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Volumn 16, Issue 5, 2014, Pages 632-641

The inner membrane complex through development of Toxoplasma gondii and Plasmodium

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN 20; LIPID BINDING PROTEIN; MEMBRANE PROTEIN; PHOSPHATIDYLINOSITIDE; PROTEIN GAP50; UNCLASSIFIED DRUG;

EID: 84898539452     PISSN: 14625814     EISSN: 14625822     Source Type: Journal    
DOI: 10.1111/cmi.12285     Document Type: Review
Times cited : (67)

References (98)
  • 2
    • 59249092921 scopus 로고    scopus 로고
    • Rab11A-controlled assembly of the inner membrane complex is required for completion of apicomplexan cytokinesis
    • Agop-Nersesian, C., Naissant, B., Ben Rached, F., Rauch, M., Kretzschmar, A., Thiberge, S., etal. (2009) Rab11A-controlled assembly of the inner membrane complex is required for completion of apicomplexan cytokinesis. PLoS Pathog 5: e1000270.
    • (2009) PLoS Pathog , vol.5
    • Agop-Nersesian, C.1    Naissant, B.2    Ben Rached, F.3    Rauch, M.4    Kretzschmar, A.5    Thiberge, S.6
  • 3
    • 77957658575 scopus 로고    scopus 로고
    • Biogenesis of the inner membrane complex is dependent on vesicular transport by the alveolate specific GTPase Rab11B
    • Agop-Nersesian, C., Egarter, S., Langsley, G., Foth, B.J., Ferguson, D.J., and Meissner, M. (2010) Biogenesis of the inner membrane complex is dependent on vesicular transport by the alveolate specific GTPase Rab11B. PLoS Pathog 6: e1001029.
    • (2010) PLoS Pathog , vol.6
    • Agop-Nersesian, C.1    Egarter, S.2    Langsley, G.3    Foth, B.J.4    Ferguson, D.J.5    Meissner, M.6
  • 4
    • 84873406471 scopus 로고    scopus 로고
    • Conditional genome engineering in Toxoplasma gondii uncovers alternative invasion mechanisms
    • Andenmatten, N., Egarter, S., Jackson, A.J., Jullien, N., Herman, J.P., and Meissner, M. (2013) Conditional genome engineering in Toxoplasma gondii uncovers alternative invasion mechanisms. Nat Methods 10: 125-127.
    • (2013) Nat Methods , vol.10 , pp. 125-127
    • Andenmatten, N.1    Egarter, S.2    Jackson, A.J.3    Jullien, N.4    Herman, J.P.5    Meissner, M.6
  • 6
    • 78650258854 scopus 로고    scopus 로고
    • A family of intermediate filament-like proteins is sequentially assembled into the cytoskeleton of Toxoplasma gondii
    • Anderson-White, B.R., Ivey, F.D., Cheng, K., Szatanek, T., Lorestani, A., Beckers, C.J., etal. (2011) A family of intermediate filament-like proteins is sequentially assembled into the cytoskeleton of Toxoplasma gondii. Cell Microbiol 13: 18-31.
    • (2011) Cell Microbiol , vol.13 , pp. 18-31
    • Anderson-White, B.R.1    Ivey, F.D.2    Cheng, K.3    Szatanek, T.4    Lorestani, A.5    Beckers, C.J.6
  • 7
    • 0029000291 scopus 로고
    • The role of the cytoskeleton in Plasmodium falciparum merozoite biology: an electron-microscopic view
    • Bannister, L.H., and Mitchell, G.H. (1995) The role of the cytoskeleton in Plasmodium falciparum merozoite biology: an electron-microscopic view. Ann Trop Med Parasitol 89: 105-111.
    • (1995) Ann Trop Med Parasitol , vol.89 , pp. 105-111
    • Bannister, L.H.1    Mitchell, G.H.2
  • 8
    • 0033844536 scopus 로고    scopus 로고
    • Ultrastructure of rhoptry development in Plasmodium falciparum erythrocytic schizonts
    • Bannister, L.H., Hopkins, J.M., Fowler, R.E., Krishna, S., and Mitchell, G.H. (2000) Ultrastructure of rhoptry development in Plasmodium falciparum erythrocytic schizonts. Parasitology 121 (Part 3): 273-287.
    • (2000) Parasitology , vol.121 , pp. 273-287
    • Bannister, L.H.1    Hopkins, J.M.2    Fowler, R.E.3    Krishna, S.4    Mitchell, G.H.5
  • 9
    • 84892638781 scopus 로고    scopus 로고
    • Apical membrane antigen 1 mediates apicomplexan parasite attachment but is dispensable for host cell invasion
    • Bargieri, D.Y., Andenmatten, N., Lagal, V., Thiberge, S., Whitelaw, J.A., Tardieux, I., etal. (2013) Apical membrane antigen 1 mediates apicomplexan parasite attachment but is dispensable for host cell invasion. Nat Commun 4: 2552.
    • (2013) Nat Commun , vol.4 , pp. 2552
    • Bargieri, D.Y.1    Andenmatten, N.2    Lagal, V.3    Thiberge, S.4    Whitelaw, J.A.5    Tardieux, I.6
  • 10
    • 80052061997 scopus 로고    scopus 로고
    • Targeted disruption of TgPhIL1 in Toxoplasma gondii results in altered parasite morphology and fitness
    • Barkhuff, W.D., Gilk, S.D., Whitmarsh, R., Tilley, L.D., Hunter, C., and Ward, G.E. (2011) Targeted disruption of TgPhIL1 in Toxoplasma gondii results in altered parasite morphology and fitness. PLoS ONE 6: e23977.
