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Volumn 8, Issue 5, 2007, Pages 523-542

Molecular identification of 26 syntaxin genes and their assignment to the different trafficking pathways in paramecium

Author keywords

Exocytosis; Golgi; Paramecium; SNAREs; Syntaxin

Indexed keywords

AMINO ACID; GREEN FLUORESCENT PROTEIN; ISOPROTEIN; MEMBRANE PROTEIN; SNARE PROTEIN; SYNTAXIN;

EID: 34247463919     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2007.00544.x     Document Type: Article
Times cited : (42)

References (102)
  • 2
    • 0344393030 scopus 로고    scopus 로고
    • SNARE protein structure and function
    • Ungar D, Hughson FM. SNARE protein structure and function. Annu Rev Cell Dev Biol 2003; 19: 493-517.
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 493-517
    • Ungar, D.1    Hughson, F.M.2
  • 3
    • 20444407298 scopus 로고    scopus 로고
    • SNAREs and traffic
    • Hong W. SNAREs and traffic. Biochim Biophys Acta 2005; 1744: 120-144.
    • (2005) Biochim Biophys Acta , vol.1744 , pp. 120-144
    • Hong, W.1
  • 4
    • 0027517462 scopus 로고
    • A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion
    • Söllner T, Bennett MK, Whiteheart SW, Scheller RH, Rothman JE. A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion. Cell 1993; 75: 409-418.
    • (1993) Cell , vol.75 , pp. 409-418
    • Söllner, T.1    Bennett, M.K.2    Whiteheart, S.W.3    Scheller, R.H.4    Rothman, J.E.5
  • 6
    • 0030846539 scopus 로고    scopus 로고
    • Neurotransmitter release-four years of SNARE complexes
    • Hanson PI, Heuser JE, Jahn R. Neurotransmitter release-four years of SNARE complexes. Curr Opin Neurobiol 1997; 7: 310-315.
    • (1997) Curr Opin Neurobiol , vol.7 , pp. 310-315
    • Hanson, P.I.1    Heuser, J.E.2    Jahn, R.3
  • 7
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution
    • Sutton RB, Fasshauer D, Jahn R, Brunger AT. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution. Nature 1998; 395: 347-353.
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 9
    • 0033749565 scopus 로고    scopus 로고
    • Testing the 3Q:1R "rule": Mutational analysis of the ionic "zero"layer in the yeast exocytic SNARE complex reveals no requirement for arginine
    • Katz L, BrennwMld P. Testing the 3Q:1R "rule": mutational analysis of the ionic "zero"layer in the yeast exocytic SNARE complex reveals no requirement for arginine. Mol Biol Cell 2000; 11: 3849-3858.
    • (2000) Mol Biol Cell , vol.11 , pp. 3849-3858
    • Katz, L.1    Brennwald, P.2
  • 10
    • 0032430423 scopus 로고    scopus 로고
    • Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs
    • Fasshauer D, Sutton RB, Brunger AT, Jahn R. Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs. Proc Natl Acad Sci U S A 1998; 95: 15781-15786.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 15781-15786
    • Fasshauer, D.1    Sutton, R.B.2    Brunger, A.T.3    Jahn, R.4
  • 11
    • 0035865345 scopus 로고    scopus 로고
    • A genomic perspective on membrane compartment organization
    • Bock JB, Matern HT, Peden AA, Scheller RH. A genomic perspective on membrane compartment organization. Nature 2001; 409: 839-841.
    • (2001) Nature , vol.409 , pp. 839-841
    • Bock, J.B.1    Matern, H.T.2    Peden, A.A.3    Scheller, R.H.4
  • 13
    • 0742272120 scopus 로고    scopus 로고
    • A complete set of SNAREs in yeast
    • Burri L, Lithgow T. A complete set of SNAREs in yeast. Traffic 2004; 5: 45-52.
