메뉴 건너뛰기




Volumn 10, Issue 9, 2014, Pages

Host Cell Invasion by Apicomplexan Parasites: The Junction Conundrum

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; APICAL MEMBRANE ANTIGEN 1; BINDING PROTEIN; FRUCTOSE BISPHOSPHATE ALDOLASE; GAP45 PROTEIN; MLC1 PROTEIN; MOTOR BINDING PROTEIN; MYOA PROTEIN; RHOPTRY NECK PROTEIN; THROMBIN RECEPTOR ACTIVATING PEPTIDE; UNCLASSIFIED DRUG; ZOITE SPECIFIC PROTEIN;

EID: 84907584482     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1004273     Document Type: Article
Times cited : (65)

References (100)
  • 1
    • 0017879439 scopus 로고
    • Erythrocyte entry by malarial parasites. A moving junction between erythrocyte and parasite
    • Aikawa M, Miller LH, Johnson J, Rabbege J, (1978) Erythrocyte entry by malarial parasites. A moving junction between erythrocyte and parasite. J Cell Biol 77: 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
    • 0023768222 scopus 로고
    • Cell motility of sporozoan protozoa
    • King CA, (1988) Cell motility of sporozoan protozoa. Parasitol Today 4: 315–319.
    • (1988) Parasitol Today , vol.4 , pp. 315-319
    • King, C.A.1
  • 3
    • 0019605349 scopus 로고
    • The role of the cytoskeleton in the motility of coccidian sporozoites
    • Russell DG, Sinden RE, (1981) The role of the cytoskeleton in the motility of coccidian sporozoites. J Cell Sci 50: 345–359.
    • (1981) J Cell Sci , vol.50 , pp. 345-359
    • Russell, D.G.1    Sinden, R.E.2
  • 4
    • 84972033865 scopus 로고
    • Host cell invasion by Apicomplexa: an expression of the parasite's contractile system?
    • Russell DG, (1983) Host cell invasion by Apicomplexa: an expression of the parasite's contractile system? Parasitology 87 (Pt 2): 199–209.
    • (1983) Parasitology , vol.87 , pp. 199-209
    • Russell, D.G.1
  • 5
    • 0020930996 scopus 로고
    • Immunofluorescent localization of myosin at the anterior pole of the coccidian, Toxoplasma gondii
    • Schwartzman JD, Pfefferkorn ER, (1983) Immunofluorescent localization of myosin at the anterior pole of the coccidian, Toxoplasma gondii. J Protozool 30: 657–661.
    • (1983) J Protozool , vol.30 , pp. 657-661
    • Schwartzman, J.D.1    Pfefferkorn, E.R.2
  • 6
    • 0031872677 scopus 로고    scopus 로고
    • Actomyosin motor in the merozoite of the malaria parasite, Plasmodium falciparum: implications for red cell invasion
    • Pinder JC, Fowler RE, Dluzewski AR, Bannister LH, Lavin FM, et al. (1998) Actomyosin motor in the merozoite of the malaria parasite, Plasmodium falciparum: implications for red cell invasion. J Cell Sci 111 (Pt 13): 1831–1839.
    • (1998) J Cell Sci , vol.111 , pp. 1831-1839
    • Pinder, J.C.1    Fowler, R.E.2    Dluzewski, A.R.3    Bannister, L.H.4    Lavin, F.M.5
  • 7
    • 0029869791 scopus 로고    scopus 로고
    • Toxoplasma invasion of mammalian cells is powered by the actin cytoskeleton of the parasite
    • Dobrowolski JM, Sibley LD, (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
  • 8
    • 0029016818 scopus 로고
    • Invasion of Toxoplasma gondii occurs by active penetration of the host cell
    • Morisaki JH, Heuser JE, Sibley LD, (1995) Invasion of Toxoplasma gondii occurs by active penetration of the host cell. J Cell Sci 108 (Pt 6): 2457–2464.
    • (1995) J Cell Sci , vol.108 , pp. 2457-2464
    • Morisaki, J.H.1    Heuser, J.E.2    Sibley, L.D.3
  • 9
    • 61849132162 scopus 로고    scopus 로고
    • Host cell entry by apicomplexa parasites requires actin polymerization in the host cell
    • Gonzalez V, Combe A, David V, Malmquist NA, Delorme V, et al. (2009) Host cell entry by apicomplexa parasites requires actin polymerization in the host cell. Cell Host Microbe 5: 259–272.
    • (2009) Cell Host Microbe , vol.5 , pp. 259-272
    • Gonzalez, V.1    Combe, A.2    David, V.3    Malmquist, N.A.4    Delorme, V.5
  • 10
    • 84870801604 scopus 로고    scopus 로고
    • Toxofilin upregulates the host cortical actin cytoskeleton dynamics, facilitating Toxoplasma invasion
    • Delorme-Walker V, Abrivard M, Lagal V, Anderson K, Perazzi A, et al. (2012) Toxofilin upregulates the host cortical actin cytoskeleton dynamics, facilitating Toxoplasma invasion. J Cell Sci 125: 4333–4342.
    • (2012) J Cell Sci , vol.125 , pp. 4333-4342
    • Delorme-Walker, V.1    Abrivard, M.2    Lagal, V.3    Anderson, K.4    Perazzi, A.5
  • 11
    • 0037910335 scopus 로고    scopus 로고
    • Actin dynamics is controlled by a casein kinase II and phosphatase 2C interplay on Toxoplasma gondii Toxofilin
    • Delorme V, Cayla X, Faure G, Garcia A, Tardieux I, (2003) Actin dynamics is controlled by a casein kinase II and phosphatase 2C interplay on Toxoplasma gondii Toxofilin. Mol Biol Cell 14: 1900–1912.
    • (2003) Mol Biol Cell , vol.14 , pp. 1900-1912
    • Delorme, V.1    Cayla, X.2    Faure, G.3    Garcia, A.4    Tardieux, I.5
  • 12
    • 0031018273 scopus 로고    scopus 로고
    • Subpellicular microtubules associate with an intramembranous particle lattice in the protozoan parasite Toxoplasma gondii
    • Morrissette NS, Murray JM, Roos DS, (1997) Subpellicular microtubules associate with an intramembranous particle lattice in the protozoan parasite Toxoplasma gondii. J Cell Sci 110 (Pt 1): 35–42.
