메뉴 건너뛰기




Volumn 6, Issue 11, 2011, Pages

Calcium-release channels in paramecium. genomic expansion, differential positioning and partial transcriptional elimination

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; GREEN FLUORESCENT PROTEIN; INOSITOL 1,4,5 TRISPHOSPHATE RECEPTOR; MONOCLONAL ANTIBODY; RYANODINE RECEPTOR; CALCIUM; RYANODINE;

EID: 80755159559     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0027111     Document Type: Article
Times cited : (41)

References (105)
  • 3
    • 37149029370 scopus 로고    scopus 로고
    • Calcium signaling
    • Clapham DE, (2007) Calcium signaling. Cell 131: 1047-1058.
    • (2007) Cell , vol.131 , pp. 1047-1058
    • Clapham, D.E.1
  • 5
    • 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
  • 6
    • 0032435180 scopus 로고    scopus 로고
    • Usefulness and limitations of linear approximations to the understanding of Ca2+ signals
    • Neher E, (1998) Usefulness and limitations of linear approximations to the understanding of Ca2+ signals. Cell Calcium 24: 345-357.
    • (1998) Cell Calcium , vol.24 , pp. 345-357
    • Neher, E.1
  • 7
    • 0028363747 scopus 로고
    • Transmembrane topology and sites of N-glycosylation of inositol 1,4,5-trisphosphate receptor
    • Michikawa T, Hamanaka H, Otsu H, Yamamoto A, Miyawaki A, et al. (1994) Transmembrane topology and sites of N-glycosylation of inositol 1,4,5-trisphosphate receptor. J Biol Chem 269: 9184-9189.
    • (1994) J Biol Chem , vol.269 , pp. 9184-9189
    • Michikawa, T.1    Hamanaka, H.2    Otsu, H.3    Yamamoto, A.4    Miyawaki, A.5
  • 8
    • 0024318429 scopus 로고
    • Primary structure and expression from complementary DNA of skeletal muscle ryanodine receptor
    • Takeshima H, Nishimura S, Matsumoto T, Ishida H, Kangawa K, et al. (1989) Primary structure and expression from complementary DNA of skeletal muscle ryanodine receptor. Nature 339: 439-445.
    • (1989) Nature , vol.339 , pp. 439-445
    • Takeshima, H.1    Nishimura, S.2    Matsumoto, T.3    Ishida, H.4    Kangawa, K.5
  • 9
    • 0025071723 scopus 로고
    • Molecular cloning of cDNA encoding human and rabbit forms of the Ca2+ release channel (ryanodine receptor) of skeletal muscle sarcoplasmic reticulum
    • Zorzato F, Fujii J, Otsu K, Phillips M, Green NM, et al. (1990) Molecular cloning of cDNA encoding human and rabbit forms of the Ca2+ release channel (ryanodine receptor) of skeletal muscle sarcoplasmic reticulum. J Biol Chem 265: 2244-2256.
    • (1990) J Biol Chem , vol.265 , pp. 2244-2256
    • Zorzato, F.1    Fujii, J.2    Otsu, K.3    Phillips, M.4    Green, N.M.5
  • 10
    • 0037168425 scopus 로고    scopus 로고
    • Topology of the Ca2+ release channel of skeletal muscle sarcoplasmic reticulum (RyR1)
    • Du GG, Sandhu B, Khanna VK, Guo XH, MacLennan DH, (2002) Topology of the Ca2+ release channel of skeletal muscle sarcoplasmic reticulum (RyR1). Proc Natl Acad Sci U S A 99: 16725-16730.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 16725-16730
    • Du, G.G.1    Sandhu, B.2    Khanna, V.K.3    Guo, X.H.4    MacLennan, D.H.5
  • 11
    • 0142155040 scopus 로고    scopus 로고
    • What we don't know about the structure of ryanodine receptor calcium release channels
    • Dulhunty AF, Pouliquin P, (2003) What we don't know about the structure of ryanodine receptor calcium release channels. Clin Exp Pharmacol Physiol 30: 713-723.
    • (2003) Clin Exp Pharmacol Physiol , vol.30 , pp. 713-723
    • Dulhunty, A.F.1    Pouliquin, P.2
  • 12
    • 24644455527 scopus 로고    scopus 로고
    • Ryanodine receptors
    • Hamilton SL, (2005) Ryanodine receptors. Cell Calcium 38: 253-260.
    • (2005) Cell Calcium , vol.38 , pp. 253-260
    • Hamilton, S.L.1
  • 13
    • 34548644786 scopus 로고    scopus 로고
    • Modulation of the ryanodine receptor and intracellular calcium
    • Zalk R, Lehnart SE, Marks AR, (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
  • 14
    • 0033976150 scopus 로고    scopus 로고
    • Novel repeats in ryanodine and IP3 receptors and protein O-mannosyltransferases
    • Ponting CP, (2000) Novel repeats in ryanodine and IP3 receptors and protein O-mannosyltransferases. Trends Biochem Sci 25: 48-50.
    • (2000) Trends Biochem Sci , vol.25 , pp. 48-50
    • Ponting, C.P.1
  • 15
    • 0029019101 scopus 로고
    • Calcium and inositol trisphosphate receptors
    • Taylor CW, Traynor D, (1995) Calcium and inositol trisphosphate receptors. J Membr Biol 145: 109-118.
