메뉴 건너뛰기




Volumn , Issue , 2013, Pages 389-453

Toxoplasma Secretory Proteins and Their Roles in Cell Invasion and Intracellular Survival

Author keywords

Dense granule; Egress; Exocytosis; Microneme; Moving junction; Parasitiophorous vacuole; Rhoptry

Indexed keywords


EID: 84904085532     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-396481-6.00012-X     Document Type: Chapter
Times cited : (22)

References (380)
  • 5
    • 0017879439 scopus 로고
    • Erythrocyte entry by malarial parasites. A moving junction between erythrocyte and parasite
    • Aikawa M., Miller L.H., Johnson J., Rabbege J. Erythrocyte entry by malarial parasites. A moving junction between erythrocyte and parasite. J. Cell Biol. 1978, 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
  • 6
    • 0019779753 scopus 로고
    • Freeze-fracture study on the erythrocyte membrane during malarial parasite invasion
    • Aikawa M., Miller L.H., Rabbege J.R., Epstein N. Freeze-fracture study on the erythrocyte membrane during malarial parasite invasion. J. Cell Biol. 1981, 91:55-62.
    • (1981) J. Cell Biol. , vol.91 , pp. 55-62
    • Aikawa, M.1    Miller, L.H.2    Rabbege, J.R.3    Epstein, N.4
  • 8
    • 2542527673 scopus 로고    scopus 로고
    • Structural and functional dissection of the adhesive domains of Plasmodium falciparum thrombospondin-related anonymous protein (TRAP)
    • Akhouri R.R., Bhattacharyya A., Pattnaik P., Malhotra P., Sharma A. Structural and functional dissection of the adhesive domains of Plasmodium falciparum thrombospondin-related anonymous protein (TRAP). Biochem. J. 2004, 379:815-822.
    • (2004) Biochem. J. , vol.379 , pp. 815-822
    • Akhouri, R.R.1    Bhattacharyya, A.2    Pattnaik, P.3    Malhotra, P.4    Sharma, A.5
  • 9
    • 33746267433 scopus 로고    scopus 로고
    • Plasmodium falciparum AMA1 (PfAMA1) binds a rhoptry neck protein homologous to TgRON4, a component of the moving junction in Toxoplasma
    • Alexander D.L., Kapur S.A., Dubremetz J.F., Boothroyd J.C. Plasmodium falciparum AMA1 (PfAMA1) binds a rhoptry neck protein homologous to TgRON4, a component of the moving junction in Toxoplasma. Eukaryot. Cell 2006, 5:1169-1173.
    • (2006) Eukaryot. Cell , vol.5 , pp. 1169-1173
    • Alexander, D.L.1    Kapur, S.A.2    Dubremetz, J.F.3    Boothroyd, J.C.4
  • 10
    • 77951026559 scopus 로고    scopus 로고
    • Identification of the Moving Junction Complex of Toxoplasma gondii: A Collaboration between Distinct Secretory Organelles
    • Alexander D.L., Mital J., Ward G.E., Bradley P., Boothroyd J.C. Identification of the Moving Junction Complex of Toxoplasma gondii: A Collaboration between Distinct Secretory Organelles. PLoS Pathog. 2005, 1:e17.
    • (2005) PLoS Pathog. , vol.1
    • Alexander, D.L.1    Mital, J.2    Ward, G.E.3    Bradley, P.4    Boothroyd, J.C.5
  • 11
    • 0031793544 scopus 로고    scopus 로고
    • The biogenesis and properties of the parasitophorous vacuoles that harbour Leishmania in murine macrophages
    • Antoine J.C., Prina E., Lang T., Courret N. The biogenesis and properties of the parasitophorous vacuoles that harbour Leishmania in murine macrophages. Trends Microbiol. 1998, 6:392-401.
    • (1998) Trends Microbiol. , vol.6 , pp. 392-401
    • Antoine, J.C.1    Prina, E.2    Lang, T.3    Courret, N.4
  • 12
    • 0024284211 scopus 로고
    • Structure and function of epidermal growth factor-like regions in proteins
    • Appella E., Weber I.T., Blasi F. Structure and function of epidermal growth factor-like regions in proteins. FEBS Lett. 1988, 231:1-4.
    • (1988) FEBS Lett. , vol.231 , pp. 1-4
    • Appella, E.1    Weber, I.T.2    Blasi, F.3
  • 13
    • 0032526224 scopus 로고    scopus 로고
    • Sorting and storage during secretory granule biogenesis: looking backward and looking forward
    • Arvan P., Castle D. Sorting and storage during secretory granule biogenesis: looking backward and looking forward. Biochem. J. 1998, 332:593-610.
    • (1998) Biochem. J. , vol.332 , pp. 593-610
    • Arvan, P.1    Castle, D.2
  • 14
    • 0032212406 scopus 로고    scopus 로고
    • Neospora caninum: tachyzoites express a potent type-I nucleoside triphosphate hydrolase
    • Asai T., Howe D.K., Nakajima K., Nozaki T., Takeuchi T., Sibley L.D. Neospora caninum: tachyzoites express a potent type-I nucleoside triphosphate hydrolase. Exp. Parasitol. 1998, 90:277-285.
    • (1998) Exp. Parasitol. , vol.90 , pp. 277-285
    • Asai, T.1    Howe, D.K.2    Nakajima, K.3    Nozaki, T.4    Takeuchi, T.5    Sibley, L.D.6
  • 15
    • 0029051349 scopus 로고
    • Biochemical and molecular characterization of nucleoside triphosphate hydrolase isozymes from the parasitic protozoan Toxoplasma gondii
    • Asai T., Miura S., Sibley L.D., Okabayashi H., Takeuchi T. Biochemical and molecular characterization of nucleoside triphosphate hydrolase isozymes from the parasitic protozoan Toxoplasma gondii. J. Biol. Chem. 1995, 270:11391-11397.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11391-11397
    • Asai, T.1    Miura, S.2    Sibley, L.D.3    Okabayashi, H.4    Takeuchi, T.5
  • 16
    • 0021099520 scopus 로고
    • A potent nucleoside triphosphate hydrolase from the parasitic protozoan Toxoplasma gondii. Purification, some properties, and activation by thiol compounds
    • Asai T., O'Sullivan W.J., Tatibana M. A potent nucleoside triphosphate hydrolase from the parasitic protozoan Toxoplasma gondii. Purification, some properties, and activation by thiol compounds. J. Biol. Chem. 1983, 258:6816-6822.
    • (1983) J. Biol. Chem. , vol.258 , pp. 6816-6822
    • Asai, T.1    O'Sullivan, W.J.2    Tatibana, M.3
  • 17
    • 24644523245 scopus 로고    scopus 로고
    • Structure of AMA1 from Plasmodium falciparum reveals a clustering of polymorphisms that surround a conserved hydrophobic pocket
    • Bai T., Becker M., Gupta A., Strike P., Murphy V.J., Anders R.F., Batchelor A.H. Structure of AMA1 from Plasmodium falciparum reveals a clustering of polymorphisms that surround a conserved hydrophobic pocket. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:12736-12741.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 12736-12741
    • Bai, T.1    Becker, M.2    Gupta, A.3    Strike, P.4    Murphy, V.J.5    Anders, R.F.6    Batchelor, A.H.7
  • 19
    • 0141502116 scopus 로고    scopus 로고
    • Plasmodium falciparum apical membrane antigen 1 (PfAMA-1) is translocated within micronemes along subpellicular microtubules during merozoite development
    • Bannister L.H., Hopkins J.M., Dluzewski A.R., Margos G., Williams I.T., Blackman M.J., Kocken C.H., Thomas A.W., Mitchell G.H. Plasmodium falciparum apical membrane antigen 1 (PfAMA-1) is translocated within micronemes along subpellicular microtubules during merozoite development. J. Cell Sci. 2003, 116:3825-3834.
    • (2003) J. Cell Sci. , vol.116 , pp. 3825-3834
    • Bannister, L.H.1    Hopkins, J.M.2    Dluzewski, A.R.3    Margos, G.4    Williams, I.T.5    Blackman, M.J.6    Kocken, C.H.7    Thomas, A.W.8    Mitchell, G.H.9
  • 20
    • 0024389888 scopus 로고
    • The fine structure of secretion by Plasmodium knowlesi merozoites during red cell invasion
    • Bannister L.H., Mitchell G.H. The fine structure of secretion by Plasmodium knowlesi merozoites during red cell invasion. J. Protozool. 1989, 36:362-367.
    • (1989) J. Protozool. , vol.36 , pp. 362-367
    • Bannister, L.H.1    Mitchell, G.H.2
  • 21
    • 0022590394 scopus 로고
    • Lamellar membranes associated with rhoptries in erythrocytic merozoites of Plasmodium knowlesi, a clue to the mechanism of invasion
    • Bannister L.H., Mitchell G.H., Butcher G.A., Dennis E.D. Lamellar membranes associated with rhoptries in erythrocytic merozoites of Plasmodium knowlesi, a clue to the mechanism of invasion. Parasitology 1986, 92(Pt 2):291-303.
    • (1986) Parasitology , vol.92 , Issue.PT 2 , pp. 291-303
    • Bannister, L.H.1    Mitchell, G.H.2    Butcher, G.A.3    Dennis, E.D.4
  • 23
    • 15944368914 scopus 로고    scopus 로고
    • Transepithelial migration of Toxoplasma gondii involves an interaction of intercellular adhesion molecule 1 (ICAM-1) with the parasite adhesin MIC2
    • Barragan A., Brossier F., Sibley L.D. Transepithelial migration of Toxoplasma gondii involves an interaction of intercellular adhesion molecule 1 (ICAM-1) with the parasite adhesin MIC2. Cell Microbiol. 2005, 7:561-568.
    • (2005) Cell Microbiol. , vol.7 , pp. 561-568
    • Barragan, A.1    Brossier, F.2    Sibley, L.D.3
  • 24
    • 0028134806 scopus 로고
    • The Toxoplasma gondii rhoptry protein ROP 2 is inserted into the parasitophorous vacuole membrane, surrounding the intracellular parasite, and is exposed to the host cell cytoplasm
    • Beckers C.J., Dubremetz J.F., Mercereau-Puijalon O., Joiner K.A. The Toxoplasma gondii rhoptry protein ROP 2 is inserted into the parasitophorous vacuole membrane, surrounding the intracellular parasite, and is exposed to the host cell cytoplasm. J. Cell Biol. 1994, 127:947-961.
    • (1994) J. Cell Biol. , vol.127 , pp. 947-961
    • Beckers, C.J.1    Dubremetz, J.F.2    Mercereau-Puijalon, O.3    Joiner, K.A.4
  • 25
    • 84870848874 scopus 로고    scopus 로고
    • The Polymorphic Pseudokinase ROP5 Controls Virulence in Toxoplasma gondii by Regulating the Active Kinase ROP18
    • Behnke M.S., Fentress S.J., Mashayekhi M., Li L.X., Taylor G.A., Sibley L.D. The Polymorphic Pseudokinase ROP5 Controls Virulence in Toxoplasma gondii by Regulating the Active Kinase ROP18. PLoS Pathog. 2012, 8:e1002992.
    • (2012) PLoS Pathog. , vol.8
    • Behnke, M.S.1    Fentress, S.J.2    Mashayekhi, M.3    Li, L.X.4    Taylor, G.A.5    Sibley, L.D.6
  • 26
  • 27
    • 0028036717 scopus 로고
    • Tandemly repeated genes encode nucleoside triphosphate hydrolase isoforms secreted into the parasitophorous vacuole of Toxoplasma gondii
    • Bermudes D., Peck K.R., Afifi M.A., Beckers C.J., Joiner K.A. Tandemly repeated genes encode nucleoside triphosphate hydrolase isoforms secreted into the parasitophorous vacuole of Toxoplasma gondii. J. Biol. Chem. 1994, 269:29252-29260.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29252-29260
    • Bermudes, D.1    Peck, K.R.2    Afifi, M.A.3    Beckers, C.J.4    Joiner, K.A.5
  • 28
    • 53149122085 scopus 로고    scopus 로고
    • Lipidomic analysis of Toxoplasma gondii tachyzoites rhoptries: further insights into the role of cholesterol
    • Besteiro S., Bertrand-Michel J., Lebrun M., Vial H., Dubremetz J.F. Lipidomic analysis of Toxoplasma gondii tachyzoites rhoptries: further insights into the role of cholesterol. Biochem. J. 2008, 415:87-96.
    • (2008) Biochem. J. , vol.415 , pp. 87-96
    • Besteiro, S.1    Bertrand-Michel, J.2    Lebrun, M.3    Vial, H.4    Dubremetz, J.F.5
  • 29
    • 79955948463 scopus 로고    scopus 로고
    • The moving junction of apicomplexan parasites: a key structure for invasion
    • Besteiro S., Dubremetz J.F., Lebrun M. The moving junction of apicomplexan parasites: a key structure for invasion. Cell Microbiol. 2011, 13:797-805.
    • (2011) Cell Microbiol. , vol.13 , pp. 797-805
    • Besteiro, S.1    Dubremetz, J.F.2    Lebrun, M.3
  • 30
    • 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 J.F., Lebrun M. Export of a Toxoplasma gondii rhoptry neck protein complex at the host cell membrane to form the moving junction during invasion. PLoS Pathog. 2009, 5:e1000309.
    • (2009) PLoS Pathog. , vol.5
    • Besteiro, S.1    Michelin, A.2    Poncet, J.3    Dubremetz, J.F.4    Lebrun, M.5
  • 31
    • 67649399023 scopus 로고    scopus 로고
    • Calcium-dependent signaling and kinases in apicomplexan parasites
    • Billker O., Lourido S., Sibley L.D. Calcium-dependent signaling and kinases in apicomplexan parasites. Cell Host Microbe 2009, 5:612-622.
    • (2009) Cell Host Microbe , vol.5 , pp. 612-622
    • Billker, O.1    Lourido, S.2    Sibley, L.D.3
  • 32
    • 8844228268 scopus 로고    scopus 로고
    • Location, location, location: trafficking and function of secreted proteases of Toxoplasma and Plasmodium
    • Binder E.M., Kim K. Location, location, location: trafficking and function of secreted proteases of Toxoplasma and Plasmodium. Traffic 2004, 5:914-924.
    • (2004) Traffic , vol.5 , pp. 914-924
    • Binder, E.M.1    Kim, K.2
  • 33
    • 49749133184 scopus 로고    scopus 로고
    • The prodomain of Toxoplasma gondii GPI-anchored subtilase TgSUB1 mediates its targeting to micronemes
    • Binder E.M., Lagal V., Kim K. The prodomain of Toxoplasma gondii GPI-anchored subtilase TgSUB1 mediates its targeting to micronemes. Traffic 2008, 9:1485-1496.
    • (2008) Traffic , vol.9 , pp. 1485-1496
    • Binder, E.M.1    Lagal, V.2    Kim, K.3
  • 34
    • 0034853631 scopus 로고    scopus 로고
    • Apical organelles of Apicomplexa: biology and isolation by subcellular fractionation
    • Blackman M.J., Bannister L.H. Apical organelles of Apicomplexa: biology and isolation by subcellular fractionation. Mol. Biochem. Parasitol. 2001, 117:11-25.
    • (2001) Mol. Biochem. Parasitol. , vol.117 , pp. 11-25
    • Blackman, M.J.1    Bannister, L.H.2
  • 35
    • 0035968207 scopus 로고    scopus 로고
    • Microarray analysis reveals previously unknown changes in Toxoplasma gondii-infected human cells
    • Blader I.J., Manger I.D., Boothroyd J.C. Microarray analysis reveals previously unknown changes in Toxoplasma gondii-infected human cells. J. Biol. Chem. 2001, 276:24223-24231.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24223-24231
    • Blader, I.J.1    Manger, I.D.2    Boothroyd, J.C.3
  • 38
    • 0032967525 scopus 로고    scopus 로고
    • Identification of the pro-mature processing site of Toxoplasma ROP1 by mass spectrometry
    • Bradley P.J., Boothroyd J.C. Identification of the pro-mature processing site of Toxoplasma ROP1 by mass spectrometry. Mol. Biochem. Parasitol. 1999, 100:103-109.
    • (1999) Mol. Biochem. Parasitol. , vol.100 , pp. 103-109
    • Bradley, P.J.1    Boothroyd, J.C.2
  • 39
    • 0034881397 scopus 로고    scopus 로고
    • The pro region of Toxoplasma ROP1 is a rhoptry-targeting signal
    • Bradley P.J., Boothroyd J.C. The pro region of Toxoplasma ROP1 is a rhoptry-targeting signal. Int. J. Parasitol. 2001, 31:1177-1186.
    • (2001) Int. J. Parasitol. , vol.31 , pp. 1177-1186
    • Bradley, P.J.1    Boothroyd, J.C.2
  • 40
    • 0036861640 scopus 로고    scopus 로고
    • Unprocessed Toxoplasma ROP1 is effectively targeted and secreted into the nascent parasitophorous vacuole
    • Bradley P.J., Hsieh C.L., Boothroyd J.C. Unprocessed Toxoplasma ROP1 is effectively targeted and secreted into the nascent parasitophorous vacuole. Mol. Biochem. Parasitol. 2002, 125:189-193.
    • (2002) Mol. Biochem. Parasitol. , vol.125 , pp. 189-193
    • Bradley, P.J.1    Hsieh, C.L.2    Boothroyd, J.C.3
  • 41
    • 3342905330 scopus 로고    scopus 로고
    • A GFP-based motif-trap reveals a novel mechanism of targeting for the Toxoplasma ROP4 protein
    • Bradley P.J., Li N., Boothroyd J.C. A GFP-based motif-trap reveals a novel mechanism of targeting for the Toxoplasma ROP4 protein. Mol. Biochem. Parasitol. 2004, 137:111-120.
    • (2004) Mol. Biochem. Parasitol. , vol.137 , pp. 111-120
    • Bradley, P.J.1    Li, N.2    Boothroyd, J.C.3
  • 46
    • 0037458587 scopus 로고    scopus 로고
    • C-terminal processing of the Toxoplasma protein MIC2 is essential for invasion into host cells
    • Brossier F., Jewett T.J., Lovett J.L., Sibley L.D. C-terminal processing of the Toxoplasma protein MIC2 is essential for invasion into host cells. J. Biol. Chem. 2003, 278:6229-6234.
    • (2003) J. Biol. Chem. , vol.278 , pp. 6229-6234
    • Brossier, F.1    Jewett, T.J.2    Lovett, J.L.3    Sibley, L.D.4
  • 47
    • 15244360655 scopus 로고    scopus 로고
    • A spatially localized rhomboid protease cleaves cell surface adhesins essential for invasion by Toxoplasma
    • Brossier F., Jewett T.J., Sibley L.D., Urban S. A spatially localized rhomboid protease cleaves cell surface adhesins essential for invasion by Toxoplasma. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:4146-4151.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 4146-4151
    • Brossier, F.1    Jewett, T.J.2    Sibley, L.D.3    Urban, S.4
  • 48
    • 41849149304 scopus 로고    scopus 로고
    • Microneme rhomboid protease TgROM1 is required for efficient intracellular growth of Toxoplasma gondii
    • Brossier F., Starnes G.L., Beatty W.L., Sibley L.D. Microneme rhomboid protease TgROM1 is required for efficient intracellular growth of Toxoplasma gondii. Eukaryot. Cell 2008, 7:664-674.
