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Volumn 47, Issue , 2008, Pages 110-120

Actin/myosin-based gliding motility in apicomplexan parasites

Author keywords

[No Author keywords available]

Indexed keywords

EUKARYOTA; PROKARYOTA;

EID: 46249100459     PISSN: 03060225     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-0-387-78267-6_9     Document Type: Article
Times cited : (20)

References (77)
  • 1
    • 0346122785 scopus 로고    scopus 로고
    • The cytoskeleton and motility in apicomplexan invasion
    • Fowler RE, Margos G, Mitchell GH. The cytoskeleton and motility in apicomplexan invasion. Adv Parasitol 2004; 56:213-263.
    • (2004) Adv Parasitol , vol.56 , pp. 213-263
    • Fowler, R.E.1    Margos, G.2    Mitchell, G.H.3
  • 2
    • 33747887924 scopus 로고    scopus 로고
    • Cellular and molecular mechanics of gliding locomotion in eukaryotes
    • Heintzelman MB. Cellular and molecular mechanics of gliding locomotion in eukaryotes. Int Rev Cytol 2006; 251:79-129.
    • (2006) Int Rev Cytol , vol.251 , pp. 79-129
    • Heintzelman, M.B.1
  • 3
    • 0347990475 scopus 로고    scopus 로고
    • Apicomplexan gliding motility and host cell invasion: Overhauling the motor model
    • Kappe SH, Buscaglia CA, Bergman LW et al. Apicomplexan gliding motility and host cell invasion: Overhauling the motor model. Trends Parasitol 2004; 20(1): 13-16.
    • (2004) Trends Parasitol , vol.20 , Issue.1 , pp. 13-16
    • Kappe, S.H.1    Buscaglia, C.A.2    Bergman, L.W.3
  • 4
    • 1842482437 scopus 로고    scopus 로고
    • Intracellular parasite invasion strategies
    • Sibley LD. Intracellular parasite invasion strategies. Science 2004; 304(5668):248-253.
    • (2004) Science , vol.304 , Issue.5668 , pp. 248-253
    • Sibley, L.D.1
  • 5
    • 4143134292 scopus 로고    scopus 로고
    • Intravital microscopy demonstrating antibody-mediated immobilization of Plasmodium berghei sporozoites injected into skin by mosquitoes
    • Vanderberg JP, Frevert U. Intravital microscopy demonstrating antibody-mediated immobilization of Plasmodium berghei sporozoites injected into skin by mosquitoes. Int J Parasitol 2004; 34(9):991-996.
    • (2004) Int J Parasitol , vol.34 , Issue.9 , pp. 991-996
    • Vanderberg, J.P.1    Frevert, U.2
  • 6
    • 32244448982 scopus 로고    scopus 로고
    • Quantitative imaging of Plasmodium transmission from mosquito to mammal
    • Amino R, Thiberge S, Martin B et al. Quantitative imaging of Plasmodium transmission from mosquito to mammal. Nat Med 2006; 12:220-224.
    • (2006) Nat Med , vol.12 , pp. 220-224
    • Amino, R.1    Thiberge, S.2    Martin, B.3
  • 7
    • 22744456850 scopus 로고    scopus 로고
    • Intravital observation of Plasmodium berghei sporozoite infection of the liver
    • Frevert U, Engelmann S, Zougbd S et al. Intravital observation of Plasmodium berghei sporozoite infection of the liver. PLoS Biol 2005; 3(6):el92.
    • (2005) PLoS Biol , vol.3 , Issue.6
    • Frevert, U.1    Engelmann, S.2    Zougbd, S.3
  • 8
    • 0037124340 scopus 로고    scopus 로고
    • Transepithelial migration of Toxoplasma gondii is linked to parasite motility and virulence
    • Barragan A, Sibley LD. Transepithelial migration of Toxoplasma gondii is linked to parasite motility and virulence. J Exp Med 2002; 195(12):1625-1633.
    • (2002) J Exp Med , vol.195 , Issue.12 , pp. 1625-1633
    • Barragan, A.1    Sibley, L.D.2
  • 9
    • 0042825888 scopus 로고    scopus 로고
    • Migration of Toxoplasma gondii across biological barriers
    • Barragan A, Sibley LD. Migration of Toxoplasma gondii across biological barriers. Trends Microbiol 2003; ll(9):426-430.
    • (2003) Trends Microbiol , vol.11 , Issue.9 , pp. 426-430
    • Barragan, A.1    Sibley, L.D.2
  • 10
    • 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. Eur J Cell Biol 1997; 73(2):114-123.
