메뉴 건너뛰기




Volumn 14, Issue 9, 2008, Pages 822-838

An introduction to the structural organization of parasitic protozoa

Author keywords

Parasitic protozoa; Structural organization

Indexed keywords

ANTIPARASITIC AGENT; ENZYME;

EID: 44349096685     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/138161208784041123     Document Type: Review
Times cited : (18)

References (139)
  • 1
    • 0036451914 scopus 로고    scopus 로고
    • Special organelles of some pathogenic protozoa
    • De Souza W. Special organelles of some pathogenic protozoa. Parasitol Res 2002; 88: 1013-25.
    • (2002) Parasitol Res , vol.88 , pp. 1013-1025
    • De Souza, W.1
  • 2
    • 0029808891 scopus 로고    scopus 로고
    • The secretory pathway of protists: Spatial and functional organization and evolution
    • Becker B, Melknian M. The secretory pathway of protists: Spatial and functional organization and evolution. Microbiol Rev 1996; 60: 697-721.
    • (1996) Microbiol Rev , vol.60 , pp. 697-721
    • Becker, B.1    Melknian, M.2
  • 3
    • 33646817707 scopus 로고    scopus 로고
    • Secretory organelles in parasitic protozoa
    • De Souza W. Secretory organelles in parasitic protozoa. Ann Acad Bras Ciênc 2006; 78: 271-91.
    • (2006) Ann Acad Bras Ciênc , vol.78 , pp. 271-291
    • De Souza, W.1
  • 4
    • 33845907673 scopus 로고    scopus 로고
    • Exploring the role of insect host factors in the dynamic of Trypanosoma cruzi-Rhodnius prolixus interaction
    • Garcia ES, Ratcliffe NA, Whitten MM, Gonzalez MS, Azambuja P. Exploring the role of insect host factors in the dynamic of Trypanosoma cruzi-Rhodnius prolixus interaction. J Insect Physiol 2007, 53: 11-21.
    • (2007) J Insect Physiol , vol.53 , pp. 11-21
    • Garcia, E.S.1    Ratcliffe, N.A.2    Whitten, M.M.3    Gonzalez, M.S.4    Azambuja, P.5
  • 5
    • 0002969784 scopus 로고
    • Components of the cell surface of trypanosomatids
    • De Souza W. Components of the cell surface of trypanosomatids. Prog Protistol 1989; 3: 87-184.
    • (1989) Prog Protistol , vol.3 , pp. 87-184
    • De Souza, W.1
  • 6
    • 0002827648 scopus 로고
    • Lumsden WHR, Evans DE, Eds, Academic Press, New York
    • Vickerman K, Preston TM. In Lumsden WHR, Evans DE, Eds. Biologv of kinetoplastida. Academic Press, New York 1974; p 35-130.
    • (1974) Biologv of kinetoplastida , pp. 35-130
    • Vickerman, K.1    Preston, T.M.2
  • 7
    • 0014804933 scopus 로고    scopus 로고
    • Membrane splitting in freeze-etching. Covalently bound ferritn as a membrane marker
    • Pinto da Silva P, Branton D. Membrane splitting in freeze-etching. Covalently bound ferritn as a membrane marker. J Cell Biol 19-70; 45: 598-605.
    • J Cell Biol 19-70 , vol.45 , pp. 598-605
    • Pinto da Silva, P.1    Branton, D.2
  • 8
    • 0017179299 scopus 로고
    • Topographical defferences in the distribution of surface coat components and intramembrane particles. A cytochemical and freeze-fracture study in culture forms of Trypanosoma cruzi
    • Martinez-Palomo A, De Souza W, Gonzales-Robles A. Topographical defferences in the distribution of surface coat components and intramembrane particles. A cytochemical and freeze-fracture study in culture forms of Trypanosoma cruzi. J Cell Biol 1976; 69: 507-13.
    • (1976) J Cell Biol , vol.69 , pp. 507-513
    • Martinez-Palomo, A.1    De Souza, W.2    Gonzales-Robles, A.3
  • 9
    • 34250760963 scopus 로고    scopus 로고
    • Micro and nanodomains in the membrane of parasitic protozoa
    • De Souza W. Macro, Micro and nanodomains in the membrane of parasitic protozoa. Parasitol Int 2007; 56: 161-70.
    • (2007) Parasitol Int , vol.56 , pp. 161-170
    • Souza, D.1    Macro, W.2
  • 10
    • 0021893210 scopus 로고
    • Distribution of intramembranous particles and filipin sterol complexes in the cell membranes of Toxoplasma gondii
    • Cintra W, De Souza W. Distribution of intramembranous particles and filipin sterol complexes in the cell membranes of Toxoplasma gondii. Eur J Cell Biol 1985; 37: 63-9.
    • (1985) Eur J Cell Biol , vol.37 , pp. 63-69
    • Cintra, W.1    De Souza, W.2
  • 11
    • 0026885313 scopus 로고
    • Surface domains in the pathogenic protozoan Tritrichomonas foetus
    • Benchimol M, Kachar B, De Souza W. Surface domains in the pathogenic protozoan Tritrichomonas foetus. J Protozool 1992; 39: 480-4
    • (1992) J Protozool , vol.39 , pp. 480-484
    • Benchimol, M.1    Kachar, B.2    De Souza, W.3
  • 12
    • 0019859146 scopus 로고
    • Quick-freeze, deep-etch visualization of the cytoskeleton beneath surface differentiations of intestinal epithelial cells
    • Hirokawa N, Heuser JE. Quick-freeze, deep-etch visualization of the cytoskeleton beneath surface differentiations of intestinal epithelial cells. J Cell Biol 1981; 91: 399-409.
    • (1981) J Cell Biol , vol.91 , pp. 399-409
    • Hirokawa, N.1    Heuser, J.E.2
  • 13
    • 0021284702 scopus 로고
    • Quick-freeze, deep-etch, rotary replication of Trypanosoma cruzi and Herpemmonas megaseliae
    • Souto-Padron T, De Souza W, Heuser JE. Quick-freeze, deep-etch, rotary replication of Trypanosoma cruzi and Herpemmonas megaseliae. J Cell Sci 1984; 69: 167-78.
    • (1984) J Cell Sci , vol.69 , pp. 167-178
    • Souto-Padron, T.1    De Souza, W.2    Heuser, J.E.3
  • 14
    • 2442657704 scopus 로고    scopus 로고
    • Biological and ultrastructural effects of the anti-micro tubule agent taxol against Trypanosoma cruzi
    • Dantas AP, Barbosa HS, de Castro S. Biological and ultrastructural effects of the anti-micro tubule agent taxol against Trypanosoma cruzi. J Submicroscop Cytol Pathol 2003; 35: 287-94.
    • (2003) J Submicroscop Cytol Pathol , vol.35 , pp. 287-294
    • Dantas, A.P.1    Barbosa, H.S.2    de Castro, S.3
  • 15
    • 0032915701 scopus 로고    scopus 로고
    • Effect of the anti tubulin drug trifluralin on the proliferation and metecyclogenesis of Trypanosoma cruzi
    • Bogitsh Bi, Middleton OL, Ribeiro Rodrigues R. Effect of the anti tubulin drug trifluralin on the proliferation and metecyclogenesis of Trypanosoma cruzi. Parasitol Res 1999; 85: 475-80.