    • (2011) PLoS ONE , vol.6
    • Barkhuff, W.D.1    Gilk, S.D.2    Whitmarsh, R.3    Tilley, L.D.4    Hunter, C.5    Ward, G.E.6
  • 11
    • 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., etal. (2006) A conserved molecular motor drives cell invasion and gliding motility across malaria life cycle stages and other apicomplexan parasites. J Biol Chem 281: 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
  • 13
    • 0037242399 scopus 로고    scopus 로고
    • Myosin A tail domain interacting protein (MTIP) localizes to the inner membrane complex of Plasmodium sporozoites
    • Bergman, L.W., Kaiser, K., Fujioka, H., Coppens, I., Daly, T.M., Fox, S., etal. (2003) Myosin A tail domain interacting protein (MTIP) localizes to the inner membrane complex of Plasmodium sporozoites. J Cell Sci 116: 39-49.
    • (2003) J Cell Sci , vol.116 , pp. 39-49
    • Bergman, L.W.1    Kaiser, K.2    Fujioka, H.3    Coppens, I.4    Daly, T.M.5    Fox, S.6
  • 14
    • 67649399023 scopus 로고    scopus 로고
    • Calcium-dependent signaling and kinases in apicomplexan parasites
    • Billker, O., Lourido, S., and Sibley, L.D. (2009) Calcium-dependent signaling and kinases in apicomplexan parasites. Cell Host Microbe 5: 612-622.
    • (2009) Cell Host Microbe , vol.5 , pp. 612-622
    • Billker, O.1    Lourido, S.2    Sibley, L.D.3
  • 15
    • 84859431587 scopus 로고    scopus 로고
    • Crystal structure of GAP50, the anchor of the invasion machinery in the inner membrane complex of Plasmodium falciparum
    • Bosch, J., Paige, M.H., Vaidya, A.B., Bergman, L.W., and Hol, W.G. (2012) Crystal structure of GAP50, the anchor of the invasion machinery in the inner membrane complex of Plasmodium falciparum. J Struct Biol 178: 61-73.
    • (2012) J Struct Biol , vol.178 , pp. 61-73
    • Bosch, J.1    Paige, M.H.2    Vaidya, A.B.3    Bergman, L.W.4    Hol, W.G.5
  • 16
    • 69949148305 scopus 로고    scopus 로고
    • A novel family of Apicomplexan glideosome-associated proteins with an inner membrane-anchoring role
    • Bullen, H.E., Tonkin, C.J., O'Donnell, R.A., Tham, W.H., Papenfuss, A.T., Gould, S., etal. (2009) A novel family of Apicomplexan glideosome-associated proteins with an inner membrane-anchoring role. J Biol Chem 284: 25353-25363.
    • (2009) J Biol Chem , vol.284 , pp. 25353-25363
    • Bullen, H.E.1    Tonkin, C.J.2    O'Donnell, R.A.3    Tham, W.H.4    Papenfuss, A.T.5    Gould, S.6
  • 17
    • 34447633524 scopus 로고    scopus 로고
    • Minimum requirements for ookinete to oocyst transformation in Plasmodium
    • Carter, V., Nacer, A.M., Underhill, A., Sinden, R.E., and Hurd, H. (2007) Minimum requirements for ookinete to oocyst transformation in Plasmodium. Int J Parasitol 37: 1221-1232.
    • (2007) Int J Parasitol , vol.37 , pp. 1221-1232
    • Carter, V.1    Nacer, A.M.2    Underhill, A.3    Sinden, R.E.4    Hurd, H.5
  • 18
    • 84866354236 scopus 로고    scopus 로고
    • Rabbit antibodies against Toxoplasma Hsp20 are able to reduce parasite invasion and gliding motility in Toxoplasma gondii and parasite invasion in Neospora caninum
    • Coceres, V.M., Alonso, A.M., Alomar, M.L., and Corvi, M.M. (2012) Rabbit antibodies against Toxoplasma Hsp20 are able to reduce parasite invasion and gliding motility in Toxoplasma gondii and parasite invasion in Neospora caninum. Exp Parasitol 132: 274-281.
    • (2012) Exp Parasitol , vol.132 , pp. 274-281
    • Coceres, V.M.1    Alonso, A.M.2    Alomar, M.L.3    Corvi, M.M.4
  • 19
    • 0141521595 scopus 로고    scopus 로고
    • Host but not parasite cholesterol controls Toxoplasma cell entry by modulating organelle discharge
    • Coppens, I., and Joiner, K.A. (2003) Host but not parasite cholesterol controls Toxoplasma cell entry by modulating organelle discharge. Mol Biol Cell 14: 3804-3820.
    • (2003) Mol Biol Cell , vol.14 , pp. 3804-3820
    • Coppens, I.1    Joiner, K.A.2
  • 20
    • 84862506944 scopus 로고    scopus 로고
    • Origin, composition, organization and function of the inner membrane complex of Plasmodium falciparum gametocytes
    • Dearnley, M.K., Yeoman, J.A., Hanssen, E., Kenny, S., Turnbull, L., Whitchurch, C.B., etal. (2012) Origin, composition, organization and function of the inner membrane complex of Plasmodium falciparum gametocytes. J Cell Sci 125: 2053-2063.
    • (2012) J Cell Sci , vol.125 , pp. 2053-2063
    • Dearnley, M.K.1    Yeoman, J.A.2    Hanssen, E.3    Kenny, S.4    Turnbull, L.5    Whitchurch, C.B.6
  • 21
    • 65549151758 scopus 로고    scopus 로고
    • Induction and regulation of conoid extrusion in Toxoplasma gondii
    • Del Carmen, M.G., Mondragon, M., Gonzalez, S., and Mondragon, R. (2009) Induction and regulation of conoid extrusion in Toxoplasma gondii. Cell Microbiol 11: 967-982.