    • (1997) J Cell Sci , vol.110 , pp. 35-42
    • Morrissette, N.S.1    Murray, J.M.2    Roos, D.S.3
  • 13
    • 0030745648 scopus 로고    scopus 로고
    • TRAP is necessary for gliding motility and infectivity of Plasmodium sporozoites
    • Sultan AA, Thathy V, Frevert U, Robson KJ, Crisanti A, et al. (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
  • 14
    • 0037174664 scopus 로고    scopus 로고
    • Role of Toxoplasma gondii myosin A in powering parasite gliding and host cell invasion
    • Meissner M, Schluter D, Soldati D, (2002) Role of Toxoplasma gondii myosin A in powering parasite gliding and host cell invasion. Science 298: 837–840.
    • (2002) Science , vol.298 , pp. 837-840
    • Meissner, M.1    Schluter, D.2    Soldati, D.3
  • 15
    • 0038637915 scopus 로고    scopus 로고
    • Aldolase forms a bridge between cell surface adhesins and the actin cytoskeleton in apicomplexan parasites
    • Jewett TJ, Sibley LD, (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
  • 16
    • 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, Coppens I, Daly TM, et al. (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
  • 17
    • 33749515928 scopus 로고    scopus 로고
    • Regulation of apicomplexan microfilament dynamics by a minimal set of actin-binding proteins
    • Schuler H, Matuschewski K, (2006) Regulation of apicomplexan microfilament dynamics by a minimal set of actin-binding proteins. Traffic 7: 1433–1439.
    • (2006) Traffic , vol.7 , pp. 1433-1439
    • Schuler, H.1    Matuschewski, K.2
  • 18
    • 80055070537 scopus 로고    scopus 로고
    • Evolutionarily divergent, unstable filamentous actin is essential for gliding motility in apicomplexan parasites
    • Skillman KM, Diraviyam K, Khan A, Tang K, Sept D, et al. (2011) Evolutionarily divergent, unstable filamentous actin is essential for gliding motility in apicomplexan parasites. PLoS Pathog 7: e1002280.
    • (2011) PLoS Pathog , vol.7 , pp. e1002280
    • Skillman, K.M.1    Diraviyam, K.2    Khan, A.3    Tang, K.4    Sept, D.5
  • 19
    • 79954584860 scopus 로고    scopus 로고
    • Actin depolymerizing factor controls actin turnover and gliding motility in Toxoplasma gondii
    • Mehta S, Sibley LD, (2011) Actin depolymerizing factor controls actin turnover and gliding motility in Toxoplasma gondii. Mol Biol Cell 22: 1290–1299.
    • (2011) Mol Biol Cell , vol.22 , pp. 1290-1299
    • Mehta, S.1    Sibley, L.D.2
  • 20
    • 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 CJ, Paul AS, Rug M, Smith BJ, et al. (2008) A malaria parasite formin regulates actin polymerization and localizes to the parasite-erythrocyte moving junction during invasion. Cell Host Microbe 3: 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
  • 21
    • 78449238637 scopus 로고    scopus 로고
    • Concerted action of two formins in gliding motility and host cell invasion by Toxoplasma gondii
    • Daher W, Plattner F, Carlier MF, Soldati-Favre D, (2010) Concerted action of two formins in gliding motility and host cell invasion by Toxoplasma gondii. PLoS Pathog 6: e1001132.
    • (2010) PLoS Pathog , vol.6 , pp. e1001132
    • Daher, W.1    Plattner, F.2    Carlier, M.F.3    Soldati-Favre, D.4
  • 22
    • 84857530326 scopus 로고    scopus 로고
    • Spatial localisation of actin filaments across developmental stages of the malaria parasite
    • Angrisano F, Riglar DT, Sturm A, Volz JC, Delves MJ, et al. (2012) Spatial localisation of actin filaments across developmental stages of the malaria parasite. PLoS ONE 7: e32188.
    • (2012) PLoS ONE , vol.7 , pp. e32188
    • Angrisano, F.1    Riglar, D.T.2    Sturm, A.3    Volz, J.C.4    Delves, M.J.5
  • 23
    • 77949903357 scopus 로고    scopus 로고
    • Toxoplasma gondii actin depolymerizing factor acts primarily to sequester G-actin
    • Mehta S, Sibley LD, (2010) Toxoplasma gondii actin depolymerizing factor acts primarily to sequester G-actin. J Biol Chem 285: 6835–6847.
    • (2010) J Biol Chem , vol.285 , pp. 6835-6847
    • Mehta, S.1    Sibley, L.D.2
  • 24
    • 84859203124 scopus 로고    scopus 로고
    • Toxoplasma gondii profilin acts primarily to sequester G-actin while formins efficiently nucleate actin filament formation in vitro
    • Skillman KM, Daher W, Ma CI, Soldati-Favre D, Sibley LD, (2012) Toxoplasma gondii profilin acts primarily to sequester G-actin while formins efficiently nucleate actin filament formation in vitro. Biochemistry 51: 2486–2495.
    • (2012) Biochemistry , vol.51 , pp. 2486-2495
    • Skillman, K.M.1    Daher, W.2    Ma, C.I.3    Soldati-Favre, D.4    Sibley, L.D.5
  • 25
    • 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 MF, et al. (2008) Toxoplasma profilin is essential for host cell invasion and TLR11-dependent induction of an interleukin-12 response. Cell Host Microbe 3: 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
  • 26
    • 84895783394 scopus 로고    scopus 로고
    • Toxoplasma aldolase is required for metabolism but dispensable for host-cell invasion
    • Shen B, Sibley LD, (2014) Toxoplasma aldolase is required for metabolism but dispensable for host-cell invasion. Proc Natl Acad Sci U S A 111: 3567–3572.
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 3567-3572
    • Shen, B.1    Sibley, L.D.2
  • 27
    • 64649106434 scopus 로고    scopus 로고
    • Aldolase is essential for energy production and bridging adhesin-actin cytoskeletal interactions during parasite invasion of host cells
    • Starnes GL, Coincon M, Sygusch J, Sibley LD, (2009) Aldolase is essential for energy production and bridging adhesin-actin cytoskeletal interactions during parasite invasion of host cells. Cell Host Microbe 5: 353–364.
