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Volumn 126, Issue 2, 2003, Pages 143-154

Phospholipids in parasitic protozoa

Author keywords

Apicomplexa; Fatty acid; Glycolipid; Parasitic protozoa; Phospholipid; Trypanosomatidae

Indexed keywords

ANTIPARASITIC AGENT; PHOSPHOLIPID;

EID: 0037325017     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(02)00281-5     Document Type: Review
Times cited : (121)

References (114)
  • 1
    • 0030792813 scopus 로고    scopus 로고
    • SAFE HAVEN: The cell biology of nonfusogenic pathogen vacuoles
    • Sinai A.P., Joiner K.A. SAFE HAVEN: the cell biology of nonfusogenic pathogen vacuoles. Annu. Rev. Microbiol. 51:1997;415-462.
    • (1997) Annu. Rev. Microbiol. , vol.51 , pp. 415-462
    • Sinai, A.P.1    Joiner, K.A.2
  • 2
    • 0035069258 scopus 로고    scopus 로고
    • Membrane transport in the malaria-infected erythrocyte
    • Kirk K. Membrane transport in the malaria-infected erythrocyte. Physiol. Rev. 81:2001;495-537.
    • (2001) Physiol. Rev. , vol.81 , pp. 495-537
    • Kirk, K.1
  • 3
    • 0034139847 scopus 로고    scopus 로고
    • Cell invasion by un-palatable parasites
    • Sibley L.D., Andrews N.W. Cell invasion by un-palatable parasites. Traffic. 1:2000;100-106.
    • (2000) Traffic , vol.1 , pp. 100-106
    • Sibley, L.D.1    Andrews, N.W.2
  • 4
    • 0030606248 scopus 로고    scopus 로고
    • Hijacking the cell: Parasites in the driver's seat
    • Beverley S.M. Hijacking the cell: parasites in the driver's seat. Cell. 87:1996;787-789.
    • (1996) Cell , vol.87 , pp. 787-789
    • Beverley, S.M.1
  • 5
    • 0034753916 scopus 로고    scopus 로고
    • Migration through host cells by apicomplexan parasites
    • Mota M.M., Rodriguez A. Migration through host cells by apicomplexan parasites. Microbes Infect. 3:2001;1123-1128.
    • (2001) Microbes Infect. , vol.3 , pp. 1123-1128
    • Mota, M.M.1    Rodriguez, A.2
  • 6
    • 0034853631 scopus 로고    scopus 로고
    • Apical organelles of Apicomplexa: Biology and isolation by subcellular fractionation
    • Blackman M.J., Bannister L.H. Apical organelles of Apicomplexa: biology and isolation by subcellular fractionation. Mol. Biochem. Parasitol. 117:2001;11-25.
    • (2001) Mol. Biochem. Parasitol. , vol.117 , pp. 11-25
    • Blackman, M.J.1    Bannister, L.H.2
  • 7
    • 0022088385 scopus 로고
    • How does Toxoplasma gondii enter host cells?
    • Werk R. How does Toxoplasma gondii enter host cells? Rev. Infect. Dis. 7:1985;449-457.
    • (1985) Rev. Infect. Dis. , vol.7 , pp. 449-457
    • Werk, R.1
  • 8
    • 0034123640 scopus 로고    scopus 로고
    • The journey of the malaria sporozoite through its hosts: Two parasite proteins lead the way
    • Menard R.U. The journey of the malaria sporozoite through its hosts: two parasite proteins lead the way. Microbes Infect. 2:2000;633-642.
    • (2000) Microbes Infect. , vol.2 , pp. 633-642
    • Menard, R.U.1
  • 9
    • 0030737802 scopus 로고    scopus 로고
    • Time lapse video microscopy and ultrastructure of penetrating sporozoites, types 1 and 2 parasitophorous vacuoles, and the transformation of sporozoites to tachyzoites of the VEG strain of Toxoplasma gondii
    • Speer C.A., Dubey J.P., Blixt J.A.et al. Time lapse video microscopy and ultrastructure of penetrating sporozoites, types 1 and 2 parasitophorous vacuoles, and the transformation of sporozoites to tachyzoites of the VEG strain of Toxoplasma gondii. J. Parasitol. 83:1997;565-574.
    • (1997) J. Parasitol. , vol.83 , pp. 565-574
    • Speer, C.A.1    Dubey, J.P.2    Blixt, J.A.3
  • 10
    • 0031081683 scopus 로고    scopus 로고
    • Cell invasion by the vertebrate stages of Plasmodium
    • Sinnis P., Sim B.K. Cell invasion by the vertebrate stages of Plasmodium. Trends Microbiol. 5:1997;52-58.
    • (1997) Trends Microbiol. , vol.5 , pp. 52-58
    • Sinnis, P.1    Sim, B.K.2
  • 11
    • 0029000291 scopus 로고
    • The role of the cytoskeleton in Plasmodium falciparum merozoite biology: An electron-microscopic view
    • Bannister L.H., Mitchell G.H. The role of the cytoskeleton in Plasmodium falciparum merozoite biology: an electron-microscopic view. Ann. Trop. Med. Parasitol. 89:1995;105-111.
    • (1995) Ann. Trop. Med. Parasitol. , vol.89 , pp. 105-111
    • Bannister, L.H.1    Mitchell, G.H.2
  • 12
    • 0033969153 scopus 로고    scopus 로고
    • Phosphatidylcholine formation is the predominant lipid biosynthetic event in the hemoparasite Babesia bovis
    • Florin-Christensen J., Suarez C.E., Florin-Christensen M.et al. Phosphatidylcholine formation is the predominant lipid biosynthetic event in the hemoparasite Babesia bovis. Mol. Biochem. Parasitol. 106:2000;147-156.
    • (2000) Mol. Biochem. Parasitol. , vol.106 , pp. 147-156
    • Florin-Christensen, J.1    Suarez, C.E.2    Florin-Christensen, M.3
  • 14
    • 0030271865 scopus 로고    scopus 로고
    • Sphingolipid synthesis and membrane formation by Plasmodium
    • Haldar K. Sphingolipid synthesis and membrane formation by Plasmodium. Trends Cell Biol. 6:1996;398-405.
    • (1996) Trends Cell Biol. , vol.6 , pp. 398-405
    • Haldar, K.1
  • 15
  • 16
    • 0025176919 scopus 로고
    • Phospholipid composition, cholesterol content and cholesterol exchange in Plasmodium falciparum-infected red cells
    • Maguire P.A., Sherman I.W.S. Phospholipid composition, cholesterol content and cholesterol exchange in Plasmodium falciparum-infected red cells. Mol. Biochem. Parasitol. 38:1990;105-112.