    • (2009) Cell Microbiol , vol.11 , pp. 967-982
    • Del Carmen, M.G.1    Mondragon, M.2    Gonzalez, S.3    Mondragon, R.4
  • 23
    • 0029869791 scopus 로고    scopus 로고
    • Toxoplasma invasion of mammalian cells is powered by the actin cytoskeleton of the parasite
    • Dobrowolski, J.M., and Sibley, L.D. (1996) Toxoplasma invasion of mammalian cells is powered by the actin cytoskeleton of the parasite. Cell 84: 933-939.
    • (1996) Cell , vol.84 , pp. 933-939
    • Dobrowolski, J.M.1    Sibley, L.D.2
  • 24
    • 0000619652 scopus 로고
    • Structure de la pellicule du sporozoite de Plasmodium yoelii etude par cryofracture
    • Dubremetz, J.F., Torpier, G., Maurois, P., Prensier, G., and Sinden, R. (1979) Structure de la pellicule du sporozoite de Plasmodium yoelii etude par cryofracture. C R Acad Sci Paris 288: 3.
    • (1979) C R Acad Sci Paris , vol.288 , pp. 3
    • Dubremetz, J.F.1    Torpier, G.2    Maurois, P.3    Prensier, G.4    Sinden, R.5
  • 25
  • 26
    • 84897976345 scopus 로고    scopus 로고
    • The Toxoplasma Acto-MyoA motor complex is important but not essential for gliding motility and host cell invasion
    • Egarter, S., Andenmatten, N., Jackson, A.J., Pall, G., Black, J.A., Ferguson, D.J., etal. (2014) The Toxoplasma Acto-MyoA motor complex is important but not essential for gliding motility and host cell invasion. PLoS ONE.
    • (2014) PLoS ONE
    • Egarter, S.1    Andenmatten, N.2    Jackson, A.J.3    Pall, G.4    Black, J.A.5    Ferguson, D.J.6
  • 28
    • 80052704470 scopus 로고    scopus 로고
    • Unusual N-glycan structures required for trafficking Toxoplasma gondii GAP50 to the inner membrane complex regulate host cell entry through parasite motility
    • Fauquenoy, S., Hovasse, A., Sloves, P.J., Morelle, W., Dilezitoko Alayi, T., Slomianny, C., etal. (2011) Unusual N-glycan structures required for trafficking Toxoplasma gondii GAP50 to the inner membrane complex regulate host cell entry through parasite motility. Mol Cell Proteomics 10: M111 008953.
    • (2011) Mol Cell Proteomics , vol.10
    • Fauquenoy, S.1    Hovasse, A.2    Sloves, P.J.3    Morelle, W.4    Dilezitoko Alayi, T.5    Slomianny, C.6
  • 30
    • 84892678585 scopus 로고    scopus 로고
    • Cell division in apicomplexan parasites
    • Francia, M.E., and Striepen, B. (2014) Cell division in apicomplexan parasites. Nat Rev Microbiol 12: 125-136.
    • (2014) Nat Rev Microbiol , vol.12 , pp. 125-136
    • Francia, M.E.1    Striepen, B.2
  • 32
    • 84862650177 scopus 로고    scopus 로고
    • Toxoplasma ISP4 is a central IMC sub-compartment protein whose localization depends on palmitoylation but not myristoylation
    • Fung, C., Beck, J.R., Robertson, S.D., Gubbels, M.J., and Bradley, P.J. (2012) Toxoplasma ISP4 is a central IMC sub-compartment protein whose localization depends on palmitoylation but not myristoylation. Mol Biochem Parasitol 184: 99-108.
    • (2012) Mol Biochem Parasitol , vol.184 , pp. 99-108
    • Fung, C.1    Beck, J.R.2    Robertson, S.D.3    Gubbels, M.J.4    Bradley, P.J.5
  • 33
    • 2442528540 scopus 로고    scopus 로고
    • Identification of the membrane receptor of a class XIV myosin in Toxoplasma gondii
    • Gaskins, E., Gilk, S., DeVore, N., Mann, T., Ward, G., and Beckers, C. (2004) Identification of the membrane receptor of a class XIV myosin in Toxoplasma gondii. J Cell Biol 165: 383-393.
    • (2004) J Cell Biol , vol.165 , pp. 383-393
    • Gaskins, E.1    Gilk, S.2    DeVore, N.3    Mann, T.4    Ward, G.5    Beckers, C.6
  • 34
    • 79955424413 scopus 로고    scopus 로고
    • Mitosis in the human malaria parasite Plasmodium falciparum
    • Gerald, N., Mahajan, B., and Kumar, S. (2011) Mitosis in the human malaria parasite Plasmodium falciparum. Eukaryot Cell 10: 474-482.
    • (2011) Eukaryot Cell , vol.10 , pp. 474-482
    • Gerald, N.1    Mahajan, B.2    Kumar, S.3
  • 35
    • 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. (2006) Identification of PhIL1, a novel cytoskeletal protein of the Toxoplasma gondii pellicle, through photosensitized labeling with 5-[125I]iodonaphthalene-1-azide. Eukaryot Cell 5: 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
  • 36
    • 59249083317 scopus 로고    scopus 로고
    • GAP45 phosphorylation controls assembly of the Toxoplasma myosin XIV complex
    • Gilk, S.D., Gaskins, E., Ward, G.E., and Beckers, C.J. (2009) GAP45 phosphorylation controls assembly of the Toxoplasma myosin XIV complex. Eukaryot Cell 8: 190-196.
