메뉴 건너뛰기




Volumn 39, Issue 2, 2009, Pages 153-162

Apicomplexan cytoskeleton and motors: Key regulators in morphogenesis, cell division, transport and motility

Author keywords

Actin; Apicomplexa; Cytoskeleton; Egress; Glideosome; Invasion; Mitosis; Myosin

Indexed keywords

CELL ORGANELLE; LYSIS; MORPHOGENESIS; MOTILITY; PROTEIN; PROTOZOAN;

EID: 57549104111     PISSN: 00207519     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijpara.2008.10.007     Document Type: Review
Times cited : (42)

References (111)
  • 1
    • 0017879439 scopus 로고
    • Erythrocyte entry by malarial parasites. A moving junction between erythrocyte and parasite
    • Aikawa M., Miller L.H., Johnson J., and Rabbege J. Erythrocyte entry by malarial parasites. A moving junction between erythrocyte and parasite. J. Cell Biol. 77 (1978) 72-82
    • (1978) J. Cell Biol. , vol.77 , pp. 72-82
    • Aikawa, M.1    Miller, L.H.2    Johnson, J.3    Rabbege, J.4
  • 2
    • 77951026559 scopus 로고    scopus 로고
    • Identification of the moving junction complex of Toxoplasma gondii: a collaboration between distinct secretory organelles
    • Alexander D.L., Mital J., Ward G.E., Bradley P., and Boothroyd J.C. Identification of the moving junction complex of Toxoplasma gondii: a collaboration between distinct secretory organelles. PLoS Pathog. 1 (2005) e17
    • (2005) PLoS Pathog. , vol.1
    • Alexander, D.L.1    Mital, J.2    Ward, G.E.3    Bradley, P.4    Boothroyd, J.C.5
  • 3
    • 33746267433 scopus 로고    scopus 로고
    • Plasmodium falciparum AMA1 binds a rhoptry neck protein homologous to TgRON4, a component of the moving junction in Toxoplasma gondii
    • Alexander D.L., Arastu-Kapur S., Dubremetz J.F., and Boothroyd J.C. Plasmodium falciparum AMA1 binds a rhoptry neck protein homologous to TgRON4, a component of the moving junction in Toxoplasma gondii. Eukaryot. Cell 5 (2006) 1169-1173
    • (2006) Eukaryot. Cell , vol.5 , pp. 1169-1173
    • Alexander, D.L.1    Arastu-Kapur, S.2    Dubremetz, J.F.3    Boothroyd, J.C.4
  • 4
    • 22944473016 scopus 로고    scopus 로고
    • A malarial cysteine protease is necessary for Plasmodium sporozoite egress from oocysts
    • Aly A.S., and Matuschewski K. A malarial cysteine protease is necessary for Plasmodium sporozoite egress from oocysts. J. Exp. Med. 202 (2005) 225-230
    • (2005) J. Exp. Med. , vol.202 , pp. 225-230
    • Aly, A.S.1    Matuschewski, K.2
  • 5
    • 45149123776 scopus 로고    scopus 로고
    • Targeted deletion of SAP1 abolishes the expression of infectivity factors necessary for successful malaria parasite liver infection
    • Aly A.S., Mikolajczak S.A., Rivera H.S., Camargo N., Jacobs-Lorena V., Labaied M., Coppens I., and Kappe S.H. Targeted deletion of SAP1 abolishes the expression of infectivity factors necessary for successful malaria parasite liver infection. Mol. Microbiol. 69 (2008) 152-163
    • (2008) Mol. Microbiol. , vol.69 , pp. 152-163
    • Aly, A.S.1    Mikolajczak, S.A.2    Rivera, H.S.3    Camargo, N.4    Jacobs-Lorena, V.5    Labaied, M.6    Coppens, I.7    Kappe, S.H.8
  • 6
    • 22544455356 scopus 로고    scopus 로고
    • In vivo imaging of malaria parasites-recent advances and future directions
    • Amino R., Menard R., and Frischknecht F. In vivo imaging of malaria parasites-recent advances and future directions. Curr. Opin. Microbiol. 8 (2005) 407-414
    • (2005) Curr. Opin. Microbiol. , vol.8 , pp. 407-414
    • Amino, R.1    Menard, R.2    Frischknecht, F.3
  • 7
    • 33750182681 scopus 로고    scopus 로고
    • Quantitative imaging of Plasmodium sporozoites in the mammalian host
    • Amino R., Thiberge S., Shorte S., Frischknecht F., and Menard R. Quantitative imaging of Plasmodium sporozoites in the mammalian host. CR Biol. 329 (2006) 858-862
    • (2006) CR Biol. , vol.329 , pp. 858-862
    • Amino, R.1    Thiberge, S.2    Shorte, S.3    Frischknecht, F.4    Menard, R.5
  • 13
    • 33645306878 scopus 로고    scopus 로고
    • A conserved molecular motor drives cell invasion and gliding motility across malaria life cycle stages and other apicomplexan parasites
    • Baum J., Richard D., Healer J., Rug M., Krnajski Z., Gilberger T.W., Green J.L., Holder A.A., and Cowman A.F. A conserved molecular motor drives cell invasion and gliding motility across malaria life cycle stages and other apicomplexan parasites. J. Biol. Chem. 281 (2006) 5197-5208
    • (2006) J. Biol. Chem. , vol.281 , pp. 5197-5208
    • Baum, J.1    Richard, D.2    Healer, J.3    Rug, M.4    Krnajski, Z.5    Gilberger, T.W.6    Green, J.L.7    Holder, A.A.8    Cowman, A.F.9
  • 14
    • 40149100618 scopus 로고    scopus 로고
