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Volumn 26, Issue 1, 1997, Pages 163-173

Participation of myosin in gliding motility and host cell invasion by Toxoplasma gondii

Author keywords

[No Author keywords available]

Indexed keywords

MYOSIN;

EID: 0030770219     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1997.5671913.x     Document Type: Article
Times cited : (210)

References (38)
  • 1
    • 0024346185 scopus 로고
    • Binding of myosin I to membrane lipids
    • Adams, R.J., and Pollard, T.D. (1989) Binding of myosin I to membrane lipids. Nature 340: 565-568.
    • (1989) Nature , vol.340 , pp. 565-568
    • Adams, R.J.1    Pollard, T.D.2
  • 2
    • 0030956863 scopus 로고    scopus 로고
    • Sequential protein secretion from three distinct organelles of Toxoplasma gondii accompanies invasion of human fibroblasts
    • Carruthers, V.B., and Sibley, L.D. (1997) Sequential protein secretion from three distinct organelles of Toxoplasma gondii accompanies invasion of human fibroblasts. Eur J Cell Biol 73: 114-123.
    • (1997) Eur J Cell Biol , vol.73 , pp. 114-123
    • Carruthers, V.B.1    Sibley, L.D.2
  • 3
    • 0025091063 scopus 로고
    • Effect of 2,3 butanedione 2 monoxime on slow inward and transient outward currents in rat ventricular myocytes
    • Coulombe, A., Lefevre, I.A., Deroubaix, E., Thuringer, D., Coraboeuf, E. (1990) Effect of 2,3 butanedione 2 monoxime on slow inward and transient outward currents in rat ventricular myocytes. J Mol Cell Cardiol 22: 921-932.
    • (1990) J Mol Cell Cardiol , vol.22 , pp. 921-932
    • Coulombe, A.1    Lefevre, I.A.2    Deroubaix, E.3    Thuringer, D.4    Coraboeuf, E.5
  • 4
    • 0029098971 scopus 로고
    • Myosin is involved in postmitotic cell spreading
    • Cramer, L.P., and Mitchison, T.J. (1995) Myosin is involved in postmitotic cell spreading. J Cell Biol 131: 179-189.
    • (1995) J Cell Biol , vol.131 , pp. 179-189
    • Cramer, L.P.1    Mitchison, T.J.2
  • 5
    • 0030847202 scopus 로고    scopus 로고
    • Investigation of the mechanism of retraction of the cell margin and rearward flow of nodules during mitotic cell rounding
    • Cramer, L.P., and Mitchison, T.J. (1997) Investigation of the mechanism of retraction of the cell margin and rearward flow of nodules during mitotic cell rounding. Mol Biol Cell 8: 109-119.
    • (1997) Mol Biol Cell , vol.8 , pp. 109-119
    • Cramer, L.P.1    Mitchison, T.J.2
  • 6
    • 0017700911 scopus 로고
    • Comparative electron microscope study of pellicular structures in coccidia (Sarcocystis, Besnoitia, Eimeria)
    • D'Haese, J., Melhorn, H., and Peters, W. (1977) Comparative electron microscope study of pellicular structures in coccidia (Sarcocystis, Besnoitia, Eimeria). Int J Parasitol 7: 505-518.
    • (1977) Int J Parasitol , vol.7 , pp. 505-518
    • D'Haese, J.1    Melhorn, H.2    Peters, W.3
  • 7
    • 0029869791 scopus 로고    scopus 로고
    • Toxoplasma invasion of mammalian cells is powered by the actin cytoskeleton of the parasite
    • Dobrowolski, J.M., and Sibley, L.D. (1996) Toxoplasma invasion of mammalian cells is powered by the actin cytoskeleton of the parasite. Cell 84: 933-939.
    • (1996) Cell , vol.84 , pp. 933-939
    • Dobrowolski, J.M.1    Sibley, L.D.2
  • 8
    • 0030754072 scopus 로고    scopus 로고
    • Actin in Toxoplasma gondii is encoded by a single-copy gene, ACT1 and exists primarily in a globular form
