메뉴 건너뛰기




Volumn 74, Issue 1, 1997, Pages 92-101

Involvement of calcium and calmodulin in Toxoplasma gondii tachyzoite invasion

Author keywords

Calcium; Calmodulin; Invasion; Toxoplasma gondii

Indexed keywords

CALCIMYCIN; CALCIUM; CALCIUM CHANNEL BLOCKING AGENT; CALMIDAZOLIUM; CALMODULIN; CALMODULIN INHIBITOR; EGTAZIC ACID; TRIFLUOPERAZINE; VERAPAMIL;

EID: 0030764367     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (63)

References (63)
  • 1
    • 0017375151 scopus 로고
    • Transmission and scanning electron microscopy of host cell entry by Toxoplasma gondii
    • Aikawa, M., Y. Komata, T. Asai, O. Midorikawa: Transmission and scanning electron microscopy of host cell entry by Toxoplasma gondii. Am. J. Pathol. 82, 285-296 (1977).
    • (1977) Am. J. Pathol. , vol.82 , pp. 285-296
    • Aikawa, M.1    Komata, Y.2    Asai, T.3    Midorikawa, O.4
  • 2
    • 0026756560 scopus 로고
    • Calcium and calmodulin function in the cell nucleus
    • Bachs, O., N. Agell, E. Carafoli: Calcium and calmodulin function in the cell nucleus. Biochim. Biophys. Acta 1113, 259-270 (1992).
    • (1992) Biochim. Biophys. Acta , vol.1113 , pp. 259-270
    • Bachs, O.1    Agell, N.2    Carafoli, E.3
  • 3
    • 0019876756 scopus 로고
    • Characterization of a novel calmodulin from Dictyostelium discoideum
    • Bazari, W. L., M. Clarke: Characterization of a novel calmodulin from Dictyostelium discoideum. J. Biol. Chem. 256, 3598-3603 (1981).
    • (1981) J. Biol. Chem. , vol.256 , pp. 3598-3603
    • Bazari, W.L.1    Clarke, M.2
  • 4
    • 0029883968 scopus 로고    scopus 로고
    • Agonist-releasable intracellular calcium stores and the phenomenon of store-dependent calcium entry
    • Bode, H. P., K. J. Netter: Agonist-releasable intracellular calcium stores and the phenomenon of store-dependent calcium entry. Biochem. Pharmacol. 51, 993-1001 (1996).
    • (1996) Biochem. Pharmacol. , vol.51 , pp. 993-1001
    • Bode, H.P.1    Netter, K.J.2
  • 5
    • 0014561003 scopus 로고
    • The life cycle of virulent Toxoplasma in cell cultures
    • Bommer, W.: The life cycle of virulent Toxoplasma in cell cultures. Austr. J. Exp. Med. Sci. 47, 505-512 (1969).
    • (1969) Austr. J. Exp. Med. Sci. , vol.47 , pp. 505-512
    • Bommer, W.1
  • 6
    • 33847612208 scopus 로고
    • Adenosinc 3′,5′phosphate in biological materials
    • Butcher, R. W., E. W. Sutherland: Adenosinc 3′,5′phosphate in biological materials. J. Biol. Chem. 237, 1244-1250 (1962).
    • (1962) J. Biol. Chem. , vol.237 , pp. 1244-1250
    • Butcher, R.W.1    Sutherland, E.W.2
  • 8
    • 0029869791 scopus 로고    scopus 로고
    • Toxoplasma invasion of mammalian cells is powered by the actin cytoskeleton of the parasite
    • Dobrowolski, J. M., L. D. Sibley: Toxoplasma invasion of mammalian cells is powered by the actin cytoskeleton of the parasite. Cell 84, 933-939 (1996).
    • (1996) Cell , vol.84 , pp. 933-939
    • Dobrowolski, J.M.1    Sibley, L.D.2
  • 9
    • 0028979316 scopus 로고
    • Intracellular Ca2+ storage in acidocalcisomes of Trypanosoma cruzi
    • Docampo, R., D. A. Scott, A. E. Vercesi, S. N. Moreno: Intracellular Ca2+ storage in acidocalcisomes of Trypanosoma cruzi. Biochem. J. 310, 1005-1012 (1995).