    • (1995) J Membr Biol , vol.145 , pp. 109-118
    • Taylor, C.W.1    Traynor, D.2
  • 17
    • 0029898559 scopus 로고    scopus 로고
    • Mutational analysis of the ligand binding site of the inositol 1,4,5-trisphosphate receptor
    • Yoshikawa F, Morita M, Monkawa T, Michikawa T, Furuichi T, et al. (1996) Mutational analysis of the ligand binding site of the inositol 1,4,5-trisphosphate receptor. J Biol Chem 271: 18277-18284.
    • (1996) J Biol Chem , vol.271 , pp. 18277-18284
    • Yoshikawa, F.1    Morita, M.2    Monkawa, T.3    Michikawa, T.4    Furuichi, T.5
  • 18
    • 0030893595 scopus 로고    scopus 로고
    • The pharmacology of ryanodine and related compounds
    • Sutko JL, Airey JA, Welch W, Ruest L, (1997) The pharmacology of ryanodine and related compounds. Pharmacol Rev 49: 53-98.
    • (1997) Pharmacol Rev , vol.49 , pp. 53-98
    • Sutko, J.L.1    Airey, J.A.2    Welch, W.3    Ruest, L.4
  • 19
    • 0038082056 scopus 로고    scopus 로고
    • The Ile2453Thr mutation in the ryanodine receptor gene 1 is associated with facilitated calcium release from sarcoplasmic reticulum by 4-chloro-m-cresol in human myotubes
    • Wehner M, Rueffert H, Koenig F, Meinecke CD, Olthoff D, (2003) The Ile2453Thr mutation in the ryanodine receptor gene 1 is associated with facilitated calcium release from sarcoplasmic reticulum by 4-chloro-m-cresol in human myotubes. Cell Calcium 34: 163-168.
    • (2003) Cell Calcium , vol.34 , pp. 163-168
    • Wehner, M.1    Rueffert, H.2    Koenig, F.3    Meinecke, C.D.4    Olthoff, D.5
  • 20
    • 0027418624 scopus 로고
    • Caffeine as an analgesic adjuvant: a review of pharmacology and mechanisms of action
    • Sawynok J, Yaksh TL, (1993) Caffeine as an analgesic adjuvant: a review of pharmacology and mechanisms of action. Pharmacol Rev 45: 43-85.
    • (1993) Pharmacol Rev , vol.45 , pp. 43-85
    • Sawynok, J.1    Yaksh, T.L.2
  • 21
    • 0031665799 scopus 로고    scopus 로고
    • Pharmacological analysis of intracellular Ca2+ signalling: problems and pitfalls
    • Taylor CW, Broad LM, (1998) Pharmacological analysis of intracellular Ca2+ signalling: problems and pitfalls. Trends Pharmacol Sci 19: 370-375.
    • (1998) Trends Pharmacol Sci , vol.19 , pp. 370-375
    • Taylor, C.W.1    Broad, L.M.2
  • 22
    • 4944246457 scopus 로고    scopus 로고
    • Comparative analysis of plant and animal calcium signal transduction element using plant full-length cDNA data
    • Nagata T, Iizumi S, Satoh K, Ooka H, Kawai J, et al. (2004) Comparative analysis of plant and animal calcium signal transduction element using plant full-length cDNA data. Mol Biol Evol 21: 1855-1870.
    • (2004) Mol Biol Evol , vol.21 , pp. 1855-1870
    • Nagata, T.1    Iizumi, S.2    Satoh, K.3    Ooka, H.4    Kawai, J.5
  • 23
    • 33748079101 scopus 로고    scopus 로고
    • Comparative genomic and phylogenetic analyses of calcium ATPases and calcium-regulated proteins in the apicomplexa
    • Nagamune K, Sibley LD, (2006) Comparative genomic and phylogenetic analyses of calcium ATPases and calcium-regulated proteins in the apicomplexa. Mol Biol Evol 23: 1613-1627.
    • (2006) Mol Biol Evol , vol.23 , pp. 1613-1627
    • Nagamune, K.1    Sibley, L.D.2
  • 24
    • 33749403485 scopus 로고    scopus 로고
    • An Ins(1,4,5)P3 receptor in Paramecium is associated with the osmoregulatory system
    • Ladenburger EM, Korn I, Kasielke N, Wassmer T, Plattner H, (2006) An Ins(1,4,5)P3 receptor in Paramecium is associated with the osmoregulatory system. J Cell Sci 119: 3705-3717.
    • (2006) J Cell Sci , vol.119 , pp. 3705-3717
    • Ladenburger, E.M.1    Korn, I.2    Kasielke, N.3    Wassmer, T.4    Plattner, H.5
  • 25
    • 67650065253 scopus 로고    scopus 로고
    • Novel types of Ca2+ release channels participate in the secretory cycle of Paramecium cells
    • Ladenburger EM, Sehring IM, Korn I, Plattner H, (2009) Novel types of Ca2+ release channels participate in the secretory cycle of Paramecium cells. Mol Cell Biol 29: 3605-3622.
    • (2009) Mol Cell Biol , vol.29 , pp. 3605-3622
    • Ladenburger, E.M.1    Sehring, I.M.2    Korn, I.3    Plattner, H.4
  • 26
    • 0034018279 scopus 로고    scopus 로고
    • Membrane trafficking and processing in Paramecium
    • Allen RD, Fok AK, (2000) Membrane trafficking and processing in Paramecium. Int Rev Cytol 198: 277-318.
