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Volumn 61, Issue 1, 2014, Pages 95-114

Calcium regulation in the protozoan model, paramecium tetraurelia

Author keywords

Ca2+; ciliate; protozoa; signal transduction; signaling

Indexed keywords

CALCIUM; CILIATE; EVOLUTION; MEMBRANE; PLASMA; PROTEIN; PROTOZOAN; SENSOR; SIGNAL; SIGNALING; TRAFFICKING;

EID: 84893677652     PISSN: 10665234     EISSN: 15507408     Source Type: Journal    
DOI: 10.1111/jeu.12070     Document Type: Review
Times cited : (34)

References (167)
  • 1
    • 0028897650 scopus 로고
    • Protein substrates for cGMP-dependent protein phosphorylation in cilia of wild type and atalanta mutants of Paramecium
    • Ann, K. S., &, Nelson, D. L., 1995. Protein substrates for cGMP-dependent protein phosphorylation in cilia of wild type and atalanta mutants of Paramecium. Cell Motil. Cytoskeleton, 30: 252-260.
    • (1995) Cell Motil. Cytoskeleton , vol.30 , pp. 252-260
    • Ann, K.S.1    Nelson, D.L.2
  • 2
    • 78651325661 scopus 로고    scopus 로고
    • ParameciumDB in 2011: New tools and new data for functional and comparative genomics of the model ciliate Paramecium tetraurelia
    • Arnaiz, O., &, Sperling, L., 2011. ParameciumDB in 2011: new tools and new data for functional and comparative genomics of the model ciliate Paramecium tetraurelia. Nucleic Acid Res., 39: D632-D636.
    • (2011) Nucleic Acid Res. , vol.39
    • Arnaiz, O.1    Sperling, L.2
  • 3
    • 0043210732 scopus 로고    scopus 로고
    • Calcium regulates exocytosis at the level of single vesicles
    • Becherer, U., Moser, T., Stuhmer, W., &, Oheim, M., 2003. Calcium regulates exocytosis at the level of single vesicles. Nat. Neurosci., 6: 846-853.
    • (2003) Nat. Neurosci. , vol.6 , pp. 846-853
    • Becherer, U.1    Moser, T.2    Stuhmer, W.3    Oheim, M.4
  • 4
    • 84865783058 scopus 로고    scopus 로고
    • Regulated exocytosis in chromaffin cells and cytotoxic T lymphocytes: How similar are they?
    • Becherer, U., Medart, M. R., Schirra, C., Krause, E., Stevens, D., &, Rettig, J., 2012. Regulated exocytosis in chromaffin cells and cytotoxic T lymphocytes: how similar are they? Cell Calcium, 52: 303-312.
    • (2012) Cell Calcium , vol.52 , pp. 303-312
    • Becherer, U.1    Medart, M.R.2    Schirra, C.3    Krause, E.4    Stevens, D.5    Rettig, J.6
  • 5
    • 0035544331 scopus 로고    scopus 로고
    • Basal body-associated nucleation center for the centrin-based cortical cytoskeletal network in Paramecium
    • Beisson, J., Clerot, J. C., Fleury-Aubusson, A., Garreau de Loubresse, N., Ruiz, F., &, Klotz, C., 2001. Basal body-associated nucleation center for the centrin-based cortical cytoskeletal network in Paramecium. Protist, 152: 339-354.
    • (2001) Protist , vol.152 , pp. 339-354
    • Beisson, J.1    Clerot, J.C.2    Fleury-Aubusson, A.3    Garreau De Loubresse, N.4    Ruiz, F.5    Klotz, C.6
  • 6
    • 72049131815 scopus 로고    scopus 로고
    • A kinome of 2600 in the ciliate Paramecium tetraurelia
    • Bemm, F., Schwarz, R., Forster, F., &, Schultz, J., 2009. A kinome of 2600 in the ciliate Paramecium tetraurelia. FEBS Lett., 583: 3589-3592.
    • (2009) FEBS Lett. , vol.583 , pp. 3589-3592
    • Bemm, F.1    Schwarz, R.2    Forster, F.3    Schultz, J.4
  • 9
    • 84861219896 scopus 로고    scopus 로고
    • Evolutionary diversity of the mitochondrial calcium uniporter
    • Bick, A., Calvo, S. E., &, Mootha, V. K., 2012. Evolutionary diversity of the mitochondrial calcium uniporter. Science, 336: 886.
    • (2012) Science , vol.336 , pp. 886
    • Bick, A.1    Calvo, S.E.2    Mootha, V.K.3
  • 10
    • 0019491884 scopus 로고
    • 2+-mediated event during the final steps of exocytosis in Paramecium cells
    • 2+-mediated event during the final steps of exocytosis in Paramecium cells. J. Cell Biol., 88: 179-188.
    • (1981) J. Cell Biol. , vol.88 , pp. 179-188
    • Bilinski, M.1    Plattner, H.2    Matt, H.3
  • 11
    • 77955108279 scopus 로고    scopus 로고
    • Molecular architecture of the inositol 1,4,5-trisphosphate receptor pore
    • Boehning, D. F., 2010. Molecular architecture of the inositol 1,4,5-trisphosphate receptor pore. Curr. Top. Membr., 66C: 191-207.
    • (2010) Curr. Top. Membr. , vol.66 C , pp. 191-207
    • Boehning, D.F.1
  • 13
    • 0018270088 scopus 로고
    • Calcium entry leads to inactivation of calcium channel in Paramecium
    • Brehm, P., &, Eckert, R., 1978. Calcium entry leads to inactivation of calcium channel in Paramecium. Science, 202: 1203-1206.
    • (1978) Science , vol.202 , pp. 1203-1206
    • Brehm, P.1    Eckert, R.2
  • 17
    • 61849128446 scopus 로고    scopus 로고
    • Evolutionary origin of the purinergic signalling system
    • Burnstock, G., &, Verkhratsky, A., 2009. Evolutionary origin of the purinergic signalling system. Acta Physiol. (Oxf.), 195: 415-447.
    • (2009) Acta Physiol. (Oxf.) , vol.195 , pp. 415-447
    • Burnstock, G.1    Verkhratsky, A.2
  • 19
    • 45849109876 scopus 로고    scopus 로고
    • 2+ signaling "toolkit" at the origin of metazoa
    • 2+ signaling "toolkit" at the origin of metazoa. Mol. Biol. Evol., 25: 1357-1361.
    • (2008) Mol. Biol. Evol. , vol.25 , pp. 1357-1361
    • Cai, X.1
  • 21
    • 0036472494 scopus 로고    scopus 로고
    • PH-dependent regulation of lysosomal calcium in macrophages
    • Christensen, K. A., Myers, J. T., &, Swanson, J. A., 2002. pH-dependent regulation of lysosomal calcium in macrophages. J. Cell Sci., 115: 599-607.
    • (2002) J. Cell Sci. , vol.115 , pp. 599-607
    • Christensen, K.A.1    Myers, J.T.2    Swanson, J.A.3
  • 22
    • 84879020614 scopus 로고    scopus 로고
    • The N-terminal region of two-pore channel 1 regulates trafficking and activation by NAADP
    • Churamani, D., Hooper, R., Rahman, T., Brailoiu, E., &, Patel, S., 2013. The N-terminal region of two-pore channel 1 regulates trafficking and activation by NAADP. Biochem. J., 453: 147-151.
    • (2013) Biochem. J. , vol.453 , pp. 147-151
    • Churamani, D.1    Hooper, R.2    Rahman, T.3    Brailoiu, E.4    Patel, S.5
  • 23
    • 37149029370 scopus 로고    scopus 로고
    • Calcium signaling
    • Clapham, D. E., 2007. Calcium signaling. Cell, 131: 1047-1058.
    • (2007) Cell , vol.131 , pp. 1047-1058
    • Clapham, D.E.1
  • 24
    • 0027151959 scopus 로고
    • External GTP alters the motility and elicits an oscillating membrane depolarization in Paramecium tetraurelia
    • Clark, K. D., Hennessey, T. M., &, Nelson, D. L., 1993. External GTP alters the motility and elicits an oscillating membrane depolarization in Paramecium tetraurelia. Proc. Natl Acad. Sci. U S A, 90: 3782-3786.
    • (1993) Proc. Natl Acad. Sci. U S A , vol.90 , pp. 3782-3786
    • Clark, K.D.1    Hennessey, T.M.2    Nelson, D.L.3
  • 26
    • 0015402237 scopus 로고
    • Qualitative and quantitative electron probe analysis of cytoplasmic granules in Tetrahymena pyriformis
    • Coleman, J. R., Nilsson, J. R., Warner, R. R., &, Batt, P., 1972. Qualitative and quantitative electron probe analysis of cytoplasmic granules in Tetrahymena pyriformis. Exp. Cell Res., 74: 207-219.