    • A malaria parasite formin regulates actin polymerization and localizes to the parasite-erythrocyte moving junction during invasion
    • Baum J., Tonkin C.J., Paul A.S., Rug M., Smith B.J., Gould S.B., Richard D., Pollard T.D., and Cowman A.F. A malaria parasite formin regulates actin polymerization and localizes to the parasite-erythrocyte moving junction during invasion. Cell Host Microbe 3 (2008) 188-198
    • (2008) Cell Host Microbe , vol.3 , pp. 188-198
    • Baum, J.1    Tonkin, C.J.2    Paul, A.S.3    Rug, M.4    Smith, B.J.5    Gould, S.B.6    Richard, D.7    Pollard, T.D.8    Cowman, A.F.9
  • 15
    • 53149122085 scopus 로고    scopus 로고
    • Lipidomic analysis of Toxoplasma gondii tachyzoites rhoptries: further insights into the role of cholesterol
    • Besteiro S., Bertrand-Michel J., Lebrun M., Vial H., and Dubremetz J.F. Lipidomic analysis of Toxoplasma gondii tachyzoites rhoptries: further insights into the role of cholesterol. Biochem J. 415 (2008) 87-96
    • (2008) Biochem J. , vol.415 , pp. 87-96
    • Besteiro, S.1    Bertrand-Michel, J.2    Lebrun, M.3    Vial, H.4    Dubremetz, J.F.5
  • 16
    • 14844334897 scopus 로고    scopus 로고
    • A surface phospholipase is involved in the migration of Plasmodium sporozoites through cells
    • Bhanot P., Schauer K., Coppens I., and Nussenzweig V. A surface phospholipase is involved in the migration of Plasmodium sporozoites through cells. J. Biol. Chem. 280 (2005) 6752-6760
    • (2005) J. Biol. Chem. , vol.280 , pp. 6752-6760
    • Bhanot, P.1    Schauer, K.2    Coppens, I.3    Nussenzweig, V.4
  • 17
    • 0034458967 scopus 로고    scopus 로고
    • Ionophore-resistant mutants of Toxoplasma gondii reveal host cell permeabilization as an early event in egress
    • Black M.W., Arrizabalaga G., and Boothroyd J.C. Ionophore-resistant mutants of Toxoplasma gondii reveal host cell permeabilization as an early event in egress. Mol. Cell Biol. 20 (2000) 9399-9408
    • (2000) Mol. Cell Biol. , vol.20 , pp. 9399-9408
    • Black, M.W.1    Arrizabalaga, G.2    Boothroyd, J.C.3
  • 19
    • 37349107981 scopus 로고    scopus 로고
    • Kiss and spit: the dual roles of Toxoplasma rhoptries
    • Boothroyd J.C., and Dubremetz J.F. Kiss and spit: the dual roles of Toxoplasma rhoptries. Nat. Rev. Microbiol. 6 (2008) 79-88
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 79-88
    • Boothroyd, J.C.1    Dubremetz, J.F.2
  • 21
    • 36549005658 scopus 로고    scopus 로고
    • Rhoptries: an arsenal of secreted virulence factors
    • Bradley P.J., and Sibley L.D. Rhoptries: an arsenal of secreted virulence factors. Curr. Opin. Microbiol. 10 (2007) 582-587
    • (2007) Curr. Opin. Microbiol. , vol.10 , pp. 582-587
    • Bradley, P.J.1    Sibley, L.D.2
  • 23
    • 0344875493 scopus 로고    scopus 로고
    • Sites of interaction between aldolase and thrombospondin-related anonymous protein in Plasmodium
    • Buscaglia C.A., Coppens I., Hol W.G., and Nussenzweig V. Sites of interaction between aldolase and thrombospondin-related anonymous protein in Plasmodium. Mol. Biol. Cell 14 (2003) 4947-4957
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4947-4957
    • Buscaglia, C.A.1    Coppens, I.2    Hol, W.G.3    Nussenzweig, V.4
  • 24
    • 34250327989 scopus 로고    scopus 로고
    • Calcium ionophore-induced egress of Toxoplasma gondii shortly after host cell invasion
    • Caldas L.A., de Souza W., and Attias M. Calcium ionophore-induced egress of Toxoplasma gondii shortly after host cell invasion. Vet. Parasitol. 147 (2007) 210-220
    • (2007) Vet. Parasitol. , vol.147 , pp. 210-220
    • Caldas, L.A.1    de Souza, W.2    Attias, M.3
  • 26
    • 0032927424 scopus 로고    scopus 로고
    • Mobilization of intracellular calcium stimulates microneme discharge in Toxoplasma gondii
    • Carruthers V.B., and Sibley L.D. Mobilization of intracellular calcium stimulates microneme discharge in Toxoplasma gondii. Mol. Microbiol. 31 (1999) 421-428
    • (1999) Mol. Microbiol. , vol.31 , pp. 421-428
    • Carruthers, V.B.1    Sibley, L.D.2
  • 27
    • 46249109602 scopus 로고    scopus 로고
    • Microneme proteins in apicomplexans
    • Carruthers V.B., and Tomley F.M. Microneme proteins in apicomplexans. Subcell Biochem. 47 (2008) 33-45
    • (2008) Subcell Biochem. , vol.47 , pp. 33-45
    • Carruthers, V.B.1    Tomley, F.M.2
  • 28
    • 12344299732 scopus 로고    scopus 로고
    • The Plasmodium circumsporozoite protein is proteolytically processed during cell invasion
    • Coppi A., Pinzon-Ortiz C., Hutter C., and Sinnis P. The Plasmodium circumsporozoite protein is proteolytically processed during cell invasion. J. Exp. Med. 201 (2005) 27-33