    • (2008) Eukaryot. Cell , vol.7 , pp. 664-674
    • Brossier, F.1    Starnes, G.L.2    Beatty, W.L.3    Sibley, L.D.4
  • 49
    • 0034654252 scopus 로고    scopus 로고
    • A microneme protein from Eimeriatenella with homology to the Apple domains of coagulation factor XI and plasma pre-kallikrein
    • Brown P.J., Billington K.J., Bumste ad J.M., Clark J.D., Tomley F.M. A microneme protein from Eimeriatenella with homology to the Apple domains of coagulation factor XI and plasma pre-kallikrein. Mol. Biochem. Parasitol. 2000, 107:91-102.
    • (2000) Mol. Biochem. Parasitol. , vol.107 , pp. 91-102
    • Brown, P.J.1    Billington, K.J.2    Bumstead, J.M.3    Clark, J.D.4    Tomley, F.M.5
  • 50
    • 0035906949 scopus 로고    scopus 로고
    • Domains of invasion organelle proteins from apicomplexan parasites are homologous with the Apple domains of blood coagulation factor XI and plasma pre-kallikrein and are members of the PAN module superfamily
    • Brown P.J., Gill A.C., Nugent P.G., McVey J.H., Tomley F.M. Domains of invasion organelle proteins from apicomplexan parasites are homologous with the Apple domains of blood coagulation factor XI and plasma pre-kallikrein and are members of the PAN module superfamily. FEBS Lett. 2001, 497:31-38.
    • (2001) FEBS Lett. , vol.497 , pp. 31-38
    • Brown, P.J.1    Gill, A.C.2    Nugent, P.G.3    McVey, J.H.4    Tomley, F.M.5
  • 51
    • 42049104245 scopus 로고    scopus 로고
    • A transient forward-targeting element for microneme-regulated secretion in Toxoplasma gondii
    • Brydges S.D., Harper J.M., Parussini F., Coppens I., Carruthers V.B. A transient forward-targeting element for microneme-regulated secretion in Toxoplasma gondii. Biol. Cell 2008, 100:253-264.
    • (2008) Biol. Cell , vol.100 , pp. 253-264
    • Brydges, S.D.1    Harper, J.M.2    Parussini, F.3    Coppens, I.4    Carruthers, V.B.5
  • 55
    • 77954078996 scopus 로고    scopus 로고
    • Rhomboid 4 (ROM4) affects the processing of surface adhesins and facilitates host cell invasion by Toxoplasma gondii
    • Buguliskis J.S., Brossier F., Shuman J., Sibley L.D. Rhomboid 4 (ROM4) affects the processing of surface adhesins and facilitates host cell invasion by Toxoplasma gondii. PLoS Pathog. 2010, 6:e1000858.
    • (2010) PLoS Pathog. , vol.6
    • Buguliskis, J.S.1    Brossier, F.2    Shuman, J.3    Sibley, L.D.4
  • 58
    • 71049186393 scopus 로고    scopus 로고
    • Dynamin inhibitor impairs Toxoplasma gondii invasion
    • Caldas L.A., Attias M., de Souza W. Dynamin inhibitor impairs Toxoplasma gondii invasion. FEMS Microbiol. Lett. 2009, 301:103-108.
    • (2009) FEMS Microbiol. Lett. , vol.301 , pp. 103-108
    • Caldas, L.A.1    Attias, M.2    de Souza, W.3
  • 59
    • 0033990607 scopus 로고    scopus 로고
    • Identification and molecular characterization of GRA8, a novel, proline-rich, dense granule protein of Toxoplasma gondii
    • Carey K.L., Donahue C.G., Ward G.E. Identification and molecular characterization of GRA8, a novel, proline-rich, dense granule protein of Toxoplasma gondii. Mol. Biochem. Parasitol. 2000, 105:25-37.
    • (2000) Mol. Biochem. Parasitol. , vol.105 , pp. 25-37
    • Carey, K.L.1    Donahue, C.G.2    Ward, G.E.3
  • 60
    • 6344294832 scopus 로고    scopus 로고
    • The Toxoplasma gondii rhoptry protein ROP4 is secreted into the parasitophorous vacuole and becomes phosphorylated in infected cells
    • Carey K.L., Jongco A.M., Kim K., Ward G.E. The Toxoplasma gondii rhoptry protein ROP4 is secreted into the parasitophorous vacuole and becomes phosphorylated in infected cells. Eukaryot. Cell 2004, 3:1320-1330.
    • (2004) Eukaryot. Cell , vol.3 , pp. 1320-1330
    • Carey, K.L.1    Jongco, A.M.2    Kim, K.3    Ward, G.E.4
  • 62
    • 0033224351 scopus 로고    scopus 로고
    • Secretion of micronemal proteins is associated with Toxoplasma invasion of host cells
    • Carruthers V.B., Giddings O.K., Sibley L.D. Secretion of micronemal proteins is associated with Toxoplasma invasion of host cells. Cell Microbiol. 1999, 1:225-235.
    • (1999) Cell Microbiol. , vol.1 , pp. 225-235
    • Carruthers, V.B.1    Giddings, O.K.2    Sibley, L.D.3
  • 63
    • 0033198852 scopus 로고    scopus 로고
    • Ethanol and acetaldehyde elevate intracellular [Ca2+] and stimulate microneme discharge in Toxoplasma gondii
    • Carruthers V.B., Moreno S.N., Sibley L.D. Ethanol and acetaldehyde elevate intracellular [Ca2+] and stimulate microneme discharge in Toxoplasma gondii. Biochem. J. 1999, 342(Pt 2):379-386.
    • (1999) Biochem. J. , vol.342 , Issue.PT 2 , pp. 379-386
    • Carruthers, V.B.1    Moreno, S.N.2    Sibley, L.D.3
  • 64
    • 0034640516 scopus 로고    scopus 로고
    • The Toxoplasma adhesive protein MIC2 is proteolytically processed at multiple sites by two parasite-derived proteases
    • Carruthers V.B., Sherman G.D., Sibley L.D. The Toxoplasma adhesive protein MIC2 is proteolytically processed at multiple sites by two parasite-derived proteases. J. Biol. Chem. 2000, 275:14346-14353.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14346-14353
    • Carruthers, V.B.1    Sherman, G.D.2    Sibley, L.D.3
  • 65
    • 0030956863 scopus 로고    scopus 로고
    • Sequential protein secretion from three distinct organelles of Toxoplasma gondii accompanies invasion of human fibroblasts
    • Carruthers V.B., Sibley L.D. Sequential protein secretion from three distinct organelles of Toxoplasma gondii accompanies invasion of human fibroblasts. Eur. J. Cell Biol. 1997, 73:114-123.
    • (1997) Eur. J. Cell Biol. , vol.73 , pp. 114-123
    • Carruthers, V.B.1    Sibley, L.D.2
  • 66
    • 0032927424 scopus 로고    scopus 로고
    • Mobilization of intracellular calcium stimulates microneme discharge in Toxoplasma gondii
    • Carruthers V.B., Sibley L.D. Mobilization of intracellular calcium stimulates microneme discharge in Toxoplasma gondii. Mol. Microbiol. 1999, 31:421-428.
    • (1999) Mol. Microbiol. , vol.31 , pp. 421-428
    • Carruthers, V.B.1    Sibley, L.D.2
  • 67
    • 0037013918 scopus 로고    scopus 로고
    • The Toxoplasma gondii protein MIC3 requires pro-peptide cleavage and dimerization to function as adhesin
    • Cerede O., Dubremetz J.F., Bout D., Lebrun M. The Toxoplasma gondii protein MIC3 requires pro-peptide cleavage and dimerization to function as adhesin. Embo. J. 2002, 21:2526-2536.
    • (2002) Embo. J. , vol.21 , pp. 2526-2536
    • Cerede, O.1    Dubremetz, J.F.2    Bout, D.3    Lebrun, M.4
  • 69
    • 41849090139 scopus 로고    scopus 로고
    • Apicomplexa in mammalian cells: trafficking to the parasitophorous vacuole
    • Cesbron-Delauw M.F., Gendrin C., Travier L., Ruffiot P., Mercier C. Apicomplexa in mammalian cells: trafficking to the parasitophorous vacuole. Traffic 2008, 9:657-664.
    • (2008) Traffic , vol.9 , pp. 657-664
    • Cesbron-Delauw, M.F.1    Gendrin, C.2    Travier, L.3    Ruffiot, P.4    Mercier, C.5
  • 72
    • 0026338163 scopus 로고
    • Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network
    • Chanat E., Huttner W.B. Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network. J. Cell Biol. 1991, 115:1505-1519.
    • (1991) J. Cell Biol. , vol.115 , pp. 1505-1519
    • Chanat, E.1    Huttner, W.B.2
  • 73
    • 0025121505 scopus 로고
    • Toxoplasma gondii: characterization and localization of antigens secreted from tachyzoites
    • Charif H., Darcy F., Torpier G., Cesbron-Delauw M.F., Capron A. Toxoplasma gondii: characterization and localization of antigens secreted from tachyzoites. Exp. Parasitol. 1990, 71:114-124.
    • (1990) Exp. Parasitol. , vol.71 , pp. 114-124
    • Charif, H.1    Darcy, F.2    Torpier, G.3    Cesbron-Delauw, M.F.4    Capron, A.5
  • 74
    • 0037493101 scopus 로고    scopus 로고
    • PfSPATR, a Plasmodium falciparum protein containing an altered thrombospondin type I repeat domain is expressed at several stages of the parasite life cycle and is the target of inhibitory antibodies
    • Chattopadhyay R., Rathore D., Fujioka H., Kumar S., de la Vega P., Haynes D., Moch K., Fryauff D., Wang R., Carucci D.J., Hoffman S.L. PfSPATR, a Plasmodium falciparum protein containing an altered thrombospondin type I repeat domain is expressed at several stages of the parasite life cycle and is the target of inhibitory antibodies. J. Biol. Chem. 2003, 278:25977-25981.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25977-25981
    • Chattopadhyay, R.1    Rathore, D.2    Fujioka, H.3    Kumar, S.4    de la Vega, P.5    Haynes, D.6    Moch, K.7    Fryauff, D.8    Wang, R.9    Carucci, D.J.10    Hoffman, S.L.11
  • 75
    • 0033593430 scopus 로고    scopus 로고
    • Constitutive calcium-independent release of Toxoplasma gondii dense granules occurs through the NSF/SNAP/SNARE/Rab machinery
    • Chaturvedi S., Qi H., Coleman D., Rodriguez A., Hanson P.I., Striepen B., Roos D.S., Joiner K.A. Constitutive calcium-independent release of Toxoplasma gondii dense granules occurs through the NSF/SNAP/SNARE/Rab machinery. J. Biol. Chem. 1999, 274:2424-2431.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2424-2431
    • Chaturvedi, S.1    Qi, H.2    Coleman, D.3    Rodriguez, A.4    Hanson, P.I.5    Striepen, B.6    Roos, D.S.7    Joiner, K.A.8
  • 76
    • 0033734494 scopus 로고    scopus 로고
    • The cell biology of thrombospondin-1
    • Chen H., Herndon M.E., Lawler J. The cell biology of thrombospondin-1. Matrix Biol. 2000, 19:597-614.
    • (2000) Matrix Biol. , vol.19 , pp. 597-614
    • Chen, H.1    Herndon, M.E.2    Lawler, J.3
  • 77
    • 0031768460 scopus 로고    scopus 로고
    • Rab11 is required for trans-golgi network-to-plasma membrane transport and a preferential target for GDP dissociation inhibitor
    • Chen W., Feng Y., Chen D., Wandinger-Ness A. Rab11 is required for trans-golgi network-to-plasma membrane transport and a preferential target for GDP dissociation inhibitor. Mol. Biol. Cell 1998, 9:3241-3257.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 3241-3257
    • Chen, W.1    Feng, Y.2    Chen, D.3    Wandinger-Ness, A.4
  • 78
    • 56349152375 scopus 로고    scopus 로고
    • In silico identification of specialized secretory-organelle proteins in apicomplexan parasites and in vivo validation in Toxoplasma gondii
    • Chen Z., Harb O.S., Roos D.S. In silico identification of specialized secretory-organelle proteins in apicomplexan parasites and in vivo validation in Toxoplasma gondii. PLoS One 2008, 3:e3611.
    • (2008) PLoS One , vol.3
    • Chen, Z.1    Harb, O.S.2    Roos, D.S.3
  • 79
    • 0025358652 scopus 로고
    • Regions of an Eimeria tenella antigen contain sequences which are conserved in circumsporozoite proteins from Plasmodium spp. and which are related to the thrombospondin gene family
    • Clarke L.E., Tomley F.M., Wisher M.H., Foulds I.J., Boursnell M.E. Regions of an Eimeria tenella antigen contain sequences which are conserved in circumsporozoite proteins from Plasmodium spp. and which are related to the thrombospondin gene family. Mol. Biochem. Parasitol. 1990, 41:269-279.
    • (1990) Mol. Biochem. Parasitol. , vol.41 , pp. 269-279
    • Clarke, L.E.1    Tomley, F.M.2    Wisher, M.H.3    Foulds, I.J.4    Boursnell, M.E.5
  • 80
    • 0036616943 scopus 로고    scopus 로고
    • Toxoplasma gondii asexual development: identification of developmentally regulated genes and distinct patterns of gene expression
    • Cleary M.D., Singh U., Blader I.J., Brewer J.L., Boothroyd J.C. Toxoplasma gondii asexual development: identification of developmentally regulated genes and distinct patterns of gene expression. Eukaryot. Cell 2002, 1:329-340.
    • (2002) Eukaryot. Cell , vol.1 , pp. 329-340
    • Cleary, M.D.1    Singh, U.2    Blader, I.J.3    Brewer, J.L.4    Boothroyd, J.C.5
  • 83
    • 59249106253 scopus 로고    scopus 로고
    • An inhibitory antibody blocks interactions between components of the malarial invasion machinery
    • Collins C.R., Withers-Martinez C., Hackett F., Blackman M.J. An inhibitory antibody blocks interactions between components of the malarial invasion machinery. PLoS Pathog. 2009, 5:e1000273.
    • (2009) PLoS Pathog. , vol.5
    • Collins, C.R.1    Withers-Martinez, C.2    Hackett, F.3    Blackman, M.J.4
  • 84
    • 0345712374 scopus 로고    scopus 로고
    • Serine protease inhibitors block invasion of host cells by Toxoplasma gondii
    • Conseil V., Soete M., Dubremetz J.F. Serine protease inhibitors block invasion of host cells by Toxoplasma gondii. Antimicrob. Agents Chemother. 1999, 43:1358-1361.
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 1358-1361
    • Conseil, V.1    Soete, M.2    Dubremetz, J.F.3
  • 85
    • 0032859858 scopus 로고    scopus 로고
    • Intracellular trafficking of dense granule proteins in Toxoplasma gondii and experimental evidences for a regulated exocytosis
    • Coppens I., Andries M., Liu J.L., Cesbron-Delauw M.F. Intracellular trafficking of dense granule proteins in Toxoplasma gondii and experimental evidences for a regulated exocytosis. Eur. J. Cell Biol. 1999, 78:463-472.
    • (1999) Eur. J. Cell Biol. , vol.78 , pp. 463-472
    • Coppens, I.1    Andries, M.2    Liu, J.L.3    Cesbron-Delauw, M.F.4
  • 87
    • 0141521595 scopus 로고    scopus 로고
    • Host but not parasite cholesterol controls Toxoplasma cell entry by modulating organelle discharge
    • Coppens I., Joiner K.A. Host but not parasite cholesterol controls Toxoplasma cell entry by modulating organelle discharge. Mol. Biol. Cell 2003, 14:3804-3820.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3804-3820
    • Coppens, I.1    Joiner, K.A.2
  • 88
    • 34247505657 scopus 로고    scopus 로고
    • Increased efficiency of homologous recombination in Toxoplasma gondii dense granule protein 3 demonstrates that GRA3 is not necessary in cell culture but does contribute to virulence
    • Craver M.P., Knoll L.J. Increased efficiency of homologous recombination in Toxoplasma gondii dense granule protein 3 demonstrates that GRA3 is not necessary in cell culture but does contribute to virulence. Mol. Biochem. Parasitol. 2007, 153:149-157.
    • (2007) Mol. Biochem. Parasitol. , vol.153 , pp. 149-157
    • Craver, M.P.1    Knoll, L.J.2
  • 89
    • 77952015851 scopus 로고    scopus 로고
    • Structural characterization of apical membrane antigen 1 (AMA1) from Toxoplasma gondii
    • Crawford J., Tonkin M.L., Grujic O., Boulanger M.J. Structural characterization of apical membrane antigen 1 (AMA1) from Toxoplasma gondii. J. Biol. Chem. 2010, 285:15644-15652.
    • (2010) J. Biol. Chem. , vol.285 , pp. 15644-15652
    • Crawford, J.1    Tonkin, M.L.2    Grujic, O.3    Boulanger, M.J.4
  • 90
    • 68049137458 scopus 로고    scopus 로고
    • Mechanisms controlling glideosome function in apicomplexans
    • Daher W., Soldati-Favre D. Mechanisms controlling glideosome function in apicomplexans. Curr. Opin. Microbiol. 2009, 12:408-414.
    • (2009) Curr. Opin. Microbiol. , vol.12 , pp. 408-414
    • Daher, W.1    Soldati-Favre, D.2
  • 91
    • 0025323613 scopus 로고
    • The many faces of epidermal growth factor repeats
    • Davis C.G. The many faces of epidermal growth factor repeats. New Biol. 1990, 2:410-419.
    • (1990) New Biol. , vol.2 , pp. 410-419
    • Davis, C.G.1
  • 93
    • 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. Actin dynamics is controlled by a casein kinase II and phosphatase 2C interplay on Toxoplasma gondii Toxofilin. Mol. Biol. Cell 2003, 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
  • 94
    • 84857179058 scopus 로고    scopus 로고
    • An inside job: hacking into Janus kinase/signal transducer and activator of transcription signaling cascades by the intracellular protozoan Toxoplasma gondii
    • Denkers E.Y., Bzik D.J., Fox B.A., Butcher B.A. An inside job: hacking into Janus kinase/signal transducer and activator of transcription signaling cascades by the intracellular protozoan Toxoplasma gondii. Infect. Immun. 2012, 80:476-482.
    • (2012) Infect. Immun. , vol.80 , pp. 476-482
    • Denkers, E.Y.1    Bzik, D.J.2    Fox, B.A.3    Butcher, B.A.4
  • 95
    • 0033830555 scopus 로고    scopus 로고
    • Two conserved amino acid motifs mediate protein targeting to the micronemes of the apicomplexan parasite Toxoplasma gondii
    • Di Cristina M., Spaccapelo R., Soldati D., Bistoni F., Crisanti A. Two conserved amino acid motifs mediate protein targeting to the micronemes of the apicomplexan parasite Toxoplasma gondii. Mol. Cell Biol. 2000, 20:7332-7341.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 7332-7341
    • Di Cristina, M.1    Spaccapelo, R.2    Soldati, D.3    Bistoni, F.4    Crisanti, A.5
  • 96
    • 0032467689 scopus 로고    scopus 로고
    • Binding of the alpha 2 integrin I domain to extracellular matrix ligands: structural and mechanistic differences between collagen and laminin binding
    • Dickeson S.K., Walsh J.J., Santoro S.A. Binding of the alpha 2 integrin I domain to extracellular matrix ligands: structural and mechanistic differences between collagen and laminin binding. Cell Adhes. Commun. 1998, 5:273-281.
    • (1998) Cell Adhes. Commun. , vol.5 , pp. 273-281
    • Dickeson, S.K.1    Walsh, J.J.2    Santoro, S.A.3
  • 97
    • 0030770219 scopus 로고    scopus 로고
    • Participation of myosin in gliding motility and host cell invasion by Toxoplasma gondii
    • Dobrowolski J.M., Carruthers V.B., Sibley L.D. Participation of myosin in gliding motility and host cell invasion by Toxoplasma gondii. Mol. Microbiol. 1997, 26:163-173.