    • (2009) Cell Host Microbe , vol.5 , pp. 353-364
    • Starnes, G.L.1    Coincon, M.2    Sygusch, J.3    Sibley, L.D.4
  • 28
    • 55449121380 scopus 로고    scopus 로고
    • Host cell egress and invasion induce marked relocations of glycolytic enzymes in Toxoplasma gondii tachyzoites
    • Pomel S, Luk FC, Beckers CJ, (2008) Host cell egress and invasion induce marked relocations of glycolytic enzymes in Toxoplasma gondii tachyzoites. PLoS Pathog 4: e1000188.
    • (2008) PLoS Pathog , vol.4 , pp. e1000188
    • Pomel, S.1    Luk, F.C.2    Beckers, C.J.3
  • 29
    • 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, et al. (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
  • 30
    • 59249083317 scopus 로고    scopus 로고
    • GAP45 phosphorylation controls assembly of the Toxoplasma myosin XIV complex
    • Gilk SD, Gaskins E, Ward GE, Beckers CJ, (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
  • 32
    • 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 AJ, Whitelaw JA, Pall G, et al. (2014) The Toxoplasma Acto-MyoA Motor Complex Is Important but Not Essential for Gliding Motility and Host Cell Invasion. PLoS ONE 9: e91819.
    • (2014) PLoS ONE , vol.9 , pp. e91819
    • Egarter, S.1    Andenmatten, N.2    Jackson, A.J.3    Whitelaw, J.A.4    Pall, G.5
  • 33
    • 75149188237 scopus 로고    scopus 로고
    • Plasmodium sporozoite motility is modulated by the turnover of discrete adhesion sites
    • Munter S, Sabass B, Selhuber-Unkel C, Kudryashev M, Hegge S, et al. (2009) Plasmodium sporozoite motility is modulated by the turnover of discrete adhesion sites. Cell Host Microbe 6: 551–562.
    • (2009) Cell Host Microbe , vol.6 , pp. 551-562
    • Munter, S.1    Sabass, B.2    Selhuber-Unkel, C.3    Kudryashev, M.4    Hegge, S.5
  • 34
    • 84881569400 scopus 로고    scopus 로고
    • Tunable substrates unveil chemical complementation of a genetic cell migration defect
    • Hellmann JK, Perschmann N, Spatz JP, Frischknecht F, (2013) Tunable substrates unveil chemical complementation of a genetic cell migration defect. Adv Healthc Mater 2: 1162–1169.
    • (2013) Adv Healthc Mater , vol.2 , pp. 1162-1169
    • Hellmann, J.K.1    Perschmann, N.2    Spatz, J.P.3    Frischknecht, F.4
  • 35
    • 0042672913 scopus 로고    scopus 로고
    • The cytoplasmic domain of the Plasmodium falciparum ligand EBA-175 is essential for invasion but not protein trafficking
    • Gilberger TW, Thompson JK, Reed MB, Good RT, Cowman AF, (2003) The cytoplasmic domain of the Plasmodium falciparum ligand EBA-175 is essential for invasion but not protein trafficking. J Cell Biol 162: 317–327.
    • (2003) J Cell Biol , vol.162 , pp. 317-327
    • Gilberger, T.W.1    Thompson, J.K.2    Reed, M.B.3    Good, R.T.4    Cowman, A.F.5
  • 36
    • 15944368263 scopus 로고    scopus 로고
    • Targeted deletion of Plasmodium knowlesi Duffy binding protein confirms its role in junction formation during invasion
    • Singh AP, Ozwara H, Kocken CH, Puri SK, Thomas AW, et al. (2005) Targeted deletion of Plasmodium knowlesi Duffy binding protein confirms its role in junction formation during invasion. Mol Microbiol 55: 1925–1934.
    • (2005) Mol Microbiol , vol.55 , pp. 1925-1934
    • Singh, A.P.1    Ozwara, H.2    Kocken, C.H.3    Puri, S.K.4    Thomas, A.W.5
  • 37
    • 84871052343 scopus 로고    scopus 로고
    • The role of the reticulocyte-binding-like protein homologues of Plasmodium in erythrocyte sensing and invasion
    • Gunalan K, Gao X, Yap SS, Huang X, Preiser PR, (2013) The role of the reticulocyte-binding-like protein homologues of Plasmodium in erythrocyte sensing and invasion. Cell Microbiol 15: 35–44.
    • (2013) Cell Microbiol , vol.15 , pp. 35-44
    • Gunalan, K.1    Gao, X.2    Yap, S.S.3    Huang, X.4    Preiser, P.R.5
  • 38
    • 79961100663 scopus 로고    scopus 로고
    • Differences in erythrocyte receptor specificity of different parts of the Plasmodium falciparum reticulocyte binding protein homologue 2a
    • Gunalan K, Gao X, Liew KJ, Preiser PR, (2011) Differences in erythrocyte receptor specificity of different parts of the Plasmodium falciparum reticulocyte binding protein homologue 2a. Infect Immun 79: 3421–3430.
    • (2011) Infect Immun , vol.79 , pp. 3421-3430
    • Gunalan, K.1    Gao, X.2    Liew, K.J.3    Preiser, P.R.4
  • 39
    • 58549099716 scopus 로고    scopus 로고
    • Reticulocyte-binding protein homologue 5 - an essential adhesin involved in invasion of human erythrocytes by Plasmodium falciparum
    • Baum J, Chen L, Healer J, Lopaticki S, Boyle M, et al. (2009) Reticulocyte-binding protein homologue 5 - an essential adhesin involved in invasion of human erythrocytes by Plasmodium falciparum. Int J Parasitol 39: 371–380.