    • (2000) Int Rev Cytol , vol.198 , pp. 277-318
    • Allen, R.D.1    Fok, A.K.2
  • 27
    • 0025876729 scopus 로고
    • Cortical alveoli of Paramecium: a vast submembranous calcium storage compartment
    • Stelly N, Mauger JP, 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
  • 28
    • 0033807767 scopus 로고    scopus 로고
    • Sub-second quenched-flow/X-ray microanalysis shows rapid Ca2+ mobilization from cortical stores paralleled by Ca2+ influx during synchronous exocytosis in Paramecium cells
    • Hardt M, Plattner H, (2000) Sub-second quenched-flow/X-ray microanalysis shows rapid Ca2+ mobilization from cortical stores paralleled by Ca2+ 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
  • 29
    • 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, et al. (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
  • 30
    • 0002351563 scopus 로고
    • Cytology
    • In: Görtz H-D, editors, Berlin, Heidelberg, Springer-Verlag
    • Allen RD, (1988) Cytology. In: Görtz H-D, editors. Paramecium Berlin, Heidelberg Springer-Verlag pp. 4-40.
    • (1988) Paramecium , pp. 4-40
    • Allen, R.D.1
  • 31
    • 0033777003 scopus 로고    scopus 로고
    • The contractile vacuole and its membrane dynamics
    • Allen RD, (2000) The contractile vacuole and its membrane dynamics. Bioessays 22: 1035-1042.
    • (2000) Bioessays , vol.22 , pp. 1035-1042
    • Allen, R.D.1
  • 32
    • 0036749792 scopus 로고    scopus 로고
    • The ionic composition of the contractile vacuole fluid of Paramecium mirrors ion transport across the plasma membrane
    • Stock C, Gronlien HK, Allen RD, (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    Gronlien, H.K.2    Allen, R.D.3
  • 33
    • 0346256847 scopus 로고    scopus 로고
    • Molecular aspects of membrane trafficking in paramecium
    • Plattner H, Kissmehl R, (2003) Molecular aspects of membrane trafficking in paramecium. Int Rev Cytol 232: 185-216.
    • (2003) Int Rev Cytol , vol.232 , pp. 185-216
    • Plattner, H.1    Kissmehl, R.2
  • 34
    • 33847388051 scopus 로고    scopus 로고
    • Calcium: a fundamental regulator of intracellular membrane fusion?
    • Hay JC, (2007) Calcium: a fundamental regulator of intracellular membrane fusion? EMBO Rep 8: 236-240.
    • (2007) EMBO Rep , vol.8 , pp. 236-240
    • Hay, J.C.1
  • 36
    • 78651415502 scopus 로고    scopus 로고
    • Ion flux and the function of endosomes and lysosomes: pH is just the start: the flux of ions across endosomal membranes influences endosome function not only through regulation of the luminal pH
    • Scott CC, Gruenberg J, (2011) Ion flux and the function of endosomes and lysosomes: pH is just the start: the flux of ions across endosomal membranes influences endosome function not only through regulation of the luminal pH. Bioessays 33: 103-110.
    • (2011) Bioessays , vol.33 , pp. 103-110
    • Scott, C.C.1    Gruenberg, J.2
  • 37
    • 33846079515 scopus 로고    scopus 로고
    • ParameciumDB: a community resource that integrates the Paramecium tetraurelia genome sequence with genetic data
    • Arnaiz O, Cain S, Cohen J, Sperling L, (2007) ParameciumDB: a community resource that integrates the Paramecium tetraurelia genome sequence with genetic data. Nucleic Acids Res 35: D439-D444.
    • (2007) Nucleic Acids Res , vol.35 , pp. 439-444
    • Arnaiz, O.1    Cain, S.2    Cohen, J.3    Sperling, L.4
  • 39
    • 0031614678 scopus 로고    scopus 로고
    • A hidden Markov model for predicting transmembrane helices in protein sequences
    • Sonnhammer EL, von HG, Krogh A, (1998) A hidden Markov model for predicting transmembrane helices in protein sequences. Proc Int Conf Intell Syst Mol Biol 6: 175-182.
    • (1998) Proc Int Conf Intell Syst Mol Biol , vol.6 , pp. 175-182
    • Sonnhammer, E.L.1    von, H.G.2    Krogh, A.3
  • 40
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolittle RF, (1982) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157: 105-132.
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 41
    • 48249151108 scopus 로고    scopus 로고
    • OCTOPUS: improving topology prediction by two-track ANN-based preference scores and an extended topological grammar
    • Viklund H, Elofsson A, (2008) OCTOPUS: improving topology prediction by two-track ANN-based preference scores and an extended topological grammar. Bioinformatics 24: 1662-1668.
    • (2008) Bioinformatics , vol.24 , pp. 1662-1668
    • Viklund, H.1    Elofsson, A.2
  • 42
    • 3042579686 scopus 로고    scopus 로고
    • Best alpha-helical transmembrane protein topology predictions are achieved using hidden Markov models and evolutionary information
    • Viklund H, Elofsson A, (2004) Best alpha-helical transmembrane protein topology predictions are achieved using hidden Markov models and evolutionary information. Protein Sci 13: 1908-1917.
    • (2004) Protein Sci , vol.13 , pp. 1908-1917
    • Viklund, H.1    Elofsson, A.2
  • 44
    • 0035660460 scopus 로고    scopus 로고
    • Structural understanding of the transmembrane domains of inositol triphosphate receptors and ryanodine receptors towards calcium channeling
    • Shah PK, Sowdhamini R, (2001) Structural understanding of the transmembrane domains of inositol triphosphate receptors and ryanodine receptors towards calcium channeling. Protein Eng 14: 867-874.