    • (1972) Exp. Cell Res. , vol.74 , pp. 207-219
    • Coleman, J.R.1    Nilsson, J.R.2    Warner, R.R.3    Batt, P.4
  • 27
    • 38149012305 scopus 로고    scopus 로고
    • Counting functional inositol 1,4,5-trisphosphate receptors into the plasma membrane
    • Dellis, O., Rossi, A. M., Dedos, S. G., &, Taylor, C. W., 2008. Counting functional inositol 1,4,5-trisphosphate receptors into the plasma membrane. J. Biol. Chem., 283: 751-755.
    • (2008) J. Biol. Chem. , vol.283 , pp. 751-755
    • Dellis, O.1    Rossi, A.M.2    Dedos, S.G.3    Taylor, C.W.4
  • 29
    • 7444237566 scopus 로고    scopus 로고
    • The timing of eukaryotic evolution: Does a relaxed molecular clock reconcile proteins and fossils?
    • Douzery, E. J., Snell, E. A., Bapteste, E., Delsuc, F., &, Philippe, H., 2004. The timing of eukaryotic evolution: does a relaxed molecular clock reconcile proteins and fossils? Proc. Natl Acad. Sci. U S A, 101: 15386-15391.
    • (2004) Proc. Natl Acad. Sci. U S A , vol.101 , pp. 15386-15391
    • Douzery, E.J.1    Snell, E.A.2    Bapteste, E.3    Delsuc, F.4    Philippe, H.5
  • 30
    • 0018400806 scopus 로고
    • Ionic mechanisms of excitation in Paramecium
    • Eckert, R., &, Brehm, P., 1979. Ionic mechanisms of excitation in Paramecium. Annu. Rev. Biophys. Bioeng., 8: 353-383.
    • (1979) Annu. Rev. Biophys. Bioeng. , vol.8 , pp. 353-383
    • Eckert, R.1    Brehm, P.2
  • 31
    • 55449130503 scopus 로고    scopus 로고
    • Elucidation of clathrin-mediated endocytosis in Tetrahymena reveals an evolutionarily convergent recruitment of dynamin
    • Elde, N. C., Morgan, G., Winey, M., Sperling, L., &, Turkewitz, A. P., 2005. Elucidation of clathrin-mediated endocytosis in Tetrahymena reveals an evolutionarily convergent recruitment of dynamin. PLoS Genet., 1: e52.
    • (2005) PLoS Genet. , vol.1
    • Elde, N.C.1    Morgan, G.2    Winey, M.3    Sperling, L.4    Turkewitz, A.P.5
  • 32
    • 0028171932 scopus 로고
    • 2+ release from subplasmalemmal stores as a primary event during exocytosis in Paramecium cells
    • 2+ release from subplasmalemmal stores as a primary event during exocytosis in Paramecium cells. J. Cell Biol., 127: 935-945.
    • (1994) J. Cell Biol. , vol.127 , pp. 935-945
    • Erxleben, C.1    Plattner, H.2
  • 34
    • 0024970150 scopus 로고
    • 2+-inhibitable calmodulin-binding proteins
    • 2+- inhibitable calmodulin-binding proteins. Biochem. J., 259: 385-396.
    • (1989) Biochem. J. , vol.259 , pp. 385-396
    • Evans, T.C.1    Nelson, D.L.2
  • 35
    • 33644764062 scopus 로고    scopus 로고
    • A Toxoplasma gondii phosphoinositide phospholipase C (TgPI-PLC) with high affinity for phosphatidylinositol
    • Fang, J., Marchesini, N., &, Moreno, S. N. J., 2006. A Toxoplasma gondii phosphoinositide phospholipase C (TgPI-PLC) with high affinity for phosphatidylinositol. Biochem. J., 394: 417-425.
    • (2006) Biochem. J. , vol.394 , pp. 417-425
    • Fang, J.1    Marchesini, N.2    Moreno, S.N.J.3
  • 36
    • 0029092699 scopus 로고
    • The pegs on the decorated tubules of the contractile vacuole complex of Paramecium are proton pumps
    • Fok, A. K., Aihara, M. S., Ishida, M., Nolta, K. V., Steck, T. L., &, Allen, R. D., 1995. The pegs on the decorated tubules of the contractile vacuole complex of Paramecium are proton pumps. J. Cell Sci., 108: 3163-3170.
    • (1995) J. Cell Sci. , vol.108 , pp. 3163-3170
    • Fok, A.K.1    Aihara, M.S.2    Ishida, M.3    Nolta, K.V.4    Steck, T.L.5    Allen, R.D.6
  • 37
    • 77956837629 scopus 로고    scopus 로고
    • Protein phosphatase 2B (PP2B, calcineurin) in Paramecium: Partial characterization reveals that two members of the unusually large catalytic subunit family have distinct roles in calcium-dependent processes
    • Fraga, D., Sehring, I. M., Kissmehl, R., Reiss, M., Gaines, R., Hinrichsen, R., &, Plattner, H., 2010. Protein phosphatase 2B (PP2B, calcineurin) in Paramecium: partial characterization reveals that two members of the unusually large catalytic subunit family have distinct roles in calcium-dependent processes. Eukaryot. Cell, 9: 1049-1063.
    • (2010) Eukaryot. Cell , vol.9 , pp. 1049-1063
    • Fraga, D.1    Sehring, I.M.2    Kissmehl, R.3    Reiss, M.4    Gaines, R.5    Hinrichsen, R.6    Plattner, H.7
  • 41
    • 0030843754 scopus 로고    scopus 로고
    • The occurrence of biogenic calcian struvite, (Mg, Ca)NH4PO4.6H2O, as intracellular crystals in Paramecium
    • Grover, J. E., Rope, A. F., &, Kaneshiro, E. S., 1997. The occurrence of biogenic calcian struvite, (Mg, Ca)NH4PO4.6H2O, as intracellular crystals in Paramecium. J. Eukaryot. Microbiol., 44: 366-373.
    • (1997) J. Eukaryot. Microbiol. , vol.44 , pp. 366-373
    • Grover, J.E.1    Rope, A.F.2    Kaneshiro, E.S.3
  • 42
    • 0030886205 scopus 로고    scopus 로고
    • Analysis of exocytosis mutants indicates close coupling between regulated secretion and transcription activation in Tetrahymena
    • Haddad, A., &, Turkewitz, A. P., 1997. Analysis of exocytosis mutants indicates close coupling between regulated secretion and transcription activation in Tetrahymena. Proc. Natl Acad. Sci. U S A, 94: 10675-10680.
    • (1997) Proc. Natl Acad. Sci. U S A , vol.94 , pp. 10675-10680
    • Haddad, A.1    Turkewitz, A.P.2
  • 43
    • 78049244488 scopus 로고    scopus 로고
    • Calcium signalling: Fishing out molecules of mitochondrial calcium transport
    • Hajnõczky, G., &, Csordás, G., 2010. Calcium signalling: fishing out molecules of mitochondrial calcium transport. Curr. Biol., 20: R888-R891.
    • (2010) Curr. Biol. , vol.20
    • Hajnõczky, G.1    Csordás, G.2
  • 44
    • 0033572328 scopus 로고    scopus 로고
    • Quantitative energy-dispersive X-ray microanalysis of calcium dynamics in cell suspensions during stimulation on a subsecond time scale: Preparative and analytical aspects as exemplified with Paramecium cells
    • Hardt, M., &, Plattner, H., 1999. Quantitative energy-dispersive X-ray microanalysis of calcium dynamics in cell suspensions during stimulation on a subsecond time scale: preparative and analytical aspects as exemplified with Paramecium cells. J. Struct. Biol., 128: 187-199.
    • (1999) J. Struct. Biol. , vol.128 , pp. 187-199
    • Hardt, M.1    Plattner, H.2
  • 45
    • 0033807767 scopus 로고    scopus 로고
    • 2+ influx during synchronous exocytosis in Paramecium cells
    • 2+ influx during synchronous exocytosis in Paramecium cells. Eur. J. Cell Biol., 79: 642-652.
    • (2000) Eur. J. Cell Biol. , vol.79 , pp. 642-652
    • Hardt, M.1    Plattner, H.2
  • 46
    • 84989617462 scopus 로고
    • Defensive function of trichocysts in Paramecium
    • Harumoto, T., &, Miyake, A., 1991. Defensive function of trichocysts in Paramecium. J. Exp. Zool., 260: 84-92.
