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Volumn 16, Issue 10, 2000, Pages 421-427

Traffic jams: Protein transport in Plasmodium falciparum

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; CELL PROTEIN; GREEN FLUORESCENT PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; SIGNAL PEPTIDE;

EID: 0034307491     PISSN: 01694758     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0169-4758(00)01792-0     Document Type: Review
Times cited : (57)

References (65)
  • 1
    • 0344624851 scopus 로고    scopus 로고
    • Apical organelles and host-cell invasion by Apicomplexa
    • Dubremetz J.F.et al. Apical organelles and host-cell invasion by Apicomplexa. Int. J. Parasitol. 28:1998;1007-1013.
    • (1998) Int. J. Parasitol. , vol.28 , pp. 1007-1013
    • Dubremetz, J.F.1
  • 2
    • 0031808982 scopus 로고    scopus 로고
    • The parasitophorous vacuole membrane surrounding Plasmodium and Toxoplasma- an unusual compartment in infected cells
    • Lingelbach K., Joiner K.A. The parasitophorous vacuole membrane surrounding Plasmodium and Toxoplasma- an unusual compartment in infected cells. J. Cell Sci. 111:1998;1467-1475.
    • (1998) J. Cell Sci. , vol.111 , pp. 1467-1475
    • Lingelbach, K.1    Joiner, K.A.2
  • 3
    • 0032213357 scopus 로고    scopus 로고
    • Protein trafficking in malaria-infected erythrocytes
    • Foley M., Tilley L. Protein trafficking in malaria-infected erythrocytes. Int. J. Parasitol. 28:1998;1671-1680.
    • (1998) Int. J. Parasitol. , vol.28 , pp. 1671-1680
    • Foley, M.1    Tilley, L.2
  • 4
    • 0030904788 scopus 로고    scopus 로고
    • Targeted gene disruption shows that knobs enable malaria-infected red cells to cytoadhere under physiological shear stress
    • Crabb B.S.et al. Targeted gene disruption shows that knobs enable malaria-infected red cells to cytoadhere under physiological shear stress. Cell. 89:1997;287-296.
    • (1997) Cell , vol.89 , pp. 287-296
    • Crabb, B.S.1
  • 5
    • 0025971118 scopus 로고
    • The ring-infected erythrocyte surface antigen of Plasmodium falciparum associates with spectrin in the erythrocytic membrane
    • Foley M.et al. The ring-infected erythrocyte surface antigen of Plasmodium falciparum associates with spectrin in the erythrocytic membrane. Mol. Biochem. Parasitol. 46:1991;137-148.
    • (1991) Mol. Biochem. Parasitol. , vol.46 , pp. 137-148
    • Foley, M.1
  • 6
    • 0028008830 scopus 로고
    • Plasmodium falciparum exports the Golgi marker sphingomyelin synthase into a tubovesicular network in the cytoplasm of mature erythrocytes
    • Elmendorf H.G., Haldar K. Plasmodium falciparum exports the Golgi marker sphingomyelin synthase into a tubovesicular network in the cytoplasm of mature erythrocytes. J. Cell Biol. 124:1994;449-462.
    • (1994) J. Cell Biol. , vol.124 , pp. 449-462
    • Elmendorf, H.G.1    Haldar, K.2
  • 7
    • 0034678922 scopus 로고    scopus 로고
    • Protein trafficking to the plastid of Plasmodium falciparum is via the secretory pathway
    • Waller R.F.et al. Protein trafficking to the plastid of Plasmodium falciparum is via the secretory pathway. EMBO J. 19:2000;1794-1802.
    • (2000) EMBO J. , vol.19 , pp. 1794-1802
    • Waller, R.F.1
  • 8
    • 0344549379 scopus 로고    scopus 로고
    • Nuclear-encoded proteins target to the plastid in Toxoplasma gondii and Plasmodium falciparum
    • Waller R.F.et al. Nuclear-encoded proteins target to the plastid in Toxoplasma gondii and Plasmodium falciparum. Proc. Natl. Acad. Sci. U. S. A. 95:1998;12352-12357.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 12352-12357
    • Waller, R.F.1
  • 9
    • 0033178777 scopus 로고    scopus 로고
    • Origins, targeting, and function of the apicomplexan plastid
    • Roos D.et al. Origins, targeting, and function of the apicomplexan plastid. Curr. Opin. Microbiol. 2:1999;426-432.