    • (2001) Protein Eng , vol.14 , pp. 867-874
    • Shah, P.K.1    Sowdhamini, R.2
  • 45
    • 0035957945 scopus 로고    scopus 로고
    • Molecular determinants of ion permeation and selectivity in inositol 1,4,5-trisphosphate receptor Ca2+ channels
    • Boehning D, Mak DO, Foskett JK, Joseph SK, (2001) Molecular determinants of ion permeation and selectivity in inositol 1,4,5-trisphosphate receptor Ca2+ channels. J Biol Chem 276: 13509-13512.
    • (2001) J Biol Chem , vol.276 , pp. 13509-13512
    • Boehning, D.1    Mak, D.O.2    Foskett, J.K.3    Joseph, S.K.4
  • 46
    • 4544315705 scopus 로고    scopus 로고
    • Functional properties of a pore mutant in the Drosophila melanogaster inositol 1,4,5-trisphosphate receptor
    • Srikanth S, Wang Z, Hasan G, Bezprozvanny I, (2004) Functional properties of a pore mutant in the Drosophila melanogaster inositol 1,4,5-trisphosphate receptor. FEBS Lett 575: 95-98.
    • (2004) FEBS Lett , vol.575 , pp. 95-98
    • Srikanth, S.1    Wang, Z.2    Hasan, G.3    Bezprozvanny, I.4
  • 47
    • 0034981326 scopus 로고    scopus 로고
    • Light at the end of the Ca2+-release channel tunnel: structures and mechanisms involved in ion translocation in ryanodine receptor channels
    • Williams AJ, West DJ, Sitsapesan R, (2001) Light at the end of the Ca2+-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
  • 48
    • 0032811551 scopus 로고    scopus 로고
    • Location of the permeation pathway in the recombinant type 1 inositol 1,4,5-trisphosphate receptor
    • Ramos-Franco J, Galvan D, Mignery GA, Fill M, (1999) Location of the permeation pathway in the recombinant type 1 inositol 1,4,5-trisphosphate receptor. J Gen Physiol 114: 243-250.
    • (1999) J Gen Physiol , vol.114 , pp. 243-250
    • Ramos-Franco, J.1    Galvan, D.2    Mignery, G.A.3    Fill, M.4
  • 49
    • 33749563056 scopus 로고    scopus 로고
    • Protein evolution is faster outside the cell
    • Julenius K, Pedersen AG, (2006) Protein evolution is faster outside the cell. Mol Biol Evol 23: 2039-2048.
    • (2006) Mol Biol Evol , vol.23 , pp. 2039-2048
    • Julenius, K.1    Pedersen, A.G.2
  • 50
    • 70449555146 scopus 로고    scopus 로고
    • Structural imperatives impose diverse evolutionary constraints on helical membrane proteins
    • Oberai A, Joh NH, Pettit FK, Bowie JU, (2009) Structural imperatives impose diverse evolutionary constraints on helical membrane proteins. Proc Natl Acad Sci U S A 106: 17747-17750.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 17747-17750
    • Oberai, A.1    Joh, N.H.2    Pettit, F.K.3    Bowie, J.U.4
  • 51
    • 38349125022 scopus 로고    scopus 로고
    • Translational control of intron splicing in eukaryotes
    • Jaillon O, Bouhouche K, Gout JF, Aury JM, Noel B, et al. (2008) Translational control of intron splicing in eukaryotes. Nature 451: 359-362.
    • (2008) Nature , vol.451 , pp. 359-362
    • Jaillon, O.1    Bouhouche, K.2    Gout, J.F.3    Aury, J.M.4    Noel, B.5
  • 52
    • 0028287567 scopus 로고
    • Extremely short 20-33 nucleotide introns are the standard length in Paramecium tetraurelia
    • Russell CB, Fraga D, Hinrichsen RD, (1994) Extremely short 20-33 nucleotide introns are the standard length in Paramecium tetraurelia. Nucleic Acids Res 22: 1221-1225.
    • (1994) Nucleic Acids Res , vol.22 , pp. 1221-1225
    • Russell, C.B.1    Fraga, D.2    Hinrichsen, R.D.3
  • 54
    • 0034002955 scopus 로고    scopus 로고
    • Changes in the endoplasmic reticulum structure of Paramecium primaurelia in relation to different cellular physiological states
    • Ramoino P, Diaspro A, Fato M, Beltrame F, Robello M, (2000) Changes in the endoplasmic reticulum structure of Paramecium primaurelia in relation to different cellular physiological states. J Photochem Photobiol B 54: 35-42.
    • (2000) J Photochem Photobiol B , vol.54 , pp. 35-42
    • Ramoino, P.1    Diaspro, A.2    Fato, M.3    Beltrame, F.4    Robello, M.5
  • 55
    • 1242298679 scopus 로고    scopus 로고
    • Subcellular distribution of the inositol 1,4,5-trisphosphate receptors: functional relevance and molecular determinants
    • Vermassen E, Parys JB, Mauger JP, (2004) Subcellular distribution of the inositol 1,4,5-trisphosphate receptors: functional relevance and molecular determinants. Biol Cell 96: 3-17.
    • (2004) Biol Cell , vol.96 , pp. 3-17
    • Vermassen, E.1    Parys, J.B.2    Mauger, J.P.3
  • 56
    • 0035544602 scopus 로고    scopus 로고
    • Phagosome formation in Paramecium: roles of somatic and oral cilia and of solid particles as revealed by video microscopy
    • Ishida M, Allen RD, Fok AK, (2001) Phagosome formation in Paramecium: roles of somatic and oral cilia and of solid particles as revealed by video microscopy. J Eukaryot Microbiol 48: 640-646.
