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Volumn 82, Issue 5, 2011, Pages 1204-1216

A Toxoplasma gondii mutant highlights the importance of translational regulation in the apicoplast during animal infection

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Indexed keywords

ELONGATION FACTOR G;

EID: 82155166250     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2011.07879.x     Document Type: Article
Times cited : (7)

References (56)
  • 2
    • 4644250428 scopus 로고    scopus 로고
    • Effect of oxidative stress on in vivo ADP-ribosylation of eukaryotic elongation factor 2
    • Bektas, M., Akcakaya, H., Aroymak, A., Nurten, R., and Bermek, E. (2005) Effect of oxidative stress on in vivo ADP-ribosylation of eukaryotic elongation factor 2. Int J Biochem Cell Biol 37: 91-99.
    • (2005) Int J Biochem Cell Biol , vol.37 , pp. 91-99
    • Bektas, M.1    Akcakaya, H.2    Aroymak, A.3    Nurten, R.4    Bermek, E.5
  • 3
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • Bendtsen, J.D., Nielsen, H., von Heijne, G., and Brunak, S. (2004) Improved prediction of signal peptides: SignalP 3.0. J Mol Biol 340: 783-795.
    • (2004) J Mol Biol , vol.340 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    von Heijne, G.3    Brunak, S.4
  • 4
    • 0001563411 scopus 로고
    • mRNAs encoding ribulose-1,5-bisphosphate carboxylase remain bound to polysomes but are not translated in amaranth seedlings transferred to darkness
    • Berry, J.O., Carr, J.P., and Klessig, D.F. (1988) mRNAs encoding ribulose-1, 5-bisphosphate carboxylase remain bound to polysomes but are not translated in amaranth seedlings transferred to darkness. Proc Natl Acad Sci USA 85: 4190-4194.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 4190-4194
    • Berry, J.O.1    Carr, J.P.2    Klessig, D.F.3
  • 5
    • 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
  • 6
    • 59749092212 scopus 로고    scopus 로고
    • Translational responses to growth factors and stress
    • Cully, M., and Downward, J. (2009) Translational responses to growth factors and stress. Biochem Soc Trans 37: 284-288.
    • (2009) Biochem Soc Trans , vol.37 , pp. 284-288
    • Cully, M.1    Downward, J.2
  • 7
    • 34249912631 scopus 로고    scopus 로고
    • Fatty acids isolated from Toxoplasma gondii reduce glycosylphosphatidylinositol-induced tumor necrosis factor alpha production through inhibition of the NF-kappaB signaling pathway
    • Debierre-Grockiego, F., Rabi, K., Schmidt, J., Geyer, H., Geyer, R., and Schwarz, R.T. (2007) Fatty acids isolated from Toxoplasma gondii reduce glycosylphosphatidylinositol-induced tumor necrosis factor alpha production through inhibition of the NF-kappaB signaling pathway. Infect Immun 75: 2886-2893.
    • (2007) Infect Immun , vol.75 , pp. 2886-2893
    • Debierre-Grockiego, F.1    Rabi, K.2    Schmidt, J.3    Geyer, H.4    Geyer, R.5    Schwarz, R.T.6
  • 8
    • 0034474466 scopus 로고    scopus 로고
    • Analysis of targeting sequences demonstrates that trafficking to the Toxoplasma gondii plastid branches off the secretory system
    • DeRocher, A., Hagen, C.B., Froehlich, J.E., Feagin, J.E., and Parsons, M. (2000) Analysis of targeting sequences demonstrates that trafficking to the Toxoplasma gondii plastid branches off the secretory system. J Cell Sci 113: 3969-3977.
    • (2000) J Cell Sci , vol.113 , pp. 3969-3977
    • DeRocher, A.1    Hagen, C.B.2    Froehlich, J.E.3    Feagin, J.E.4    Parsons, M.5
  • 9
    • 14644415904 scopus 로고    scopus 로고
    • Dissection of brefeldin A-sensitive and -insensitive steps in apicoplast protein targeting
    • DeRocher, A., Gilbert, B., Feagin, J.E., and Parsons, M. (2005) Dissection of brefeldin A-sensitive and -insensitive steps in apicoplast protein targeting. J Cell Sci 118: 565-574.