    • (1990) Mol. Biochem. Parasitol. , vol.38 , pp. 105-112
    • Maguire, P.A.1    Sherman, I.W.S.2
  • 17
    • 0027526061 scopus 로고
    • Plasmodium chabaudi-parasitized erythrocytes: Phosphatidylcholine species of parasites and host cell membranes
    • Simões A.P., Fiebig S., Wunderlich F.et al. Plasmodium chabaudi-parasitized erythrocytes: phosphatidylcholine species of parasites and host cell membranes. Mol. Biochem. Parasitol. 57:1993;345-348.
    • (1993) Mol. Biochem. Parasitol. , vol.57 , pp. 345-348
    • Simões, A.P.1    Fiebig, S.2    Wunderlich, F.3
  • 18
    • 0025216889 scopus 로고
    • Plasmodium knowlesi induces alterations in phosphatidylcholine and phosphatidylethanolamine molecular species composition of parasitized monkey erythrocytes
    • Simões A.P., Moll G.N., Beaumelle B.et al. Plasmodium knowlesi induces alterations in phosphatidylcholine and phosphatidylethanolamine molecular species composition of parasitized monkey erythrocytes. Biochim. Biophys. Acta. 1022:1990;135-145.
    • (1990) Biochim. Biophys. Acta , vol.1022 , pp. 135-145
    • Simões, A.P.1    Moll, G.N.2    Beaumelle, B.3
  • 19
    • 0025816240 scopus 로고
    • Lipids and fatty acids of tachyzoites and purified pellicles of Toxoplasma gondii
    • Foussard F., Gallois Y., Girault A.et al. Lipids and fatty acids of tachyzoites and purified pellicles of Toxoplasma gondii. Parasitol. Res. 77:1991;475-477.
    • (1991) Parasitol. Res. , vol.77 , pp. 475-477
    • Foussard, F.1    Gallois, Y.2    Girault, A.3
  • 20
    • 0035400296 scopus 로고    scopus 로고
    • Characterization of the subpellicular network, a filamentous membrane skeletal component in the parasite Toxoplasma gondii
    • Mann T., Beckers C. Characterization of the subpellicular network, a filamentous membrane skeletal component in the parasite Toxoplasma gondii. Mol. Biochem. Parasitol. 115:2001;257-268.
    • (2001) Mol. Biochem. Parasitol. , vol.115 , pp. 257-268
    • Mann, T.1    Beckers, C.2
  • 21
    • 0025732915 scopus 로고
    • Characterization of the lipid content of Toxoplasma gondii rhoptries
    • Foussard F., Leriche M.A., Dubremetz J.F. Characterization of the lipid content of Toxoplasma gondii rhoptries. Parasitology. 102:1991;367-370.
    • (1991) Parasitology , vol.102 , pp. 367-370
    • Foussard, F.1    Leriche, M.A.2    Dubremetz, J.F.3
  • 22
    • 0025733516 scopus 로고
    • Rhoptry lipids and parasitophorous vacuole formation: A slippery issue
    • Joiner K.A. Rhoptry lipids and parasitophorous vacuole formation: a slippery issue. Parasitol. Today. 7:1991;226-227.
    • (1991) Parasitol. Today , vol.7 , pp. 226-227
    • Joiner, K.A.1
  • 23
  • 24
    • 0031016286 scopus 로고    scopus 로고
    • Endocytosis and secretion in trypanosomatid parasites - Tumultuous traffic in a pocket
    • Overath P., Stierhof Y.-D., Wiese M. Endocytosis and secretion in trypanosomatid parasites - tumultuous traffic in a pocket. Trends Cell Biol. 7:1997;27-33.
    • (1997) Trends Cell Biol. , vol.7 , pp. 27-33
    • Overath, P.1    Stierhof, Y.-D.2    Wiese, M.3
  • 25
    • 0027394055 scopus 로고
    • Molecular species analysis of phospholipids from Trypanosoma brucei bloodstream and procyclic forms
    • Patnaik P.K., Field M.C., Menon A.K.et al. Molecular species analysis of phospholipids from Trypanosoma brucei bloodstream and procyclic forms. Mol. Biochem. Parasitol. 58:1993;97-105.
    • (1993) Mol. Biochem. Parasitol. , vol.58 , pp. 97-105
    • Patnaik, P.K.1    Field, M.C.2    Menon, A.K.3
  • 26
    • 0035936850 scopus 로고    scopus 로고
    • GPI-anchored proteins and glycoconjugates segregate into lipid rafts in Kinetoplastida
    • Denny P.W., Field M.C., Smith D.F. GPI-anchored proteins and glycoconjugates segregate into lipid rafts in Kinetoplastida. FEBS Lett. 491:2001;148-153.
    • (2001) FEBS Lett. , vol.491 , pp. 148-153
    • Denny, P.W.1    Field, M.C.2    Smith, D.F.3
  • 27
    • 0024433170 scopus 로고
    • Isolation and characterization of a highly purified flagellar membrane fraction from trypanosomatids
    • da Cunha e Silva N.L., Hasson Voloch A., de Souza W. Isolation and characterization of a highly purified flagellar membrane fraction from trypanosomatids. Mol. Biochem. Parasitol. 37:1989;129-136.
    • (1989) Mol. Biochem. Parasitol. , vol.37 , pp. 129-136
    • Da Cunha E Silva, N.L.1    Hasson Voloch, A.2    De Souza, W.3
  • 28
    • 0022019697 scopus 로고
    • Lipid analyses of isolated surface membranes of Leishmania donovani promastigotes
    • Wassef M.K., Fioretti T.B., Dwyer D.M. Lipid analyses of isolated surface membranes of Leishmania donovani promastigotes. Lipids. 20:1985;108-115.
    • (1985) Lipids , vol.20 , pp. 108-115
    • Wassef, M.K.1    Fioretti, T.B.2    Dwyer, D.M.3
  • 29
    • 0025204534 scopus 로고    scopus 로고
    • Biosynthesis and dynamics of lipids in Plasmodium-infected mature mammalian erythrocytes
    • Vial HJ, Ancelin ML, Philippot JR, et al. Biosynthesis and dynamics of lipids in Plasmodium-infected mature mammalian erythrocytes. Blood Cells 1990;16:531-55 & ibid. 59-61.
    • (1990) Blood Cells , vol.16 , pp. 531-555
    • Vial, H.J.1    Ancelin, M.L.2    Philippot, J.R.3
  • 30
    • 0025204534 scopus 로고    scopus 로고
    • Vial HJ, Ancelin ML, Philippot JR, et al. Biosynthesis and dynamics of lipids in Plasmodium-infected mature mammalian erythrocytes. Blood Cells 1990;16:531-55 & ibid. 59-61.