    • (2009) Int J Parasitol , vol.39 , pp. 371-380
    • Baum, J.1    Chen, L.2    Healer, J.3    Lopaticki, S.4    Boyle, M.5
  • 40
    • 84886780001 scopus 로고    scopus 로고
    • RALP1 is a rhoptry neck erythrocyte-binding protein of Plasmodium falciparum merozoites and a potential blood-stage vaccine candidate antigen
    • Ito D, Hasegawa T, Miura K, Yamasaki T, Arumugam TU, et al. (2013) RALP1 is a rhoptry neck erythrocyte-binding protein of Plasmodium falciparum merozoites and a potential blood-stage vaccine candidate antigen. Infect Immun 81: 4290–4298.
    • (2013) Infect Immun , vol.81 , pp. 4290-4298
    • Ito, D.1    Hasegawa, T.2    Miura, K.3    Yamasaki, T.4    Arumugam, T.U.5
  • 41
    • 43149091439 scopus 로고    scopus 로고
    • Microneme protein 8—a new essential invasion factor in Toxoplasma gondii
    • Kessler H, Herm-Gotz A, Hegge S, Rauch M, Soldati-Favre D, et al. (2008) Microneme protein 8—a new essential invasion factor in Toxoplasma gondii. J Cell Sci 121: 947–956.
    • (2008) J Cell Sci , vol.121 , pp. 947-956
    • Kessler, H.1    Herm-Gotz, A.2    Hegge, S.3    Rauch, M.4    Soldati-Favre, D.5
  • 43
    • 33748066307 scopus 로고    scopus 로고
    • Toxoplasma MIC2 is a major determinant of invasion and virulence
    • Huynh MH, Carruthers VB, (2006) Toxoplasma MIC2 is a major determinant of invasion and virulence. PLoS Pathog 2: e84.
    • (2006) PLoS Pathog , vol.2 , pp. e84
    • Huynh, M.H.1    Carruthers, V.B.2
  • 44
    • 84871841664 scopus 로고    scopus 로고
    • Shape change in the receptor for gliding motility in Plasmodium sporozoites
    • Song G, Koksal AC, Lu C, Springer TA, (2012) Shape change in the receptor for gliding motility in Plasmodium sporozoites. Proc Natl Acad Sci U S A 109: 21420–21425.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 21420-21425
    • Song, G.1    Koksal, A.C.2    Lu, C.3    Springer, T.A.4
  • 45
    • 79961169243 scopus 로고    scopus 로고
    • Vital functions of the malarial ookinete protein, CTRP, reside in the A domains
    • Ramakrishnan C, Dessens JT, Armson R, Pinto SB, Talman AM, et al. (2011) Vital functions of the malarial ookinete protein, CTRP, reside in the A domains. Int J Parasitol 41: 1029–1039.
    • (2011) Int J Parasitol , vol.41 , pp. 1029-1039
    • Ramakrishnan, C.1    Dessens, J.T.2    Armson, R.3    Pinto, S.B.4    Talman, A.M.5
  • 46
    • 77951026559 scopus 로고    scopus 로고
    • Identification of the moving junction complex of Toxoplasma gondii: a collaboration between distinct secretory organelles
    • Alexander DL, Mital J, Ward GE, Bradley P, Boothroyd JC, (2005) Identification of the moving junction complex of Toxoplasma gondii: a collaboration between distinct secretory organelles. PLoS Pathog 1: e17.
    • (2005) PLoS Pathog , vol.1 , pp. e17
    • Alexander, D.L.1    Mital, J.2    Ward, G.E.3    Bradley, P.4    Boothroyd, J.C.5
  • 47
    • 28044454537 scopus 로고    scopus 로고
    • The rhoptry neck protein RON4 re-localizes at the moving junction during Toxoplasma gondii invasion
    • Lebrun M, Michelin A, El Hajj H, Poncet J, Bradley PJ, et al. (2005) The rhoptry neck protein RON4 re-localizes at the moving junction during Toxoplasma gondii invasion. Cell Microbiol 7: 1823–1833.
    • (2005) Cell Microbiol , vol.7 , pp. 1823-1833
    • Lebrun, M.1    Michelin, A.2    El Hajj, H.3    Poncet, J.4    Bradley, P.J.5
  • 48
    • 78751478841 scopus 로고    scopus 로고
    • Super-resolution dissection of coordinated events during malaria parasite invasion of the human erythrocyte
    • Riglar DT, Richard D, Wilson DW, Boyle MJ, Dekiwadia C, et al. (2011) Super-resolution dissection of coordinated events during malaria parasite invasion of the human erythrocyte. Cell Host Microbe 9: 9–20.
    • (2011) Cell Host Microbe , vol.9 , pp. 9-20
    • Riglar, D.T.1    Richard, D.2    Wilson, D.W.3    Boyle, M.J.4    Dekiwadia, C.5
  • 49
    • 0019975873 scopus 로고
    • Rat monoclonal antibodies which inhibit the in vitro multiplication of Plasmodium knowlesi
    • Deans JA, Alderson T, Thomas AW, Mitchell GH, Lennox ES, et al. (1982) Rat monoclonal antibodies which inhibit the in vitro multiplication of Plasmodium knowlesi. Clin Exp Immunol 49: 297–309.
    • (1982) Clin Exp Immunol , vol.49 , pp. 297-309
    • Deans, J.A.1    Alderson, T.2    Thomas, A.W.3    Mitchell, G.H.4    Lennox, E.S.5
  • 50
    • 0028588984 scopus 로고
    • High prevalence of natural antibodies against Plasmodium falciparum 83-kilodalton apical membrane antigen (PF83/AMA-1) as detected by capture-enzyme-linked immunosorbent assay using full-length baculovirus recombinant PF83/AMA-1
    • Thomas AW, Trape JF, Rogier C, Goncalves A, Rosario VE, et al. (1994) High prevalence of natural antibodies against Plasmodium falciparum 83-kilodalton apical membrane antigen (PF83/AMA-1) as detected by capture-enzyme-linked immunosorbent assay using full-length baculovirus recombinant PF83/AMA-1. Am J Trop Med Hyg 51: 730–740.