    • (2001) J Eukaryot Microbiol , vol.48 , pp. 640-646
    • Ishida, M.1    Allen, R.D.2    Fok, A.K.3
  • 57
    • 0026528046 scopus 로고
    • Endosomal system of Paramecium: coated pits to early endosomes
    • Allen RD, Schroeder CC, Fok AK, (1992) Endosomal system of Paramecium: coated pits to early endosomes. J Cell Sci 101 (Pt 2): 449-461.
    • (1992) J Cell Sci , vol.101 , Issue.PART 2 , pp. 449-461
    • Allen, R.D.1    Schroeder, C.C.2    Fok, A.K.3
  • 58
    • 33750858684 scopus 로고    scopus 로고
    • Global trends of whole-genome duplications revealed by the ciliate Paramecium tetraurelia
    • Aury JM, Jaillon O, Duret L, Noel B, Jubin C, et al. (2006) Global trends of whole-genome duplications revealed by the ciliate Paramecium tetraurelia. Nature 444: 171-178.
    • (2006) Nature , vol.444 , pp. 171-178
    • Aury, J.M.1    Jaillon, O.2    Duret, L.3    Noel, B.4    Jubin, C.5
  • 59
    • 0033852724 scopus 로고    scopus 로고
    • Green fluorescent protein-tagged sarco(endo)plasmic reticulum Ca2+-ATPase overexpression in Paramecium cells: isoforms, subcellular localization, biogenesis of cortical calcium stores and functional aspects
    • Hauser K, Pavlovic N, Klauke N, Geissinger D, Plattner H, (2000) Green fluorescent protein-tagged sarco(endo)plasmic reticulum Ca2+-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
  • 60
    • 77957946461 scopus 로고    scopus 로고
    • Membrane trafficking in protozoa SNARE proteins, H+-ATPase, actin, and other key players in ciliates
    • Plattner H, (2010) Membrane trafficking in protozoa SNARE proteins, H+-ATPase, actin, and other key players in ciliates. Int Rev Cell Mol Biol 280: 79-184.
    • (2010) Int Rev Cell Mol Biol , vol.280 , pp. 79-184
    • Plattner, H.1
  • 61
    • 0037067181 scopus 로고    scopus 로고
    • Synaptotagmin II could confer Ca2+ sensitivity to phagocytosis in human neutrophils
    • Lindmark IM, Karlsson A, Serrander L, Francois P, Lew D, et al. (2002) Synaptotagmin II could confer Ca2+ sensitivity to phagocytosis in human neutrophils. Biochim Biophys Acta 1590: 159-166.
    • (2002) Biochim Biophys Acta , vol.1590 , pp. 159-166
    • Lindmark, I.M.1    Karlsson, A.2    Serrander, L.3    Francois, P.4    Lew, D.5
  • 62
    • 54049128127 scopus 로고    scopus 로고
    • The exocytosis regulator synaptotagmin V controls phagocytosis in macrophages
    • Vinet AF, Fukuda M, Descoteaux A, (2008) The exocytosis regulator synaptotagmin V controls phagocytosis in macrophages. J Immunol 181: 5289-5295.
    • (2008) J Immunol , vol.181 , pp. 5289-5295
    • Vinet, A.F.1    Fukuda, M.2    Descoteaux, A.3
  • 63
    • 38149012305 scopus 로고    scopus 로고
    • Counting functional inositol 1,4,5-trisphosphate receptors into the plasma membrane
    • Dellis O, Rossi AM, Dedos SG, Taylor CW, (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
  • 64
    • 0025731040 scopus 로고
    • Large conductance calcium-activated non-selective cation channel in smooth muscle cells isolated from rat portal vein
    • Loirand G, Pacaud P, Baron A, Mironneau C, Mironneau J, (1991) Large conductance calcium-activated non-selective cation channel in smooth muscle cells isolated from rat portal vein. J Physiol 437: 461-475.
    • (1991) J Physiol , vol.437 , pp. 461-475
    • Loirand, G.1    Pacaud, P.2    Baron, A.3    Mironneau, C.4    Mironneau, J.5
  • 65
    • 0000017069 scopus 로고
    • Electrophysiology
    • In: Görtz H-D, editors, Berlin, Heidelberg, Springer-Verlag
    • Machemer H, (1988) Electrophysiology. In: Görtz H-D, editors. Paramecium Berlin, Heidelberg Springer-Verlag pp. 185-215.
    • (1988) Paramecium , pp. 185-215
    • Machemer, H.1
  • 66
    • 0031011668 scopus 로고    scopus 로고
    • Extracellular calcium sensed by a novel cation channel in hippocampal neurons
    • Xiong Z, Lu W, MacDonald JF, (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
  • 67
    • 0030614350 scopus 로고    scopus 로고
    • Microdomain Ca2+ activation during exocytosis in Paramecium cells. Superposition of local subplasmalemmal calcium store activation by local Ca2+ influx
    • Erxleben C, Klauke N, Flotenmeyer M, Blanchard MP, Braun C, et al. (1997) Microdomain Ca2+ activation during exocytosis in Paramecium cells. Superposition of local subplasmalemmal calcium store activation by local Ca2+ influx. J Cell Biol 136: 597-607.
    • (1997) J Cell Biol , vol.136 , pp. 597-607
    • Erxleben, C.1    Klauke, N.2    Flotenmeyer, M.3    Blanchard, M.P.4    Braun, C.5
  • 68
    • 1642523571 scopus 로고    scopus 로고
    • Distinct roles of inositol 1,4,5-trisphosphate receptor types 1 and 3 in Ca2+ signaling
    • Hattori M, Suzuki AZ, Higo T, Miyauchi H, Michikawa T, et al. (2004) Distinct roles of inositol 1,4,5-trisphosphate receptor types 1 and 3 in Ca2+ signaling. J Biol Chem 279: 11967-11975.