    • (2004) Traffic , vol.5 , pp. 45-52
    • Burri, L.1    Lithgow, T.2
  • 14
    • 0034018279 scopus 로고    scopus 로고
    • Membrane trafficking and processing in Paramecium
    • Allen RD, Fok AK. Membrane trafficking and processing in Paramecium. Int Rev Cytol 2000; 198: 277-318.
    • (2000) Int Rev Cytol , vol.198 , pp. 277-318
    • Allen, R.D.1    Fok, A.K.2
  • 15
    • 0346256847 scopus 로고    scopus 로고
    • Molecular aspects of membrane trafficking in Paramecium
    • Plattner H, Kissmehl R. Molecular aspects of membrane trafficking in Paramecium. Int Rev Cytol 2003; 232: 185-216.
    • (2003) Int Rev Cytol , vol.232 , pp. 185-216
    • Plattner, H.1    Kissmehl, R.2
  • 16
    • 0026528046 scopus 로고
    • Endosomal system of Paramecium: Coated pits to early endosomes
    • Allen RD, Schroeder CC, Fok AK. Endosomal system of Paramecium: Coated pits to early endosomes. J Cell Sci 1992; 101: 449-461.
    • (1992) J Cell Sci , vol.101 , pp. 449-461
    • Allen, R.D.1    Schroeder, C.C.2    Fok, A.K.3
  • 17
    • 55449130503 scopus 로고    scopus 로고
    • Elucidation of clathrin-mediated endocytosis in TETRAHYMENA reveals an evolutionarily convergent recruitment of dynamin
    • Elde NC, Morgan G, Winey M, Sperling L, Turkewitz AP. Elucidation of clathrin-mediated endocytosis in TETRAHYMENA reveals an evolutionarily convergent recruitment of dynamin. PLoS Genet 2005; 1: E52.
    • (2005) PLoS Genet , vol.1
    • Elde, N.C.1    Morgan, G.2    Winey, M.3    Sperling, L.4    Turkewitz, A.P.5
  • 18
    • 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. Immunolabeling analysis of biosynthetic and degradative pathways of cell surface components (glycocalyx) in Paramecium cells. Eur J Cell Biol 1999; 78: 67-77.
    • (1999) Eur J Cell Biol , vol.78 , pp. 67-77
    • Flötenmeyer, M.1    Momayezi, M.2    Plattner, H.3
  • 19
    • 0034122147 scopus 로고    scopus 로고
    • Molecular genetics of regulated secretion in Paramecium
    • VayssiéL, Skouri F, Sperling L, Cohen J. Molecular genetics of regulated secretion in Paramecium. Biochimie 2000; 82: 269-288.
    • (2000) Biochimie , vol.82 , pp. 269-288
    • Vayssie, L.1    Skouri, F.2    Sperling, L.3    Cohen, J.4
  • 20
    • 0041659178 scopus 로고    scopus 로고
    • Dense-core secretory vesicle docking and exocytotic membrane fusion in Paramecium cells
    • Plattner H, Kissmehl R. Dense-core secretory vesicle docking and exocytotic membrane fusion in Paramecium cells. Biochim Biophys Acta 2003; 1641: 183-193.
    • (2003) Biochim Biophys Acta , vol.1641 , pp. 183-193
    • Plattner, H.1    Kissmehl, R.2
  • 21
    • 0016289173 scopus 로고
    • Food vacuole membrane growth with microtubule-associated membrane transport in Paramecium
    • Allen RD. Food vacuole membrane growth with microtubule-associated membrane transport in Paramecium. J Cell Biol 1974; 63: 904-922.
    • (1974) J Cell Biol , vol.63 , pp. 904-922
    • Allen, R.D.1
  • 22
    • 0036204472 scopus 로고    scopus 로고
    • Osmoregulation and contractile vacuoles of protozoa
    • Allen RD, Naitoh Y. Osmoregulation and contractile vacuoles of protozoa. Int Rev Cytol 2002; 215: 351-394.
