메뉴 건너뛰기




Volumn 55, Issue 1, 2005, Pages 39-53

The malaria parasite Plasmodium falciparum has only one pyruvate dehydrogenase complex, which is located in the apicoplast

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; GREEN FLUORESCENT PROTEIN; ISOENZYME; PYRUVATE DEHYDROGENASE COMPLEX;

EID: 12344312032     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2004.04407.x     Document Type: Article
Times cited : (150)

References (64)
  • 1
    • 0032813519 scopus 로고    scopus 로고
    • Crystal structure of 2-oxoisovalerate and dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes
    • Aevarsson, A., Seger, K., Turley, S., Sokatch, U.R., and Hol, W.G. (1999) Crystal structure of 2-oxoisovalerate and dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes. Nat Struct Biol 6: 785-792.
    • (1999) Nat Struct Biol , vol.6 , pp. 785-792
    • Aevarsson, A.1    Seger, K.2    Turley, S.3    Sokatch, U.R.4    Hol, W.G.5
  • 2
    • 0034653468 scopus 로고    scopus 로고
    • Crystal structure of human branched-chain alpha-ketoacid dehydrogenase and the molecular basis of multienzyme complex deficiency in maple syrup urine disease
    • Aevarsson, A., Chuang, J.L., Wynn, R.M., Turley, S., Chuang, D.T., and Hol, W.G. (2000) Crystal structure of human branched-chain alpha-ketoacid dehydrogenase and the molecular basis of multienzyme complex deficiency in maple syrup urine disease. Structure Fold Des 8: 277-291.
    • (2000) Structure Fold Des , vol.8 , pp. 277-291
    • Aevarsson, A.1    Chuang, J.L.2    Wynn, R.M.3    Turley, S.4    Chuang, D.T.5    Hol, W.G.6
  • 4
    • 0033999271 scopus 로고    scopus 로고
    • Overcoming codon bias: A method for high-level overexpression of Plasmodium and other AT-rich parasite genes in Escherichia coli
    • Baca, A.M., and Hol, W.G. (2000) Overcoming codon bias: a method for high-level overexpression of Plasmodium and other AT-rich parasite genes in Escherichia coli. Int J Parasitol 30: 113-118.
    • (2000) Int J Parasitol , vol.30 , pp. 113-118
    • Baca, A.M.1    Hol, W.G.2
  • 5
    • 0034112053 scopus 로고    scopus 로고
    • Understanding in vivo carbon precursor supply for fatty acid synthesis in leaf tissue
    • Bao, X., Focke, M., Pollard, M., and Ohlrogge, J. (2000) Understanding in vivo carbon precursor supply for fatty acid synthesis in leaf tissue. Plant J 22: 39-50.
    • (2000) Plant J , vol.22 , pp. 39-50
    • Bao, X.1    Focke, M.2    Pollard, M.3    Ohlrogge, J.4
  • 6
    • 0034932250 scopus 로고    scopus 로고
    • Methionine regeneration and aspartate aminotransferase in parasitic protozoa
    • Berger, L.C., Wilson, J., Wood, P., and Berger, B.J. (2001) Methionine regeneration and aspartate aminotransferase in parasitic protozoa. J Bacteriol 183: 4421-4434.
    • (2001) J Bacteriol , vol.183 , pp. 4421-4434
    • Berger, L.C.1    Wilson, J.2    Wood, P.3    Berger, B.J.4
  • 7
    • 4243071596 scopus 로고    scopus 로고
    • The transcriptome of the intraerythrocytic developmental cycle of Plasmodium falciparum
    • Bozdech, Z., Llinas, M., Pulliam, B.L., Wong, E.D., Zhu, J., and DeRisi, J.L. (2003) The transcriptome of the intraerythrocytic developmental cycle of Plasmodium falciparum. Plos Biol 1: 5.
    • (2003) Plos Biol , vol.1 , pp. 5
    • Bozdech, Z.1    Llinas, M.2    Pulliam, B.L.3    Wong, E.D.4    Zhu, J.5    DeRisi, J.L.6
  • 8
    • 0037015592 scopus 로고    scopus 로고
    • Genome sequence and comparative analysis of the model rodent malaria parasite Plasmodium yoelii yoelii
    • Carlton, J.M., Angiuoli, S.V., Suh, B.B., Kooij, T.W., Pertea, M., Silva, J.C., et al. (2002) Genome sequence and comparative analysis of the model rodent malaria parasite Plasmodium yoelii yoelii. Nature 419: 512-519.