    • (2005) J. Exp. Med. , vol.201 , pp. 27-33
    • Coppi, A.1    Pinzon-Ortiz, C.2    Hutter, C.3    Sinnis, P.4
  • 29
    • 35848931896 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans provide a signal to Plasmodium sporozoites to stop migrating and productively invade host cells
    • Coppi A., Tewari R., Bishop J.R., Bennett B.L., Lawrence R., Esko J.D., Billker O., and Sinnis P. Heparan sulfate proteoglycans provide a signal to Plasmodium sporozoites to stop migrating and productively invade host cells. Cell Host Microbe 2 (2007) 316-327
    • (2007) Cell Host Microbe , vol.2 , pp. 316-327
    • Coppi, A.1    Tewari, R.2    Bishop, J.R.3    Bennett, B.L.4    Lawrence, R.5    Esko, J.D.6    Billker, O.7    Sinnis, P.8
  • 31
    • 34250322091 scopus 로고    scopus 로고
    • Cryoelectron tomography reveals periodic material at the inner side of subpellicular microtubules in apicomplexan parasites
    • Cyrklaff M., Kudryashev M., Leis A., Leonard K., Baumeister W., Menard R., Meissner M., and Frischknecht F. Cryoelectron tomography reveals periodic material at the inner side of subpellicular microtubules in apicomplexan parasites. J. Exp. Med. 204 (2007) 1281-1287
    • (2007) J. Exp. Med. , vol.204 , pp. 1281-1287
    • Cyrklaff, M.1    Kudryashev, M.2    Leis, A.3    Leonard, K.4    Baumeister, W.5    Menard, R.6    Meissner, M.7    Frischknecht, F.8
  • 33
    • 0015577737 scopus 로고
    • Ultrastructural study of schizogonic mitosis in the coccidian, Eimeria necatrix (Johnson 1930)
    • Dubremetz J.F. Ultrastructural study of schizogonic mitosis in the coccidian, Eimeria necatrix (Johnson 1930). J. Ultrastruct. Res. 42 (1973) 354-376
    • (1973) J. Ultrastruct. Res. , vol.42 , pp. 354-376
    • Dubremetz, J.F.1
  • 34
    • 0016466479 scopus 로고
    • Genesis of merozoites in the coccidia, Eimeria necatrix. Ultrastructural study
    • Dubremetz J.F. Genesis of merozoites in the coccidia, Eimeria necatrix. Ultrastructural study. J. Protozool. 22 (1975) 71-84
    • (1975) J. Protozool. , vol.22 , pp. 71-84
    • Dubremetz, J.F.1
  • 35
    • 0019993146 scopus 로고
    • Toxoplasma gondii: calcium ionophore A23187-mediated exit of trophozoites from infected murine macrophages
    • Endo T., Sethi K.K., and Piekarski G. Toxoplasma gondii: calcium ionophore A23187-mediated exit of trophozoites from infected murine macrophages. Exp. Parasitol. 53 (1982) 179-188
    • (1982) Exp. Parasitol. , vol.53 , pp. 179-188
    • Endo, T.1    Sethi, K.K.2    Piekarski, G.3
  • 36
    • 0021664343 scopus 로고
    • Interaction of sporozoites of Theileria parva with bovine lymphocytes in vitro. I. Early events after invasion
    • Fawcett D., Musoke A., and Voigt W. Interaction of sporozoites of Theileria parva with bovine lymphocytes in vitro. I. Early events after invasion. Tissue Cell 16 (1984) 873-884
    • (1984) Tissue Cell , vol.16 , pp. 873-884
    • Fawcett, D.1    Musoke, A.2    Voigt, W.3
  • 38
    • 0025732915 scopus 로고
    • Characterization of the lipid content of Toxoplasma gondii rhoptries
    • Foussard F., Leriche M.A., and 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
  • 40
    • 35148895750 scopus 로고    scopus 로고
    • Toxoplasma gondii: induction of egress by the potassium ionophore nigericin
    • Fruth I.A., and Arrizabalaga G. Toxoplasma gondii: induction of egress by the potassium ionophore nigericin. Int. J. Parasitol. 37 (2007) 1559-1567
    • (2007) Int. J. Parasitol. , vol.37 , pp. 1559-1567
    • Fruth, I.A.1    Arrizabalaga, G.2
  • 41
    • 33750363325 scopus 로고    scopus 로고
    • Identification of PhIL1, a novel cytoskeletal protein of the Toxoplasma gondii pellicle, through photosensitized labeling with 5-[125I] iodonaphthalene-1-azide
    • Gilk S.D., Raviv Y., Hu K., Murray J.M., Beckers C.J., and Ward G.E. Identification of PhIL1, a novel cytoskeletal protein of the Toxoplasma gondii pellicle, through photosensitized labeling with 5-[125I] iodonaphthalene-1-azide. Eukaryot. Cell 5 (2006) 1622-1634
    • (2006) Eukaryot. Cell , vol.5 , pp. 1622-1634
    • Gilk, S.D.1    Raviv, Y.2    Hu, K.3    Murray, J.M.4    Beckers, C.J.5    Ward, G.E.6
  • 42
    • 24944495451 scopus 로고    scopus 로고
    • Membrane transformation during malaria parasite release from human red blood cells
    • Glushakova S., Yin D., Li T., and Zimmerberg J. Membrane transformation during malaria parasite release from human red blood cells. Curr. Biol. 15 (2005) 1645-1650
    • (2005) Curr. Biol. , vol.15 , pp. 1645-1650
    • Glushakova, S.1    Yin, D.2    Li, T.3    Zimmerberg, J.4
  • 43
    • 43049157520 scopus 로고    scopus 로고