    • Dobrowolski, J.M., Niesman, I.R., and Sibley, L.D. (1997) Actin in Toxoplasma gondii is encoded by a single-copy gene, ACT1 and exists primarily in a globular form. Cell Motil Cytoskel 37: 253-262.
    • (1997) Cell Motil Cytoskel , vol.37 , pp. 253-262
    • Dobrowolski, J.M.1    Niesman, I.R.2    Sibley, L.D.3
  • 9
    • 0000851766 scopus 로고
    • Toxoplasma, Hammondia, Besniotia, Sarcocystis, and other Tissue Cyst-forming Coccidia of Man and Animals
    • Kreier, J.P. (ed.). New York: Academic Press
    • Dubey, J.P. (1977) Toxoplasma, Hammondia, Besniotia, Sarcocystis, and other Tissue Cyst-forming Coccidia of Man and Animals. In Parasitic Protozoa Kreier, J.P. (ed.). New York: Academic Press, pp. 101-237.
    • (1977) Parasitic Protozoa , pp. 101-237
    • Dubey, J.P.1
  • 10
    • 0017818294 scopus 로고
    • Freeze fracture study of the pellicle of an Eimerian sporozoite (Protozoa, Coccidia)
    • Dubremetz, J.F., and Torpier, G. (1978) Freeze fracture study of the pellicle of an Eimerian sporozoite (Protozoa, Coccidia). J Ultrastr Res 62: 94-109.
    • (1978) J Ultrastr Res , vol.62 , pp. 94-109
    • Dubremetz, J.F.1    Torpier, G.2
  • 11
  • 12
    • 0031559564 scopus 로고    scopus 로고
    • A novel class of unconventional myosins from Toxoplasma gondii
    • Heintzelman, M.B., and Schwartzman, J.D. (1997) A novel class of unconventional myosins from Toxoplasma gondii. J Mol Biol 271: 139-146.
    • (1997) J Mol Biol , vol.271 , pp. 139-146
    • Heintzelman, M.B.1    Schwartzman, J.D.2
  • 13
    • 0024709495 scopus 로고
    • Dictyostelium discoideum contains a gene encoding a myosin I heavy chain
    • Jung, J., Saxe, C.L., Kimmel, A.R., and Hammer, J.A. (1989) Dictyostelium discoideum contains a gene encoding a myosin I heavy chain. Proc Natl Acad Sci USA 86: 6186-6190.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 6186-6190
    • Jung, J.1    Saxe, C.L.2    Kimmel, A.R.3    Hammer, J.A.4
  • 14
    • 0023768222 scopus 로고
    • Cell motility of sporozoan protozoa
    • King, C.A. (1988) Cell motility of sporozoan protozoa. Parasitol Today 11: 315-318.
    • (1988) Parasitol Today , vol.11 , pp. 315-318
    • King, C.A.1
  • 15
    • 0024550448 scopus 로고
    • Calphostin C, a novel microbial compound, is a highly potent and specific inhibitor of protein kinase C
    • Kobayashi, E., Nakano, H., Morimoto, M., and Tamaoki, T. (1989) Calphostin C, a novel microbial compound, is a highly potent and specific inhibitor of protein kinase C. Biochem Biophys Res Commun 159: 584-553.
    • (1989) Biochem Biophys Res Commun , vol.159 , pp. 584-1553
    • Kobayashi, E.1    Nakano, H.2    Morimoto, M.3    Tamaoki, T.4
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0023803882 scopus 로고
    • Two monoclonal antibodies to actin: One muscle selective and one generally reactive
    • Lessard, J.L. (1988) Two monoclonal antibodies to actin: one muscle selective and one generally reactive. Cell Motil Cytoskel 10: 349-362.
    • (1988) Cell Motil Cytoskel , vol.10 , pp. 349-362
    • Lessard, J.L.1
  • 18
    • 0029863153 scopus 로고    scopus 로고
    • Myosin drives retrograde F-actin flow in neuronal growth cones
    • Lin, C.H., Espreafico, E.M., Mooseker, M.S., and Forscher, P. (1996) Myosin drives retrograde F-actin flow in neuronal growth cones. Neuron 16: 769-782.
    • (1996) Neuron , vol.16 , pp. 769-782
    • Lin, C.H.1    Espreafico, E.M.2    Mooseker, M.S.3    Forscher, P.4
  • 19