    • (1999) Curr. Opin. Microbiol. , vol.2 , pp. 426-432
    • Roos, D.1
  • 10
    • 0030775595 scopus 로고    scopus 로고
    • Identification of an endoplasmic reticulum-resident calcium-binding protein with multiple ef-hand motifs in asexual stages of Plasmodium falciparum
    • La Greca N.et al. Identification of an endoplasmic reticulum-resident calcium-binding protein with multiple ef-hand motifs in asexual stages of Plasmodium falciparum. Mol. Biochem. Parasitol. 89:1997;283-293.
    • (1997) Mol. Biochem. Parasitol. , vol.89 , pp. 283-293
    • La Greca, N.1
  • 11
    • 0025743647 scopus 로고
    • Induction and localization of Plasmodium falciparum stress proteins related to the heat shock protein 70 family
    • Kumar N.et al. Induction and localization of Plasmodium falciparum stress proteins related to the heat shock protein 70 family. Mol. Biochem. Parasitol. 48:1991;47-58.
    • (1991) Mol. Biochem. Parasitol. , vol.48 , pp. 47-58
    • Kumar, N.1
  • 12
    • 0032526698 scopus 로고    scopus 로고
    • The protozoan parasite Toxoplasma gondii targets proteins to dense granules and the vacuolar space using both conserved and unusual mechanisms
    • Karsten V.et al. The protozoan parasite Toxoplasma gondii targets proteins to dense granules and the vacuolar space using both conserved and unusual mechanisms. J. Cell Biol. 141:1998;1323-1333.
    • (1998) J. Cell Biol. , vol.141 , pp. 1323-1333
    • Karsten, V.1
  • 13
    • 0032845689 scopus 로고    scopus 로고
    • The nuclear envelope serves as an intermediary between the ER and Golgi complex in the intracellular parasite Toxoplasma gondii
    • Hager K.M.et al. The nuclear envelope serves as an intermediary between the ER and Golgi complex in the intracellular parasite Toxoplasma gondii. J. Cell Sci. 112:1999;2631-2638.
    • (1999) J. Cell Sci. , vol.112 , pp. 2631-2638
    • Hager, K.M.1
  • 14
    • 0033772272 scopus 로고    scopus 로고
    • Targeting to rhoptry organelles of Toxoplasma gondii involves evolutionarily conserved protein-sorting mechanisms
    • Hoppe H.et al. Targeting to rhoptry organelles of Toxoplasma gondii involves evolutionarily conserved protein-sorting mechanisms. Nat. Cell Biol. 2:2000;449-456.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 449-456
    • Hoppe, H.1
  • 15
    • 0021856417 scopus 로고
    • Signal sequences: The limits of variation
    • von Heijne G. Signal sequences. the limits of variation J. Mol. Biol. 184:1985;99-105.
    • (1985) J. Mol. Biol. , vol.184 , pp. 99-105
    • Von Heijne, G.1
  • 16
    • 0029415127 scopus 로고
    • The secretory pathway of Plasmodium falciparum regulates transport of p82/rap-1 to the rhoptries
    • Howard R.F., Schmidt C.M. The secretory pathway of Plasmodium falciparum regulates transport of p82/rap-1 to the rhoptries. Mol. Biochem. Parasitol. 74:1995;43-54.
    • (1995) Mol. Biochem. Parasitol. , vol.74 , pp. 43-54
    • Howard, R.F.1    Schmidt, C.M.2
  • 17
    • 0026636788 scopus 로고
    • A family of erythrocyte-binding proteins of malaria parasites
    • Adams J.H.et al. A family of erythrocyte-binding proteins of malaria parasites. Proc. Natl. Acad. Sci. U. S. A. 89:1992;7085-7089.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 7085-7089
    • Adams, J.H.1
  • 18
    • 0027267399 scopus 로고
    • Plasmodium falciparum: A molecular view of protein transport from the parasite into the host erythrocyte
    • Lingelbach K.R. Plasmodium falciparum. a molecular view of protein transport from the parasite into the host erythrocyte Exp. Parasitol. 76:1993;318-327.