    • (1997) Mol. Microbiol. , vol.26 , pp. 163-173
    • Dobrowolski, J.M.1    Carruthers, V.B.2    Sibley, L.D.3
  • 98
    • 0033763903 scopus 로고    scopus 로고
    • The Toxoplasma homologue of Plasmodium apical membrane antigen-1 (AMA-1) is a microneme protein secreted in response to elevated intracellular calcium levels
    • Donahue C.G., Carruthers V.B., Gilk S.D., Ward G.E. The Toxoplasma homologue of Plasmodium apical membrane antigen-1 (AMA-1) is a microneme protein secreted in response to elevated intracellular calcium levels. Mol. Biochem. Parasitol. 2000, 111:15-30.
    • (2000) Mol. Biochem. Parasitol. , vol.111 , pp. 15-30
    • Donahue, C.G.1    Carruthers, V.B.2    Gilk, S.D.3    Ward, G.E.4
  • 99
    • 0037046099 scopus 로고    scopus 로고
    • Molecular characterization of a coccidian parasite cGMP dependent protein kinase
    • Donald R.G., Liberator P.A. Molecular characterization of a coccidian parasite cGMP dependent protein kinase. Mol. Biochem. Parasitol. 2002, 120:165-175.
    • (2002) Mol. Biochem. Parasitol. , vol.120 , pp. 165-175
    • Donald, R.G.1    Liberator, P.A.2
  • 100
    • 84873295066 scopus 로고    scopus 로고
    • Non-canonical maturation of two papain-family proteases in Toxoplasma gondii
    • Dou Z., Coppens I., Carruthers V.B. Non-canonical maturation of two papain-family proteases in Toxoplasma gondii. J. Biol. Chem. 2012, 288:3523-3534.
    • (2012) J. Biol. Chem. , vol.288 , pp. 3523-3534
    • Dou, Z.1    Coppens, I.2    Carruthers, V.B.3
  • 101
    • 19444382777 scopus 로고    scopus 로고
    • Apicomplexan rhomboids have a potential role in microneme protein cleavage during host cell invasion
    • Dowse T.J., Pascall J.C., Brown K.D., Soldati D. Apicomplexan rhomboids have a potential role in microneme protein cleavage during host cell invasion. Int. J. Parasitol. 2005, 35:747-756.
    • (2005) Int. J. Parasitol. , vol.35 , pp. 747-756
    • Dowse, T.J.1    Pascall, J.C.2    Brown, K.D.3    Soldati, D.4
  • 102
    • 19444369929 scopus 로고    scopus 로고
    • Rhomboid-like proteins in Apicomplexa: phylogeny and nomenclature
    • Dowse T.J., Soldati D. Rhomboid-like proteins in Apicomplexa: phylogeny and nomenclature. Trends Parasitol. 2005, 21:254-258.
    • (2005) Trends Parasitol. , vol.21 , pp. 254-258
    • Dowse, T.J.1    Soldati, D.2
  • 103
    • 33947109437 scopus 로고    scopus 로고
    • Rhoptries are major players in Toxoplasma gondii invasion and host cell interaction
    • Dubremetz J.F. Rhoptries are major players in Toxoplasma gondii invasion and host cell interaction. Cell Microbiol. 2007, 9:841-848.
    • (2007) Cell Microbiol. , vol.9 , pp. 841-848
    • Dubremetz, J.F.1
  • 104
    • 0027199059 scopus 로고
    • Kinetics and pattern of organelle exocytosis during Toxoplasma gondii/host cell interaction
    • Dubremetz J.F., Achbarou A., Bermudes D., Joiner K.A. Kinetics and pattern of organelle exocytosis during Toxoplasma gondii/host cell interaction. Parasitol. Res. 1993, 79:402-408.
    • (1993) Parasitol. Res. , vol.79 , pp. 402-408
    • Dubremetz, J.F.1    Achbarou, A.2    Bermudes, D.3    Joiner, K.A.4
  • 105
    • 0003201719 scopus 로고
    • Capping of cationized ferritin by coccidian zoites
    • Dubremetz J.F., Ferreira E. Capping of cationized ferritin by coccidian zoites. J. Protozool. 1978, 25:9B.
    • (1978) J. Protozool. , vol.25
    • Dubremetz, J.F.1    Ferreira, E.2
  • 107
    • 33847332992 scopus 로고    scopus 로고
    • ROP18 is a rhoptry kinase controlling the intracellular proliferation of Toxoplasma gondii
    • El Hajj H., Lebrun M., Arold S.T., Vial H., Labesse G., Dubremetz J.F. ROP18 is a rhoptry kinase controlling the intracellular proliferation of Toxoplasma gondii. PLoS Pathog. 2007, 3:e14.
    • (2007) PLoS Pathog. , vol.3
    • El Hajj, H.1    Lebrun, M.2    Arold, S.T.3    Vial, H.4    Labesse, G.5    Dubremetz, J.F.6
  • 108
    • 33845457992 scopus 로고    scopus 로고
    • Inverted topology of the Toxoplasma gondii ROP5 rhoptry protein provides new insights into the association of the ROP2 protein family with the parasitophorous vacuole membrane
    • El Hajj H., Lebrun M., Fourmaux M.N., Vial H., Dubremetz J.F. Inverted topology of the Toxoplasma gondii ROP5 rhoptry protein provides new insights into the association of the ROP2 protein family with the parasitophorous vacuole membrane. Cell Microbiol. 2007, 9:54-64.
    • (2007) Cell Microbiol. , vol.9 , pp. 54-64
    • El Hajj, H.1    Lebrun, M.2    Fourmaux, M.N.3    Vial, H.4    Dubremetz, J.F.5
  • 112
    • 80051670279 scopus 로고    scopus 로고
    • The secreted kinase ROP18 defends Toxoplasma's border
    • Fentress S.J., Sibley L.D. The secreted kinase ROP18 defends Toxoplasma's border. Bioessays 2011, 33:693-700.
    • (2011) Bioessays , vol.33 , pp. 693-700
    • Fentress, S.J.1    Sibley, L.D.2
  • 113
    • 1542345726 scopus 로고    scopus 로고
    • Use of molecular and ultrastructural markers to evaluate stage conversion of Toxoplasma gondii in both the intermediate and definitive host
    • Ferguson D.J. Use of molecular and ultrastructural markers to evaluate stage conversion of Toxoplasma gondii in both the intermediate and definitive host. Int. J. Parasitol. 2004, 34:347-360.
    • (2004) Int. J. Parasitol. , vol.34 , pp. 347-360
    • Ferguson, D.J.1
  • 114
    • 0032804797 scopus 로고    scopus 로고
    • The expression and distribution of dense granule proteins in the enteric (coccidian) forms of Toxoplasma gondii in the small intestine of the cat
    • Ferguson D.J., Cesbron-Delauw M.F., Dubremetz J.F., Sibley L.D., Joiner K.A., Wright S. The expression and distribution of dense granule proteins in the enteric (coccidian) forms of Toxoplasma gondii in the small intestine of the cat. Exp. Parasitol. 1999, 91:203-211.
    • (1999) Exp. Parasitol. , vol.91 , pp. 203-211
    • Ferguson, D.J.1    Cesbron-Delauw, M.F.2    Dubremetz, J.F.3    Sibley, L.D.4    Joiner, K.A.5    Wright, S.6
  • 115
    • 0024344380 scopus 로고
    • Tissue cyst rupture in mice chronically infected with Toxoplasma gondii. An immunocytochemical and ultrastructural study
    • Ferguson D.J., Hutchison W.M., Pettersen E. Tissue cyst rupture in mice chronically infected with Toxoplasma gondii. An immunocytochemical and ultrastructural study. Parasitol. Res. 1989, 75:599-603.
    • (1989) Parasitol. Res. , vol.75 , pp. 599-603
    • Ferguson, D.J.1    Hutchison, W.M.2    Pettersen, E.3
  • 116
    • 0032879585 scopus 로고    scopus 로고
    • In vivo expression and distribution of dense granule protein 7 (GRA7) in the exoenteric (tachyzoite, bradyzoite) and enteric (coccidian) forms of Toxoplasma gondii
    • Ferguson D.J., Jacobs D., Saman E., Dubremetz J.F., Wright S.E. In vivo expression and distribution of dense granule protein 7 (GRA7) in the exoenteric (tachyzoite, bradyzoite) and enteric (coccidian) forms of Toxoplasma gondii. Parasitology 1999, 119:259-265.
    • (1999) Parasitology , vol.119 , pp. 259-265
    • Ferguson, D.J.1    Jacobs, D.2    Saman, E.3    Dubremetz, J.F.4    Wright, S.E.5
  • 117
    • 0030964241 scopus 로고    scopus 로고
    • Exploitation of mammalian host cell functions by bacterial pathogens
    • Finlay B.B., Cossart P. Exploitation of mammalian host cell functions by bacterial pathogens. Science 1997, 276:718-725.
    • (1997) Science , vol.276 , pp. 718-725
    • Finlay, B.B.1    Cossart, P.2
  • 118
    • 0032521215 scopus 로고    scopus 로고
    • GRA7, an excretory 29 kDa Toxoplasma gondii dense granule antigen released by infected host cells
    • Fischer H.G., Stachelhaus S., Sahm M., Meyer H.E., Reichmann G. GRA7, an excretory 29 kDa Toxoplasma gondii dense granule antigen released by infected host cells. Mol. Biochem. Parasitol. 1998, 91:251-262.
    • (1998) Mol. Biochem. Parasitol. , vol.91 , pp. 251-262
    • Fischer, H.G.1    Stachelhaus, S.2    Sahm, M.3    Meyer, H.E.4    Reichmann, G.5
  • 122
    • 0025732915 scopus 로고
    • Characterization of the lipid content of Toxoplasma gondii rhoptries
    • Foussard F., Leriche M.A., Dubremetz J.F. Characterization of the lipid content of Toxoplasma gondii rhoptries. Parasitology 1991, 102(Pt 3):367-370.
    • (1991) Parasitology , vol.102 , Issue.PT 3 , pp. 367-370
    • Foussard, F.1    Leriche, M.A.2    Dubremetz, J.F.3
  • 124
    • 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 T.S., Kappe S.H., Narum D.L., VanBuskirk K.M., Adams J.H. Erythrocyte-binding activity of Plasmodium yoelii apical membrane antigen-1 expressed on the surface of transfected COS-7 cells. Mol. Biochem. Parasitol. 2001, 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
  • 126
    • 76249095009 scopus 로고    scopus 로고
    • Members of a novel protein family containing microneme adhesive repeat domains act as sialic acid-binding lectins during host cell invasion by apicomplexan parasites
    • Friedrich N., Santos J.M., Liu Y., Palma A.S., Leon E., Saouros S., Kiso M., Blackman M.J., Matthews S., Feizi T., Soldati-Favre D. Members of a novel protein family containing microneme adhesive repeat domains act as sialic acid-binding lectins during host cell invasion by apicomplexan parasites. J. Biol. Chem. 2010, 285:2064-2076.
    • (2010) J. Biol. Chem. , vol.285 , pp. 2064-2076
    • Friedrich, N.1    Santos, J.M.2    Liu, Y.3    Palma, A.S.4    Leon, E.5    Saouros, S.6    Kiso, M.7    Blackman, M.J.8    Matthews, S.9    Feizi, T.10    Soldati-Favre, D.11
  • 127
    • 77950458573 scopus 로고    scopus 로고
    • DOC2B, C2 domains, and calcium: A tale of intricate interactions
    • Friedrich R., Yeheskel A., Ashery U. DOC2B, C2 domains, and calcium: A tale of intricate interactions. Mol. Neurobiol. 2010, 41:42-51.
    • (2010) Mol. Neurobiol. , vol.41 , pp. 42-51
    • Friedrich, R.1    Yeheskel, A.2    Ashery, U.3
  • 128
    • 84855923559 scopus 로고    scopus 로고
    • Proteomic analysis of fractionated Toxoplasma oocysts reveals clues to their environmental resistance
    • Fritz H.M., Bowyer P.W., Bogyo M., Conrad P.A., Boothroyd J.C. Proteomic analysis of fractionated Toxoplasma oocysts reveals clues to their environmental resistance. PLoS One 2012, 7:e29955.
    • (2012) PLoS One , vol.7
    • Fritz, H.M.1    Bowyer, P.W.2    Bogyo, M.3    Conrad, P.A.4    Boothroyd, J.C.5
  • 129
    • 84863124932 scopus 로고    scopus 로고
    • Transcriptomic analysis of Toxoplasma development reveals many novel functions and structures specific to sporozoites and oocysts
    • Fritz H.M., Buchholz K.R., Chen X., Durbin-Johnson B., Rocke D.M., Conrad P.A., Boothroyd J.C. Transcriptomic analysis of Toxoplasma development reveals many novel functions and structures specific to sporozoites and oocysts. PLoS One 2012, 7:e29998.
    • (2012) PLoS One , vol.7
    • Fritz, H.M.1    Buchholz, K.R.2    Chen, X.3    Durbin-Johnson, B.4    Rocke, D.M.5    Conrad, P.A.6    Boothroyd, J.C.7
  • 130
    • 2142646464 scopus 로고    scopus 로고
    • Erythrocyte invasion by Babesia bovis merozoites is inhibited by polyclonal antisera directed against peptides derived from a homologue of Plasmodium falciparum apical membrane antigen 1
    • Gaffar F.R., Yatsuda A.P., Franssen F.F., de Vries E. Erythrocyte invasion by Babesia bovis merozoites is inhibited by polyclonal antisera directed against peptides derived from a homologue of Plasmodium falciparum apical membrane antigen 1. Infect. Immun. 2004, 72:2947-2955.
    • (2004) Infect. Immun. , vol.72 , pp. 2947-2955
    • Gaffar, F.R.1    Yatsuda, A.P.2    Franssen, F.F.3    de Vries, E.4
  • 131
    • 0034882887 scopus 로고    scopus 로고
    • Transcriptional profile of Toxoplasma gondii-infected human fibroblasts as revealed by gene-array hybridization
    • Gail M., Gross U., Bohne W. Transcriptional profile of Toxoplasma gondii-infected human fibroblasts as revealed by gene-array hybridization. Mol. Genet. Genomics 2001, 265:905-912.
    • (2001) Mol. Genet. Genomics , vol.265 , pp. 905-912
    • Gail, M.1    Gross, U.2    Bohne, W.3
  • 132
    • 79958773527 scopus 로고    scopus 로고
    • Forward targeting of Toxoplasma gondii proproteins to the micronemes involves conserved aliphatic amino acids
    • Gaji R.Y., Flammer H.P., Carruthers V.B. Forward targeting of Toxoplasma gondii proproteins to the micronemes involves conserved aliphatic amino acids. Traffic 2011, 12:840-853.
    • (2011) Traffic , vol.12 , pp. 840-853
    • Gaji, R.Y.1    Flammer, H.P.2    Carruthers, V.B.3
  • 135
    • 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., Beckers C. Identification of the membrane receptor of a class XIV myosin in Toxoplasma gondii. J. Cell Biol. 2004, 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
  • 136
    • 77954761325 scopus 로고    scopus 로고
    • Post-translational membrane sorting of the Toxoplasma gondii GRA6 protein into the parasite-containing vacuole is driven by its N-terminal domain
    • Gendrin C., Bittame A., Mercier C., Cesbron-Delauw M.F. Post-translational membrane sorting of the Toxoplasma gondii GRA6 protein into the parasite-containing vacuole is driven by its N-terminal domain. Int. J. Parasitol. 2010, 40:1325-1334.
    • (2010) Int. J. Parasitol. , vol.40 , pp. 1325-1334
    • Gendrin, C.1    Bittame, A.2    Mercier, C.3    Cesbron-Delauw, M.F.4
  • 137
    • 51849164572 scopus 로고    scopus 로고
    • Toxoplasma gondii uses unusual sorting mechanisms to deliver transmembrane proteins into the host cell vacuole
    • Gendrin C., Mercier C., Braun L., Musset K., Dubremetz J.F., Cesbron-Delauw M.F. Toxoplasma gondii uses unusual sorting mechanisms to deliver transmembrane proteins into the host cell vacuole. Traffic 2008, 9:1665-1680.
    • (2008) Traffic , vol.9 , pp. 1665-1680
    • Gendrin, C.1    Mercier, C.2    Braun, L.3    Musset, K.4    Dubremetz, J.F.5    Cesbron-Delauw, M.F.6
  • 140
    • 84856005104 scopus 로고    scopus 로고
    • A novel PAN/apple domain-containing protein from Toxoplasma gondii: characterization and receptor identification
    • Gong H., Kobayashi K., Sugi T., Takemae H., Kurokawa H., Horimoto T., Akashi H., Kato K. A novel PAN/apple domain-containing protein from Toxoplasma gondii: characterization and receptor identification. PLoS One 2012, 7:e30169.
    • (2012) PLoS One , vol.7
    • Gong, H.1    Kobayashi, K.2    Sugi, T.3    Takemae, H.4    Kurokawa, H.5    Horimoto, T.6    Akashi, H.7    Kato, K.8
  • 143
    • 0026546679 scopus 로고
    • Heparin- and sulfatide-binding peptides from the type I repeats of human thrombospondin promote melanoma cell adhesion
    • Guo N.H., Krutzsch H.C., Negre E., Vogel T., Blake D.A., Roberts D.D. Heparin- and sulfatide-binding peptides from the type I repeats of human thrombospondin promote melanoma cell adhesion. Proc. Natl. Acad. Sci. U. S. A. 1992, 89:3040-3044.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 3040-3044
    • Guo, N.H.1    Krutzsch, H.C.2    Negre, E.3    Vogel, T.4    Blake, D.A.5    Roberts, D.D.6
  • 144
    • 0024448568 scopus 로고
    • Complete primary structure and functional characterization of the sixth component of the human complement system. Identification of the C5b-binding domain in complement C6
    • Haefliger J.A., Tschopp J., Vial N., Jenne D.E. Complete primary structure and functional characterization of the sixth component of the human complement system. Identification of the C5b-binding domain in complement C6. J. Biol. Chem. 1989, 264:18041-18051.
    • (1989) J. Biol. Chem. , vol.264 , pp. 18041-18051
    • Haefliger, J.A.1    Tschopp, J.2    Vial, N.3    Jenne, D.E.4
  • 146
    • 31144447066 scopus 로고    scopus 로고
    • Characterization, biosynthesis and fate of ROP7, a ROP2 related rhoptry protein of Toxoplasma gondii
    • Hajj H.E., Lebrun M., Fourmaux M.N., Vial H., Dubremetz J.F. Characterization, biosynthesis and fate of ROP7, a ROP2 related rhoptry protein of Toxoplasma gondii. Mol. Biochem. Parasitol 2005, 146:98-100.
    • (2005) Mol. Biochem. Parasitol , vol.146 , pp. 98-100
    • Hajj, H.E.1    Lebrun, M.2    Fourmaux, M.N.3    Vial, H.4    Dubremetz, J.F.5
  • 147
    • 0035875917 scopus 로고    scopus 로고
    • Toxoplasma evacuoles: a two-step process of secretion and fusion forms the parasitophorous vacuole
    • Hakansson S., Charron A.J., Sibley L.D. Toxoplasma evacuoles: a two-step process of secretion and fusion forms the parasitophorous vacuole. Embo. J. 2001, 20:3132-3144.