    • (1997) Eur J Cell Biol , vol.73 , Issue.2 , pp. 114-123
    • Carruthers, V.B.1    Sibley, L.D.2
  • 11
    • 24644441368 scopus 로고    scopus 로고
    • The comings and goings of actin: Coupling protrusion and retraction in cell motility
    • Small JV, Resch GP. The comings and goings of actin: Coupling protrusion and retraction in cell motility. Curr Opin Cell Biol 2005; 17(5):517-523.
    • (2005) Curr Opin Cell Biol , vol.17 , Issue.5 , pp. 517-523
    • Small, J.V.1    Resch, G.P.2
  • 13
    • 0019605349 scopus 로고
    • The role of the cytoskeleton in the motility of coccidian sporozoites
    • Russell DG, Sinden RE. The role of the cytoskeleton in the motility of coccidian sporozoites. J Cell Sci 1981; 50:345-359.
    • (1981) J Cell Sci , vol.50 , pp. 345-359
    • Russell, D.G.1    Sinden, R.E.2
  • 14
    • 0023768222 scopus 로고
    • Cell motility of sporozoan protozoa
    • King CA. Cell motility of sporozoan protozoa. Parasitol Today 1988; 4(11):315-319.
    • (1988) Parasitol Today , vol.4 , Issue.11 , pp. 315-319
    • King, C.A.1
  • 15
    • 0016276337 scopus 로고
    • Studies on the motility of Plasmodium sporozoites
    • Vanderberg JP. Studies on the motility of Plasmodium sporozoites. J Protozool 1974; 21(4):527-537.
    • (1974) J Protozool , vol.21 , Issue.4 , pp. 527-537
    • Vanderberg, J.P.1
  • 16
    • 0016669543 scopus 로고
    • Development of infectivity by the Plasmodium berghei sporozoite
    • Vanderberg JP. Development of infectivity by the Plasmodium berghei sporozoite. J Parasitol 1975; 61(1):43-50.
    • (1975) J Parasitol , vol.61 , Issue.1 , pp. 43-50
    • Vanderberg, J.P.1
  • 17
    • 3042667026 scopus 로고    scopus 로고
    • Imsing movement of malaria parasites during transmission by Anopheles mosquitoes
    • Frischknecht F, Baldacci P, Martin B et al. Imsing movement of malaria parasites during transmission by Anopheles mosquitoes. Cell Microbiol 2004; 6(7):687-694.
    • (2004) Cell Microbiol , vol.6 , Issue.7 , pp. 687-694
    • Frischknecht, F.1    Baldacci, P.2    Martin, B.3
  • 18
    • 0343162619 scopus 로고    scopus 로고
    • Time-lapse video microscopy of gliding motility in Toxoplasma gondii reveals a novel, biphasic mechanism of cell locomotion
    • Hakansson S, Morisaki H, Heuser J et al. Time-lapse video microscopy of gliding motility in Toxoplasma gondii reveals a novel, biphasic mechanism of cell locomotion. Mol Biol Cell 1999; 10(11):3539-3547.
    • (1999) Mol Biol Cell , vol.10 , Issue.11 , pp. 3539-3547
    • Hakansson, S.1    Morisaki, H.2    Heuser, J.3
  • 19
    • 3042676622 scopus 로고    scopus 로고
    • Real-time, in vivo analysis of malaria ookinete locomotion and mosquito midgut invasion
    • Vlachou D, Zimmermann T, Cantera R et al. Real-time, in vivo analysis of malaria ookinete locomotion and mosquito midgut invasion. Cell Microbiol 2004; 6(7):671-685.
    • (2004) Cell Microbiol , vol.6 , Issue.7 , pp. 671-685
    • Vlachou, D.1    Zimmermann, T.2    Cantera, R.3
  • 20
    • 0025602648 scopus 로고
    • Plasmodium sporozoite interactions with macrophages in vitro: A videomicroscopic analysis
    • Vanderberg JP, Chew S, Stewart MJ. Plasmodium sporozoite interactions with macrophages in vitro: A videomicroscopic analysis. J Protozool 1990; 37(6):528-536.
    • (1990) J Protozool , vol.37 , Issue.6 , pp. 528-536
    • Vanderberg, J.P.1    Chew, S.2    Stewart, M.J.3
  • 21
    • 0035808562 scopus 로고    scopus 로고
    • Migration of Plasmodium sporozoites through cells before infection
    • Mota MM, Pradel G, Vanderberg JP et al. Migration of Plasmodium sporozoites through cells before infection. Science 2001; 291(5501):l4l-l44.