    • Blood Cells , pp. 59-61
  • 31
    • 0003046120 scopus 로고    scopus 로고
    • Malarial Lipids
    • Sherman IW, editor. Washington, DC: American Association of Microbiology Press
    • Vial HJ, Ancelin ML. Malarial Lipids. In: Sherman IW, editor. Malaria: parasite biology, biogenesis, protection. Washington, DC: American Association of Microbiology Press; 1998. p. 159-75.
    • (1998) Malaria: Parasite Biology, Biogenesis, Protection , pp. 159-175
    • Vial, H.J.1    Ancelin, M.L.2
  • 32
    • 0026027304 scopus 로고
    • Lipid traffic between high density lipoproteins and Plasmodium falciparum-infected red blood cells
    • Grellier P., Rigomier D., Clavey V.et al. Lipid traffic between high density lipoproteins and Plasmodium falciparum-infected red blood cells. J. Cell Biol. 112:1991;267-277.
    • (1991) J. Cell Biol. , vol.112 , pp. 267-277
    • Grellier, P.1    Rigomier, D.2    Clavey, V.3
  • 33
    • 0015029486 scopus 로고
    • The apparent transfer of fatty acid from phosphatidylcholine to phosphatidylethanolamine in human erythrocytes
    • Shohet S.B. The apparent transfer of fatty acid from phosphatidylcholine to phosphatidylethanolamine in human erythrocytes. J. Lipid Res. 12:1971;139-141.
    • (1971) J. Lipid Res. , vol.12 , pp. 139-141
    • Shohet, S.B.1
  • 34
    • 0021211920 scopus 로고
    • A reevaluation of the status of cholesterol in erythrocytes infected by Plasmodium knowlesi and P. falciparum
    • Vial H.J., Philippot J.R., Wallach D.F. A reevaluation of the status of cholesterol in erythrocytes infected by Plasmodium knowlesi and P. falciparum. Mol. Biochem. Parasitol. 13:1984;53-65.
    • (1984) Mol. Biochem. Parasitol. , vol.13 , pp. 53-65
    • Vial, H.J.1    Philippot, J.R.2    Wallach, D.F.3
  • 35
    • 0028865299 scopus 로고
    • Molecular cloning of CTP: Phosphocholine cytidylyltransferase from Plasmodium falciparum
    • Yeo H.J., Sri Widada J., Mercereau-Puijalon O.et al. Molecular cloning of CTP: phosphocholine cytidylyltransferase from Plasmodium falciparum. Eur. J. Biochem. 233:1995;62-72.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 62-72
    • Yeo, H.J.1    Sri Widada, J.2    Mercereau-Puijalon, O.3
  • 36
    • 0030754483 scopus 로고    scopus 로고
    • Plasmodium falciparum CTP: Phosphocholine cytidylyltransferase expressed in Escherichia coli: Purification, characterization and lipid regulation
    • Yeo H.J., Larvor M.P., Ancelin M.L.et al. Plasmodium falciparum CTP: phosphocholine cytidylyltransferase expressed in Escherichia coli: purification, characterization and lipid regulation. Biochem. J. 324(Pt 3):1997;903-910.
    • (1997) Biochem. J. , vol.324 , Issue.PART 3 , pp. 903-910
    • Yeo, H.J.1    Larvor, M.P.2    Ancelin, M.L.3
  • 37
    • 0033824079 scopus 로고    scopus 로고
    • Characterization of Plasmodium falciparum CDP-diacylglycerol synthase a proteolytically cleaved enzyme
    • Martin D., Gannoun-Zaki L., Bonnefoy S.et al. Characterization of Plasmodium falciparum CDP-diacylglycerol synthase a proteolytically cleaved enzyme. Mol. Biochem. Parasitol. 110:2000;93-105.
    • (2000) Mol. Biochem. Parasitol. , vol.110 , pp. 93-105
    • Martin, D.1    Gannoun-Zaki, L.2    Bonnefoy, S.3
  • 38
    • 0030908445 scopus 로고    scopus 로고
    • Phospholipid metabolism of serine in Plasmodium-infected erythrocytes involves phosphatidylserine and direct serine decarboxylation
    • Elabbadi N., Ancelin M.L., Vial H.J. Phospholipid metabolism of serine in Plasmodium-infected erythrocytes involves phosphatidylserine and direct serine decarboxylation. Biochem. J. 324(Pt 2):1997;435-445.
    • (1997) Biochem. J. , vol.324 , Issue.PART 2 , pp. 435-445
    • Elabbadi, N.1    Ancelin, M.L.2    Vial, H.J.3
  • 39
    • 0033769468 scopus 로고    scopus 로고
    • Molecular cloning, functional complementation in Saccharomyces cerevisiae and enzymatic properties of phosphatidylinositol synthase from the protozoan parasite Toxoplasma gondii
    • Seron K., Dzierszinski F., Tomavo S. Molecular cloning, functional complementation in Saccharomyces cerevisiae and enzymatic properties of phosphatidylinositol synthase from the protozoan parasite Toxoplasma gondii. Eur. J. Biochem. 267:2000;6571-6579.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6571-6579
    • Seron, K.1    Dzierszinski, F.2    Tomavo, S.3
  • 40
    • 0029963923 scopus 로고    scopus 로고
    • Genetic regulation of phospholipid biosynthesis in Saccharomyces cerevisiae
    • Greenberg M.L., Lopes J.M. Genetic regulation of phospholipid biosynthesis in Saccharomyces cerevisiae. Microbiol. Rev. 60:1996;1-20.
    • (1996) Microbiol. Rev. , vol.60 , pp. 1-20
    • Greenberg, M.L.1    Lopes, J.M.2
  • 41
    • 0037197768 scopus 로고    scopus 로고
    • A 24 bp cis-acting element essential for the transcriptional activity of Plasmodium falciparum CDP-diacylglycerol synthase gene promoter
    • Osta M., Gannoun-Zaki L., Bonnefoy S.et al. A 24 bp cis-acting element essential for the transcriptional activity of Plasmodium falciparum CDP-diacylglycerol synthase gene promoter. Mol. Biochem. Parasitol. 121:2002;87-98.
    • (2002) Mol. Biochem. Parasitol. , vol.121 , pp. 87-98
    • Osta, M.1    Gannoun-Zaki, L.2    Bonnefoy, S.3
  • 42
    • 0034599991 scopus 로고    scopus 로고
    • Toxoplasma gondii exploits host low-density lipoprotein receptor-mediated endocytosis for cholesterol acquisition
    • Coppens I., Sinai A.P., Joiner K.A. Toxoplasma gondii exploits host low-density lipoprotein receptor-mediated endocytosis for cholesterol acquisition. J. Cell Biol. 149:2000;167-180.