    • (2001) Embo. J. , vol.20 , pp. 3132-3144
    • Hakansson, S.1    Charron, A.J.2    Sibley, L.D.3
  • 148
    • 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., Sibley L.D. Time-lapse video microscopy of gliding motility in Toxoplasma gondii reveals a novel, biphasic mechanism of cell locomotion. Mol. Biol. Cell 1999, 10:3539-3547.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3539-3547
    • Hakansson, S.1    Morisaki, H.2    Heuser, J.3    Sibley, L.D.4
  • 150
    • 0027947231 scopus 로고
    • Overcoating of Toxoplasma Parasitophorous Vacuoles with Host Cell Vimentin Type Intermediate Filaments
    • Halonen S.K., Weidner E. Overcoating of Toxoplasma Parasitophorous Vacuoles with Host Cell Vimentin Type Intermediate Filaments. J. Eukaryot. Microbiol. 1994, 41:65-71.
    • (1994) J. Eukaryot. Microbiol. , vol.41 , pp. 65-71
    • Halonen, S.K.1    Weidner, E.2
  • 151
    • 1542375192 scopus 로고    scopus 로고
    • Multimerization of the Toxoplasma gondii MIC2 integrin-like A-domain is required for binding to heparin and human cells
    • Harper J.M., Hoff E.F., Carruthers V.B. Multimerization of the Toxoplasma gondii MIC2 integrin-like A-domain is required for binding to heparin and human cells. Mol. Biochem. Parasitol. 2004, 134:201-212.
    • (2004) Mol. Biochem. Parasitol. , vol.134 , pp. 201-212
    • Harper, J.M.1    Hoff, E.F.2    Carruthers, V.B.3
  • 152
    • 33749484972 scopus 로고    scopus 로고
    • A cleavable propeptide influences Toxoplasma infection by facilitating the trafficking and secretion of the TgMIC2-M2AP invasion complex
    • Harper J.M., Huynh M.H., Coppens I., Parussini F., Moreno S., Carruthers V.B. A cleavable propeptide influences Toxoplasma infection by facilitating the trafficking and secretion of the TgMIC2-M2AP invasion complex. Mol. Biol. Cell 2006, 17:4551-4563.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4551-4563
    • Harper, J.M.1    Huynh, M.H.2    Coppens, I.3    Parussini, F.4    Moreno, S.5    Carruthers, V.B.6
  • 153
    • 4143066921 scopus 로고    scopus 로고
    • The novel coccidian micronemal protein MIC11 undergoes proteolytic maturation by sequential cleavage to remove an internal propeptide
    • Harper J.M., Zhou X.W., Pszenny V., Kafsack B.F., Carruthers V.B. The novel coccidian micronemal protein MIC11 undergoes proteolytic maturation by sequential cleavage to remove an internal propeptide. Int. J. Parasitol. 2004, 34:1047-1058.
    • (2004) Int. J. Parasitol. , vol.34 , pp. 1047-1058
    • Harper, J.M.1    Zhou, X.W.2    Pszenny, V.3    Kafsack, B.F.4    Carruthers, V.B.5
  • 157
    • 0029884310 scopus 로고    scopus 로고
    • Mapping of the discontinuous kininogen binding site of prekallikrein. A distal binding segment is located in the heavy chain domain A4
    • Herwald H., Renne T., Meijers J.C., Chung D.W., Page J.D., Colman R.W., Muller-Esterl W. Mapping of the discontinuous kininogen binding site of prekallikrein. A distal binding segment is located in the heavy chain domain A4. J. Biol. Chem. 1996, 271:13061-13067.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13061-13067
    • Herwald, H.1    Renne, T.2    Meijers, J.C.3    Chung, D.W.4    Page, J.D.5    Colman, R.W.6    Muller-Esterl, W.7
  • 158
    • 0028363745 scopus 로고
    • Isolation, cDNA sequences, and biochemical characterization of the major cyclosporin-binding proteins of Toxoplasma gondii
    • High K.P., Joiner K.A., Handschumacher R.E. Isolation, cDNA sequences, and biochemical characterization of the major cyclosporin-binding proteins of Toxoplasma gondii. J. Biol. Chem. 1994, 269:9105-9112.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9105-9112
    • High, K.P.1    Joiner, K.A.2    Handschumacher, R.E.3
  • 159
    • 0032568840 scopus 로고    scopus 로고
    • A binding site for heparin in the apple 3 domain of factor XI
    • Ho D.H., Badellino K., Baglia F.A., Walsh P.N. A binding site for heparin in the apple 3 domain of factor XI. J. Biol. Chem. 1998, 273:16382-16390.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16382-16390
    • Ho, D.H.1    Badellino, K.2    Baglia, F.A.3    Walsh, P.N.4
  • 162
    • 0025269617 scopus 로고
    • Properdin binds to sulfatide [Gal(3-SO4)beta 1-1 Cer] and has a sequence homology with other proteins that bind sulfated glycoconjugates
    • Holt G.D., Pangburn M.K., Ginsburg V. Properdin binds to sulfatide [Gal(3-SO4)beta 1-1 Cer] and has a sequence homology with other proteins that bind sulfated glycoconjugates. J. Biol. Chem. 1990, 265:2852-2855.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2852-2855
    • Holt, G.D.1    Pangburn, M.K.2    Ginsburg, V.3
  • 163
    • 0034519998 scopus 로고    scopus 로고
    • Cytoplasmic tail motifs mediate endoplasmic reticulum localization and export of transmembrane reporters in the protozoan parasite Toxoplasma gondii
    • Hoppe H.C., Joiner K.A. Cytoplasmic tail motifs mediate endoplasmic reticulum localization and export of transmembrane reporters in the protozoan parasite Toxoplasma gondii. Cell Microbiol. 2000, 2:569-578.
    • (2000) Cell Microbiol. , vol.2 , pp. 569-578
    • Hoppe, H.C.1    Joiner, K.A.2
  • 164
    • 0033772272 scopus 로고    scopus 로고
    • Targeting to rhoptry organelles of Toxoplasma gondii involves evolutionarily conserved mechanisms
    • Hoppe H.C., Ngo H.M., Yang M., Joiner K.A. Targeting to rhoptry organelles of Toxoplasma gondii involves evolutionarily conserved mechanisms. Nat. Cell Biol. 2000, 2:449-456.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 449-456
    • Hoppe, H.C.1    Ngo, H.M.2    Yang, M.3    Joiner, K.A.4
  • 166
    • 0035903097 scopus 로고    scopus 로고
    • Proteolytic processing and primary structure of Plasmodium falciparum apical membrane antigen-1
    • Howell S.A., Withers-Martinez C., Kocken C.H., Thomas A.W., Blackman M.J. Proteolytic processing and primary structure of Plasmodium falciparum apical membrane antigen-1. J. Biol. Chem. 2001, 276:31311-31320.
    • (2001) J. Biol. Chem. , vol.276 , pp. 31311-31320
    • Howell, S.A.1    Withers-Martinez, C.2    Kocken, C.H.3    Thomas, A.W.4    Blackman, M.J.5
  • 168
    • 33748066307 scopus 로고    scopus 로고
    • Toxoplasma MIC2 is a major determinant of invasion and virulence
    • Huynh M.H., Carruthers V.B. Toxoplasma MIC2 is a major determinant of invasion and virulence. PLoS Pathog. 2006, 2:e84.
    • (2006) PLoS Pathog. , vol.2
    • Huynh, M.H.1    Carruthers, V.B.2
  • 169
    • 4043155559 scopus 로고    scopus 로고
    • Trans-genera reconstitution and complementation of an adhesion complex in Toxoplasma gondii
    • Huynh M.H., Opitz C., Kwok L.Y., Tomley F.M., Carruthers V.B., Soldati D. Trans-genera reconstitution and complementation of an adhesion complex in Toxoplasma gondii. Cell Microbiol. 2004, 6:771-782.
    • (2004) Cell Microbiol. , vol.6 , pp. 771-782
    • Huynh, M.H.1    Opitz, C.2    Kwok, L.Y.3    Tomley, F.M.4    Carruthers, V.B.5    Soldati, D.6
  • 170
    • 0038558167 scopus 로고    scopus 로고
    • Rapid invasion of host cells by Toxoplasma requires secretion of the MIC2-M2AP adhesive protein complex
    • Huynh M.H., Rabenau K.E., Harper J.M., Beatty W.L., Sibley L.D., Carruthers V.B. Rapid invasion of host cells by Toxoplasma requires secretion of the MIC2-M2AP adhesive protein complex. Embo. J. 2003, 22:2082-2090.
    • (2003) Embo. J. , vol.22 , pp. 2082-2090
    • Huynh, M.H.1    Rabenau, K.E.2    Harper, J.M.3    Beatty, W.L.4    Sibley, L.D.5    Carruthers, V.B.6
  • 171
    • 0017276791 scopus 로고
    • Effects of antiphagocytic agents on penetration of Eimeria magna sporozoites into cultured cells
    • Jensen J.B., Edgar S.A. Effects of antiphagocytic agents on penetration of Eimeria magna sporozoites into cultured cells. J. Parasitol. 1976, 62:203-206.
    • (1976) J. Parasitol. , vol.62 , pp. 203-206
    • Jensen, J.B.1    Edgar, S.A.2
  • 172
    • 23944482510 scopus 로고    scopus 로고
    • Fetuin-A, a hepatocyte-specific protein that binds Plasmodium berghei thrombospondin-related adhesive protein: a potential role in infectivity
    • Jethwaney D., Lepore T., Hassan S., Mello K., Rangarajan R., Jahnen-Dechent W., Wirth D., Sultan A.A. Fetuin-A, a hepatocyte-specific protein that binds Plasmodium berghei thrombospondin-related adhesive protein: a potential role in infectivity. Infect. Immun. 2005, 73:5883-5891.
    • (2005) Infect. Immun. , vol.73 , pp. 5883-5891
    • Jethwaney, D.1    Lepore, T.2    Hassan, S.3    Mello, K.4    Rangarajan, R.5    Jahnen-Dechent, W.6    Wirth, D.7    Sultan, A.A.8
  • 173
    • 0038637915 scopus 로고    scopus 로고
    • Aldolase forms a bridge between cell surface adhesins and the actin cytoskeleton in apicomplexan parasites
    • Jewett T.J., Sibley L.D. Aldolase forms a bridge between cell surface adhesins and the actin cytoskeleton in apicomplexan parasites. Mol. Cell 2003, 11:885-894.
    • (2003) Mol. Cell , vol.11 , pp. 885-894
    • Jewett, T.J.1    Sibley, L.D.2
  • 174
    • 1542364495 scopus 로고    scopus 로고
    • The Toxoplasma proteins MIC2 and M2AP form a hexameric complex necessary for intracellular survival
    • Jewett T.J., Sibley L.D. The Toxoplasma proteins MIC2 and M2AP form a hexameric complex necessary for intracellular survival. J. Biol. Chem. 2004, 279:9362-9369.
    • (2004) J. Biol. Chem. , vol.279 , pp. 9362-9369
    • Jewett, T.J.1    Sibley, L.D.2
  • 175
    • 0025905710 scopus 로고
    • Cloning of Toxoplasma gondii gene fragments encoding diagnostic antigens
    • Johnson A.M., Illana S. Cloning of Toxoplasma gondii gene fragments encoding diagnostic antigens. Gene 1991, 99:127-132.
    • (1991) Gene , vol.99 , pp. 127-132
    • Johnson, A.M.1    Illana, S.2
  • 176
    • 0015432947 scopus 로고
    • The interaction between Toxoplasma gondii and mammalian cells. II. The absence of lysosomal fusion with phagocytic vacuoles containing living parasites
    • Jones T.C., Hirsch J.G. The interaction between Toxoplasma gondii and mammalian cells. II. The absence of lysosomal fusion with phagocytic vacuoles containing living parasites. J. Exp. Med. 1972, 136:1173-1194.
    • (1972) J. Exp. Med. , vol.136 , pp. 1173-1194
    • Jones, T.C.1    Hirsch, J.G.2
  • 177
    • 58849087549 scopus 로고    scopus 로고
    • Rapid membrane disruption by a perforin-like protein facilitates parasite exit from host cells
    • Kafsack B.F., Pena J.D., Coppens I., Ravindran S., Boothroyd J.C., Carruthers V.B. Rapid membrane disruption by a perforin-like protein facilitates parasite exit from host cells. Science 2009, 323:530-533.
    • (2009) Science , vol.323 , pp. 530-533
    • Kafsack, B.F.1    Pena, J.D.2    Coppens, I.3    Ravindran, S.4    Boothroyd, J.C.5    Carruthers, V.B.6
  • 178
    • 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., Menard R. Conservation of a gliding motility and cell invasion machinery in Apicomplexan parasites. J. Cell Biol. 1999, 147:937-944.
    • (1999) J. Cell Biol. , vol.147 , pp. 937-944
    • Kappe, S.1    Bruderer, T.2    Gantt, S.3    Fujioka, H.4    Nussenzweig, V.5    Menard, R.6
  • 179
    • 13844289333 scopus 로고    scopus 로고
    • Identification and disruption of a rhoptry-localized homologue of sodium hydrogen exchangers in Toxoplasma gondii
    • Karasov A.O., Boothroyd J.C., Arrizabalaga G. Identification and disruption of a rhoptry-localized homologue of sodium hydrogen exchangers in Toxoplasma gondii. Int. J. Parasitol. 2005, 35:285-291.
    • (2005) Int. J. Parasitol. , vol.35 , pp. 285-291
    • Karasov, A.O.1    Boothroyd, J.C.2    Arrizabalaga, G.3
  • 180
    • 0032526698 scopus 로고    scopus 로고
    • The protozoan parasite Toxoplasma gondii targets proteins to dense granules and the vacuolar space using both conserved and unusual mechanisms
    • Karsten V., Qi H., Beckers C.J., Reddy A., Dubremetz J.F., Webster P., Joiner K.A. The protozoan parasite Toxoplasma gondii targets proteins to dense granules and the vacuolar space using both conserved and unusual mechanisms. J. Cell Biol. 1998, 141:1323-1333.
    • (1998) J. Cell Biol. , vol.141 , pp. 1323-1333
    • Karsten, V.1    Qi, H.2    Beckers, C.J.3    Reddy, A.4    Dubremetz, J.F.5    Webster, P.6    Joiner, K.A.7
  • 181
    • 17244375211 scopus 로고    scopus 로고
    • Domain III of Plasmodium falciparum apical membrane antigen 1 binds to the erythrocyte membrane protein Kx
    • Kato K., Mayer D.C., Singh S., Reid M., Miller L.H. Domain III of Plasmodium falciparum apical membrane antigen 1 binds to the erythrocyte membrane protein Kx. Proc. Natl. Acad. Sci. U. S. A. 2005, 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
  • 182
  • 184
    • 4644345259 scopus 로고    scopus 로고
    • The glideosome: a molecular machine powering motility and host cell invasion by Apicomplexa
    • Keeley A., Soldati D. The glideosome: a molecular machine powering motility and host cell invasion by Apicomplexa. Trends Cell Biol. 2004, 14:528-532.
    • (2004) Trends Cell Biol. , vol.14 , pp. 528-532
    • Keeley, A.1    Soldati, D.2
  • 186
    • 0035853753 scopus 로고    scopus 로고
    • Toxoplasma gondii attachment to host cells is regulated by a calmodulin-like domain protein kinase
    • Kieschnick H., Wakefield T., Narducci C.A., Beckers C. Toxoplasma gondii attachment to host cells is regulated by a calmodulin-like domain protein kinase. J. Biol. Chem. 2001, 276:12369-12377.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12369-12377
    • Kieschnick, H.1    Wakefield, T.2    Narducci, C.A.3    Beckers, C.4
  • 188
    • 0027730341 scopus 로고
    • Gene replacement in Toxoplasma gondii with chloramphenicol acetyltransferase as selectable marker
    • Kim K., Soldati D., Boothroyd J.C. Gene replacement in Toxoplasma gondii with chloramphenicol acetyltransferase as selectable marker. Science 1993, 262:911-914.
    • (1993) Science , vol.262 , pp. 911-914
    • Kim, K.1    Soldati, D.2    Boothroyd, J.C.3
  • 189
    • 0031809626 scopus 로고    scopus 로고
    • Expression, purification, and biochemical characterization of a recombinant lectin of Sarcocystis muris (Apicomplexa) cyst merozoites
    • Klein H., Loschner B., Zyto N., Portner M., Montag T. Expression, purification, and biochemical characterization of a recombinant lectin of Sarcocystis muris (Apicomplexa) cyst merozoites. Glycoconj. J. 1998, 15:147-153.
    • (1998) Glycoconj. J. , vol.15 , pp. 147-153
    • Klein, H.1    Loschner, B.2    Zyto, N.3    Portner, M.4    Montag, T.5
  • 190
    • 0024315131 scopus 로고
    • A 60-kDa Plasmodium falciparum protein at the moving junction formed between merozoite and erythrocyte during invasion
    • Klotz F.W., Hadley T.J., Aikawa M., Leech J., Howard R.J., Miller L.H. A 60-kDa Plasmodium falciparum protein at the moving junction formed between merozoite and erythrocyte during invasion. Mol. Biochem. Parasitol. 1989, 36:177-185.
    • (1989) Mol. Biochem. Parasitol. , vol.36 , pp. 177-185
    • Klotz, F.W.1    Hadley, T.J.2    Aikawa, M.3    Leech, J.4    Howard, R.J.5    Miller, L.H.6
  • 192
    • 0032783135 scopus 로고    scopus 로고
    • Differential membrane targeting of the secretory proteins GRA4 and GRA6 within the parasitophorous vacuole formed by Toxoplasma gondii
    • Labruyere E., Lingnau M., Mercier C., Sibley L.D. Differential membrane targeting of the secretory proteins GRA4 and GRA6 within the parasitophorous vacuole formed by Toxoplasma gondii. Mol. Biochem. Parasitol. 1999, 102:311-324.
    • (1999) Mol. Biochem. Parasitol. , vol.102 , pp. 311-324
    • Labruyere, E.1    Lingnau, M.2    Mercier, C.3    Sibley, L.D.4
  • 193
    • 78449308526 scopus 로고    scopus 로고
    • Toxoplasma gondii protease TgSUB1 is required for cell surface processing of micronemal adhesive complexes and efficient adhesion of tachyzoites
    • Lagal V., Binder E.M., Huynh M.H., Kafsack B.F., Harris P.K., Diez R., Chen D., Cole R.N., Carruthers V.B., Kim K. Toxoplasma gondii protease TgSUB1 is required for cell surface processing of micronemal adhesive complexes and efficient adhesion of tachyzoites. Cell Microbiol. 2010, 12:1792-1808.
    • (2010) Cell Microbiol. , vol.12 , pp. 1792-1808
    • Lagal, V.1    Binder, E.M.2    Huynh, M.H.3    Kafsack, B.F.4    Harris, P.K.5    Diez, R.6    Chen, D.7    Cole, R.N.8    Carruthers, V.B.9    Kim, K.10
  • 195
    • 79952446141 scopus 로고    scopus 로고
    • Toxoplasma gondii toxolysin 4 is an extensively processed putative metalloproteinase secreted from micronemes
    • Laliberte J., Carruthers V.B. Toxoplasma gondii toxolysin 4 is an extensively processed putative metalloproteinase secreted from micronemes. Mol. Biochem. Parasitol. 2011, 177:49-56.