    • (1991) J. Exp. Zool. , vol.260 , pp. 84-92
    • Harumoto, T.1    Miyake, A.2
  • 47
    • 0030908946 scopus 로고    scopus 로고
    • Identification of isoforms of the exocytosis-sensitive phosphoprotein PP63/parafusin in Paramecium tetraurelia and demonstration of phosphoglucomutase activity
    • Hauser, K., Kissmehl, R., Linder, J., Schultz, J. E., Lottspeich, F., &, Plattner, H., 1997. Identification of isoforms of the exocytosis-sensitive phosphoprotein PP63/parafusin in Paramecium tetraurelia and demonstration of phosphoglucomutase activity. Biochem. J., 323: 289-296.
    • (1997) Biochem. J. , vol.323 , pp. 289-296
    • Hauser, K.1    Kissmehl, R.2    Linder, J.3    Schultz, J.E.4    Lottspeich, F.5    Plattner, H.6
  • 48
    • 0032528902 scopus 로고    scopus 로고
    • 2+-ATPase gene from Paramecium tetraurelia and localization of its gene product to sub-plasmalemmal calcium stores
    • 2+-ATPase gene from Paramecium tetraurelia and localization of its gene product to sub-plasmalemmal calcium stores. Biochem. J., 334: 31-38.
    • (1998) Biochem. J. , vol.334 , pp. 31-38
    • Hauser, K.1    Pavlovic, N.2    Kissmehl, R.3    Plattner, H.4
  • 49
    • 0033852724 scopus 로고    scopus 로고
    • 2+-ATPase overexpression in Paramecium cells: Isoforms, subcellular localization, biogenesis of cortical calcium stores and functional aspects
    • 2+-ATPase overexpression in Paramecium cells: isoforms, subcellular localization, biogenesis of cortical calcium stores and functional aspects. Mol. Microbiol., 37: 773-787.
    • (2000) Mol. Microbiol. , vol.37 , pp. 773-787
    • Hauser, K.1    Pavlovic, N.2    Klauke, N.3    Geissinger, D.4    Plattner, H.5
  • 50
    • 2942568227 scopus 로고    scopus 로고
    • A molecular timescale of eukaryote evolution and the rise of complex multicellular life
    • Hedges, S. B., Blair, J. E., Venturi, M. L., &, Shoe, J. L., 2004. A molecular timescale of eukaryote evolution and the rise of complex multicellular life. BMC Evol. Biol., 4: 2.
    • (2004) BMC Evol. Biol. , vol.4 , pp. 2
    • Hedges, S.B.1    Blair, J.E.2    Venturi, M.L.3    Shoe, J.L.4
  • 51
    • 0026646436 scopus 로고
    • A cortical phosphoprotein ('PP63') sensitive to exocytosis triggering in Paramecium cells. Immunolocalization and quenched-flow correlation of time course of dephosphorylation with membrane fusion
    • Höhne-Zell, B., Knoll, G., Riedel-Gras, U., Hofer, W., &, Plattner, H., 1992. A cortical phosphoprotein ('PP63') sensitive to exocytosis triggering in Paramecium cells. Immunolocalization and quenched-flow correlation of time course of dephosphorylation with membrane fusion. Biochem. J., 286: 843-849.
    • (1992) Biochem. J. , vol.286 , pp. 843-849
    • Höhne-Zell, B.1    Knoll, G.2    Riedel-Gras, U.3    Hofer, W.4    Plattner, H.5
  • 52
    • 9244224718 scopus 로고    scopus 로고
    • One-way calcium spill-over during signal transduction in Paramecium cells: From the cell cortex into cilia, but not in the reverse direction
    • Husser, M. R., Hardt, M., Blanchard, M.-P., Hentschel, J., Klauke, N., &, Plattner, H., 2004. One-way calcium spill-over during signal transduction in Paramecium cells: from the cell cortex into cilia, but not in the reverse direction. Cell Calcium, 36: 349-358.
    • (2004) Cell Calcium , vol.36 , pp. 349-358
    • Husser, M.R.1    Hardt, M.2    Blanchard, M.-P.3    Hentschel, J.4    Klauke, N.5    Plattner, H.6
  • 53
    • 0028131997 scopus 로고
    • Spatiotemporal distribution of protein kinase and phosphatase activities
    • Inagaki, N., Ito, M., Nakano, T., &, Inagaki, M., 1994. Spatiotemporal distribution of protein kinase and phosphatase activities. Trends Biochem. Sci., 19: 448-452.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 448-452
    • Inagaki, N.1    Ito, M.2    Nakano, T.3    Inagaki, M.4
  • 54
    • 0025365264 scopus 로고
    • Cytosolic free calcium elevation mediates the phagosome-lysosome fusion during phagocytosis in human neutrophils
    • Jaconi, M. E., Lew, D. P., Carpentier, J. L., Magnusson, K. E., Sjögren, M., &, Stendahl, O., 1990. Cytosolic free calcium elevation mediates the phagosome-lysosome fusion during phagocytosis in human neutrophils. J. Cell Biol., 110: 1555-1564.
    • (1990) J. Cell Biol. , vol.110 , pp. 1555-1564
    • Jaconi, M.E.1    Lew, D.P.2    Carpentier, J.L.3    Magnusson, K.E.4    Sjögren, M.5    Stendahl, O.6
  • 57
    • 0025580331 scopus 로고
    • 2+ influx associated with exocytosis is specifically abolished in a Paramecium exocytotic mutant
    • 2+ influx associated with exocytosis is specifically abolished in a Paramecium exocytotic mutant. J. Cell Biol., 111: 2527-2535.
    • (1990) J. Cell Biol. , vol.111 , pp. 2527-2535
    • Kerboeuf, D.1    Cohen, J.2
  • 58
    • 0027184405 scopus 로고
    • Calmodulin is essential for assembling links necessary for exocytotic membrane fusion in Paramecium
    • Kerboeuf, D., Le Berre, A., Dedieu, J. C., &, Cohen, J., 1993. Calmodulin is essential for assembling links necessary for exocytotic membrane fusion in Paramecium. EMBO J., 12: 3385-3390.
    • (1993) EMBO J. , vol.12 , pp. 3385-3390
    • Kerboeuf, D.1    Le Berre, A.2    Dedieu, J.C.3    Cohen, J.4
  • 60
    • 0029891406 scopus 로고    scopus 로고
    • Protein phosphatase and kinase activities possibly involved in exocytosis regulation in Paramecium tetraurelia
    • Kissmehl, R., Treptau, T., Hofer, H. W., &, Plattner, H., 1996. Protein phosphatase and kinase activities possibly involved in exocytosis regulation in Paramecium tetraurelia. Biochem. J., 317: 65-76.
    • (1996) Biochem. J. , vol.317 , pp. 65-76
    • Kissmehl, R.1    Treptau, T.2    Hofer, H.W.3    Plattner, H.4
  • 61
    • 0031041882 scopus 로고    scopus 로고
    • A novel, calcium-inhibitable casein kinase in Paramecium cells
    • Kissmehl, R., Treptau, T., Hauser, K., &, Plattner, H., 1997a. A novel, calcium-inhibitable casein kinase in Paramecium cells. FEBS Lett., 402: 227-235.
    • (1997) FEBS Lett. , vol.402 , pp. 227-235
    • Kissmehl, R.1    Treptau, T.2    Hauser, K.3    Plattner, H.4
  • 62
    • 0031571648 scopus 로고    scopus 로고
    • Occurrence of a para-nitrophenyl phosphate-phosphatase with calcineurin-like characteristics in Paramecium tetraurelia
    • Kissmehl, R., Treptau, T., Kottwitz, B., &, Plattner, H., 1997b. Occurrence of a para-nitrophenyl phosphate-phosphatase with calcineurin-like characteristics in Paramecium tetraurelia. Arch. Biochem. Biophys., 344: 260-270.
    • (1997) Arch. Biochem. Biophys. , vol.344 , pp. 260-270
    • Kissmehl, R.1    Treptau, T.2    Kottwitz, B.3    Plattner, H.4
  • 64
    • 0030926842 scopus 로고    scopus 로고
    • 2+ transients induced in Paramecium cells by a polyamine secretagogue
    • 2+ transients induced in Paramecium cells by a polyamine secretagogue. J. Cell Sci., 110: 975-983.
    • (1997) J. Cell Sci. , vol.110 , pp. 975-983
    • Klauke, N.1    Plattner, H.2
  • 65
    • 0031594556 scopus 로고    scopus 로고
    • 2+ imaging and quenched-flow/freeze-fracture analysis
    • 2+ imaging and quenched-flow/freeze-fracture analysis. J. Membr. Biol., 161: 65-81.