    • (2000) J. Cell Biol. , vol.149 , pp. 167-180
    • Coppens, I.1    Sinai, A.P.2    Joiner, K.A.3
  • 43
    • 0034616181 scopus 로고    scopus 로고
    • Specialized fatty acid synthesis in African trypanosomes: Myristate for GPI anchors
    • Morita Y.S., Paul K.S., Englund P.T. Specialized fatty acid synthesis in African trypanosomes: myristate for GPI anchors. Science. 288:2000;140-143.
    • (2000) Science , vol.288 , pp. 140-143
    • Morita, Y.S.1    Paul, K.S.2    Englund, P.T.3
  • 44
    • 0024023720 scopus 로고
    • Metabolism of phospholipids and lysophospholipids by Trypanosoma brucei
    • Samad A., Licht B., Stalmach M.E.et al. Metabolism of phospholipids and lysophospholipids by Trypanosoma brucei. Mol. Biochem. Parasitol. 29:1988;159-169.
    • (1988) Mol. Biochem. Parasitol. , vol.29 , pp. 159-169
    • Samad, A.1    Licht, B.2    Stalmach, M.E.3
  • 45
    • 0000416470 scopus 로고
    • Receptors for the host low density lipoproteins on the hemoflagellate Trypanosoma brucei: Purification and involvement in the growth of the parasite
    • Coppens I., Baudhuin P., Opperdoes F.R.et al. Receptors for the host low density lipoproteins on the hemoflagellate Trypanosoma brucei: purification and involvement in the growth of the parasite. Proc. Natl. Acad Sci. U.S.A. 85:1988;6753-6757.
    • (1988) Proc. Natl. Acad Sci. U.S.A. , vol.85 , pp. 6753-6757
    • Coppens, I.1    Baudhuin, P.2    Opperdoes, F.R.3
  • 46
    • 0031590269 scopus 로고    scopus 로고
    • The surface glycoconjugates of trypanosomatid parasites
    • Ferguson M.A. The surface glycoconjugates of trypanosomatid parasites. Philos. Trans. R Soc. Lond. B Biol. Sci. 352:1997;1295-1302.
    • (1997) Philos. Trans. R Soc. Lond. B Biol. Sci. , vol.352 , pp. 1295-1302
    • Ferguson, M.A.1
  • 47
    • 0033758270 scopus 로고    scopus 로고
    • Ether-lipid (alkyl-phospholipid) metabolism and the mechanism of action of ether-lipid analogues in Leishmania
    • Lux H., Heise N., Klenner T.et al. Ether-lipid (alkyl-phospholipid) metabolism and the mechanism of action of ether-lipid analogues in Leishmania. Mol. Biochem. Parasitol. 111:2000;1-14.
    • (2000) Mol. Biochem. Parasitol. , vol.111 , pp. 1-14
    • Lux, H.1    Heise, N.2    Klenner, T.3
  • 48
    • 0035414280 scopus 로고    scopus 로고
    • Fatty acid synthesis in African trypanosomes: A solution to the myristate mystery
    • Paul K.S., Jiang D., Morita Y.S.et al. Fatty acid synthesis in African trypanosomes: a solution to the myristate mystery. Trends Parasitol. 17:2001;381-387.
    • (2001) Trends Parasitol. , vol.17 , pp. 381-387
    • Paul, K.S.1    Jiang, D.2    Morita, Y.S.3
  • 49
    • 0027263411 scopus 로고
    • Phosphatidylethanolamine is the donor of the terminal phosphoethanolamine group in trypanosome glycosylphosphatidylinositols
    • Menon A.K., Eppinger M., Mayor S.et al. Phosphatidylethanolamine is the donor of the terminal phosphoethanolamine group in trypanosome glycosylphosphatidylinositols. EMBO. J. 12:1993;1907-1914.
    • (1993) EMBO. J. , vol.12 , pp. 1907-1914
    • Menon, A.K.1    Eppinger, M.2    Mayor, S.3
  • 50
    • 0029038304 scopus 로고
    • Specificity of ethanolamine transport and its further metabolism in Trypanosoma brucei
    • Rifkin M.R., Strobos C.A., Fairlamb A.H. Specificity of ethanolamine transport and its further metabolism in Trypanosoma brucei. J. Biol. Chem. 270:1995;16160-16166.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16160-16166
    • Rifkin, M.R.1    Strobos, C.A.2    Fairlamb, A.H.3
  • 51
    • 0030845186 scopus 로고    scopus 로고
    • The dihydroxyacetonephosphate pathway for biosynthesis of ether lipids in Leishmania mexicana promastigotes
    • Heise N., Opperdoes F.R. The dihydroxyacetonephosphate pathway for biosynthesis of ether lipids in Leishmania mexicana promastigotes. Mol. Biochem. Parasitol. 89:1997;61-72.
    • (1997) Mol. Biochem. Parasitol. , vol.89 , pp. 61-72
    • Heise, N.1    Opperdoes, F.R.2
  • 52
    • 0034333236 scopus 로고    scopus 로고
    • Metabolic aspects of glycosomes in trypanosomatidae - New data and views
    • Michels P.A., Hannaert V., Bringaud F. Metabolic aspects of glycosomes in trypanosomatidae - new data and views. Parasitol. Today. 16:2000;482-489.
    • (2000) Parasitol. Today , vol.16 , pp. 482-489
    • Michels, P.A.1    Hannaert, V.2    Bringaud, F.3
  • 53
    • 0034831503 scopus 로고    scopus 로고
    • Transport proteins of Plasmodium falciparum: Defining the limits of metabolism
    • Krishna S., Webb R., Woodrow C. Transport proteins of Plasmodium falciparum: defining the limits of metabolism. Int. J. Parasitol. 31:2001;1331-1342.
    • (2001) Int. J. Parasitol. , vol.31 , pp. 1331-1342
    • Krishna, S.1    Webb, R.2    Woodrow, C.3
  • 54
    • 0345151828 scopus 로고    scopus 로고
    • Toxoplasma gondii resides in a vacuole that avoids fusion with host cell endocytic and exocytic vesicular trafficking pathways
    • Mordue D.G., Hakansson S., Niesman I.et al. Toxoplasma gondii resides in a vacuole that avoids fusion with host cell endocytic and exocytic vesicular trafficking pathways. Exp. Parasitol. 92:1999;87-99.