    • (2002) Int Rev Cytol , vol.215 , pp. 351-394
    • Allen, R.D.1    Naitoh, Y.2
  • 23
    • 0033777003 scopus 로고    scopus 로고
    • The contractile vacuole and its membrane dynamics
    • Allen RD. The contractile vacuole and its membrane dynamics. Bioessays 2000; 22: 1035-1042.
    • (2000) Bioessays , vol.22 , pp. 1035-1042
    • Allen, R.D.1
  • 24
    • 0035989389 scopus 로고    scopus 로고
    • N-ethylmaleimide-sensitive factor is required to organize functional exocytotic microdomains in Paramecium
    • Froissard M, Kissmehl R, Dedieu JC, Gulik-Krzywicki T, Plattner H, Cohen J. N-ethylmaleimide-sensitive factor is required to organize functional exocytotic microdomains in Paramecium. Genetics 2002; 161: 643-650.
    • (2002) Genetics , vol.161 , pp. 643-650
    • Froissard, M.1    Kissmehl, R.2    Dedieu, J.C.3    Gulik-Krzywicki, T.4    Plattner, H.5    Cohen, J.6
  • 25
    • 0037107589 scopus 로고    scopus 로고
    • NSF regulates membrane traffic along multiple pathways in Paramecium
    • Kissmehl R, Froissard M, Plattner H, Momayezi M, Cohen J. NSF regulates membrane traffic along multiple pathways in Paramecium. J Cell Sci 2002; 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
  • 26
    • 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. A multigene family encoding R-SNAREs in the ciliate Paramecium tetraurelia. Traffic 2006; 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
  • 28
    • 0028287567 scopus 로고
    • Extremely short 20-33 nucleotide introns are the standard length in Paramecium tetraurelia
    • Russell CB, Fraga D, Hinrichsen RD. Extremely short 20-33 nucleotide introns are the standard length in Paramecium tetraurelia. Nucleic Acids Res 1994; 22: 1221-1225.
    • (1994) Nucleic Acids Res , vol.22 , pp. 1221-1225
    • Russell, C.B.1    Fraga, D.2    Hinrichsen, R.D.3
  • 33
    • 0036166318 scopus 로고    scopus 로고
    • Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs
    • Antonin W, Fasshauer D, Becker S, Jahn R, Schneider TR. Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs. Nat Struct Biol 2002; 9: 107-111.
    • (2002) Nat Struct Biol , vol.9 , pp. 107-111
    • Antonin, W.1    Fasshauer, D.2    Becker, S.3    Jahn, R.4    Schneider, T.R.5
  • 36
    • 0032544441 scopus 로고    scopus 로고
    • Three-dimensional structure of an evolutionarily conserved N-terminal domain of syntaxin 1A
    • Fernandez I, Ubach J, Dulubova I, Zhang X, Sudhof TC, Rizo J. Three-dimensional structure of an evolutionarily conserved N-terminal domain of syntaxin 1A. Cell 1998; 94: 841-849.
    • (1998) Cell , vol.94 , pp. 841-849
    • Fernandez, I.1    Ubach, J.2    Dulubova, I.3    Zhang, X.4    Sudhof, T.C.5    Rizo, J.6
  • 37
    • 0035918229 scopus 로고    scopus 로고
    • Self-association of the H3 region of syntaxin 1A. Implications for intermediates in SNARE complex assembly
    • Misura KM, Scheller RH, Weis WI. Self-association of the H3 region of syntaxin 1A. Implications for intermediates in SNARE complex assembly. J Biol Chem 2001; 276: 13273-13282.
    • (2001) J Biol Chem , vol.276 , pp. 13273-13282
    • Misura, K.M.1    Scheller, R.H.2    Weis, W.I.3
  • 38
  • 39
    • 0029990362 scopus 로고    scopus 로고
    • Reconstitution of transcytosis in SLO-permeabilized MDCK cells: Existence of an NSF-dependent fusion mechanism with the apical surface of MDCK cells
    • Apodaca G, Cardone MH, Whiteheart SW, DasGupta BR, Mostov KE. Reconstitution of transcytosis in SLO-permeabilized MDCK cells: existence of an NSF-dependent fusion mechanism with the apical surface of MDCK cells. EMBO J 1996; 15: 1471-1481.
