메뉴 건너뛰기




Volumn 30, Issue 4, 2000, Pages 427-439

Impact of a plastid-bearing endocytobiont on apicomplexan genomes

Author keywords

Antibiotics; Biogenesis; Elongation factor Tu; Phylogeny; Plasmodium falciparum; Plastid genome; Structure; Toxoplasma gondii

Indexed keywords

ANTIBIOTIC AGENT; CIPROFLOXACIN; ELONGATION FACTOR; FOSMIDOMYCIN; MOCIMYCIN; RIFAMPICIN; RNA POLYMERASE; SIGNAL PEPTIDE; TRANSFER RNA;

EID: 0034114697     PISSN: 00207519     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0020-7519(99)00185-X     Document Type: Article
Times cited : (31)

References (90)
  • 1
    • 0030590259 scopus 로고    scopus 로고
    • Complete gene map of the plastid-like DNA of the malaria parasite Plasmodium falciparum
    • Wilson R.J.M., Denny P.W., Prieser P.R.et al. Complete gene map of the plastid-like DNA of the malaria parasite Plasmodium falciparum. J Mol Biol. 261:1996;155-172.
    • (1996) J Mol Biol , vol.261 , pp. 155-172
    • Wilson, R.J.M.1    Denny, P.W.2    Prieser, P.R.3
  • 2
    • 0040982083 scopus 로고    scopus 로고
    • A plastid of probable green algal origin in apicomplexan parasites
    • Kohler S., Delwiche C.F., Denny P.et al. A plastid of probable green algal origin in apicomplexan parasites. Science. 275:1997;1485-1489.
    • (1997) Science , vol.275 , pp. 1485-1489
    • Kohler, S.1    Delwiche, C.F.2    Denny, P.3
  • 3
    • 0030828806 scopus 로고    scopus 로고
    • Partial nucleotide sequence and organization of extrachromosomal plastid-like DNA in Plasmodium berghei
    • Yap M.W.C., Kara U.A.K., Heggel-Bordier B.T.et al. Partial nucleotide sequence and organization of extrachromosomal plastid-like DNA in Plasmodium berghei. Gene. 200:1997;91-98.
    • (1997) Gene , vol.200 , pp. 91-98
    • Yap, M.W.C.1    Kara, U.A.K.2    Heggel-Bordier, B.T.3
  • 4
    • 0031850991 scopus 로고    scopus 로고
    • Evidence for a single origin of the 35 kb plastid DNA in apicomplexans
    • Denny P., Preiser P., Williamson D.et al. Evidence for a single origin of the 35 kb plastid DNA in apicomplexans. Protist. 1:1998;51-59.
    • (1998) Protist , vol.1 , pp. 51-59
    • Denny, P.1    Preiser, P.2    Williamson, D.3
  • 5
    • 0032211044 scopus 로고    scopus 로고
    • Plastids are widespread and ancient in parasites of the phylum Apicomplexa
    • Lang-Unnasch N., Reith M.E., Munholland J.et al. Plastids are widespread and ancient in parasites of the phylum Apicomplexa. Int J Parasitol. 28:1998;1743-1754.
    • (1998) Int J Parasitol , vol.28 , pp. 1743-1754
    • Lang-Unnasch, N.1    Reith, M.E.2    Munholland, J.3
  • 6
    • 0024674380 scopus 로고
    • The complete sequence of the rice (Oryza sativa) chloroplast genome; Intermolecular recombination between distinct tRNA genes accounts for a major plastid inversion during the evolution of the cereals
    • Hiratsuka J., Shimada H., Whittier R.et al. The complete sequence of the rice (Oryza sativa) chloroplast genome; intermolecular recombination between distinct tRNA genes accounts for a major plastid inversion during the evolution of the cereals. Mol Gen Genet. 217:1989;185-194.
    • (1989) Mol Gen Genet , vol.217 , pp. 185-194
    • Hiratsuka, J.1    Shimada, H.2    Whittier, R.3
  • 7
    • 0019485803 scopus 로고
    • The chloroplasts of some algal groups may have evolved from endosymbiotic eukaryotic algae
    • Gibbs S.P. The chloroplasts of some algal groups may have evolved from endosymbiotic eukaryotic algae. Ann NY Acad Sci. 361:1981;193-208.
    • (1981) Ann NY Acad Sci , vol.361 , pp. 193-208
    • Gibbs, S.P.1
  • 8
    • 0030598645 scopus 로고    scopus 로고
    • Second-hand chloroplasts and the case of the disappearing nucleus
    • Palmer J.D., Delwiche C.F. Second-hand chloroplasts and the case of the disappearing nucleus. Proc Natl Acad Sci USA. 93:1996;7432-7435.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 7432-7435
    • Palmer, J.D.1    Delwiche, C.F.2
  • 12
    • 0344549379 scopus 로고    scopus 로고
    • Nuclear-encoded proteins target to the plastid in Toxoplasma gondii and Plasmodium falciparum
    • Waller R.F., Keeling P.J., Donald R.G.K.et al. Nuclear-encoded proteins target to the plastid in Toxoplasma gondii and Plasmodium falciparum. Proc Natl Acad Sci USA. 95:1998;12352-12357.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12352-12357
    • Waller, R.F.1    Keeling, P.J.2    Donald, R.G.K.3
  • 13
    • 0033213013 scopus 로고    scopus 로고
    • The plastid in Plasmodium falciparum asexual blood stages: A three-dimensional ultrastructural analysis
    • Hopkins J, Fowler R, Krishna S et al. The plastid in Plasmodium falciparum asexual blood stages: a three-dimensional ultrastructural analysis. Protist 1999;150:283 - 95.