    • (1999) Exp. Parasitol. , vol.92 , pp. 87-99
    • Mordue, D.G.1    Hakansson, S.2    Niesman, I.3
  • 55
    • 0028201436 scopus 로고
    • Preferential binding of Plasmodium falciparum sera and rhoptry proteins to erythrocyte membrane inner leaflet phospholipids
    • Perkins M.E., Ziefer A. Preferential binding of Plasmodium falciparum sera and rhoptry proteins to erythrocyte membrane inner leaflet phospholipids. Infect. Immun. 62:1994;1207-1212.
    • (1994) Infect. Immun. , vol.62 , pp. 1207-1212
    • Perkins, M.E.1    Ziefer, A.2
  • 56
    • 0030221960 scopus 로고    scopus 로고
    • Rhoptry protein of the Apicomplexa: Their role in host cell invasion and intracellular survival
    • Sam-Yellowe T.Y. Rhoptry protein of the Apicomplexa: their role in host cell invasion and intracellular survival. Parasitol. Today. 12:1996;308-316.
    • (1996) Parasitol. Today , vol.12 , pp. 308-316
    • Sam-Yellowe, T.Y.1
  • 57
    • 0032820595 scopus 로고    scopus 로고
    • The structure, biosynthesis and functions of glycosylphosphatidylinositol anchors, and the contributions of trypanosome research
    • Ferguson M.A. The structure, biosynthesis and functions of glycosylphosphatidylinositol anchors, and the contributions of trypanosome research. J. Cell Sci. 112(17):1999;2799-2809.
    • (1999) J. Cell Sci. , vol.112 , Issue.17 , pp. 2799-2809
    • Ferguson, M.A.1
  • 58
    • 0027398121 scopus 로고
    • The current status of the glycobiology of Toxoplasma gondii: Glycosylphosphatidylinositols. N- and O-linked glycans
    • Schwarz R.T., Tomavo S. The current status of the glycobiology of Toxoplasma gondii: glycosylphosphatidylinositols. N- and O-linked glycans. Res. Immunol. 144:1993;24-31.
    • (1993) Res. Immunol. , vol.144 , pp. 24-31
    • Schwarz, R.T.1    Tomavo, S.2
  • 59
    • 0026802099 scopus 로고
    • Biosynthesis of glycolipid precursors for glycosylphosphatidylinositol membrane anchors in a Toxoplasma gondii cell-free system
    • Tomavo S., Dubremetz J.F., Schwarz R.T. Biosynthesis of glycolipid precursors for glycosylphosphatidylinositol membrane anchors in a Toxoplasma gondii cell-free system. J. Biol. Chem. 267:1992;21446-21458.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21446-21458
    • Tomavo, S.1    Dubremetz, J.F.2    Schwarz, R.T.3
  • 60
    • 0031557392 scopus 로고    scopus 로고
    • Molecular structure of the low molecular weight antigen of Toxoplasma gondii: A glucose alpha 1-4-N-acetylgalactosamine makes free glycosyl-phosphatidylinositols highly immunogenic
    • Striepen B., Zinecker C.F., Damm J.B.et al. Molecular structure of the low molecular weight antigen of Toxoplasma gondii: a glucose alpha 1-4-N-acetylgalactosamine makes free glycosyl-phosphatidylinositols highly immunogenic. J. Mol. Biol. 266:1997;797-813.
    • (1997) J. Mol. Biol. , vol.266 , pp. 797-813
    • Striepen, B.1    Zinecker, C.F.2    Damm, J.B.3
  • 61
    • 12944309894 scopus 로고    scopus 로고
    • Critical roles of glycosylphosphatidylinositol for Trypanosoma brucei
    • Nagamune K., Nozaki T., Maeda Y.et al. Critical roles of glycosylphosphatidylinositol for Trypanosoma brucei. Proc. Natl. Acad Sci. U.S.A. 97:2000;10336-10341.
    • (2000) Proc. Natl. Acad Sci. U.S.A. , vol.97 , pp. 10336-10341
    • Nagamune, K.1    Nozaki, T.2    Maeda, Y.3
  • 62
    • 0025350498 scopus 로고
    • Fatty acid remodeling: A novel reaction sequence in the biosynthesis of trypanosome glycosyl phosphatidylinositol membrane anchors
    • Masterson W.J., Raper J., Doering T.L.et al. Fatty acid remodeling: a novel reaction sequence in the biosynthesis of trypanosome glycosyl phosphatidylinositol membrane anchors. Cell. 62:1990;73-80.
    • (1990) Cell , vol.62 , pp. 73-80
    • Masterson, W.J.1    Raper, J.2    Doering, T.L.3
  • 63
    • 0034091742 scopus 로고    scopus 로고
    • Recent developments in the cell biology and biochemistry of glycosylphosphatidylinositol lipids (review)
    • McConville M.J., Menon A.K. Recent developments in the cell biology and biochemistry of glycosylphosphatidylinositol lipids (review). Mol. Membr. Biol. 17:2000;1-16.
    • (2000) Mol. Membr. Biol. , vol.17 , pp. 1-16
    • McConville, M.J.1    Menon, A.K.2
  • 64
    • 0028851494 scopus 로고
    • Toxoplasma gondii: Redistribution of tachyzoite surface protein during host cell invasion and intracellular development
    • Grimwood J., Smith J.E. Toxoplasma gondii: redistribution of tachyzoite surface protein during host cell invasion and intracellular development. Parasitol. Res. 81:1995;657-661.
    • (1995) Parasitol. Res. , vol.81 , pp. 657-661
    • Grimwood, J.1    Smith, J.E.2
  • 65
    • 0030069954 scopus 로고    scopus 로고
    • Toxoplasma gondii: The role of parasite surface and secreted proteins in host cell invasion
    • Grimwood J., Smith J.E. Toxoplasma gondii: the role of parasite surface and secreted proteins in host cell invasion. Int. J. Parasitol. 26:1996;169-173.
    • (1996) Int. J. Parasitol. , vol.26 , pp. 169-173
    • Grimwood, J.1    Smith, J.E.2
  • 66
    • 0034845272 scopus 로고    scopus 로고
    • Glycobiology of Plasmodium falciparum
    • Davidson E.A., Gowda D.C. Glycobiology of Plasmodium falciparum. Biochimie. 83:2001;601-604.
    • (2001) Biochimie , vol.83 , pp. 601-604
    • Davidson, E.A.1    Gowda, D.C.2
  • 67
    • 0032785077 scopus 로고    scopus 로고
    • Specificity in signal transduction among glycosylphosphatidylinositols of Plasmodium falciparum, Trypanosoma brucei, Trypanosoma cruzi and Leishmania spp.
    • Tachado S.D., Mazhari-Tabrizi R., Schofield L. Specificity in signal transduction among glycosylphosphatidylinositols of Plasmodium falciparum, Trypanosoma brucei, Trypanosoma cruzi and Leishmania spp. Parasite Immunol. 21:1999;609-617.