    • (2002) Nature , vol.419 , pp. 512-519
    • Carlton, J.M.1    Angiuoli, S.V.2    Suh, B.B.3    Kooij, T.W.4    Pertea, M.5    Silva, J.C.6
  • 9
    • 0040424324 scopus 로고
    • Overproduction of bacterial chaperones improves the solubility of recombinant protein tyrosine kinases in Escherichia coli
    • Gaspers, P., Stieger, M., and Burn, P. (1994) Overproduction of bacterial chaperones improves the solubility of recombinant protein tyrosine kinases in Escherichia coli. Cell Mol Biol (Noisy-le-grand) 40: 635-644.
    • (1994) Cell Mol Biol (Noisy-le-grand) , vol.40 , pp. 635-644
    • Gaspers, P.1    Stieger, M.2    Burn, P.3
  • 10
    • 0038418364 scopus 로고    scopus 로고
    • Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase
    • Ciszak, E.M., Korotchkina, L.G., Dominiak, P.M., Sidhu, S., and Patel, M.S. (2003) Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase. J Biol Chem 278: 21240-21246.
    • (2003) J Biol Chem , vol.278 , pp. 21240-21246
    • Ciszak, E.M.1    Korotchkina, L.G.2    Dominiak, P.M.3    Sidhu, S.4    Patel, M.S.5
  • 11
    • 0029915525 scopus 로고    scopus 로고
    • Computational method to predict mitochondrially imported proteins and their targeting sequences
    • Claros, M.G., and Vincens, P. (1996) Computational method to predict mitochondrially imported proteins and their targeting sequences. Eur J Biochem 241: 779-786.
    • (1996) Eur J Biochem , vol.241 , pp. 779-786
    • Claros, M.G.1    Vincens, P.2
  • 12
    • 0029960688 scopus 로고    scopus 로고
    • Identification and purification of a distinct dihydrolipoamide dehydrogenase from pea chloroplasts
    • Conner, M., Krell, T., and Lindsay, J.G. (1996) Identification and purification of a distinct dihydrolipoamide dehydrogenase from pea chloroplasts. Planta 200: 195-202.
    • (1996) Planta , vol.200 , pp. 195-202
    • Conner, M.1    Krell, T.2    Lindsay, J.G.3
  • 14
    • 0037189526 scopus 로고    scopus 로고
    • Processing of an apicoplast leader sequence in Plasmodium falciparum, and the identification of a putative leader cleavage enzyme
    • van Dooren, G.G., Su, V., D'Ombrain, M.C., and McFadden, G.I. (2002) Processing of an apicoplast leader sequence in Plasmodium falciparum, and the identification of a putative leader cleavage enzyme. J Biol Chem 277: 23612-23619.
    • (2002) J Biol Chem , vol.277 , pp. 23612-23619
    • Van Dooren, G.G.1    Su, V.2    D'Ombrain, M.C.3    McFadden, G.I.4
  • 15
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • Emanuelsson, O., Nielsen, H., Brunak, S., and von Heijne, G. (2000) Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. J Mol Biol 300: 1005-1016.
    • (2000) J Mol Biol , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    Von Heijne, G.4
  • 16
    • 0037738615 scopus 로고    scopus 로고
    • The apicoplast: A plastid in Plasmodium falciparum and other Apicomplexan parasites
    • Foth, B.J., and McFadden, G.I. (2003) The apicoplast: a plastid in Plasmodium falciparum and other Apicomplexan parasites. Int Rev Cytol 224: 57-110.
    • (2003) Int Rev Cytol , vol.224 , pp. 57-110
    • Foth, B.J.1    McFadden, G.I.2
  • 17
    • 0037474121 scopus 로고    scopus 로고
    • Dissecting apicoplast targeting in the malaria parasite Plasmodium falciparum
    • Foth, B.J., Ralph, S.A., Tonkin, C.J., Struck, N.S., Fraunholz, M., Roos, D.S., et al. (2003) Dissecting apicoplast targeting in the malaria parasite Plasmodium falciparum. Science 299: 705-708.