    • (1998) J. Membr. Biol. , vol.161 , pp. 65-81
    • Klauke, N.1    Plattner, H.2
  • 66
    • 0031832342 scopus 로고    scopus 로고
    • An exocytotic mutant of Paramecium caudatum: Membrane fusion without secretory contents release
    • Klauke, N., Kissmehl, R., Plattner, H., Haga, N., &, Watanabe, T., 1998. An exocytotic mutant of Paramecium caudatum: membrane fusion without secretory contents release. Cell Calcium, 23: 349-360.
    • (1998) Cell Calcium , vol.23 , pp. 349-360
    • Klauke, N.1    Kissmehl, R.2    Plattner, H.3    Haga, N.4    Watanabe, T.5
  • 68
    • 0032577483 scopus 로고    scopus 로고
    • Regulation of the calmodulin-stimulated protein phosphatase, calcineurin
    • Klee, C. B., Ren, H., &, Wang, X., 1998. Regulation of the calmodulin-stimulated protein phosphatase, calcineurin. J. Biol. Chem., 273: 13367-13370.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13367-13370
    • Klee, C.B.1    Ren, H.2    Wang, X.3
  • 69
    • 68549115188 scopus 로고    scopus 로고
    • Two isoforms of eukaryotic phospholipase C in Paramecium affecting transport and release of GPI-anchored proteins in vivo
    • Klöppel, C., Müller, A., Marker, S., &, Simon, M., 2009. Two isoforms of eukaryotic phospholipase C in Paramecium affecting transport and release of GPI-anchored proteins in vivo. Eur. J. Cell Biol., 88: 577-592.
    • (2009) Eur. J. Cell Biol. , vol.88 , pp. 577-592
    • Klöppel, C.1    Müller, A.2    Marker, S.3    Simon, M.4
  • 70
    • 0021112651 scopus 로고
    • 3+: Calmodulin specificity and properties of the reconstituted guanylate cyclase
    • 3+: calmodulin specificity and properties of the reconstituted guanylate cyclase. J. Biol. Chem., 258: 12455-12459.
    • (1983) J. Biol. Chem. , vol.258 , pp. 12455-12459
    • Klumpp, S.1    Kleefeld, G.2    Schultz, J.E.3
  • 71
    • 0025827296 scopus 로고
    • Quenched flow analysis of exocytosis in Paramecium cells: Time course, changes in membrane structure, and calcium requirements revealed after rapid mixing and rapid freezing of intact cells
    • Knoll, G., Braun, C., &, Plattner, H., 1991a. Quenched flow analysis of exocytosis in Paramecium cells: time course, changes in membrane structure, and calcium requirements revealed after rapid mixing and rapid freezing of intact cells. J. Cell Biol., 113: 1295-1304.
    • (1991) J. Cell Biol. , vol.113 , pp. 1295-1304
    • Knoll, G.1    Braun, C.2    Plattner, H.3
  • 72
    • 0001509897 scopus 로고
    • Local trichocyst exocytosis provides an efficient escape mechanism for Paramecium cells
    • Knoll, G., Haacke-Bell, B., &, Plattner, H, 1991b. Local trichocyst exocytosis provides an efficient escape mechanism for Paramecium cells. Eur. J. Protistol., 27: 381-385.
    • (1991) Eur. J. Protistol. , vol.27 , pp. 381-385
    • Knoll, G.1    Haacke-Bell, B.2    Plattner, H.3
  • 73
    • 0026629251 scopus 로고
    • A rapid calcium influx during exocytosis in Paramecium cells is followed by a rise in cyclic GMP within 1 s
    • Knoll, G., Kerboeuf, D., &, Plattner, H., 1992. A rapid calcium influx during exocytosis in Paramecium cells is followed by a rise in cyclic GMP within 1 s. FEBS Lett., 304: 265-268.
    • (1992) FEBS Lett. , vol.304 , pp. 265-268
    • Knoll, G.1    Kerboeuf, D.2    Plattner, H.3
  • 74
    • 0027535244 scopus 로고
    • A calcium influx is neither strictly associated with nor necessary for exocytotic membrane fusion in Paramecium cells
    • Knoll, G., Grässle, A., Braun, C., Probst, W., Höhne-Zell, B., &, Plattner, H., 1993. A calcium influx is neither strictly associated with nor necessary for exocytotic membrane fusion in Paramecium cells. Cell Calcium, 14: 173-183.
    • (1993) Cell Calcium , vol.14 , pp. 173-183
    • Knoll, G.1    Grässle, A.2    Braun, C.3    Probst, W.4    Höhne-Zell, B.5    Plattner, H.6
  • 75
    • 0026689607 scopus 로고
    • In vivo Paramecium mutants show that calmodulin orchestrates membrane responses to stimuli
    • Kung, C., Preston, R. R., Maley, M. E., Ling, K. Y., Kanabrocki, J. A., Seavey, B. R., &, Saimi, Y., 1992. In vivo Paramecium mutants show that calmodulin orchestrates membrane responses to stimuli. Cell Calcium, 13: 413-425.
    • (1992) Cell Calcium , vol.13 , pp. 413-425
    • Kung, C.1    Preston, R.R.2    Maley, M.E.3    Ling, K.Y.4    Kanabrocki, J.A.5    Seavey, B.R.6    Saimi, Y.7
  • 76
    • 80755159559 scopus 로고    scopus 로고
    • Calcium-release channels in Paramecium. Genomic expansion, differential positioning and partial transcriptional elimination
    • Ladenburger, E.-M., &, Plattner, H., 2011. Calcium-release channels in Paramecium. Genomic expansion, differential positioning and partial transcriptional elimination. PLoS One, 6 (11): e27111.
    • (2011) PLoS One , vol.6 , Issue.11
    • Ladenburger, E.-M.1    Plattner, H.2
  • 79
    • 82255195437 scopus 로고    scopus 로고
    • A knockout mutation of a constitutive GPCR in Tetrahymena decreases both G-protein activity and chemoattraction
    • Lampert, T. J., Coleman, K. D., &, Hennessey, T. M., 2011. A knockout mutation of a constitutive GPCR in Tetrahymena decreases both G-protein activity and chemoattraction. PLoS One, 6: e28022.
    • (2011) PLoS One , vol.6
    • Lampert, T.J.1    Coleman, K.D.2    Hennessey, T.M.3
  • 80
    • 0028988878 scopus 로고
    • 2+ stores of probable relevance for exocytosis in Paramecium. Alveolar sacs share some but not all characteristics with sarcoplasmic reticulum
    • 2+ stores of probable relevance for exocytosis in Paramecium. Alveolar sacs share some but not all characteristics with sarcoplasmic reticulum. Cell Calcium, 17: 335-344.
    • (1995) Cell Calcium , vol.17 , pp. 335-344
    • Länge, S.1    Klauke, N.2    Plattner, H.3
  • 81
    • 0029670713 scopus 로고    scopus 로고
    • 2+ uptake by subplasmalemmal calcium stores ('alveolar sacs') isolated from Paramecium cells
    • 2+ uptake by subplasmalemmal calcium stores ('alveolar sacs') isolated from Paramecium cells. Biochim. Biophys. Acta, 1278: 191-196.
    • (1996) Biochim. Biophys. Acta , vol.1278 , pp. 191-196
    • Länge, S.1    Wissmann, J.D.2    Plattner, H.3
  • 82
    • 84866361328 scopus 로고    scopus 로고
    • Cyclic ADP-ribose and nicotinic acid adenine dinucleotide phosphate (NAADP) as messengers for calcium mobilization
    • Lee, H. C., 2012. Cyclic ADP-ribose and nicotinic acid adenine dinucleotide phosphate (NAADP) as messengers for calcium mobilization. J. Biol. Chem., 287: 31633-31640.
    • (2012) J. Biol. Chem. , vol.287 , pp. 31633-31640
    • Lee, H.C.1
  • 83
    • 84859527754 scopus 로고    scopus 로고
    • Emerging roles of phosphoinositide-specific phospholipases C in the ciliates Tetrahymena and Paramecium
    • Leondaritis, G., &, Galanopoulou, D., 2011. Emerging roles of phosphoinositide-specific phospholipases C in the ciliates Tetrahymena and Paramecium. Commun. Integr. Biol., 4: 576-578.