    • (2005) J Cell Sci , vol.118 , pp. 565-574
    • DeRocher, A.1    Gilbert, B.2    Feagin, J.E.3    Parsons, M.4
  • 10
    • 51649116051 scopus 로고    scopus 로고
    • A thioredoxin family protein of the apicoplast periphery identifies abundant candidate transport vesicles in Toxoplasma gondii
    • DeRocher, A.E., Coppens, I., Karnataki, A., Gilbert, L.A., Rome, M.E., Feagin, J.E., etal. (2008) A thioredoxin family protein of the apicoplast periphery identifies abundant candidate transport vesicles in Toxoplasma gondii. Eukaryot Cell 7: 1518-1529.
    • (2008) Eukaryot Cell , vol.7 , pp. 1518-1529
    • DeRocher, A.E.1    Coppens, I.2    Karnataki, A.3    Gilbert, L.A.4    Rome, M.E.5    Feagin, J.E.6
  • 11
    • 0027136119 scopus 로고
    • Stable molecular transformation of Toxoplasma gondii: a selectable dihydrofolate reductase-thymidylate synthase marker based on drug-resistance mutations in malaria
    • Donald, R.G., and Roos, D.S. (1993) Stable molecular transformation of Toxoplasma gondii: a selectable dihydrofolate reductase-thymidylate synthase marker based on drug-resistance mutations in malaria. Proc Natl Acad Sci USA 90: 11703-11707.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11703-11707
    • Donald, R.G.1    Roos, D.S.2
  • 12
    • 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
  • 13
    • 0028113659 scopus 로고
    • Toxoplasmosis
    • Dubey, J.P. (1994) Toxoplasmosis. J Am Vet Med Assoc 205: 1593-1598.
    • (1994) J Am Vet Med Assoc , vol.205 , pp. 1593-1598
    • Dubey, J.P.1
  • 14
    • 0032128434 scopus 로고    scopus 로고
    • Advances in the life cycle of Toxoplasma gondii
    • Dubey, J.P. (1998) Advances in the life cycle of Toxoplasma gondii. Int J Parasitol 28: 1019-1024.
    • (1998) Int J Parasitol , vol.28 , pp. 1019-1024
    • Dubey, J.P.1
  • 17
    • 0029044369 scopus 로고
    • In vitro assays elucidate peculiar kinetics of clindamycin action against Toxoplasma gondii
    • Fichera, M.E., Bhopale, M.K., and Roos, D.S. (1995) In vitro assays elucidate peculiar kinetics of clindamycin action against Toxoplasma gondii. Antimicrob Agents Chemother 39: 1530-1537.
    • (1995) Antimicrob Agents Chemother , vol.39 , pp. 1530-1537
    • Fichera, M.E.1    Bhopale, M.K.2    Roos, D.S.3
  • 18
    • 0344826569 scopus 로고    scopus 로고
    • Fitness effects of DHFR-TS mutations associated with pyrimethamine resistance in apicomplexan parasites
    • Fohl, L.M., and Roos, D.S. (2003) Fitness effects of DHFR-TS mutations associated with pyrimethamine resistance in apicomplexan parasites. Mol Microbiol 50: 1319-1327.
    • (2003) Mol Microbiol , vol.50 , pp. 1319-1327
    • Fohl, L.M.1    Roos, D.S.2
  • 19
    • 34547200189 scopus 로고    scopus 로고
    • Discovery of parasite virulence genes reveals a unique regulator of chromosome condensation 1 ortholog critical for efficient nuclear trafficking
    • Frankel, M.B., Mordue, D.G., and Knoll, L.J. (2007) Discovery of parasite virulence genes reveals a unique regulator of chromosome condensation 1 ortholog critical for efficient nuclear trafficking. Proc Natl Acad Sci USA 104: 10181-10186.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 10181-10186
    • Frankel, M.B.1    Mordue, D.G.2    Knoll, L.J.3
  • 20
    • 33845987535 scopus 로고    scopus 로고
    • Fatty acid biosynthesis as a drug target in apicomplexan parasites
    • Goodman, C.D., and McFadden, G.I. (2007) Fatty acid biosynthesis as a drug target in apicomplexan parasites. Curr Drug Targets 8: 15-30.