    • (1993) Exp. Parasitol. , vol.76 , pp. 318-327
    • Lingelbach, K.R.1
  • 19
    • 0022431819 scopus 로고
    • The gene for an exported antigen of the malaria parasite Plasmodium falciparum cloned and expressed in Escherichia coli
    • Hope I.A.et al. The gene for an exported antigen of the malaria parasite Plasmodium falciparum cloned and expressed in Escherichia coli. Nucleic Acids Res. 13:1985;369-387.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 369-387
    • Hope, I.A.1
  • 20
    • 0026561901 scopus 로고
    • Brefeldin A: Insights into the control of membrane traffic and organelle structure
    • Klausner R.D.et al. Brefeldin A: insights into the control of membrane traffic and organelle structure. J. Cell Biol. 116:1992;1071-1080.
    • (1992) J. Cell Biol. , vol.116 , pp. 1071-1080
    • Klausner, R.D.1
  • 21
    • 0032855341 scopus 로고    scopus 로고
    • A homologue of Sar1p localises to a novel trafficking pathway in malaria-infected erythrocytes
    • Albano F.R.et al. A homologue of Sar1p localises to a novel trafficking pathway in malaria-infected erythrocytes. Eur. J. Cell Biol. 78:1999;453-462.
    • (1999) Eur. J. Cell Biol. , vol.78 , pp. 453-462
    • Albano, F.R.1
  • 22
    • 0028198724 scopus 로고
    • Brefeldin A inhibits transport of the glycophorin-binding protein from Plasmodium falciparum into the host erythrocyte
    • Benting J.et al. Brefeldin A inhibits transport of the glycophorin-binding protein from Plasmodium falciparum into the host erythrocyte. Biochem. J. 300:1994;821-826.
    • (1994) Biochem. J. , vol.300 , pp. 821-826
    • Benting, J.1
  • 23
    • 0027962346 scopus 로고
    • Plasmodium falciparum- The pf332 antigen is secreted from the parasite by a Brefeldin A-dependent pathway and is translocated to the erythrocyte membrane via the Maurer's clefts
    • Hinterberg K.et al. Plasmodium falciparum- the pf332 antigen is secreted from the parasite by a Brefeldin A-dependent pathway and is translocated to the erythrocyte membrane via the Maurer's clefts. Exp. Parasitol. 79:1994;279-291.
    • (1994) Exp. Parasitol. , vol.79 , pp. 279-291
    • Hinterberg, K.1
  • 24
    • 0031044707 scopus 로고    scopus 로고
    • Molecular characterization of an expressed sequence tag locus of Toxoplasma gondii encoding the micronemal protein MIC2
    • Wan K.et al. Molecular characterization of an expressed sequence tag locus of Toxoplasma gondii encoding the micronemal protein MIC2. Mol. Biochem. Parasitol. 84:1997;203-214.
    • (1997) Mol. Biochem. Parasitol. , vol.84 , pp. 203-214
    • Wan, K.1
  • 25
    • 0032582554 scopus 로고    scopus 로고
    • Processing of Toxoplasma ROP1 protein in nascent rhoptries
    • Soldati D.et al. Processing of Toxoplasma ROP1 protein in nascent rhoptries. Mol. Biochem. Parasitol. 96:1998;37-48.
    • (1998) Mol. Biochem. Parasitol. , vol.96 , pp. 37-48
    • Soldati, D.1
  • 26
    • 0032859858 scopus 로고    scopus 로고
    • Intracellular trafficking of dense granule proteins in Toxoplasma gondii and experimental evidences for a regulated exocytosis
    • Coppens I.et al. Intracellular trafficking of dense granule proteins in Toxoplasma gondii and experimental evidences for a regulated exocytosis. Eur. J. Cell Biol. 78:1999;463-472.