    • (2011) Commun. Integr. Biol. , vol.4 , pp. 576-578
    • Leondaritis, G.1    Galanopoulou, D.2
  • 84
    • 79952305981 scopus 로고    scopus 로고
    • Biochemical and genetic evidence for the presence of multiple phosphatidylinositol- and phosphatidylinositol 4,5-bisphosphate-specific phospholipases C in Tetrahymena
    • Leondaritis, G., Sarri, T., Dafnis, I., Efstathiou, A., &, Galanopoulou, D., 2011. Biochemical and genetic evidence for the presence of multiple phosphatidylinositol- and phosphatidylinositol 4,5-bisphosphate- specific phospholipases C in Tetrahymena. Eukaryot. Cell, 10: 412-422.
    • (2011) Eukaryot. Cell , vol.10 , pp. 412-422
    • Leondaritis, G.1    Sarri, T.2    Dafnis, I.3    Efstathiou, A.4    Galanopoulou, D.5
  • 85
    • 0033119289 scopus 로고    scopus 로고
    • It is calmodulin after all! Mediator of the calcium modulation of multiple ion channels
    • Levitan, I. B., 1999. It is calmodulin after all! Mediator of the calcium modulation of multiple ion channels. Neuron, 22: 645-648.
    • (1999) Neuron , vol.22 , pp. 645-648
    • Levitan, I.B.1
  • 86
    • 0033517147 scopus 로고    scopus 로고
    • Guanylyl cyclases with the topology of mammalian adenylyl cyclases and an N-terminal P-type ATPase-like domain in Paramecium, Tetrahymena and Plasmodium
    • Linder, J. U., Engel, P., Reimer, A., Krüger, T., Plattner, H., Schultz, A., &, Schultz, J. E., 1999. Guanylyl cyclases with the topology of mammalian adenylyl cyclases and an N-terminal P-type ATPase-like domain in Paramecium, Tetrahymena and Plasmodium. EMBO J., 18: 4222-4232.
    • (1999) EMBO J. , vol.18 , pp. 4222-4232
    • Linder, J.U.1    Engel, P.2    Reimer, A.3    Krüger, T.4    Plattner, H.5    Schultz, A.6    Schultz, J.E.7
  • 88
    • 0000017069 scopus 로고
    • Electrophysiology
    • Görtz, H.-D. (ed.), Springer-Verlag, Berlin, Heidelberg. p.
    • Machemer, H., 1988. Electrophysiology. In:, Görtz, H.-D., (ed.), Paramecium. Springer-Verlag, Berlin, Heidelberg. p. 185-215.
    • (1988) Paramecium , pp. 185-215
    • Machemer, H.1
  • 89
    • 0018541078 scopus 로고
    • Ionic conductances of membranes in ciliated and deciliated Paramecium
    • Machemer, H., &, Ogura, A., 1979. Ionic conductances of membranes in ciliated and deciliated Paramecium. J. Physiol., 296: 49-60.
    • (1979) J. Physiol. , vol.296 , pp. 49-60
    • Machemer, H.1    Ogura, A.2
  • 90
    • 0002888828 scopus 로고    scopus 로고
    • Sensory motor coupling and motor responses
    • Bradbury, P. C. & Hausmann, K. (ed.), Gustav Fischer Verlag, Stuttgart. p.
    • Machemer, H., &, Teunis, P. F. M., 1996. Sensory motor coupling and motor responses. In:, Bradbury, P. C., &, Hausmann, K., (ed.), Ciliates. Cells and Organisms. Gustav Fischer Verlag, Stuttgart. p. 379-402.
    • (1996) Ciliates. Cells and Organisms , pp. 379-402
    • Machemer, H.1    Teunis, P.F.M.2
  • 91
    • 0033083405 scopus 로고    scopus 로고
    • 2+-release channel function
    • 2+-release channel function. Biochem. J., 337 (345): 361.
    • (1999) Biochem. J. , vol.337 , Issue.345 , pp. 361
    • Mackrill, J.J.1
  • 92
    • 0037040968 scopus 로고    scopus 로고
    • Acidocalcisomes are functionally liked to the contractile vacuole of Dictyostelium discoidium
    • Marchesini, N., Ruiz, F. A., Vieira, M., &, Docampo, R., 2002. Acidocalcisomes are functionally liked to the contractile vacuole of Dictyostelium discoidium. J. Biol. Chem., 277: 8146-8153.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8146-8153
    • Marchesini, N.1    Ruiz, F.A.2    Vieira, M.3    Docampo, R.4
  • 93
    • 0032543766 scopus 로고    scopus 로고
    • Calcium triggers calcineurin-dependent synaptic vesicle recycling in mammalian nerve terminals
    • Marks, B., &, McMahon, H. T., 1998. Calcium triggers calcineurin-dependent synaptic vesicle recycling in mammalian nerve terminals. Curr. Biol., 8: 740-749.
    • (1998) Curr. Biol. , vol.8 , pp. 740-749
    • Marks, B.1    McMahon, H.T.2
  • 96
    • 0038420835 scopus 로고    scopus 로고
    • Refilling of cortical calcium stores in Paramecium cells: In situ analysis in correlation with store-operated calcium influx
    • Mohamed, I., Husser, M., Sehring, I., Hentschel, J., Hentschel, C., &, Plattner, H., 2003. Refilling of cortical calcium stores in Paramecium cells: in situ analysis in correlation with store-operated calcium influx. Cell Calcium, 34: 87-96.
    • (2003) Cell Calcium , vol.34 , pp. 87-96
    • Mohamed, I.1    Husser, M.2    Sehring, I.3    Hentschel, J.4    Hentschel, C.5    Plattner, H.6
  • 97
    • 0022905365 scopus 로고
    • Calmodulin in Paramecium tetraurelia: Localization from the in vivo to the ultrastructural level
    • Momayezi, M., Kersken, H., Gras, U., Vilmart-Seuwen, J., &, Plattner, H., 1986. Calmodulin in Paramecium tetraurelia: localization from the in vivo to the ultrastructural level. J. Histochem. Cytochem., 34: 1621-1638.
    • (1986) J. Histochem. Cytochem. , vol.34 , pp. 1621-1638
    • Momayezi, M.1    Kersken, H.2    Gras, U.3    Vilmart-Seuwen, J.4    Plattner, H.5
  • 98
    • 0023376810 scopus 로고
    • Exocytosis induction in Paramecium tetraurelia cells by exogenous phosphoprotein phosphatase in vivo and in vitro: Possible involvement of calcineurin in exocytotic membrane fusion
    • Momayezi, M., Lumpert, C. J., Kersken, H., Gras, U., Plattner, H., Krinks, M. H., &, Klee, C. B., 1987. Exocytosis induction in Paramecium tetraurelia cells by exogenous phosphoprotein phosphatase in vivo and in vitro: possible involvement of calcineurin in exocytotic membrane fusion. J. Cell Biol., 105: 181-189.
    • (1987) J. Cell Biol. , vol.105 , pp. 181-189
    • Momayezi, M.1    Lumpert, C.J.2    Kersken, H.3    Gras, U.4    Plattner, H.5    Krinks, M.H.6    Klee, C.B.7
  • 99
    • 0029835627 scopus 로고    scopus 로고
    • Immunolocalization of protein phosphatase type 1 in Paramecium cells using antibodies against recombinant protein and peptides
    • Momayezi, M., Wloga, D., Kissmehl, R., Plattner, H., Jung, G., Klumpp, S., &, Schultz, J. E., 1996. Immunolocalization of protein phosphatase type 1 in Paramecium cells using antibodies against recombinant protein and peptides. J. Histochem. Cytochem., 44: 891-905.
    • (1996) J. Histochem. Cytochem. , vol.44 , pp. 891-905
    • Momayezi, M.1    Wloga, D.2    Kissmehl, R.3    Plattner, H.4    Jung, G.5    Klumpp, S.6    Schultz, J.E.7
  • 100
    • 0033852346 scopus 로고    scopus 로고
    • Quantitative immunogold localization of protein phosphatase 2B (calcineurin) in Paramecium cells
    • Momayezi, M., Kissmehl, R., &, Plattner, H., 2000. Quantitative immunogold localization of protein phosphatase 2B (calcineurin) in Paramecium cells. J. Histochem. Cytochem., 48: 1269-1281.
    • (2000) J. Histochem. Cytochem. , vol.48 , pp. 1269-1281
    • Momayezi, M.1    Kissmehl, R.2    Plattner, H.3
  • 101
    • 0033066922 scopus 로고    scopus 로고
    • 2+-ATPase PAT1 and the contractile vacuole in calcium regulation in Dictyostelium
    • 2+-ATPase PAT1 and the contractile vacuole in calcium regulation in Dictyostelium. J. Cell Sci., 112: 405-414.