    • (1999) Parasite Immunol. , vol.21 , pp. 609-617
    • Tachado, S.D.1    Mazhari-Tabrizi, R.2    Schofield, L.3
  • 68
    • 0032888453 scopus 로고    scopus 로고
    • Conservation of structure among glycosylphosphatidylinositol toxins from different geographic isolates of Plasmodium falciparum
    • Berhe S., Schofield L., Schwarz R.T.et al. Conservation of structure among glycosylphosphatidylinositol toxins from different geographic isolates of Plasmodium falciparum. Mol. Biochem. Parasitol. 103:1999;273-278.
    • (1999) Mol. Biochem. Parasitol. , vol.103 , pp. 273-278
    • Berhe, S.1    Schofield, L.2    Schwarz, R.T.3
  • 69
    • 0030932207 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol anchors represents the major carbohydrate modifications in proteins of intraerythrocytic stage Plasmodium falciparum
    • Gowda D., Gupta P., Davidson E. Glycosylphosphatidylinositol anchors represents the major carbohydrate modifications in proteins of intraerythrocytic stage Plasmodium falciparum. J. Biol. Chem. 272:1997;6428-6439.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6428-6439
    • Gowda, D.1    Gupta, P.2    Davidson, E.3
  • 70
    • 0037102205 scopus 로고    scopus 로고
    • Synthetic GPI as a candidate anti-toxic vaccine in a model of malaria
    • Schofield L., Hewitt M.C., Evans K.et al. Synthetic GPI as a candidate anti-toxic vaccine in a model of malaria. Nature. 418:2002;785-789.
    • (2002) Nature , vol.418 , pp. 785-789
    • Schofield, L.1    Hewitt, M.C.2    Evans, K.3
  • 71
    • 0031879934 scopus 로고    scopus 로고
    • Plasmodium falciparum: Asexual erythrocytic stages synthesize two structurally distinct free and protein-bound glycosylphosphatidylinositols in a maturation-dependent manner
    • Schmidt A., Schwarz R.T., Gerold P. Plasmodium falciparum: asexual erythrocytic stages synthesize two structurally distinct free and protein-bound glycosylphosphatidylinositols in a maturation-dependent manner. Exp. Parasitol. 88:1998;95-102.
    • (1998) Exp. Parasitol. , vol.88 , pp. 95-102
    • Schmidt, A.1    Schwarz, R.T.2    Gerold, P.3
  • 72
    • 0035862702 scopus 로고    scopus 로고
    • Biosynthesis of glycosphingolipids de-novo by the human malaria parasite Plasmodium falciparum
    • Gerold P., Schwarz R.T. Biosynthesis of glycosphingolipids de-novo by the human malaria parasite Plasmodium falciparum. Mol. Biochem. Parasitol. 112:2001;29-37.
    • (2001) Mol. Biochem. Parasitol. , vol.112 , pp. 29-37
    • Gerold, P.1    Schwarz, R.T.2
  • 73
    • 0036223798 scopus 로고    scopus 로고
    • Evidence for de novo sphingolipid biosynthesis in Toxoplasma gondii
    • Azzouz N., Rauscher B., Gerold P.et al. Evidence for de novo sphingolipid biosynthesis in Toxoplasma gondii. Int. J. Parasitol. 32:2002;677-684.
    • (2002) Int. J. Parasitol. , vol.32 , pp. 677-684
    • Azzouz, N.1    Rauscher, B.2    Gerold, P.3
  • 74
    • 0028265959 scopus 로고
    • Lipid Second Messengers
    • Liscovitch M., Cantley L.C. Lipid Second Messengers. Cell. 77:1994;329-334.
    • (1994) Cell , vol.77 , pp. 329-334
    • Liscovitch, M.1    Cantley, L.C.2
  • 76
    • 0028266741 scopus 로고
    • Characterization of phosphatidylinositol synthase and evidence of a polyphosphoinositide cycle in Plasmodium-infected erythrocytes
    • Elabbadi N., Ancelin M.L., Vial H.J. Characterization of phosphatidylinositol synthase and evidence of a polyphosphoinositide cycle in Plasmodium-infected erythrocytes. Mol. Biochem. Parasitol. 63:1994;179-192.
    • (1994) Mol. Biochem. Parasitol. , vol.63 , pp. 179-192
    • Elabbadi, N.1    Ancelin, M.L.2    Vial, H.J.3
  • 77
    • 0026659202 scopus 로고
    • Inositol phosphate biochemistry
    • Majerus P.W. Inositol phosphate biochemistry. Annu. Rev. Biochem. 61:1992;225-250.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 225-250
    • Majerus, P.W.1
  • 78
    • 0027397544 scopus 로고
    • Inositol trisphosphate and calcium signalling
    • Berridge M.J. Inositol trisphosphate and calcium signalling. Nature. 361:1993;315-325.
    • (1993) Nature , vol.361 , pp. 315-325
    • Berridge, M.J.1
  • 79
    • 0030839074 scopus 로고    scopus 로고
    • Signal transduction in malaria parasites
    • Doerig C.D. Signal transduction in malaria parasites. Parasitol. Today. 13:1997;307-313.
    • (1997) Parasitol. Today , vol.13 , pp. 307-313
    • Doerig, C.D.1
  • 80
    • 0031028333 scopus 로고    scopus 로고
    • Modulation of protein kinase C activity in Plasmodium falciparum-infected erythrocytes
    • Belinda S., Daramola O., Bargen G.et al. Modulation of protein kinase C activity in Plasmodium falciparum-infected erythrocytes. Blood. 89:1997;1770-1778.
    • (1997) Blood , vol.89 , pp. 1770-1778
    • Belinda, S.1    Daramola, O.2    Bargen, G.3
  • 81
    • 0028260815 scopus 로고
    • Correlation of phosphoinositide hydrolysis with exflagellation in the malaria microgametocyte
    • Martin S.K., Jett M., Schneider I. Correlation of phosphoinositide hydrolysis with exflagellation in the malaria microgametocyte. J. Parasitol. 80:1994;371-378.
    • (1994) J. Parasitol. , vol.80 , pp. 371-378
    • Martin, S.K.1    Jett, M.2    Schneider, I.3
  • 82
    • 0027208793 scopus 로고
    • Factors affecting exflagellation of in vitro cultivated Plasmodium-falciparum gametocytes
    • Ogwang R.A., Mwangi J.K., Githure J.et al. Factors affecting exflagellation of in vitro cultivated Plasmodium-falciparum gametocytes. Am. J. Trop. Med. Hyg. 49:1993;25-29.