    • (2001) Science , vol.291 , Issue.5501 , pp. 141-144
    • Mota, M.M.1    Pradel, G.2    Vanderberg, J.P.3
  • 22
    • 49749086211 scopus 로고    scopus 로고
    • Pulling together: An integrated model of Toxoplasma cell invasion
    • Carruthers V, Boothroyd JC. Pulling together: An integrated model of Toxoplasma cell invasion. Curr Opin Microbiol 2006; 9:1-7.
    • (2006) Curr Opin Microbiol , vol.9 , pp. 1-7
    • Carruthers, V.1    Boothroyd, J.C.2
  • 24
    • 0035400296 scopus 로고    scopus 로고
    • Characterization of the subpeUicular network, a filamentous membrane skeletal component in the parasite Toxoplasma gondii
    • Mann T, Beckers C. Characterization of the subpeUicular network, a filamentous membrane skeletal component in the parasite Toxoplasma gondii. Mol Biochem Parasitol 2001; 115(2):257-268.
    • (2001) Mol Biochem Parasitol , vol.115 , Issue.2 , pp. 257-268
    • Mann, T.1    Beckers, C.2
  • 25
    • 0031018273 scopus 로고    scopus 로고
    • SubpeUicular microtubules associate with an intramembranous particle lattice in the protozoan parasite Toxoplasma gondii
    • Morrissette NS, Murray JM, Roos DS. SubpeUicular microtubules associate with an intramembranous particle lattice in the protozoan parasite Toxoplasma gondii. J Cell Sci 1997; 110(Pt l):35-42.
    • (1997) J Cell Sci , vol.110 , pp. 35-42
    • Morrissette, N.S.1    Murray, J.M.2    Roos, D.S.3
  • 26
    • 33645767721 scopus 로고    scopus 로고
    • Cytoskeletal components of an invasion machine-the apical complex of Toxoplasma gondii
    • Hu K, Johnson J, Florens L et al. Cytoskeletal components of an invasion machine-the apical complex of Toxoplasma gondii. PLoS Pathog 2006; 2(2):el3.
    • (2006) PLoS Pathog , vol.2 , Issue.2
    • Hu, K.1    Johnson, J.2    Florens, L.3
  • 27
    • 0037174664 scopus 로고    scopus 로고
    • Role of Toxoplasma gondii myosin A in powering parasite gliding and host cell invasion
    • Meissner M, Schliiter D, Soldati D. Role of Toxoplasma gondii myosin A in powering parasite gliding and host cell invasion. Science 2002; 298(5594):837-840.
    • (2002) Science , vol.298 , Issue.5594 , pp. 837-840
    • Meissner, M.1    Schliiter, D.2    Soldati, D.3
  • 28
    • 0031559564 scopus 로고    scopus 로고
    • A novel class of unconventional myosins from Toxoplasma gondii
    • Heintzelman MB, Schwartzman JD. A novel class of unconventional myosins from Toxoplasma gondii. J Mol Biol 1997; 271(1):139-146.
    • (1997) J Mol Biol , vol.271 , Issue.1 , pp. 139-146
    • Heintzelman, M.B.1    Schwartzman, J.D.2
  • 29
    • 33644856260 scopus 로고    scopus 로고
    • New insights into myosin evolution and classification
    • Foth BJ, Goedecke MC, Soldati D. New insights into myosin evolution and classification. Proc Natl Acad Sci USA 2006; 103(10):3681-3686.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.10 , pp. 3681-3686
    • Foth, B.J.1    Goedecke, M.C.2    Soldati, D.3
  • 30
    • 18344362027 scopus 로고    scopus 로고
    • Toxoplasma gondii myosin A and its Ught chain: A fast, single-headed, plus-end-directed motor
    • Herm-Gotz A, Weiss S, Stratmann R et al. Toxoplasma gondii myosin A and its Ught chain: A fast, single-headed, plus-end-directed motor. EMBO J 2002; 21(9):2149-2158.
    • (2002) EMBO J , vol.21 , Issue.9 , pp. 2149-2158
    • Herm-Gotz, A.1    Weiss, S.2    Stratmann, R.3
  • 31
    • 0032559349 scopus 로고    scopus 로고
    • Unconventional myosins in cell movement, membrane traffic, and signal transduction
    • Mermall V, Post PL, Mooseker MS. Unconventional myosins in cell movement, membrane traffic, and signal transduction. Science 1998; 279(5350):527-533.
    • (1998) Science , vol.279 , Issue.5350 , pp. 527-533
    • Mermall, V.1    Post, P.L.2    Mooseker, M.S.3
  • 32
    • 2442528540 scopus 로고    scopus 로고
    • Identification of the membrane receptor of a class XIV myosin in Toxoplasma gondii
    • Gaskins E, Gilk S, DeVore N et al. Identification of the membrane receptor of a class XIV myosin in Toxoplasma gondii. J Cell Biol 2004; 165(3):383-393.