    • (1999) Parasitol Res , vol.85 , pp. 475-480
    • Bi, B.1    Middleton, O.L.2    Ribeiro Rodrigues, R.3
  • 16
    • 0037128925 scopus 로고    scopus 로고
    • A novel polymer of tubulin forms the conoid of Toxoplasma gondii
    • Hu K, Roos DS, Murray JM. A novel polymer of tubulin forms the conoid of Toxoplasma gondii. J Cell Biol 2002; 156: 1039-50.
    • (2002) J Cell Biol , vol.156 , pp. 1039-1050
    • Hu, K.1    Roos, D.S.2    Murray, J.M.3
  • 17
    • 33846860640 scopus 로고    scopus 로고
    • Pulling together: An integrated model of Toxoplasma cell invasion
    • Carruthers V, Boothrooyd JC. Pulling together: An integrated model of Toxoplasma cell invasion. Curr Op Microbiol 2007; 10: 83-9.
    • (2007) Curr Op Microbiol , vol.10 , pp. 83-89
    • Carruthers, V.1    Boothrooyd, J.C.2
  • 18
    • 0027296307 scopus 로고    scopus 로고
    • The structural organization of the pathogenic protozoan Tritrichomonas foetus as seen in replicas of quick frozen, freeze-fractured and deep etched cells
    • Benchimol M, Kachar B, De Souza W. The structural organization of the pathogenic protozoan Tritrichomonas foetus as seen in replicas of quick frozen, freeze-fractured and deep etched cells. Biol cell 199; 77: 289- 95.
    • Biol cell , vol.199 , Issue.77 , pp. 289-295
    • Benchimol, M.1    Kachar, B.2    De Souza, W.3
  • 19
    • 29344456393 scopus 로고    scopus 로고
    • The cytoskeleton of Entamoeha histolytica; structure, function, and regulation by signaling pathways
    • Meza I, Talamas-Rohana P, Vargas MA. The cytoskeleton of Entamoeha histolytica; structure, function, and regulation by signaling pathways. Arch Med Res 2006; 37: 234-43.
    • (2006) Arch Med Res , vol.37 , pp. 234-243
    • Meza, I.1    Talamas-Rohana, P.2    Vargas, M.A.3
  • 22
    • 2942544987 scopus 로고    scopus 로고
    • Visualization of the funis of Giardia lamblia by high-resolution scanning electron microscopy-new insights
    • Benchimol M, Piva B, Campanati L, De Souza W. Visualization of the funis of Giardia lamblia by high-resolution scanning electron microscopy-new insights. J Struct Biol 2004; 147: 102-15.
    • (2004) J Struct Biol , vol.147 , pp. 102-115
    • Benchimol, M.1    Piva, B.2    Campanati, L.3    De Souza, W.4
  • 23
    • 24344451709 scopus 로고    scopus 로고
    • Improvements on the visulization of cytoskeletal structures of protozoan parasites using high resolution field emission electron microscopy (FESEM)
    • Sant'ana C, Campanati L, Gadelha C, Lourenço D, Labati-Terra L, Bittencourt-Silvestre J, et al. Improvements on the visulization of cytoskeletal structures of protozoan parasites using high resolution field emission electron microscopy (FESEM). Histochem Cell Biol 2005; 124: 87-95.
    • (2005) Histochem Cell Biol , vol.124 , pp. 87-95
    • Sant'ana, C.1    Campanati, L.2    Gadelha, C.3    Lourenço, D.4    Labati-Terra, L.5    Bittencourt-Silvestre, J.6
  • 24
    • 0343081592 scopus 로고    scopus 로고
    • Localization of gamma-tubulin in interphasic and mitotic cells of a unicellular eukariote, Giardia intestinalis
    • Nohynkova E, Dráber P, Reischig J, Kulda J. Localization of gamma-tubulin in interphasic and mitotic cells of a unicellular eukariote, Giardia intestinalis. Eur J Cell Biol 2000; 79: 438-45.
    • (2000) Eur J Cell Biol , vol.79 , pp. 438-445
    • Nohynkova, E.1    Dráber, P.2    Reischig, J.3    Kulda, J.4
  • 25
    • 0022863150 scopus 로고
    • Further studies on the structural organization of the paraxial structure of trypanosomatids
    • Farina M, Attias M, Souto-Padron T, De Souza W. Further studies on the structural organization of the paraxial structure of trypanosomatids. J Protozool 1986; 33: 552-7.
    • (1986) J Protozool , vol.33 , pp. 552-557
    • Farina, M.1    Attias, M.2    Souto-Padron, T.3    De Souza, W.4
  • 26
    • 0032724638 scopus 로고    scopus 로고
    • The cytoskeleton of trypanosomatid parasites
    • Gull K. The cytoskeleton of trypanosomatid parasites. Annu Rev Microbiol 1999, 53: 629-55.
    • (1999) Annu Rev Microbiol , vol.53 , pp. 629-655
    • Gull, K.1
  • 27
    • 0016541064 scopus 로고
    • The chondriome of selected trypanosomatids. A three-dimensional study based on serial sections and high voltage electron microscopy
    • Paulin JJ. The chondriome of selected trypanosomatids. A three-dimensional study based on serial sections and high voltage electron microscopy. J Cell Biol 1975; 66: 404-13.
    • (1975) J Cell Biol , vol.66 , pp. 404-413
    • Paulin, J.J.1
  • 28
    • 0033928205 scopus 로고    scopus 로고
    • The single mitochondria of trophozoites of Toxoplasma gondii
    • Melo EJ, Attias M, De Souza W. The single mitochondria of trophozoites of Toxoplasma gondii. J Struct Biol 2000; 130: 27-33.
    • (2000) J Struct Biol , vol.130 , pp. 27-33
    • Melo, E.J.1    Attias, M.2    De Souza, W.3
  • 29
    • 0034616181 scopus 로고    scopus 로고
    • Specialized fatty acid synthesis in African trypanosomes: Myristate for GPI anchors
    • Morita YS, Paul KS, Englund PT. Specialized fatty acid synthesis in African trypanosomes: Myristate for GPI anchors. Science 2000; 288: 140-3.
    • (2000) Science , vol.288 , pp. 140-143
    • Morita, Y.S.1    Paul, K.S.2    Englund, P.T.3
  • 30
    • 33947414585 scopus 로고    scopus 로고
    • Mitochondrial fatty acid synthesis in Trypanosoma brucei
    • Stephens JL, Lee SH, Paul KS, Englund PT. Mitochondrial fatty acid synthesis in Trypanosoma brucei. J Biol Chem 2007; 282: 4427-36
    • (2007) J Biol Chem , vol.282 , pp. 4427-4436
    • Stephens, J.L.1    Lee, S.H.2    Paul, K.S.3    Englund, P.T.4
  • 31
    • 0014317261 scopus 로고
    • The fine structure of flagellum and kinetoplast-chondriome of Trypanosoma (Schyzotrypanum) cruzi in tissue cultures
    • Meyer H. The fine structure of flagellum and kinetoplast-chondriome of Trypanosoma (Schyzotrypanum) cruzi in tissue cultures. J Protozool 1968; 15: 614-21.
    • (1968) J Protozool , vol.15 , pp. 614-621
    • Meyer, H.1
  • 32
    • 0344945208 scopus 로고
    • Synthesis of deoxyribonucleic acid in the parabasal body of Trypanosoma mega
    • Steinert G, Firket H, Steinert M. Synthesis of deoxyribonucleic acid in the parabasal body of Trypanosoma mega. Exp Cell Res 1968; 15: 632-5.