    • Malaria liver stage susceptibility locus identified on mouse chromosome 17 by congenic mapping
    • Goncalves L.A., Almeida P., Mota M.M., and Penha-Goncalves C. Malaria liver stage susceptibility locus identified on mouse chromosome 17 by congenic mapping. PLoS ONE 3 (2008) e1874
    • (2008) PLoS ONE , vol.3
    • Goncalves, L.A.1    Almeida, P.2    Mota, M.M.3    Penha-Goncalves, C.4
  • 44
    • 29244437897 scopus 로고    scopus 로고
    • Comparative genome analysis reveals a conserved family of actin-like proteins in apicomplexan parasites
    • Gordon J.L., and Sibley L.D. Comparative genome analysis reveals a conserved family of actin-like proteins in apicomplexan parasites. BMC Genomics 6 (2005) 179
    • (2005) BMC Genomics , vol.6 , pp. 179
    • Gordon, J.L.1    Sibley, L.D.2
  • 45
    • 51649092580 scopus 로고    scopus 로고
    • A novel actin-related protein is associated with daughter cell formation in Toxoplasma
    • Gordon J.L., Beatty W.L., and Sibley L.D. A novel actin-related protein is associated with daughter cell formation in Toxoplasma. Eukaryot. Cell 7 (2008) 1500-1512
    • (2008) Eukaryot. Cell , vol.7 , pp. 1500-1512
    • Gordon, J.L.1    Beatty, W.L.2    Sibley, L.D.3
  • 46
    • 33745480357 scopus 로고    scopus 로고
    • A MORN-repeat protein is a dynamic component of the Toxoplasma gondii cell division apparatus
    • Gubbels M.J., Vaishnava S., Boot N., Dubremetz J.F., and Striepen B. A MORN-repeat protein is a dynamic component of the Toxoplasma gondii cell division apparatus. J. Cell Sci. 119 (2006) 2236-2245
    • (2006) J. Cell Sci. , vol.119 , pp. 2236-2245
    • Gubbels, M.J.1    Vaishnava, S.2    Boot, N.3    Dubremetz, J.F.4    Striepen, B.5
  • 48
    • 51249101916 scopus 로고    scopus 로고
    • The cell cycle and Toxoplasma gondii cell division: tightly knit or loosely stitched?
    • Gubbels M.J., White M., and Szatanek T. The cell cycle and Toxoplasma gondii cell division: tightly knit or loosely stitched?. Int. J. Parasitol. 38 (2008) 1343-1358
    • (2008) Int. J. Parasitol. , vol.38 , pp. 1343-1358
    • Gubbels, M.J.1    White, M.2    Szatanek, T.3
  • 49
    • 0035875917 scopus 로고    scopus 로고
    • Toxoplasma evacuoles: a two-step process of secretion and fusion forms the parasitophorous vacuole
    • Hakansson S., Charron A.J., and Sibley L.D. Toxoplasma evacuoles: a two-step process of secretion and fusion forms the parasitophorous vacuole. EMBO J. 20 (2001) 3132-3144
    • (2001) EMBO J. , vol.20 , pp. 3132-3144
    • Hakansson, S.1    Charron, A.J.2    Sibley, L.D.3
  • 50
    • 46949102452 scopus 로고    scopus 로고
    • Functional characterization of a redundant Plasmodium TRAP family invasin, TRAP-like protein, by aldolase binding and a genetic complementation test
    • Heiss K., Nie H., Kumar S., Daly T.M., Bergman L.W., and Matuschewski K. Functional characterization of a redundant Plasmodium TRAP family invasin, TRAP-like protein, by aldolase binding and a genetic complementation test. Eukaryot. Cell 7 (2008) 1062-1070
    • (2008) Eukaryot. Cell , vol.7 , pp. 1062-1070
    • Heiss, K.1    Nie, H.2    Kumar, S.3    Daly, T.M.4    Bergman, L.W.5    Matuschewski, K.6
  • 52
    • 11144281883 scopus 로고    scopus 로고
    • Phylogenetic analysis of the formin homology 2 domain
    • Higgs H.N., and Peterson K.J. Phylogenetic analysis of the formin homology 2 domain. Mol. Biol. Cell 16 (2005) 1-13
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1-13
    • Higgs, H.N.1    Peterson, K.J.2
  • 53
    • 38949206641 scopus 로고    scopus 로고
    • Organizational changes of the daughter basal complex during the parasite replication of Toxoplasma gondii
    • Hu K. Organizational changes of the daughter basal complex during the parasite replication of Toxoplasma gondii. PLoS Pathog. 4 (2008) e10
    • (2008) PLoS Pathog. , vol.4
    • Hu, K.1
  • 54
    • 0037128925 scopus 로고    scopus 로고
    • A novel polymer of tubulin forms the conoid of Toxoplasma gondii
    • Hu K., Roos D.S., and Murray J.M. A novel polymer of tubulin forms the conoid of Toxoplasma gondii. J. Cell Biol. 156 (2002) 1039-1050
    • (2002) J. Cell Biol. , vol.156 , pp. 1039-1050
    • Hu, K.1    Roos, D.S.2    Murray, J.M.3
  • 56
    • 19344370327 scopus 로고    scopus 로고
    • Cell-passage activity is required for the malarial parasite to cross the liver sinusoidal cell layer
    • Ishino T., Yano K., Chinzei Y., and Yuda M. Cell-passage activity is required for the malarial parasite to cross the liver sinusoidal cell layer. PLoS Biol. 2 (2004) e4
    • (2004) PLoS Biol. , vol.2
    • Ishino, T.1    Yano, K.2    Chinzei, Y.3    Yuda, M.4
  • 57
    • 28244480361 scopus 로고    scopus 로고