    • (2009) Eukaryot Cell , vol.8 , pp. 190-196
    • Gilk, S.D.1    Gaskins, E.2    Ward, G.E.3    Beckers, C.J.4
  • 37
    • 51649092580 scopus 로고    scopus 로고
    • A novel actin-related protein is associated with daughter cell formation in Toxoplasma gondii
    • Gordon, J.L., Beatty, W.L., and Sibley, L.D. (2008) A novel actin-related protein is associated with daughter cell formation in Toxoplasma gondii. Eukaryot Cell 7: 1500-1512.
    • (2008) Eukaryot Cell , vol.7 , pp. 1500-1512
    • Gordon, J.L.1    Beatty, W.L.2    Sibley, L.D.3
  • 38
    • 77649112718 scopus 로고    scopus 로고
    • Actin-like protein 1 (ALP1) is a component of dynamic, high molecular weight complexes in Toxoplasma gondii
    • Gordon, J.L., Buguliskis, J.S., Buske, P.J., and Sibley, L.D. (2010) Actin-like protein 1 (ALP1) is a component of dynamic, high molecular weight complexes in Toxoplasma gondii. Cytoskeleton (Hoboken) 67: 23-31.
    • (2010) Cytoskeleton (Hoboken) , vol.67 , pp. 23-31
    • Gordon, J.L.1    Buguliskis, J.S.2    Buske, P.J.3    Sibley, L.D.4
  • 39
    • 44649123685 scopus 로고    scopus 로고
    • Alveolins, a new family of cortical proteins that define the protist infrakingdom Alveolata
    • Gould, S.B., Tham, W.H., Cowman, A.F., McFadden, G.I., and Waller, R.F. (2008) Alveolins, a new family of cortical proteins that define the protist infrakingdom Alveolata. Mol Biol Evol 25: 1219-1230.
    • (2008) Mol Biol Evol , vol.25 , pp. 1219-1230
    • Gould, S.B.1    Tham, W.H.2    Cowman, A.F.3    McFadden, G.I.4    Waller, R.F.5
  • 40
    • 3343008962 scopus 로고    scopus 로고
    • Fluorescent protein tagging in Toxoplasma gondii: identification of a novel inner membrane complex component conserved among Apicomplexa
    • Gubbels, M.J., Wieffer, M., and Striepen, B. (2004) Fluorescent protein tagging in Toxoplasma gondii: identification of a novel inner membrane complex component conserved among Apicomplexa. Mol Biochem Parasitol 137: 99-110.
    • (2004) Mol Biochem Parasitol , vol.137 , pp. 99-110
    • Gubbels, M.J.1    Wieffer, M.2    Striepen, B.3
  • 41
    • 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. (2006) A MORN-repeat protein is a dynamic component of the Toxoplasma gondii cell division apparatus. J Cell Sci 119: 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
  • 42
    • 84866917879 scopus 로고    scopus 로고
    • A unique protein phosphatase with kelch-like domains (PPKL) in Plasmodium modulates ookinete differentiation, motility and invasion
    • Guttery, D.S., Poulin, B., Ferguson, D.J., Szoor, B., Wickstead, B., Carroll, P.L., etal. (2012) A unique protein phosphatase with kelch-like domains (PPKL) in Plasmodium modulates ookinete differentiation, motility and invasion. PLoS Pathog 8: e1002948.
    • (2012) PLoS Pathog , vol.8
    • Guttery, D.S.1    Poulin, B.2    Ferguson, D.J.3    Szoor, B.4    Wickstead, B.5    Carroll, P.L.6
  • 43
    • 77649243266 scopus 로고    scopus 로고
    • TgMORN1 is a key organizer for the basal complex of Toxoplasma gondii
    • Heaslip, A.T., Dzierszinski, F., Stein, B., and Hu, K. (2010) TgMORN1 is a key organizer for the basal complex of Toxoplasma gondii. PLoS Pathog 6: e1000754.
    • (2010) PLoS Pathog , vol.6
    • Heaslip, A.T.1    Dzierszinski, F.2    Stein, B.3    Hu, K.4
  • 44
    • 18344362027 scopus 로고    scopus 로고
    • Toxoplasma gondii myosin A and its light chain: a fast, single-headed, plus-end-directed motor
    • Herm-Gotz, A., Weiss, S., Stratmann, R., Fujita-Becker, S., Ruff, C., Meyhofer, E., etal. (2002) Toxoplasma gondii myosin A and its light chain: a fast, single-headed, plus-end-directed motor. EMBO J 21: 2149-2158.
    • (2002) EMBO J , vol.21 , pp. 2149-2158
    • Herm-Gotz, A.1    Weiss, S.2    Stratmann, R.3    Fujita-Becker, S.4    Ruff, C.5    Meyhofer, E.6
  • 45
    • 84863818787 scopus 로고    scopus 로고
    • Calcium dependent protein kinase 1 and calcium fluxes in the malaria parasite
    • Holder, A.A., Mohd Ridzuan, M.A., and Green, J.L. (2012) Calcium dependent protein kinase 1 and calcium fluxes in the malaria parasite. Microbes Infect 14: 825-830.
    • (2012) Microbes Infect , vol.14 , pp. 825-830
    • Holder, A.A.1    Mohd Ridzuan, M.A.2    Green, J.L.3
  • 46
    • 74049111230 scopus 로고    scopus 로고
    • Transcriptional profiling of growth perturbations of the human malaria parasite Plasmodium falciparum
    • Hu, G., Cabrera, A., Kono, M., Mok, S., Chaal, B.K., Haase, S., etal. (2010) Transcriptional profiling of growth perturbations of the human malaria parasite Plasmodium falciparum. Nat Biotechnol 28: 91-98.