    • 0028871168 scopus 로고
    • myoA of Aspergillus nidulans encodes an essential myosin I required for secretion and polarized growth
    • McGoldrick, C.A., Gruver, C., and May, G.S. (1995) myoA of Aspergillus nidulans encodes an essential myosin I required for secretion and polarized growth. J Cell Biol 128: 577-587.
    • (1995) J Cell Biol , vol.128 , pp. 577-587
    • McGoldrick, C.A.1    Gruver, C.2    May, G.S.3
  • 20
    • 0030049170 scopus 로고    scopus 로고
    • Actin-based cell motility and cell locomotion
    • Mitchison, T.J., and Cramer, L.P. (1996) Actin-based cell motility and cell locomotion. Cell 84: 37-379.
    • (1996) Cell , vol.84 , pp. 37-379
    • Mitchison, T.J.1    Cramer, L.P.2
  • 22
    • 0029016818 scopus 로고
    • Invasion of Toxoplasma gondii occurs by active penetration of the host cell
    • Morisaki, J.H., Heuser, J.E., and Sibley, L.D. (1995) Invasion of Toxoplasma gondii occurs by active penetration of the host cell. J Cell Sci 108: 2457-2464.
    • (1995) J Cell Sci , vol.108 , pp. 2457-2464
    • Morisaki, J.H.1    Heuser, J.E.2    Sibley, L.D.3
  • 23
    • 0031018273 scopus 로고    scopus 로고
    • Subpellicular microtubules associate with an intramembranous particle lattice in the protozoan parasite Toxoplasma gondii
    • Morrissette, N.S., Murray, J.M., and Roos, D.S. (1997) Subpellicular microtubules associate with an intramembranous particle lattice in the protozoan parasite Toxoplasma gondii. J Cell Sci 110: 35-42.
    • (1997) J Cell Sci , vol.110 , pp. 35-42
    • Morrissette, N.S.1    Murray, J.M.2    Roos, D.S.3
  • 24
    • 0025305025 scopus 로고
    • KT5926, a potent and selective inhibitor of myosin light chain kinase
    • Nakanishi, S., Yamada, K., Iwahashi, K., Kuroda, K., and Kase, H. (1990) KT5926, a potent and selective inhibitor of myosin light chain kinase. Mol Pharmacol 37: 482-488.
    • (1990) Mol Pharmacol , vol.37 , pp. 482-488
    • Nakanishi, S.1    Yamada, K.2    Iwahashi, K.3    Kuroda, K.4    Kase, H.5
  • 25
    • 0023264484 scopus 로고
    • Cytoskeleton of Toxoplasma gondii
    • Nichols, B., and Chiappino, M. (1987) Cytoskeleton of Toxoplasma gondii. J Protozool 34: 217-226.
    • (1987) J Protozool , vol.34 , pp. 217-226
    • Nichols, B.1    Chiappino, M.2
  • 26
    • 0030569517 scopus 로고    scopus 로고
    • 2,3 butanedione 2-monoxime (BDM) induces calcium release from canine cardiac sarcoplasmic reticulum
    • Phillips, R.M., and Altschuld, R.A. (1996) 2,3 butanedione 2-monoxime (BDM) induces calcium release from canine cardiac sarcoplasmic reticulum. Biochem Biophys Res Commun 229: 154-157.
    • (1996) Biochem Biophys Res Commun , vol.229 , pp. 154-157
    • Phillips, R.M.1    Altschuld, R.A.2
  • 28
    • 0026573519 scopus 로고
    • Evidence for the expression of an actomyosin in the infective stage of the sporozoan protist Eimeria
    • Preston, T.M., and King, C.A. (1992) Evidence for the expression of an actomyosin in the infective stage of the sporozoan protist Eimeria. Cell Biol Int 16: 377-381.
    • (1992) Cell Biol Int , vol.16 , pp. 377-381
    • Preston, T.M.1    King, C.A.2
  • 29
    • 0019605349 scopus 로고
    • The role of the cytoskeleton in the motility of coccidian sporozoites
    • Russell, D.G., and Sinden, R.E. (1981) The role of the cytoskeleton in the motility of coccidian sporozoites. J Cell Sci 50: 345-359.
    • (1981) J Cell Sci , vol.50 , pp. 345-359
    • Russell, D.G.1    Sinden, R.E.2