    • (2004) J Cell Biol , vol.165 , Issue.3 , pp. 383-393
    • Gaskins, E.1    Gilk, S.2    DeVore, N.3
  • 33
    • 0037242399 scopus 로고    scopus 로고
    • Myosin A tail domain interacting protein (MTIP) localizes to the inner membrane complex of Plasmodium sporozoites
    • Bergman LW, Kaiser K, Fujioka H et al. Myosin A tail domain interacting protein (MTIP) localizes to the inner membrane complex of Plasmodium sporozoites. J Cell Sci 2003; 116(Pt l):39-49.
    • (2003) J Cell Sci , vol.116 , pp. 39-49
    • Bergman, L.W.1    Kaiser, K.2    Fujioka, H.3
  • 34
    • 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 et al. A conserved molecular motor drives cell invasion and gliding motility across malaria life cycle stages and other apicomplexan parasites. J Biol Chem 2006; 281(8):5197-5208.
    • (2006) J Biol Chem , vol.281 , Issue.8 , pp. 5197-5208
    • Baum, J.1    Richard, D.2    Healer, J.3
  • 35
    • 29444442923 scopus 로고    scopus 로고
    • The MTIP-myosin A complex in blood stage malaria parasites
    • Green JL, Martin SR, Fielden J et al. The MTIP-myosin A complex in blood stage malaria parasites. J Mol Biol 2006; 355(5):933-94l.
    • (2006) J Mol Biol , vol.355 , Issue.5 , pp. 933-941
    • Green, J.L.1    Martin, S.R.2    Fielden, J.3
  • 36
    • 33645855615 scopus 로고    scopus 로고
    • Plasmodium falciparum erythrocyte invasion: A conserved myosin associated complex
    • Jones ML, Kitson EL, Rayner JC. Plasmodium falciparum erythrocyte invasion: A conserved myosin associated complex. Mol Biochem Parasitol 2006; l47(1):74-84.
    • (2006) Mol Biochem Parasitol , vol.147 , Issue.1 , pp. 74-84
    • Jones, M.L.1    Kitson, E.L.2    Rayner, J.C.3
  • 37
    • 33645531531 scopus 로고    scopus 로고
    • Structure of the MTIP-MyoA complex, a key component of the malaria parasite invasion motor
    • Bosch J, Turley S, Daly TM et al. Structure of the MTIP-MyoA complex, a key component of the malaria parasite invasion motor. Proc Natl Acad Sci USA 2006; 103(13):4852-4857.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.13 , pp. 4852-4857
    • Bosch, J.1    Turley, S.2    Daly, T.M.3
  • 38
    • 0029869791 scopus 로고    scopus 로고
    • Toxoplasma invasion of mammalian cells is powered by the actin cytoskeleton of the parasite
    • Dobrowolski JM, Sibley LD. Toxoplasma invasion of mammalian cells is powered by the actin cytoskeleton of the parasite. Cell 1996; 84(6):933-939.
    • (1996) Cell , vol.84 , Issue.6 , pp. 933-939
    • Dobrowolski, J.M.1    Sibley, L.D.2
  • 39
    • 0018777194 scopus 로고
    • Interaction between cytochalasin B-treated malarial parasites and erythrocytes: Attachment and junction formation
    • Miller LH, Aikawa M, Johnson JG et al. Interaction between cytochalasin B-treated malarial parasites and erythrocytes: Attachment and junction formation. J Exp Med 1979; 149(1):172-184.
    • (1979) J Exp Med , vol.149 , Issue.1 , pp. 172-184
    • Miller, L.H.1    Aikawa, M.2    Johnson, J.G.3
  • 40
    • 0041738315 scopus 로고    scopus 로고
    • Structural evidence for actin-like filaments in Toxoplasma gondii using high-resolution low-voltage field emission scanning electron microscopy
    • Schatten H, Sibley LD, Ris H. Structural evidence for actin-like filaments in Toxoplasma gondii using high-resolution low-voltage field emission scanning electron microscopy. Microsc Microanal 2003; 9(4):330-335.
    • (2003) Microsc Microanal , vol.9 , Issue.4 , pp. 330-335
    • Schatten, H.1    Sibley, L.D.2    Ris, H.3
  • 41
    • 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 et al. Unusual kinetic and structural properties control rapid assembly and turnover of actin in the parasite Toxoplasma gondii. Mol Biol Cell 2006; 17(2):895-906.