    • (2010) Nat Biotechnol , vol.28 , pp. 91-98
    • Hu, G.1    Cabrera, A.2    Kono, M.3    Mok, S.4    Chaal, B.K.5    Haase, S.6
  • 48
    • 33645767721 scopus 로고    scopus 로고
    • Cytoskeletal components of an invasion machine - the apical complex of Toxoplasma gondii
    • Hu, K., Johnson, J., Florens, L., Fraunholz, M., Suravajjala, S., DiLullo, C., etal. (2006) Cytoskeletal components of an invasion machine - the apical complex of Toxoplasma gondii. PLoS Pathog 2: e13.
    • (2006) PLoS Pathog , vol.2
    • Hu, K.1    Johnson, J.2    Florens, L.3    Fraunholz, M.4    Suravajjala, S.5    DiLullo, C.6
  • 49
    • 33748066307 scopus 로고    scopus 로고
    • Toxoplasma MIC2 is a major determinant of invasion and virulence
    • Huynh, M.H., and Carruthers, V.B. (2006) Toxoplasma MIC2 is a major determinant of invasion and virulence. PLoS Pathog 2: e84.
    • (2006) PLoS Pathog , vol.2
    • Huynh, M.H.1    Carruthers, V.B.2
  • 50
    • 84885389086 scopus 로고    scopus 로고
    • Toxoplasma gondii Syntaxin 6 is required for vesicular transport between endosomal-like compartments and the Golgi complex
    • Jackson, A.J., Clucas, C., Mamczur, N.J., Ferguson, D.J., and Meissner, M. (2013) Toxoplasma gondii Syntaxin 6 is required for vesicular transport between endosomal-like compartments and the Golgi complex. Traffic 14: 1166-1181.
    • (2013) Traffic , vol.14 , pp. 1166-1181
    • Jackson, A.J.1    Clucas, C.2    Mamczur, N.J.3    Ferguson, D.J.4    Meissner, M.5
  • 51
    • 77956338984 scopus 로고    scopus 로고
    • Metamorphosis of the malaria parasite in the liver is associated with organelle clearance
    • Jayabalasingham, B., Bano, N., and Coppens, I. (2010) Metamorphosis of the malaria parasite in the liver is associated with organelle clearance. Cell Res 20: 1043-1059.
    • (2010) Cell Res , vol.20 , pp. 1043-1059
    • Jayabalasingham, B.1    Bano, N.2    Coppens, I.3
  • 52
    • 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. (2003) Aldolase forms a bridge between cell surface adhesins and the actin cytoskeleton in apicomplexan parasites. Mol Cell 11: 885-894.
    • (2003) Mol Cell , vol.11 , pp. 885-894
    • Jewett, T.J.1    Sibley, L.D.2
  • 53
    • 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. (2007) Immobilization of the type XIV myosin complex in Toxoplasma gondii. Mol Biol Cell 18: 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
  • 54
    • 33645855615 scopus 로고    scopus 로고
    • Plasmodium falciparum erythrocyte invasion: a conserved myosin associated complex
    • Jones, M.L., Kitson, E.L., and Rayner, J.C. (2006) Plasmodium falciparum erythrocyte invasion: a conserved myosin associated complex. Mol Biochem Parasitol 147: 74-84.
    • (2006) Mol Biochem Parasitol , vol.147 , pp. 74-84
    • Jones, M.L.1    Kitson, E.L.2    Rayner, J.C.3
  • 55
    • 0037460060 scopus 로고    scopus 로고
    • Transformation of sporozoites into early exoerythrocytic malaria parasites does not require host cells
    • Kaiser, K., Camargo, N., and Kappe, S.H. (2003) Transformation of sporozoites into early exoerythrocytic malaria parasites does not require host cells. J Exp Med 197: 1045-1050.
    • (2003) J Exp Med , vol.197 , pp. 1045-1050
    • Kaiser, K.1    Camargo, N.2    Kappe, S.H.3
  • 56
    • 8444241483 scopus 로고    scopus 로고
    • A malaria membrane skeletal protein is essential for normal morphogenesis, motility, and infectivity of sporozoites
    • Khater, E.I., Sinden, R.E., and Dessens, J.T. (2004) A malaria membrane skeletal protein is essential for normal morphogenesis, motility, and infectivity of sporozoites. J Cell Biol 167: 425-432.
    • (2004) J Cell Biol , vol.167 , pp. 425-432
    • Khater, E.I.1    Sinden, R.E.2    Dessens, J.T.3
  • 57
    • 84863084161 scopus 로고    scopus 로고
    • Evolution and architecture of the inner membrane complex in asexual and sexual stages of the malaria parasite
    • Kono, M., Herrmann, S., Loughran, N.B., Cabrera, A., Engelberg, K., Lehmann, C., etal. (2012) Evolution and architecture of the inner membrane complex in asexual and sexual stages of the malaria parasite. Mol Biol Evol 29: 2113-2132.
    • (2012) Mol Biol Evol , vol.29 , pp. 2113-2132
    • Kono, M.1    Herrmann, S.2    Loughran, N.B.3    Cabrera, A.4    Engelberg, K.5    Lehmann, C.6
  • 59
    • 0021918243 scopus 로고
    • Plasmodium gallinaceum: critical role for microtubules in the transformation of zygotes into ookinetes
    • Kumar, N., Aikawa, M., and Grotendorst, C. (1985) Plasmodium gallinaceum: critical role for microtubules in the transformation of zygotes into ookinetes. Exp Parasitol 59: 239-247.
    • (1985) Exp Parasitol , vol.59 , pp. 239-247
    • Kumar, N.1    Aikawa, M.2    Grotendorst, C.3
  • 61
    • 84898408079 scopus 로고    scopus 로고
    • Disruption of TgPHIL1 alters specific parameters of Toxoplasma gondii motility measured in a quantitative, three-dimensional live motility assay
    • Leung, J.M., Rould, M.A., Konradt, C., Hunter, C.A., and Ward, G.E. (2014) Disruption of TgPHIL1 alters specific parameters of Toxoplasma gondii motility measured in a quantitative, three-dimensional live motility assay. PLoS ONE 9: e85763.