    • (1996) EMBO J , vol.15 , pp. 1471-1481
    • Apodaca, G.1    Cardone, M.H.2    Whiteheart, S.W.3    DasGupta, B.R.4    Mostov, K.E.5
  • 40
    • 0029847075 scopus 로고    scopus 로고
    • Differential localization of syntaxin isoforms in polarized Madin-Darby canine kidney cells
    • Low SH, Chapin SJ, Weimbs T, Komuves LG, Bennett MK, Mostov KE. Differential localization of syntaxin isoforms in polarized Madin-Darby canine kidney cells. Mol Biol Cell 1996; 7: 2007-2018.
    • (1996) Mol Biol Cell , vol.7 , pp. 2007-2018
    • Low, S.H.1    Chapin, S.J.2    Weimbs, T.3    Komuves, L.G.4    Bennett, M.K.5    Mostov, K.E.6
  • 41
    • 0025282485 scopus 로고
    • BET1, BOS1, and SEC22 are members of a group of interacting yeast genes required for transport from the endoplasmic reticulum to the Golgi complex
    • Newman AP, Shim J, Ferro-Novick S. BET1, BOS1, and SEC22 are members of a group of interacting yeast genes required for transport from the endoplasmic reticulum to the Golgi complex. Mol Cell Biol 1990; 10: 3405-3414.
    • (1990) Mol Cell Biol , vol.10 , pp. 3405-3414
    • Newman, A.P.1    Shim, J.2    Ferro-Novick, S.3
  • 42
    • 0029932226 scopus 로고    scopus 로고
    • SNARE-mediated retrograde traffic from the Golgi complex to the endoplasmic reticulum
    • Lewis MJ, Pelham HR. SNARE-mediated retrograde traffic from the Golgi complex to the endoplasmic reticulum. Cell 1996; 85: 205-215.
    • (1996) Cell , vol.85 , pp. 205-215
    • Lewis, M.J.1    Pelham, H.R.2
  • 43
    • 0026561901 scopus 로고
    • Brefeldin A: Insights into the control of membrane traffic and organelle structure
    • Klausner RD, Donaldson JG, Lippincott-Schwartz J. Brefeldin A: Insights into the control of membrane traffic and organelle structure. J Cell Biol 1992; 116: 1071-1080.
    • (1992) J Cell Biol , vol.116 , pp. 1071-1080
    • Klausner, R.D.1    Donaldson, J.G.2    Lippincott-Schwartz, J.3
  • 45
    • 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. Changes in the endoplasmic reticulum structure of Paramecium primaurelia in relation to different cellular physiological states. J Photochem Photobiol B 2000; 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
  • 46
    • 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 2000; 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
  • 47
    • 0031885535 scopus 로고    scopus 로고
    • Green fluorescent protein as a noninvasive intracellular pH indicator
    • Kneen M, Farinas J, Li Y, Verkman AS. Green fluorescent protein as a noninvasive intracellular pH indicator. Biophys J 1998; 74: 1591-1599.
    • (1998) Biophys J , vol.74 , pp. 1591-1599
    • Kneen, M.1    Farinas, J.2    Li, Y.3    Verkman, A.S.4
  • 48
    • 0036137143 scopus 로고    scopus 로고
    • RNA interference by feeding in Paramecium
    • Galvani A, Sperling L. RNA interference by feeding in Paramecium. Trends Genet 2002; 18: 11-12.
    • (2002) Trends Genet , vol.18 , pp. 11-12
    • Galvani, A.1    Sperling, L.2
  • 50
    • 2942527445 scopus 로고    scopus 로고
    • Molecular and phylogenetic characterization of syntaxin genes from parasitic protozoa
    • Dacks JB, Doolittle WF. Molecular and phylogenetic characterization of syntaxin genes from parasitic protozoa. Mol Biochem Parasitol 2004; 136: 123-136.