    • (1999) Protist , vol.150 , pp. 283-295
    • Hopkins, J.1    Fowler, R.2    Krishna, S.3
  • 14
    • 0029989451 scopus 로고    scopus 로고
    • The evolution of stramenopiles and alveolates as derived by "substitution rate calibration" of small ribosomal subunit RNA
    • Van de Peer Y., Van de Auwera G., De Wachter R. The evolution of stramenopiles and alveolates as derived by "substitution rate calibration" of small ribosomal subunit RNA. J Mol Evol. 42:1996;201-210.
    • (1996) J Mol Evol , vol.42 , pp. 201-210
    • Van De Peer, Y.1    Van De Auwera, G.2    De Wachter, R.3
  • 15
    • 0026423881 scopus 로고
    • Cryptomonad algae are evolutionary chimaeras of two phylogenetically distinct unicellular eukaryotes
    • Douglas S.E., Murphy C.A., Spencer D.F.et al. Cryptomonad algae are evolutionary chimaeras of two phylogenetically distinct unicellular eukaryotes. Nature. 350:1991;148-151.
    • (1991) Nature , vol.350 , pp. 148-151
    • Douglas, S.E.1    Murphy, C.A.2    Spencer, D.F.3
  • 16
    • 0032434097 scopus 로고    scopus 로고
    • The phylogeny of glyceraldehye-3-phosphate dehydrogenase indicates lateral gene transfer from cryptomonads to dinoflagellates
    • Fagan T., Hastings J.W., Morse D. The phylogeny of glyceraldehye-3-phosphate dehydrogenase indicates lateral gene transfer from cryptomonads to dinoflagellates. J Mol Evol. 47:1998;633-639.
    • (1998) J Mol Evol , vol.47 , pp. 633-639
    • Fagan, T.1    Hastings, J.W.2    Morse, D.3
  • 17
    • 0029139369 scopus 로고
    • Something borrowed, something green: Lateral transfer of chloroplasts by secondary endosymbiosis
    • McFadden G., Gilson P. Something borrowed, something green: lateral transfer of chloroplasts by secondary endosymbiosis. Trends Evol. 10:1995;12-17.
    • (1995) Trends Evol , vol.10 , pp. 12-17
    • McFadden, G.1    Gilson, P.2
  • 18
    • 0030850422 scopus 로고    scopus 로고
    • The evolution of the Calvin cycle from prokaryotic to eukaryotic chromosomes: A case study of functional redundancy in ancient pathways through endosymbiosis
    • Martin W., Schnarrenberger C. The evolution of the Calvin cycle from prokaryotic to eukaryotic chromosomes: a case study of functional redundancy in ancient pathways through endosymbiosis. Curr Genet. 32:1997;1-18.
    • (1997) Curr Genet , vol.32 , pp. 1-18
    • Martin, W.1    Schnarrenberger, C.2
  • 19
    • 0028280998 scopus 로고
    • Molecular characterisation of the enolase gene from the human malaria parasite Plasmodium falciparum
    • Read M., Hicks K.E., Sims P.F.G.et al. Molecular characterisation of the enolase gene from the human malaria parasite Plasmodium falciparum. Eur J Biochem. 220:1994;513-520.
    • (1994) Eur J Biochem , vol.220 , pp. 513-520
    • Read, M.1    Hicks, K.E.2    Sims, P.F.G.3
  • 20
    • 0032987667 scopus 로고    scopus 로고
    • The apicoplast as a potential therapeutic target in Toxoplasma and other apicomplexan parasites
    • Soldati D. The apicoplast as a potential therapeutic target in Toxoplasma and other apicomplexan parasites. Parasitol Today. 15:1999;5-7.
    • (1999) Parasitol Today , vol.15 , pp. 5-7
    • Soldati, D.1
  • 21
    • 0015264523 scopus 로고
    • Purification and characterization of phosphoenolpyruvate carboxylase from Plasmodium berghei
    • McDaniel H.G., Siu P.M. Purification and characterization of phosphoenolpyruvate carboxylase from Plasmodium berghei. J Bacteriol. 109:1972;385-390.
    • (1972) J Bacteriol , vol.109 , pp. 385-390
    • McDaniel, H.G.1    Siu, P.M.2
  • 22
    • 0000283890 scopus 로고
    • The many-faceted function of phosphoenolpyruvate carboxylase in C3 plants
    • Latzko E., Kelly G.J. The many-faceted function of phosphoenolpyruvate carboxylase in C3 plants. Physiol Veg. 5:1983;817-825.