    • (2004) J Biol Chem , vol.279 , pp. 11967-11975
    • Hattori, M.1    Suzuki, A.Z.2    Higo, T.3    Miyauchi, H.4    Michikawa, T.5
  • 69
    • 0031003487 scopus 로고    scopus 로고
    • Dynamics of calcium regulation in Paramecium and possible morphogenetic implication
    • Prajer M, Fleury A, Laurent M, (1997) Dynamics of calcium regulation in Paramecium and possible morphogenetic implication. J Cell Sci 110 (Pt 5): 529-535.
    • (1997) J Cell Sci , vol.110 , Issue.PART 5 , pp. 529-535
    • Prajer, M.1    Fleury, A.2    Laurent, M.3
  • 71
    • 79955527115 scopus 로고    scopus 로고
    • Endocytic membrane fusion and buckling-induced microtubule severing mediate cell abscission
    • Schiel JA, Park K, Morphew MK, Reid E, Hoenger A, et al. (2011) Endocytic membrane fusion and buckling-induced microtubule severing mediate cell abscission. J Cell Sci 124: 1411-1424.
    • (2011) J Cell Sci , vol.124 , pp. 1411-1424
    • Schiel, J.A.1    Park, K.2    Morphew, M.K.3    Reid, E.4    Hoenger, A.5
  • 72
    • 0029583423 scopus 로고
    • A localized elevation of cytosolic free calcium is associated with cytokinesis in the zebrafish embryo
    • Chang DC, Meng C, (1995) A localized elevation of cytosolic free calcium is associated with cytokinesis in the zebrafish embryo. J Cell Biol 131: 1539-1545.
    • (1995) J Cell Biol , vol.131 , pp. 1539-1545
    • Chang, D.C.1    Meng, C.2
  • 73
    • 23244432630 scopus 로고    scopus 로고
    • PIP2 hydrolysis and calcium release are required for cytokinesis in Drosophila spermatocytes
    • Wong R, Hadjiyanni I, Wei HC, Polevoy G, McBride R, et al. (2005) PIP2 hydrolysis and calcium release are required for cytokinesis in Drosophila spermatocytes. Curr Biol 15: 1401-1406.
    • (2005) Curr Biol , vol.15 , pp. 1401-1406
    • Wong, R.1    Hadjiyanni, I.2    Wei, H.C.3    Polevoy, G.4    McBride, R.5
  • 74
    • 0037107589 scopus 로고    scopus 로고
    • NSF regulates membrane traffic along multiple pathways in Paramecium
    • Kissmehl R, Froissard M, Plattner H, Momayezi M, Cohen J, (2002) NSF regulates membrane traffic along multiple pathways in Paramecium. J Cell Sci 115: 3935-3946.
    • (2002) J Cell Sci , vol.115 , pp. 3935-3946
    • Kissmehl, R.1    Froissard, M.2    Plattner, H.3    Momayezi, M.4    Cohen, J.5
  • 75
    • 75849116774 scopus 로고    scopus 로고
    • Distinct subcellular localization of a group of synaptobrevin-like SNAREs in Paramecium tetraurelia and effects of silencing SNARE-specific chaperone NSF
    • Schilde C, Schonemann B, Sehring IM, Plattner H, (2010) Distinct subcellular localization of a group of synaptobrevin-like SNAREs in Paramecium tetraurelia and effects of silencing SNARE-specific chaperone NSF. Eukaryot Cell 9: 288-305.
    • (2010) Eukaryot Cell , vol.9 , pp. 288-305
    • Schilde, C.1    Schonemann, B.2    Sehring, I.M.3    Plattner, H.4
  • 76
    • 0344428151 scopus 로고    scopus 로고
    • Immunolabeling analysis of biosynthetic and degradative pathways of cell surface components (glycocalyx) in Paramecium cells
    • Flötenmeyer M, Momayezi M, Plattner H, (1999) Immunolabeling analysis of biosynthetic and degradative pathways of cell surface components (glycocalyx) in Paramecium cells. Eur J Cell Biol 78: 67-77.
    • (1999) Eur J Cell Biol , vol.78 , pp. 67-77
    • Flötenmeyer, M.1    Momayezi, M.2    Plattner, H.3
  • 77
    • 77952671939 scopus 로고    scopus 로고
    • TPCs: Endolysosomal channels for Ca2+ mobilization from acidic organelles triggered by NAADP
    • Zhu MX, Ma J, Parrington J, Galione A, Evans AM, (2010) TPCs: Endolysosomal channels for Ca2+ mobilization from acidic organelles triggered by NAADP. FEBS Lett 584: 1966-1974.
    • (2010) FEBS Lett , vol.584 , pp. 1966-1974
    • Zhu, M.X.1    Ma, J.2    Parrington, J.3    Galione, A.4    Evans, A.M.5
  • 78
    • 33748989031 scopus 로고    scopus 로고
    • Ca2+ and synaptotagmin VII-dependent delivery of lysosomal membrane to nascent phagosomes
    • Czibener C, Sherer NM, Becker SM, Pypaert M, Hui E, et al. (2006) Ca2+ and synaptotagmin VII-dependent delivery of lysosomal membrane to nascent phagosomes. J Cell Biol 174: 997-1007.