    • (2011) Mol. Biochem. Parasitol. , vol.177 , pp. 49-56
    • Laliberte, J.1    Carruthers, V.B.2
  • 198
    • 70350417600 scopus 로고    scopus 로고
    • Toxoplasma gondii cathepsin L is the primary target of the invasion-inhibitory compound morpholinurea-leucyl-homophenyl-vinyl sulfone phenyl
    • Larson E.T., Parussini F., Huynh M.H., Giebel J.D., Kelley A.M., Zhang L., Bogyo M., Merritt E.A., Carruthers V.B. Toxoplasma gondii cathepsin L is the primary target of the invasion-inhibitory compound morpholinurea-leucyl-homophenyl-vinyl sulfone phenyl. J. Biol. Chem. 2009, 284:26839-26850.
    • (2009) J. Biol. Chem. , vol.284 , pp. 26839-26850
    • Larson, E.T.1    Parussini, F.2    Huynh, M.H.3    Giebel, J.D.4    Kelley, A.M.5    Zhang, L.6    Bogyo, M.7    Merritt, E.A.8    Carruthers, V.B.9
  • 199
    • 0022495145 scopus 로고
    • The structural and functional properties of thrombospondin
    • Lawler J. The structural and functional properties of thrombospondin. Blood 1986, 67:1197-1209.
    • (1986) Blood , vol.67 , pp. 1197-1209
    • Lawler, J.1
  • 201
    • 0032947846 scopus 로고    scopus 로고
    • Transmembrane insertion of the Toxoplasma gondii GRA5 protein occurs after soluble secretion into the host cell
    • Lecordier L., Mercier C., Sibley L.D., Cesbron-Delauw M.F. Transmembrane insertion of the Toxoplasma gondii GRA5 protein occurs after soluble secretion into the host cell. Mol. Biol. Cell 1999, 10:1277-1287.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1277-1287
    • Lecordier, L.1    Mercier, C.2    Sibley, L.D.3    Cesbron-Delauw, M.F.4
  • 204
    • 0028986196 scopus 로고
    • Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18)
    • Lee J.O., Rieu P., Arnaout M.A., Liddington R. Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18). Cell 1995, 80:631-638.
    • (1995) Cell , vol.80 , pp. 631-638
    • Lee, J.O.1    Rieu, P.2    Arnaout, M.A.3    Liddington, R.4
  • 205
    • 0025004703 scopus 로고
    • Exocytosis of Toxoplasma gondii dense granules into the parasitophorous vacuole after host cell invasion
    • Leriche M.A., Dubremetz J.F. Exocytosis of Toxoplasma gondii dense granules into the parasitophorous vacuole after host cell invasion. Parasitol. Res. 1990, 76:559-562.
    • (1990) Parasitol. Res. , vol.76 , pp. 559-562
    • Leriche, M.A.1    Dubremetz, J.F.2
  • 206
    • 0026033705 scopus 로고
    • Characterization of the protein contents of rhoptries and dense granules of Toxoplasma gondii tachyzoites by subcellular fractionation and monoclonal antibodies
    • Leriche M.A., Dubremetz J.F. Characterization of the protein contents of rhoptries and dense granules of Toxoplasma gondii tachyzoites by subcellular fractionation and monoclonal antibodies. Mol. Biochem. Parasitol. 1991, 45:249-259.
    • (1991) Mol. Biochem. Parasitol. , vol.45 , pp. 249-259
    • Leriche, M.A.1    Dubremetz, J.F.2
  • 207
    • 0034017106 scopus 로고    scopus 로고
    • Toxoplasma gondii: conserved protein machinery in an unusual secretory pathway?
    • Liendo A., Joiner K.A. Toxoplasma gondii: conserved protein machinery in an unusual secretory pathway?. Microbes Infect. 2000, 2:137-144.
    • (2000) Microbes Infect. , vol.2 , pp. 137-144
    • Liendo, A.1    Joiner, K.A.2
  • 208
    • 77649207443 scopus 로고    scopus 로고
    • A highly sensitive FRET-based approach reveals secretion of the actin-binding protein toxofilin during Toxoplasma gondii infection
    • Lodoen M.B., Gerke C., Boothroyd J.C. A highly sensitive FRET-based approach reveals secretion of the actin-binding protein toxofilin during Toxoplasma gondii infection. Cell Microbiol. 2010, 12:55-66.
    • (2010) Cell Microbiol. , vol.12 , pp. 55-66
    • Lodoen, M.B.1    Gerke, C.2    Boothroyd, J.C.3
  • 211
    • 77952723730 scopus 로고    scopus 로고
    • Calcium-dependent protein kinase 1 is an essential regulator of exocytosis in Toxoplasma
    • Lourido S., Shuman J., Zhang C., Shokat K.M., Hui R., Sibley L.D. Calcium-dependent protein kinase 1 is an essential regulator of exocytosis in Toxoplasma. Nature 2010, 465:359-362.
    • (2010) Nature , vol.465 , pp. 359-362
    • Lourido, S.1    Shuman, J.2    Zhang, C.3    Shokat, K.M.4    Hui, R.5    Sibley, L.D.6
  • 212
    • 0037135597 scopus 로고    scopus 로고
    • Toxoplasma gondii microneme secretion involves intracellular Ca(2+) release from inositol 1,4,5-triphosphate (IP(3))/ryanodine-sensitive stores
    • Lovett J.L., Marchesini N., Moreno S.N., Sibley L.D. Toxoplasma gondii microneme secretion involves intracellular Ca(2+) release from inositol 1,4,5-triphosphate (IP(3))/ryanodine-sensitive stores. J. Biol. Chem. 2002, 277:25870-25876.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25870-25876
    • Lovett, J.L.1    Marchesini, N.2    Moreno, S.N.3    Sibley, L.D.4
  • 213
    • 0041402826 scopus 로고    scopus 로고
    • Intracellular calcium stores in Toxoplasma gondii govern invasion of host cells
    • Lovett J.L., Sibley L.D. Intracellular calcium stores in Toxoplasma gondii govern invasion of host cells. J. Cell Sci. 2003, 116:3009-3016.
    • (2003) J. Cell Sci. , vol.116 , pp. 3009-3016
    • Lovett, J.L.1    Sibley, L.D.2
  • 214
    • 22544434016 scopus 로고    scopus 로고
    • Intravacuolar network may act as a mechanical support for Toxoplasma gondii inside the parasitophorous vacuole
    • Magno R.C., Lemgruber L., Vommaro R.C., De Souza W., Attias M. Intravacuolar network may act as a mechanical support for Toxoplasma gondii inside the parasitophorous vacuole. Microsc. Res. Tech. 2005, 67:45-52.
    • (2005) Microsc. Res. Tech. , vol.67 , pp. 45-52
    • Magno, R.C.1    Lemgruber, L.2    Vommaro, R.C.3    De Souza, W.4    Attias, M.5
  • 215
    • 23944475182 scopus 로고    scopus 로고
    • Identification, cloning, expression, and characterization of the gene for Plasmodium knowlesi surface protein containing an altered thrombospondin repeat domain
    • Mahajan B., Jani D., Chattopadhyay R., Nagarkatti R., Zheng H., Majam V., Weiss W., Kumar S., Rathore D. Identification, cloning, expression, and characterization of the gene for Plasmodium knowlesi surface protein containing an altered thrombospondin repeat domain. Infect. Immun. 2005, 73:5402-5409.
    • (2005) Infect. Immun. , vol.73 , pp. 5402-5409
    • Mahajan, B.1    Jani, D.2    Chattopadhyay, R.3    Nagarkatti, R.4    Zheng, H.5    Majam, V.6    Weiss, W.7    Kumar, S.8    Rathore, D.9
  • 217
  • 218
    • 0042328130 scopus 로고    scopus 로고
    • Role of the parafusin orthologue, PRP1, in microneme exocytosis and cell invasion in Toxoplasma gondii
    • Matthiesen S.H., Shenoy S.M., Kim K., Singer R.H., Satir B.H. Role of the parafusin orthologue, PRP1, in microneme exocytosis and cell invasion in Toxoplasma gondii. Cell Microbiol. 2003, 5:613-624.
    • (2003) Cell Microbiol. , vol.5 , pp. 613-624
    • Matthiesen, S.H.1    Shenoy, S.M.2    Kim, K.3    Singer, R.H.4    Satir, B.H.5
  • 219
    • 0037007205 scopus 로고    scopus 로고
    • Plasmodium sporozoite invasion into insect and mammalian cells is directed by the same dual binding system
    • Matuschewski K., Nunes A.C., Nussenzweig V., Menard R. Plasmodium sporozoite invasion into insect and mammalian cells is directed by the same dual binding system. Embo. J. 2002, 21:1597-1606.
    • (2002) Embo. J. , vol.21 , pp. 1597-1606
    • Matuschewski, K.1    Nunes, A.C.2    Nussenzweig, V.3    Menard, R.4
  • 220
    • 0032966841 scopus 로고    scopus 로고
    • Identification of heparin as a ligand for the A-domain of Plasmodium falciparum thrombospondin-related adhesion protein
    • McCormick C.J., Tuckwell D.S., Crisanti A., Humphries M.J., Hollingdale M.R. Identification of heparin as a ligand for the A-domain of Plasmodium falciparum thrombospondin-related adhesion protein. Mol. Biochem. Parasitol. 1999, 100:111-124.
    • (1999) Mol. Biochem. Parasitol. , vol.100 , pp. 111-124
    • McCormick, C.J.1    Tuckwell, D.S.2    Crisanti, A.3    Humphries, M.J.4    Hollingdale, M.R.5
  • 221
    • 0036473089 scopus 로고    scopus 로고
    • A family of transmembrane microneme proteins of Toxoplasma gondii contain EGF-like domains and function as escorters
    • Meissner M., Reiss M., Viebig N., Carruthers V.B., Toursel C., Tomavo S., Ajioka J.W., Soldati D. A family of transmembrane microneme proteins of Toxoplasma gondii contain EGF-like domains and function as escorters. J. Cell Sci. 2002, 115:563-574.
    • (2002) J. Cell Sci. , vol.115 , pp. 563-574
    • Meissner, M.1    Reiss, M.2    Viebig, N.3    Carruthers, V.B.4    Toursel, C.5    Tomavo, S.6    Ajioka, J.W.7    Soldati, D.8
  • 222
    • 0035005405 scopus 로고    scopus 로고
    • Behaviour of microtubules in cells infected with Toxoplasma gondii
    • Melo E.J., Carvalho T.M., De Souza W. Behaviour of microtubules in cells infected with Toxoplasma gondii. Biocell 2001, 25:53-59.
    • (2001) Biocell , vol.25 , pp. 53-59
    • Melo, E.J.1    Carvalho, T.M.2    De Souza, W.3
  • 223
    • 0035137385 scopus 로고    scopus 로고
    • Gliding motility and cell invasion by Apicomplexa: insights from the Plasmodium sporozoite
    • Menard R. Gliding motility and cell invasion by Apicomplexa: insights from the Plasmodium sporozoite. Cell Microbiol. 2001, 3:63-73.
    • (2001) Cell Microbiol. , vol.3 , pp. 63-73
    • Menard, R.1
  • 224
    • 21344467746 scopus 로고    scopus 로고
    • Dense granules: Are they key organelles to help understand the parasitophorous vacuole of all apicomplexa parasites?
    • Mercier C., Adjogble K.D., Daubener W., Delauw M.F. Dense granules: Are they key organelles to help understand the parasitophorous vacuole of all apicomplexa parasites?. Int. J. Parasitol. 2005, 35:829-849.
    • (2005) Int. J. Parasitol. , vol.35 , pp. 829-849
    • Mercier, C.1    Adjogble, K.D.2    Daubener, W.3    Delauw, M.F.4
  • 225
    • 0031696061 scopus 로고    scopus 로고
    • The amphipathic alpha helices of the Toxoplasma protein GRA2 mediate post-secretory membrane association
    • Mercier C., Cesbron-Delauw M.F., Sibley L.D. The amphipathic alpha helices of the Toxoplasma protein GRA2 mediate post-secretory membrane association. J. Cell Sci. 1998, 111:2171-2180.
    • (1998) J. Cell Sci. , vol.111 , pp. 2171-2180
    • Mercier, C.1    Cesbron-Delauw, M.F.2    Sibley, L.D.3
  • 227
    • 0031662948 scopus 로고    scopus 로고
    • Targeted disruption of the GRA2 locus in Toxoplasma gondii decreases acute virulence in mice
    • Mercier C., Howe D.K., Mordue D., Lingnau M., Sibley L.D. Targeted disruption of the GRA2 locus in Toxoplasma gondii decreases acute virulence in mice. Infect. Immun. 1998, 66:4176-4182.
    • (1998) Infect. Immun. , vol.66 , pp. 4176-4182
    • Mercier, C.1    Howe, D.K.2    Mordue, D.3    Lingnau, M.4    Sibley, L.D.5
  • 229
    • 58549097441 scopus 로고    scopus 로고
    • GRA12, a Toxoplasma dense granule protein associated with the intravacuolar 1 membranous 2 nanotubular network
    • Michelin A., Bittame A., Bordat Y., Travier L., Mercier C., Dubremetz J.F., Lebrun M. GRA12, a Toxoplasma dense granule protein associated with the intravacuolar 1 membranous 2 nanotubular network. Int. J. Parasitol. 2008, 39:299-306.
    • (2008) Int. J. Parasitol. , vol.39 , pp. 299-306
    • Michelin, A.1    Bittame, A.2    Bordat, Y.3    Travier, L.4    Mercier, C.5    Dubremetz, J.F.6    Lebrun, M.7
  • 230
    • 0018777194 scopus 로고
    • Interaction between cytochalasin B-treated malarial parasites and erythrocytes. Attachment and junction formation
    • Miller L.H., Aikawa M., Johnson J.G., Shiroishi T. Interaction between cytochalasin B-treated malarial parasites and erythrocytes. Attachment and junction formation. J. Exp. Med. 1979, 149:172-184.
    • (1979) J. Exp. Med. , vol.149 , pp. 172-184
    • Miller, L.H.1    Aikawa, M.2    Johnson, J.G.3    Shiroishi, T.4
  • 231
    • 0035976961 scopus 로고    scopus 로고
    • A conserved subtilisin-like protein TgSUB1 in microneme organelles of Toxoplasma gondii
    • Miller S.A., Binder E.M., Blackman M.J., Carruthers V.B., Kim K. A conserved subtilisin-like protein TgSUB1 in microneme organelles of Toxoplasma gondii. J. Biol. Chem. 2001, 276:45341-45348.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45341-45348
    • Miller, S.A.1    Binder, E.M.2    Blackman, M.J.3    Carruthers, V.B.4    Kim, K.5
  • 232
  • 234
    • 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 G.E. Conditional expression of Toxoplasma gondii apical membrane antigen-1 (TgAMA1) demonstrates that TgAMA1 plays a critical role in host cell invasion. Mol. Biol. Cell 2005, 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
  • 235
    • 0346251040 scopus 로고    scopus 로고
    • Apical membrane antigen 1, a major malaria vaccine candidate, mediates the close attachment of invasive merozoites to host red blood cells
    • Mitchell G.H., Thomas A.W., Margos G., Dluzewski A.R., Bannister L.H. Apical membrane antigen 1, a major malaria vaccine candidate, mediates the close attachment of invasive merozoites to host red blood cells. Infect. Immun. 2004, 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
  • 236
    • 0030095229 scopus 로고    scopus 로고
    • Ca(2+)-dependence of conoid extrusion in Toxoplasma gondii tachyzoites
    • Mondragon R., Frixione E. Ca(2+)-dependence of conoid extrusion in Toxoplasma gondii tachyzoites. J. Eukaryot Microbiol. 1996, 43:120-127.
    • (1996) J. Eukaryot Microbiol. , vol.43 , pp. 120-127
    • Mondragon, R.1    Frixione, E.2
  • 237
    • 0032528078 scopus 로고    scopus 로고
    • Host cell surface sialic acid residues are involved on the process of penetration of Toxoplasma gondii into mammalian cells
    • Monteiro V.G., Soares C.P., de Souza W. Host cell surface sialic acid residues are involved on the process of penetration of Toxoplasma gondii into mammalian cells. FEMS Microbiol. Lett. 1998, 164:323-327.
    • (1998) FEMS Microbiol. Lett. , vol.164 , pp. 323-327
    • Monteiro, V.G.1    Soares, C.P.2    de Souza, W.3
  • 238
    • 0033397899 scopus 로고    scopus 로고
    • Invasion by Toxoplasma gondii establishes a moving junction that selectively excludes host cell plasma membrane proteins on the basis of their membrane anchoring
    • Mordue D.G., Desai N., Dustin M., Sibley L.D. Invasion by Toxoplasma gondii establishes a moving junction that selectively excludes host cell plasma membrane proteins on the basis of their membrane anchoring. J. Exp. Med. 1999, 190:1783-1792.
    • (1999) J. Exp. Med. , vol.190 , pp. 1783-1792
    • Mordue, D.G.1    Desai, N.2    Dustin, M.3    Sibley, L.D.4
  • 239
    • 0345151828 scopus 로고    scopus 로고
    • Toxoplasma gondii resides in a vacuole that avoids fusion with host cell endocytic and exocytic vesicular trafficking pathways
    • Mordue D.G., Hakansson S., Niesman I., Sibley L.D. Toxoplasma gondii resides in a vacuole that avoids fusion with host cell endocytic and exocytic vesicular trafficking pathways. Exp. Parasitol. 1999, 92:87-99.
    • (1999) Exp. Parasitol. , vol.92 , pp. 87-99
    • Mordue, D.G.1    Hakansson, S.2    Niesman, I.3    Sibley, L.D.4
  • 240
    • 0031278412 scopus 로고    scopus 로고
    • Intracellular fate of vacuoles containing Toxoplasma gondii is determined at the time of formation and depends on the mechanism of entry
    • Mordue D.G., Sibley L.D. Intracellular fate of vacuoles containing Toxoplasma gondii is determined at the time of formation and depends on the mechanism of entry. J. Immunol. 1997, 159:4452-4459.
    • (1997) J. Immunol. , vol.159 , pp. 4452-4459
    • Mordue, D.G.1    Sibley, L.D.2
  • 241
    • 0042195182 scopus 로고    scopus 로고
    • Calcium regulation in protozoan parasites
    • Moreno S.N., Docampo R. Calcium regulation in protozoan parasites. Curr. Opin. Microbiol. 2003, 6:359-364.
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 359-364
    • Moreno, S.N.1    Docampo, R.2
  • 242
    • 0029016818 scopus 로고
    • Invasion of Toxoplasma gondii occurs by active penetration of the host cell
    • Morisaki J.H., Heuser J.E., Sibley L.D. Invasion of Toxoplasma gondii occurs by active penetration of the host cell. J. Cell Sci. 1995, 108(Pt 6):2457-2464.
    • (1995) J. Cell Sci. , vol.108 , Issue.PT 6 , pp. 2457-2464
    • Morisaki, J.H.1    Heuser, J.E.2    Sibley, L.D.3
  • 243
    • 0037466363 scopus 로고    scopus 로고
    • Identification and partial characterization of a second Kazal inhibitor in Toxoplasma gondii
    • Morris M.T., Carruthers V.B. Identification and partial characterization of a second Kazal inhibitor in Toxoplasma gondii. Mol. Biochem. Parasitol. 2003, 128:119-122.