    • (2003) Science , vol.299 , pp. 705-708
    • Foth, B.J.1    Ralph, S.A.2    Tonkin, C.J.3    Struck, N.S.4    Fraunholz, M.5    Roos, D.S.6
  • 18
    • 0037015614 scopus 로고    scopus 로고
    • The genome sequence of the human malaria parasite Plasmodium falciparum
    • Gardner, M.J., Hall, N., Fung, E., White, O., Berriman, M., Hyman, R.W., et al. (2002) The genome sequence of the human malaria parasite Plasmodium falciparum. Nature 419: 498-511.
    • (2002) Nature , vol.419 , pp. 498-511
    • Gardner, M.J.1    Hall, N.2    Fung, E.3    White, O.4    Berriman, M.5    Hyman, R.W.6
  • 19
    • 0142061141 scopus 로고    scopus 로고
    • Apicoplast fatty acid biosynthesis as a target for medical intervention in apicomplexan parasites
    • Gornicki, P. (2003) Apicoplast fatty acid biosynthesis as a target for medical intervention in apicomplexan parasites. Int J Parasitol 33: 885-896.
    • (2003) Int J Parasitol , vol.33 , pp. 885-896
    • Gornicki, P.1
  • 20
    • 0031148648 scopus 로고    scopus 로고
    • Characterization of the mouse dihydrolipoamide dehydrogenase (Dld) gene: Genomic structure, promoter sequence, and chromosomal localization
    • Johnson, M., Yang, H.S., Johanning, G.L., and Patel, M.S. (1997) Characterization of the mouse dihydrolipoamide dehydrogenase (Dld) gene: genomic structure, promoter sequence, and chromosomal localization. Genomics 41: 320-326.
    • (1997) Genomics , vol.41 , pp. 320-326
    • Johnson, M.1    Yang, H.S.2    Johanning, G.L.3    Patel, M.S.4
  • 21
    • 0034025564 scopus 로고    scopus 로고
    • 2-Oxoacid dehydrogenase multienzyme complexes in the halophilic Archaea? Gene sequences and protein structural predictions
    • Jolley, K.A., Maddocks, D.G., Gyles, S.L., Mullan, Z., Tang, S.L., Dyall-Smith, M.L., et al. (2000) 2-Oxoacid dehydrogenase multienzyme complexes in the halophilic Archaea? Gene sequences and protein structural predictions. Microbiology 146: 1061-1069.
    • (2000) Microbiology , vol.146 , pp. 1061-1069
    • Jolley, K.A.1    Maddocks, D.G.2    Gyles, S.L.3    Mullan, Z.4    Tang, S.L.5    Dyall-Smith, M.L.6
  • 22
    • 12644252019 scopus 로고    scopus 로고
    • Expression cloning and characterization of a cDNA encoding a novel membrane protein required for the formation of O-acetylated ganglioside: A putative acetyl-CoA transporter
    • Kanamori, A., Nakayama, J., Fukuda, M.N., Stallcup, W.B., Sasaki, K., Fukuda, M., and Hirabayashi, Y. (1997) Expression cloning and characterization of a cDNA encoding a novel membrane protein required for the formation of O-acetylated ganglioside: a putative acetyl-CoA transporter. Proc Natl Acad Sci USA 94: 2897-2902.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2897-2902
    • Kanamori, A.1    Nakayama, J.2    Fukuda, M.N.3    Stallcup, W.B.4    Sasaki, K.5    Fukuda, M.6    Hirabayashi, Y.7
  • 23
    • 0034047473 scopus 로고    scopus 로고
    • The role of pyruvate dehydrogenase and acetyl-coenzyme A synthetase in fatty acid synthesis in developing Arabidopsis seeds
    • Ke, J., Behal, R.H., Back, S.L., Nikolau, B.J., Wurtele, E.S., and Oliver, D.J. (2000) The role of pyruvate dehydrogenase and acetyl-coenzyme A synthetase in fatty acid synthesis in developing Arabidopsis seeds. Plant Physiol 123: 497-508.