    • (2006) Mol Biol Cell , vol.17 , Issue.2 , pp. 895-906
    • Sahoo, N.1    Beatty, W.2    Heuser, J.3
  • 42
    • 18144412735 scopus 로고    scopus 로고
    • Malaria parasite actin filaments are very short
    • Schmitz S, Grainger M, Howell S et al. Malaria parasite actin filaments are very short. J Mol Biol 2005; 349(1):113-125.
    • (2005) J Mol Biol , vol.349 , Issue.1 , pp. 113-125
    • Schmitz, S.1    Grainger, M.2    Howell, S.3
  • 43
    • 12744272468 scopus 로고    scopus 로고
    • Unusual properties of Plasmodium falciparum actin: New insights into microfilament dynamics of apicomplexan parasites
    • Schiller H, Mueller AK, Matuschewski K. Unusual properties of Plasmodium falciparum actin: New insights into microfilament dynamics of apicomplexan parasites. FEBS Lett 2005; 579(3):655-660.
    • (2005) FEBS Lett , vol.579 , Issue.3 , pp. 655-660
    • Schiller, H.1    Mueller, A.K.2    Matuschewski, K.3
  • 44
    • 33645072710 scopus 로고    scopus 로고
    • Plasmodium motility: Actin not actin' like actin
    • Schiller H, Matuschewski K. Plasmodium motility: Actin not actin' like actin. Trends Parasitol 2006; 22(4):146-147.
    • (2006) Trends Parasitol , vol.22 , Issue.4 , pp. 146-147
    • Schiller, H.1    Matuschewski, K.2
  • 45
    • 33749515928 scopus 로고    scopus 로고
    • Regulation of apicomplexan microfilament dynamics by a minimal set of actin-binding proteins
    • Schiller H, Matuschewski K. Regulation of apicomplexan microfilament dynamics by a minimal set of actin-binding proteins. Traffic 2006; 7(11):1433-1439.
    • (2006) Traffic , vol.7 , Issue.11 , pp. 1433-1439
    • Schiller, H.1    Matuschewski, K.2
  • 46
    • 0038637915 scopus 로고    scopus 로고
    • Aldolase forms a bridge between cell surface adhesins and the actin cytoskeleton in apicomplexan parasites
    • Jewett TJ, Sibley LD. Aldolase forms a bridge between cell surface adhesins and the actin cytoskeleton in apicomplexan parasites. Mol Cell 2003; ll(4):885-894.
    • (2003) Mol Cell , vol.11 , Issue.4 , pp. 885-894
    • Jewett, T.J.1    Sibley, L.D.2
  • 47
    • 0344875493 scopus 로고    scopus 로고
    • Sites of interaction between aldolase and thrombospondin-related anonymous protein in Plasmodium
    • Buscaglia CA, Coppens I, Hoi WG et al. Sites of interaction between aldolase and thrombospondin-related anonymous protein in Plasmodium. Mol Biol Cell 2003; l4(12):4947-4957.
    • (2003) Mol Biol Cell , vol.14 , Issue.12 , pp. 4947-4957
    • Buscaglia, C.A.1    Coppens, I.2    Hoi, W.G.3
  • 48
    • 33747189218 scopus 로고    scopus 로고
    • Regulation of apicomplexan actin-based motility
    • Baum J, Papenfuss AT, Baum B et al. Regulation of apicomplexan actin-based motility. Nat Rev Microbiol 2006; 4(8):621-628.
    • (2006) Nat Rev Microbiol , vol.4 , Issue.8 , pp. 621-628
    • Baum, J.1    Papenfuss, A.T.2    Baum, B.3
  • 49
    • 24344440631 scopus 로고    scopus 로고
    • A Plasmodium actin-depolymerizing factor that binds exclusively to actin monomers
    • Schiller H, Mueller AK, Matuschewski K. A Plasmodium actin-depolymerizing factor that binds exclusively to actin monomers. Mol Biol Cell 2005; 16(9):4013-4023.
    • (2005) Mol Biol Cell , vol.16 , Issue.9 , pp. 4013-4023
    • Schiller, H.1    Mueller, A.K.2    Matuschewski, K.3
  • 50
    • 0023741661 scopus 로고
    • A highly conserved amino-acid sequence in thrombospondin, properdin and in proteins from sporozoites and blood stages of a human malaria parasite
    • Robson KJ, Hall JR, Jennings MW et al. A highly conserved amino-acid sequence in thrombospondin, properdin and in proteins from sporozoites and blood stages of a human malaria parasite. Nature 1988; 335(6185):79-82.
