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Volumn 11, Issue 1, 2015, Pages 164-174

Genetic investigation of tricarboxylic acid metabolism during the plasmodium falciparum life cycle

Author keywords

[No Author keywords available]

Indexed keywords

TRICARBOXYLIC ACID; ANTIMALARIAL AGENT; ENZYME;

EID: 84927697401     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2015.03.011     Document Type: Article
Times cited : (122)

References (40)
  • 3
    • 80052695300 scopus 로고    scopus 로고
    • Arrested oocyst maturation in Plasmodium parasites lacking type II NADH:ubiquinone dehydrogenase
    • Boysen K.E., Matuschewski K. Arrested oocyst maturation in Plasmodium parasites lacking type II NADH:ubiquinone dehydrogenase. J.Biol. Chem. 2011, 286:32661-32671.
    • (2011) J.Biol. Chem. , vol.286 , pp. 32661-32671
    • Boysen, K.E.1    Matuschewski, K.2
  • 4
    • 4243071596 scopus 로고    scopus 로고
    • The transcriptome of the intraerythrocytic developmental cycle of Plasmodium falciparum
    • Bozdech Z., Llinás M., Pulliam B.L., Wong E.D., Zhu J., DeRisi J.L. The transcriptome of the intraerythrocytic developmental cycle of Plasmodium falciparum. PLoS Biol. 2003, 1:E5.
    • (2003) PLoS Biol. , vol.1 , pp. E5
    • Bozdech, Z.1    Llinás, M.2    Pulliam, B.L.3    Wong, E.D.4    Zhu, J.5    DeRisi, J.L.6
  • 5
    • 79953213641 scopus 로고    scopus 로고
    • Metabolic fate of fumarate, a side product of the purine salvage pathway in the intraerythrocytic stages of Plasmodium falciparum
    • Bulusu V., Jayaraman V., Balaram H. Metabolic fate of fumarate, a side product of the purine salvage pathway in the intraerythrocytic stages of Plasmodium falciparum. J.Biol. Chem. 2011, 286:9236-9245.
    • (2011) J.Biol. Chem. , vol.286 , pp. 9236-9245
    • Bulusu, V.1    Jayaraman, V.2    Balaram, H.3
  • 7
    • 79958768780 scopus 로고    scopus 로고
    • Role of aminotransferases in glutamate metabolism of human erythrocytes
    • Ellinger J.J., Lewis I.A., Markley J.L. Role of aminotransferases in glutamate metabolism of human erythrocytes. J.Biomol. NMR 2011, 49:221-229.
    • (2011) J.Biomol. NMR , vol.49 , pp. 221-229
    • Ellinger, J.J.1    Lewis, I.A.2    Markley, J.L.3
  • 9
    • 0028301469 scopus 로고
    • Inhibitory action of the anti-malarial compound atovaquone (566C80) against Plasmodium berghei ANKA in the mosquito, Anopheles stephensi
    • Fowler R.E., Billingsley P.F., Pudney M., Sinden R.E. Inhibitory action of the anti-malarial compound atovaquone (566C80) against Plasmodium berghei ANKA in the mosquito, Anopheles stephensi. Parasitology 1994, 108:383-388.
    • (1994) Parasitology , vol.108 , pp. 383-388
    • Fowler, R.E.1    Billingsley, P.F.2    Pudney, M.3    Sinden, R.E.4
  • 10
    • 0026605065 scopus 로고
    • Site of action of the antimalarial hydroxynaphthoquinone, 2-[trans-4-(4'-chlorophenyl) cyclohexyl]-3-hydroxy-1,4-naphthoquinone (566C80)
    • Fry M., Pudney M. Site of action of the antimalarial hydroxynaphthoquinone, 2-[trans-4-(4'-chlorophenyl) cyclohexyl]-3-hydroxy-1,4-naphthoquinone (566C80). Biochem. Pharmacol. 1992, 43:1545-1553.
    • (1992) Biochem. Pharmacol. , vol.43 , pp. 1545-1553
    • Fry, M.1    Pudney, M.2
  • 12
    • 27844559736 scopus 로고    scopus 로고
    • Plasmodium falciparum possesses organelle-specific alpha-keto acid dehydrogenase complexes and lipoylation pathways
