Methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase. A multifunctional protein from porcine liver
    • Tan, L.U., Drury, E.J. MacKenzie, R.E. (1977) Methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase. A multifunctional protein from porcine liver. J Biol Chem 252 : 1117 1122.
    • (1977) J Biol Chem , vol.252 , pp. 1117-1122
    • Tan, L.U.1    Drury, E.J.2    MacKenzie, R.E.3
  • 69
    • 0037022225 scopus 로고    scopus 로고
    • Eukaryotic-type elongator tRNAMet of Trypanosoma brucei becomes formylated after import into mitochondria
    • Tan, T.H., Bochud-Allemann, N., Horn, E.K. Schneider, A. (2002) Eukaryotic-type elongator tRNAMet of Trypanosoma brucei becomes formylated after import into mitochondria. Proc Natl Acad Sci USA 99 : 1152 1157.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 1152-1157
    • Tan, T.H.1    Bochud-Allemann, N.2    Horn, E.K.3    Schneider, A.4
  • 70
    • 0020034886 scopus 로고
    • Synthesis of pseudo cofactor analogues as potential inhibitors of the folate enzymes
    • Jr. Jr
    • Temple, C., Bennett, L.L., Jr, Rose, J.D., Jr, Elliott, R.D., Montgomery J.A. Mangum, J.H. (1982) Synthesis of pseudo cofactor analogues as potential inhibitors of the folate enzymes. J Med Chem 25 : 161 166.
    • (1982) J Med Chem , vol.25 , pp. 161-166
    • Temple, C.1    Bennett, L.L.2    Rose, J.D.3    Elliott, R.D.4    Montgomery, J.A.5    Mangum, J.H.6
  • 71
    • 1942423110 scopus 로고    scopus 로고
    • Antimicrobial dihydrofolate reductase inhibitors - Achievements and future options: Review
    • Then, R.L. (2004) Antimicrobial dihydrofolate reductase inhibitors - achievements and future options: review. J Chemother 16 : 3 12.
    • (2004) J Chemother , vol.16 , pp. 3-12
    • Then, R.L.1
  • 72
    • 0032454658 scopus 로고    scopus 로고
    • The antiproliferative and cell cycle effects of 5,6,7,8-tetrahydro-N5, N10-carbonylfolic acid, an inhibitor of methylenetetrahydrofolate dehydrogenase, are potentiated by hypoxanthine
    • Tonkinson, J.L., Habeck, L.L., Toth, J.E., Mendelsohn, L.G., Bewley, J., Shackelford, K.A., et al. (1998) The antiproliferative and cell cycle effects of 5,6,7,8-tetrahydro-N5,N10-carbonylfolic acid, an inhibitor of methylenetetrahydrofolate dehydrogenase, are potentiated by hypoxanthine. J Pharmacol Exp Ther 287 : 315 321.
    • (1998) J Pharmacol Exp Ther , vol.287 , pp. 315-321
    • Tonkinson, J.L.1    Habeck, L.L.2    Toth, J.E.3    Mendelsohn, L.G.4    Bewley, J.5    Shackelford, K.A.6
  • 74
    • 28044445460 scopus 로고    scopus 로고
    • Targeted disruption of cytosolic SIR2 deacetylase discloses its essential role in Leishmania survival and proliferation
    • Vergnes, B., Sereno, D., Tavares, J., Cordeiro-da-Silva, A., Vanhille, L., Madjidian-Sereno, N., et al. (2005) Targeted disruption of cytosolic SIR2 deacetylase discloses its essential role in Leishmania survival and proliferation. Gene 363 : 85 96.
    • (2005) Gene , vol.363 , pp. 85-96
    • Vergnes, B.1    Sereno, D.2    Tavares, J.3    Cordeiro-Da-Silva, A.4    Vanhille, L.5    Madjidian-Sereno, N.6
  • 75
    • 0037417724 scopus 로고    scopus 로고
    • Mitochondrial methionyl-tRNAfMet formyltransferase from Saccharomyces cerevisiae: Gene disruption and tRNA substrate specificity
    • Vial, L., Gomez, P., Panvert, M., Schmitt, E., Blanquet, S. Mechulam, Y. (2003) Mitochondrial methionyl-tRNAfMet formyltransferase from Saccharomyces cerevisiae: gene disruption and tRNA substrate specificity. Biochemistry 42 : 932 939.
    • (2003) Biochemistry , vol.42 , pp. 932-939
    • Vial, L.1    Gomez, P.2    Panvert, M.3    Schmitt, E.4    Blanquet, S.5    Mechulam, Y.6
  • 76
    • 33845988740 scopus 로고    scopus 로고
    • Biochemical and genetic analysis of methylenetetrahydrofolate reductase in Leishmania metabolism and virulence
    • Vickers, T.J., Orsomando, G., de la Garza, R.D., Scott, D.A., Kang, S.O., Hanson, A.D. Beverley, S.M. (2006) Biochemical and genetic analysis of methylenetetrahydrofolate reductase in Leishmania metabolism and virulence. J Biol Chem 281 : 38150 38158.
    • (2006) J Biol Chem , vol.281 , pp. 38150-38158
    • Vickers, T.J.1    Orsomando, G.2    De La Garza, R.D.3    Scott, D.A.4    Kang, S.O.5    Hanson, A.D.6    Beverley, S.M.7
  • 77
    • 13844256579 scopus 로고    scopus 로고
    • Light-driven enzymatic catalysis of DNA repair: A review of recent biophysical studies on photolyase
    • Weber, S. (2005) Light-driven enzymatic catalysis of DNA repair: a review of recent biophysical studies on photolyase. Biochim Biophys Acta 1707 : 1 23.
    • (2005) Biochim Biophys Acta , vol.1707 , pp. 1-23
    • Weber, S.1
  • 78
    • 0029929264 scopus 로고    scopus 로고
    • Metabolic role of cytoplasmic isozymes of 5,10-methylenetetrahydrofolate dehydrogenase in Saccharomyces cerevisiae
    • West, M.G., Horne, D.W. Appling, D.R. (1996) Metabolic role of cytoplasmic isozymes of 5,10-methylenetetrahydrofolate dehydrogenase in Saccharomyces cerevisiae. Biochemistry 35 : 3122 3132.
    • (1996) Biochemistry , vol.35 , pp. 3122-3132
    • West, M.G.1    Horne, D.W.2    Appling, D.R.3
  • 79
    • 0037846072 scopus 로고    scopus 로고
    • Rational design, synthesis, evaluation, and crystal structure of a potent inhibitor of human GAR Tfase: 10-(trifluoroacetyl)-5, 10-dideazaacyclic-5,6,7, 8-tetrahydrofolic acid
    • Zhang, Y., Desharnais, J., Marsilje, T.H., Li, C., Hedrick, M.P., Gooljarsingh, L.T., et al. (2003) Rational design, synthesis, evaluation, and crystal structure of a potent inhibitor of human GAR Tfase: 10-(trifluoroacetyl) -5, 10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid. Biochemistry 42 : 6043 6056.
    • (2003) Biochemistry , vol.42 , pp. 6043-6056
    • Zhang, Y.1    Desharnais, J.2    Marsilje, T.H.3    Li, C.4    Hedrick, M.P.5    Gooljarsingh, L.T.6


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