    • (1999) Eur. J. Cell Biol. , vol.78 , pp. 463-472
    • Coppens, I.1
  • 27
    • 0033092940 scopus 로고    scopus 로고
    • A Plasmodium chabaudi chabaudi high molecular mass glycoprotein translocated to the host cell membrane by a non-classical secretary pathway
    • Moura I.C., Pudles J. A Plasmodium chabaudi chabaudi high molecular mass glycoprotein translocated to the host cell membrane by a non-classical secretary pathway. Eur. J. Cell Biol. 78:1999;186-193.
    • (1999) Eur. J. Cell Biol. , vol.78 , pp. 186-193
    • Moura, I.C.1    Pudles, J.2
  • 28
    • 0025638998 scopus 로고
    • A cytochemical ultrastructural study of the lysosomal system of different species of malaria parasites
    • Slomianny C., Prensier G. A cytochemical ultrastructural study of the lysosomal system of different species of malaria parasites. J. Protozool. 37:1990;465-470.
    • (1990) J. Protozool. , vol.37 , pp. 465-470
    • Slomianny, C.1    Prensier, G.2
  • 29
    • 0033982042 scopus 로고    scopus 로고
    • Evidence for vesicle-mediated trafficking of parasite proteins to the host cell cytosol and erythrocyte surface membrane in Plasmodium falciparum-infected erythrocytes
    • Trelka D.P.et al. Evidence for vesicle-mediated trafficking of parasite proteins to the host cell cytosol and erythrocyte surface membrane in Plasmodium falciparum-infected erythrocytes. Mol. Biochem. Parasitol. 106:2000;131-145.
    • (2000) Mol. Biochem. Parasitol. , vol.106 , pp. 131-145
    • Trelka, D.P.1
  • 30
    • 0027501330 scopus 로고
    • Identification and localization of erd2 in the malaria parasite Plasmodium falciparum - separation from sites of sphingomyelin synthesis and implications for organization of the Golgi
    • Elmendorf H.G., Haldar K. Identification and localization of erd2 in the malaria parasite Plasmodium falciparum - separation from sites of sphingomyelin synthesis and implications for organization of the Golgi. EMBO J. 12:1993;4763-4773.
    • (1993) EMBO J. , vol.12 , pp. 4763-4773
    • Elmendorf, H.G.1    Haldar, K.2
  • 31
    • 0030249050 scopus 로고    scopus 로고
    • Identification of a family of rab g-proteins in Plasmodium falciparum and a detailed characterization of pfrab6
    • de Castro F.A.et al. Identification of a family of rab g-proteins in Plasmodium falciparum and a detailed characterization of pfrab6. Mol. Biochem. Parasitol. 80:1996;77-88.
    • (1996) Mol. Biochem. Parasitol. , vol.80 , pp. 77-88
    • De Castro, F.A.1
  • 32
    • 0030566712 scopus 로고    scopus 로고
    • Identification and localization of rab6, separation of rab6 from erd2 and implications for an unstacked Golgi, in Plasmodium falciparum
    • Van Wye J.et al. Identification and localization of rab6, separation of rab6 from erd2 and implications for an unstacked Golgi, in Plasmodium falciparum. Mol. Biochem. Parasitol. 83:1996;107-120.
    • (1996) Mol. Biochem. Parasitol. , vol.83 , pp. 107-120
    • Van Wye, J.1
  • 33
    • 0033597829 scopus 로고    scopus 로고
    • Bulk flow redux?
    • Warren G., Mellman I. Bulk flow redux? Cell. 98:1999;125-127.
    • (1999) Cell , vol.98 , pp. 125-127
    • Warren, G.1    Mellman, I.2
  • 34
    • 0030813492 scopus 로고    scopus 로고
    • Protein trafficking in the Plasmodium falciparum-infected erythrocyte - From models to mechanisms
    • Lingelbach K. Protein trafficking in the Plasmodium falciparum-infected erythrocyte - from models to mechanisms. Ann. Trop. Med. Parasitol. 91:1997;543-549.
    • (1997) Ann. Trop. Med. Parasitol. , vol.91 , pp. 543-549
    • Lingelbach, K.1
  • 35
  • 36
    • 0030006120 scopus 로고    scopus 로고
    • Protein sorting in Plasmodium falciparum-infected red blood cells permeabilized with the pore-forming protein streptolysin O
    • Ansorge I.et al. Protein sorting in Plasmodium falciparum-infected red blood cells permeabilized with the pore-forming protein streptolysin O. Biochem. J. 315:1996;307-314.