    • Günther S., McMillan P.J., Wallace L.J., Müller S. Plasmodium falciparum possesses organelle-specific alpha-keto acid dehydrogenase complexes and lipoylation pathways. Biochem. Soc. Trans. 2005, 33:977-980.
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 977-980
    • Günther, S.1    McMillan, P.J.2    Wallace, L.J.3    Müller, S.4
  • 13
    • 84865722938 scopus 로고    scopus 로고
    • Critical roles of the mitochondrial complex II in oocyst formation of rodent malaria parasite Plasmodium berghei
    • Hino A., Hirai M., Tanaka T.Q., Watanabe Y., Matsuoka H., Kita K. Critical roles of the mitochondrial complex II in oocyst formation of rodent malaria parasite Plasmodium berghei. J.Biochem. 2012, 152:259-268.
    • (2012) J.Biochem. , vol.152 , pp. 259-268
    • Hino, A.1    Hirai, M.2    Tanaka, T.Q.3    Watanabe, Y.4    Matsuoka, H.5    Kita, K.6
  • 15
    • 79961089179 scopus 로고    scopus 로고
    • Variation among Plasmodium falciparum strains in their reliance on mitochondrial electron transport chain function
    • Ke H., Morrisey J.M., Ganesan S.M., Painter H.J., Mather M.W., Vaidya A.B. Variation among Plasmodium falciparum strains in their reliance on mitochondrial electron transport chain function. Eukaryot. Cell 2011, 10:1053-1061.
    • (2011) Eukaryot. Cell , vol.10 , pp. 1053-1061
    • Ke, H.1    Morrisey, J.M.2    Ganesan, S.M.3    Painter, H.J.4    Mather, M.W.5    Vaidya, A.B.6
  • 17
    • 77951072181 scopus 로고    scopus 로고
    • Metabolomic analysis via reversed-phase ion-pairing liquid chromatography coupled to a stand alone orbitrap mass spectrometer
    • Lu W., Clasquin M.F., Melamud E., Amador-Noguez D., Caudy A.A., Rabinowitz J.D. Metabolomic analysis via reversed-phase ion-pairing liquid chromatography coupled to a stand alone orbitrap mass spectrometer. Anal. Chem. 2010, 82:3212-3221.
    • (2010) Anal. Chem. , vol.82 , pp. 3212-3221
    • Lu, W.1    Clasquin, M.F.2    Melamud, E.3    Amador-Noguez, D.4    Caudy, A.A.5    Rabinowitz, J.D.6
  • 18
    • 84869167609 scopus 로고    scopus 로고
    • Mitochondrial metabolism of glucose and glutamine is required for intracellular growth of Toxoplasma gondii
    • MacRae J.I., Sheiner L., Nahid A., Tonkin C., Striepen B., McConville M.J. Mitochondrial metabolism of glucose and glutamine is required for intracellular growth of Toxoplasma gondii. Cell Host Microbe 2012, 12:682-692.
    • (2012) Cell Host Microbe , vol.12 , pp. 682-692
    • MacRae, J.I.1    Sheiner, L.2    Nahid, A.3    Tonkin, C.4    Striepen, B.5    McConville, M.J.6
  • 20
    • 78649695759 scopus 로고    scopus 로고
    • Metabolomic analysis and visualization engine for LC-MS data
    • Melamud E., Vastag L., Rabinowitz J.D. Metabolomic analysis and visualization engine for LC-MS data. Anal. Chem. 2010, 82:9818-9826.
    • (2010) Anal. Chem. , vol.82 , pp. 9818-9826
    • Melamud, E.1    Vastag, L.2    Rabinowitz, J.D.3
  • 21
    • 84883378968 scopus 로고    scopus 로고
    • Malaria parasite-synthesized heme is essential in the mosquito and liver stages and complements host heme in the blood stages of infection
    • Nagaraj V.A., Sundaram B., Varadarajan N.M., Subramani P.A., Kalappa D.M., Ghosh S.K., Padmanaban G. Malaria parasite-synthesized heme is essential in the mosquito and liver stages and complements host heme in the blood stages of infection. PLoS Pathog. 2013, 9:e1003522.
    • (2013) PLoS Pathog. , vol.9 , pp. e1003522