    • (2000) Plant Physiol , vol.123 , pp. 497-508
    • Ke, J.1    Behal, R.H.2    Back, S.L.3    Nikolau, B.J.4    Wurtele, E.S.5    Oliver, D.J.6
  • 24
    • 0035807864 scopus 로고    scopus 로고
    • 3D structure and significance of the GPhiXXG helix packing motif in tetramers of the E1beta subunit of pyruvate dehydrogenase from the archeon Pyrobaculum aerophilum
    • Kleiger, G., Perry, J., and Eisenberg, D. (2001) 3D structure and significance of the GPhiXXG helix packing motif in tetramers of the E1beta subunit of pyruvate dehydrogenase from the archeon Pyrobaculum aerophilum. Biochemistry 40: 14484-14492.
    • (2001) Biochemistry , vol.40 , pp. 14484-14492
    • Kleiger, G.1    Perry, J.2    Eisenberg, D.3
  • 25
    • 0141633042 scopus 로고    scopus 로고
    • Discovery of gene function by expression profiling of the malaria parasite life cycle
    • Le Roch, K.G., Zhou, Y., Blair, P.L., Grainger, M., Moch, J.K., Haynes, J.D., et al. (2003) Discovery of gene function by expression profiling of the malaria parasite life cycle. Science 301: 1503-1508.
    • (2003) Science , vol.301 , pp. 1503-1508
    • Le Roch, K.G.1    Zhou, Y.2    Blair, P.L.3    Grainger, M.4    Moch, J.K.5    Haynes, J.D.6
  • 26
    • 0035889133 scopus 로고    scopus 로고
    • An IRP-like protein from Plasmodium falciparum binds to a mammalian iron-responsive element
    • Loyevsky, M., LaVaute, T., Allerson, C.R., Stearman, R., Kassim, O.O., Cooperman, S., et al. (2001) An IRP-like protein from Plasmodium falciparum binds to a mammalian iron-responsive element. Blood 98: 2555-2562.
    • (2001) Blood , vol.98 , pp. 2555-2562
    • Loyevsky, M.1    LaVaute, T.2    Allerson, C.R.3    Stearman, R.4    Kassim, O.O.5    Cooperman, S.6
  • 27
    • 0034721739 scopus 로고    scopus 로고
    • Molecular evidence of a unique lipoamide dehydrogenase in plastids: Analysis of plastidic lipoamide dehydrogenase from Arabidopsis thaliana
    • Lutziger, I., and Oliver, D.J. (2000) Molecular evidence of a unique lipoamide dehydrogenase in plastids: analysis of plastidic lipoamide dehydrogenase from Arabidopsis thaliana. FEBS Lett 484: 12-16.
    • (2000) FEBS Lett , vol.484 , pp. 12-16
    • Lutziger, I.1    Oliver, D.J.2
  • 28
    • 0034777745 scopus 로고    scopus 로고
    • Characterization of two cDNAs encoding mitochondrial lipoamide dehydrogenase from Arabidopsis
    • Lutziger, I., and Oliver, D.J. (2001) Characterization of two cDNAs encoding mitochondrial lipoamide dehydrogenase from Arabidopsis. Plant Physiol 127: 615-623.
    • (2001) Plant Physiol , vol.127 , pp. 615-623
    • Lutziger, I.1    Oliver, D.J.2
  • 29
    • 0026510711 scopus 로고
    • Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex
    • Mattevi, A., Obmolova, G., Schulze, E., Kalk, K.H., Westphal, A.M., de Kok, A., and Hol, W.G. (1992a) Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex. Science 255: 1544-1550.
    • (1992) Science , vol.255 , pp. 1544-1550
    • Mattevi, A.1    Obmolova, G.2    Schulze, E.3    Kalk, K.H.4    Westphal, A.M.5    De Kok, A.6    Hol, W.G.7
  • 30
    • 0026696413 scopus 로고
    • The refined crystal structure of Pseudomonas putida lipoamide dehydrogenase complexed with NAD+ at 2.45 A resolution
    • Mattevi, A., Obmolova, G., Sokatch, J.R., Betzel, C., and Hol, W.G. (1992b) The refined crystal structure of Pseudomonas putida lipoamide dehydrogenase complexed with NAD+ at 2.45 A resolution. Proteins 13: 336-351.