    • (2007) Curr Drug Targets , vol.8 , pp. 15-30
    • Goodman, C.D.1    McFadden, G.I.2
  • 21
    • 2942631511 scopus 로고    scopus 로고
    • Multiple functionally redundant signals mediate targeting to the apicoplast in the apicomplexan parasite Toxoplasma gondii
    • Harb, O.S., Chatterjee, B., Fraunholz, M.J., Crawford, M.J., Nishi, M., and Roos, D.S. (2004) Multiple functionally redundant signals mediate targeting to the apicoplast in the apicomplexan parasite Toxoplasma gondii. Eukaryot Cell 3: 663-674.
    • (2004) Eukaryot Cell , vol.3 , pp. 663-674
    • Harb, O.S.1    Chatterjee, B.2    Fraunholz, M.J.3    Crawford, M.J.4    Nishi, M.5    Roos, D.S.6
  • 22
    • 0028040002 scopus 로고
    • In vivo selection of conditional-lethal mutations in the gene encoding elongation factor G of Escherichia coli
    • Hou, Y., Lin, Y.P., Sharer, J.D., and March, P.E. (1994a) In vivo selection of conditional-lethal mutations in the gene encoding elongation factor G of Escherichia coli. J Bacteriol 176: 123-129.
    • (1994) J Bacteriol , vol.176 , pp. 123-129
    • Hou, Y.1    Lin, Y.P.2    Sharer, J.D.3    March, P.E.4
  • 23
    • 0028037409 scopus 로고
    • Carboxyl-terminal amino acid residues in elongation factor G essential for ribosome association and translocation
    • Hou, Y., Yaskowiak, E.S., and March, P.E. (1994b) Carboxyl-terminal amino acid residues in elongation factor G essential for ribosome association and translocation. J Bacteriol 176: 7038-7044.
    • (1994) J Bacteriol , vol.176 , pp. 7038-7044
    • Hou, Y.1    Yaskowiak, E.S.2    March, P.E.3
  • 24
    • 0035852296 scopus 로고    scopus 로고
    • Molecular chaperones involved in chloroplast protein import
    • Jackson-Constan, D., Akita, M., and Keegstra, K. (2001) Molecular chaperones involved in chloroplast protein import. Biochim Biophys Acta 1541: 102-113.
    • (2001) Biochim Biophys Acta , vol.1541 , pp. 102-113
    • Jackson-Constan, D.1    Akita, M.2    Keegstra, K.3
  • 25
    • 0033520336 scopus 로고    scopus 로고
    • Inhibitors of the nonmevalonate pathway of isoprenoid biosynthesis as antimalarial drugs
    • Jomaa, H., Wiesner, J., Sanderbrand, S., Altincicek, B., Weidemeyer, C., Hintz, M., etal. (1999) Inhibitors of the nonmevalonate pathway of isoprenoid biosynthesis as antimalarial drugs. Science 285: 1573-1576.
    • (1999) Science , vol.285 , pp. 1573-1576
    • Jomaa, H.1    Wiesner, J.2    Sanderbrand, S.3    Altincicek, B.4    Weidemeyer, C.5    Hintz, M.6
  • 26
    • 0038009150 scopus 로고    scopus 로고
    • A mechanism for light-induced translation of the rbcL mRNA encoding the large subunit of ribulose-1,5-bisphosphate carboxylase in barley chloroplasts
    • Kim, J., and Mullet, J.E. (2003) A mechanism for light-induced translation of the rbcL mRNA encoding the large subunit of ribulose-1, 5-bisphosphate carboxylase in barley chloroplasts. Plant Cell Physiol 44: 491-499.
    • (2003) Plant Cell Physiol , vol.44 , pp. 491-499
    • Kim, J.1    Mullet, J.E.2
  • 27
    • 0035815314 scopus 로고    scopus 로고
    • Optimized expression of green fluorescent protein in Toxoplasma gondii using thermostable green fluorescent protein mutants
    • Kim, K., Eaton, M.S., Schubert, W., Wu, S., and Tang, J. (2001) Optimized expression of green fluorescent protein in Toxoplasma gondii using thermostable green fluorescent protein mutants. Mol Biochem Parasitol 113: 309-313.