    • Nagaraj, V.A.1    Sundaram, B.2    Varadarajan, N.M.3    Subramani, P.A.4    Kalappa, D.M.5    Ghosh, S.K.6    Padmanaban, G.7
  • 23
    • 80054926288 scopus 로고    scopus 로고
    • Cell-free synthesis, reconstitution, and characterization of a mitochondrial dicarboxylate-tricarboxylate carrier of Plasmodium falciparum
    • Nozawa A., Fujimoto R., Matsuoka H., Tsuboi T., Tozawa Y. Cell-free synthesis, reconstitution, and characterization of a mitochondrial dicarboxylate-tricarboxylate carrier of Plasmodium falciparum. Biochem. Biophys. Res. Commun. 2011, 414:612-617.
    • (2011) Biochem. Biophys. Res. Commun. , vol.414 , pp. 612-617
    • Nozawa, A.1    Fujimoto, R.2    Matsuoka, H.3    Tsuboi, T.4    Tozawa, Y.5
  • 26
    • 33847398001 scopus 로고    scopus 로고
    • Specific role of mitochondrial electron transport in blood-stage Plasmodium falciparum
    • Painter H.J., Morrisey J.M., Mather M.W., Vaidya A.B. Specific role of mitochondrial electron transport in blood-stage Plasmodium falciparum. Nature 2007, 446:88-91.
    • (2007) Nature , vol.446 , pp. 88-91
    • Painter, H.J.1    Morrisey, J.M.2    Mather, M.W.3    Vaidya, A.B.4
  • 27
    • 45749119578 scopus 로고    scopus 로고
    • Triazolopyrimidine-based dihydroorotate dehydrogenase inhibitors with potent and selective activity against the malaria parasite Plasmodium falciparum
    • Phillips M.A., Gujjar R., Malmquist N.A., White J., El Mazouni F., Baldwin J., Rathod P.K. Triazolopyrimidine-based dihydroorotate dehydrogenase inhibitors with potent and selective activity against the malaria parasite Plasmodium falciparum. J.Med. Chem. 2008, 51:3649-3653.
    • (2008) J.Med. Chem. , vol.51 , pp. 3649-3653
    • Phillips, M.A.1    Gujjar, R.2    Malmquist, N.A.3    White, J.4    El Mazouni, F.5    Baldwin, J.6    Rathod, P.K.7
  • 28
    • 0032760945 scopus 로고    scopus 로고
    • Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes
    • Schofield C.J., Zhang Z. Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes. Curr. Opin. Struct. Biol. 1999, 9:722-731.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 722-731
    • Schofield, C.J.1    Zhang, Z.2
  • 29
    • 28444497046 scopus 로고    scopus 로고
    • Invivo carbon-13 magnetization transfer effect. Detection of aspartate aminotransferase reaction
    • Shen J. Invivo carbon-13 magnetization transfer effect. Detection of aspartate aminotransferase reaction. Magn. Reson. Med. 2005, 54:1321-1326.
    • (2005) Magn. Reson. Med. , vol.54 , pp. 1321-1326
    • Shen, J.1
  • 30
    • 0000060558 scopus 로고
    • The preparation of S-succinyl coenzyme A
    • Simon E.J., Shemin D. The preparation of S-succinyl coenzyme A. J.Am. Chem. Soc. 1953, 75:2520.
    • (1953) J.Am. Chem. Soc. , vol.75 , pp. 2520
    • Simon, E.J.1    Shemin, D.2
  • 31
    • 0031052025 scopus 로고    scopus 로고
    • Atovaquone, a broad spectrum antiparasitic drug, collapses mitochondrial membrane potential in a malarial parasite
    • Srivastava I.K., Rottenberg H., Vaidya A.B. Atovaquone, a broad spectrum antiparasitic drug, collapses mitochondrial membrane potential in a malarial parasite. J.Biol. Chem. 1997, 272:3961-3966.
    • (1997) J.Biol. Chem. , vol.272 , pp. 3961-3966
    • Srivastava, I.K.1    Rottenberg, H.2    Vaidya, A.B.3
  • 33
    • 0035152999 scopus 로고    scopus 로고
    • Isolation of mitochondria from Plasmodium falciparum showing dihydroorotate dependent respiration