  • 30
    • 0020147662 scopus 로고
    • Three-dimensional study of the intact cytoskeleton of coccidian sporozoites
    • Russell, D.G., and Sinden, R.E. (1982) Three-dimensional study of the intact cytoskeleton of coccidian sporozoites. Int J Parasitol 12: 221-226.
    • (1982) Int J Parasitol , vol.12 , pp. 221-226
    • Russell, D.G.1    Sinden, R.E.2
  • 31
    • 0020930996 scopus 로고
    • Immunofluorescent localization of myosin at the anterior pole of the coccidian, Toxoplasma gondii
    • Schwartzman, J.D., and Pfefferkorn, E.R. (1983) Immunofluorescent localization of myosin at the anterior pole of the coccidian, Toxoplasma gondii. J Protozool 30: 657-661.
    • (1983) J Protozool , vol.30 , pp. 657-661
    • Schwartzman, J.D.1    Pfefferkorn, E.R.2
  • 32
    • 0029670076 scopus 로고    scopus 로고
    • Escherichia coli β-galactosidase as an in vitro and in vivo reporter enzyme and stable transfection marker in the intracellular protozoan parasite Toxoplasma gondii
    • Seeber, F., and Boothroyd, J.C. (1996) Escherichia coli β-galactosidase as an in vitro and in vivo reporter enzyme and stable transfection marker in the intracellular protozoan parasite Toxoplasma gondii. Gene 169: 39-45.
    • (1996) Gene , vol.169 , pp. 39-45
    • Seeber, F.1    Boothroyd, J.C.2
  • 33
    • 0023795608 scopus 로고
    • Malaria sporozoites leave behind gliding trails of circumsporozoite protein during gliding motility
    • Stewart, M.J., and Vanderberg, J.P. (1988) Malaria sporozoites leave behind gliding trails of circumsporozoite protein during gliding motility. J Protozool 35: 389-393.
    • (1988) J Protozool , vol.35 , pp. 389-393
    • Stewart, M.J.1    Vanderberg, J.P.2
  • 35
    • 0027399722 scopus 로고
    • The unconventional myosin encoded by the myoA gene plays a role in Dictyostelium motility
    • Titus, M.A., Wessels, D., Spudich, J.A., and Soll, D. (1993) The unconventional myosin encoded by the myoA gene plays a role in Dictyostelium motility. Mol Biol Cell 4: 233-246.
    • (1993) Mol Biol Cell , vol.4 , pp. 233-246
    • Titus, M.A.1    Wessels, D.2    Spudich, J.A.3    Soll, D.4
  • 36
    • 0024450377 scopus 로고
    • Evidence for glycosyl-phosphatidylinositol anchoring of Toxoplasma gondii major surface antigens
    • Tomavo, S., Scwartz, R.T., and Dubremetz, J.F. (1989) Evidence for glycosyl-phosphatidylinositol anchoring of Toxoplasma gondii major surface antigens. Mol Cell Biol 9: 4576-4580.
    • (1989) Mol Cell Biol , vol.9 , pp. 4576-4580
    • Tomavo, S.1    Scwartz, R.T.2    Dubremetz, J.F.3
  • 37
    • 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., and Ajioka, J.W. (1996) Molecular characterisation of an expressed sequence tag locus of Toxoplasma gondii encoding the micronemal protein MIC2. Mol Biochem Parasitol 84: 203-214.
    • (1996) Mol Biochem Parasitol , vol.84 , pp. 203-214
    • Wan, K.L.1    Carruthers, V.B.2    Sibley, L.D.3    Ajioka, J.W.4
  • 38
    • 0026332426 scopus 로고
    • Myosin IB null mutants of Dictyostelium exhibit abnormalities in motility
    • Wessels, D., Murray, J., Jung, G., Hammer, J.A., and Soll, D.R. (1991) Myosin IB null mutants of Dictyostelium exhibit abnormalities in motility. Cell Motil Cytoskel 20: 301-315.
    • (1991) Cell Motil Cytoskel , vol.20 , pp. 301-315
    • Wessels, D.1    Murray, J.2    Jung, G.3    Hammer, J.A.4    Soll, D.R.5


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