    • (1983) Physiol Veg , vol.5 , pp. 817-825
    • Latzko, E.1    Kelly, G.J.2
  • 23
    • 0029121431 scopus 로고
    • A mutant Bradyrhizobium japonicum δ-aminolevulinic acid dehydratase with an altered metal requirement functions in situ for tetrapyrrole synthesis in soybean root nodules
    • Chauhan S., O'Brian M.R. A mutant Bradyrhizobium japonicum δ-aminolevulinic acid dehydratase with an altered metal requirement functions in situ for tetrapyrrole synthesis in soybean root nodules. J Biol Chem. 270:1995;19823-19827.
    • (1995) J Biol Chem , vol.270 , pp. 19823-19827
    • Chauhan, S.1    O'Brian, M.R.2
  • 24
    • 0030758361 scopus 로고    scopus 로고
    • Heme biosynthesis by the malarial parasite. Import of delta-aminolevulinate dehydrase from the host cell
    • Bonday Z.Q., Taketani S., Gupta P.D., Padmanaban G. Heme biosynthesis by the malarial parasite. Import of delta-aminolevulinate dehydrase from the host cell. J Biol Chem. 272:1997;21839-21846.
    • (1997) J Biol Chem , vol.272 , pp. 21839-21846
    • Bonday, Z.Q.1    Taketani, S.2    Gupta, P.D.3    Padmanaban, G.4
  • 25
    • 0026785410 scopus 로고
    • De novo biosynthesis of heme offers a new chemotherapeutic target in the human malarial parasite
    • Surolia N., Padmanaban G. De novo biosynthesis of heme offers a new chemotherapeutic target in the human malarial parasite. Biochem Biophys Res Commun. 187:1992;744-750.
    • (1992) Biochem Biophys Res Commun , vol.187 , pp. 744-750
    • Surolia, N.1    Padmanaban, G.2
  • 26
    • 0029670146 scopus 로고    scopus 로고
    • Characterization of the d-aminolevulinate synthase gene homologue in P. falciparum
    • Wilson C.M., Smith A.B., Baylon R.V. Characterization of the d-aminolevulinate synthase gene homologue in P. falciparum. Mol Biochem Parasitol. 75:1996;271-276.
    • (1996) Mol Biochem Parasitol , vol.75 , pp. 271-276
    • Wilson, C.M.1    Smith, A.B.2    Baylon, R.V.3
  • 27
    • 0033590505 scopus 로고    scopus 로고
    • Shikimate pathway in apicomplexan parasites
    • Keeling P.J., Palmer J.D., Donald R.G.K.et al. Shikimate pathway in apicomplexan parasites. Nature. 397:1998;219-220.
    • (1998) Nature , vol.397 , pp. 219-220
    • Keeling, P.J.1    Palmer, J.D.2    Donald, R.G.K.3
  • 28
    • 84984768638 scopus 로고    scopus 로고
    • Shikimate pathway in apicomplexan parasites
    • Roberts C.W., Finnerty J., Johnson J.J.et al. Shikimate pathway in apicomplexan parasites. Nature. 397:1998;220.
    • (1998) Nature , vol.397 , pp. 220
    • Roberts, C.W.1    Finnerty, J.2    Johnson, J.J.3
  • 29
    • 0025743648 scopus 로고
    • Organisation and expression of small subunit ribosomal RNA genes encoded by a 35-kilobase circular DNA in Plasmodium falciparum
    • Gardner M.J., Feagin J.E., Moore D.J.et al. Organisation and expression of small subunit ribosomal RNA genes encoded by a 35-kilobase circular DNA in Plasmodium falciparum. Mol Biochem Parasitol. 48:1991;77-88.
    • (1991) Mol Biochem Parasitol , vol.48 , pp. 77-88
    • Gardner, M.J.1    Feagin, J.E.2    Moore, D.J.3
  • 30
    • 0033167106 scopus 로고    scopus 로고
    • The non-photosynthetic plastid in malarial parasites and other apicomplexans is derived outside the green plastid lineage
    • Blanchard J.L., Hicks J.S. The non-photosynthetic plastid in malarial parasites and other apicomplexans is derived outside the green plastid lineage. J Euk Microbiol. 46:1999;367-375.
    • (1999) J Euk Microbiol , vol.46 , pp. 367-375
    • Blanchard, J.L.1    Hicks, J.S.2
  • 31
    • 0031282142 scopus 로고    scopus 로고
    • Plastids in parasites of humans
    • McFadden G.I., Waller R.F. Plastids in parasites of humans. Bioessays. 19:1997;1033-1040.
    • (1997) Bioessays , vol.19 , pp. 1033-1040
    • McFadden, G.I.1    Waller, R.F.2
  • 32
    • 0026723118 scopus 로고
    • trp with CmCA anticodon
    • trp with CmCA anticodon. EMBO J. 11:1992;4167-4173.