    • (1968) Exp Cell Res , vol.15 , pp. 632-635
    • Steinert, G.1    Firket, H.2    Steinert, M.3
  • 33
    • 0014353860 scopus 로고
    • Fine structure and replication ot the kinetoplast of Trypanosoma lewisi
    • Burton PR, Dusainc DG. Fine structure and replication ot the kinetoplast of Trypanosoma lewisi. J Cell Biol 1968; 39: 318-31.
    • (1968) J Cell Biol , vol.39 , pp. 318-331
    • Burton, P.R.1    Dusainc, D.G.2
  • 34
    • 0014512842 scopus 로고    scopus 로고
    • Hill GC, Anderson WA. Effects of acriflavine on the mitochondria and kinetoplast of Crithidia fasciculata. Correlation of fine structure changes with decreased mitochondrial enzyme activity. J Cell Biol 1969; 41(2)211: 547-61.
    • Hill GC, Anderson WA. Effects of acriflavine on the mitochondria and kinetoplast of Crithidia fasciculata. Correlation of fine structure changes with decreased mitochondrial enzyme activity. J Cell Biol 1969; 41(2)211: 547-61.
  • 35
    • 0014583706 scopus 로고
    • Abnormal circular DNA molecules induced by ethidium bromide in the kinetoplast of Trypanosoma cruzi
    • Riou G, Delain E. Abnormal circular DNA molecules induced by ethidium bromide in the kinetoplast of Trypanosoma cruzi. Proc Natl Acad Sci USA 1979; 64: 618-25.
    • (1979) Proc Natl Acad Sci USA , vol.64 , pp. 618-625
    • Riou, G.1    Delain, E.2
  • 38
    • 0021315215 scopus 로고
    • Cell Biology of Trypanosoma cruzi
    • De Souza, W. Cell Biology of Trypanosoma cruzi. Int Rev Cytol 1984; 86: 197-283.
    • (1984) Int Rev Cytol , vol.86 , pp. 197-283
    • De Souza, W.1
  • 39
    • 0018087719 scopus 로고
    • Ultrastructual localization of basic proteins in Trypanosoma cruzi
    • Souto-Padrón T, De Souza W. Ultrastructual localization of basic proteins in Trypanosoma cruzi. J Histochem Cytochem 1978: 26: 349-58.
    • (1978) J Histochem Cytochem , vol.26 , pp. 349-358
    • Souto-Padrón, T.1    De Souza, W.2
  • 40
    • 0027499503 scopus 로고
    • Isolation of proteins associated with the kinetoplast-DNA networks in vivo
    • Xu C, Ray DS. Isolation of proteins associated with the kinetoplast-DNA networks in vivo. Proc Natl Acad Sci USA 1993; 90: 1786-9.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 1786-1789
    • Xu, C.1    Ray, D.S.2
  • 42
    • 74049121769 scopus 로고    scopus 로고
    • Isolation and compositional analysis of trypanosomatids editosomes
    • Panigrahi AK, Schnaufer A, Stuart KD. Isolation and compositional analysis of trypanosomatids editosomes. Meth Enzymol 2007; 424: 3-21
    • (2007) Meth Enzymol , vol.424 , pp. 3-21
    • Panigrahi, A.K.1    Schnaufer, A.2    Stuart, K.D.3
  • 45
    • 33747887707 scopus 로고    scopus 로고
    • Mitochondria, hydrogenosomes and mitososmes: Products of evolutionary tinkering
    • Hackstein JH, Tjaden J, Huynen M. Mitochondria, hydrogenosomes and mitososmes: Products of evolutionary tinkering. Curr Genet 2006, 50: 225-45.
    • (2006) Curr Genet , vol.50 , pp. 225-245
    • Hackstein, J.H.1    Tjaden, J.2    Huynen, M.3
  • 46
    • 0002294537 scopus 로고    scopus 로고
    • The hydrogenosome
    • Benchimol M. The hydrogenosome. Acta Microsc 1999; 8: 1-22.
    • (1999) Acta Microsc , vol.8 , pp. 1-22
    • Benchimol, M.1
  • 48
    • 34547919212 scopus 로고    scopus 로고
    • Flataxin, a conserved mitochondrial protein in the hydrogenosome of Trichomonas vaginalis
    • Dolezal P, Dancis A, Lesuisse E, Sutak R, Hrdy I, Embley TM, et al. Flataxin, a conserved mitochondrial protein in the hydrogenosome of Trichomonas vaginalis. Eukaryot Cell 2007; 6: 1431-8.
    • (2007) Eukaryot Cell , vol.6 , pp. 1431-1438
    • Dolezal, P.1    Dancis, A.2    Lesuisse, E.3    Sutak, R.4    Hrdy, I.5    Embley, T.M.6
  • 50
    • 0344633597 scopus 로고    scopus 로고
    • Mitochondrial remnant organelles of Giardia function in iron-sulphur protein maturation
    • Tovar J, León-Avila G, Sánches LB, Sutak R, Tachezy J, van der Giezen M, et al. Mitochondrial remnant organelles of Giardia function in iron-sulphur protein maturation. Nature 2003; 426: 172-6.
    • (2003) Nature , vol.426 , pp. 172-176
    • Tovar, J.1    León-Avila, G.2    Sánches, L.B.3    Sutak, R.4    Tachezy, J.5    van der Giezen, M.6
  • 51
    • 33750436226 scopus 로고    scopus 로고
    • Microsoporidian mitosomes retain elements of the general mitochondrial targeting system
    • Burri L, Williams BAP, Bursac D, Lithgow T, Keeling PJ. Microsoporidian mitosomes retain elements of the general mitochondrial targeting system. Proc. Natl Acad Sci USA 2006: 103: 15916-20.
    • (2006) Proc. Natl Acad Sci USA , vol.103 , pp. 15916-15920
    • Burri, L.1    Williams, B.A.P.2    Bursac, D.3    Lithgow, T.4    Keeling, P.J.5
  • 52
    • 0032988857 scopus 로고    scopus 로고
    • The mitosome, a novel organelle related to mitochondria in the amitochondrial parasite Entamoeba histolytica
    • Tovar J, Fischer A, Clark CG. The mitosome, a novel organelle related to mitochondria in the amitochondrial parasite Entamoeba histolytica. Mol Microbiol 1999; 32: 1013-21.
    • (1999) Mol Microbiol , vol.32 , pp. 1013-1021
    • Tovar, J.1    Fischer, A.2    Clark, C.G.3
  • 53
    • 0033020661 scopus 로고    scopus 로고
    • Hsp60 is targeted to a cryptic mitochondria-derived organelle crypton) in the microaerophilic protozoan parasite Entamoeba histolytica
    • Mai Z, Ghosh S, Frisardi M, Rosenthal B, Rogers R, Samuelson J. Hsp60 is targeted to a cryptic mitochondria-derived organelle crypton) in the microaerophilic protozoan parasite Entamoeba histolytica. Mol. Cell Biol 1999; 19: 2198-205.