    • (1996) Biochem. J. , vol.315 , pp. 307-314
    • Ansorge, I.1
  • 37
    • 0029036498 scopus 로고
    • Parasite-regulated membrane transport processes and metabolic control in malaria-infected erythrocytes
    • Elford B.C.et al. Parasite-regulated membrane transport processes and metabolic control in malaria-infected erythrocytes. Biochem. J. 308:1995;361-374.
    • (1995) Biochem. J. , vol.308 , pp. 361-374
    • Elford, B.C.1
  • 38
    • 0028131368 scopus 로고
    • Biosynthesis, export and processing of a 45 kDa protein detected in membrane clefts of erythrocytes infected with Plasmodium falciparum
    • Das A.et al. Biosynthesis, export and processing of a 45 kDa protein detected in membrane clefts of erythrocytes infected with Plasmodium falciparum. Biochem. J. 302:1994;487-496.
    • (1994) Biochem. J. , vol.302 , pp. 487-496
    • Das, A.1
  • 39
    • 0031050374 scopus 로고    scopus 로고
    • Macromolecular transport in malaria- does the duct exist?
    • Hibbs A.R.et al. Macromolecular transport in malaria- does the duct exist? Eur. J. Cell Biol. 72:1997;182-188.
    • (1997) Eur. J. Cell Biol. , vol.72 , pp. 182-188
    • Hibbs, A.R.1
  • 40
    • 0023993272 scopus 로고
    • The parasitophorous vacuole membrane of Plasmodium falciparum: Demonstration of vesicle formation using an immunoprobe
    • Kara U.A.et al. The parasitophorous vacuole membrane of Plasmodium falciparum: demonstration of vesicle formation using an immunoprobe. Eur. J. Cell Biol. 46:1988;9-17.
    • (1988) Eur. J. Cell Biol. , vol.46 , pp. 9-17
    • Kara, U.A.1
  • 41
    • 0027049796 scopus 로고
    • Trafficking of malarial proteins to the host cell cytoplasm and erythrocyte surface membrane involves multiple pathways
    • Gormley J.A.et al. Trafficking of malarial proteins to the host cell cytoplasm and erythrocyte surface membrane involves multiple pathways. J. Cell Sci. 119:1992;1481-1495.
    • (1992) J. Cell Sci. , vol.119 , pp. 1481-1495
    • Gormley, J.A.1
  • 42
    • 0033152342 scopus 로고    scopus 로고
    • Novel secretory pathways in Plasmodium?
    • Mattei D.et al. Novel secretory pathways in Plasmodium? Parasitol. Today. 15:1999;235-237.
    • (1999) Parasitol. Today , vol.15 , pp. 235-237
    • Mattei, D.1
  • 43
    • 0040537042 scopus 로고    scopus 로고
    • Competition between Sec- And TAT-dependent protein translocation in Escherichia coli
    • Cristobal S.et al. Competition between Sec- and TAT-dependent protein translocation in Escherichia coli. EMBO J. 18:1999;2982-2990.
    • (1999) EMBO J. , vol.18 , pp. 2982-2990
    • Cristobal, S.1
  • 44
    • 0034141202 scopus 로고    scopus 로고
    • Differential sorting and post-secretory targeting of proteins in parasitic invasion
    • Ngo H.et al. Differential sorting and post-secretory targeting of proteins in parasitic invasion. Trends Cell Biol. 10:2000;67-72.
    • (2000) Trends Cell Biol. , vol.10 , pp. 67-72
    • Ngo, H.1
  • 45
    • 0033130151 scopus 로고    scopus 로고
    • Export of Plasmodium proteins via a novel secretory pathway
    • Wiser M.F.et al. Export of Plasmodium proteins via a novel secretory pathway. Parasitol. Today. 15:1999;194-198.