    • (1994) Am J Trop Med Hyg , vol.51 , pp. 730-740
    • Thomas, A.W.1    Trape, J.F.2    Rogier, C.3    Goncalves, A.4    Rosario, V.E.5
  • 52
    • 84894187377 scopus 로고    scopus 로고
    • Extended safety, immunogenicity and efficacy of a blood-stage malaria vaccine in malian children: 24-month follow-up of a randomized, double-blinded phase 2 trial
    • Laurens MB, Thera MA, Coulibaly D, Ouattara A, Kone AK, et al. (2013) Extended safety, immunogenicity and efficacy of a blood-stage malaria vaccine in malian children: 24-month follow-up of a randomized, double-blinded phase 2 trial. PLoS ONE 8: e79323.
    • (2013) PLoS ONE , vol.8 , pp. e79323
    • Laurens, M.B.1    Thera, M.A.2    Coulibaly, D.3    Ouattara, A.4    Kone, A.K.5
  • 53
    • 84881113901 scopus 로고    scopus 로고
    • Toxoplasma gondii sporozoites invade host cells using two novel paralogues of RON2 and AMA1
    • Poukchanski A, Fritz HM, Tonkin ML, Treeck M, Boulanger MJ, et al. (2013) Toxoplasma gondii sporozoites invade host cells using two novel paralogues of RON2 and AMA1. PLoS ONE 8: e70637.
    • (2013) PLoS ONE , vol.8 , pp. e70637
    • Poukchanski, A.1    Fritz, H.M.2    Tonkin, M.L.3    Treeck, M.4    Boulanger, M.J.5
  • 54
    • 55849119149 scopus 로고    scopus 로고
    • Identification and characterization of the Plasmodium yoelii PyP140/RON4 protein, an orthologue of Toxoplasma gondii RON4, whose cysteine-rich domain does not protect against lethal parasite challenge infection
    • Narum DL, Nguyen V, Zhang Y, Glen J, Shimp RL, et al. (2008) Identification and characterization of the Plasmodium yoelii PyP140/RON4 protein, an orthologue of Toxoplasma gondii RON4, whose cysteine-rich domain does not protect against lethal parasite challenge infection. Infect Immun 76: 4876–4882.
    • (2008) Infect Immun , vol.76 , pp. 4876-4882
    • Narum, D.L.1    Nguyen, V.2    Zhang, Y.3    Glen, J.4    Shimp, R.L.5
  • 55
    • 62149116563 scopus 로고    scopus 로고
    • Novel components of the Apicomplexan moving junction reveal conserved and coccidia-restricted elements
    • Straub KW, Cheng SJ, Sohn CS, Bradley PJ, (2009) Novel components of the Apicomplexan moving junction reveal conserved and coccidia-restricted elements. Cell Microbiol 11: 590–603.
    • (2009) Cell Microbiol , vol.11 , pp. 590-603
    • Straub, K.W.1    Cheng, S.J.2    Sohn, C.S.3    Bradley, P.J.4
  • 56
    • 79952231758 scopus 로고    scopus 로고
    • The RON2-AMA1 interaction is a critical step in moving junction-dependent invasion by apicomplexan parasites
    • Lamarque M, Besteiro S, Papoin J, Roques M, Vulliez-Le Normand B, et al. (2011) The RON2-AMA1 interaction is a critical step in moving junction-dependent invasion by apicomplexan parasites. PLoS Pathog 7: e1001276.
    • (2011) PLoS Pathog , vol.7 , pp. e1001276
    • Lamarque, M.1    Besteiro, S.2    Papoin, J.3    Roques, M.4    Vulliez-Le Normand, B.5
  • 57
    • 79952234824 scopus 로고    scopus 로고
    • The C-terminus of Toxoplasma RON2 provides the crucial link between AMA1 and the host-associated invasion complex
    • Tyler JS, Boothroyd JC, (2011) The C-terminus of Toxoplasma RON2 provides the crucial link between AMA1 and the host-associated invasion complex. PLoS Pathog 7: e1001282.
    • (2011) PLoS Pathog , vol.7 , pp. e1001282
    • Tyler, J.S.1    Boothroyd, J.C.2
  • 58
    • 60349121591 scopus 로고    scopus 로고
    • Export of a Toxoplasma gondii rhoptry neck protein complex at the host cell membrane to form the moving junction during invasion
    • Besteiro S, Michelin A, Poncet J, Dubremetz JF, Lebrun M, (2009) Export of a Toxoplasma gondii rhoptry neck protein complex at the host cell membrane to form the moving junction during invasion. PLoS Pathog 5: e1000309.
    • (2009) PLoS Pathog , vol.5 , pp. e1000309
    • Besteiro, S.1    Michelin, A.2    Poncet, J.3    Dubremetz, J.F.4    Lebrun, M.5
  • 59
    • 84887739560 scopus 로고    scopus 로고
    • Characterization of the interaction between Toxoplasma gondii rhoptry neck protein 4 and host cellular beta-tubulin
    • Takemae H, Sugi T, Kobayashi K, Gong H, Ishiwa A, et al. (2013) Characterization of the interaction between Toxoplasma gondii rhoptry neck protein 4 and host cellular beta-tubulin. Sci Rep 3: 3199.
    • (2013) Sci Rep , vol.3 , pp. 3199
    • Takemae, H.1    Sugi, T.2    Kobayashi, K.3    Gong, H.4    Ishiwa, A.5
  • 60
    • 79960668340 scopus 로고    scopus 로고
    • Host cell invasion by apicomplexan parasites: insights from the co-structure of AMA1 with a RON2 peptide
    • Tonkin ML, Roques M, Lamarque MH, Pugniere M, Douguet D, et al. (2011) Host cell invasion by apicomplexan parasites: insights from the co-structure of AMA1 with a RON2 peptide. Science 333: 463–467.
    • (2011) Science , vol.333 , pp. 463-467
    • Tonkin, M.L.1    Roques, M.2    Lamarque, M.H.3    Pugniere, M.4    Douguet, D.5
  • 61
    • 84864054673 scopus 로고    scopus 로고
    • Structural and functional insights into the malaria parasite moving junction complex
    • Vulliez-Le Normand B, Tonkin ML, Lamarque MH, Langer S, Hoos S, et al. (2012) Structural and functional insights into the malaria parasite moving junction complex. PLoS Pathog 8: e1002755.