    • (1999) Mol. Cell Biol , vol.19 , pp. 2198-2205
    • Mai, Z.1    Ghosh, S.2    Frisardi, M.3    Rosenthal, B.4    Rogers, R.5    Samuelson, J.6
  • 54
    • 0032499785 scopus 로고    scopus 로고
    • Secondary absence of mitochondria in Giardia lamblia and Trichomonas vaginalis revealed by valyl-tRNA synthetase philogeny
    • Hashimoto T, Sánchez IB, Shirakura T., Muller M, Hasegawa M. Secondary absence of mitochondria in Giardia lamblia and Trichomonas vaginalis revealed by valyl-tRNA synthetase philogeny Proc. Natl Acad Sci USA 1998; 95:6860-5.
    • (1998) Proc. Natl Acad Sci USA , vol.95 , pp. 6860-6865
    • Hashimoto, T.1    Sánchez, I.B.2    Shirakura, T.3    Muller, M.4    Hasegawa, M.5
  • 55
    • 0031892089 scopus 로고    scopus 로고
    • A mitochondria-like chaperonin 60 gene in Giardia lamblia: Evidence that diplomonads once harbored an endosymbiont related to the progenitor mitochondria
    • Roger AJ, Svard SG, Tovar J, Clark CG, Smith MW, Gillin FD, et al. A mitochondria-like chaperonin 60 gene in Giardia lamblia: evidence that diplomonads once harbored an endosymbiont related to the progenitor mitochondria. Proc Natl Acad Sci USA 1998; 95: 229-34.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 229-234
    • Roger, A.J.1    Svard, S.G.2    Tovar, J.3    Clark, C.G.4    Smith, M.W.5    Gillin, F.D.6
  • 56
    • 2642561822 scopus 로고    scopus 로고
    • Isolation and characterization of the mitochondrion-like orgenelle from Blastocystis hominis
    • Nasirudeen AM, Tan KS. Isolation and characterization of the mitochondrion-like orgenelle from Blastocystis hominis. J Microbiol Meth 2004; 58: 101-9.
    • (2004) J Microbiol Meth , vol.58 , pp. 101-109
    • Nasirudeen, A.M.1    Tan, K.S.2
  • 57
    • 0034799296 scopus 로고    scopus 로고
    • Alpha and beta subunits of pyruvate dehydrogenase E1 from the microsporidian Nosema locustae: Mitochondria-derived carbon metabolism in microsporida
    • Fast NM, Keeling PJ. Alpha and beta subunits of pyruvate dehydrogenase E1 from the microsporidian Nosema locustae: Mitochondria-derived carbon metabolism in microsporida. Mol Biochem Parasitol 2001; 117: 201-9.
    • (2001) Mol Biochem Parasitol , vol.117 , pp. 201-209
    • Fast, N.M.1    Keeling, P.J.2
  • 58
    • 13144251194 scopus 로고    scopus 로고
    • A mitochondrial Hsp70 ortologue in Vairimorpha necatrix: Molecular evidence that microsporida once contained mitochondria
    • Hirt RP, Heuly B, Vossbrinck CR, Canning EU, Embley TM. A mitochondrial Hsp70 ortologue in Vairimorpha necatrix: Molecular evidence that microsporida once contained mitochondria. Curr Biol 1997; 7: 995-8.
    • (1997) Curr Biol , vol.7 , pp. 995-998
    • Hirt, R.P.1    Heuly, B.2    Vossbrinck, C.R.3    Canning, E.U.4    Embley, T.M.5
  • 59
    • 0037158721 scopus 로고    scopus 로고
    • A mitochondria remnant in the microsporida Trachipelistophora hominis
    • Williams BAP, Hirt RP, Lucocq JM, Embley TM. A mitochondria remnant in the microsporida Trachipelistophora hominis. Nature 2002; 418: 865-9.
    • (2002) Nature , vol.418 , pp. 865-869
    • Williams, B.A.P.1    Hirt, R.P.2    Lucocq, J.M.3    Embley, T.M.4
  • 61
    • 33846840372 scopus 로고    scopus 로고
    • Protein targeting in parasites with cryptoc mitochondria
    • Burri, L, Keeling PJ. Protein targeting in parasites with cryptoc mitochondria. Int J Parasitol 2007: 37: 265-72.
    • (2007) Int J Parasitol , vol.37 , pp. 265-272
    • Burri, L.1    Keeling, P.J.2
  • 62
    • 0036260395 scopus 로고    scopus 로고
    • The primitive microaerophile Giardia intestinalis (syn., lamblia, duodenalis) has specialized membranes with electron transport and membrane-potential generating functions
    • Lloyd D, Harris JC, Maroulis S, Wadley R, Ralphs JR, Hann AC, et al. The primitive microaerophile Giardia intestinalis (syn., lamblia, duodenalis) has specialized membranes with electron transport and membrane-potential generating functions. Microbiology 2002; 148: 1349-54.
    • (2002) Microbiology , vol.148 , pp. 1349-1354
    • Lloyd, D.1    Harris, J.C.2    Maroulis, S.3    Wadley, R.4    Ralphs, J.R.5    Hann, A.C.6
  • 66
    • 0024402191 scopus 로고
    • Sequences similar to genes for two mitochondrial proteins and portions of ribosomal RNA in tandemly arrayed 6-kilobase-pair DNA of a malarial parasite
    • Vaidya R, Akella R, Suplick K. Sequences similar to genes for two mitochondrial proteins and portions of ribosomal RNA in tandemly arrayed 6-kilobase-pair DNA of a malarial parasite. Mol Biochem Parasitol 1989; 35: 97-107.
    • (1989) Mol Biochem Parasitol , vol.35 , pp. 97-107
    • Vaidya, R.1    Akella, R.2    Suplick, K.3
  • 67
    • 0024458833 scopus 로고
    • Characterization of a conserved extrachromosomal element isolated from the avian malarial parasite Plasmodium gallinaceum
    • Joseph JT, Adrift SM, Unnasch T, Puijalon O, Wirth DF. Characterization of a conserved extrachromosomal element isolated from the avian malarial parasite Plasmodium gallinaceum. Mol. Cell Biol 1989; 9: 3621-9.
    • (1989) Mol. Cell Biol , vol.9 , pp. 3621-3629
    • Joseph, J.T.1    Adrift, S.M.2    Unnasch, T.3    Puijalon, O.4    Wirth, D.F.5
  • 68
    • 0028090066 scopus 로고
    • The extrachromosomal DNAs of apicomplexa parasites
    • Feagin JE. The extrachromosomal DNAs of apicomplexa parasites. Ann Rev Microbiol 1994; 48: 81-104.
    • (1994) Ann Rev Microbiol , vol.48 , pp. 81-104
    • Feagin, J.E.1
  • 71
    • 33746306514 scopus 로고    scopus 로고
    • Evidence for Golgi-independent transport from the early secretory pathway to the plastid in malaria parasites
    • Tonkin CJ, Struck NS, Mullin KA, Stimmler LM, McFadden GI. Evidence for Golgi-independent transport from the early secretory pathway to the plastid in malaria parasites. Mol Microbiol 2006: 61: 614-30.
    • (2006) Mol Microbiol , vol.61 , pp. 614-630
    • Tonkin, C.J.1    Struck, N.S.2    Mullin, K.A.3    Stimmler, L.M.4    McFadden, G.I.5
  • 72
    • 33746284200 scopus 로고    scopus 로고
    • Protein targeting to destinations for the secretory pathway in the malaria parasite Plasmodium falciparum
    • Tonkin CJ, Pearce JA, McFadden GL, Cowman AF. Protein targeting to destinations for the secretory pathway in the malaria parasite Plasmodium falciparum. Curr. Op. Microbiol 2006; 9: 381-7.