    • (1992) Proteins , vol.13 , pp. 336-351
    • Mattevi, A.1    Obmolova, G.2    Sokatch, J.R.3    Betzel, C.4    Hol, W.G.5
  • 31
    • 0027285476 scopus 로고
    • Crystallographic analysis of substrate binding and catalysis in dihydrolipoyl transacetylase (E2p)
    • Mattevi, A., Obmolova, G., Kalk, K.H., Teplyakov, A., and Hol, W.G. (1993) Crystallographic analysis of substrate binding and catalysis in dihydrolipoyl transacetylase (E2p). Biochemistry 32: 3887-3901.
    • (1993) Biochemistry , vol.32 , pp. 3887-3901
    • Mattevi, A.1    Obmolova, G.2    Kalk, K.H.3    Teplyakov, A.4    Hol, W.G.5
  • 32
    • 12344298301 scopus 로고    scopus 로고
    • The human malaria parasite Plasmodium falciparum possesses two distinct dihydrolipoamide dehydrogenases
    • doi:10.1111/ j.1365-2958.2004.04398.x
    • McMillan, P., Stimmler, L.M., Foth, B.J., McFadden, G.I., and Müller, S. (2004) The human malaria parasite Plasmodium falciparum possesses two distinct dihydrolipoamide dehydrogenases. Mol Microbiol doi:10.1111/ j.1365-2958.2004.04398.x
    • (2004) Mol Microbiol
    • McMillan, P.1    Stimmler, L.M.2    Foth, B.J.3    McFadden, G.I.4    Müller, S.5
  • 34
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H., Engelbrecht, J., Brunak, S., and von Heijne, G. (1997) Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng 10: 1-6.
    • (1997) Protein Eng , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 36
    • 0025221771 scopus 로고
    • Molecular biology and biochemistry of pyruvate dehydrogenase complexes
    • Patel, M.S., and Roche, T.E. (1990) Molecular biology and biochemistry of pyruvate dehydrogenase complexes. FASEB J 4: 3224-3233.
    • (1990) FASEB J , vol.4 , pp. 3224-3233
    • Patel, M.S.1    Roche, T.E.2
  • 38
    • 8444244485 scopus 로고    scopus 로고
    • Evolutionary pressures on apicoplast transit peptides
    • in press
    • Ralph, S.A., Foth, B.J., Hall, N., and McFadden, G.I. (2004a) Evolutionary pressures on apicoplast transit peptides. Mol Biol Evol (in press).
    • (2004) Mol Biol Evol
    • Ralph, S.A.1    Foth, B.J.2    Hall, N.3    McFadden, G.I.4
  • 40
    • 0036139124 scopus 로고    scopus 로고
    • Carbon flux and fatty acid synthesis in plants
    • Rawsthorne, S. (2002) Carbon flux and fatty acid synthesis in plants. Prog Lipid Res 41: 182-196.
    • (2002) Prog Lipid Res , vol.41 , pp. 182-196
    • Rawsthorne, S.1
  • 41
    • 0025977185 scopus 로고
    • Sequence similarities within the family of dihydrolipoamide acyltransferases and discovery of a previously unidentified fungal enzyme
    • Russell, G.C., and Guest, J.R. (1991) Sequence similarities within the family of dihydrolipoamide acyltransferases and discovery of a previously unidentified fungal enzyme. Biochim Biophys Acta 1076: 225-232.
    • (1991) Biochim Biophys Acta , vol.1076 , pp. 225-232
    • Russell, G.C.1    Guest, J.R.2
  • 43
    • 0036190131 scopus 로고    scopus 로고
    • Evolution of the enzymes of the citric acid cycle and the glyoxylate cycle of higher plants. A case study of endosymbiotic gene transfer
    • Schnarrenberger, C., and Martin, W. (2002) Evolution of the enzymes of the citric acid cycle and the glyoxylate cycle of higher plants. A case study of endosymbiotic gene transfer. Eur J Biochem 269: 868-883.
    • (2002) Eur J Biochem , vol.269 , pp. 868-883
    • Schnarrenberger, C.1    Martin, W.2
  • 44
    • 0031024753 scopus 로고    scopus 로고
    • Cloning, sequencing and functional expression of dihydrolipoamide dehydrogenase from the human pathogen Trypanosoma cruzi
    • Schoneck, R., Billaut-Mulot, O., Numrich, P., Ouaissi, M.A., and Krauth-Siegel, R.L. (1997) Cloning, sequencing and functional expression of dihydrolipoamide dehydrogenase from the human pathogen Trypanosoma cruzi. Eur J Biochem 243: 739-747.