    • (2014) PLoS ONE , vol.9
    • Leung, J.M.1    Rould, M.A.2    Konradt, C.3    Hunter, C.A.4    Ward, G.E.5
  • 62
    • 84855261963 scopus 로고    scopus 로고
    • Deficiency of a Niemann-Pick, type C1-related protein in toxoplasma is associated with multiple lipidoses and increased pathogenicity
    • Lige, B., Romano, J.D., Bandaru, V.V., Ehrenman, K., Levitskaya, J., Sampels, V., etal. (2011) Deficiency of a Niemann-Pick, type C1-related protein in toxoplasma is associated with multiple lipidoses and increased pathogenicity. PLoS Pathog 7: e1002410.
    • (2011) PLoS Pathog , vol.7
    • Lige, B.1    Romano, J.D.2    Bandaru, V.V.3    Ehrenman, K.4    Levitskaya, J.5    Sampels, V.6
  • 63
    • 77957894835 scopus 로고    scopus 로고
    • A Toxoplasma MORN1 null mutant undergoes repeated divisions but is defective in basal assembly, apicoplast division and cytokinesis
    • Lorestani, A., Sheiner, L., Yang, K., Robertson, S.D., Sahoo, N., Brooks, C.F., etal. (2010) A Toxoplasma MORN1 null mutant undergoes repeated divisions but is defective in basal assembly, apicoplast division and cytokinesis. PLoS ONE 5: e12302.
    • (2010) PLoS ONE , vol.5
    • Lorestani, A.1    Sheiner, L.2    Yang, K.3    Robertson, S.D.4    Sahoo, N.5    Brooks, C.F.6
  • 66
    • 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. (2001) Characterization of the subpellicular network, a filamentous membrane skeletal component in the parasite Toxoplasma gondii. Mol Biochem Parasitol 115: 257-268.
    • (2001) Mol Biochem Parasitol , vol.115 , pp. 257-268
    • Mann, T.1    Beckers, C.2
  • 67
    • 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. (2002) Proteolytic processing of TgIMC1 during maturation of the membrane skeleton of Toxoplasma gondii. J Biol Chem 277: 41240-41246.
    • (2002) J Biol Chem , vol.277 , pp. 41240-41246
    • Mann, T.1    Gaskins, E.2    Beckers, C.3
  • 68
    • 0021837134 scopus 로고
    • Transformation of sporozoites of Plasmodium berghei into exoerythrocytic forms in the liver of its mammalian host
    • Meis, J.F., Verhave, J.P., Jap, P.H., and Meuwissen, J.H. (1985) Transformation of sporozoites of Plasmodium berghei into exoerythrocytic forms in the liver of its mammalian host. Cell Tissue Res 241: 353-360.
    • (1985) Cell Tissue Res , vol.241 , pp. 353-360
    • Meis, J.F.1    Verhave, J.P.2    Jap, P.H.3    Meuwissen, J.H.4
  • 69
    • 0019951595 scopus 로고
    • Plasmodium berghei: architectural analysis by freeze-fracturing of the intraoocyst sporozoite's pellicular system
    • Meszoely, C.A., Erbe, E.F., Steere, R.L., Pacheco, N.D., and Beaudoin, R.L. (1982) Plasmodium berghei: architectural analysis by freeze-fracturing of the intraoocyst sporozoite's pellicular system. Exp Parasitol 53: 229-241.
    • (1982) Exp Parasitol , vol.53 , pp. 229-241
    • Meszoely, C.A.1    Erbe, E.F.2    Steere, R.L.3    Pacheco, N.D.4    Beaudoin, R.L.5
  • 70
    • 48749099075 scopus 로고    scopus 로고
    • Toxoplasma gondii Hsp20 is a stripe-arranged chaperone-like protein associated with the outer leaflet of the inner membrane complex
    • de Miguel, N., Lebrun, M., Heaslip, A., Hu, K., Beckers, C.J., Matrajt, M., etal. (2008) Toxoplasma gondii Hsp20 is a stripe-arranged chaperone-like protein associated with the outer leaflet of the inner membrane complex. Biol Cell 100: 479-489.
    • (2008) Biol Cell , vol.100 , pp. 479-489
    • de Miguel, N.1    Lebrun, M.2    Heaslip, A.3    Hu, K.4    Beckers, C.J.5    Matrajt, M.6
  • 73
    • 0036193424 scopus 로고    scopus 로고
    • Cytoskeleton of apicomplexan parasites
    • table of contents.
    • Morrissette, N.S., and Sibley, L.D. (2002) Cytoskeleton of apicomplexan parasites. Microbiol Mol Biol Rev 66: 21-38, table of contents.
    • (2002) Microbiol Mol Biol Rev , vol.66 , pp. 21-38
    • Morrissette, N.S.1    Sibley, L.D.2
  • 74
    • 0031018273 scopus 로고    scopus 로고
    • Subpellicular microtubules associate with an intramembranous particle lattice in the protozoan parasite Toxoplasma gondii
    • Morrissette, N.S., Murray, J.M., and Roos, D.S. (1997) Subpellicular microtubules associate with an intramembranous particle lattice in the protozoan parasite Toxoplasma gondii. J Cell Sci 110 (Part 1): 35-42.
    • (1997) J Cell Sci , vol.110 , pp. 35-42
    • Morrissette, N.S.1    Murray, J.M.2    Roos, D.S.3
  • 75
    • 80053458415 scopus 로고    scopus 로고
    • Quantitative in vivo analyses reveal calcium-dependent phosphorylation sites and identifies a novel component of the Toxoplasma invasion motor complex
    • Nebl, T., Prieto, J.H., Kapp, E., Smith, B.J., Williams, M.J., Yates, J.R., 3rd, etal. (2011) Quantitative in vivo analyses reveal calcium-dependent phosphorylation sites and identifies a novel component of the Toxoplasma invasion motor complex. PLoS Pathog 7: e1002222.