    • (1995) Biochem. J. , vol.310 , pp. 1005-1012
    • Docampo, R.1    Scott, D.A.2    Vercesi, A.E.3    Moreno, S.N.4
  • 10
    • 0029671158 scopus 로고    scopus 로고
    • The role of Ca2+ in the process of cell invasion by intracellular parasites
    • Docampo, R., S. N. J. Moreno: The role of Ca2+ in the process of cell invasion by intracellular parasites. Parasitol. Today 12, 61-65 (1996).
    • (1996) Parasitol. Today , vol.12 , pp. 61-65
    • Docampo, R.1    Moreno, S.N.J.2
  • 11
    • 0026489950 scopus 로고
    • Laminin on Toxoplasma gondii mediates parasite binding to the β1 integrin receptor α6β1 on human foreskin fibroblasts and chinese hamster ovary cells
    • Furtado, G. C., Y. Cao, K. A. Joiner: Laminin on Toxoplasma gondii mediates parasite binding to the β1 integrin receptor α6β1 on human foreskin fibroblasts and chinese hamster ovary cells. Infect. Immun. 60, 4925-4931 (1992).
    • (1992) Infect. Immun. , vol.60 , pp. 4925-4931
    • Furtado, G.C.1    Cao, Y.2    Joiner, K.A.3
  • 12
    • 0028936576 scopus 로고
    • Integrin binding revealed
    • Graves, J. B.: Integrin binding revealed. Struct. Biol. 2, 181-183 (1995).
    • (1995) Struct. Biol. , vol.2 , pp. 181-183
    • Graves, J.B.1
  • 13
    • 1842349055 scopus 로고
    • Purification of calmodulin and its peptides
    • M. P. Thompson (ed.): CRS Press, London
    • Haiech, J., J. P. Capony: Purification of calmodulin and its peptides. In: M. P. Thompson (ed.): Calcium Binding Protein. Vol 1. pp 12-18. CRS Press, London 1988.
    • (1988) Calcium Binding Protein , vol.1 , pp. 12-18
    • Haiech, J.1    Capony, J.P.2
  • 14
    • 0000480941 scopus 로고
    • The microprobe assay of chemical elements
    • G. Oter (ed.): Academic Press. New York
    • Hall, T. A.: The microprobe assay of chemical elements. In: G. Oter (ed.): Physical Techniques in Biochemical Research. pp 157-275. Academic Press. New York 1971.
    • (1971) Physical Techniques in Biochemical Research , pp. 157-275
    • Hall, T.A.1
  • 15
    • 0008774363 scopus 로고
    • Le signal calcium dans la cellule: L'enveloppe nucléaire est-elle un réservoir à calcium?
    • Humbert, J. P., P. Köppler, N. Matter, D. Lang, A. N. Malviya: Le signal calcium dans la cellule: l'enveloppe nucléaire est-elle un réservoir à calcium? Medecine/Sciences 11, 1437-1441 (1995).
    • (1995) Medecine/Sciences , vol.11 , pp. 1437-1441
    • Humbert, J.P.1    Köppler, P.2    Matter, N.3    Lang, D.4    Malviya, A.N.5
  • 16
    • 0343987384 scopus 로고
    • Influences of freeze-drying and plastic embedding on electrolyte distribution
    • J. P. Revel, T. Barnard, G. H. Haggis (eds): SEM, AMF O'Hare, IL 60666
    • Ingram, F. D., M. J. Ingram: Influences of freeze-drying and plastic embedding on electrolyte distribution. In: J. P. Revel, T. Barnard, G. H. Haggis (eds): The Science of Biological Specimen preparation. pp 167-174. SEM, AMF O'Hare, IL 60666 1984.
    • (1984) The Science of Biological Specimen Preparation , pp. 167-174
    • Ingram, F.D.1    Ingram, M.J.2
  • 17
    • 8044244444 scopus 로고
    • The C-terminal half molecular domain of calmodulin is responsible for high-affinity interaction with target enzymes
    • Kimura, E., I. Matsuura, K. Tai, K. Nakashima, M. Yazawa: The C-terminal half molecular domain of calmodulin is responsible for high-affinity interaction with target enzymes. Proc. Japan Acad. 71, 293-298 (1995).
    • (1995) Proc. Japan Acad. , vol.71 , pp. 293-298
    • Kimura, E.1    Matsuura, I.2    Tai, K.3    Nakashima, K.4    Yazawa, M.5
  • 18
    • 0025336187 scopus 로고
    • Calcium metabolism in malaria-infected erythrocytes
    • Krishna, S., L. Squire-Pollard: Calcium metabolism in malaria-infected erythrocytes. Parasitol. Today 6, 196-198 (1990).