    • (2006) J Cell Biol , vol.174 , pp. 997-1007
    • Czibener, C.1    Sherer, N.M.2    Becker, S.M.3    Pypaert, M.4    Hui, E.5
  • 79
    • 0032506349 scopus 로고    scopus 로고
    • Ca2+/calmodulin signals the completion of docking and triggers a late step of vacuole fusion
    • Peters C, Mayer A, (1998) Ca2+/calmodulin signals the completion of docking and triggers a late step of vacuole fusion. Nature 396: 575-580.
    • (1998) Nature , vol.396 , pp. 575-580
    • Peters, C.1    Mayer, A.2
  • 80
    • 34548188753 scopus 로고    scopus 로고
    • Targeting and retention of type 1 ryanodine receptors to the endoplasmic reticulum
    • Meur G, Parker AK, Gergely FV, Taylor CW, (2007) Targeting and retention of type 1 ryanodine receptors to the endoplasmic reticulum. J Biol Chem 282: 23096-23103.
    • (2007) J Biol Chem , vol.282 , pp. 23096-23103
    • Meur, G.1    Parker, A.K.2    Gergely, F.V.3    Taylor, C.W.4
  • 81
    • 79959554451 scopus 로고    scopus 로고
    • Differential distribution, clustering and lateral diffusion of subtypes of inositol 1,4,5-trisphosphate receptor
    • Pantazaka E, Taylor CW, (2011) Differential distribution, clustering and lateral diffusion of subtypes of inositol 1,4,5-trisphosphate receptor. J Biol Chem.
    • (2011) J Biol Chem
    • Pantazaka, E.1    Taylor, C.W.2
  • 83
    • 34247463919 scopus 로고    scopus 로고
    • Molecular identification of 26 syntaxin genes and their assignment to the different trafficking pathways in Paramecium
    • Kissmehl R, Schilde C, Wassmer T, Danzer C, Nuehse K, et al. (2007) Molecular identification of 26 syntaxin genes and their assignment to the different trafficking pathways in Paramecium. Traffic 8: 523-542.
    • (2007) Traffic , vol.8 , pp. 523-542
    • Kissmehl, R.1    Schilde, C.2    Wassmer, T.3    Danzer, C.4    Nuehse, K.5
  • 84
    • 33644887166 scopus 로고    scopus 로고
    • A multigene family encoding R-SNAREs in the ciliate Paramecium tetraurelia
    • Schilde C, Wassmer T, Mansfeld J, Plattner H, Kissmehl R, (2006) A multigene family encoding R-SNAREs in the ciliate Paramecium tetraurelia. Traffic 7: 440-455.
    • (2006) Traffic , vol.7 , pp. 440-455
    • Schilde, C.1    Wassmer, T.2    Mansfeld, J.3    Plattner, H.4    Kissmehl, R.5
  • 85
    • 78449255389 scopus 로고    scopus 로고
    • Comprehensive analysis reveals dynamic and evolutionary plasticity of Rab GTPases and membrane traffic in Tetrahymena thermophila
    • Bright LJ, Kambesis N, Nelson SB, Jeong B, Turkewitz AP, (2010) Comprehensive analysis reveals dynamic and evolutionary plasticity of Rab GTPases and membrane traffic in Tetrahymena thermophila. PLoS Genet 6: e1001155.
    • (2010) PLoS Genet , vol.6
    • Bright, L.J.1    Kambesis, N.2    Nelson, S.B.3    Jeong, B.4    Turkewitz, A.P.5
  • 86
    • 9244219677 scopus 로고    scopus 로고
    • Inositol 1,4,5-trisphosphate and ryanodine receptors mobilize calcium from a common functional pool in human U373 MG cells
    • Galiano M, Gasparre G, Lippe C, Cassano G, (2004) Inositol 1,4,5-trisphosphate and ryanodine receptors mobilize calcium from a common functional pool in human U373 MG cells. Cell Calcium 36: 359-365.
    • (2004) Cell Calcium , vol.36 , pp. 359-365
    • Galiano, M.1    Gasparre, G.2    Lippe, C.3    Cassano, G.4
  • 87
    • 43749107122 scopus 로고    scopus 로고
    • A single luminally continuous sarcoplasmic reticulum with apparently separate Ca2+ stores in smooth muscle
    • McCarron JG, Olson ML, (2008) A single luminally continuous sarcoplasmic reticulum with apparently separate Ca2+ stores in smooth muscle. J Biol Chem 283: 7206-7218.
    • (2008) J Biol Chem , vol.283 , pp. 7206-7218
    • McCarron, J.G.1    Olson, M.L.2
  • 88
    • 0042166005 scopus 로고    scopus 로고
    • Neuronal endoplasmic reticulum acts as a single functional Ca2+ store shared by ryanodine and inositol-1,4,5-trisphosphate receptors as revealed by intra-ER [Ca2+] recordings in single rat sensory neurones
    • Solovyova N, Verkhratsky A, (2003) Neuronal endoplasmic reticulum acts as a single functional Ca2+ store shared by ryanodine and inositol-1,4,5-trisphosphate receptors as revealed by intra-ER [Ca2+] recordings in single rat sensory neurones. Pflugers Arch 446: 447-454.
    • (2003) Pflugers Arch , vol.446 , pp. 447-454
    • Solovyova, N.1    Verkhratsky, A.2
  • 89
    • 0033781387 scopus 로고    scopus 로고
    • Evidence for splice site pairing via intron definition in Schizosaccharomyces pombe
    • Romfo CM, Alvarez CJ, van Heeckeren WJ, Webb CJ, Wise JA, (2000) Evidence for splice site pairing via intron definition in Schizosaccharomyces pombe. Mol Cell Biol 20: 7955-7970.