    • (2011) PLoS Pathog , vol.7
    • Nebl, T.1    Prieto, J.H.2    Kapp, E.3    Smith, B.J.4    Williams, M.J.5    Yates III, J.R.6
  • 76
    • 0036372942 scopus 로고    scopus 로고
    • 'The glideosome': a dynamic complex powering gliding motion and host cell invasion by Toxoplasma gondii
    • Opitz, C., and Soldati, D. (2002) 'The glideosome': a dynamic complex powering gliding motion and host cell invasion by Toxoplasma gondii. Mol Microbiol 45: 597-604.
    • (2002) Mol Microbiol , vol.45 , pp. 597-604
    • Opitz, C.1    Soldati, D.2
  • 77
    • 84866007554 scopus 로고    scopus 로고
    • A unique Kelch domain phosphatase in Plasmodium regulates ookinete morphology, motility and invasion
    • Philip, N., Vaikkinen, H.J., Tetley, L., and Waters, A.P. (2012) A unique Kelch domain phosphatase in Plasmodium regulates ookinete morphology, motility and invasion. PLoS ONE 7: e44617.
    • (2012) PLoS ONE , vol.7
    • Philip, N.1    Vaikkinen, H.J.2    Tetley, L.3    Waters, A.P.4
  • 78
    • 84885411475 scopus 로고    scopus 로고
    • The role of clathrin in post-Golgi trafficking in Toxoplasma gondii
    • Pieperhoff, M.S., Schmitt, M., Ferguson, D.J., and Meissner, M. (2013) The role of clathrin in post-Golgi trafficking in Toxoplasma gondii. PLoS ONE 8: e77620.
    • (2013) PLoS ONE , vol.8
    • Pieperhoff, M.S.1    Schmitt, M.2    Ferguson, D.J.3    Meissner, M.4
  • 79
  • 80
    • 0017649751 scopus 로고
    • [Freeze fracture study of Toxoplasma and Sarcocystis infective stages]
    • (author's transl.).
    • Porchet, E., and Torpier, G. (1977) [Freeze fracture study of Toxoplasma and Sarcocystis infective stages] (author's transl.). Z Parasitenkd 54: 101-124.
    • (1977) Z Parasitenkd , vol.54 , pp. 101-124
    • Porchet, E.1    Torpier, G.2
  • 81
    • 84978538778 scopus 로고    scopus 로고
    • Unique apicomplexan IMC sub-compartment proteins are early markers for apical polarity in the malaria parasite
    • Poulin, B., Patzewitz, E.M., Brady, D., Silvie, O., Wright, M.H., Ferguson, D.J., etal. (2013) Unique apicomplexan IMC sub-compartment proteins are early markers for apical polarity in the malaria parasite. Biol Open 2: 1160-1170.
    • (2013) Biol Open , vol.2 , pp. 1160-1170
    • Poulin, B.1    Patzewitz, E.M.2    Brady, D.3    Silvie, O.4    Wright, M.H.5    Ferguson, D.J.6
  • 82
    • 0035782679 scopus 로고    scopus 로고
    • Cryofracture electron microscopy of the ookinete pellicle of Plasmodium gallinaceum reveals the existence of novel pores in the alveolar membranes
    • Raibaud, A., Lupetti, P., Paul, R.E., Mercati, D., Brey, P.T., Sinden, R.E., etal. (2001) Cryofracture electron microscopy of the ookinete pellicle of Plasmodium gallinaceum reveals the existence of novel pores in the alveolar membranes. J Struct Biol 135: 47-57.
    • (2001) J Struct Biol , vol.135 , pp. 47-57
    • Raibaud, A.1    Lupetti, P.2    Paul, R.E.3    Mercati, D.4    Brey, P.T.5    Sinden, R.E.6
  • 85
    • 84859152006 scopus 로고    scopus 로고
    • Subcellular location, phosphorylation and assembly into the motor complex of GAP45 during Plasmodium falciparum schizont development
    • Ridzuan, M.A., Moon, R.W., Knuepfer, E., Black, S., Holder, A.A., and Green, J.L. (2012) Subcellular location, phosphorylation and assembly into the motor complex of GAP45 during Plasmodium falciparum schizont development. PLoS ONE 7: e33845.
    • (2012) PLoS ONE , vol.7
    • Ridzuan, M.A.1    Moon, R.W.2    Knuepfer, E.3    Black, S.4    Holder, A.A.5    Green, J.L.6
  • 86
    • 84870986452 scopus 로고    scopus 로고
    • A Plasmodium calcium-dependent protein kinase controls zygote development and transmission by translationally activating repressed mRNAs
    • Sebastian, S., Brochet, M., Collins, M.O., Schwach, F., Jones, M.L., Goulding, D., etal. (2012) A Plasmodium calcium-dependent protein kinase controls zygote development and transmission by translationally activating repressed mRNAs. Cell Host Microbe 12: 9-19.
    • (2012) Cell Host Microbe , vol.12 , pp. 9-19
    • Sebastian, S.1    Brochet, M.2    Collins, M.O.3    Schwach, F.4    Jones, M.L.5    Goulding, D.6
  • 87
    • 0014271555 scopus 로고
    • The fine structure and reproduction of Toxoplasma gondii
    • Sheffield, H.G., and Melton, M.L. (1968) The fine structure and reproduction of Toxoplasma gondii. J Parasitol 54: 209-226.