    • (2003) Mol. Biochem. Parasitol. , vol.128 , pp. 119-122
    • Morris, M.T.1    Carruthers, V.B.2
  • 244
    • 0346668362 scopus 로고    scopus 로고
    • Functional analysis of Toxoplasma gondii protease inhibitor 1
    • Morris M.T., Coppin A., Tomavo S., Carruthers V.B. Functional analysis of Toxoplasma gondii protease inhibitor 1. J. Biol. Chem. 2002, 277:45259-45266.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45259-45266
    • Morris, M.T.1    Coppin, A.2    Tomavo, S.3    Carruthers, V.B.4
  • 245
    • 0035798694 scopus 로고    scopus 로고
    • The loss of cytoplasmic potassium upon host cell breakdown triggers egress of Toxoplasma gondii
    • Moudy R., Manning T.J., Beckers C.J. The loss of cytoplasmic potassium upon host cell breakdown triggers egress of Toxoplasma gondii. J. Biol. Chem. 2001, 276:41492-41501.
    • (2001) J. Biol. Chem. , vol.276 , pp. 41492-41501
    • Moudy, R.1    Manning, T.J.2    Beckers, C.J.3
  • 246
    • 0027326632 scopus 로고
    • Thrombospondin related anonymous protein (TRAP) of Plasmodium falciparum binds specifically to sulfated glycoconjugates and to HepG2 hepatoma cells suggesting a role for this molecule in sporozoite invasion of hepatocytes
    • Muller H.M., Reckmann I., Hollingdale M.R., Bujard H., Robson K.J., Crisanti A. Thrombospondin related anonymous protein (TRAP) of Plasmodium falciparum binds specifically to sulfated glycoconjugates and to HepG2 hepatoma cells suggesting a role for this molecule in sporozoite invasion of hepatocytes. Embo. J. 1993, 12:2881-2889.
    • (1993) Embo. J. , vol.12 , pp. 2881-2889
    • Muller, H.M.1    Reckmann, I.2    Hollingdale, M.R.3    Bujard, H.4    Robson, K.J.5    Crisanti, A.6
  • 247
    • 38049165494 scopus 로고    scopus 로고
    • Abscisic acid controls calcium-dependent egress and development in Toxoplasma gondii
    • Nagamune K., Hicks L.M., Fux B., Brossier F., Chini E.N., Sibley L.D. Abscisic acid controls calcium-dependent egress and development in Toxoplasma gondii. Nature 2008, 451:207-210.
    • (2008) Nature , vol.451 , pp. 207-210
    • Nagamune, K.1    Hicks, L.M.2    Fux, B.3    Brossier, F.4    Chini, E.N.5    Sibley, L.D.6
  • 248
    • 0010370623 scopus 로고    scopus 로고
    • Upstream elements required for expression of nucleoside triphosphate hydrolase genes of Toxoplasma gondii
    • Nakaar V., Bermudes D., Peck K.R., Joiner K.A. Upstream elements required for expression of nucleoside triphosphate hydrolase genes of Toxoplasma gondii. Mol. Biochem. Parasitol. 1998, 92:229-239.
    • (1998) Mol. Biochem. Parasitol. , vol.92 , pp. 229-239
    • Nakaar, V.1    Bermudes, D.2    Peck, K.R.3    Joiner, K.A.4
  • 249
    • 0037672558 scopus 로고    scopus 로고
    • Pleiotropic effect due to targeted depletion of secretory rhoptry protein ROP2 in Toxoplasma gondii
    • Nakaar V., Ngo H.M., Aaronson E.P., Coppens I., Stedman T.T., Joiner K.A. Pleiotropic effect due to targeted depletion of secretory rhoptry protein ROP2 in Toxoplasma gondii. J. Cell Sci. 2003, 116:2311-2320.
    • (2003) J. Cell Sci. , vol.116 , pp. 2311-2320
    • Nakaar, V.1    Ngo, H.M.2    Aaronson, E.P.3    Coppens, I.4    Stedman, T.T.5    Joiner, K.A.6
  • 250
    • 0033582535 scopus 로고    scopus 로고
    • Targeted reduction of nucleoside triphosphate hydrolase by antisense RNA inhibits Toxoplasma gondii proliferation
    • Nakaar V., Samuel B.U., Ngo E.O., Joiner K.A. Targeted reduction of nucleoside triphosphate hydrolase by antisense RNA inhibits Toxoplasma gondii proliferation. J. Biol. Chem. 1999, 274:5083-5087.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5083-5087
    • Nakaar, V.1    Samuel, B.U.2    Ngo, E.O.3    Joiner, K.A.4
  • 251
    • 0033861577 scopus 로고    scopus 로고
    • Toxoplasma gondii: are host cell adenosine nucleotides a direct source for purine salvage?
    • Ngo H.M., Ngo E.O., Bzik D.J., Joiner K.A. Toxoplasma gondii: are host cell adenosine nucleotides a direct source for purine salvage?. Exp. Parasitol. 2000, 95:148-153.
    • (2000) Exp. Parasitol. , vol.95 , pp. 148-153
    • Ngo, H.M.1    Ngo, E.O.2    Bzik, D.J.3    Joiner, K.A.4
  • 252
    • 3042557931 scopus 로고    scopus 로고
    • Are rhoptries in Apicomplexan parasites secretory granules or secretory lysosomal granules?
    • Ngo H.M., Yang M., Joiner K.A. Are rhoptries in Apicomplexan parasites secretory granules or secretory lysosomal granules?. Mol. Microbiol. 2004, 52:1531-1541.
    • (2004) Mol. Microbiol. , vol.52 , pp. 1531-1541
    • Ngo, H.M.1    Yang, M.2    Joiner, K.A.3
  • 253
    • 0038237513 scopus 로고    scopus 로고
    • AP-1 in Toxoplasma gondii mediates biogenesis of the rhoptry secretory organelle from a post-Golgi compartment
    • Ngo H.M., Yang M., Paprotka K., Pypaert M., Hoppe H., Joiner K.A. AP-1 in Toxoplasma gondii mediates biogenesis of the rhoptry secretory organelle from a post-Golgi compartment. J. Biol. Chem. 2003, 278:5343-5352.
    • (2003) J. Biol. Chem. , vol.278 , pp. 5343-5352
    • Ngo, H.M.1    Yang, M.2    Paprotka, K.3    Pypaert, M.4    Hoppe, H.5    Joiner, K.A.6
  • 254
    • 0022081561 scopus 로고
    • Interactions between Toxoplasma and host phagocytes
    • Nichols B.A. Interactions between Toxoplasma and host phagocytes. Int. Ophthalmol. Clin. 1985, 25:71-80.
    • (1985) Int. Ophthalmol. Clin. , vol.25 , pp. 71-80
    • Nichols, B.A.1
  • 255
    • 0020957006 scopus 로고
    • Secretion from the rhoptries of Toxoplasma gondii during host cell invasion
    • Nichols B.A., Chiappino M.L., O'Connor G.R. Secretion from the rhoptries of Toxoplasma gondii during host cell invasion. J. Ultrastruct. Res. 1983, 83:85-98.
    • (1983) J. Ultrastruct. Res. , vol.83 , pp. 85-98
    • Nichols, B.A.1    Chiappino, M.L.2    O'Connor, G.R.3
  • 257
    • 46649114361 scopus 로고    scopus 로고
    • Organellar dynamics during the cell cycle of Toxoplasma gondii
    • Nishi M., Hu K., Murray J.M., Roos D.S. Organellar dynamics during the cell cycle of Toxoplasma gondii. J. Cell Sci. 2008, 121:1559-1568.
    • (2008) J. Cell Sci. , vol.121 , pp. 1559-1568
    • Nishi, M.1    Hu, K.2    Murray, J.M.3    Roos, D.S.4
  • 259
    • 77956538745 scopus 로고    scopus 로고
    • Toxoplasma rhoptry protein 16 (ROP16) subverts host function by direct tyrosine phosphorylation of STAT6
    • Ong Y.C., Reese M.L., Boothroyd J.C. Toxoplasma rhoptry protein 16 (ROP16) subverts host function by direct tyrosine phosphorylation of STAT6. J. Biol. Chem. 2010, 285:28731-28740.
    • (2010) J. Biol. Chem. , vol.285 , pp. 28731-28740
    • Ong, Y.C.1    Reese, M.L.2    Boothroyd, J.C.3
  • 260
    • 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., Ruppert T., Crisanti A., Soldati D. Intramembrane cleavage of microneme proteins at the surface of the apicomplexan parasite Toxoplasma gondii. Embo. J. 2002, 21:1577-1585.
    • (2002) Embo. J. , vol.21 , pp. 1577-1585
    • Opitz, C.1    Di Cristina, M.2    Reiss, M.3    Ruppert, T.4    Crisanti, A.5    Soldati, D.6
  • 261
    • 0036372942 scopus 로고    scopus 로고
    • 'The glideosome': a dynamic complex powering gliding motion and host cell invasion by Toxoplasma gondii
    • Opitz C., Soldati D. 'The glideosome': a dynamic complex powering gliding motion and host cell invasion by Toxoplasma gondii. Mol. Microbiol. 2002, 45:597-604.
    • (2002) Mol. Microbiol. , vol.45 , pp. 597-604
    • Opitz, C.1    Soldati, D.2
  • 262
    • 0026544061 scopus 로고
    • A Toxoplasma gondii rhoptry protein associated with host cell penetration has unusual charge asymmetry
    • Ossorio P.N., Schwartzman J.D., Boothroyd J.C. A Toxoplasma gondii rhoptry protein associated with host cell penetration has unusual charge asymmetry. Mol. Biochem. Parasitol. 1992, 50:1-15.
    • (1992) Mol. Biochem. Parasitol. , vol.50 , pp. 1-15
    • Ossorio, P.N.1    Schwartzman, J.D.2    Boothroyd, J.C.3
  • 263
    • 77953512608 scopus 로고    scopus 로고
    • Cathepsin L occupies a vacuolar compartment and is a protein maturase within the endo/exocytic system of Toxoplasma gondii
    • Parussini F., Coppens I., Shah P.P., Diamond S.L., Carruthers V.B. Cathepsin L occupies a vacuolar compartment and is a protein maturase within the endo/exocytic system of Toxoplasma gondii. Mol. Microbiol. 2010, 76:1340-1357.
    • (2010) Mol. Microbiol. , vol.76 , pp. 1340-1357
    • Parussini, F.1    Coppens, I.2    Shah, P.P.3    Diamond, S.L.4    Carruthers, V.B.5
  • 264
    • 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 S.M., Mital J., Urban S., Ward G.E. Intramembrane proteolysis of Toxoplasma apical membrane antigen 1 facilitates host cell invasion but is dispensable for replication. Proc. Natl. Acad. Sci. U. S. A. 2012, 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    Ward, G.E.6
  • 266
    • 23944468221 scopus 로고    scopus 로고
    • Calcium binding activity of the epidermal growth factor-like domains of the apicomplexan microneme protein EtMIC4
    • Periz J., Gill A.C., Knott V., Handford P.A., Tomley F.M. Calcium binding activity of the epidermal growth factor-like domains of the apicomplexan microneme protein EtMIC4. Mol. Biochem. Parasitol. 2005, 143:192-199.
    • (2005) Mol. Biochem. Parasitol. , vol.143 , pp. 192-199
    • Periz, J.1    Gill, A.C.2    Knott, V.3    Handford, P.A.4    Tomley, F.M.5
  • 267
    • 80855159996 scopus 로고    scopus 로고
    • Association of host mitochondria with the parasitophorous vacuole during Toxoplasma infection is not dependent on rhoptry proteins ROP2/8
    • Pernas L., Boothroyd J.C. Association of host mitochondria with the parasitophorous vacuole during Toxoplasma infection is not dependent on rhoptry proteins ROP2/8. Int. J. Parasitol. 2010, 40:1367-1371.
    • (2010) Int. J. Parasitol. , vol.40 , pp. 1367-1371
    • Pernas, L.1    Boothroyd, J.C.2
  • 269
    • 53649111607 scopus 로고    scopus 로고
    • Toxoplasma gondii rhoptry discharge correlates with activation of the early growth response 2 host cell transcription factor
    • Phelps E.D., Sweeney K.R., Blader I.J. Toxoplasma gondii rhoptry discharge correlates with activation of the early growth response 2 host cell transcription factor. Infect. Immun. 2008, 76:4703-4712.
    • (2008) Infect. Immun. , vol.76 , pp. 4703-4712
    • Phelps, E.D.1    Sweeney, K.R.2    Blader, I.J.3
  • 271
    • 0017649751 scopus 로고
    • Freeze fracture study of Toxoplasma and Sarcocystis infective stages (author's transl)
    • Porchet E., Torpier G. Freeze fracture study of Toxoplasma and Sarcocystis infective stages (author's transl). Z. Parasitenkd 1977, 54:101-124.
    • (1977) Z. Parasitenkd , vol.54 , pp. 101-124
    • Porchet, E.1    Torpier, G.2
  • 272
    • 0033980626 scopus 로고    scopus 로고
    • Toxofilin, a novel actin-binding protein from Toxoplasma gondii, sequesters actin monomers and caps actin filaments
    • Poupel O., Boleti H., Axisa S., Couture-Tosi E., Tardieux I. Toxofilin, a novel actin-binding protein from Toxoplasma gondii, sequesters actin monomers and caps actin filaments. Mol. Biol. Cell 2000, 11:355-368.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 355-368
    • Poupel, O.1    Boleti, H.2    Axisa, S.3    Couture-Tosi, E.4    Tardieux, I.5
  • 275
    • 0024004133 scopus 로고
    • Amino acid sequence of the murine Mac-1 alpha chain reveals homology with the integrin family and an additional domain related to von Willebrand factor
    • Pytela R. Amino acid sequence of the murine Mac-1 alpha chain reveals homology with the integrin family and an additional domain related to von Willebrand factor. Embo. J. 1988, 7:1371-1378.
    • (1988) Embo. J. , vol.7 , pp. 1371-1378
    • Pytela, R.1
  • 277
    • 0037067759 scopus 로고    scopus 로고
    • The cathepsin B of Toxoplasma gondii, toxopain-1, is critical for parasite invasion and rhoptry protein processing
    • Que X., Ngo H., Lawton J., Gray M., Liu Q., Engel J., Brinen L., Ghosh P., Joiner K.A., Reed S.L. The cathepsin B of Toxoplasma gondii, toxopain-1, is critical for parasite invasion and rhoptry protein processing. J. Biol. Chem. 2002, 277:25791-25797.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25791-25797
    • Que, X.1    Ngo, H.2    Lawton, J.3    Gray, M.4    Liu, Q.5    Engel, J.6    Brinen, L.7    Ghosh, P.8    Joiner, K.A.9    Reed, S.L.10
  • 278
    • 0034883267 scopus 로고    scopus 로고
    • TgM2AP participates in Toxoplasma gondii invasion of host cells and is tightly associated with the adhesive protein TgMIC2
    • Rabenau K.E., Sohrabi A., Tripathy A., Reitter C., Ajioka J.W., Tomley F.M., Carruthers V.B. TgM2AP participates in Toxoplasma gondii invasion of host cells and is tightly associated with the adhesive protein TgMIC2. Mol. Microbiol. 2001, 41:537-547.
    • (2001) Mol. Microbiol. , vol.41 , pp. 537-547
    • Rabenau, K.E.1    Sohrabi, A.2    Tripathy, A.3    Reitter, C.4    Ajioka, J.W.5    Tomley, F.M.6    Carruthers, V.B.7
  • 279
    • 77949533354 scopus 로고    scopus 로고
    • 4-Bromophenacyl bromide specifically inhibits rhoptry secretion during Toxoplasma invasion
    • Ravindran S., Lodoen M.B., Verhelst S.H., Bogyo M., Boothroyd J.C. 4-Bromophenacyl bromide specifically inhibits rhoptry secretion during Toxoplasma invasion. PLoS One 2009, 4:e8143.
    • (2009) PLoS One , vol.4
    • Ravindran, S.1    Lodoen, M.B.2    Verhelst, S.H.3    Bogyo, M.4    Boothroyd, J.C.5
  • 280
    • 0026077358 scopus 로고
    • A new family of serine-type peptidases related to prolyl oligopeptidase
    • Rawlings N.D., Polgar L., Barrett A.J. A new family of serine-type peptidases related to prolyl oligopeptidase. Biochem. J. 1991, 279(Pt 3):907-908.
    • (1991) Biochem. J. , vol.279 , Issue.PT 3 , pp. 907-908
    • Rawlings, N.D.1    Polgar, L.2    Barrett, A.J.3
  • 281
    • 70350409651 scopus 로고    scopus 로고
    • A helical membrane-binding domain targets the Toxoplasma ROP2 family to the parasitophorous vacuole
    • Reese M.L., Boothroyd J.C. A helical membrane-binding domain targets the Toxoplasma ROP2 family to the parasitophorous vacuole. Traffic 2009, 10:1458-1470.
    • (2009) Traffic , vol.10 , pp. 1458-1470
    • Reese, M.L.1    Boothroyd, J.C.2
  • 282
    • 80051680133 scopus 로고    scopus 로고
    • A conserved non-canonical motif in the pseudoactive site of the ROP5 pseudokinase domain mediates its effect on Toxoplasma virulence
    • Reese M.L., Boothroyd J.C. A conserved non-canonical motif in the pseudoactive site of the ROP5 pseudokinase domain mediates its effect on Toxoplasma virulence. J. Biol. Chem. 2011, 286:29366-29375.
    • (2011) J. Biol. Chem. , vol.286 , pp. 29366-29375
    • Reese, M.L.1    Boothroyd, J.C.2
  • 284
    • 0036139224 scopus 로고    scopus 로고
    • Characterization of TgROP9 (p36), a novel rhoptry protein of Toxoplasma gondii tachyzoites identified by T cell clone
    • Reichmann G., Dlugonska H., Fischer H.G. Characterization of TgROP9 (p36), a novel rhoptry protein of Toxoplasma gondii tachyzoites identified by T cell clone. Mol. Biochem. Parasitol. 2002, 119:43-54.
    • (2002) Mol. Biochem. Parasitol. , vol.119 , pp. 43-54
    • Reichmann, G.1    Dlugonska, H.2    Fischer, H.G.3
  • 286
    • 79953219814 scopus 로고    scopus 로고
    • A genome-wide chromatin-associated nuclear peroxiredoxin from the malaria parasite Plasmodium falciparum
    • Richard D., Bartfai R., Volz J., Ralph S.A., Muller S., Stunnenberg H.G., Cowman A.F. A genome-wide chromatin-associated nuclear peroxiredoxin from the malaria parasite Plasmodium falciparum. J. Biol. Chem. 2011, 286:11746-11755.
    • (2011) J. Biol. Chem. , vol.286 , pp. 11746-11755
    • Richard, D.1    Bartfai, R.2    Volz, J.3    Ralph, S.A.4    Muller, S.5    Stunnenberg, H.G.6    Cowman, A.F.7
  • 287
    • 63449134429 scopus 로고    scopus 로고
    • Identification of rhoptry trafficking determinants and evidence for a novel sorting mechanism in the malaria parasite Plasmodium falciparum
    • Richard D., Kats L.M., Langer C., Black C.G., Mitri K., Boddey J.A., Cowman A.F., Coppel R.L. Identification of rhoptry trafficking determinants and evidence for a novel sorting mechanism in the malaria parasite Plasmodium falciparum. PLoS Pathog. 2009, 5:e1000328.
    • (2009) PLoS Pathog. , vol.5
    • Richard, D.1    Kats, L.M.2    Langer, C.3    Black, C.G.4    Mitri, K.5    Boddey, J.A.6    Cowman, A.F.7    Coppel, R.L.8
  • 288
    • 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 C.A., Riglar D.T., Chan J.A., Foley M., Baum J., Ralph S.A., Norton R.S., Cowman A.F. 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. 2010, 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    Baum, J.6    Ralph, S.A.7    Norton, R.S.8    Cowman, A.F.9
  • 290
    • 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 K.J., Hall J.R., Jennings M.W., Harris T.J., Marsh K., Newbold C.I., Tate V.E., Weatherall D.J. A highly conserved amino-acid sequence in thrombospondin, properdin and in proteins from sporozoites and blood stages of a human malaria parasite. Nature 1988, 335:79-82.