    • (2001) Mol Biochem Parasitol , vol.113 , pp. 309-313
    • Kim, K.1    Eaton, M.S.2    Schubert, W.3    Wu, S.4    Tang, J.5
  • 29
    • 84944366930 scopus 로고
    • Toxoplasmic encephalitis in patients with acquired immune deficiency syndrome
    • Luft, B.J., Brooks, R.G., Conley, F.K., McCabe, R.E., and Remington, J.S. (1984) Toxoplasmic encephalitis in patients with acquired immune deficiency syndrome. JAMA 252: 913-917.
    • (1984) JAMA , vol.252 , pp. 913-917
    • Luft, B.J.1    Brooks, R.G.2    Conley, F.K.3    McCabe, R.E.4    Remington, J.S.5
  • 30
    • 0035194239 scopus 로고    scopus 로고
    • Large amounts of apicoplast nucleoid DNA and its segregation in Toxoplasma gondii
    • Matsuzaki, M., Kikuchi, T., Kita, K., Kojima, S., and Kuroiwa, T. (2001) Large amounts of apicoplast nucleoid DNA and its segregation in Toxoplasma gondii. Protoplasma 218: 180-191.
    • (2001) Protoplasma , vol.218 , pp. 180-191
    • Matsuzaki, M.1    Kikuchi, T.2    Kita, K.3    Kojima, S.4    Kuroiwa, T.5
  • 31
    • 33748353213 scopus 로고    scopus 로고
    • Apicoplast fatty acid synthesis is essential for organelle biogenesis and parasite survival in Toxoplasma gondii
    • Mazumdar, J., Wilson, E.H., Masek, K., Hunter, C.A, and Striepen, B. (2006) Apicoplast fatty acid synthesis is essential for organelle biogenesis and parasite survival in Toxoplasma gondii. Proc Natl Acad Sci USA 103: 13192-13197.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 13192-13197
    • Mazumdar, J.1    Wilson, E.H.2    Masek, K.3    Hunter, C.A.4    Striepen, B.5
  • 32
    • 0037308625 scopus 로고    scopus 로고
    • Translational control by the 3'-UTR: the ends specify the means
    • Mazumder, B., Seshadri, V., and Fox, P.L. (2003) Translational control by the 3'-UTR: the ends specify the means. Trends Biochem Sci 28: 91-98.
    • (2003) Trends Biochem Sci , vol.28 , pp. 91-98
    • Mazumder, B.1    Seshadri, V.2    Fox, P.L.3
  • 33
    • 33846043591 scopus 로고    scopus 로고
    • A patatin-like protein protects Toxoplasma gondii from degradation in activated macrophages
    • Mordue, D.G., Scott-Weathers, C.F., Tobin, C.M., and Knoll, L.J. (2007) A patatin-like protein protects Toxoplasma gondii from degradation in activated macrophages. Mol Microbiol 63: 482-496.
    • (2007) Mol Microbiol , vol.63 , pp. 482-496
    • Mordue, D.G.1    Scott-Weathers, C.F.2    Tobin, C.M.3    Knoll, L.J.4
  • 34
    • 41049091036 scopus 로고    scopus 로고
    • Anti-infectives targeting the isoprenoid pathway of Toxoplasma gondii
    • Moreno, S.N., and Li, Z.H. (2008) Anti-infectives targeting the isoprenoid pathway of Toxoplasma gondii. Expert Opin Ther Targets 12: 253-263.
    • (2008) Expert Opin Ther Targets , vol.12 , pp. 253-263
    • Moreno, S.N.1    Li, Z.H.2
  • 35
    • 0032516884 scopus 로고    scopus 로고
    • Light-dependent formation of the photosynthetic proton gradient regulates translation elongation in chloroplasts
    • Muhlbauer, S.K., and Eichacker, L.A. (1998) Light-dependent formation of the photosynthetic proton gradient regulates translation elongation in chloroplasts. J Biol Chem 273: 20935-20940.
    • (1998) J Biol Chem , vol.273 , pp. 20935-20940
    • Muhlbauer, S.K.1    Eichacker, L.A.2
  • 36
    • 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
  • 37
    • 26944457020 scopus 로고    scopus 로고
    • Dominant-negative mutant phenotypes and the regulation of translation elongation factor 2 levels in yeast
    • Ortiz, P.A., and Kinzy, T.G. (2005) Dominant-negative mutant phenotypes and the regulation of translation elongation factor 2 levels in yeast. Nucleic Acids Res 33: 5740-5748.