    • (1988) Nature , vol.335 , Issue.6185 , pp. 79-82
    • Robson, K.J.1    Hall, J.R.2    Jennings, M.W.3
  • 51
    • 0035019694 scopus 로고    scopus 로고
    • Mix and match modules: Structure and function of microneme proteins in apicomplexan parasites
    • Tomley FM, Soldati DS, Mix and match modules: Structure and function of microneme proteins in apicomplexan parasites. Trends Parasitol 2001; 17(2):81-88.
    • (2001) Trends Parasitol , vol.17 , Issue.2 , pp. 81-88
    • Tomley, F.M.1    Soldati, D.S.2
  • 52
    • 3242772439 scopus 로고    scopus 로고
    • The thrombospondin type 1 repeat superfamily
    • Tucker RP. The thrombospondin type 1 repeat superfamily. Int J Biochem Cell Biol 2004; 36(6):969-974.
    • (2004) Int J Biochem Cell Biol , vol.36 , Issue.6 , pp. 969-974
    • Tucker, R.P.1
  • 53
    • 0036796740 scopus 로고    scopus 로고
    • Distribution and evolution of von Willebrand/integrin A domains: Widely dispersed domains with roles in cell adhesion and elsewhere
    • Whittaker CA, Hynes RO. Distribution and evolution of von Willebrand/integrin A domains: Widely dispersed domains with roles in cell adhesion and elsewhere. Mol Biol Cell 2002; 13(10):3369-3387.
    • (2002) Mol Biol Cell , vol.13 , Issue.10 , pp. 3369-3387
    • Whittaker, C.A.1    Hynes, R.O.2
  • 54
    • 0030745648 scopus 로고    scopus 로고
    • TRAP is necessary for gliding motility and infectivity of Plasmodium sporozoites
    • Sultan AA, Thathy V, Frevert U et al. TRAP is necessary for gliding motility and infectivity of Plasmodium sporozoites. Cell 1997; 90(3):511-522.
    • (1997) Cell , vol.90 , Issue.3 , pp. 511-522
    • Sultan, A.A.1    Thathy, V.2    Frevert, U.3
  • 55
    • 0033615981 scopus 로고    scopus 로고
    • Conservation of a gliding motility and cell invasion machinery in apicomplexan parasites
    • Kappe S, Bruderer T, Gantt S et al. Conservation of a gliding motility and cell invasion machinery in apicomplexan parasites. J Cell Biol 1999; l47(5):937-943.
    • (1999) J Cell Biol , vol.147 , Issue.5 , pp. 937-943
    • Kappe, S.1    Bruderer, T.2    Gantt, S.3
  • 56
    • 0037007205 scopus 로고    scopus 로고
    • Plasmodium sporozoite invasion into insect and mammalian cells is directed by the same dual binding system
    • Matuschewski K, Nunes AC, Nussenzweig V et al. Plasmodium sporozoite invasion into insect and mammalian cells is directed by the same dual binding system. EMBO J 2002; 21(7): 1597-1606.
    • (2002) EMBO J , vol.21 , Issue.7 , pp. 1597-1606
    • Matuschewski, K.1    Nunes, A.C.2    Nussenzweig, V.3
  • 57
    • 0026757766 scopus 로고
    • Characterization of Plasmodium falciparum sporozoite surface protein 2
    • Rogers WO, Malik A, Mellouk S et al. Characterization of Plasmodium falciparum sporozoite surface protein 2. Proc Nad Acad Sci USA 1992; 89(19):9176-9180.
    • (1992) Proc Nad Acad Sci USA , vol.89 , Issue.19 , pp. 9176-9180
    • Rogers, W.O.1    Malik, A.2    Mellouk, S.3
  • 58
    • 0033570888 scopus 로고    scopus 로고
    • CTRP is essential for mosquito infection by malaria ookinetes
    • Dessens JT, Beetsma AL, Dimopoulos G et al. CTRP is essential for mosquito infection by malaria ookinetes. EMBO J 1999; 18(22):6221-6227.
    • (1999) EMBO J , vol.18 , Issue.22 , pp. 6221-6227
    • Dessens, J.T.1    Beetsma, A.L.2    Dimopoulos, G.3
  • 59
    • 0033429047 scopus 로고    scopus 로고
    • Targeted disruption of the Plasmodium berghei CTRP gene reveals its essential role in malaria infection of the vector mosquito
    • Yuda M, Sakaida H, Chinzei Y. Targeted disruption of the Plasmodium berghei CTRP gene reveals its essential role in malaria infection of the vector mosquito. J Exp Med 1999; 190(11):1711-1716.