    • (1997) Eur J Biochem , vol.243 , pp. 739-747
    • Schoneck, R.1    Billaut-Mulot, O.2    Numrich, P.3    Ouaissi, M.A.4    Krauth-Siegel, R.L.5
  • 45
    • 0014691256 scopus 로고
    • Alpha-keto acid dehydrogenase complexes. XII. Effects of acetylation on the activity and structure of the dihydrolipoyl transacetylase of Escherichia coli
    • Schwartz, E.R., and Reed, L.J. (1969) Alpha-keto acid dehydrogenase complexes. XII. Effects of acetylation on the activity and structure of the dihydrolipoyl transacetylase of Escherichia coli. J Biol Chem 244: 6074-6079.
    • (1969) J Biol Chem , vol.244 , pp. 6074-6079
    • Schwartz, E.R.1    Reed, L.J.2
  • 46
    • 0242580787 scopus 로고    scopus 로고
    • Identification, characterization and inhibition of Plasmodium falciparum beta-hydroxyacylacyl carrier protein dehydratase (FabZ)
    • Sharma, S.K., Kapoor, M., Ramya, T.N., Kumar, S., Kumar, G., Modak, R., et al. (2003) Identification, characterization and inhibition of Plasmodium falciparum beta-hydroxyacylacyl carrier protein dehydratase (FabZ). J Biol Chem 278: 45661-45671.
    • (2003) J Biol Chem , vol.278 , pp. 45661-45671
    • Sharma, S.K.1    Kapoor, M.2    Ramya, T.N.3    Kumar, S.4    Kumar, G.5    Modak, R.6
  • 47
    • 0021994766 scopus 로고
    • The murine plasma cell antigen PC-1: Purification and partial amino acid sequence
    • Stearne, P.A., van Driel, I.R., Grego, B., Simpson, R.J., and Goding, J.W. (1985) The murine plasma cell antigen PC-1: purification and partial amino acid sequence. J Immunol 134: 443-448.
    • (1985) J Immunol , vol.134 , pp. 443-448
    • Stearne, P.A.1    Van Driel, I.R.2    Grego, B.3    Simpson, R.J.4    Goding, J.W.5
  • 48
    • 0035126479 scopus 로고    scopus 로고
    • Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum
    • Surolia, N., and Surolia, A. (2001) Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum. Nat Med 7: 167-173.
    • (2001) Nat Med , vol.7 , pp. 167-173
    • Surolia, N.1    Surolia, A.2
  • 51
    • 0000644785 scopus 로고
    • Immunological comparison of the pyruvate dehydrogenase complexes from pea mitochondria and chloroplasts
    • Taylor, A.E., Cogdell, R.J., and Lindsay, J.G. (1992) Immunological comparison of the pyruvate dehydrogenase complexes from pea mitochondria and chloroplasts. Planta 188: 225-231.
    • (1992) Planta , vol.188 , pp. 225-231
    • Taylor, A.E.1    Cogdell, R.J.2    Lindsay, J.G.3
  • 52
    • 0038304827 scopus 로고    scopus 로고
    • Apicomplexan parasites contain a single lipoic acid synthase located in the plastid
    • Thomsen-Zieger, N., Schachtner, J., and Seeber, F. (2003) Apicomplexan parasites contain a single lipoic acid synthase located in the plastid. FEBS Lett 547: 80-86.
    • (2003) FEBS Lett , vol.547 , pp. 80-86
    • Thomsen-Zieger, N.1    Schachtner, J.2    Seeber, F.3
  • 53
    • 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., et al. (2004) Localization of organellar proteins in Plasmodium falciparum using a novel set of transfection vectors and a new immunofluorescence fixation method. Mol Biochem Parasitol 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
  • 54
    • 0031958863 scopus 로고    scopus 로고
    • Crystal structure of eucaryotic E3, lipoamide dehydrogenase from yeast
    • Toyoda, T., Suzuki, K., Sekiguchi, T., Reed, L.J., and Takenaka, A. (1998) Crystal structure of eucaryotic E3, lipoamide dehydrogenase from yeast. J Biochem (Tokyo) 123: 668-674.