    • (1992) EMBO J , vol.11 , pp. 4167-4173
    • Zerfass, K.1    Beier, H.2
  • 33
    • 0031007907 scopus 로고    scopus 로고
    • An ancestral mitochondrial DNA resembling a eubacterial genome in miniature
    • Lang B.F., Burger G., O'Kelly C.J.et al. An ancestral mitochondrial DNA resembling a eubacterial genome in miniature. Nature. 387:1997;493-497.
    • (1997) Nature , vol.387 , pp. 493-497
    • Lang, B.F.1    Burger, G.2    O'Kelly, C.J.3
  • 34
    • 0028064540 scopus 로고
    • Phylogenetic analysis of the rpoB gene from the plastid-like DNA of Plasmodium falciparum
    • Gardner M.J., Goldman N., Barnett P.et al. Phylogenetic analysis of the rpoB gene from the plastid-like DNA of Plasmodium falciparum. Mol Biochem Parasitol. 66:1994;221-231.
    • (1994) Mol Biochem Parasitol , vol.66 , pp. 221-231
    • Gardner, M.J.1    Goldman, N.2    Barnett, P.3
  • 35
    • 1842411934 scopus 로고    scopus 로고
    • Mitochondrial and chloroplast phage-type RNA polymerases in Arabidopsis
    • Hetke B., Borner T., Weihe A. Mitochondrial and chloroplast phage-type RNA polymerases in Arabidopsis. Science. 277:1997;809-811.
    • (1997) Science , vol.277 , pp. 809-811
    • Hetke, B.1    Borner, T.2    Weihe, A.3
  • 36
    • 0033536215 scopus 로고    scopus 로고
    • Single gene circles in dinoflagellate chloroplast genomes
    • Zhang Z., Green B.R., Cavalier-Smith T. Single gene circles in dinoflagellate chloroplast genomes. Nature. 400:1999;155-159.
    • (1999) Nature , vol.400 , pp. 155-159
    • Zhang, Z.1    Green, B.R.2    Cavalier-Smith, T.3
  • 37
    • 0033536113 scopus 로고    scopus 로고
    • Ever decreasing circles
    • McFadden G. Ever decreasing circles. Nature. 400:1999;119-120.
    • (1999) Nature , vol.400 , pp. 119-120
    • McFadden, G.1
  • 38
    • 0343360073 scopus 로고
    • Regulation of gene expression in non-photosynthetic plastids of higher plants
    • In: Boyer CD, Shannon JC, Hardison RC, editors. Physiology, biochemistry, and genetics of non-green plastids
    • Gruissem W. Regulation of gene expression in non-photosynthetic plastids of higher plants. In: Boyer CD, Shannon JC, Hardison RC, editors. Physiology, biochemistry, and genetics of non-green plastids. The American Society of Plant Physiologists, 1989;227-40.
    • (1989) The American Society of Plant Physiologists , pp. 227-240
    • Gruissem, W.1
  • 39
    • 0033178777 scopus 로고    scopus 로고
    • Origin, targeting, and function of the apicomplexan plastid
    • Roos DS, Crawford MJ, Donald RGK et al. Origin, targeting, and function of the apicomplexan plastid. Curr Opin, Microbiol 1999;2:426 - 32.
    • (1999) Curr Opin, Microbiol , vol.2 , pp. 426-432
    • Roos, D.S.1    Crawford, M.J.2    Donald, R.G.K.3
  • 40
    • 0032553297 scopus 로고    scopus 로고
    • Protein transport into "complex" diatom plastids utilizes two different targeting signals
    • Lang M., Apt K.E., Kroth P.G. Protein transport into "complex" diatom plastids utilizes two different targeting signals. J Mol Biol. 273:1998;30973-30978.
    • (1998) J Mol Biol , vol.273 , pp. 30973-30978
    • Lang, M.1    Apt, K.E.2    Kroth, P.G.3
  • 41
    • 0029030925 scopus 로고
    • The polyprotein precursor to the Euglena light-harvesting chlorophyll a/b-binding protein is transported to the Golgi apparatus prior to chloroplast import and polyprotein processing
    • Sulli C., Schwartzbach S.D. The polyprotein precursor to the Euglena light-harvesting chlorophyll a/b-binding protein is transported to the Golgi apparatus prior to chloroplast import and polyprotein processing. J Biol Chem. 270:1995;13084-13090.
    • (1995) J Biol Chem , vol.270 , pp. 13084-13090
    • Sulli, C.1    Schwartzbach, S.D.2
  • 42
    • 0033180525 scopus 로고    scopus 로고
    • Protein synthesis in the plastid of Plasmodium falciparum
    • Roy A., Cox R.A., Williamson D.H.et al. Protein synthesis in the plastid of Plasmodium falciparum. Protist. 150:1999;183-188.