    • (1990) Parasitol. Today , vol.6 , pp. 196-198
    • Krishna, S.1    Squire-Pollard, L.2
  • 19
    • 0016156102 scopus 로고
    • Cyclic 3′:5′ nuclcotide phosphodiesterase. Purification, characterization, and active form of the protein activator from bovine brain
    • Lin, Y. M., Y. P. Liu, W. Y. Cheung: Cyclic 3′:5′ nuclcotide phosphodiesterase. Purification, characterization, and active form of the protein activator from bovine brain. J. Biol. Chem. 249, 4943-4954 (1974).
    • (1974) J. Biol. Chem. , vol.249 , pp. 4943-4954
    • Lin, Y.M.1    Liu, Y.P.2    Cheung, W.Y.3
  • 20
    • 0016721761 scopus 로고
    • Interactions between Toxoplasma gondii and its host cells: Function in the penetration enhancing factor of Toxoplasma
    • Lycke E., K. Carlberg, R. Norrby: Interactions between Toxoplasma gondii and its host cells: function in the penetration enhancing factor of Toxoplasma. Infect. Immun. 11, 853-861 (1975).
    • (1975) Infect. Immun. , vol.11 , pp. 853-861
    • Lycke, E.1    Carlberg, K.2    Norrby, R.3
  • 21
    • 0023507296 scopus 로고
    • Role of calmodulin in Plasmodium falciparum: Implications for erythrocyte invasion by the merozoite
    • Matsumoto, Y., G. Perry, L. W. Scheibel, M. Aikawa: Role of calmodulin in Plasmodium falciparum: implications for erythrocyte invasion by the merozoite. Eur. J. Cell Biol. 45, 36-43 (1987).
    • (1987) Eur. J. Cell Biol. , vol.45 , pp. 36-43
    • Matsumoto, Y.1    Perry, G.2    Scheibel, L.W.3    Aikawa, M.4
  • 22
    • 0026571564 scopus 로고
    • The role of calcium in the invasion of human erythrocytes by Plasmodium falciparum
    • McCallum-Deghton, N., A. A. Holder: The role of calcium in the invasion of human erythrocytes by Plasmodium falciparum. Mol. Biochem. Parasitol. 50, 317-324 (1992).
    • (1992) Mol. Biochem. Parasitol. , vol.50 , pp. 317-324
    • McCallum-Deghton, N.1    Holder, A.A.2
  • 25
    • 0028470231 scopus 로고
    • Divalent cation and ATP-dependent motility of Toxoplasma gondii tachyzoites after mild treatment with trypsin
    • Mondragon, R., I. Meza, E. Frixione: Divalent cation and ATP-dependent motility of Toxoplasma gondii tachyzoites after mild treatment with trypsin. J. Euk. Microbiol. 41, 330-337 (1994).
    • (1994) J. Euk. Microbiol. , vol.41 , pp. 330-337
    • Mondragon, R.1    Meza, I.2    Frixione, E.3
  • 26
    • 0030095229 scopus 로고    scopus 로고
    • Ca2+-dependence of conoid extrusion in Toxoplasma gondii tachyzoites
    • Mondragon, R., E. Frixione: Ca2+-dependence of conoid extrusion in Toxoplasma gondii tachyzoites. J. Euk. Microbiol. 43, 120-127 (1996).
    • (1996) J. Euk. Microbiol. , vol.43 , pp. 120-127
    • Mondragon, R.1    Frixione, E.2
  • 27
    • 0029671128 scopus 로고    scopus 로고
    • Acidocalcisomes in Toxoplasma gondii tachyzoites
    • Moreno, S. N. J., L. Zhong: Acidocalcisomes in Toxoplasma gondii tachyzoites. Biochem. J. 313, 655-659 (1996).
    • (1996) Biochem. J. , vol.313 , pp. 655-659
    • Moreno, S.N.J.1    Zhong, L.2
  • 28
    • 0029016818 scopus 로고
    • Invasion of Toxoplasma gondii occurs by active penetration of the host cell
    • Morisaki, J. H., J. E. Heuser, L. D. Sibley: Invasion of Toxoplasma gondii occurs by active penetration of the host cell. J. Cell Sci. 108, 2457-2464 (1995).