    • (2005) Nucleic Acids Res , vol.33 , pp. 5740-5748
    • Ortiz, P.A.1    Kinzy, T.G.2
  • 38
    • 0036314780 scopus 로고    scopus 로고
    • Cellular stresses profoundly inhibit protein synthesis and modulate the states of phosphorylation of multiple translation factors
    • Patel, J., McLeod, L.E., Vries, R.G., Flynn, A., Wang, X., and Proud, C.G. (2002) Cellular stresses profoundly inhibit protein synthesis and modulate the states of phosphorylation of multiple translation factors. Eur J Biochem 269: 3076-3085.
    • (2002) Eur J Biochem , vol.269 , pp. 3076-3085
    • Patel, J.1    McLeod, L.E.2    Vries, R.G.3    Flynn, A.4    Wang, X.5    Proud, C.G.6
  • 39
    • 0026777173 scopus 로고
    • Parasiticidal effect of clindamycin on Toxoplasma gondii grown in cultured cells and selection of a drug-resistant mutant
    • Pfefferkorn, E.R., Nothnagel, R.F., and Borotz, S.E. (1992) Parasiticidal effect of clindamycin on Toxoplasma gondii grown in cultured cells and selection of a drug-resistant mutant. Antimicrob Agents Chemother 36: 1091-1096.
    • (1992) Antimicrob Agents Chemother , vol.36 , pp. 1091-1096
    • Pfefferkorn, E.R.1    Nothnagel, R.F.2    Borotz, S.E.3
  • 41
  • 42
    • 1942444611 scopus 로고    scopus 로고
    • Enzymes for heme biosynthesis are found in both the mitochondrion and plastid of the malaria parasite Plasmodium falciparum
    • Sato, S., Clough, B., Coates, L., and Wilson, R.J. (2004) Enzymes for heme biosynthesis are found in both the mitochondrion and plastid of the malaria parasite Plasmodium falciparum. Protist 155: 117-125.
    • (2004) Protist , vol.155 , pp. 117-125
    • Sato, S.1    Clough, B.2    Coates, L.3    Wilson, R.J.4
  • 43
    • 0037844597 scopus 로고    scopus 로고
    • Biosynthetic pathways of plastid-derived organelles as potential drug targets against parasitic apicomplexa
    • Seeber, F. (2003) Biosynthetic pathways of plastid-derived organelles as potential drug targets against parasitic apicomplexa. Curr Drug Targets Immune Endocr Metabol Disord 3: 99-109.
    • (2003) Curr Drug Targets Immune Endocr Metabol Disord , vol.3 , pp. 99-109
    • Seeber, F.1
  • 44
    • 23844532238 scopus 로고    scopus 로고
    • The plant-type ferredoxin-NADP+ reductase/ferredoxin redox system as a possible drug target against apicomplexan human parasites
    • Seeber, F., Aliverti, A., and Zanetti, G. (2005) The plant-type ferredoxin-NADP+ reductase/ferredoxin redox system as a possible drug target against apicomplexan human parasites. Curr Pharm Des 11: 3159-3172.
    • (2005) Curr Pharm Des , vol.11 , pp. 3159-3172
    • Seeber, F.1    Aliverti, A.2    Zanetti, G.3
  • 45
    • 0032987667 scopus 로고    scopus 로고
    • The apicoplast as a potential therapeutic target in and other apicomplexan parasites
    • Soldati, D. (1999) The apicoplast as a potential therapeutic target in and other apicomplexan parasites. Parasitol Today 15: 5-7.
    • (1999) Parasitol Today , vol.15 , pp. 5-7
    • Soldati, D.1
  • 46
    • 0028936153 scopus 로고
    • A selector of transcription initiation in the protozoan parasite Toxoplasma gondii
    • Soldati, D., and Boothroyd, J.C. (1995) A selector of transcription initiation in the protozoan parasite Toxoplasma gondii. Mol Cell Biol 15: 87-93.
    • (1995) Mol Cell Biol , vol.15 , pp. 87-93
    • Soldati, D.1    Boothroyd, J.C.2
  • 47
    • 2942714921 scopus 로고    scopus 로고
    • Parasite-specific eIF2 (eukaryotic initiation factor-2) kinase required for stress-induced translation control
    • Sullivan, W.J., Jr, Narasimhan, J., Bhatti, M.M., and Wek, R.C. (2004) Parasite-specific eIF2 (eukaryotic initiation factor-2) kinase required for stress-induced translation control. Biochem J 380: 523-531.