    • (1999) Protist , vol.150 , pp. 183-188
    • Roy, A.1    Cox, R.A.2    Williamson, D.H.3
  • 43
    • 0028998727 scopus 로고
    • Evolutionary origin of Plasmodium and other Apicomplexa based on rRNA genes
    • Escalante A.A., Ayala F.J. Evolutionary origin of Plasmodium and other Apicomplexa based on rRNA genes. Proc Natl Acad Sci USA. 92:1995;5793-5797.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5793-5797
    • Escalante, A.A.1    Ayala, F.J.2
  • 44
    • 0026447426 scopus 로고
    • Function and evolution of a minimal plastid genome from a non-photosynthetic parasitic plant
    • Wolfe K.H., Morden C.W., Palmer J.D. Function and evolution of a minimal plastid genome from a non-photosynthetic parasitic plant. Proc Natl Acad Sci USA. 89:1992;10648-10652.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10648-10652
    • Wolfe, K.H.1    Morden, C.W.2    Palmer, J.D.3
  • 45
    • 0031016902 scopus 로고    scopus 로고
    • Organelle genomes: Going, going gone!
    • Palmer J.D. Organelle genomes: Going, going gone! Science. 275:1997;790-791.
    • (1997) Science , vol.275 , pp. 790-791
    • Palmer, J.D.1
  • 46
    • 0033580325 scopus 로고    scopus 로고
    • Photosynthetic control of chloroplast gene expression
    • Pfannschmidt T., Nilsson A., Allen J.F. Photosynthetic control of chloroplast gene expression. Nature. 397:1999;625-628.
    • (1999) Nature , vol.397 , pp. 625-628
    • Pfannschmidt, T.1    Nilsson, A.2    Allen, J.F.3
  • 47
    • 0028220332 scopus 로고
    • The evolutionary origin of the malaria parasite's 35 kb circular DNA; New evidence supports a possible rhodophyte ancestry
    • Williamson D.H., Gardner M.J., Preiser P.et al. The evolutionary origin of the malaria parasite's 35 kb circular DNA; new evidence supports a possible rhodophyte ancestry. Mol Gen Genet. 243:1994;249-252.
    • (1994) Mol Gen Genet , vol.243 , pp. 249-252
    • Williamson, D.H.1    Gardner, M.J.2    Preiser, P.3
  • 49
    • 0001343250 scopus 로고
    • A high resolution gene map of the chloroplast genome of the red alga Porphyra purpurea
    • Reith M., Munholland J. A high resolution gene map of the chloroplast genome of the red alga Porphyra purpurea. Plant Cell. 5:1993;465-475.
    • (1993) Plant Cell , vol.5 , pp. 465-475
    • Reith, M.1    Munholland, J.2
  • 50
    • 0032900424 scopus 로고    scopus 로고
    • The plastid genome of the cryptophyte alga Guillaria theta: Complete sequence and conserved synteny groups confirm its common ancestry with red algae
    • Douglas S.E., Penny S.L. The plastid genome of the cryptophyte alga Guillaria theta: complete sequence and conserved synteny groups confirm its common ancestry with red algae. J Mol Evol. 48:1999;236-244.
    • (1999) J Mol Evol , vol.48 , pp. 236-244
    • Douglas, S.E.1    Penny, S.L.2
  • 51
    • 12744257602 scopus 로고    scopus 로고
    • Chromosome 2 sequence of the human malaria parasite Plasmodium falciparum
    • Gardner M.J., Tettelin H., Carucci D.et al. Chromosome 2 sequence of the human malaria parasite Plasmodium falciparum. Science. 282:1998;1126-1132.
    • (1998) Science , vol.282 , pp. 1126-1132
    • Gardner, M.J.1    Tettelin, H.2    Carucci, D.3
  • 52
    • 0030024359 scopus 로고    scopus 로고
    • Recombination associated with replication of malarial mitochondrial DNA
    • Preiser P.R., Wilson R.J.M., Moore P.W.et al. Recombination associated with replication of malarial mitochondrial DNA. EMBO J. 15:1996;684-693.
    • (1996) EMBO J , vol.15 , pp. 684-693
    • Preiser, P.R.1    Wilson, R.J.M.2    Moore, P.W.3
  • 53
    • 0031918131 scopus 로고    scopus 로고
    • Eimeria tenella: Two species of extrachromosomal DNA revealed by pulsed-field gel electrophoresis
    • Dunn P.P.J., Stephens P.J., Shirley M.W. Eimeria tenella: two species of extrachromosomal DNA revealed by pulsed-field gel electrophoresis. Parasitol Res. 84:1998;272-275.
    • (1998) Parasitol Res , vol.84 , pp. 272-275
    • Dunn, P.P.J.1    Stephens, P.J.2    Shirley, M.W.3
  • 54
    • 0032702202 scopus 로고    scopus 로고
    • Physical characterisation of the Neospora caninum plastid
    • Gleeson M, Johnson AM. Physical characterisation of the Neospora caninum plastid. Int J Parasitol, 1999;29:1563 - 73.