    • (1999) J Exp Med , vol.190 , Issue.11 , pp. 1711-1716
    • Yuda, M.1    Sakaida, H.2    Chinzei, Y.3
  • 60
    • 33748066307 scopus 로고    scopus 로고
    • Toxoplasma MIC2 is a major determinant of invasion and virulence
    • Huynh MH, Carruthers VB. Toxoplasma MIC2 is a major determinant of invasion and virulence. PLoS Pathog 2006; 2(8):e84.
    • (2006) PLoS Pathog , vol.2 , Issue.8
    • Huynh, M.H.1    Carruthers, V.B.2
  • 61
    • 0034883267 scopus 로고    scopus 로고
    • TgM2AP participates in Toxoplasma gondii invasion of host cells and is tightly associated with the adhesive protein TgMIC2
    • Rabenau KE, Sohrabi A, Tripathy A et al. TgM2AP participates in Toxoplasma gondii invasion of host cells and is tightly associated with the adhesive protein TgMIC2. Mol Microbiol 2001; 41(1):537-547.
    • (2001) Mol Microbiol , vol.41 , Issue.1 , pp. 537-547
    • Rabenau, K.E.1    Sohrabi, A.2    Tripathy, A.3
  • 62
    • 0038558167 scopus 로고    scopus 로고
    • Rapid invasion of host cells by Toxoplasma requires secretion of the MIC2-M2AP adhesive protein complex
    • Huynh MH, Rabenau KE, Harper JM et al. Rapid invasion of host cells by Toxoplasma requires secretion of the MIC2-M2AP adhesive protein complex. EMBO J 2003; 22(9):2082-2090.
    • (2003) EMBO J , vol.22 , Issue.9 , pp. 2082-2090
    • Huynh, M.H.1    Rabenau, K.E.2    Harper, J.M.3
  • 63
    • 0023795608 scopus 로고
    • Malaria sporozoites leave behind trails of circumsporozoite protein during gliding motiUty
    • Stewart MJ, Vanderberg JP. Malaria sporozoites leave behind trails of circumsporozoite protein during gliding motiUty. J Protozool 1988; 35(3):389-393.
    • (1988) J Protozool , vol.35 , Issue.3 , pp. 389-393
    • Stewart, M.J.1    Vanderberg, J.P.2
  • 64
    • 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; l(3):225-235.
    • (1999) Cell Microbiol , vol.1 , Issue.3 , pp. 225-235
    • Carruthers, V.B.1    Giddings, O.K.2    Sibley, L.D.3
  • 65
    • 0033231908 scopus 로고    scopus 로고
    • An overview of Plasmodium protein kinases
    • Kappes B, Doerig CD, Graeser R. An overview of Plasmodium protein kinases. Parasitol Today 1999; 15(11):449-454.
    • (1999) Parasitol Today , vol.15 , Issue.11 , pp. 449-454
    • Kappes, B.1    Doerig, C.D.2    Graeser, R.3
  • 66
    • 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 et al. A calcium-dependent protein kinase regulates Plasmodium ookinete access to the midgut epithelial cell. Mol Microbiol 2006; 59(4):1175-1184.
    • (2006) Mol Microbiol , vol.59 , Issue.4 , pp. 1175-1184
    • Ishino, T.1    Orito, Y.2    Chinzei, Y.3
  • 67
    • 33744482044 scopus 로고    scopus 로고
    • Plasmodium berghei calcium-dependent protein kinase 3 is required for ookinete gliding motility and mosquito midgut invasion
    • Siden-Kiamos I, Ecker A, Nyback S et al. Plasmodium berghei calcium-dependent protein kinase 3 is required for ookinete gliding motility and mosquito midgut invasion. Mol Microbiol 2006; 60(6):1355-1363.
    • (2006) Mol Microbiol , vol.60 , Issue.6 , pp. 1355-1363
    • Siden-Kiamos, I.1    Ecker, A.2    Nyback, S.3
  • 68
    • 2442463350 scopus 로고    scopus 로고
    • A small-molecule approach to studying invasive mechanisms of Toxoplasma gondii
    • Carey KL, Westwood NJ, Mitchison TJ et al. A small-molecule approach to studying invasive mechanisms of Toxoplasma gondii. Proc Natl Acad Sci USA 2004; 101(19):7433-7438.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.19 , pp. 7433-7438
    • Carey, K.L.1    Westwood, N.J.2    Mitchison, T.J.3
  • 69
    • 0037007235 scopus 로고    scopus 로고
    • Intramembrane cleavage of microneme proteins at the surface of the apicomplexan parasite Toxoplasma gondii
    • Opitz C, Di Cristina M, Reiss M et al. Intramembrane cleavage of microneme proteins at the surface of the apicomplexan parasite Toxoplasma gondii. EMBO J 2002; 21(7): 1577-1585.