    • Two proteins with 6-cys motifs are required for malarial parasites to commit to infection of the hepatocyte
    • Ishino T., Chinzei Y., and Yuda M. Two proteins with 6-cys motifs are required for malarial parasites to commit to infection of the hepatocyte. Mol. Microbiol. 58 (2005) 1264-1275
    • (2005) Mol. Microbiol. , vol.58 , pp. 1264-1275
    • Ishino, T.1    Chinzei, Y.2    Yuda, M.3
  • 58
    • 13844309801 scopus 로고    scopus 로고
    • A Plasmodium sporozoite protein with a membrane attack complex domain is required for breaching the liver sinusoidal cell layer prior to hepatocyte infection
    • Ishino T., Chinzei Y., and Yuda M. A Plasmodium sporozoite protein with a membrane attack complex domain is required for breaching the liver sinusoidal cell layer prior to hepatocyte infection. Cell Microbiol. 7 (2005) 199-208
    • (2005) Cell Microbiol. , vol.7 , pp. 199-208
    • Ishino, T.1    Chinzei, Y.2    Yuda, M.3
  • 59
    • 33645077874 scopus 로고    scopus 로고
    • A calcium-dependent protein kinase regulates Plasmodium ookinete access to the midgut epithelial cell
    • Ishino T., Orito Y., Chinzei Y., and Yuda M. A calcium-dependent protein kinase regulates Plasmodium ookinete access to the midgut epithelial cell. Mol. Microbiol. 59 (2006) 1175-1184
    • (2006) Mol. Microbiol. , vol.59 , pp. 1175-1184
    • Ishino, T.1    Orito, Y.2    Chinzei, Y.3    Yuda, M.4
  • 60
    • 0038637915 scopus 로고    scopus 로고
    • Aldolase forms a bridge between cell surface adhesins and the actin cytoskeleton in apicomplexan parasites
    • Jewett T.J., and Sibley L.D. Aldolase forms a bridge between cell surface adhesins and the actin cytoskeleton in apicomplexan parasites. Mol. Cell 11 (2003) 885-894
    • (2003) Mol. Cell , vol.11 , pp. 885-894
    • Jewett, T.J.1    Sibley, L.D.2
  • 61
    • 34547761730 scopus 로고    scopus 로고
    • Immobilization of the type XIV myosin complex in Toxoplasma gondii
    • Johnson T.M., Rajfur Z., Jacobson K., and Beckers C.J. Immobilization of the type XIV myosin complex in Toxoplasma gondii. Mol. Biol. Cell 18 (2007) 3039-3046
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3039-3046
    • Johnson, T.M.1    Rajfur, Z.2    Jacobson, K.3    Beckers, C.J.4
  • 62
    • 33645855615 scopus 로고    scopus 로고
    • Plasmodium falciparum erythrocyte invasion: a conserved myosin associated complex
    • Jones M.L., Kitson E.L., and Rayner J.C. Plasmodium falciparum erythrocyte invasion: a conserved myosin associated complex. Mol. Biochem. Parasitol. 147 (2006) 74-84
    • (2006) Mol. Biochem. Parasitol. , vol.147 , pp. 74-84
    • Jones, M.L.1    Kitson, E.L.2    Rayner, J.C.3
  • 63
    • 8744252247 scopus 로고    scopus 로고
    • Essential role of membrane-attack protein in malarial transmission to mosquito host
    • Kadota K., Ishino T., Matsuyama T., Chinzei Y., and Yuda M. Essential role of membrane-attack protein in malarial transmission to mosquito host. Proc. Natl. Acad. Sci. USA 101 (2004) 16310-16315
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 16310-16315
    • Kadota, K.1    Ishino, T.2    Matsuyama, T.3    Chinzei, Y.4    Yuda, M.5
  • 64
    • 33645088696 scopus 로고    scopus 로고
    • CelTOS, a novel malarial protein that mediates transmission to mosquito and vertebrate hosts
    • Kariu T., Ishino T., Yano K., Chinzei Y., and Yuda M. CelTOS, a novel malarial protein that mediates transmission to mosquito and vertebrate hosts. Mol. Microbiol. 59 (2006) 1369-1379
    • (2006) Mol. Microbiol. , vol.59 , pp. 1369-1379
    • Kariu, T.1    Ishino, T.2    Yano, K.3    Chinzei, Y.4    Yuda, M.5
  • 65
    • 0035853753 scopus 로고    scopus 로고
    • Toxoplasma gondii attachment to host cells is regulated by a calmodulin-like domain protein kinase
    • Kieschnick H., Wakefield T., Narducci C.A., and Beckers C. Toxoplasma gondii attachment to host cells is regulated by a calmodulin-like domain protein kinase. J. Biol. Chem. 276 (2001) 12369-12377
    • (2001) J. Biol. Chem. , vol.276 , pp. 12369-12377
    • Kieschnick, H.1    Wakefield, T.2    Narducci, C.A.3    Beckers, C.4
  • 66
    • 34548412297 scopus 로고    scopus 로고
    • Exposure of Plasmodium sporozoites to the intracellular concentration of potassium enhances infectivity and reduces cell passage activity
    • Kumar K.A., Garcia C.R., Chandran V.R., Van Rooijen N., Zhou Y., Winzeler E., and Nussenzweig V. Exposure of Plasmodium sporozoites to the intracellular concentration of potassium enhances infectivity and reduces cell passage activity. Mol. Biochem. Parasitol. 156 (2007) 32-40
    • (2007) Mol. Biochem. Parasitol. , vol.156 , pp. 32-40