    • (2006) Curr. Op. Microbiol , vol.9 , pp. 381-387
    • Tonkin, C.J.1    Pearce, J.A.2    McFadden, G.L.3    Cowman, A.F.4
  • 73
    • 0033520336 scopus 로고    scopus 로고
    • Inhibitors of the nonmevalonate pathway of isoprenoid biosyntheis as antimalarial parasites
    • Jomaa H, Wiesner J, Sanderbrand S, Altincicek B, Weidemeyer C, Hintz M, et al. Inhibitors of the nonmevalonate pathway of isoprenoid biosyntheis as antimalarial parasites. Science 1999; 285: 1573-6.
    • (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
  • 74
    • 0032815207 scopus 로고    scopus 로고
    • Apicomplexa plastids as drug targets
    • McFadden GL, Roos DS. Apicomplexa plastids as drug targets. Trends Microbiol 1999; 7: 328-33.
    • (1999) Trends Microbiol , vol.7 , pp. 328-333
    • McFadden, G.L.1    Roos, D.S.2
  • 75
    • 0036230756 scopus 로고    scopus 로고
    • The genome of Plasmodium falciparum encodes an active delta-aminolevulinic acid dehydratase
    • Sato S, Wilson RJ. The genome of Plasmodium falciparum encodes an active delta-aminolevulinic acid dehydratase. Curr Genet 2000; 40: 391-8.
    • (2000) Curr Genet , vol.40 , pp. 391-398
    • Sato, S.1    Wilson, R.J.2
  • 76
    • 1342325384 scopus 로고    scopus 로고
    • Delta aminolevulinic acid dehydratase from Plasmodium falciparum: Indigenous versus imported
    • Danasekaran S, Chandra NR, Sagar KC, Rangarajan PN, Padmanaban G. Delta aminolevulinic acid dehydratase from Plasmodium falciparum: indigenous versus imported. J Biol Chem 2004; 279: 6934-42.
    • (2004) J Biol Chem , vol.279 , pp. 6934-6942
    • Danasekaran, S.1    Chandra, N.R.2    Sagar, K.C.3    Rangarajan, P.N.4    Padmanaban, G.5
  • 79
    • 0017652927 scopus 로고
    • Recent ultrastructural studies on trypanosomes
    • Vickerman K, Tetley L. Recent ultrastructural studies on trypanosomes. Ann Soc Belge Med Trop 1977; 57: 441-57.
    • (1977) Ann Soc Belge Med Trop , vol.57 , pp. 441-457
    • Vickerman, K.1    Tetley, L.2
  • 80
    • 0020039499 scopus 로고
    • Fine structure and cytochemistry of peroxisomes (microbodies) in Leptomonas samueli
    • Souto-Padron T, De Souza W. Fine structure and cytochemistry of peroxisomes (microbodies) in Leptomonas samueli. Cell Tiss Res 1982; 22: 153-8.
    • (1982) Cell Tiss Res , vol.22 , pp. 153-158
    • Souto-Padron, T.1    De Souza, W.2
  • 81
    • 33947221526 scopus 로고    scopus 로고
    • Metabolism of Leishmania: Proven and predicted
    • Opperdoes FR, Coombs GH. Metabolism of Leishmania: Proven and predicted. Trend Parasitol 2007; 23: 149-58.
    • (2007) Trend Parasitol , vol.23 , pp. 149-158
    • Opperdoes, F.R.1    Coombs, G.H.2
  • 82
    • 84986435865 scopus 로고
    • Comparative analysis of the structure of four isolates of trypanosomatids of the genus Phytomonas
    • Attias M, Roitman I, Camargo EP, Dollet M, De Souza W. Comparative analysis of the structure of four isolates of trypanosomatids of the genus Phytomonas. J Protozool 1988; 35: 370-7.
    • (1988) J Protozool , vol.35 , pp. 370-377
    • Attias, M.1    Roitman, I.2    Camargo, E.P.3    Dollet, M.4    De Souza, W.5
  • 83
    • 2542442262 scopus 로고
    • Microbodies in Crithidia fasciculata
    • Muse KE, Roberts JF. Microbodies in Crithidia fasciculata. Protoplasma 1973; 78: 343-8.
    • (1973) Protoplasma , vol.78 , pp. 343-348
    • Muse, K.E.1    Roberts, J.F.2
  • 84
    • 0033983257 scopus 로고    scopus 로고
    • Targeting and subcellular localization of Toxoplasma gondii catalase
    • Kaasch AJ, Joiner KA. Targeting and subcellular localization of Toxoplasma gondii catalase. J. Biol Chem 2000; 275: 1112-8.
    • (2000) J. Biol Chem , vol.275 , pp. 1112-1118
    • Kaasch, A.J.1    Joiner, K.A.2
  • 85
    • 0033890199 scopus 로고    scopus 로고
    • Toxoplasma gondii catalase: Are there peroxisomes in Toxoplasma?
    • Ding M, Clayton C, Soldati D. Toxoplasma gondii catalase: Are there peroxisomes in Toxoplasma? J Cell Sci 2000; 113: 2409-19
    • (2000) J Cell Sci , vol.113 , pp. 2409-2419
    • Ding, M.1    Clayton, C.2    Soldati, D.3
  • 86
    • 0023464501 scopus 로고
    • Compartmentalization of carbohydrate metabolism in trypanosomes
    • Opperdoes FR. Compartmentalization of carbohydrate metabolism in trypanosomes. Annu Rev Microbiol 1987; 41: 127-51.
    • (1987) Annu Rev Microbiol , vol.41 , pp. 127-151
    • Opperdoes, F.R.1
  • 87
    • 0023895045 scopus 로고
    • Cytoplasmic organelles of trypanosomatids: A cytochemical and stereological study
    • Soares MJ, De Souza W. Cytoplasmic organelles of trypanosomatids: A cytochemical and stereological study. J Submicrosc Cytol Pathol 1988; 20: 349-61.
    • (1988) J Submicrosc Cytol Pathol , vol.20 , pp. 349-361
    • Soares, M.J.1    De Souza, W.2
  • 88
    • 0016725645 scopus 로고
    • Quantitative ultrastructural investigation of the life cycle of Trypanosoma brucei: A morphometrical analysis
    • Bohringer S, Hecker H. Quantitative ultrastructural investigation of the life cycle of Trypanosoma brucei: A morphometrical analysis. J Protozool 1975; 22: 463-7.
    • (1975) J Protozool , vol.22 , pp. 463-467
    • Bohringer, S.1    Hecker, H.2
  • 89
    • 0018613060 scopus 로고
    • Cytochemical analysis at the fine structural level of trypanosomatids stained with phosphotungstic acid
    • Souto-Padron T, De Souza W. Cytochemical analysis at the fine structural level of trypanosomatids stained with phosphotungstic acid. J Protozool 1979; 26: 551-5.
    • (1979) J Protozool , vol.26 , pp. 551-555
    • Souto-Padron, T.1    De Souza, W.2
  • 90
    • 85058198883 scopus 로고
    • Involvement of the glycosome of Trypanosoma brucei in carbon dioxide fixation
    • Opperdoes FR, Cottem D. Involvement of the glycosome of Trypanosoma brucei in carbon dioxide fixation. FEBS Lett 1982; 143: 60-4.