    • (1999) Parasitol. Today , vol.15 , pp. 194-198
    • Wiser, M.F.1
  • 46
    • 0030745899 scopus 로고    scopus 로고
    • A novel alternate secretory pathway for the export of Plasmodium proteins into the host erythrocyte
    • Wiser M.F.et al. A novel alternate secretory pathway for the export of Plasmodium proteins into the host erythrocyte. Proc. Natl. Acad. Sci. U. S. A. 94:1997;9108-9113.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 9108-9113
    • Wiser, M.F.1
  • 47
    • 0032520083 scopus 로고    scopus 로고
    • Sorting of invertase signal peptide mutants in yeast dependent and independent on the signal-recognition particle
    • Rothe C., Lehle L. Sorting of invertase signal peptide mutants in yeast dependent and independent on the signal-recognition particle. Eur. J. Biochem. 252:1998;16-24.
    • (1998) Eur. J. Biochem. , vol.252 , pp. 16-24
    • Rothe, C.1    Lehle, L.2
  • 48
    • 0031397410 scopus 로고    scopus 로고
    • Brefeldin A effects in plants- are different Golgi responses caused by different sites of action
    • Staehelin L.A., Driouich A. Brefeldin A effects in plants- are different Golgi responses caused by different sites of action. Plant Physiol. 114:1997;401-403.
    • (1997) Plant Physiol. , vol.114 , pp. 401-403
    • Staehelin, L.A.1    Driouich, A.2
  • 49
    • 0024364949 scopus 로고
    • Mannose 6-phosphate receptors and lysosomal enzyme targeting
    • Dahms N.M.et al. Mannose 6-phosphate receptors and lysosomal enzyme targeting. J. Biol. Chem. 264:1989;12115-12118.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12115-12118
    • Dahms, N.M.1
  • 50
    • 0033118395 scopus 로고    scopus 로고
    • Protein glycosylation in the malaria parasite
    • Gowda D.C., Davidson E.A. Protein glycosylation in the malaria parasite. Parasitol. Today. 15:1999;147-152.
    • (1999) Parasitol. Today , vol.15 , pp. 147-152
    • Gowda, D.C.1    Davidson, E.A.2
  • 51
    • 0030801249 scopus 로고    scopus 로고
    • Dictyostelium lysosomal proteins with different sugar modifications sort to functionally distinct compartments
    • Souza G.M.et al. Dictyostelium lysosomal proteins with different sugar modifications sort to functionally distinct compartments. J. Cell Sci. 110:1997;2239-2248.
    • (1997) J. Cell Sci. , vol.110 , pp. 2239-2248
    • Souza, G.M.1
  • 52
    • 0029947655 scopus 로고    scopus 로고
    • Targeting of proteins to granule subsets is determined by timing and not by sorting- The specific granule protein NGAL is localized to azurophil granules when expressed in HL-60 cells
    • Le Cabec V.et al. Targeting of proteins to granule subsets is determined by timing and not by sorting- the specific granule protein NGAL is localized to azurophil granules when expressed in HL-60 cells. Proc. Natl. Acad. Sci. U. S. A. 93:1996;6454-6457.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 6454-6457
    • Le Cabec, V.1
  • 53
    • 0032510979 scopus 로고    scopus 로고
    • Precise timing of expression of a Plasmodium falciparum-derived transgene in Plasmodium berghei is a critical determinant of subsequent subcellular localization
    • Kocken C.et al. Precise timing of expression of a Plasmodium falciparum-derived transgene in Plasmodium berghei is a critical determinant of subsequent subcellular localization. J. Biol. Chem. 273:1998;15119-15124.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15119-15124
    • Kocken, C.1
  • 54
    • 0032815207 scopus 로고    scopus 로고
    • Apicomplexan plastids as drug targets
    • McFadden G.I., Roos D.S. Apicomplexan plastids as drug targets. Trends Microbiol. 6:1999;328-333.
    • (1999) Trends Microbiol. , vol.6 , pp. 328-333
    • McFadden, G.I.1    Roos, D.S.2
  • 55
    • 0033520336 scopus 로고    scopus 로고
    • Inhibitors of the nonmevalonate pathway of isoprenoid biosynthesis as antimalarial drugs
    • Jomaa H.et al. Inhibitors of the nonmevalonate pathway of isoprenoid biosynthesis as antimalarial drugs. Science. 285:1999;1573-1576.