    • Kumar, K.A.1    Garcia, C.R.2    Chandran, V.R.3    Van Rooijen, N.4    Zhou, Y.5    Winzeler, E.6    Nussenzweig, V.7
  • 67
    • 34247492194 scopus 로고    scopus 로고
    • Depletion of the Plasmodium berghei thrombospondin-related sporozoite protein reveals a role in host cell entry by sporozoites
    • Labaied M., Camargo N., and Kappe S.H. Depletion of the Plasmodium berghei thrombospondin-related sporozoite protein reveals a role in host cell entry by sporozoites. Mol. Biochem. Parasitol. 153 (2007) 158-166
    • (2007) Mol. Biochem. Parasitol. , vol.153 , pp. 158-166
    • Labaied, M.1    Camargo, N.2    Kappe, S.H.3
  • 68
    • 38849147787 scopus 로고    scopus 로고
    • Exit from host cells by the pathogenic parasite Toxoplasma gondii does not require motility
    • Lavine M.D., and Arrizabalaga G. Exit from host cells by the pathogenic parasite Toxoplasma gondii does not require motility. Eukaryot. Cell 7 (2008) 131-140
    • (2008) Eukaryot. Cell , vol.7 , pp. 131-140
    • Lavine, M.D.1    Arrizabalaga, G.2
  • 70
    • 0041402826 scopus 로고    scopus 로고
    • Intracellular calcium stores in Toxoplasma gondii govern invasion of host cells
    • Lovett J.L., and Sibley L.D. Intracellular calcium stores in Toxoplasma gondii govern invasion of host cells. J. Cell Sci. 116 (2003) 3009-3016
    • (2003) J. Cell Sci. , vol.116 , pp. 3009-3016
    • Lovett, J.L.1    Sibley, L.D.2
  • 71
    • 0035400296 scopus 로고    scopus 로고
    • Characterization of the subpellicular network, a filamentous membrane skeletal component in the parasite Toxoplasma gondii
    • Mann T., and 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
  • 72
    • 0037174876 scopus 로고    scopus 로고
    • Proteolytic processing of TgIMC1 during maturation of the membrane skeleton of Toxoplasma gondii
    • Mann T., Gaskins E., and Beckers C. Proteolytic processing of TgIMC1 during maturation of the membrane skeleton of Toxoplasma gondii. J. Biol. Chem. 277 (2002) 41240-41246
    • (2002) J. Biol. Chem. , vol.277 , pp. 41240-41246
    • Mann, T.1    Gaskins, E.2    Beckers, C.3
  • 73
    • 39749091031 scopus 로고    scopus 로고
    • Electron microscopic observation of cytoskeletal frame structures and detection of tubulin on the apical region of Cryptosporidium parvum sporozoites
    • Matsubayashi M., Takase H., Kimata I., Nakagawa H., Tani H., Sasai K., and Baba E. Electron microscopic observation of cytoskeletal frame structures and detection of tubulin on the apical region of Cryptosporidium parvum sporozoites. Parasitology 135 (2008) 295-301
    • (2008) Parasitology , vol.135 , pp. 295-301
    • Matsubayashi, M.1    Takase, H.2    Kimata, I.3    Nakagawa, H.4    Tani, H.5    Sasai, K.6    Baba, E.7
  • 74
    • 24344439282 scopus 로고    scopus 로고
    • Conditional expression of Toxoplasma gondii apical membrane antigen-1 (TgAMA1) demonstrates that TgAMA1 plays a critical role in host cell invasion
    • Mital J., Meissner M., Soldati D., and Ward G.E. Conditional expression of Toxoplasma gondii apical membrane antigen-1 (TgAMA1) demonstrates that TgAMA1 plays a critical role in host cell invasion. Mol. Biol. Cell 16 (2005) 4341-4349
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4341-4349
    • Mital, J.1    Meissner, M.2    Soldati, D.3    Ward, G.E.4
  • 75
    • 0346251040 scopus 로고    scopus 로고
    • Apical membrane antigen 1, a major malaria vaccine candidate, mediates the close attachment of invasive merozoites to host red blood cells
    • Mitchell G.H., Thomas A.W., Margos G., Dluzewski A.R., and Bannister L.H. Apical membrane antigen 1, a major malaria vaccine candidate, mediates the close attachment of invasive merozoites to host red blood cells. Infect. Immun. 72 (2004) 154-158
    • (2004) Infect. Immun. , vol.72 , pp. 154-158
    • Mitchell, G.H.1    Thomas, A.W.2    Margos, G.3    Dluzewski, A.R.4    Bannister, L.H.5
  • 76
    • 0030095229 scopus 로고    scopus 로고
    • Ca(2+)-dependence of conoid extrusion in Toxoplasma gondii tachyzoites
    • Mondragon R., and Frixione E. Ca(2+)-dependence of conoid extrusion in Toxoplasma gondii tachyzoites. J. Eukaryot. Microbiol. 43 (1996) 120-127
    • (1996) J. Eukaryot. Microbiol. , vol.43 , pp. 120-127
    • Mondragon, R.1    Frixione, E.2
  • 77
    • 0032528078 scopus 로고    scopus 로고
    • Host cell surface sialic acid residues are involved on the process of penetration of Toxoplasma gondii into mammalian cells
    • Monteiro V.G., Soares C.P., and de Souza W. Host cell surface sialic acid residues are involved on the process of penetration of Toxoplasma gondii into mammalian cells. FEMS Microbiol. Lett. 164 (1998) 323-327