    • (2012) PLoS Pathog , vol.8 , pp. e1002755
    • Vulliez-Le Normand, B.1    Tonkin, M.L.2    Lamarque, M.H.3    Langer, S.4    Hoos, S.5
  • 62
    • 59249106253 scopus 로고    scopus 로고
    • An inhibitory antibody blocks interactions between components of the malarial invasion machinery
    • Collins CR, Withers-Martinez C, Hackett F, Blackman MJ, (2009) An inhibitory antibody blocks interactions between components of the malarial invasion machinery. PLoS Pathog 5: e1000273.
    • (2009) PLoS Pathog , vol.5 , pp. e1000273
    • Collins, C.R.1    Withers-Martinez, C.2    Hackett, F.3    Blackman, M.J.4
  • 63
    • 77952007992 scopus 로고    scopus 로고
    • Interaction between Plasmodium falciparum apical membrane antigen 1 and the rhoptry neck protein complex defines a key step in the erythrocyte invasion process of malaria parasites
    • Richard D, MacRaild CA, Riglar DT, Chan JA, Foley M, et al. (2010) Interaction between Plasmodium falciparum apical membrane antigen 1 and the rhoptry neck protein complex defines a key step in the erythrocyte invasion process of malaria parasites. J Biol Chem 285: 14815–14822.
    • (2010) J Biol Chem , vol.285 , pp. 14815-14822
    • Richard, D.1    Macraild, C.A.2    Riglar, D.T.3    Chan, J.A.4    Foley, M.5
  • 64
    • 80051964398 scopus 로고    scopus 로고
    • Binding of Plasmodium merozoite proteins RON2 and AMA1 triggers commitment to invasion
    • Srinivasan P, Beatty WL, Diouf A, Herrera R, Ambroggio X, et al. (2011) Binding of Plasmodium merozoite proteins RON2 and AMA1 triggers commitment to invasion. Proc Natl Acad Sci U S A 108: 13275–13280.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 13275-13280
    • Srinivasan, P.1    Beatty, W.L.2    Diouf, A.3    Herrera, R.4    Ambroggio, X.5
  • 65
    • 84881442475 scopus 로고    scopus 로고
    • Disrupting malaria parasite AMA1-RON2 interaction with a small molecule prevents erythrocyte invasion
    • Srinivasan P, Yasgar A, Luci DK, Beatty WL, Hu X, et al. (2013) Disrupting malaria parasite AMA1-RON2 interaction with a small molecule prevents erythrocyte invasion. Nat Commun 4: 2261.
    • (2013) Nat Commun , vol.4 , pp. 2261
    • Srinivasan, P.1    Yasgar, A.2    Luci, D.K.3    Beatty, W.L.4    Hu, X.5
  • 66
    • 79960691662 scopus 로고    scopus 로고
    • Biochemistry. Revealing a parasite's invasive trick
    • Baum J, Cowman AF, (2011) Biochemistry. Revealing a parasite's invasive trick. Science 333: 410–411.
    • (2011) Science , vol.333 , pp. 410-411
    • Baum, J.1    Cowman, A.F.2
  • 67
    • 84865281003 scopus 로고    scopus 로고
    • The moving junction, a key portal to host cell invasion by apicomplexan parasites
    • Shen B, Sibley LD, (2012) The moving junction, a key portal to host cell invasion by apicomplexan parasites. Curr Opin Microbiol 15: 449–455.
    • (2012) Curr Opin Microbiol , vol.15 , pp. 449-455
    • Shen, B.1    Sibley, L.D.2
  • 69
    • 84873557949 scopus 로고    scopus 로고
    • Malaria biology and disease pathogenesis: insights for new treatments
    • Miller LH, Ackerman HC, Su XZ, Wellems TE, (2013) Malaria biology and disease pathogenesis: insights for new treatments. Nat Med 19: 156–167.
    • (2013) Nat Med , vol.19 , pp. 156-167
    • Miller, L.H.1    Ackerman, H.C.2    Su, X.Z.3    Wellems, T.E.4
  • 70
    • 84873406471 scopus 로고    scopus 로고
    • Conditional genome engineering in Toxoplasma gondii uncovers alternative invasion mechanisms
    • Andenmatten N, Egarter S, Jackson AJ, Jullien N, Herman JP, et al. (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
  • 72
    • 83655164555 scopus 로고    scopus 로고
    • Independent roles of apical membrane antigen 1 and rhoptry neck proteins during host cell invasion by apicomplexa
    • Giovannini D, Spath S, Lacroix C, Perazzi A, Bargieri D, et al. (2011) Independent roles of apical membrane antigen 1 and rhoptry neck proteins during host cell invasion by apicomplexa. Cell Host Microbe 10: 591–602.
    • (2011) Cell Host Microbe , vol.10 , pp. 591-602
    • Giovannini, D.1    Spath, S.2    Lacroix, C.3    Perazzi, A.4    Bargieri, D.5
  • 74
    • 84897442989 scopus 로고    scopus 로고
    • RON5 is critical for organization and function of the Toxoplasma moving junction complex
    • Beck JR, Chen AL, kim EW, Bradley PJ, (2014) RON5 is critical for organization and function of the Toxoplasma moving junction complex. PLoS Pathog 10: e1004025.
    • (2014) PLoS Pathog , vol.10 , pp. e1004025
    • Beck, J.R.1    Chen, A.L.2    Kim, E.W.3    Bradley, P.J.4
  • 75
    • 84902845644 scopus 로고    scopus 로고
    • Plasticity and redundancy among AMA-RON pairs ensure host cell entry of Toxoplasma parasites
    • Lamarque MH, Roques M, Kong-Hap M, Tonkin ML, Rugarabamu G, et al. (2014) Plasticity and redundancy among AMA-RON pairs ensure host cell entry of Toxoplasma parasites. Nat Commun 5: 4098.
    • (2014) Nat Commun , vol.5 , pp. 4098
    • Lamarque, M.H.1    Roques, M.2    Kong-Hap, M.3    Tonkin, M.L.4    Rugarabamu, G.5
  • 76
    • 84892638781 scopus 로고    scopus 로고
    • Apical membrane antigen 1 mediates apicomplexan parasite attachment but is dispensable for host cell invasion
    • Bargieri DY, Andenmatten N, Lagal V, Thiberge S, Whitelaw JA, et al. (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
  • 77
    • 84898545498 scopus 로고    scopus 로고
    • Conditional expression of apical membrane antigen 1 in Plasmodium falciparum shows it is required for erythrocyte invasion by merozoites
    • Yap A, Azevedo MF, Gilson PR, Weiss GE, O'Neill MT, et al. (2014) Conditional expression of apical membrane antigen 1 in Plasmodium falciparum shows it is required for erythrocyte invasion by merozoites. Cell Microbiol 16: 642–656.