    • (1999) J. Cell Sci. , vol.112 , pp. 405-414
    • Moniakis, J.1    Coukell, M.B.2    Janiec, A.3
  • 102
    • 0042195182 scopus 로고    scopus 로고
    • Calcium regulation in protozoan parasites
    • Moreno, S. N. J., &, Docampo, R., 2003. Calcium regulation in protozoan parasites. Curr. Opin. Microbiol., 6: 359-364.
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 359-364
    • Moreno, S.N.J.1    Docampo, R.2
  • 103
    • 0036289152 scopus 로고    scopus 로고
    • Crystal structure analysis of the exocytosis-sensitive phosphoprotein, pp 63/parafusin (phosphoglucomutase), from Paramecium reveals significant conformational variability
    • Müller, S., Diederichs, K., Breed, J., Kissmehl, R., Hauser, K., Plattner, H., &, Welte, W., 2002. Crystal structure analysis of the exocytosis-sensitive phosphoprotein, pp 63/parafusin (phosphoglucomutase), from Paramecium reveals significant conformational variability. J. Mol. Biol., 315: 141-153.
    • (2002) J. Mol. Biol. , vol.315 , pp. 141-153
    • Müller, S.1    Diederichs, K.2    Breed, J.3    Kissmehl, R.4    Hauser, K.5    Plattner, H.6    Welte, W.7
  • 104
    • 0242582465 scopus 로고    scopus 로고
    • A direct mass-action mechanism explains capacitative calcium entry in Jurkat and skeletal L6 muscle cells
    • Narayanan, B., Islam, M. N., Bartelt, D., &, Ochs, R. S., 2003. A direct mass-action mechanism explains capacitative calcium entry in Jurkat and skeletal L6 muscle cells. J. Biol. Chem., 278: 44188-44196.
    • (2003) J. Biol. Chem. , vol.278 , pp. 44188-44196
    • Narayanan, B.1    Islam, M.N.2    Bartelt, D.3    Ochs, R.S.4
  • 105
    • 84865781211 scopus 로고    scopus 로고
    • Introduction: Regulated exocytosis
    • Neher, E., 2012. Introduction: regulated exocytosis. Cell Calcium, 52: 196-198.
    • (2012) Cell Calcium , vol.52 , pp. 196-198
    • Neher, E.1
  • 106
    • 0017372359 scopus 로고
    • Separation of membrane currents using a Paramecium mutant
    • Oertel, D., Schein, S. J., &, Kung, C., 1977. Separation of membrane currents using a Paramecium mutant. Nature, 268: 120-124.
    • (1977) Nature , vol.268 , pp. 120-124
    • Oertel, D.1    Schein, S.J.2    Kung, C.3
  • 110
    • 73949092362 scopus 로고    scopus 로고
    • In with the TRP channels: Intracellular functions for TRPM1 and TRPM2
    • Patel, S., &, Docampo, R., 2009. In with the TRP channels: intracellular functions for TRPM1 and TRPM2. Sci. Signal., 2: pe69.
    • (2009) Sci. Signal. , vol.2
    • Patel, S.1    Docampo, R.2
  • 113
    • 0001857542 scopus 로고
    • Synchronous exocytosis in Paramecium cells
    • Sowers, A. E. (ed.), Plenum Press, New York. p.
    • Plattner, H., 1987. Synchronous exocytosis in Paramecium cells. In:, Sowers, A. E., (ed.), Cell Fusion. Plenum Press, New York. p. 69-98.
    • (1987) Cell Fusion , pp. 69-98
    • Plattner, H.1
  • 114
    • 77955660969 scopus 로고    scopus 로고
    • How to design a highly organized cell: An unexpectedly high number of widely diversified SNARE proteins positioned at strategic sites in the ciliate, Paramecium tetraurelia
    • Plattner, H., 2010. How to design a highly organized cell: an unexpectedly high number of widely diversified SNARE proteins positioned at strategic sites in the ciliate, Paramecium tetraurelia. Protist, 161: 497-516.
    • (2010) Protist , vol.161 , pp. 497-516
    • Plattner, H.1
  • 115
    • 0016744239 scopus 로고
    • X-ray microanalysis of calcium binding sites in Paramecium with special reference to exocytosis
    • Plattner, H., &, Fuchs, S., 1975. X-ray microanalysis of calcium binding sites in Paramecium with special reference to exocytosis. Histochemistry, 45: 23-47.
    • (1975) Histochemistry , vol.45 , pp. 23-47
    • Plattner, H.1    Fuchs, S.2
  • 116
    • 33845438047 scopus 로고    scopus 로고
    • Sub-second cellular dynamics: Time-resolved electron microscopy and functional correlation
    • Plattner, H., &, Hentschel, J., 2006. Sub-second cellular dynamics: Time-resolved electron microscopy and functional correlation. Int. Rev. Cytol., 255: 133-176.
    • (2006) Int. Rev. Cytol. , vol.255 , pp. 133-176
    • Plattner, H.1    Hentschel, J.2
  • 117
    • 0033781424 scopus 로고    scopus 로고
    • Calcium in ciliated protozoa: Sources, regulation, and calcium-regulated cell functions
    • Plattner, H., &, Klauke, N., 2001. Calcium in ciliated protozoa: sources, regulation, and calcium-regulated cell functions. Int. Rev. Cytol., 201: 115-208.
    • (2001) Int. Rev. Cytol. , vol.201 , pp. 115-208
    • Plattner, H.1    Klauke, N.2
  • 118
  • 119
    • 0021347080 scopus 로고
    • Synchronous exocytosis in Paramecium cells. I. A novel approach
    • Plattner, H., Matt, H., Kersken, H., Haacke, B., &, Stürzl, R., 1984. Synchronous exocytosis in Paramecium cells. I. A novel approach. Exp. Cell Res., 151: 6-13.
    • (1984) Exp. Cell Res. , vol.151 , pp. 6-13
    • Plattner, H.1    Matt, H.2    Kersken, H.3    Haacke, B.4    Stürzl, R.5
  • 120
    • 0021932549 scopus 로고
    • Synchronous exocytosis in Paramecium cells. IV. Polyamino compounds as potent trigger agents for repeatable trigger-redocking cycles
    • Plattner, H., Stürzl, R., &, Matt, H., 1985. Synchronous exocytosis in Paramecium cells. IV. Polyamino compounds as potent trigger agents for repeatable trigger-redocking cycles. Eur. J. Cell Biol., 36: 32-37.
    • (1985) Eur. J. Cell Biol. , vol.36 , pp. 32-37
    • Plattner, H.1    Stürzl, R.2    Matt, H.3
  • 121
    • 0001930854 scopus 로고
    • Synchronization of different steps of the secretory cycle in Paramecium tetraurelia: Trichocyst exocytosis, exocytosis-coupled endocytosis and intracellular transport
    • Plattner, H. (ed.), JAI Press, Greenwich (CT); London. p.
    • Plattner, H., Knoll, G., &, Pape, R., 1993. Synchronization of different steps of the secretory cycle in Paramecium tetraurelia: Trichocyst exocytosis, exocytosis-coupled endocytosis and intracellular transport. In:, Plattner, H., (ed.), Membrane Traffic in Protozoa. JAI Press, Greenwich (CT); London. p. 123-148.
    • (1993) Membrane Traffic in Protozoa , pp. 123-148
    • Plattner, H.1    Knoll, G.2    Pape, R.3
  • 122
    • 0030801106 scopus 로고    scopus 로고
    • Facilitation of membrane fusion during exocytosis and exocytosis-coupled endocytosis and acceleration of "ghost" detachment in Paramecium by extracellular calcium. A quenched-flow/freeze-fracture analysis
    • Plattner, H., Braun, C., &, Hentschel, J., 1997a. Facilitation of membrane fusion during exocytosis and exocytosis-coupled endocytosis and acceleration of "ghost" detachment in Paramecium by extracellular calcium. A quenched-flow/freeze-fracture analysis. J. Membr. Biol., 158: 197-208.
    • (1997) J. Membr. Biol. , vol.158 , pp. 197-208
    • Plattner, H.1    Braun, C.2    Hentschel, J.3
  • 123
    • 0030971213 scopus 로고    scopus 로고
    • Differential distribution of calcium stores in Paramecium cells. Occurrence of a subplasmalemmal store with a calsequestrin-like protein
    • Plattner, H., Habermann, A., Kissmehl, R., Klauke, N., Majoul, I., &, Söling, H. D., 1997b. Differential distribution of calcium stores in Paramecium cells. Occurrence of a subplasmalemmal store with a calsequestrin-like protein. Eur. J. Cell Biol., 72: 297-306.