    • (1998) FEMS Microbiol. Lett. , vol.164 , pp. 323-327
    • Monteiro, V.G.1    Soares, C.P.2    de Souza, W.3
  • 78
    • 0035782887 scopus 로고    scopus 로고
    • Morphological changes during conoid extrusion in Toxoplasma gondii tachyzoites treated with calcium ionophore
    • Monteiro V.G., de Melo E.J., Attias M., and de Souza W. Morphological changes during conoid extrusion in Toxoplasma gondii tachyzoites treated with calcium ionophore. J. Struct. Biol. 136 (2001) 181-189
    • (2001) J. Struct. Biol. , vol.136 , pp. 181-189
    • Monteiro, V.G.1    de Melo, E.J.2    Attias, M.3    de Souza, W.4
  • 79
    • 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., and Sibley L.D. 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    Sibley, L.D.4
  • 82
    • 0035798694 scopus 로고    scopus 로고
    • The loss of cytoplasmic potassium upon host cell breakdown triggers egress of Toxoplasma gondii
    • Moudy R., Manning T.J., and Beckers C.J. The loss of cytoplasmic potassium upon host cell breakdown triggers egress of Toxoplasma gondii. J. Biol. Chem. 276 (2001) 41492-41501
    • (2001) J. Biol. Chem. , vol.276 , pp. 41492-41501
    • Moudy, R.1    Manning, T.J.2    Beckers, C.J.3
  • 83
    • 38049165494 scopus 로고    scopus 로고
    • Abscisic acid controls calcium-dependent egress and development in Toxoplasma gondii
    • Nagamune K., Hicks L.M., Fux B., Brossier F., Chini E.N., and Sibley L.D. Abscisic acid controls calcium-dependent egress and development in Toxoplasma gondii. Nature 451 (2008) 207-210
    • (2008) Nature , vol.451 , pp. 207-210
    • Nagamune, K.1    Hicks, L.M.2    Fux, B.3    Brossier, F.4    Chini, E.N.5    Sibley, L.D.6
  • 84
    • 0020957006 scopus 로고
    • Secretion from the rhoptries of Toxoplasma gondii during host-cell invasion
    • Nichols B.A., Chiappino M.L., and O'Connor G.R. Secretion from the rhoptries of Toxoplasma gondii during host-cell invasion. J. Ultrastruct. Res. 83 (1983) 85-98
    • (1983) J. Ultrastruct. Res. , vol.83 , pp. 85-98
    • Nichols, B.A.1    Chiappino, M.L.2    O'Connor, G.R.3
  • 85
    • 46649114361 scopus 로고    scopus 로고
    • Organellar dynamics during the cell cycle of Toxoplasma gondii
    • Nishi M., Hu K., Murray J.M., and Roos D.S. Organellar dynamics during the cell cycle of Toxoplasma gondii. J. Cell Sci. 121 (2008) 1559-1568
    • (2008) J. Cell Sci. , vol.121 , pp. 1559-1568
    • Nishi, M.1    Hu, K.2    Murray, J.M.3    Roos, D.S.4
  • 87
    • 38849095132 scopus 로고    scopus 로고
    • Toxoplasma profilin is essential for host cell invasion and TLR11-dependent induction of an interleukin-12 response
    • Plattner F., Yarovinsky F., Romero S., Didry D., Carlier M.F., Sher A., and Soldati-Favre D. Toxoplasma profilin is essential for host cell invasion and TLR11-dependent induction of an interleukin-12 response. Cell Host Microbe 3 (2008) 77-87
    • (2008) Cell Host Microbe , vol.3 , pp. 77-87
    • Plattner, F.1    Yarovinsky, F.2    Romero, S.3    Didry, D.4    Carlier, M.F.5    Sher, A.6    Soldati-Favre, D.7
  • 88
    • 0033980626 scopus 로고    scopus 로고
    • Toxofilin, a novel actin-binding protein from Toxoplasma gondii, sequesters actin monomers and caps actin filaments
    • Poupel O., Boleti H., Axisa S., Couture-Tosi E., and Tardieux I. Toxofilin, a novel actin-binding protein from Toxoplasma gondii, sequesters actin monomers and caps actin filaments. Mol. Biol. Cell 11 (2000) 355-368
    • (2000) Mol. Biol. Cell , vol.11 , pp. 355-368
    • Poupel, O.1    Boleti, H.2    Axisa, S.3    Couture-Tosi, E.4    Tardieux, I.5
  • 90
    • 0015077829 scopus 로고
    • Penetration of Eimeria larimerensis sporozoites into cultured cells as observed with the light and electron microscopes
    • Roberts W.L., Speer C.A., and Hammond D.M. Penetration of Eimeria larimerensis sporozoites into cultured cells as observed with the light and electron microscopes. J. Parasitol. 57 (1971) 615-625
    • (1971) J. Parasitol. , vol.57 , pp. 615-625
    • Roberts, W.L.1    Speer, C.A.2    Hammond, D.M.3
  • 91
    • 31944445311 scopus 로고    scopus 로고
    • Unusual kinetic and structural properties control rapid assembly and turnover of actin in the parasite Toxoplasma gondii
    • Sahoo N., Beatty W., Heuser J., Sept D., and Sibley L.D. Unusual kinetic and structural properties control rapid assembly and turnover of actin in the parasite Toxoplasma gondii. Mol. Biol. Cell 17 (2006) 895-906
    • (2006) Mol. Biol. Cell , vol.17 , pp. 895-906
    • Sahoo, N.1    Beatty, W.2    Heuser, J.3    Sept, D.4    Sibley, L.D.5
  • 93
    • 0017686341 scopus 로고
    • Ultrastructural study of multiple mitoses during sporogony of Plasmodium b. Berghei