    • (1998) J Biochem (Tokyo) , vol.123 , pp. 668-674
    • Toyoda, T.1    Suzuki, K.2    Sekiguchi, T.3    Reed, L.J.4    Takenaka, A.5
  • 55
    • 0017311840 scopus 로고
    • Human malaria parasites in continuous culture
    • Trager, W., and Jensen, J. (1976) Human malaria parasites in continuous culture. Science 193: 673-675.
    • (1976) Science , vol.193 , pp. 673-675
    • Trager, W.1    Jensen, J.2
  • 57
    • 0034678922 scopus 로고    scopus 로고
    • Protein trafficking to the plastid of Plasmodium falciparum is via the secretory pathway
    • Waller, R.F., Reed, M.B., Cowman, A.F., and McFadden, G.I. (2000) Protein trafficking to the plastid of Plasmodium falciparum is via the secretory pathway. EMBO J 19: 1794-1802.
    • (2000) EMBO J , vol.19 , pp. 1794-1802
    • Waller, R.F.1    Reed, M.B.2    Cowman, A.F.3    McFadden, G.I.4
  • 59
    • 0038408998 scopus 로고    scopus 로고
    • Isocitrate dehydrogenase of Plasmodium falciparum
    • Wrenger, C., and Muller, S. (2003) Isocitrate dehydrogenase of Plasmodium falciparum. Eur J Biochem 270: 1775-1783.
    • (2003) Eur J Biochem , vol.270 , pp. 1775-1783
    • Wrenger, C.1    Muller, S.2
  • 60
    • 3142630285 scopus 로고    scopus 로고
    • The human malaria parasite Plasmodium falciparum has distinct organelle-specific lipoylation pathways
    • Wrenger, C., and Muller, S. (2004) The human malaria parasite Plasmodium falciparum has distinct organelle-specific lipoylation pathways. Mol Microbiol 53: 103-113.
    • (2004) Mol Microbiol , vol.53 , pp. 103-113
    • Wrenger, C.1    Muller, S.2
  • 61
    • 0028985140 scopus 로고
    • Transfection of Plasmodium falciparum within human red blood cells
    • Wu, Y., Sifri, C.D., Lei, H.H., Su, X.Z., and Wellems, T.E. (1995) Transfection of Plasmodium falciparum within human red blood cells. Proc Natl Acad Sci USA 92: 973-977.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 973-977
    • Wu, Y.1    Sifri, C.D.2    Lei, H.H.3    Su, X.Z.4    Wellems, T.E.5
  • 62
    • 0030965608 scopus 로고    scopus 로고
    • Assembly and full functionality of recombinantly expressed dihydrolipoyl acetyltransferase component of the human pyruvate dehydrogenase complex
    • Yang, D., Song, J., Wagenknecht, T., and Roche, T.E. (1997) Assembly and full functionality of recombinantly expressed dihydrolipoyl acetyltransferase component of the human pyruvate dehydrogenase complex. J Biol Chem 272: 6361-6369.
    • (1997) J Biol Chem , vol.272 , pp. 6361-6369
    • Yang, D.1    Song, J.2    Wagenknecht, T.3    Roche, T.E.4
  • 63
    • 0035909958 scopus 로고    scopus 로고
    • The remarkable structural and functional organization of the eukaryotic pyruvate dehydrogenase complexes
    • Zhou, Z.H., McCarthy, D.B., O'Connor, C.M., Reed, L.J., and Stoops, J.K. (2001) The remarkable structural and functional organization of the eukaryotic pyruvate dehydrogenase complexes. Proc Natl Acad Sci USA 98: 14802-14807.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14802-14807
    • Zhou, Z.H.1    McCarthy, D.B.2    O'Connor, C.M.3    Reed, L.J.4    Stoops, J.K.5
  • 64
    • 0035666657 scopus 로고    scopus 로고
    • Deciphering apicoplast targeting signals - Feature extraction from nuclear-encoded precursors of Plasmodium falciparum apicoplast proteins
    • Zuegge, J., Ralph, S., Schmuker, M., McFadden, G.I., and Schneider, G. (2001) Deciphering apicoplast targeting signals - feature extraction from nuclear-encoded precursors of Plasmodium falciparum apicoplast proteins. Gene 280: 19-26.
    • (2001) Gene , vol.280 , pp. 19-26
    • Zuegge, J.1    Ralph, S.2    Schmuker, M.3    McFadden, G.I.4    Schneider, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.