    • (1997) Eur. J. Cell Biol. , vol.72 , pp. 297-306
    • Plattner, H.1    Habermann, A.2    Kissmehl, R.3    Klauke, N.4    Majoul, I.5    Söling, H.D.6
  • 125
    • 24644439582 scopus 로고    scopus 로고
    • Molecular aspects of rapid, reversible, Ca2+-dependent de-phosphorylation of pp 63/parafusin during stimulated exo-endocytosis in Paramecium cells
    • Plattner, H., &, Kissmehl, R., 2005. Molecular aspects of rapid, reversible, Ca2+-dependent de-phosphorylation of pp 63/parafusin during stimulated exo-endocytosis in Paramecium cells. Cell Calcium, 38: 319-327.
    • (2005) Cell Calcium , vol.38 , pp. 319-327
    • Plattner, H.1    Kissmehl, R.2
  • 126
    • 33646349985 scopus 로고    scopus 로고
    • Sub-second calcium coupling between outside medium and subplasmalemmal stores during overstimulation/depolarisation-induced ciliary beat reversal in Paramecium cells
    • Plattner, H., Diehl, S., Husser, M. R., &, Hentschel, J., 2006. Sub-second calcium coupling between outside medium and subplasmalemmal stores during overstimulation/depolarisation-induced ciliary beat reversal in Paramecium cells. Cell Calcium, 396: 509-516.
    • (2006) Cell Calcium , vol.396 , pp. 509-516
    • Plattner, H.1    Diehl, S.2    Husser, M.R.3    Hentschel, J.4
  • 127
    • 59649101366 scopus 로고    scopus 로고
    • Pharmacology of ciliated protozoa-drug (in)sensitivity and experimental drug (ab)use
    • Plattner, H., Sehring, I. M., Schilde, C., &, Ladenburger, E.-M., 2009. Pharmacology of ciliated protozoa-drug (in)sensitivity and experimental drug (ab)use. Int. Rev. Cell Mol. Biol., 273: 163-218.
    • (2009) Int. Rev. Cell Mol. Biol. , vol.273 , pp. 163-218
    • Plattner, H.1    Sehring, I.M.2    Schilde, C.3    Ladenburger, E.-M.4
  • 128
    • 84859559340 scopus 로고    scopus 로고
    • Calcium signaling in closely related protozoan groups (Alveolata): Non-parasitic ciliates (Paramecium, Tetrahymena) vs parasitic Apicomplexa (Plasmodium, Toxoplasma)
    • Plattner, H., Sehring, I. M., Mohamed, I. K., Miranda, K., De Souza, W., Billington, R., Genazzani, A., &, Ladenburger, E.-M., 2012. Calcium signaling in closely related protozoan groups (Alveolata): non-parasitic ciliates (Paramecium, Tetrahymena) vs. parasitic Apicomplexa (Plasmodium, Toxoplasma). Cell Calcium, 51: 351-382.
    • (2012) Cell Calcium , vol.51 , pp. 351-382
    • Plattner, H.1    Sehring, I.M.2    Mohamed, I.K.3    Miranda, K.4    De Souza, W.5    Billington, R.6    Genazzani, A.7    Ladenburger, E.-M.8
  • 129
    • 0026739599 scopus 로고
    • Calcium current activated upon hyperpolarization of Paramecium tetraurelia
    • Preston, R. R., Saimi, Y., &, Kung, C., 1992. Calcium current activated upon hyperpolarization of Paramecium tetraurelia. J. Gen. Physiol., 100: 233-251.
    • (1992) J. Gen. Physiol. , vol.100 , pp. 233-251
    • Preston, R.R.1    Saimi, Y.2    Kung, C.3
  • 132
    • 84875486544 scopus 로고    scopus 로고
    • The microdomain forming stomatin family in the ciliated protozoan Paramecium tetraurelia: Identification, localization and functional implications
    • Reuter, A. T., Stuermer, C. A. O., &, Plattner, H., 2013. The microdomain forming stomatin family in the ciliated protozoan Paramecium tetraurelia: Identification, localization and functional implications. Eukaryot. Microbiol., 12: 529-544.
    • (2013) Eukaryot. Microbiol. , vol.12 , pp. 529-544
    • Reuter, A.T.1    Stuermer, C.A.O.2    Plattner, H.3
  • 133
    • 77954593415 scopus 로고    scopus 로고
    • A molecular clock for malaria parasites
    • Ricklefs, R. E., &, Outlaw, D. C., 2010. A molecular clock for malaria parasites. Science, 329: 226-229.
    • (2010) Science , vol.329 , pp. 226-229
    • Ricklefs, R.E.1    Outlaw, D.C.2
  • 134
    • 33745938170 scopus 로고    scopus 로고
    • Unraveling the mechanisms of synaptotagmin and SNARE function in neurotransmitter release
    • Rizo, J., Chen, X., &, Arac, D., 2006. Unraveling the mechanisms of synaptotagmin and SNARE function in neurotransmitter release. Trends Cell Biol., 16: 339-350.
    • (2006) Trends Cell Biol. , vol.16 , pp. 339-350
    • Rizo, J.1    Chen, X.2    Arac, D.3
  • 135
    • 37349014076 scopus 로고    scopus 로고
    • A contractile vacuole complex is involved in osmoregulation in Trypanosoma cruzi
    • Rohloff, P., &, Docampo, R., 2008. A contractile vacuole complex is involved in osmoregulation in Trypanosoma cruzi. Exp. Parasistol., 118: 17-24.
    • (2008) Exp. Parasistol. , vol.118 , pp. 17-24
    • Rohloff, P.1    Docampo, R.2
  • 136
    • 0033779701 scopus 로고    scopus 로고
    • Calcineurin: Form and function
    • Rusnak, F., &, Mertz, P., 2000. Calcineurin: form and function. Physiol. Rev., 80: 1483-1521.
    • (2000) Physiol. Rev. , vol.80 , pp. 1483-1521
    • Rusnak, F.1    Mertz, P.2
  • 137
    • 84875238852 scopus 로고    scopus 로고
    • A set of SNARE proteins in the contractile vacuole complex of Paramecium regulates cellular calcium tolerance and also contributes to organelle biogenesis
    • Schönemann, B., Bledowski, A., Sehring, I. M., &, Plattner, H., 2013. A set of SNARE proteins in the contractile vacuole complex of Paramecium regulates cellular calcium tolerance and also contributes to organelle biogenesis. Cell Calcium, 53: 204-216.
    • (2013) Cell Calcium , vol.53 , pp. 204-216
    • Schönemann, B.1    Bledowski, A.2    Sehring, I.M.3    Plattner, H.4
  • 140
    • 58149194928 scopus 로고    scopus 로고
    • 2+-signal after exocytosis stimulation in Paramecium cells: Essential role of a centrin-rich filamentous cortical network, the infraciliary lattice
    • 2+-signal after exocytosis stimulation in Paramecium cells: essential role of a centrin-rich filamentous cortical network, the infraciliary lattice. Cell Calcium, 45: 89-97.
    • (2009) Cell Calcium , vol.45 , pp. 89-97
    • Sehring, I.M.1    Klotz, C.2    Beisson, J.3    Plattner, H.4
  • 141
    • 0028170809 scopus 로고
    • Protein serine/threonine phosphatases - New avenues for cell regulation
    • Shenolikar, S., 1994. Protein serine/threonine phosphatases-new avenues for cell regulation. Annu. Rev. Cell Biol., 10: 55-86.
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 55-86
    • Shenolikar, S.1
  • 143
    • 0025876729 scopus 로고
    • Cortical alveoli of Paramecium: A vast submembranous calcium storage compartment
    • Stelly, N., Mauger, J. P., Claret, M., &, Adoutte, A., 1991. Cortical alveoli of Paramecium: a vast submembranous calcium storage compartment. J. Cell Biol., 113: 103-112.
    • (1991) J. Cell Biol. , vol.113 , pp. 103-112
    • Stelly, N.1    Mauger, J.P.2    Claret, M.3    Adoutte, A.4
  • 144
    • 0036749792 scopus 로고    scopus 로고
    • The ionic composition of the contractile vacuole fluid of Paramecium mirrors ion transport across the plasma membrane
    • Stock, C., Grønlien, H. K., &, Allen, R. D., 2002. The ionic composition of the contractile vacuole fluid of Paramecium mirrors ion transport across the plasma membrane. Eur. J. Cell Biol., 81: 505-515.