    • (1999) Int J Parasitol , vol.29 , pp. 1563-1573
    • Gleeson, M.1    Johnson, A.M.2
  • 55
    • 0021331657 scopus 로고
    • DNA circles with cruciforms from Isospora (Toxoplasma) gondii
    • Borst P., Overdulve J.P., Weijers P.J.et al. DNA circles with cruciforms from Isospora (Toxoplasma) gondii. Biochim Biophys Acta. 781:1984;100-111.
    • (1984) Biochim Biophys Acta , vol.781 , pp. 100-111
    • Borst, P.1    Overdulve, J.P.2    Weijers, P.J.3
  • 56
    • 0030245576 scopus 로고    scopus 로고
    • Organelle DNAs: The bit players in malaria parasite DNA replication
    • Williamson D.H., Preiser P.R., Wilson R.J.M. Organelle DNAs: the bit players in malaria parasite DNA replication. Parasitol Today. 12:1996;357-362.
    • (1996) Parasitol Today , vol.12 , pp. 357-362
    • Williamson, D.H.1    Preiser, P.R.2    Wilson, R.J.M.3
  • 57
    • 0031431683 scopus 로고    scopus 로고
    • Topoisomerase II inhibitors induce cleavage of nuclear and 35-kb plastid DNAs in the malarial parasite Plasmodium falciparum
    • Weissig V., Vetro-Widenhouse T.S., Rowe T.C. Topoisomerase II inhibitors induce cleavage of nuclear and 35-kb plastid DNAs in the malarial parasite Plasmodium falciparum. DNA Cell Biol. 16:1997;1483-1492.
    • (1997) DNA Cell Biol , vol.16 , pp. 1483-1492
    • Weissig, V.1    Vetro-Widenhouse, T.S.2    Rowe, T.C.3
  • 58
    • 0031444101 scopus 로고    scopus 로고
    • A plastid organelle as a drug target in apicomplexan parasites
    • Fichera M.E., Roos D.S. A plastid organelle as a drug target in apicomplexan parasites. Nature. 390:1997;407-409.
    • (1997) Nature , vol.390 , pp. 407-409
    • Fichera, M.E.1    Roos, D.S.2
  • 59
    • 0029044369 scopus 로고
    • In vitro assays elucidate peculiar kinetics of clindamycin action against Toxoplasma gondii
    • Fichera M.E., Bhopale M.K., Roos D.S. In vitro assays elucidate peculiar kinetics of clindamycin action against Toxoplasma gondii. Antimicrob Agents Chemother. 39:1995;1530-1537.
    • (1995) Antimicrob Agents Chemother , vol.39 , pp. 1530-1537
    • Fichera, M.E.1    Bhopale, M.K.2    Roos, D.S.3
  • 60
    • 0021723252 scopus 로고
    • Clindamycin activity against chloroquine-resistant Plasmodium falciparum
    • Seaberg L.S., Parquette A.R., Gluzman I.Y.et al. Clindamycin activity against chloroquine-resistant Plasmodium falciparum. J Infect Dis. 150:1984;904-911.
    • (1984) J Infect Dis , vol.150 , pp. 904-911
    • Seaberg, L.S.1    Parquette, A.R.2    Gluzman, I.Y.3
  • 61
    • 0030662570 scopus 로고    scopus 로고
    • An alternative mechanism of ribosome-inactivating protein cytotoxocity; Degradation of extrachromosomal DNA
    • Nicolas E., Goodyer I.D., Taraschi T.F. An alternative mechanism of ribosome-inactivating protein cytotoxocity; degradation of extrachromosomal DNA. Biochem J. 327:1997;413-417.
    • (1997) Biochem J , vol.327 , pp. 413-417
    • Nicolas, E.1    Goodyer, I.D.2    Taraschi, T.F.3
  • 62
    • 0026603433 scopus 로고
    • Homologies between the contiguous and fragmented rRNAs of the two Plasmodium falciparum extrachromosomal DNAs are limited to core sequences
    • Feagin J.E., Werner E., Gardner M.J.et al. Homologies between the contiguous and fragmented rRNAs of the two Plasmodium falciparum extrachromosomal DNAs are limited to core sequences. Nucleic Acids Res. 20:1992;879-887.
    • (1992) Nucleic Acids Res , vol.20 , pp. 879-887
    • Feagin, J.E.1    Werner, E.2    Gardner, M.J.3
  • 63
    • 0031917769 scopus 로고    scopus 로고
    • The antibiotic micrococcin is a potent inhibitor of growth and protein synthesis in the malaria parasite
    • Rogers M.J., Cundliffe E., McCutchan T.F. The antibiotic micrococcin is a potent inhibitor of growth and protein synthesis in the malaria parasite. Antimicrob Agents Chemother. 42:1998;715-716.
    • (1998) Antimicrob Agents Chemother , vol.42 , pp. 715-716
    • Rogers, M.J.1    Cundliffe, E.2    McCutchan, T.F.3
  • 64
    • 0023857217 scopus 로고
    • Primary sequences of two small subunit ribosomal RNA genes from Plasmodium falciparum
    • McCutchen T.J., de la Cruz V.F., Lal A.A.et al. Primary sequences of two small subunit ribosomal RNA genes from Plasmodium falciparum. Mol Biochem Parasitol. 28:1988;63-68.