    • (1988) Nature , vol.335 , pp. 79-82
    • Robson, K.J.1    Hall, J.R.2    Jennings, M.W.3    Harris, T.J.4    Marsh, K.5    Newbold, C.I.6    Tate, V.E.7    Weatherall, D.J.8
  • 292
    • 55849084997 scopus 로고    scopus 로고
    • Intervacuolar transport and unique topology of GRA14, a novel dense granule protein in Toxoplasma gondii
    • Rome M.E., Beck J.R., Turetzky J.M., Webster P., Bradley P.J. Intervacuolar transport and unique topology of GRA14, a novel dense granule protein in Toxoplasma gondii. Infect. Immun. 2008, 76:4865-4875.
    • (2008) Infect. Immun. , vol.76 , pp. 4865-4875
    • Rome, M.E.1    Beck, J.R.2    Turetzky, J.M.3    Webster, P.4    Bradley, P.J.5
  • 293
    • 78651504365 scopus 로고    scopus 로고
    • Strain-specific activation of the NF-kappaB pathway by GRA15, a novel Toxoplasma gondii dense granule protein
    • Rosowski E.E., Lu D., Julien L., Rodda L., Gaiser R.A., Jensen K.D., Saeij J.P. Strain-specific activation of the NF-kappaB pathway by GRA15, a novel Toxoplasma gondii dense granule protein. J. Exp. Med. 2011, 208:195-212.
    • (2011) J. Exp. Med. , vol.208 , pp. 195-212
    • Rosowski, E.E.1    Lu, D.2    Julien, L.3    Rodda, L.4    Gaiser, R.A.5    Jensen, K.D.6    Saeij, J.P.7
  • 294
    • 0019605349 scopus 로고
    • The role of the cytoskeleton in the motility of coccidian sporozoites
    • Russell D.G., Sinden R.E. 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
  • 295
    • 0018092436 scopus 로고
    • Effect of cytochalasin D on Toxoplasma gondii cell entry
    • Ryning F.W., Remington J.S. Effect of cytochalasin D on Toxoplasma gondii cell entry. Infect. Immun. 1978, 20:739-743.
    • (1978) Infect. Immun. , vol.20 , pp. 739-743
    • Ryning, F.W.1    Remington, J.S.2
  • 296
    • 0023946345 scopus 로고
    • Characterization of a family of rhoptry proteins of Toxoplasma gondii
    • Sadak A., Taghy Z., Fortier B., Dubremetz J.F. Characterization of a family of rhoptry proteins of Toxoplasma gondii. Mol. Biochem. Parasitol. 1988, 29:203-211.
    • (1988) Mol. Biochem. Parasitol. , vol.29 , pp. 203-211
    • Sadak, A.1    Taghy, Z.2    Fortier, B.3    Dubremetz, J.F.4
  • 298
    • 33846322896 scopus 로고    scopus 로고
    • Toxoplasma co-opts host gene expression by injection of a polymorphic kinase homologue
    • Saeij J.P., Coller S., Boyle J.P., Jerome M.E., White M.W., Boothroyd J.C. Toxoplasma co-opts host gene expression by injection of a polymorphic kinase homologue. Nature 2007, 445:324-327.
    • (2007) Nature , vol.445 , pp. 324-327
    • Saeij, J.P.1    Coller, S.2    Boyle, J.P.3    Jerome, M.E.4    White, M.W.5    Boothroyd, J.C.6
  • 299
    • 0026885958 scopus 로고
    • Localization of a Toxoplasma gondii rhoptry protein by immunoelectron microscopy during and after host cell penetration
    • Saffer L.D., Mercereau-Puijalon O., Dubremetz J.F., Schwartzman J.D. Localization of a Toxoplasma gondii rhoptry protein by immunoelectron microscopy during and after host cell penetration. J. Protozool. 1992, 39:526-530.
    • (1992) J. Protozool. , vol.39 , pp. 526-530
    • Saffer, L.D.1    Mercereau-Puijalon, O.2    Dubremetz, J.F.3    Schwartzman, J.D.4
  • 300
    • 79251602713 scopus 로고    scopus 로고
    • Intramembrane cleavage of AMA1 triggers Toxoplasma to switch from an invasive to a replicative mode
    • Santos J.M., Ferguson D.J., Blackman M.J., Soldati-Favre D. Intramembrane cleavage of AMA1 triggers Toxoplasma to switch from an invasive to a replicative mode. Science 2011, 331:473-477.
    • (2011) Science , vol.331 , pp. 473-477
    • Santos, J.M.1    Ferguson, D.J.2    Blackman, M.J.3    Soldati-Favre, D.4
  • 301
    • 84867813772 scopus 로고    scopus 로고
    • Microneme protein 5 regulates the activity of Toxoplasma subtilisin 1 by mimicking a subtilisin prodomain
    • Saouros S., Dou Z., Henry M., Marchant J., Carruthers V.B., Matthews S. Microneme protein 5 regulates the activity of Toxoplasma subtilisin 1 by mimicking a subtilisin prodomain. J. Biol. Chem. 2012, 287:36029-36040.
    • (2012) J. Biol. Chem. , vol.287 , pp. 36029-36040
    • Saouros, S.1    Dou, Z.2    Henry, M.3    Marchant, J.4    Carruthers, V.B.5    Matthews, S.6
  • 304
    • 0035688757 scopus 로고    scopus 로고
    • Aldolase-localization in cultured cells: cell-type and substrate-specific regulation of cytoskeletal associations
    • Schindler R., Weichselsdorfer E., Wagner O., Bereiter-Hahn J. Aldolase-localization in cultured cells: cell-type and substrate-specific regulation of cytoskeletal associations. Biochem. Cell Biol. 2001, 79:719-728.
    • (2001) Biochem. Cell Biol. , vol.79 , pp. 719-728
    • Schindler, R.1    Weichselsdorfer, E.2    Wagner, O.3    Bereiter-Hahn, J.4
  • 305
    • 37249042323 scopus 로고    scopus 로고
    • Vesicle trafficking during sporozoite development in Plasmodium berghei: ultrastructural evidence for a novel trafficking mechanism
    • Schrevel J., Asfaux-Foucher G., Hopkins J.M., Robert V., Bourgouin C., Prensier G., Bannister L.H. Vesicle trafficking during sporozoite development in Plasmodium berghei: ultrastructural evidence for a novel trafficking mechanism. Parasitology 2008, 135:1-12.
    • (2008) Parasitology , vol.135 , pp. 1-12
    • Schrevel, J.1    Asfaux-Foucher, G.2    Hopkins, J.M.3    Robert, V.4    Bourgouin, C.5    Prensier, G.6    Bannister, L.H.7
  • 306
    • 0028115808 scopus 로고
    • The parasitophorous vacuole membrane surrounding intracellular Toxoplasma gondii functions as a molecular sieve
    • Schwab J.C., Beckers C.J., Joiner K.A. The parasitophorous vacuole membrane surrounding intracellular Toxoplasma gondii functions as a molecular sieve. Proc. Natl. Acad. Sci. U. S. A. 1994, 91:509-513.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 509-513
    • Schwab, J.C.1    Beckers, C.J.2    Joiner, K.A.3
  • 307
    • 0022596428 scopus 로고
    • Inhibition of a penetration-enhancing factor of Toxoplasma gondii by monoclonal antibodies specific for rhoptries
    • Schwartzman J.D. Inhibition of a penetration-enhancing factor of Toxoplasma gondii by monoclonal antibodies specific for rhoptries. Infect. Immun. 1986, 51:760-764.
    • (1986) Infect. Immun. , vol.51 , pp. 760-764
    • Schwartzman, J.D.1
  • 308
    • 0027033272 scopus 로고
    • How Toxoplasma gondii gets in and out of host cells
    • Schwartzman J.D., Saffer L.D. How Toxoplasma gondii gets in and out of host cells. Subcell Biochem. 1992, 18:333-364.
    • (1992) Subcell Biochem. , vol.18 , pp. 333-364
    • Schwartzman, J.D.1    Saffer, L.D.2
  • 310
    • 2442602365 scopus 로고    scopus 로고
    • Plant PP2C phosphatases: emerging functions in stress signaling
    • Schweighofer A., Hirt H., Meskiene I. Plant PP2C phosphatases: emerging functions in stress signaling. Trends Plant. Sci. 2004, 9:236-243.
    • (2004) Trends Plant. Sci. , vol.9 , pp. 236-243
    • Schweighofer, A.1    Hirt, H.2    Meskiene, I.3
  • 311
    • 0032557645 scopus 로고    scopus 로고
    • X-ray crystal structure of the human galectin-3 carbohydrate recognition domain at 2.1-A resolution
    • Seetharaman J., Kanigsberg A., Slaaby R., Leffler H., Barondes S.H., Rini J.M. X-ray crystal structure of the human galectin-3 carbohydrate recognition domain at 2.1-A resolution. J. Biol. Chem. 1998, 273:13047-13052.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13047-13052
    • Seetharaman, J.1    Kanigsberg, A.2    Slaaby, R.3    Leffler, H.4    Barondes, S.H.5    Rini, J.M.6
  • 312
    • 0031759012 scopus 로고    scopus 로고
    • Acidic compartments and rhoptry formation in Toxoplasma gondii
    • Shaw M.K., Roos D.S., Tilney L.G. Acidic compartments and rhoptry formation in Toxoplasma gondii. Parasitology 1998, 117(Pt 5):435-443.
    • (1998) Parasitology , vol.117 , Issue.PT 5 , pp. 435-443
    • Shaw, M.K.1    Roos, D.S.2    Tilney, L.G.3
  • 313
    • 41849117736 scopus 로고    scopus 로고
    • Identification of trafficking determinants for polytopic rhomboid proteases in Toxoplasma gondii
    • Sheiner L., Dowse T.J., Soldati-Favre D. Identification of trafficking determinants for polytopic rhomboid proteases in Toxoplasma gondii. Traffic 2008, 9:665-677.
    • (2008) Traffic , vol.9 , pp. 665-677
    • Sheiner, L.1    Dowse, T.J.2    Soldati-Favre, D.3
  • 315
    • 0041856096 scopus 로고    scopus 로고
    • Toxoplasma gondii: perfecting an intracellular life style
    • Sibley L.D. Toxoplasma gondii: perfecting an intracellular life style. Traffic 2003, 4:581-586.
    • (2003) Traffic , vol.4 , pp. 581-586
    • Sibley, L.D.1
  • 316
    • 77957371578 scopus 로고    scopus 로고
    • How apicomplexan parasites move in and out of cells
    • Sibley L.D. How apicomplexan parasites move in and out of cells. Curr. Opin. Biotechnol. 2010, 21:592-598.
    • (2010) Curr. Opin. Biotechnol. , vol.21 , pp. 592-598
    • Sibley, L.D.1
  • 317
    • 0034139847 scopus 로고    scopus 로고
    • Cell invasion by un-palatable parasites
    • Sibley L.D., Andrews N.W. Cell invasion by un-palatable parasites. Traffic 2000, 1:100-106.
    • (2000) Traffic , vol.1 , pp. 100-106
    • Sibley, L.D.1    Andrews, N.W.2
  • 318
    • 0022980730 scopus 로고
    • Toxoplasma modifies macrophage phagosomes by secretion of a vesicular network rich in surface proteins
    • Sibley L.D., Krahenbuhl J.L., Adams G.M., Weidner E. Toxoplasma modifies macrophage phagosomes by secretion of a vesicular network rich in surface proteins. J. Cell. Biol. 1986, 103:867-874.
    • (1986) J. Cell. Biol. , vol.103 , pp. 867-874
    • Sibley, L.D.1    Krahenbuhl, J.L.2    Adams, G.M.3    Weidner, E.4
  • 319
    • 0027973621 scopus 로고
    • Toxoplasma gondii: secretion of a potent nucleoside triphosphate hydrolase into the parasitophorous vacuole
    • Sibley L.D., Niesman I.R., Asai T., Takeuchi T. Toxoplasma gondii: secretion of a potent nucleoside triphosphate hydrolase into the parasitophorous vacuole. Exp. Parasitol. 1994, 79:301-311.
    • (1994) Exp. Parasitol. , vol.79 , pp. 301-311
    • Sibley, L.D.1    Niesman, I.R.2    Asai, T.3    Takeuchi, T.4
  • 320
    • 0028954043 scopus 로고
    • Regulated secretion of multi-lamellar vesicles leads to formation of a tubulo-vesicular network in host cell vacuoles occupied by Toxoplasma gondii
    • Sibley L.D., Niesman I.R., Parmley S.F., Cesbron-Delauw M.F. Regulated secretion of multi-lamellar vesicles leads to formation of a tubulo-vesicular network in host cell vacuoles occupied by Toxoplasma gondii. J. Cell Sci. 1995, 108:1669-1677.
    • (1995) J. Cell Sci. , vol.108 , pp. 1669-1677
    • Sibley, L.D.1    Niesman, I.R.2    Parmley, S.F.3    Cesbron-Delauw, M.F.4
  • 321
    • 0025987923 scopus 로고
    • Proposal for a uniform genetic nomenclature in Toxoplasma gondii
    • Sibley L.D., Pfefferkorn E.R., Boothroyd J.C. Proposal for a uniform genetic nomenclature in Toxoplasma gondii. Parasitol. Today 1991, 7:327-328.
    • (1991) Parasitol. Today , vol.7 , pp. 327-328
    • Sibley, L.D.1    Pfefferkorn, E.R.2    Boothroyd, J.C.3
  • 322
    • 0021827581 scopus 로고
    • Phagosome acidification blocked by intracellular Toxoplasma gondii
    • Sibley L.D., Weidner E., Krahenbuhl J.L. Phagosome acidification blocked by intracellular Toxoplasma gondii. Nature 1985, 315:416-419.
    • (1985) Nature , vol.315 , pp. 416-419
    • Sibley, L.D.1    Weidner, E.2    Krahenbuhl, J.L.3
  • 323
    • 0032524883 scopus 로고    scopus 로고
    • Induced activation of the Toxoplasma gondii nucleoside triphosphate hydrolase leads to depletion of host cell ATP levels and rapid exit of intracellular parasites from infected cells
    • Silverman J.A., Qi H., Riehl A., Beckers C., Nakaar V., Joiner K.A. Induced activation of the Toxoplasma gondii nucleoside triphosphate hydrolase leads to depletion of host cell ATP levels and rapid exit of intracellular parasites from infected cells. J. Biol. Chem. 1998, 273:12352-12359.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12352-12359
    • Silverman, J.A.1    Qi, H.2    Riehl, A.3    Beckers, C.4    Nakaar, V.5    Joiner, K.A.6
  • 325
    • 0035833263 scopus 로고    scopus 로고
    • The Toxoplasma gondii protein ROP2 mediates host organelle association with the parasitophorous vacuole membrane
    • Sinai A.P., Joiner K.A. The Toxoplasma gondii protein ROP2 mediates host organelle association with the parasitophorous vacuole membrane. J. Cell Biol. 2001, 154:95-108.
    • (2001) J. Cell Biol. , vol.154 , pp. 95-108
    • Sinai, A.P.1    Joiner, K.A.2
  • 326
    • 0030783010 scopus 로고    scopus 로고
    • Association of host cell endoplasmic reticulum and mitochondria with the Toxoplasma gondii parasitophorous vacuole membrane: a high affinity interaction
    • Sinai A.P., Webster P., Joiner K.A. Association of host cell endoplasmic reticulum and mitochondria with the Toxoplasma gondii parasitophorous vacuole membrane: a high affinity interaction. J. Cell Sci. 1997, 110(Pt 17):2117-2128.
    • (1997) J. Cell Sci. , vol.110 , Issue.PT 17 , pp. 2117-2128
    • Sinai, A.P.1    Webster, P.2    Joiner, K.A.3
  • 327
    • 77649263117 scopus 로고    scopus 로고
    • Distinct external signals trigger sequential release of apical organelles during erythrocyte invasion by malaria parasites
    • Singh S., Alam M.M., Pal-Bhowmick I., Brzostowski J.A., Chitnis C.E. Distinct external signals trigger sequential release of apical organelles during erythrocyte invasion by malaria parasites. PLoS Pathog. 2010, 6:e1000746.
    • (2010) PLoS Pathog. , vol.6
    • Singh, S.1    Alam, M.M.2    Pal-Bhowmick, I.3    Brzostowski, J.A.4    Chitnis, C.E.5
  • 332
    • 1642396715 scopus 로고    scopus 로고
    • Toxoplasma as a novel system for motility
    • Soldati D., Meissner M. Toxoplasma as a novel system for motility. Curr. Opin. Cell Biol. 2004, 16:32-40.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 32-40
    • Soldati, D.1    Meissner, M.2
  • 333
    • 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., Puri C., Wright S., Crisanti A. Molecular cloning and expression analysis of a Cryptosporidium parvum gene encoding a new member of the thrombospondin family. Mol. Biochem. Parasitol. 1998, 92:147-162.
    • (1998) Mol. Biochem. Parasitol. , vol.92 , pp. 147-162
    • Spano, F.1    Putignani, L.2    Naitza, S.3    Puri, C.4    Wright, S.5    Crisanti, A.6
  • 334
    • 0030737802 scopus 로고    scopus 로고
    • Time lapse video microscopy and ultrastructure of penetrating sporozoites, types 1 and 2 parasitophorous vacuoles, and the transformation of sporozoites to tachyzoites of the VEG strain of Toxoplasma gondii
    • Speer C.A., Dubey J.P., Blixt J.A., Prokop K. Time lapse video microscopy and ultrastructure of penetrating sporozoites, types 1 and 2 parasitophorous vacuoles, and the transformation of sporozoites to tachyzoites of the VEG strain of Toxoplasma gondii. J. Parasitol. 1997, 83:565-574.
    • (1997) J. Parasitol. , vol.83 , pp. 565-574
    • Speer, C.A.1    Dubey, J.P.2    Blixt, J.A.3    Prokop, K.4
  • 335
    • 0029561956 scopus 로고
    • Sporozoites of Toxoplasma gondii lack dense-granule protein GRA3 and form a unique parasitophorous vacuole
    • Speer C.A., Tilley M., Temple M.E., Blixt J.A., Dubey J.P., White M.W. Sporozoites of Toxoplasma gondii lack dense-granule protein GRA3 and form a unique parasitophorous vacuole. Mol. Biochem. Parasitol. 1995, 75:75-86.
    • (1995) Mol. Biochem. Parasitol. , vol.75 , pp. 75-86
    • Speer, C.A.1    Tilley, M.2    Temple, M.E.3    Blixt, J.A.4    Dubey, J.P.5    White, M.W.6
  • 337
    • 33750077590 scopus 로고    scopus 로고
    • Two separate, conserved acidic amino acid domains within the Toxoplasma gondii MIC2 cytoplasmic tail are required for parasite survival
    • Starnes G.L., Jewett T.J., Carruthers V.B., Sibley L.D. Two separate, conserved acidic amino acid domains within the Toxoplasma gondii MIC2 cytoplasmic tail are required for parasite survival. J. Biol. Chem. 2006, 281:30745-30754.
    • (2006) J. Biol. Chem. , vol.281 , pp. 30745-30754
    • Starnes, G.L.1    Jewett, T.J.2    Carruthers, V.B.3    Sibley, L.D.4
  • 338
    • 0037893251 scopus 로고    scopus 로고
    • En route to the vacuole. Tracing the secretory pathway of Toxoplasma gondii
    • JAI Press Inc., Stamford, Connecticut, G. S. (Ed.)