    • (2002) EMBO J , vol.21 , Issue.7 , pp. 1577-1585
    • Opitz, C.1    Di Cristina, M.2    Reiss, M.3
  • 70
    • 2442690776 scopus 로고    scopus 로고
    • Proteomic analysis of cleavage events reveals a dynamic two-step mechanism for proteolysis of a key parasite adhesive complex
    • Zhou XW, Blackman MJ, Howell SA et al. Proteomic analysis of cleavage events reveals a dynamic two-step mechanism for proteolysis of a key parasite adhesive complex. Mol Cell Proteomics 2004; 3(6):565-576.
    • (2004) Mol Cell Proteomics , vol.3 , Issue.6 , pp. 565-576
    • Zhou, X.W.1    Blackman, M.J.2    Howell, S.A.3
  • 71
    • 15244360655 scopus 로고    scopus 로고
    • A spatially localized rhomboid protease cleaves cell surface adhesions essential for invasion by Toxoplasma
    • Brossier F, Jewett TJ, Sibley LD et al. A spatially localized rhomboid protease cleaves cell surface adhesions essential for invasion by Toxoplasma. Proc Natl Acad Sci USA 2005; (11)102:4146-4151.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.11 , pp. 4146-4151
    • Brossier, F.1    Jewett, T.J.2    Sibley, L.D.3
  • 72
    • 19444382777 scopus 로고    scopus 로고
    • Apicomplexan rhomboids have a potential role in microneme protein cleave during host cell invasion
    • Dowse TJ, Pascall JC, Brown KD et al. Apicomplexan rhomboids have a potential role in microneme protein cleave during host cell invasion. Int J Parasitol 2005; 35(7):747-756.
    • (2005) Int J Parasitol , vol.35 , Issue.7 , pp. 747-756
    • Dowse, T.J.1    Pascall, J.C.2    Brown, K.D.3
  • 73
    • 19444369929 scopus 로고    scopus 로고
    • Rhomboid-like proteins in Apicomplexa: Phylogeny and nomenclature
    • Dowse TJ, Soldati D. Rhomboid-like proteins in Apicomplexa: Phylogeny and nomenclature. Trends Parasitol 2005; 21(6):254-258.
    • (2005) Trends Parasitol , vol.21 , Issue.6 , pp. 254-258
    • Dowse, T.J.1    Soldati, D.2
  • 74
    • 33750465167 scopus 로고    scopus 로고
    • Two Plasmodium rhomboid proteases preferentially cleave different adhesions implicated in all invasive stages of malaria
    • Baker RP, Wijetilaka R, Urban S. Two Plasmodium rhomboid proteases preferentially cleave different adhesions implicated in all invasive stages of malaria. PLoS Pathog 2006; 2(10):ell3.
    • (2006) PLoS Pathog , vol.2 , Issue.10
    • Baker, R.P.1    Wijetilaka, R.2    Urban, S.3
  • 75
    • 23944458205 scopus 로고    scopus 로고
    • Gliding motility leads to active cellular invasion by Cryptosporidium parvum sporozoites
    • Wetzel DM, Schmidt J, Kuhlenschmidt MS et al. Gliding motility leads to active cellular invasion by Cryptosporidium parvum sporozoites. Infect Immun 2005; 73(9):5379-5387.
    • (2005) Infect Immun , vol.73 , Issue.9 , pp. 5379-5387
    • Wetzel, D.M.1    Schmidt, J.2    Kuhlenschmidt, M.S.3
  • 76
    • 0032054344 scopus 로고    scopus 로고
    • Molecular cloning and expression analysis of a Cryptosporidium parvum gene encoding a new member of the thrombospondin family
    • Spano F, Putignani L, Naitza S et al. Molecular cloning and expression analysis of a Cryptosporidium parvum gene encoding a new member of the thrombospondin family. Mol Biochem Parasitol 1998; 92(1):147-162.
    • (1998) Mol Biochem Parasitol , vol.92 , Issue.1 , pp. 147-162
    • Spano, F.1    Putignani, L.2    Naitza, S.3
  • 77
    • 8444241483 scopus 로고    scopus 로고
    • A malaria membrane skeletal protein is essential for normal morphogenesis, motility, and infectivity of sporozoites
    • Khater EI, Sinden RE, Dessens JT. A malaria membrane skeletal protein is essential for normal morphogenesis, motility, and infectivity of sporozoites. J Cell Biol 2004; 167(3):425-432.
    • (2004) J Cell Biol , vol.167 , Issue.3 , pp. 425-432
    • Khater, E.I.1    Sinden, R.E.2    Dessens, J.T.3


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