    • (2004) Biochem J , vol.380 , pp. 523-531
    • Sullivan Jr, W.J.1    Narasimhan, J.2    Bhatti, M.M.3    Wek, R.C.4
  • 48
    • 0026785410 scopus 로고
    • de novo biosynthesis of heme offers a new chemotherapeutic target in the human malarial parasite
    • Surolia, N., and Padmanaban, G. (1992) de novo biosynthesis of heme offers a new chemotherapeutic target in the human malarial parasite. Biochem Biophys Res Commun 187: 744-750.
    • (1992) Biochem Biophys Res Commun , vol.187 , pp. 744-750
    • Surolia, N.1    Padmanaban, G.2
  • 49
    • 33746284200 scopus 로고    scopus 로고
    • Protein targeting to destinations of the secretory pathway in the malaria parasite Plasmodium falciparum
    • Tonkin, C.J., Pearce, J.A., McFadden, G.I., and Cowman, A.F. (2006) Protein targeting to destinations of the secretory pathway in the malaria parasite Plasmodium falciparum. Curr Opin Microbiol 9: 381-387.
    • (2006) Curr Opin Microbiol , vol.9 , pp. 381-387
    • Tonkin, C.J.1    Pearce, J.A.2    McFadden, G.I.3    Cowman, A.F.4
  • 50
    • 0033959891 scopus 로고    scopus 로고
    • Translation of chloroplast psbA mRNA is modulated in the light by counteracting oxidizing and reducing activities
    • Trebitsh, T., Levitan, A., Sofer, A., and Danon, A. (2000) Translation of chloroplast psbA mRNA is modulated in the light by counteracting oxidizing and reducing activities. Mol Cell Biol 20: 1116-1123.
    • (2000) Mol Cell Biol , vol.20 , pp. 1116-1123
    • Trebitsh, T.1    Levitan, A.2    Sofer, A.3    Danon, A.4
  • 51
    • 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
  • 52
    • 33846020045 scopus 로고    scopus 로고
    • Isoprenoid biosynthesis of the apicoplast as drug target
    • Wiesner, J., and Jomaa, H. (2007) Isoprenoid biosynthesis of the apicoplast as drug target. Curr Drug Targets 8: 3-13.
    • (2007) Curr Drug Targets , vol.8 , pp. 3-13
    • Wiesner, J.1    Jomaa, H.2
  • 54
    • 0242669945 scopus 로고    scopus 로고
    • Regulation of mRNA translation by 5'- and 3'-UTR-binding factors
    • Wilkie, G.S., Dickson, K.S., and Gray, N.K. (2003) Regulation of mRNA translation by 5'- and 3'-UTR-binding factors. Trends Biochem Sci 28: 182-188.
    • (2003) Trends Biochem Sci , vol.28 , pp. 182-188
    • Wilkie, G.S.1    Dickson, K.S.2    Gray, N.K.3
  • 55
    • 0035895424 scopus 로고    scopus 로고
    • The in vivo conformation of the plastid DNA of Toxoplasma gondii: implications for replication
    • Williamson, D.H., Denny, P.W., Moore, P.W., Sato, S., McCready, S., and Wilson, R.J. (2001) The in vivo conformation of the plastid DNA of Toxoplasma gondii: implications for replication. J Mol Biol 306: 159-168.
    • (2001) J Mol Biol , vol.306 , pp. 159-168
    • Williamson, D.H.1    Denny, P.W.2    Moore, P.W.3    Sato, S.4    McCready, S.5    Wilson, R.J.6
  • 56
    • 0033791940 scopus 로고    scopus 로고
    • Biogenesis of the chloroplast-encoded D1 protein: regulation of translation elongation, insertion, and assembly into photosystem II
    • Zhang, L., Paakkarinen, V., van Wijk, K.J., and Aro, E.M. (2000) Biogenesis of the chloroplast-encoded D1 protein: regulation of translation elongation, insertion, and assembly into photosystem II. Plant Cell 12: 1769-1782.
    • (2000) Plant Cell , vol.12 , pp. 1769-1782
    • Zhang, L.1    Paakkarinen, V.2    van Wijk, K.J.3    Aro, E.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.