    • (1988) Mol Biochem Parasitol , vol.28 , pp. 63-68
    • McCutchen, T.J.1    De La Cruz, V.F.2    Lal, A.A.3
  • 65
    • 0030915683 scopus 로고    scopus 로고
    • Thiostrepton binds to malarial plastid rRNA
    • Clough B., Strath M., Preiser P.et al. Thiostrepton binds to malarial plastid rRNA. FEBS Lett. 406:1997;123-125.
    • (1997) FEBS Lett , vol.406 , pp. 123-125
    • Clough, B.1    Strath, M.2    Preiser, P.3
  • 66
    • 0030791711 scopus 로고    scopus 로고
    • Interaction of thiostrepton with an RNA fragment derived from the plastid-encoded ribosomal RNA of the malaria parasite
    • Rogers M.J., Bukhman Y.V., McCutchan T.F., Draper D.E. Interaction of thiostrepton with an RNA fragment derived from the plastid-encoded ribosomal RNA of the malaria parasite. RNA. 3:1997;815-820.
    • (1997) RNA , vol.3 , pp. 815-820
    • Rogers, M.J.1    Bukhman, Y.V.2    McCutchan, T.F.3    Draper, D.E.4
  • 67
    • 0028355760 scopus 로고
    • The antibiotics micrococcin and thiostrepton interact directly with 23S rRNA nucleotides 1067A and 1095A
    • Rosendahl G., Douthwaite S. The antibiotics micrococcin and thiostrepton interact directly with 23S rRNA nucleotides 1067A and 1095A. Nucleic Acids Res. 22:1994;357-363.
    • (1994) Nucleic Acids Res , vol.22 , pp. 357-363
    • Rosendahl, G.1    Douthwaite, S.2
  • 68
    • 0030788539 scopus 로고    scopus 로고
    • Identification of additional rRNA fragments encoded by the Plasmodium falciparum 6 kb element
    • Feagin J.E., Mericle B.L., Werner E., Morris M. Identification of additional rRNA fragments encoded by the Plasmodium falciparum 6 kb element. Nucleic Acids Res. 25:1997;438-446.
    • (1997) Nucleic Acids Res , vol.25 , pp. 438-446
    • Feagin, J.E.1    Mericle, B.L.2    Werner, E.3    Morris, M.4
  • 70
    • 0033180232 scopus 로고    scopus 로고
    • Antibiotic inhibitors of organellar protein synthesis in Plasmodium falciparum
    • Clough B., Rangachari K., Strath M.et al. Antibiotic inhibitors of organellar protein synthesis in Plasmodium falciparum. Protist. 150:1999;189-195.
    • (1999) Protist , vol.150 , pp. 189-195
    • Clough, B.1    Rangachari, K.2    Strath, M.3
  • 71
    • 0030587857 scopus 로고    scopus 로고
    • Helix unwinding in the effector region of elongation factor EF-Tu-GDP
    • Polekhina G., Thirup S., Kjeldgaard M.et al. Helix unwinding in the effector region of elongation factor EF-Tu-GDP. Structure. 4:1996;1141-1151.
    • (1996) Structure , vol.4 , pp. 1141-1151
    • Polekhina, G.1    Thirup, S.2    Kjeldgaard, M.3
  • 72
    • 0027917990 scopus 로고
    • The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation
    • Kjeldgaard M., Nissen P., Thirup S.et al. The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation. Structure. 1:1993;35-50.
    • (1993) Structure , vol.1 , pp. 35-50
    • Kjeldgaard, M.1    Nissen, P.2    Thirup, S.3
  • 73
    • 0033081413 scopus 로고    scopus 로고
    • cys-EF-Tu-GDPNP reveals general and specific features in the ternary complex and in tRNA
    • cys-EF-Tu-GDPNP reveals general and specific features in the ternary complex and in tRNA. Structure. 7:1999;143-156.
    • (1999) Structure , vol.7 , pp. 143-156
    • Nissen, P.1    Thirup, S.2    Kjeldgaard, M.3    Nyborg, J.4
  • 74
    • 0027179878 scopus 로고
    • Crystal structure of active elongation factor Tu reveals major domain rearrangements
    • Berchtold H., Reshetnikova L., Reiser C.O.A.et al. Crystal structure of active elongation factor Tu reveals major domain rearrangements. Nature. 365:1993;126-132.
    • (1993) Nature , vol.365 , pp. 126-132
    • Berchtold, H.1    Reshetnikova, L.2    Reiser, C.O.A.3
  • 75
    • 0033593370 scopus 로고    scopus 로고
    • Crystal structure of intact elongation factor EF-Tu from Escherichia coli in GDP conformation at 2.05 A resolution
    • Song H., Parsons M.R., Rowsell S.et al. Crystal structure of intact elongation factor EF-Tu from Escherichia coli in GDP conformation at 2.05 A resolution. J Mol Biol. 285:1999;1245-1256.