    • (2014) Cell Microbiol , vol.16 , pp. 642-656
    • Yap, A.1    Azevedo, M.F.2    Gilson, P.R.3    Weiss, G.E.4    O'neill, M.T.5
  • 78
    • 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, Ward GE, (2005) 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: 4341–4349.
    • (2005) Mol Biol Cell , vol.16 , pp. 4341-4349
    • Mital, J.1    Meissner, M.2    Soldati, D.3    Ward, G.E.4
  • 79
    • 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 GH, Thomas AW, Margos G, Dluzewski AR, Bannister LH, (2004) Apical membrane antigen 1, a major malaria vaccine candidate, mediates the close attachment of invasive merozoites to host red blood cells. Infect Immun 72: 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
  • 80
    • 0034839406 scopus 로고    scopus 로고
    • Erythrocyte-binding activity of Plasmodium yoelii apical membrane antigen-1 expressed on the surface of transfected COS-7 cells
    • Fraser TS, Kappe SH, Narum DL, VanBuskirk KM, Adams JH, (2001) Erythrocyte-binding activity of Plasmodium yoelii apical membrane antigen-1 expressed on the surface of transfected COS-7 cells. Mol Biochem Parasitol 117: 49–59.
    • (2001) Mol Biochem Parasitol , vol.117 , pp. 49-59
    • Fraser, T.S.1    Kappe, S.H.2    Narum, D.L.3    Vanbuskirk, K.M.4    Adams, J.H.5
  • 81
    • 0034668218 scopus 로고    scopus 로고
    • Plasmodium falciparum AMA-1 erythrocyte binding peptides implicate AMA-1 as erythrocyte binding protein
    • Urquiza M, Suarez JE, Cardenas C, Lopez R, Puentes A, et al. (2000) Plasmodium falciparum AMA-1 erythrocyte binding peptides implicate AMA-1 as erythrocyte binding protein. Vaccine 19: 508–513.
    • (2000) Vaccine , vol.19 , pp. 508-513
    • Urquiza, M.1    Suarez, J.E.2    Cardenas, C.3    Lopez, R.4    Puentes, A.5
  • 82
    • 33751040315 scopus 로고    scopus 로고
    • Synthetic peptides from Plasmodium falciparum apical membrane antigen 1 (AMA-1) specifically interacting with human hepatocytes
    • Valbuena J, Rodriguez L, Vera R, Puentes A, Curtidor H, et al. (2006) Synthetic peptides from Plasmodium falciparum apical membrane antigen 1 (AMA-1) specifically interacting with human hepatocytes. Biochimie 88: 1447–1455.
    • (2006) Biochimie , vol.88 , pp. 1447-1455
    • Valbuena, J.1    Rodriguez, L.2    Vera, R.3    Puentes, A.4    Curtidor, H.5
  • 83
    • 17244375211 scopus 로고    scopus 로고
    • Domain III of Plasmodium falciparum apical membrane antigen 1 binds to the erythrocyte membrane protein Kx
    • Kato K, Mayer DC, Singh S, Reid M, Miller LH, (2005) Domain III of Plasmodium falciparum apical membrane antigen 1 binds to the erythrocyte membrane protein Kx. Proc Natl Acad Sci U S A 102: 5552–5557.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 5552-5557
    • Kato, K.1    Mayer, D.C.2    Singh, S.3    Reid, M.4    Miller, L.H.5
  • 84
    • 84881113901 scopus 로고    scopus 로고
    • Toxoplasma gondii sporozoites invade host cells using two novel paralogues of RON2 and AMA1
    • Poukchanski A, Fritz HM, Tonkin ML, Treeck M, Boulanger MJ, et al. (2013) Toxoplasma gondii sporozoites invade host cells using two novel paralogues of RON2 and AMA1. PLoS ONE 8: e70637.
    • (2013) PLoS ONE , vol.8 , pp. e70637
    • Poukchanski, A.1    Fritz, H.M.2    Tonkin, M.L.3    Treeck, M.4    Boulanger, M.J.5
  • 85
    • 0037141150 scopus 로고    scopus 로고
    • MAEBL is essential for malarial sporozoite infection of the mosquito salivary gland
    • Kariu T, Yuda M, Yano K, Chinzei Y, (2002) MAEBL is essential for malarial sporozoite infection of the mosquito salivary gland. J Exp Med 195: 1317–1323.
    • (2002) J Exp Med , vol.195 , pp. 1317-1323
    • Kariu, T.1    Yuda, M.2    Yano, K.3    Chinzei, Y.4
  • 86
    • 48449086113 scopus 로고    scopus 로고
    • The transmembrane isoform of Plasmodium falciparum MAEBL is essential for the invasion of Anopheles salivary glands
    • Saenz FE, Balu B, Smith J, Mendonca SR, Adams JH, (2008) The transmembrane isoform of Plasmodium falciparum MAEBL is essential for the invasion of Anopheles salivary glands. PLoS ONE 3: e2287.
    • (2008) PLoS ONE , vol.3 , pp. e2287
    • Saenz, F.E.1    Balu, B.2    Smith, J.3    Mendonca, S.R.4    Adams, J.H.5
  • 87
    • 84855282762 scopus 로고    scopus 로고
    • Juxtamembrane shedding of Plasmodium falciparum AMA1 is sequence independent and essential, and helps evade invasion-inhibitory antibodies
    • Olivieri A, Collins CR, Hackett F, Withers-Martinez C, Marshall J, et al. (2011) Juxtamembrane shedding of Plasmodium falciparum AMA1 is sequence independent and essential, and helps evade invasion-inhibitory antibodies. PLoS Pathog 7: e1002448.