    • Takashima E., Takamiya S., Takeo S., Mi-ichi F., Amino H., Kita K. Isolation of mitochondria from Plasmodium falciparum showing dihydroorotate dependent respiration. Parasitol. Int. 2001, 50:273-278.
    • (2001) Parasitol. Int. , vol.50 , pp. 273-278
    • Takashima, E.1    Takamiya, S.2    Takeo, S.3    Mi-ichi, F.4    Amino, H.5    Kita, K.6
  • 34
    • 0034656342 scopus 로고    scopus 로고
    • Succinate dehydrogenase in Plasmodium falciparum mitochondria: molecular characterization of the SDHA and SDHB genes for the catalytic subunits, the flavoprotein (Fp) and iron-sulfur (Ip) subunits
    • Takeo S., Kokaze A., Ng C.S., Mizuchi D., Watanabe J.I., Tanabe K., Kojima S., Kita K. Succinate dehydrogenase in Plasmodium falciparum mitochondria: molecular characterization of the SDHA and SDHB genes for the catalytic subunits, the flavoprotein (Fp) and iron-sulfur (Ip) subunits. Mol. Biochem. Parasitol. 2000, 107:191-205.
    • (2000) Mol. Biochem. Parasitol. , vol.107 , pp. 191-205
    • Takeo, S.1    Kokaze, A.2    Ng, C.S.3    Mizuchi, D.4    Watanabe, J.I.5    Tanabe, K.6    Kojima, S.7    Kita, K.8
  • 35
    • 84865984255 scopus 로고    scopus 로고
    • Toward understanding the role of mitochondrial complex II in the intraerythrocytic stages of Plasmodium falciparum: gene targeting of the Fp subunit
    • Tanaka T.Q., Hirai M., Watanabe Y., Kita K. Toward understanding the role of mitochondrial complex II in the intraerythrocytic stages of Plasmodium falciparum: gene targeting of the Fp subunit. Parasitol. Int. 2012, 61:726-728.
    • (2012) Parasitol. Int. , vol.61 , pp. 726-728
    • Tanaka, T.Q.1    Hirai, M.2    Watanabe, Y.3    Kita, K.4
  • 36
    • 3343010591 scopus 로고    scopus 로고
    • Localization of organellar proteins in Plasmodium falciparum using a novel set of transfection vectors and a new immunofluorescence fixation method
    • Tonkin C.J., van Dooren G.G., Spurck T.P., Struck N.S., Good R.T., Handman E., Cowman A.F., McFadden G.I. Localization of organellar proteins in Plasmodium falciparum using a novel set of transfection vectors and a new immunofluorescence fixation method. Mol. Biochem. Parasitol. 2004, 137:13-21.
    • (2004) Mol. Biochem. Parasitol. , vol.137 , pp. 13-21
    • Tonkin, C.J.1    van Dooren, G.G.2    Spurck, T.P.3    Struck, N.S.4    Good, R.T.5    Handman, E.6    Cowman, A.F.7    McFadden, G.I.8
  • 37
    • 70349536103 scopus 로고    scopus 로고
    • Mitochondrial evolution and functions in malaria parasites
    • Vaidya A.B., Mather M.W. Mitochondrial evolution and functions in malaria parasites. Annu. Rev. Microbiol. 2009, 63:249-267.
    • (2009) Annu. Rev. Microbiol. , vol.63 , pp. 249-267
    • Vaidya, A.B.1    Mather, M.W.2
  • 38
    • 84927692151 scopus 로고    scopus 로고
    • World Malaria Report.
    • WHO (2013). World Malaria Report. http://www.who.int/malaria/publications/world_malaria_report_2013/report/en.
    • (2013)
  • 39
    • 0023909061 scopus 로고
    • Two biochemically distinct classes of fumarase in Escherichia coli
    • Woods S.A., Schwartzbach S.D., Guest J.R. Two biochemically distinct classes of fumarase in Escherichia coli. Biochim. Biophys. Acta 1988, 954:14-26.
    • (1988) Biochim. Biophys. Acta , vol.954 , pp. 14-26
    • Woods, S.A.1    Schwartzbach, S.D.2    Guest, J.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.