    • (1982) FEBS Lett , vol.143 , pp. 60-64
    • Opperdoes, F.R.1    Cottem, D.2
  • 91
    • 0031936186 scopus 로고    scopus 로고
    • Localization and targeting of the Leishmania donovani hypoxanthine-guanine phosphoribosyltransferase to the glycosome
    • Shih S, Hwang H-Y, Carter D, Stenberg P, Ullman B. Localization and targeting of the Leishmania donovani hypoxanthine-guanine phosphoribosyltransferase to the glycosome. J Biol Chem 1998; 273: 1534-41.
    • (1998) J Biol Chem , vol.273 , pp. 1534-1541
    • Shih, S.1    Hwang, H.-Y.2    Carter, D.3    Stenberg, P.4    Ullman, B.5
  • 93
    • 84982335012 scopus 로고
    • Ultrastructure of Trypanosoma lewisi: Flagellum, microtubules and the kinetoplast
    • Anderson WA, Ellis RA. Ultrastructure of Trypanosoma lewisi: flagellum, microtubules and the kinetoplast. J Protozool 1965; 12: 483-9.
    • (1965) J Protozool , vol.12 , pp. 483-489
    • Anderson, W.A.1    Ellis, R.A.2
  • 95
    • 0031594576 scopus 로고    scopus 로고
    • Ca2- content and expression of an acidocalcisomal calcium pump are elevated in intracellular forms of Trypanosoma cruzi
    • Lu H-G, Zhong L, De Souza W, Benchimol M, Moreno SJN, Docampo R. Ca2- content and expression of an acidocalcisomal calcium pump are elevated in intracellular forms of Trypanosoma cruzi. Mol Cell Biol 1998; 18: 2309-23.
    • (1998) Mol Cell Biol , vol.18 , pp. 2309-2323
    • Lu, H.-G.1    Zhong, L.2    De Souza, W.3    Benchimol, M.4    Moreno, S.J.N.5    Docampo, R.6
  • 96
    • 0033835836 scopus 로고    scopus 로고
    • The fine structure of acidocalcisomes in Trypanosoma cruzi
    • Miranda K, Benchimol M, Docampo R, De Souza W. The fine structure of acidocalcisomes in Trypanosoma cruzi. Parasitol Res 2000; 86: 373-84.
    • (2000) Parasitol Res , vol.86 , pp. 373-384
    • Miranda, K.1    Benchimol, M.2    Docampo, R.3    De Souza, W.4
  • 97
    • 0028171327 scopus 로고
    • Ca2-/H+exchange in acidic vacuoles of Trypanosoma brucei
    • Vercesi AE, Moreno SNJ, Docampo R. Ca2-/H+exchange in acidic vacuoles of Trypanosoma brucei. Biochem J 1994; 304: 227-33.
    • (1994) Biochem J , vol.304 , pp. 227-233
    • Vercesi, A.E.1    Moreno, S.N.J.2    Docampo, R.3
  • 98
    • 8844266174 scopus 로고    scopus 로고
    • Intracellular membrane transport systems in Trypanosoma brucei
    • Field, MC, Carrington M. Intracellular membrane transport systems in Trypanosoma brucei. Traffic 2004; 5: 1-9.
    • (2004) Traffic , vol.5 , pp. 1-9
    • Field, M.C.1    Carrington, M.2
  • 100
    • 26844554364 scopus 로고    scopus 로고
    • Trypanosoma brucei: TbRAB4 regulates membrane recycling and expression of surface proteins in procyclic forms
    • Hall BS, Goulding D, Acosta-Serrano A, Field MC. Trypanosoma brucei: TbRAB4 regulates membrane recycling and expression of surface proteins in procyclic forms. Exp Parasitol 2005; 111: 160-71.
    • (2005) Exp Parasitol , vol.111 , pp. 160-171
    • Hall, B.S.1    Goulding, D.2    Acosta-Serrano, A.3    Field, M.C.4
  • 101
    • 0033647396 scopus 로고    scopus 로고
    • Porto-Carreiro I, Attias M, Miranda K, De Souza W, Cunha e Silva NL. Trypanosoma cruzi epimastigotes endocytic pathway: Cargo enters the cytostome and passes through an early endosomal network before reservosome storage. Eur J Cell Biol 2000; 79: 858-69.
    • Porto-Carreiro I, Attias M, Miranda K, De Souza W, Cunha e Silva NL. Trypanosoma cruzi epimastigotes endocytic pathway: Cargo enters the cytostome and passes through an early endosomal network before reservosome storage. Eur J Cell Biol 2000; 79: 858-69.
  • 102
    • 4644292892 scopus 로고    scopus 로고
    • A functional aquaporin co-localizes with the vacuolar proton pyrophosphatase to acidocalcisomes and the contractile vacuole complex of Trypanosoma cruzi
    • Monatalvetti A, Rohloff P, Docampo R. A functional aquaporin co-localizes with the vacuolar proton pyrophosphatase to acidocalcisomes and the contractile vacuole complex of Trypanosoma cruzi. J Biol Chem. 2004; 279: 38673-82.
    • (2004) J Biol Chem , vol.279 , pp. 38673-38682
    • Monatalvetti, A.1    Rohloff, P.2    Docampo, R.3
  • 103
    • 0018101764 scopus 로고
    • Ultrastructural localization of basic proteins on the conoid, rhoptries and micronemes of Toxoplasma gondii
    • De Souza W, Souto-Padron T. Ultrastructural localization of basic proteins on the conoid, rhoptries and micronemes of Toxoplasma gondii. Z Parasitenkd 1978; 56: 123-7.
    • (1978) Z Parasitenkd , vol.56 , pp. 123-127
    • De Souza, W.1    Souto-Padron, T.2
  • 104
    • 0025821664 scopus 로고
    • Localization of lectin-binding sites and sugar-binding proteins in tachyzoites of Toxoplasma gondii
    • Carvalho TU, Souto-Padron T, De Souza W. Localization of lectin-binding sites and sugar-binding proteins in tachyzoites of Toxoplasma gondii. J Parasitol 1991; 77: 156-61.
    • (1991) J Parasitol , vol.77 , pp. 156-161
    • Carvalho, T.U.1    Souto-Padron, T.2    De Souza, W.3
  • 106
    • 0034881397 scopus 로고    scopus 로고
    • The pro region ol Toxoplasma ROPI is a rhoptry-targeting signal
    • Bradley PJ, Boothroyd JC. The pro region ol Toxoplasma ROPI is a rhoptry-targeting signal. Int J Parasitol 2001; 31: 1177-86.
    • (2001) Int J Parasitol , vol.31 , pp. 1177-1186
    • Bradley, P.J.1    Boothroyd, J.C.2
  • 108
    • 0029585902 scopus 로고
    • Toxoplasma gondii: Characterization of a monoclonal antibody recognizing antigens of 36 and 38 kDa with acid phosphatase activity located in dense granules and rhoptries
    • Metsis A, Pettersen E. Toxoplasma gondii: Characterization of a monoclonal antibody recognizing antigens of 36 and 38 kDa with acid phosphatase activity located in dense granules and rhoptries. Exp Parasitol 1995, 81: 472-9.