    • Stedman T.T., Joiner K.A. En route to the vacuole. Tracing the secretory pathway of Toxoplasma gondii. Phagocytosis: microbial invasion 1999, 233-261. JAI Press Inc., Stamford, Connecticut. G. S. (Ed.).
    • (1999) Phagocytosis: microbial invasion , pp. 233-261
    • Stedman, T.T.1    Joiner, K.A.2
  • 340
    • 0022588228 scopus 로고
    • Rhoptry secretion of membranous whorls by Plasmodium falciparum merozoites
    • Stewart M.J., Schulman S., Vanderberg J.P. Rhoptry secretion of membranous whorls by Plasmodium falciparum merozoites. Am. J. Trop. Med. Hyg. 1986, 35:37-44.
    • (1986) Am. J. Trop. Med. Hyg. , vol.35 , pp. 37-44
    • Stewart, M.J.1    Schulman, S.2    Vanderberg, J.P.3
  • 341
    • 0031260381 scopus 로고    scopus 로고
    • Toxoplasma gondii: dithiol-induced Ca2+ flux causes egress of parasites from the parasitophorous vacuole
    • Stommel E.W., Ely K.H., Schwartzman J.D., Kasper L.H. Toxoplasma gondii: dithiol-induced Ca2+ flux causes egress of parasites from the parasitophorous vacuole. Exp. Parasitol. 1997, 87:88-97.
    • (1997) Exp. Parasitol. , vol.87 , pp. 88-97
    • Stommel, E.W.1    Ely, K.H.2    Schwartzman, J.D.3    Kasper, L.H.4
  • 342
    • 62149116563 scopus 로고    scopus 로고
    • Novel components of the Apicomplexan moving junction reveal conserved and coccidia-restricted elements
    • Straub K.W., Cheng S.J., Sohn C.S., Bradley P.J. Novel components of the Apicomplexan moving junction reveal conserved and coccidia-restricted elements. Cell Microbiol. 2009, 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
  • 343
    • 79953287282 scopus 로고    scopus 로고
    • The moving junction protein RON8 facilitates firm attachment and host cell invasion in Toxoplasma gondii
    • Straub K.W., Peng E.D., Hajagos B.E., Tyler J.S., Bradley P.J. The moving junction protein RON8 facilitates firm attachment and host cell invasion in Toxoplasma gondii. PLoS Pathog. 2011, 7:e1002007.
    • (2011) PLoS Pathog. , vol.7
    • Straub, K.W.1    Peng, E.D.2    Hajagos, B.E.3    Tyler, J.S.4    Bradley, P.J.5
  • 344
    • 0032078205 scopus 로고    scopus 로고
    • Expression, selection, and organellar targeting of the green fluorescent protein in Toxoplasma gondii
    • Striepen B., He C.Y., Matrajt M., Soldati D., Roos D.S. Expression, selection, and organellar targeting of the green fluorescent protein in Toxoplasma gondii. Mol. Biochem. Parasitol. 1998, 92:325-338.
    • (1998) Mol. Biochem. Parasitol. , vol.92 , pp. 325-338
    • Striepen, B.1    He, C.Y.2    Matrajt, M.3    Soldati, D.4    Roos, D.S.5
  • 345
    • 0029738461 scopus 로고    scopus 로고
    • Toxoplasma invasion: the parasitophorous vacuole is formed from host cell plasma membrane and pinches off via a fission pore
    • Suss-Toby E., Zimmerberg J., Ward G.E. Toxoplasma invasion: the parasitophorous vacuole is formed from host cell plasma membrane and pinches off via a fission pore. Proc. Natl. Acad. Sci. U. S. A. 1996, 93:8413-8418.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 8413-8418
    • Suss-Toby, E.1    Zimmerberg, J.2    Ward, G.E.3
  • 346
    • 78149255164 scopus 로고    scopus 로고
    • Host cell invasion by Toxoplasma gondii is temporally regulated by the host microtubule cytoskeleton
    • Sweeney K.R., Morrissette N.S., LaChapelle S., Blader I.J. Host cell invasion by Toxoplasma gondii is temporally regulated by the host microtubule cytoskeleton. Eukaryot. Cell 2010, 9:1680-1689.
    • (2010) Eukaryot. Cell , vol.9 , pp. 1680-1689
    • Sweeney, K.R.1    Morrissette, N.S.2    LaChapelle, S.3    Blader, I.J.4
  • 347
    • 0037191047 scopus 로고    scopus 로고
    • Crystal structure of the TSP-1 type 1 repeats: a novel layered fold and its biological implication
    • Tan K., Duquette M., Liu J.H., Dong Y., Zhang R., Joachimiak A., Lawler J., Wang J.H. Crystal structure of the TSP-1 type 1 repeats: a novel layered fold and its biological implication. J. Cell Biol. 2002, 159:373-382.
    • (2002) J. Cell Biol. , vol.159 , pp. 373-382
    • Tan, K.1    Duquette, M.2    Liu, J.H.3    Dong, Y.4    Zhang, R.5    Joachimiak, A.6    Lawler, J.7    Wang, J.H.8
  • 349
    • 0021680399 scopus 로고
    • The Fab fragments of monoclonal IgG to a merozoite surface antigen inhibit Plasmodium knowlesi invasion of erythrocytes
    • Thomas A.W., Deans J.A., Mitchell G.H., Alderson T., Cohen S. The Fab fragments of monoclonal IgG to a merozoite surface antigen inhibit Plasmodium knowlesi invasion of erythrocytes. Mol. Biochem. Parasitol. 1984, 13:187-199.
    • (1984) Mol. Biochem. Parasitol. , vol.13 , pp. 187-199
    • Thomas, A.W.1    Deans, J.A.2    Mitchell, G.H.3    Alderson, T.4    Cohen, S.5
  • 350
    • 0030734119 scopus 로고    scopus 로고
    • Toxoplasma gondii sporozoites form a transient parasitophorous vacuole that is impermeable and contains only a subset of dense-granule proteins
    • Tilley M., Fichera M.E., Jerome M.E., Roos D.S., White M.W. Toxoplasma gondii sporozoites form a transient parasitophorous vacuole that is impermeable and contains only a subset of dense-granule proteins. Infect. Immun. 1997, 65:4598-4605.
    • (1997) Infect. Immun. , vol.65 , pp. 4598-4605
    • Tilley, M.1    Fichera, M.E.2    Jerome, M.E.3    Roos, D.S.4    White, M.W.5
  • 351
    • 0034818322 scopus 로고    scopus 로고
    • EtMIC4: a microneme protein from Eimeria tenella that contains tandem arrays of epidermal growth factor-like repeats and thrombospondin type-I repeats
    • Tomley F.M., Billington K.J., Bumstead J.M., Clark J.D., Monaghan P. EtMIC4: a microneme protein from Eimeria tenella that contains tandem arrays of epidermal growth factor-like repeats and thrombospondin type-I repeats. Int. J. Parasitol. 2001, 31:1303-1310.
    • (2001) Int. J. Parasitol. , vol.31 , pp. 1303-1310
    • Tomley, F.M.1    Billington, K.J.2    Bumstead, J.M.3    Clark, J.D.4    Monaghan, P.5
  • 352
    • 84873051813 scopus 로고    scopus 로고
    • Babesia divergens and Neospora caninum Apical Membrane Antigen 1 (AMA1) structures reveal selectivity and plasticity in apicomplexan parasite host cell invasion
    • Tonkin M.L., Crawford J., Lebrun M.L., Boulanger M.J. Babesia divergens and Neospora caninum Apical Membrane Antigen 1 (AMA1) structures reveal selectivity and plasticity in apicomplexan parasite host cell invasion. Protein Sci. 2012, 22:114-127.
    • (2012) Protein Sci. , vol.22 , pp. 114-127
    • Tonkin, M.L.1    Crawford, J.2    Lebrun, M.L.3    Boulanger, M.J.4
  • 353
    • 77957316549 scopus 로고    scopus 로고
    • Structure of the micronemal protein 2 A/I domain from Toxoplasma gondii
    • Tonkin M.L., Grujic O., Pearce M., Crawford J., Boulanger M.J. Structure of the micronemal protein 2 A/I domain from Toxoplasma gondii. Protein Sci. 2010, 19:1985-1990.
    • (2010) Protein Sci. , vol.19 , pp. 1985-1990
    • Tonkin, M.L.1    Grujic, O.2    Pearce, M.3    Crawford, J.4    Boulanger, M.J.5
  • 355
    • 1042289743 scopus 로고    scopus 로고
    • Characterization of a membrane-associated rhoptry protein of Plasmodium falciparum
    • Topolska A.E., Lidgett A., Truman D., Fujioka H., Coppel R.L. Characterization of a membrane-associated rhoptry protein of Plasmodium falciparum. J. Biol. Chem. 2004, 279:4648-4656.
    • (2004) J. Biol. Chem. , vol.279 , pp. 4648-4656
    • Topolska, A.E.1    Lidgett, A.2    Truman, D.3    Fujioka, H.4    Coppel, R.L.5
  • 356
    • 0345534771 scopus 로고    scopus 로고
    • The PAN module: the N-terminal domains of plasminogen and hepatocyte growth factor are homologous with the apple domains of the prekallikrein family and with a novel domain found in numerous nematode proteins
    • Tordai H., Banyai L., Patthy L. The PAN module: the N-terminal domains of plasminogen and hepatocyte growth factor are homologous with the apple domains of the prekallikrein family and with a novel domain found in numerous nematode proteins. FEBS Lett. 1999, 461:63-67.
    • (1999) FEBS Lett. , vol.461 , pp. 63-67
    • Tordai, H.1    Banyai, L.2    Patthy, L.3
  • 357
    • 0027319983 scopus 로고
    • Toxoplasma gondii: differential location of antigens secreted from encysted bradyzoites
    • Torpier G., Charif H., Darcy F., Liu J., Darde M.L., Capron A. Toxoplasma gondii: differential location of antigens secreted from encysted bradyzoites. Exp. Parasitol. 1993, 77:13-22.
    • (1993) Exp. Parasitol. , vol.77 , pp. 13-22
    • Torpier, G.1    Charif, H.2    Darcy, F.3    Liu, J.4    Darde, M.L.5    Capron, A.6
  • 358
    • 77953915276 scopus 로고    scopus 로고
    • Processing and secretion of ROP13: A unique Toxoplasma effector protein
    • Turetzky J.M., Chu D.K., Hajagos B.E., Bradley P.J. Processing and secretion of ROP13: A unique Toxoplasma effector protein. Int. J. Parasitol. 2010, 40:1037-1044.
    • (2010) Int. J. Parasitol. , vol.40 , pp. 1037-1044
    • Turetzky, J.M.1    Chu, D.K.2    Hajagos, B.E.3    Bradley, P.J.4
  • 359
    • 79952234824 scopus 로고    scopus 로고
    • The C-Terminus of Toxoplasma RON2 Provides the Crucial Link between AMA1 and the Host-Associated Invasion Complex
    • Tyler J.S., Boothroyd J.C. The C-Terminus of Toxoplasma RON2 Provides the Crucial Link between AMA1 and the Host-Associated Invasion Complex. PLoS Pathog. 2011, 7:e1001282.
    • (2011) PLoS Pathog. , vol.7
    • Tyler, J.S.1    Boothroyd, J.C.2
  • 360
    • 0029850677 scopus 로고    scopus 로고
    • Rab11 regulates recycling through the pericentriolar recycling endosome
    • Ullrich O., Reinsch S., Urbe S., Zerial M., Parton R.G. Rab11 regulates recycling through the pericentriolar recycling endosome. J. Cell Biol. 1996, 135:913-924.
    • (1996) J. Cell Biol. , vol.135 , pp. 913-924
    • Ullrich, O.1    Reinsch, S.2    Urbe, S.3    Zerial, M.4    Parton, R.G.5
  • 361
    • 0344838627 scopus 로고    scopus 로고
    • Conformational differences in liganded and unliganded states of Galectin-3
    • Umemoto K., Leffler H., Venot A., Valafar H., Prestegard J.H. Conformational differences in liganded and unliganded states of Galectin-3. Biochemistry 2003, 42:3688-3695.
    • (2003) Biochemistry , vol.42 , pp. 3688-3695
    • Umemoto, K.1    Leffler, H.2    Venot, A.3    Valafar, H.4    Prestegard, J.H.5
  • 362
    • 0038771224 scopus 로고    scopus 로고
    • Substrate specificity of rhomboid intramembrane proteases is governed by helix-breaking residues in the substrate transmembrane domain
    • Urban S., Freeman M. Substrate specificity of rhomboid intramembrane proteases is governed by helix-breaking residues in the substrate transmembrane domain. Mol. Cell 2003, 11:1425-1434.
    • (2003) Mol. Cell , vol.11 , pp. 1425-1434
    • Urban, S.1    Freeman, M.2
  • 363
    • 0016276337 scopus 로고
    • Studies on the motility of Plasmodium sporozoites
    • Vanderberg J.P. Studies on the motility of Plasmodium sporozoites. J. Protozool. 1974, 21:527-537.
    • (1974) J. Protozool. , vol.21 , pp. 527-537
    • Vanderberg, J.P.1
  • 364
    • 0033965312 scopus 로고    scopus 로고
    • Mobilization of intracellular calcium upon attachment of Toxoplasma gondii tachyzoites to human fibroblasts is required for invasion
    • Vieira M.C., Moreno S.N. Mobilization of intracellular calcium upon attachment of Toxoplasma gondii tachyzoites to human fibroblasts is required for invasion. Mol. Biochem. Parasitol. 2000, 106:157-162.
    • (2000) Mol. Biochem. Parasitol. , vol.106 , pp. 157-162
    • Vieira, M.C.1    Moreno, S.N.2
  • 367
    • 0031044707 scopus 로고    scopus 로고
    • Molecular characterisation of an expressed sequence tag locus of Toxoplasma gondii encoding the micronemal protein MIC2
    • Wan K.L., Carruthers V.B., Sibley L.D., Ajioka J.W. Molecular characterisation of an expressed sequence tag locus of Toxoplasma gondii encoding the micronemal protein MIC2. Mol. Biochem. Parasitol. 1997, 84:203-214.
    • (1997) Mol. Biochem. Parasitol. , vol.84 , pp. 203-214
    • Wan, K.L.1    Carruthers, V.B.2    Sibley, L.D.3    Ajioka, J.W.4
  • 368
    • 0031574256 scopus 로고    scopus 로고
    • Metabolic compartmentation in living cells: structural association of aldolase
    • Wang J., Tolan D.R., Pagliaro L. Metabolic compartmentation in living cells: structural association of aldolase. Exp. Cell Res. 1997, 237:445-451.
    • (1997) Exp. Cell Res. , vol.237 , pp. 445-451
    • Wang, J.1    Tolan, D.R.2    Pagliaro, L.3
  • 369
    • 0020084825 scopus 로고
    • Attempts to infect plant protoplasts with Toxoplasma gondii
    • Werk R., Fischer S. Attempts to infect plant protoplasts with Toxoplasma gondii. J. Gen. Microbiol. 1982, 128:211-213.
    • (1982) J. Gen. Microbiol. , vol.128 , pp. 211-213
    • Werk, R.1    Fischer, S.2
  • 370
    • 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 C.A., Hynes R.O. Distribution and evolution of von Willebrand/integrin A domains: widely dispersed domains with roles in cell adhesion and elsewhere. Mol. Biol. Cell 2002, 13:3369-3387.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3369-3387
    • Whittaker, C.A.1    Hynes, R.O.2
  • 372
    • 0030037338 scopus 로고    scopus 로고
    • Differences in hydropathic properties of ligand binding at four independent sites in wheat germ agglutinin-oligosaccharide crystal complexes
    • Wright C.S., Kellogg G.E. Differences in hydropathic properties of ligand binding at four independent sites in wheat germ agglutinin-oligosaccharide crystal complexes. Protein Sci. 1996, 5:1466-1476.
    • (1996) Protein Sci. , vol.5 , pp. 1466-1476
    • Wright, C.S.1    Kellogg, G.E.2
  • 373
    • 0025721792 scopus 로고
    • Evolution of a family of N-acetylglucosamine binding proteins containing the disulfide-rich domain of wheat germ agglutinin
    • Wright H.T., Sandrasegaram G., Wright C.S. Evolution of a family of N-acetylglucosamine binding proteins containing the disulfide-rich domain of wheat germ agglutinin. J. Mol. Evol. 1991, 33:283-294.
    • (1991) J. Mol. Evol. , vol.33 , pp. 283-294
    • Wright, H.T.1    Sandrasegaram, G.2    Wright, C.S.3
  • 376
    • 3042667972 scopus 로고    scopus 로고
    • The Plasmodium falciparum Vps4 homologue mediates multivesicular body formation
    • Yang M., Coppens I., Wormsley S., Baevova P., Hoppe H.C., Joiner K.A. The Plasmodium falciparum Vps4 homologue mediates multivesicular body formation. J. Cell Sci. 2004, 117:3831-3838.
    • (2004) J. Cell Sci. , vol.117 , pp. 3831-3838
    • Yang, M.1    Coppens, I.2    Wormsley, S.3    Baevova, P.4    Hoppe, H.C.5    Joiner, K.A.6
  • 377
    • 67649537958 scopus 로고    scopus 로고
    • MIC6 associates with aldolase in host cell invasion by Toxoplasma gondii
    • Zheng B., He A., Gan M., Li Z., He H., Zhan X. MIC6 associates with aldolase in host cell invasion by Toxoplasma gondii. Parasitol. Res. 2009, 105:441-445.
    • (2009) Parasitol. Res. , vol.105 , pp. 441-445
    • Zheng, B.1    He, A.2    Gan, M.3    Li, Z.4    He, H.5    Zhan, X.6
  • 378
    • 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 X.W., Blackman M.J., Howell S.A., Carruthers V.B. Proteomic analysis of cleavage events reveals a dynamic two-step mechanism for proteolysis of a key parasite adhesive complex. Mol. Cell Proteomics 2004, 3:565-576.
    • (2004) Mol. Cell Proteomics , vol.3 , pp. 565-576
    • Zhou, X.W.1    Blackman, M.J.2    Howell, S.A.3    Carruthers, V.B.4
  • 379
    • 26644473883 scopus 로고    scopus 로고
    • The opportunistic pathogen Toxoplasma gondii deploys a diverse legion of invasion and survival proteins
    • Zhou X.W., Kafsack B.F., Cole R.N., Beckett P., Shen R.F., Carruthers V.B. The opportunistic pathogen Toxoplasma gondii deploys a diverse legion of invasion and survival proteins. J. Biol. Chem. 2005, 280:34233-34244.
    • (2005) J. Biol. Chem. , vol.280 , pp. 34233-34244
    • Zhou, X.W.1    Kafsack, B.F.2    Cole, R.N.3    Beckett, P.4    Shen, R.F.5    Carruthers, V.B.6
  • 380
    • 0032583162 scopus 로고    scopus 로고
    • The dense granule antigen, GRA2 of Toxoplasma gondii is a glycoprotein containing O-linked oligosaccharides
    • Zinecker C.F., Striepen B., Tomavo S., Dubremetz J.F., Schwarz R.T. The dense granule antigen, GRA2 of Toxoplasma gondii is a glycoprotein containing O-linked oligosaccharides. Mol. Biochem. Parasitol. 1998, 97:241-246.
    • (1998) Mol. Biochem. Parasitol. , vol.97 , pp. 241-246
    • Zinecker, C.F.1    Striepen, B.2    Tomavo, S.3    Dubremetz, J.F.4    Schwarz, R.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.