    • (1999) Science , vol.285 , pp. 1573-1576
    • Jomaa, H.1
  • 56
    • 0026097503 scopus 로고
    • Chloroplast transit peptides: The perfect random coil?
    • von Heijne G., Nishikawa K. Chloroplast transit peptides: the perfect random coil? FEBS Lett. 278:1991;1-3.
    • (1991) FEBS Lett. , vol.278 , pp. 1-3
    • Von Heijne, G.1    Nishikawa, K.2
  • 57
    • 0032168004 scopus 로고    scopus 로고
    • Protein translocation into and across the chloroplastic envelope membranes
    • Soll J., Tien R. Protein translocation into and across the chloroplastic envelope membranes. Plant Mol. Biol. 38:1998;191-207.
    • (1998) Plant Mol. Biol. , vol.38 , pp. 191-207
    • Soll, J.1    Tien, R.2
  • 58
    • 0033213013 scopus 로고    scopus 로고
    • The plastid in Plasmodium falciparum asexual blood stages: A three-dimensional ultrastructural analysis
    • Hopkins J.et al. The plastid in Plasmodium falciparum asexual blood stages: a three-dimensional ultrastructural analysis. Protist. 150:1999;283-295.
    • (1999) Protist , vol.150 , pp. 283-295
    • Hopkins, J.1
  • 59
    • 0033167259 scopus 로고    scopus 로고
    • Plastids and protein targeting
    • McFadden G.I. Plastids and protein targeting. J. Euk. Microbiol. 46:1999;339-346.
    • (1999) J. Euk. Microbiol. , vol.46 , pp. 339-346
    • McFadden, G.I.1
  • 60
    • 0033485273 scopus 로고    scopus 로고
    • Endosymbiosis and evolution of the plant cell
    • McFadden G.I. Endosymbiosis and evolution of the plant cell. Curr. Opin. Plant Biol. 2:1999;513-519.
    • (1999) Curr. Opin. Plant Biol. , vol.2 , pp. 513-519
    • McFadden, G.I.1
  • 61
    • 0023737790 scopus 로고
    • Molecular analysis of the gene encoding the major surface antigen of Toxoplasma gondii
    • Burg J.et al. Molecular analysis of the gene encoding the major surface antigen of Toxoplasma gondii. J. Immunol. 141:1988;3583-3591.
    • (1988) J. Immunol. , vol.141 , pp. 3583-3591
    • Burg, J.1
  • 62
    • 0032838597 scopus 로고    scopus 로고
    • Principles of protein and lipid targeting in secondary symbiogenesis: Euglenoid, dinoflagellate, and sporozoan plastid origins and the eukaryotic family tree
    • Cavalier-Smith T. Principles of protein and lipid targeting in secondary symbiogenesis. euglenoid, dinoflagellate, and sporozoan plastid origins and the eukaryotic family tree J. Euk. Microbiol. 46:1999;347-366.
    • (1999) J. Euk. Microbiol. , vol.46 , pp. 347-366
    • Cavalier-Smith, T.1
  • 63
    • 0032784582 scopus 로고    scopus 로고
    • The structural flexibility of the preferredoxin transit peptide
    • Wienk H.L.J.et al. The structural flexibility of the preferredoxin transit peptide. FEBS Lett. 453:1999;318-326.
    • (1999) FEBS Lett. , vol.453 , pp. 318-326
    • Wienk, H.L.J.1
  • 64
    • 0032078205 scopus 로고    scopus 로고
    • Expression, selection and organellar targeting of the green fluorescent protein in Toxoplasma gondii
    • Striepen B.et al. Expression, selection and organellar targeting of the green fluorescent protein in Toxoplasma gondii. Mol. Biochem. Parasitol. 92:1998;325-338.
    • (1998) Mol. Biochem. Parasitol. , vol.92 , pp. 325-338
    • Striepen, B.1
  • 65
    • 0033063592 scopus 로고    scopus 로고
    • Subcellular fractionation, electromigration analysis and mapping of organelles
    • Pasquali C.et al. Subcellular fractionation, electromigration analysis and mapping of organelles. J. Chromatogr. B. 722:1999;89-102.
    • (1999) J. Chromatogr. B. , vol.722 , pp. 89-102
    • Pasquali, C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.