    • (1995) J. Cell Sci. , vol.108 , pp. 2457-2464
    • Morisaki, J.H.1    Heuser, J.E.2    Sibley, L.D.3
  • 29
    • 0005669426 scopus 로고
    • Calcium transport by resting and stimulated cells
    • F. Bronner (ed.): John Wiley & Sons. New York
    • Muallem, S.: Calcium transport by resting and stimulated cells. In: F. Bronner (ed.): Intracellular Calcium Regulation. pp 349-380. John Wiley & Sons. New York 1990.
    • (1990) Intracellular Calcium Regulation , pp. 349-380
    • Muallem, S.1
  • 30
    • 0020957006 scopus 로고
    • Secretion from the rhoptries of Toxoplasma gondii during host cell invasion
    • Nichols, B. A., M. L. Chiappino, G. R. O'Connor: Secretion from the rhoptries of Toxoplasma gondii during host cell invasion. J. Ultrastruct. Res. 83, 85-98 (1983).
    • (1983) J. Ultrastruct. Res. , vol.83 , pp. 85-98
    • Nichols, B.A.1    Chiappino, M.L.2    O'Connor, G.R.3
  • 31
    • 0024995816 scopus 로고
    • Trypanosoma eruzi: Calcium ion movement during internalization in host HeLa cells
    • Osuna, A., S. Castanys, M. N. Rodriguez-Cabezas, F. Gamarro: Trypanosoma eruzi: calcium ion movement during internalization in host HeLa cells. Int. J. Parasitol. 20, 673-676 (1990).
    • (1990) Int. J. Parasitol. , vol.20 , pp. 673-676
    • Osuna, A.1    Castanys, S.2    Rodriguez-Cabezas, M.N.3    Gamarro, F.4
  • 32
    • 0023932545 scopus 로고
    • Role of the RGD sequence in parasite adhesion to host cells
    • Ouaissi, M. A.: Role of the RGD sequence in parasite adhesion to host cells. Parasitol. Today 4, 169-173 (1988).
    • (1988) Parasitol. Today , vol.4 , pp. 169-173
    • Ouaissi, M.A.1
  • 33
    • 0028790130 scopus 로고
    • Effects of phenothiazine neuroleptic drugs on the microtubular-membrane complex in bloodstream forms of Trypanosoma brucei
    • Page, A. M., J. R. Lagnado: Effects of phenothiazine neuroleptic drugs on the microtubular-membrane complex in bloodstream forms of Trypanosoma brucei. Parasitology 111, 493-504 (1995).
    • (1995) Parasitology , vol.111 , pp. 493-504
    • Page, A.M.1    Lagnado, J.R.2
  • 34
    • 0024390994 scopus 로고
    • Regulation of intracellular calcium in promastigotes of the human protozoan parasite Leishmania donovani
    • Philosoph, H., D. Zilberstein: Regulation of intracellular calcium in promastigotes of the human protozoan parasite Leishmania donovani. J. Biol. Chem. 264, 10420-10424 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 10420-10424
    • Philosoph, H.1    Zilberstein, D.2
  • 35
    • 0027338204 scopus 로고
    • Emptying of intracellular Ca2+ stores releases a novel small messenger that stimulates Ca2+ influx
    • Radriamampita, C., R. Y. Tsien: Emptying of intracellular Ca2+ stores releases a novel small messenger that stimulates Ca2+ influx. Nature 364, 809-814 (1993).
    • (1993) Nature , vol.364 , pp. 809-814
    • Radriamampita, C.1    Tsien, R.Y.2
  • 36
    • 0019774371 scopus 로고
    • Calmodulin is a major component of extruded trichocysts from Paramecium tetaurelia
    • Rauh, J., D. L. Nelson: Calmodulin is a major component of extruded trichocysts from Paramecium tetaurelia. J. Cell Biol. 91, 860-865 (1981).
    • (1981) J. Cell Biol. , vol.91 , pp. 860-865
    • Rauh, J.1    Nelson, D.L.2
  • 37
    • 0025217591 scopus 로고
    • Ca2+-dependent protein phosphorylation in Babesia bovis and its role in growth regulation
    • Ray, A., J. Quade, A. Carson, B. K. Ray: Ca2+-dependent protein phosphorylation in Babesia bovis and its role in growth regulation. J. Parasitol. 76, 153-161 (1990).