    • (1968) J Parasitol , vol.54 , pp. 209-226
    • Sheffield, H.G.1    Melton, M.L.2
  • 88
    • 0020047689 scopus 로고
    • Gametocytogenesis of Plasmodium falciparum in vitro: an electron microscopic study
    • Sinden, R.E. (1982) Gametocytogenesis of Plasmodium falciparum in vitro: an electron microscopic study. Parasitology 84: 1-11.
    • (1982) Parasitology , vol.84 , pp. 1-11
    • Sinden, R.E.1
  • 89
    • 0020635478 scopus 로고
    • The cell biology of sexual development in plasmodium
    • Sinden, R.E. (1983) The cell biology of sexual development in plasmodium. Parasitology 86 (Part 4): 7-28.
    • (1983) Parasitology , vol.86 , Issue.PART 4 , pp. 7-28
    • Sinden, R.E.1
  • 91
    • 0030745648 scopus 로고    scopus 로고
    • TRAP is necessary for gliding motility and infectivity of plasmodium sporozoites
    • Sultan, A.A., Thathy, V., Frevert, U., Robson, K.J., Crisanti, A., Nussenzweig, V., etal. (1997) TRAP is necessary for gliding motility and infectivity of plasmodium sporozoites. Cell 90: 511-522.
    • (1997) Cell , vol.90 , pp. 511-522
    • Sultan, A.A.1    Thathy, V.2    Frevert, U.3    Robson, K.J.4    Crisanti, A.5    Nussenzweig, V.6
  • 92
    • 84860486844 scopus 로고    scopus 로고
    • Regulation of Plasmodium falciparum glideosome associated protein 45 (PfGAP45) phosphorylation
    • Thomas, D.C., Ahmed, A., Gilberger, T.W., and Sharma, P. (2012) Regulation of Plasmodium falciparum glideosome associated protein 45 (PfGAP45) phosphorylation. PLoS ONE 7: e35855.
    • (2012) PLoS ONE , vol.7
    • Thomas, D.C.1    Ahmed, A.2    Gilberger, T.W.3    Sharma, P.4
  • 93
    • 84887272711 scopus 로고    scopus 로고
    • Protein trafficking through the endosomal system prepares intracellular parasites for a home invasion
    • Tomavo, S., Slomianny, C., Meissner, M., and Carruthers, V.B. (2013) Protein trafficking through the endosomal system prepares intracellular parasites for a home invasion. PLoS Pathog 9: e1003629.
    • (2013) PLoS Pathog , vol.9
    • Tomavo, S.1    Slomianny, C.2    Meissner, M.3    Carruthers, V.B.4
  • 94
    • 79953130552 scopus 로고    scopus 로고
    • Malaria IMC1 membrane skeleton proteins operate autonomously and participate in motility independently of cell shape
    • Tremp, A.Z., and Dessens, J.T. (2011) Malaria IMC1 membrane skeleton proteins operate autonomously and participate in motility independently of cell shape. J Biol Chem 286: 5383-5391.
    • (2011) J Biol Chem , vol.286 , pp. 5383-5391
    • Tremp, A.Z.1    Dessens, J.T.2
  • 95
    • 55549099256 scopus 로고    scopus 로고
    • IMC1b is a putative membrane skeleton protein involved in cell shape, mechanical strength, motility, and infectivity of malaria ookinetes
    • Tremp, A.Z., Khater, E.I., and Dessens, J.T. (2008) IMC1b is a putative membrane skeleton protein involved in cell shape, mechanical strength, motility, and infectivity of malaria ookinetes. J Biol Chem 283: 27604-27611.
    • (2008) J Biol Chem , vol.283 , pp. 27604-27611
    • Tremp, A.Z.1    Khater, E.I.2    Dessens, J.T.3
  • 96
    • 84880835209 scopus 로고    scopus 로고
    • Morphogenesis of Plasmodium zoites is uncoupled from tensile strength
    • Tremp, A.Z., Carter, V., Saeed, S., and Dessens, J.T. (2013) Morphogenesis of Plasmodium zoites is uncoupled from tensile strength. Mol Microbiol 89: 552-564.
    • (2013) Mol Microbiol , vol.89 , pp. 552-564
    • Tremp, A.Z.1    Carter, V.2    Saeed, S.3    Dessens, J.T.4
  • 97
    • 0036076262 scopus 로고    scopus 로고
    • Clostridium septicum alpha-toxin is active against the parasitic protozoan Toxoplasma gondii and targets members of the SAG family of glycosylphosphatidylinositol-anchored surface proteins
    • Wichroski, M.J., Melton, J.A., Donahue, C.G., Tweten, R.K., and Ward, G.E. (2002) Clostridium septicum alpha-toxin is active against the parasitic protozoan Toxoplasma gondii and targets members of the SAG family of glycosylphosphatidylinositol-anchored surface proteins. Infect Immun 70: 4353-4361.
    • (2002) Infect Immun , vol.70 , pp. 4353-4361
    • Wichroski, M.J.1    Melton, J.A.2    Donahue, C.G.3    Tweten, R.K.4    Ward, G.E.5
  • 98
    • 79955368787 scopus 로고    scopus 로고
    • Tracking Glideosome-associated protein 50 reveals the development and organization of the inner membrane complex of Plasmodium falciparum
    • Yeoman, J.A., Hanssen, E., Maier, A.G., Klonis, N., Maco, B., Baum, J., etal. (2011) Tracking Glideosome-associated protein 50 reveals the development and organization of the inner membrane complex of Plasmodium falciparum. Eukaryot Cell 10: 556-564.
    • (2011) Eukaryot Cell , vol.10 , pp. 556-564
    • Yeoman, J.A.1    Hanssen, E.2    Maier, A.G.3    Klonis, N.4    Maco, B.5    Baum, J.6


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