    • (1993) Am. J. Trop. Med. Hyg. , vol.49 , pp. 25-29
    • Ogwang, R.A.1    Mwangi, J.K.2    Githure, J.3
  • 83
    • 0024727456 scopus 로고
    • Plasmodium falciparum gametocyte formation in vitro: Its stimulation by phorbol diesters and by 8-bromo cyclic adenosine monophosphate
    • Trager W., Gill G.S. Plasmodium falciparum gametocyte formation in vitro: its stimulation by phorbol diesters and by 8-bromo cyclic adenosine monophosphate. J. Protozool. 36:1989;451-454.
    • (1989) J. Protozool. , vol.36 , pp. 451-454
    • Trager, W.1    Gill, G.S.2
  • 84
    • 0032799784 scopus 로고    scopus 로고
    • Phospholipid signalling pathways in Trypanosoma cruzi growth control
    • Malaquias A.T., Oliveira M.M. Phospholipid signalling pathways in Trypanosoma cruzi growth control. Acta Trop. 73:1999;93-108.
    • (1999) Acta Trop. , vol.73 , pp. 93-108
    • Malaquias, A.T.1    Oliveira, M.M.2
  • 85
    • 0032535425 scopus 로고    scopus 로고
    • Calcium entry in Trypanosoma brucei is regulated by phospholipase A2 and arachidonic acid
    • Eintracht J., Maathai R., Mellors A.et al. Calcium entry in Trypanosoma brucei is regulated by phospholipase A2 and arachidonic acid. Biochem. J. 336:1998;659-666.
    • (1998) Biochem. J. , vol.336 , pp. 659-666
    • Eintracht, J.1    Maathai, R.2    Mellors, A.3
  • 86
    • 0033958832 scopus 로고    scopus 로고
    • Calcium mobilization by arachidonic acid in trypanosomatids
    • Catisti R., Uyemura S.A., Docampo R.et al. Calcium mobilization by arachidonic acid in trypanosomatids. Mol. Biochem. Parasitol. 105:2000;261-271.
    • (2000) Mol. Biochem. Parasitol. , vol.105 , pp. 261-271
    • Catisti, R.1    Uyemura, S.A.2    Docampo, R.3
  • 87
    • 0032519825 scopus 로고    scopus 로고
    • Antimalarial activity of 77 phospholipid polar head analogs: Close correlation between inhibition of phospholipid metabolism and in vitro Plasmodium falciparum growth
    • Ancelin M.L., Calas M., Bompart J.et al. Antimalarial activity of 77 phospholipid polar head analogs: close correlation between inhibition of phospholipid metabolism and in vitro Plasmodium falciparum growth. Blood. 91:1998;1426-1437.
    • (1998) Blood , vol.91 , pp. 1426-1437
    • Ancelin, M.L.1    Calas, M.2    Bompart, J.3
  • 88
    • 0030725087 scopus 로고    scopus 로고
    • Antimalarial activity of molecules interfering with Plasmodium falciparum phospholipid metabolism. Structure-activity relationship analysis
    • Calas M., Cordina G., Bompart J.et al. Antimalarial activity of molecules interfering with Plasmodium falciparum phospholipid metabolism. Structure-activity relationship analysis. J. Med. Chem. 40:1997;3557-3566.
    • (1997) J. Med. Chem. , vol.40 , pp. 3557-3566
    • Calas, M.1    Cordina, G.2    Bompart, J.3
  • 89
    • 0034628578 scopus 로고    scopus 로고
    • Antimalarial activity of compounds interfering with Plasmodium falciparum phospholipid metabolism: Comparison between mono- and bi-squaternary ammonium salts
    • Calas M., Ancelin M.L., Cordina G.et al. Antimalarial activity of compounds interfering with Plasmodium falciparum phospholipid metabolism: comparison between mono- and bi-squaternary ammonium salts. J. Med. Chem. 43:2000;505-516.
    • (2000) J. Med. Chem. , vol.43 , pp. 505-516
    • Calas, M.1    Ancelin, M.L.2    Cordina, G.3
  • 90
    • 0037083529 scopus 로고    scopus 로고
    • A class of potent antimalarials and their specific accumulation in infected erythrocytes
    • Wengelnik K., Vidal V., Ancelin M.L.et al. A class of potent antimalarials and their specific accumulation in infected erythrocytes. Science. 295:2002;1311-1314.
    • (2002) Science , vol.295 , pp. 1311-1314
    • Wengelnik, K.1    Vidal, V.2    Ancelin, M.L.3
  • 93
    • 0033178777 scopus 로고    scopus 로고
    • Origin, targeting, and function of the apicomplexan plastid
    • Roos D.S., Crawford M.J., Donald R.G.et al. Origin, 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.S.1    Crawford, M.J.2    Donald, R.G.3
  • 94
    • 0036307786 scopus 로고    scopus 로고
    • Progress with parasite plastids
    • Wilson R.J.M. Progress with parasite plastids. J. Mol. Biol. 319:2002;257-274.
    • (2002) J. Mol. Biol. , vol.319 , pp. 257-274
    • Wilson, R.J.M.1
  • 95
    • 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.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    Keeling, P.J.2    Donald, R.G.3
  • 96
    • 0034804919 scopus 로고    scopus 로고
    • Lipid biosynthesis as a target for antibacterial agents
    • Heath R.J., White S.W., Rock C.O. Lipid biosynthesis as a target for antibacterial agents. Prog. Lipid. Res. 40:2001;467-497.
    • (2001) Prog. Lipid. Res. , vol.40 , pp. 467-497
    • Heath, R.J.1    White, S.W.2    Rock, C.O.3
  • 97
    • 18644368430 scopus 로고    scopus 로고
    • Functional characterization of the acyl carrier protein (PfACP) and beta-ketoacyl ACP synthase III (PfKASIII) from Plasmodium falciparum
    • In Press
    • Waters NC, Kopydlowski KM, Guszczynski T, et al. Functional characterization of the acyl carrier protein (PfACP) and beta-ketoacyl ACP synthase III (PfKASIII) from Plasmodium falciparum. Mol Biochem Parasitol 2002; In Press.
    • (2002) Mol Biochem Parasitol
    • Waters, N.C.1    Kopydlowski, K.M.2    Guszczynski, T.3
  • 98
    • 0033539685 scopus 로고    scopus 로고
    • Growth of Toxoplasma gondii is inhibited by arylphenoxypropionate herbicides targeting acetyl-CoA carboxylase
    • Zuther E., Johnson J., Haselkorn R.et al. Growth of Toxoplasma gondii is inhibited by arylphenoxypropionate herbicides targeting acetyl-CoA carboxylase. Proc. Natl. Acad. Sci. U.S.A. 96:1999;13387-13392.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 13387-13392
    • Zuther, E.1    Johnson, J.2    Haselkorn, R.3
  • 99
    • 0035956937 scopus 로고    scopus 로고
    • Subcellular localization of acetyl-CoA carboxylase in the apicomplexan parasite Toxoplasma gondii
    • Jelenska J., Crawford M.J., Harb O.S.et al. Subcellular localization of acetyl-CoA carboxylase in the apicomplexan parasite Toxoplasma gondii. Proc. Natl. Acad Sci. U.S.A. 98:2001;2723-2728.