    • (2011) PLoS Pathog , vol.7 , pp. e1002448
    • Olivieri, A.1    Collins, C.R.2    Hackett, F.3    Withers-Martinez, C.4    Marshall, J.5
  • 88
    • 84860798774 scopus 로고    scopus 로고
    • Intramembrane proteolysis of Toxoplasma apical membrane antigen 1 facilitates host-cell invasion but is dispensable for replication
    • Parussini F, Tang Q, Moin SM, Mital J, Urban S, et al. (2012) Intramembrane proteolysis of Toxoplasma apical membrane antigen 1 facilitates host-cell invasion but is dispensable for replication. Proc Natl Acad Sci U S A 109: 7463–7468.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 7463-7468
    • Parussini, F.1    Tang, Q.2    Moin, S.M.3    Mital, J.4    Urban, S.5
  • 89
    • 0037213023 scopus 로고    scopus 로고
    • Cell invasion by Theileria sporozoites
    • Shaw MK, (2003) Cell invasion by Theileria sporozoites. Trends Parasitol 19: 2–6.
    • (2003) Trends Parasitol , vol.19 , pp. 2-6
    • Shaw, M.K.1
  • 90
    • 41549110118 scopus 로고    scopus 로고
    • Implications of a poroelastic cytoplasm for the dynamics of animal cell shape
    • Mitchison TJ, Charras GT, Mahadevan L, (2008) Implications of a poroelastic cytoplasm for the dynamics of animal cell shape. Semin Cell Dev Biol 19: 215–223.
    • (2008) Semin Cell Dev Biol , vol.19 , pp. 215-223
    • Mitchison, T.J.1    Charras, G.T.2    Mahadevan, L.3
  • 93
    • 79955965936 scopus 로고    scopus 로고
    • A Toxoplasma gondii protein with homology to intracellular type Na(+)/H(+) exchangers is important for osmoregulation and invasion
    • Francia ME, Wicher S, Pace DA, Sullivan J, Moreno SN, et al. (2011) A Toxoplasma gondii protein with homology to intracellular type Na(+)/H(+) exchangers is important for osmoregulation and invasion. Exp Cell Res 317: 1382–1396.
    • (2011) Exp Cell Res , vol.317 , pp. 1382-1396
    • Francia, M.E.1    Wicher, S.2    Pace, D.A.3    Sullivan, J.4    Moreno, S.N.5
  • 94
    • 13844289333 scopus 로고    scopus 로고
    • Identification and disruption of a rhoptry-localized homologue of sodium hydrogen exchangers in Toxoplasma gondii
    • Karasov AO, Boothroyd JC, Arrizabalaga G, (2005) Identification and disruption of a rhoptry-localized homologue of sodium hydrogen exchangers in Toxoplasma gondii. Int J Parasitol 35: 285–291.
    • (2005) Int J Parasitol , vol.35 , pp. 285-291
    • Karasov, A.O.1    Boothroyd, J.C.2    Arrizabalaga, G.3
  • 95
    • 2942633901 scopus 로고    scopus 로고
    • Ionophore-resistant mutant of Toxoplasma gondii reveals involvement of a sodium/hydrogen exchanger in calcium regulation
    • Arrizabalaga G, Ruiz F, Moreno S, Boothroyd JC, (2004) Ionophore-resistant mutant of Toxoplasma gondii reveals involvement of a sodium/hydrogen exchanger in calcium regulation. J Cell Biol 165: 653–662.
    • (2004) J Cell Biol , vol.165 , pp. 653-662
    • Arrizabalaga, G.1    Ruiz, F.2    Moreno, S.3    Boothroyd, J.C.4
  • 96
    • 0023253544 scopus 로고
    • Effects of extracellular potassium on acid release and motility initiation in Toxoplasma gondii
    • Endo T, Tokuda H, Yagita K, Koyama T, (1987) Effects of extracellular potassium on acid release and motility initiation in Toxoplasma gondii. J Protozool 34: 291–295.
    • (1987) J Protozool , vol.34 , pp. 291-295
    • Endo, T.1    Tokuda, H.2    Yagita, K.3    Koyama, T.4
  • 97
    • 0025390770 scopus 로고
    • Effect of extracellular ions on motility and cell entry in Toxoplasma gondii
    • Endo T, Yagita K, (1990) Effect of extracellular ions on motility and cell entry in Toxoplasma gondii. J Protozool 37: 133–138.
    • (1990) J Protozool , vol.37 , pp. 133-138
    • Endo, T.1    Yagita, K.2
  • 98
    • 43849099983 scopus 로고    scopus 로고
    • Cryptosporidia: epicellular parasites embraced by the host cell membrane
    • Valigurova A, Jirku M, Koudela B, Gelnar M, Modry D, et al. (2008) Cryptosporidia: epicellular parasites embraced by the host cell membrane. Int J Parasitol 38: 913–922.
    • (2008) Int J Parasitol , vol.38 , pp. 913-922
    • Valigurova, A.1    Jirku, M.2    Koudela, B.3    Gelnar, M.4    Modry, D.5
  • 99
    • 18144405400 scopus 로고    scopus 로고
    • Localized glucose and water influx facilitates Cryptosporidium parvum cellular invasion by means of modulation of host-cell membrane protrusion
    • Chen XM, O'Hara SP, Huang BQ, Splinter PL, Nelson JB, et al. (2005) Localized glucose and water influx facilitates Cryptosporidium parvum cellular invasion by means of modulation of host-cell membrane protrusion. Proc Natl Acad Sci U S A 102: 6338–6343.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 6338-6343
    • Chen, X.M.1    O'hara, S.P.2    Huang, B.Q.3    Splinter, P.L.4    Nelson, J.B.5
  • 100
    • 0033615981 scopus 로고    scopus 로고
    • Conservation of a gliding motility and cell invasion machinery in apicomplexan parasites
    • Kappe S, Bruderer T, Gantt S, Fujioka H, Nussenzweig V, et al. (1999) Conservation of a gliding motility and cell invasion machinery in apicomplexan parasites. J Cell Biol 147: 937–943.
    • (1999) J Cell Biol , vol.147 , pp. 937-943
    • Kappe, S.1    Bruderer, T.2    Gantt, S.3    Fujioka, H.4    Nussenzweig, V.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.