    • (1995) Exp Parasitol , vol.81 , pp. 472-479
    • Metsis, A.1    Pettersen, E.2
  • 109
    • 0031759012 scopus 로고    scopus 로고
    • Acidic compartments and rhoptry formation in Toxoplasma gondii
    • Shaw MK, Roos DS, Tilney LG. Acidic compartments and rhoptry formation in Toxoplasma gondii, Parasitology 1998; 117: 308-16.
    • (1998) Parasitology , vol.117 , pp. 308-316
    • Shaw, M.K.1    Roos, D.S.2    Tilney, L.G.3
  • 110
    • 3042557931 scopus 로고    scopus 로고
    • Are rhoptries in Apicomplexan parasites secretory granules or secretory lysosomal granules?
    • Ngô HM, Yan M, Joinei K. Are rhoptries in Apicomplexan parasites secretory granules or secretory lysosomal granules? Mol Microbiol 2004; 52: 1531-41.
    • (2004) Mol Microbiol , vol.52 , pp. 1531-1541
    • Ngô, H.M.1    Yan, M.2    Joinei, K.3
  • 111
    • 13844289333 scopus 로고    scopus 로고
    • Identification and disruption of a rhoptry-localized homologue of sodium hydrogen exchangers in Toxoplasma gondii
    • karasov AO, Boothroyd JC, Arrizabalaga G. Identification and disruption of a rhoptry-localized homologue of sodium hydrogen exchangers in Toxoplasma gondii. Int J Parasitol 2005; 35: 285-91.
    • (2005) Int J Parasitol , vol.35 , pp. 285-291
    • karasov, A.O.1    Boothroyd, J.C.2    Arrizabalaga, G.3
  • 112
    • 0034853631 scopus 로고    scopus 로고
    • Apical organelles of Apicomplexa: Biology and isolation by subcellular fractionation
    • Blackman MJ, Bannister LH. Apical organelles of Apicomplexa: Biology and isolation by subcellular fractionation. Mol Biochem Parasitol 2001; 117: 11-25.
    • (2001) Mol Biochem Parasitol , vol.117 , pp. 11-25
    • Blackman, M.J.1    Bannister, L.H.2
  • 113
    • 0030956863 scopus 로고    scopus 로고
    • Sequential protein secretion from three distinct organelles of Toxoplasma gondii accompanies invasion of human fibroblasts
    • Carruthers VB, Sibley LD. Sequential protein secretion from three distinct organelles of Toxoplasma gondii accompanies invasion of human fibroblasts. J Cell Biol 1997; 73: 114-23.
    • (1997) J Cell Biol , vol.73 , pp. 114-123
    • Carruthers, V.B.1    Sibley, L.D.2
  • 114
    • 0025732915 scopus 로고
    • Characterization of the lipid content of Toxoplasma gondii rhoptries
    • Foussard F, Lerici MA, Dubremetz JF. Characterization of the lipid content of Toxoplasma gondii rhoptries. Parasitology 1991; 102: 367-70.
    • (1991) Parasitology , vol.102 , pp. 367-370
    • Foussard, F.1    Lerici, M.A.2    Dubremetz, J.F.3
  • 115
    • 26644451857 scopus 로고    scopus 로고
    • Proteomic analysis of rhoptry organelles reveals many novel constituents for host-parasite interaction in Toxoplasma gondii
    • Bradley PJ, Ward C, Cheng SJ, Alexander DL, Coller S, Coombs GH, et al. Proteomic analysis of rhoptry organelles reveals many novel constituents for host-parasite interaction in Toxoplasma gondii. J Biol Chem 2005; 280: 34245-58.
    • (2005) J Biol Chem , vol.280 , pp. 34245-34258
    • Bradley, P.J.1    Ward, C.2    Cheng, S.J.3    Alexander, D.L.4    Coller, S.5    Coombs, G.H.6
  • 116
    • 0033224351 scopus 로고    scopus 로고
    • Secretion of micronemal proteins is associated with toxoplasma invasion of host cells
    • Carruthers VB, Giddings OK, Sibley LD. Secretion of micronemal proteins is associated with toxoplasma invasion of host cells. Cell Microbiol 1999; 1: 225-35.
    • (1999) Cell Microbiol , vol.1 , pp. 225-235
    • Carruthers, V.B.1    Giddings, O.K.2    Sibley, L.D.3
  • 117
    • 0032927424 scopus 로고    scopus 로고
    • Mobilization of intracellular calcium stimulates microneme discharge in Toxoplasma gondii
    • Carruthers VB, Sibley LD. Mobilization of intracellular calcium stimulates microneme discharge in Toxoplasma gondii. Mol Microbiol 1999; 31: 421-8.
    • (1999) Mol Microbiol , vol.31 , pp. 421-428
    • Carruthers, V.B.1    Sibley, L.D.2
  • 118
    • 0032859858 scopus 로고    scopus 로고
    • Coppens I, Andrews M. Liu JL, Cesbron-Delauw MF Intracellular trafficking of dense granule proteins in Toxoplasma gondii anu experimental evidences for a regulated exocytosis. Eur J Cell Biol 1999; 78: 463-72.
    • Coppens I, Andrews M. Liu JL, Cesbron-Delauw MF Intracellular trafficking of dense granule proteins in Toxoplasma gondii anu experimental evidences for a regulated exocytosis. Eur J Cell Biol 1999; 78: 463-72.
  • 119
    • 0035809213 scopus 로고    scopus 로고
    • Identification and characterization of an escorter for two secretory adhesins in Toxoplasma gondii
    • Reiss M, Viebig N, Brecht S, Formaux MN, Soete M, Di Cristina M, et al. Identification and characterization of an escorter for two secretory adhesins in Toxoplasma gondii. J Cell Biol 2001; 152: 563-78.
    • (2001) J Cell Biol , vol.152 , pp. 563-578
    • Reiss, M.1    Viebig, N.2    Brecht, S.3    Formaux, M.N.4    Soete, M.5    Di Cristina, M.6
  • 120
    • 0141973383 scopus 로고
    • Fluorescent antibody Staining of human malarial parasites
    • Tobie JE, Coatney GR. Fluorescent antibody Staining of human malarial parasites. Exp Parasitol 1961; 11: 128-32.
    • (1961) Exp Parasitol , vol.11 , pp. 128-132
    • Tobie, J.E.1    Coatney, G.R.2
  • 121
    • 0013994219 scopus 로고
    • The fine structure of Plasmodium falciparum and its host erythrocyte in natural malarial infections in man
    • Trager W, Rudzinska MA, Bradbury PC. The fine structure of Plasmodium falciparum and its host erythrocyte in natural malarial infections in man. Bull World Health Organ 1966; 35: 883-5.
    • (1966) Bull World Health Organ , vol.35 , pp. 883-885
    • Trager, W.1    Rudzinska, M.A.2    Bradbury, P.C.3
  • 123
    • 34648827241 scopus 로고    scopus 로고
    • The complex morphology of Maurer's clelts: From discovery to the three-dimensional reconstruction
    • Wickert H. Krohne G. The complex morphology of Maurer's clelts: From discovery to the three-dimensional reconstruction. Trends Parasitol 2007; 23: 502-9.
    • (2007) Trends Parasitol , vol.23 , pp. 502-509
    • Wickert, H.1    Krohne, G.2
  • 124
    • 30044443910 scopus 로고    scopus 로고
    • Maurer's clefts: A novel multi-functional organelle in the cytoplasm of Plasmodium falciparum-infected erythrocytes
    • Blisnick T, Vincensini L, Barale JC, Namane A, Breton CB. Maurer's clefts: A novel multi-functional organelle in the cytoplasm of Plasmodium falciparum-infected erythrocytes. Int J Parasitol 2006; 36: 23-36.