    • (1990) J. Parasitol. , vol.76 , pp. 153-161
    • Ray, A.1    Quade, J.2    Carson, A.3    Ray, B.K.4
  • 38
    • 0028989041 scopus 로고
    • Role of Ca2+ and CaM in ehrlichial infection in macrophages
    • Rikihisa, Y., Y. Zhang, J. Park: Role of Ca2+ and CaM in ehrlichial infection in macrophages. Infect. Immun. 63, 2310-2316 (1995).
    • (1995) Infect. Immun. , vol.63 , pp. 2310-2316
    • Rikihisa, Y.1    Zhang, Y.2    Park, J.3
  • 39
    • 0029055039 scopus 로고
    • A trypanosome-soluble factor induces IP3 formation, intracellular Ca2+ mobilization and microfilament rearrangement in host cells
    • Rodriguez, A., M. G. Rioult, A. Ora, N. W. Andrews: A trypanosome-soluble factor induces IP3 formation, intracellular Ca2+ mobilization and microfilament rearrangement in host cells. J. Cell Biol. 129, 1263-1273 (1995).
    • (1995) J. Cell Biol. , vol.129 , pp. 1263-1273
    • Rodriguez, A.1    Rioult, M.G.2    Ora, A.3    Andrews, N.W.4
  • 40
    • 0020959336 scopus 로고
    • African trypanosomes contain CaM which is distinct from host CaM
    • Ruben, L., G. Egwuagu, C. L. Patton: African trypanosomes contain CaM which is distinct from host CaM. Biochim. Biophys. Acta 758, 104-113 (1983).
    • (1983) Biochim. Biophys. Acta , vol.758 , pp. 104-113
    • Ruben, L.1    Egwuagu, G.2    Patton, C.L.3
  • 41
    • 0024556575 scopus 로고
    • The role of phospholipase in host cell penetration by Toxoplasma gondii
    • Saffer, L. D., S. A. Long-Krug, J. D. Schwartzman: The role of phospholipase in host cell penetration by Toxoplasma gondii. Am. J. Trop. Med. Hyg. 40, 145-149 (1989).
    • (1989) Am. J. Trop. Med. Hyg. , vol.40 , pp. 145-149
    • Saffer, L.D.1    Long-Krug, S.A.2    Schwartzman, J.D.3
  • 42
    • 0026720143 scopus 로고
    • Role of calcium/calmodulin-mediaied processes in protozoa
    • Scheibel, L. W.: Role of calcium/calmodulin-mediaied processes in protozoa. Int. Rev. Cytol. 134, 165-242 (1992).
    • (1992) Int. Rev. Cytol. , vol.134 , pp. 165-242
    • Scheibel, L.W.1
  • 43
    • 0023432272 scopus 로고
    • Calcium and calmodulin antagonists inhibit human malaria parasites (Plasmodium falciparum): Implications for drug design
    • Scheibel, L. W., P. M. Colombani, A. D. Hess, M. Aikawa, C. T. Atkinson, W. K. Milhous: Calcium and calmodulin antagonists inhibit human malaria parasites (Plasmodium falciparum): implications for drug design. Proc. Natl. Acad. Sci. USA 84, 7310-7314 (1987).
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7310-7314
    • Scheibel, L.W.1    Colombani, P.M.2    Hess, A.D.3    Aikawa, M.4    Atkinson, C.T.5    Milhous, W.K.6
  • 44
    • 0030071617 scopus 로고    scopus 로고
    • Calmidazolium leads to an increase in the cytosolic Ca2+ concentration in Dictyostelium discoideum by induction of Ca2+ release from intracellular stores and influx of extracellular Ca2+
    • Schlatterer, C., R. Schaloske: Calmidazolium leads to an increase in the cytosolic Ca2+ concentration in Dictyostelium discoideum by induction of Ca2+ release from intracellular stores and influx of extracellular Ca2+. Biochem. J. 313, 661-667 (1996).
    • (1996) Biochem. J. , vol.313 , pp. 661-667
    • Schlatterer, C.1    Schaloske, R.2
  • 45
    • 0020993328 scopus 로고
    • Calcium/calmodulin-regulated guanylate cyclase and calcium-permeability in the ciliary membrane from Tetrahymena
    • Schultz, J. E., U. Schönefeld, S. Klumpp: Calcium/calmodulin-regulated guanylate cyclase and calcium-permeability in the ciliary membrane from Tetrahymena. Eur. J. Biochem. 137, 89-94 (1983).