    • (2002) Eur. J. Cell Biol. , vol.81 , pp. 505-515
    • Stock, C.1    Grønlien, H.K.2    Allen, R.D.3
  • 146
    • 84859526754 scopus 로고    scopus 로고
    • Calmodulin-domain protein kinase
    • Celio, M. R. Pauls, T. L. & Schwaller, B. (ed.), Oxford University Press, Oxford, GB. p.
    • Sussmann, M. R., Hrabak, E. M., &, Satterlee, J. S., 1996. Calmodulin-domain protein kinase. In:, Celio, M. R., Pauls, T. L., &, Schwaller, B., (ed.), Calcium-Binding Proteins. Oxford University Press, Oxford, GB. p. 46-48.
    • (1996) Calcium-Binding Proteins , pp. 46-48
    • Sussmann, M.R.1    Hrabak, E.M.2    Satterlee, J.S.3
  • 149
    • 0347064006 scopus 로고    scopus 로고
    • Molecular identification of a calcium-inhibited catalytic subunit of casein kinase type 2 from Paramecium tetraurelia
    • Vetter, D., Kissmehl, R., Treptau, T., Hauser, K., Kellermann, J., &, Plattner, H., 2003. Molecular identification of a calcium-inhibited catalytic subunit of casein kinase type 2 from Paramecium tetraurelia. Eukaryot. Cell, 2: 1220-1233.
    • (2003) Eukaryot. Cell , vol.2 , pp. 1220-1233
    • Vetter, D.1    Kissmehl, R.2    Treptau, T.3    Hauser, K.4    Kellermann, J.5    Plattner, H.6
  • 150
    • 0022969327 scopus 로고
    • ATP keeps exocytosis sites in a primed state but is not required for membrane fusion: An analysis with Paramecium cells in vivo and in vitro
    • Vilmart-Seuwen, J., Kersken, H., Stürzl, R., &, Plattner, H., 1986. ATP keeps exocytosis sites in a primed state but is not required for membrane fusion: an analysis with Paramecium cells in vivo and in vitro. J. Cell Biol., 103: 1279-1288.
    • (1986) J. Cell Biol. , vol.103 , pp. 1279-1288
    • Vilmart-Seuwen, J.1    Kersken, H.2    Stürzl, R.3    Plattner, H.4
  • 151
    • 0030904525 scopus 로고    scopus 로고
    • Ryanodine receptors: Structure and macromolecular interactions
    • Wagenknecht, T., &, Radermacher, M., 1997. Ryanodine receptors: structure and macromolecular interactions. Curr. Opin. Struct. Biol., 7: 258-265.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 258-265
    • Wagenknecht, T.1    Radermacher, M.2
  • 153
    • 0031278919 scopus 로고    scopus 로고
    • Effect of SERCA pump inhibitors on chemoresponses in Paramecium
    • Wassenberg, J. J., Clark, K. D., &, Nelson, D. L., 1997. Effect of SERCA pump inhibitors on chemoresponses in Paramecium. J. Eukaryot. Microbiol., 44: 574-581.
    • (1997) J. Eukaryot. Microbiol. , vol.44 , pp. 574-581
    • Wassenberg, J.J.1    Clark, K.D.2    Nelson, D.L.3
  • 154
    • 23744443106 scopus 로고    scopus 로고
    • The vacuolar proton-ATPase plays a major role in several membrane-bounded organelles in Paramecium
    • Wassmer, T., Froissard, M., Plattner, H., Kissmehl, R., &, Cohen, J., 2005. The vacuolar proton-ATPase plays a major role in several membrane-bounded organelles in Paramecium. J. Cell Sci., 118: 2813-2825.
    • (2005) J. Cell Sci. , vol.118 , pp. 2813-2825
    • Wassmer, T.1    Froissard, M.2    Plattner, H.3    Kissmehl, R.4    Cohen, J.5
  • 155
    • 31944432438 scopus 로고    scopus 로고
    • Seventeen a-subunit isoforms of Paramecium V-ATPase provide high specialization in localization and function
    • Wassmer, T., Kissmehl, R., Cohen, J., &, Plattner, H., 2006. Seventeen a-subunit isoforms of Paramecium V-ATPase provide high specialization in localization and function. Mol. Biol. Cell, 17: 917-930.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 917-930
    • Wassmer, T.1    Kissmehl, R.2    Cohen, J.3    Plattner, H.4
  • 156
    • 62149113668 scopus 로고    scopus 로고
    • The V-ATPase in Paramecium: Functional specialization by multiple gene isoforms
    • Wassmer, T., Sehring, I. M., Kissmehl, R., &, Plattner, H., 2009. The V-ATPase in Paramecium: functional specialization by multiple gene isoforms. Pflugers Arch., 457: 599-607.
    • (2009) Pflugers Arch. , vol.457 , pp. 599-607
    • Wassmer, T.1    Sehring, I.M.2    Kissmehl, R.3    Plattner, H.4
  • 157
    • 0034981326 scopus 로고    scopus 로고
    • 2+-release channel tunnel: Structures and mechanisms involved in ion translocation in ryanodine receptor channels
    • 2+-release channel tunnel: structures and mechanisms involved in ion translocation in ryanodine receptor channels. Q. Rev. Biophys., 34: 61-104.
    • (2001) Q. Rev. Biophys. , vol.34 , pp. 61-104
    • Williams, A.J.1    West, D.J.2    Sitsapesan, R.3
  • 161
    • 0031011668 scopus 로고    scopus 로고
    • Extracellular calcium sensed by a novel cation channel in hippocampal neurons
    • Xiong, Z., Lu, W., &, MacDonald, J. F., 1997. Extracellular calcium sensed by a novel cation channel in hippocampal neurons. Proc. Natl Acad. Sci. U S A, 94: 7012-7017.
    • (1997) Proc. Natl Acad. Sci. U S A , vol.94 , pp. 7012-7017
    • Xiong, Z.1    Lu, W.2    Macdonald, J.F.3
  • 162
    • 0030856277 scopus 로고    scopus 로고
    • Cyclic nucleotides in glutamate chemosensory signal transduction of Paramecium
    • Yang, W. Q., Braun, C., Plattner, H., Purvee, J., &, Van Houten, J. L., 1997. Cyclic nucleotides in glutamate chemosensory signal transduction of Paramecium. J. Cell Sci., 110: 2567-2572.
    • (1997) J. Cell Sci. , vol.110 , pp. 2567-2572
    • Yang, W.Q.1    Braun, C.2    Plattner, H.3    Purvee, J.4    Van Houten, J.L.5
  • 164
    • 79151479286 scopus 로고    scopus 로고
    • Inositol 1,4,5-trisphosphate receptor in chromaffin secretory granules and its relation to chromogranins
    • Yoo, S. H., Huh, Y. H., &, Hur, Y. S., 2010. Inositol 1,4,5-trisphosphate receptor in chromaffin secretory granules and its relation to chromogranins. Cell. Mol. Neurobiol., 30: 1155-1161.
    • (2010) Cell. Mol. Neurobiol. , vol.30 , pp. 1155-1161
    • Yoo, S.H.1    Huh, Y.H.2    Hur, Y.S.3
  • 165
    • 34548644786 scopus 로고    scopus 로고
    • Modulation of the ryanodine receptor and intracellular calcium
    • Zalk, R., Lehnart, S. E., &, Marks, A. R., 2007. Modulation of the ryanodine receptor and intracellular calcium. Annu. Rev. Biochem., 76: 367-385.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 367-385
    • Zalk, R.1    Lehnart, S.E.2    Marks, A.R.3
  • 166
    • 0022392704 scopus 로고
    • Synchronous exocytosis in Paramecium cells involves very rapid (<1 s), reversible dephosphorylation of a 65-kD phosphoprotein in exocytosis-competent strains
    • Zieseniss, E., &, Plattner, H., 1985. Synchronous exocytosis in Paramecium cells involves very rapid (<1 s), reversible dephosphorylation of a 65-kD phosphoprotein in exocytosis-competent strains. J. Cell Biol., 101: 2028-2035.
    • (1985) J. Cell Biol. , vol.101 , pp. 2028-2035
    • Zieseniss, E.1    Plattner, H.2
  • 167
    • 0030610319 scopus 로고    scopus 로고
    • 2+ channel/ryanodine receptor: Modulation by endogenous effectors, drugs and disease states
    • 2+ channel/ryanodine receptor: modulation by endogenous effectors, drugs and disease states. Pharmacol. Rev., 49: 1-51.
    • (1997) Pharmacol. Rev. , vol.49 , pp. 1-51
    • Zucchi, R.1    Ronca-Testoni, S.2


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