    • Schrevel J., Asfaux-Foucher G., and Bafort J.M. Ultrastructural study of multiple mitoses during sporogony of Plasmodium b. Berghei. J. Ultrastruct. Res. 59 (1977) 332-350
    • (1977) J. Ultrastruct. Res. , vol.59 , pp. 332-350
    • Schrevel, J.1    Asfaux-Foucher, G.2    Bafort, J.M.3
  • 94
    • 33749515928 scopus 로고    scopus 로고
    • Regulation of apicomplexan microfilament dynamics by a minimal set of actin-binding proteins
    • Schuler H., and Matuschewski K. Regulation of apicomplexan microfilament dynamics by a minimal set of actin-binding proteins. Traffic 7 (2006) 1433-1439
    • (2006) Traffic , vol.7 , pp. 1433-1439
    • Schuler, H.1    Matuschewski, K.2
  • 95
    • 24344440631 scopus 로고    scopus 로고
    • A Plasmodium actin-depolymerizing factor that binds exclusively to actin monomers
    • Schuler H., Mueller A.K., and Matuschewski K. A Plasmodium actin-depolymerizing factor that binds exclusively to actin monomers. Mol. Biol. Cell 16 (2005) 4013-4023
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4013-4023
    • Schuler, H.1    Mueller, A.K.2    Matuschewski, K.3
  • 99
    • 33750077590 scopus 로고    scopus 로고
    • Two separate, conserved acidic amino acid domains within the Toxoplasma gondii MIC2 cytoplasmic tail are required for parasite survival
    • Starnes G.L., Jewett T.J., Carruthers V.B., and Sibley L.D. Two separate, conserved acidic amino acid domains within the Toxoplasma gondii MIC2 cytoplasmic tail are required for parasite survival. J. Biol. Chem. 281 (2006) 30745-30754
    • (2006) J. Biol. Chem. , vol.281 , pp. 30745-30754
    • Starnes, G.L.1    Jewett, T.J.2    Carruthers, V.B.3    Sibley, L.D.4
  • 102
    • 0032426419 scopus 로고    scopus 로고
    • A Plasmodium falciparum novel gene encoding a coronin-like protein which associates with actin filaments
    • Tardieux I., Liu X., Poupel O., Parzy D., Dehoux P., and Langsley G. A Plasmodium falciparum novel gene encoding a coronin-like protein which associates with actin filaments. FEBS Lett. 441 (1998) 251-256
    • (1998) FEBS Lett. , vol.441 , pp. 251-256
    • Tardieux, I.1    Liu, X.2    Poupel, O.3    Parzy, D.4    Dehoux, P.5    Langsley, G.6
  • 105
    • 22744456158 scopus 로고    scopus 로고
    • Structural basis for the EBA-175 erythrocyte invasion pathway of the malaria parasite Plasmodium falciparum
    • Tolia N.H., Enemark E.J., Sim B.K., and Joshua-Tor L. Structural basis for the EBA-175 erythrocyte invasion pathway of the malaria parasite Plasmodium falciparum. Cell 29 (2005) 183-193
    • (2005) Cell , vol.29 , pp. 183-193
    • Tolia, N.H.1    Enemark, E.J.2    Sim, B.K.3    Joshua-Tor, L.4
  • 106
    • 44849129576 scopus 로고    scopus 로고
    • Sporozoite-mediated hepatocyte wounding limits Plasmodium parasite development via MyD88-mediated NF-kappaB activation and inducible NO synthase expression
    • Torgler R., Bongfen S.E., Romero J.C., Tardivel A., Thome M., and Corradin G. Sporozoite-mediated hepatocyte wounding limits Plasmodium parasite development via MyD88-mediated NF-kappaB activation and inducible NO synthase expression. J. Immunol. 180 (2008) 3990-3999
    • (2008) J. Immunol. , vol.180 , pp. 3990-3999
    • Torgler, R.1    Bongfen, S.E.2    Romero, J.C.3    Tardivel, A.4    Thome, M.5    Corradin, G.6
  • 107
    • 34848843529 scopus 로고    scopus 로고
    • Malaria circumsporozoite protein inhibits the respiratory burst in Kupffer cells
    • Usynin I., Klotz C., and Frevert U. Malaria circumsporozoite protein inhibits the respiratory burst in Kupffer cells. Cell Microbiol. 9 (2007) 2610-2628
    • (2007) Cell Microbiol. , vol.9 , pp. 2610-2628
    • Usynin, I.1    Klotz, C.2    Frevert, U.3
  • 108
    • 23944458205 scopus 로고    scopus 로고
    • Gliding motility leads to active cellular invasion by Cryptosporidium parvum sporozoites
    • Wetzel D.M., Schmidt J., Kuhlenschmidt M.S., Dubey J.P., and Sibley L.D. Gliding motility leads to active cellular invasion by Cryptosporidium parvum sporozoites. Infect. Immun. 73 (2005) 5379-5387
    • (2005) Infect. Immun. , vol.73 , pp. 5379-5387
    • Wetzel, D.M.1    Schmidt, J.2    Kuhlenschmidt, M.S.3    Dubey, J.P.4    Sibley, L.D.5
  • 110
    • 34147127535 scopus 로고    scopus 로고
    • Plasmodium sporozoites trickle out of the injection site
    • Yamauchi L.M., Coppi A., Snounou G., and Sinnis P. Plasmodium sporozoites trickle out of the injection site. Cell Microbiol. 9 (2007) 1215-1222
    • (2007) Cell Microbiol. , vol.9 , pp. 1215-1222
    • Yamauchi, L.M.1    Coppi, A.2    Snounou, G.3    Sinnis, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.