    • (1983) Eur. J. Biochem. , vol.137 , pp. 89-94
    • Schultz, J.E.1    Schönefeld, U.2    Klumpp, S.3
  • 46
    • 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. 51, 760-764 (1986).
    • (1986) Infect. Immun. , vol.51 , pp. 760-764
    • Schwartzman, J.D.1
  • 47
    • 0028979389 scopus 로고
    • C2+ storage in Trypanosoma brucei: The influence of cytoplasmic pH and importance of vacuolar acidity
    • Scott, D. A., S. N. J. Moreno, R. Docampo: C2+ storage in Trypanosoma brucei: the influence of cytoplasmic pH and importance of vacuolar acidity. Biochem. J. 310, 789-794 (1995).
    • (1995) Biochem. J. , vol.310 , pp. 789-794
    • Scott, D.A.1    Moreno, S.N.J.2    Docampo, R.3
  • 48
    • 0028990986 scopus 로고
    • Mobilization of intrasporozoite Ca2+ is essential for Theileria parva sporozoite invasion of bovine lymphocytes
    • Shaw, M. K.: Mobilization of intrasporozoite Ca2+ is essential for Theileria parva sporozoite invasion of bovine lymphocytes. Eur. J. Cell Biol. 68, 78-87 (1995).
    • (1995) Eur. J. Cell Biol. , vol.68 , pp. 78-87
    • Shaw, M.K.1
  • 49
    • 0028986627 scopus 로고
    • Invasion of vertebrate cells by Toxoplasma gondii
    • Sibley, L. D.: Invasion of vertebrate cells by Toxoplasma gondii. Trends Cell Biol. 5, 129-137 (1995).
    • (1995) Trends Cell Biol. , vol.5 , pp. 129-137
    • Sibley, L.D.1
  • 50
    • 0023900654 scopus 로고
    • Two trifluoperazine-binding sites on calmodulin predicted from comparative molecular modeling with troponin-C
    • Strynadka, N. J. C., M. N. J. James: Two trifluoperazine-binding sites on calmodulin predicted from comparative molecular modeling with troponin-C. Proteins Struct. Funct. Genet. 3, 1-17 (1988).
    • (1988) Proteins Struct. Funct. Genet. , vol.3 , pp. 1-17
    • Strynadka, N.J.C.1    James, M.N.J.2
  • 51
    • 0018677364 scopus 로고
    • Isolation and electrophoretic properties of a calcium-binding protein from the ciliate Tetrahymena pyriformis
    • Suzuki, Y., J. Hirabyashi, Y. Watanabe: Isolation and electrophoretic properties of a calcium-binding protein from the ciliate Tetrahymena pyriformis. Biochem. Biophys. Res. Commun. 90, 253-260 (1979).
    • (1979) Biochem. Biophys. Res. Commun. , vol.90 , pp. 253-260
    • Suzuki, Y.1    Hirabyashi, J.2    Watanabe, Y.3
  • 52
    • 0020560725 scopus 로고
    • Calmodulin antagonists' binding sites on calmodulin
    • Tanaka, T., T. Ohmura, H. Hidaka: Calmodulin antagonists' binding sites on calmodulin. Pharmacology 26, 249-257 (1983).
    • (1983) Pharmacology , vol.26 , pp. 249-257
    • Tanaka, T.1    Ohmura, T.2    Hidaka, H.3
  • 53
    • 0027980104 scopus 로고
    • Role in host cell invasion of Trypanosoma cruzi induced cytosolic free Ca2+ transients
    • Tardieux, I., M. H. Nathanson, W. Andrews. Role in host cell invasion of Trypanosoma cruzi induced cytosolic free Ca2+ transients. J. Exp. Med. 179, 1017-1022 (1994).
    • (1994) J. Exp. Med. , vol.179 , pp. 1017-1022
    • Tardieux, I.1    Nathanson, M.H.2    Andrews, W.3
  • 55
    • 0015821547 scopus 로고
    • Mechanism of activation of a cyclic adenosine 3′:5′-monophosphate phosphodiesterase from bovine heart by calcium ions
    • Teo, T. S., J. H. Wang: Mechanism of activation of a cyclic adenosine 3′:5′-monophosphate phosphodiesterase from bovine heart by calcium ions. J. Biol. Chem. 248, 5950-5955 (1973).