    • (2006) Int J Parasitol , vol.36 , pp. 23-36
    • Blisnick, T.1    Vincensini, L.2    Barale, J.C.3    Namane, A.4    Breton, C.B.5
  • 125
    • 16244363102 scopus 로고    scopus 로고
    • LNCL1, an erythrocyte protein recruited to the Maurer's clefts during Plasmodium falciparum development
    • Blisnick T, Vincensini L, Barale JC, Namane A, Breton CB. LNCL1, an erythrocyte protein recruited to the Maurer's clefts during Plasmodium falciparum development. Mol Biochem Parasitol 2005; 141: 39-47.
    • (2005) Mol Biochem Parasitol , vol.141 , pp. 39-47
    • Blisnick, T.1    Vincensini, L.2    Barale, J.C.3    Namane, A.4    Breton, C.B.5
  • 126
    • 27944471039 scopus 로고    scopus 로고
    • Signal-mediated export of proteins from, the malaria parasite to the host erythrocyte
    • Marti M, Baum J, Rug M, Tilney L, Cowman AF. Signal-mediated export of proteins from, the malaria parasite to the host erythrocyte. J Cell Biol 2005: 171: 587-92.
    • (2005) J Cell Biol , vol.171 , pp. 587-592
    • Marti, M.1    Baum, J.2    Rug, M.3    Tilney, L.4    Cowman, A.F.5
  • 127
    • 0037036617 scopus 로고    scopus 로고
    • Characterization of a delta-COP homologue in the malaria parasite, Plasmodium falciparum
    • Adisa A, Rug M, Foley M, Tilney L. Characterization of a delta-COP homologue in the malaria parasite, Plasmodium falciparum. Mol Biochem Parasitol 2001; 123: 11-21.
    • (2001) Mol Biochem Parasitol , vol.123 , pp. 11-21
    • Adisa, A.1    Rug, M.2    Foley, M.3    Tilney, L.4
  • 128
    • 0038048449 scopus 로고    scopus 로고
    • Evidence for trafficking of PfEMP1 to the surface of P. falciparum-infected erythrocytes via a camplex membrane network
    • Wickert H. Wissing F, Andrews KT, Stich A, Krohne G. Lanzer M. Evidence for trafficking of PfEMP1 to the surface of P. falciparum-infected erythrocytes via a camplex membrane network. Eur J Cell Biol 2002; 82: 271-84.
    • (2002) Eur J Cell Biol , vol.82 , pp. 271-284
    • Wickert, H.1    Wissing, F.2    Andrews, K.T.3    Stich, A.4    Krohne, G.5    Lanzer, M.6
  • 129
    • 17144386621 scopus 로고    scopus 로고
    • Protein transport and trafficking in Plasmodium falciparum-infected erythrocytes
    • Priborski JM, Lanzer M. Protein transport and trafficking in Plasmodium falciparum-infected erythrocytes. Parasitology 2005; 130: 373-88.
    • (2005) Parasitology , vol.130 , pp. 373-388
    • Priborski, J.M.1    Lanzer, M.2
  • 131
    • 0032213352 scopus 로고    scopus 로고
    • The molecular mechanism of Giardia encystation
    • Lujan HD, Mowatt MR, Nash TE. The molecular mechanism of Giardia encystation. Parasitol Today 1998; 14: 446-50.
    • (1998) Parasitol Today , vol.14 , pp. 446-450
    • Lujan, H.D.1    Mowatt, M.R.2    Nash, T.E.3
  • 132
    • 6444228418 scopus 로고    scopus 로고
    • Contribution of microscopy to a better knowledge of the biology of Giardia lamblia
    • De Souza W, Lanfredi-Rangel A, Campanati L. Contribution of microscopy to a better knowledge of the biology of Giardia lamblia. Microscop Microanal 2004; 10: 513-27.
    • (2004) Microscop Microanal , vol.10 , pp. 513-527
    • De Souza, W.1    Lanfredi-Rangel, A.2    Campanati, L.3
  • 133
    • 15944408828 scopus 로고    scopus 로고
    • Amylopectin biogenesis and characterization in the protozoan parasite Toxoplasma gondii, the intracellular development of which is restricted in GepG2 cell line
    • Guerardel Y, Leleu D, Coppin A, Lienard L, Slomianny C, Strecker G, et al. Amylopectin biogenesis and characterization in the protozoan parasite Toxoplasma gondii, the intracellular development of which is restricted in GepG2 cell line. Microb Infect 2005; 7: 41-8.
    • (2005) Microb Infect , vol.7 , pp. 41-48
    • Guerardel, Y.1    Leleu, D.2    Coppin, A.3    Lienard, L.4    Slomianny, C.5    Strecker, G.6
  • 134
    • 0029353950 scopus 로고
    • Mitosis and genotile partition in trypanosomes
    • Solari AJ. Mitosis and genotile partition in trypanosomes. Biocell 1995; 19: 65-84.
    • (1995) Biocell , vol.19 , pp. 65-84
    • Solari, A.J.1
  • 135
    • 0032584983 scopus 로고    scopus 로고
    • Chromosomes numbers of Tritrichomonas foetus and Tritrichomonas suis
    • Xu WD, Lun ZR, Gajadhar A. Chromosomes numbers of Tritrichomonas foetus and Tritrichomonas suis. Vet Parasitol 1998; 78: 247-51.
    • (1998) Vet Parasitol , vol.78 , pp. 247-251
    • Xu, W.D.1    Lun, Z.R.2    Gajadhar, A.3
  • 136
    • 0021881869 scopus 로고
    • Fine structure and cytochemistry of endoplasmic reticulum and its association with the plasma membrane of Leishmania mexicana amazonensis
    • Pimenta PF, De Souza W. Fine structure and cytochemistry of endoplasmic reticulum and its association with the plasma membrane of Leishmania mexicana amazonensis. J Submicroscop Cytol 1985; 17: 413-9.
    • (1985) J Submicroscop Cytol , vol.17 , pp. 413-419
    • Pimenta, P.F.1    De Souza, W.2
  • 137
    • 0021914619 scopus 로고
    • Fine structure and cytochemistry of Phytomonas davidi
    • Attias M, De Souza W. Fine structure and cytochemistry of Phytomonas davidi. J Submicroscop Cytol 1985; 17: 201-12.
    • (1985) J Submicroscop Cytol , vol.17 , pp. 201-212
    • Attias, M.1    De Souza, W.2
  • 138
    • 0036095372 scopus 로고    scopus 로고
    • Some observations on the fine structure of trophozoites of the haemogregarine Cyrilia lignieresi (Adeleina: Haemogregarinidae) in erythrocytes of the fish Synbranchus marmoratus (Synbranchidae)
    • Diniz JA, Silva EO, De Souza W, Lainson R. Some observations on the fine structure of trophozoites of the haemogregarine Cyrilia lignieresi (Adeleina: Haemogregarinidae) in erythrocytes of the fish Synbranchus marmoratus (Synbranchidae). Parasitol Res 2002; 88: 593-7.
    • (2002) Parasitol Res , vol.88 , pp. 593-597
    • Diniz, J.A.1    Silva, E.O.2    De Souza, W.3    Lainson, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.