    • (2001) Proc. Natl. Acad Sci. U.S.A. , vol.98 , pp. 2723-2728
    • Jelenska, J.1    Crawford, M.J.2    Harb, O.S.3
  • 101
    • 0035126479 scopus 로고    scopus 로고
    • Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum
    • Surolia N., Surolia A. Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum. Nat. Med. 7:2001;167-173.
    • (2001) Nat. Med. , vol.7 , pp. 167-173
    • Surolia, N.1    Surolia, A.2
  • 102
    • 0035119443 scopus 로고    scopus 로고
    • Triclosan inhibits the growth of Plasmodium falciparum and Toxoplasma gondii by inhibition of Apicomplexan Fab I
    • McLeod R., Muench S.P., Rafferty J.B.et al. Triclosan inhibits the growth of Plasmodium falciparum and Toxoplasma gondii by inhibition of Apicomplexan Fab I. Int. J. Parasitol. 31:2001;109-113.
    • (2001) Int. J. Parasitol. , vol.31 , pp. 109-113
    • McLeod, R.1    Muench, S.P.2    Rafferty, J.B.3
  • 103
    • 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
  • 104
    • 0032815207 scopus 로고    scopus 로고
    • Apicomplexan plastids as drug targets
    • McFadden G.I., Roos D.S. Apicomplexan plastids as drug targets. Trends Microbiol. 7:1999;328-333.
    • (1999) Trends Microbiol. , vol.7 , pp. 328-333
    • McFadden, G.I.1    Roos, D.S.2
  • 105
    • 0033119057 scopus 로고    scopus 로고
    • Molecular basis of triclosan activity
    • Levy C.W., Roujeinikova A., Sedelnikova S.et al. Molecular basis of triclosan activity. Nature. 398:1999;383-384.
    • (1999) Nature , vol.398 , pp. 383-384
    • Levy, C.W.1    Roujeinikova, A.2    Sedelnikova, S.3
  • 106
    • 0037066782 scopus 로고    scopus 로고
    • Structural elucidation of the specificity of the antibacterial agent triclosan for malarial enoyl acyl carrier protein reductase
    • Perozzo R., Kuo M., Sidhu A.b.S.et al. Structural elucidation of the specificity of the antibacterial agent triclosan for malarial enoyl acyl carrier protein reductase. J. Biol. Chem. 277:2002;13106-13114.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13106-13114
    • Perozzo, R.1    Kuo, M.2    Sidhu, A.B.S.3
  • 107
    • 0034283869 scopus 로고    scopus 로고
    • Serum factors governing intraerythrocytic development and cell cycle progression of Plasmodium falciparum
    • Mitamura T., Hanada K., Ko-Mitamura E.P.et al. Serum factors governing intraerythrocytic development and cell cycle progression of Plasmodium falciparum. Parasitol. Int. 49:2000;219-229.
    • (2000) Parasitol. Int. , vol.49 , pp. 219-229
    • Mitamura, T.1    Hanada, K.2    Ko-Mitamura, E.P.3
  • 108
    • 0033977411 scopus 로고    scopus 로고
    • Molecular analysis of a Type I fatty acid synthase in Cryptosporidium parvum
    • Zhu G., Marchewka M.J., Woods K.M.et al. Molecular analysis of a Type I fatty acid synthase in Cryptosporidium parvum. Mol. Biochem. Parasitol. 105:2000;253-260.
    • (2000) Mol. Biochem. Parasitol. , vol.105 , pp. 253-260
    • Zhu, G.1    Marchewka, M.J.2    Woods, K.M.3
  • 109
    • 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. 285:1999;1573-1576.
    • (1999) Science , vol.285 , pp. 1573-1576
    • Jomaa, H.1    Wiesner, J.2    Sanderbrand, S.3
  • 110
    • 0030921232 scopus 로고    scopus 로고
    • Lipid biosynthesis pathways as chemotherapeutic targets in kinetoplastid parasites
    • Urbina J.A. Lipid biosynthesis pathways as chemotherapeutic targets in kinetoplastid parasites. Parasitology. 114(Suppl):1997;S91-9.
    • (1997) Parasitology , vol.114 , Issue.SUPPL. , pp. 91-99
    • Urbina, J.A.1
  • 111
    • 0034718454 scopus 로고    scopus 로고
    • Parasite-specific inhibition of the glycosylphosphatidylinositol biosynthetic pathway by stereoisomeric substrate analogues
    • Smith T.K., Paterson M.J., Crossman A.et al. Parasite-specific inhibition of the glycosylphosphatidylinositol biosynthetic pathway by stereoisomeric substrate analogues. Biochemistry (Mosc.). 39:2000;11801-11807.
    • (2000) Biochemistry (Mosc.) , vol.39 , pp. 11801-11807
    • Smith, T.K.1    Paterson, M.J.2    Crossman, A.3
  • 112
    • 0035796558 scopus 로고    scopus 로고
    • Specificity of GlcNAc-PI de-N-acetylase of GPI biosynthesis and synthesis of parasite-specific suicide substrate inhibitors
    • Smith T.K., Crossman A., Borissow C.N.et al. Specificity of GlcNAc-PI de-N-acetylase of GPI biosynthesis and synthesis of parasite-specific suicide substrate inhibitors. EMBO J. 20:2001;3322-3332.
    • (2001) EMBO J. , vol.20 , pp. 3322-3332
    • Smith, T.K.1    Crossman, A.2    Borissow, C.N.3
  • 113
    • 0031889889 scopus 로고    scopus 로고
    • Host cell invasion by Toxoplasma gondii
    • Dubremetz J.F. Host cell invasion by Toxoplasma gondii. Trends Microbiol. 6:1998;27-30.
    • (1998) Trends Microbiol. , vol.6 , pp. 27-30
    • Dubremetz, J.F.1
  • 114
    • 0014475076 scopus 로고
    • The fine structure of Trypanosoma congolense in its bloodstream phase
    • Vickerman K. The fine structure of Trypanosoma congolense in its bloodstream phase. J. Protozool. 16:1969;54-69.
    • (1969) J. Protozool. , vol.16 , pp. 54-69
    • Vickerman, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.