    • (1973) J. Biol. Chem. , vol.248 , pp. 5950-5955
    • Teo, T.S.1    Wang, J.H.2
  • 56
    • 0025739736 scopus 로고
    • Regulation of intracellular calcium homeostasis in Trypanosoma cruzi. Effects of calmidazolium and trifluoperazine
    • Vercesi, A. E., M. E. Hoffman, C. F. Bernades, R. Docampo: Regulation of intracellular calcium homeostasis in Trypanosoma cruzi. Effects of calmidazolium and trifluoperazine. Cell Calcium 12, 361-369 (1991).
    • (1991) Cell Calcium , vol.12 , pp. 361-369
    • Vercesi, A.E.1    Hoffman, M.E.2    Bernades, C.F.3    Docampo, R.4
  • 57
    • 0028360642 scopus 로고
    • Quantitative X-ray microanalysis of P, Ca and S in the mucus secretory granules of cryofixed frog palate epithelium
    • Wagner, D., E. Puchelle, J. Hinrasky, P. Girard, G. Balossier: Quantitative X-ray microanalysis of P, Ca and S in the mucus secretory granules of cryofixed frog palate epithelium. Microsc. Res. Tech. 28, 141-148 (1994).
    • (1994) Microsc. Res. Tech. , vol.28 , pp. 141-148
    • Wagner, D.1    Puchelle, E.2    Hinrasky, J.3    Girard, P.4    Balossier, G.5
  • 58
    • 0022088385 scopus 로고
    • How does Toxoplasma gondii enter host cell?
    • Werck, R.: How does Toxoplasma gondii enter host cell? Rev. Infect. Dis. 7, 449-457 (1985).
    • (1985) Rev. Infect. Dis. , vol.7 , pp. 449-457
    • Werck, R.1
  • 59
    • 0027672187 scopus 로고
    • Cell culture supports for slam-frozen and molecular distillation dried procedures
    • White, S. L., D. A. Laska, P. S. Foxworthy, J. L. Gimble, D. M. Hoover: Cell culture supports for slam-frozen and molecular distillation dried procedures. Microsc. Res. Tech. 26, 184-185 (1993).
    • (1993) Microsc. Res. Tech. , vol.26 , pp. 184-185
    • White, S.L.1    Laska, D.A.2    Foxworthy, P.S.3    Gimble, J.L.4    Hoover, D.M.5
  • 60
    • 0025923669 scopus 로고
    • Ca2+/calmodulin-binding proteins in Dictyostelium discoideum
    • Winckler, T., H. Dammann, R. Mutzel: Ca2+/calmodulin-binding proteins in Dictyostelium discoideum. Res. Microbiol. 142, 509-519 (1991).
    • (1991) Res. Microbiol. , vol.142 , pp. 509-519
    • Winckler, T.1    Dammann, H.2    Mutzel, R.3
  • 61
    • 0028170370 scopus 로고
    • Changes in Trypanosoma cruzi infectivity by treatments that affect calcium ion levels
    • Yakubu, M. A., S. Majeinder, F. Kierszenbaum: Changes in Trypanosoma cruzi infectivity by treatments that affect calcium ion levels. Mol. Biochem. Parasitol. 66, 119-125 (1994).
    • (1994) Mol. Biochem. Parasitol. , vol.66 , pp. 119-125
    • Yakubu, M.A.1    Majeinder, S.2    Kierszenbaum, F.3
  • 62
    • 0026083256 scopus 로고
    • Cryofixation methods for ion localization in cells by electron probe microanalysis: A review
    • Oxf.
    • Zierold, K.: Cryofixation methods for ion localization in cells by electron probe microanalysis: a review. J. Microsc. (Oxf.) 161, 357-366 (1991).
    • (1991) J. Microsc. , vol.161 , pp. 357-366
    • Zierold, K.1
  • 63
    • 0005639191 scopus 로고
    • Rapid freezing techniques for biological electron probe microanalysis
    • D. C. Siege, A. J. Morgan, A. T. Summer, A. Warley (eds.): Cambridge University Press. Cambridge
    • Zierold, K.: Rapid freezing techniques for biological electron probe microanalysis. In: D. C. Siege, A. J. Morgan, A. T. Summer, A. Warley (eds.): X-ray Microanalysis in Biology: experimental techniques and applications. pp 101-116. Cambridge University Press. Cambridge 1993.
    • (1993) X-ray Microanalysis in Biology: Experimental Techniques and Applications
    • Zierold, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.