    • (2000) Mol Cell Biol , vol.20 , pp. 7955-7970
    • Romfo, C.M.1    Alvarez, C.J.2    van Heeckeren, W.J.3    Webb, C.J.4    Wise, J.A.5
  • 90
    • 2342456308 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay: terminating erroneous gene expression
    • Baker KE, Parker R, (2004) Nonsense-mediated mRNA decay: terminating erroneous gene expression. Curr Opin Cell Biol 16: 293-299.
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 293-299
    • Baker, K.E.1    Parker, R.2
  • 91
    • 33846804142 scopus 로고    scopus 로고
    • A broad spectrum of actin paralogs in Paramecium tetraurelia cells display differential localization and function
    • Sehring IM, Reiner C, Mansfeld J, Plattner H, Kissmehl R, (2007) A broad spectrum of actin paralogs in Paramecium tetraurelia cells display differential localization and function. J Cell Sci 120: 177-190.
    • (2007) J Cell Sci , vol.120 , pp. 177-190
    • Sehring, I.M.1    Reiner, C.2    Mansfeld, J.3    Plattner, H.4    Kissmehl, R.5
  • 92
    • 38349161170 scopus 로고    scopus 로고
    • Functional diversification of centrins and cell morphological complexity
    • Gogendeau D, Klotz C, Arnaiz O, Malinowska A, Dadlez M, et al. (2008) Functional diversification of centrins and cell morphological complexity. J Cell Sci 121: 65-74.
    • (2008) J Cell Sci , vol.121 , pp. 65-74
    • Gogendeau, D.1    Klotz, C.2    Arnaiz, O.3    Malinowska, A.4    Dadlez, M.5
  • 93
    • 4143067041 scopus 로고    scopus 로고
    • High coding density on the largest Paramecium tetraurelia somatic chromosome
    • Zagulski M, Nowak JK, Le MA, Nowacki M, Migdalski A, et al. (2004) High coding density on the largest Paramecium tetraurelia somatic chromosome. Curr Biol 14: 1397-1404.
    • (2004) Curr Biol , vol.14 , pp. 1397-1404
    • Zagulski, M.1    Nowak, J.K.2    Le, M.A.3    Nowacki, M.4    Migdalski, A.5
  • 94
    • 0000225464 scopus 로고
    • Paramecium aurelia
    • In: Kung C, editors, New York, Plenum Press
    • Sonneborn TM, (1974) Paramecium aurelia. In: Kung C, editors. Handbook of Genetics, Vol. 2 New York Plenum Press pp. 469-594.
    • (1974) Handbook of Genetics, Vol. 2 , pp. 469-594
    • Sonneborn, T.M.1
  • 95
    • 0018351979 scopus 로고
    • The fatty-acid composition of Paramecium aurelia cells and cilia - changes with culture age
    • Kaneshiro ES, Beischel LS, Merkel SJ, Rhoads DE, (1979) The fatty-acid composition of Paramecium aurelia cells and cilia- changes with culture age. Journal of Protozoology 26: 147-158.
    • (1979) Journal of Protozoology , vol.26 , pp. 147-158
    • Kaneshiro, E.S.1    Beischel, L.S.2    Merkel, S.J.3    Rhoads, D.E.4
  • 96
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    • Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, et al. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 25: 3389-3402.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5
  • 97
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ, (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 98
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: Integrated software for Molecular Evolutionary Genetics Analysis and sequence alignment
    • Kumar S, Tamura K, Nei M, (2004) MEGA3: Integrated software for Molecular Evolutionary Genetics Analysis and sequence alignment. Brief Bioinform 5: 150-163.
    • (2004) Brief Bioinform , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 99
    • 33244495782 scopus 로고    scopus 로고
    • Accuracy of coalescent likelihood estimates: do we need more sites, more sequences, or more loci?
    • Felsenstein J, (2006) Accuracy of coalescent likelihood estimates: do we need more sites, more sequences, or more loci? Mol Biol Evol 23: 691-700.
    • (2006) Mol Biol Evol , vol.23 , pp. 691-700
    • Felsenstein, J.1
  • 100
    • 0000063837 scopus 로고
    • Use of polymerase chain reaction for the rapid construction of synthetic genes
    • Dillon PJ, Rosen CA, (1993) Use of polymerase chain reaction for the rapid construction of synthetic genes. Methods Mol Biol 15: 263-268.
    • (1993) Methods Mol Biol , vol.15 , pp. 263-268
    • Dillon, P.J.1    Rosen, C.A.2
  • 101
    • 8744300794 scopus 로고    scopus 로고
    • Cloning of ß-tubulin and succinate dehydrogenase genes from Uromyces fabae and establishing selection conditions for their use in transformation
    • Wirsel SGR, Vögele R, Bänninger R, Mendgen KW, (2004) Cloning of ß-tubulin and succinate dehydrogenase genes from Uromyces fabae and establishing selection conditions for their use in transformation. Eur J Plant Pathol 110: 767-777.
    • (2004) Eur J Plant Pathol , vol.110 , pp. 767-777
    • Wirsel, S.G.R.1    Vögele, R.2    Bänninger, R.3    Mendgen, K.W.4
  • 103
    • 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
  • 104
    • 0029197093 scopus 로고
    • Preparation of cilia and subciliary fractions from Paramecium
    • Nelson DL, (1995) Preparation of cilia and subciliary fractions from Paramecium. Methods Cell Biol 47: 17-24.
    • (1995) Methods Cell Biol , vol.47 , pp. 17-24
    • Nelson, D.L.1
  • 105
    • 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, (1991) 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.