    • (1999) J Mol Biol , vol.285 , pp. 1245-1256
    • Song, H.1    Parsons, M.R.2    Rowsell, S.3
  • 77
    • 0028000039 scopus 로고
    • The structural and functional basis for the kirromycin resistance of mutant EF-Tu species in Escherichia coli
    • Mesters J.R., Zeef L.A.H., Hilgenfeld R.et al. The structural and functional basis for the kirromycin resistance of mutant EF-Tu species in Escherichia coli. EMBO J. 13:1994;4877-4885.
    • (1994) EMBO J , vol.13 , pp. 4877-4885
    • Mesters, J.R.1    Zeef, L.A.H.2    Hilgenfeld, R.3
  • 78
    • 0028913213 scopus 로고
    • Novel antibiotics, amythiamicins IV. A mutation in the elongation factor Tu gene in a resistant mutant of B. subtilis
    • Shimanaka K., Iinuma H., Hamada M.et al. Novel antibiotics, amythiamicins IV. A mutation in the elongation factor Tu gene in a resistant mutant of B. subtilis. J Antibiot. 48:1995;182-184.
    • (1995) J Antibiot , vol.48 , pp. 182-184
    • Shimanaka, K.1    Iinuma, H.2    Hamada, M.3
  • 79
    • 0028018013 scopus 로고
    • Mutations to kirromycin resistance occur in the interface of domains I and III of EF-Tu.GTP
    • Abdulkarim F., Liljas L., Hughes D. Mutations to kirromycin resistance occur in the interface of domains I and III of EF-Tu.GTP. FEBS Lett. 352:1994;118-122.
    • (1994) FEBS Lett , vol.352 , pp. 118-122
    • Abdulkarim, F.1    Liljas, L.2    Hughes, D.3
  • 80
    • 0029835797 scopus 로고    scopus 로고
    • An elongation factor Tu (EF-Tu) resistant to the EF-Tu inhibitor GE2270 in the producing organism Planobispora rosea
    • Sosio M., Amati G., Cappellano C.et al. An elongation factor Tu (EF-Tu) resistant to the EF-Tu inhibitor GE2270 in the producing organism Planobispora rosea. Mol Microbiol. 22:1999;43-51.
    • (1999) Mol Microbiol , vol.22 , pp. 43-51
    • Sosio, M.1    Amati, G.2    Cappellano, C.3
  • 81
    • 0030025671 scopus 로고    scopus 로고
    • The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution
    • Kawashima T., Berthet-Colomina C., Wulff M.et al. The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution. Nature. 379:1996;511-518.
    • (1996) Nature , vol.379 , pp. 511-518
    • Kawashima, T.1    Berthet-Colomina, C.2    Wulff, M.3
  • 82
    • 0030764672 scopus 로고    scopus 로고
    • Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus
    • Wang Y., Jiang Y., Mayering-Voss M.et al. Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus. Nat Struct Biol. 4:1997;650-656.
    • (1997) Nat Struct Biol , vol.4 , pp. 650-656
    • Wang, Y.1    Jiang, Y.2    Mayering-Voss, M.3
  • 83
    • 0027968068 scopus 로고
    • CLUSTALW: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTALW: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 84
    • 0025398721 scopus 로고
    • WHAT-IF: A molecular modelling and drug design program
    • Vriend G. WHAT-IF: A molecular modelling and drug design program. J Mol Graph. 8:1990;52-56.
    • (1990) J Mol Graph , vol.8 , pp. 52-56
    • Vriend, G.1
  • 85
    • 0029940470 scopus 로고    scopus 로고
    • Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease
    • Tews I., Perrakis A., Oppenheim A.et al. Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease. Nat Struct Biol. 3:1996;638-648.
    • (1996) Nat Struct Biol , vol.3 , pp. 638-648
    • Tews, I.1    Perrakis, A.2    Oppenheim, A.3
  • 86
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:1983;2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 87
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton G.J. ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6:1993;37-40.
    • (1993) Protein Eng , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 88
    • 0000732609 scopus 로고
    • GRASP: Graphical representation and analysis of surface properties
    • Nicholls A., Bharadwaj R., Honig B. GRASP: graphical representation and analysis of surface properties. Biophys J. 64:1993;166-170.
    • (1993) Biophys J , vol.64 , pp. 166-170
    • Nicholls, A.1    Bharadwaj, R.2    Honig, B.3
  • 89
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr. 24:1991;946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 90
    • 0033520336 scopus 로고    scopus 로고
    • Inhibitors of the nonmevalonate pathway of isoprenoid biosynthesis as antimalarial drugs
    • Jomaa H, Wiesner J, Sanderbrand S. et al. Inhibitors of the nonmevalonate pathway of isoprenoid biosynthesis as antimalarial drugs, Science 1999;285:1573 - 76.
    • (1999) Science , vol.285 , pp. 1573-1576
    • Jomaa, H.1    Wiesner, J.2    Sanderbrand, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.