    • (2004) Mol Biochem Parasitol , vol.136 , pp. 123-136
    • Dacks, J.B.1    Doolittle, W.F.2
  • 51
    • 4444309237 scopus 로고    scopus 로고
    • Systematic analysis of SNARE molecules in Arabidopsis: Dissection of the post-Golgi network in plant cells
    • Uemura T, Ueda T, Ohniwa RL, Nakano A, Takeyasu K, Sato MH. Systematic analysis of SNARE molecules in Arabidopsis: Dissection of the post-Golgi network in plant cells. Cell Struct Funct 2004; 29: 49-65.
    • (2004) Cell Struct Funct , vol.29 , pp. 49-65
    • Uemura, T.1    Ueda, T.2    Ohniwa, R.L.3    Nakano, A.4    Takeyasu, K.5    Sato, M.H.6
  • 53
    • 0037089090 scopus 로고    scopus 로고
    • Novel syntaxin gene sequences from Giardia, Trypanosoma and algae: Implications for the ancient evolution of the eukaryotic endomembrane system
    • Dacks JB, Doolittle WF. Novel syntaxin gene sequences from Giardia, Trypanosoma and algae: Implications for the ancient evolution of the eukaryotic endomembrane system. J Cell Sci 2002; 115: 1635-1642.
    • (2002) J Cell Sci , vol.115 , pp. 1635-1642
    • Dacks, J.B.1    Doolittle, W.F.2
  • 55
    • 0030863058 scopus 로고    scopus 로고
    • An isoform of the Golgi t-SNARE, syntaxin 5, with an endoplasmic reticulum retrieval signal
    • Hui N, Nakamura N, Sonnichsen B, Shima DT, Nilsson T, Warren G. An isoform of the Golgi t-SNARE, syntaxin 5, with an endoplasmic reticulum retrieval signal. Mol Biol Cell 1997; 8: 1777-1787.
    • (1997) Mol Biol Cell , vol.8 , pp. 1777-1787
    • Hui, N.1    Nakamura, N.2    Sonnichsen, B.3    Shima, D.T.4    Nilsson, T.5    Warren, G.6
  • 56
    • 0345237979 scopus 로고    scopus 로고
    • Syntaxin 2 splice variants exhibit differential expression patterns, biochemical properties and subcellular localizations
    • Quinones B, Riento K, Olkkonen VM, Hardy S, Bennett MK. Syntaxin 2 splice variants exhibit differential expression patterns, biochemical properties and subcellular localizations. J Cell Sci 1999; 112: 4291-4304.
    • (1999) J Cell Sci , vol.112 , pp. 4291-4304
    • Quinones, B.1    Riento, K.2    Olkkonen, V.M.3    Hardy, S.4    Bennett, M.K.5
  • 57
    • 0035807871 scopus 로고    scopus 로고
    • The ionic layer is required for efficient dissociation of the SNARE complex by alpha-SNAP and NSF
    • Scales SJ, Yoo BY, Scheller RH. The ionic layer is required for efficient dissociation of the SNARE complex by alpha-SNAP and NSF. Proc Natl Acad Sci U S A 2001; 98: 14262-14267.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 14262-14267
    • Scales, S.J.1    Yoo, B.Y.2    Scheller, R.H.3
  • 58
    • 0035126830 scopus 로고    scopus 로고
    • Vam3p structure reveals conserved and divergent properties of syntaxins
    • Dulubova I, Yamaguchi T, Wang Y, Sudhof TC, Rizo J. Vam3p structure reveals conserved and divergent properties of syntaxins. Nat Struct Biol 2001; 8: 258-264.
    • (2001) Nat Struct Biol , vol.8 , pp. 258-264
    • Dulubova, I.1    Yamaguchi, T.2    Wang, Y.3    Sudhof, T.C.4    Rizo, J.5
  • 59
    • 0037184043 scopus 로고    scopus 로고
    • The N-terminal domains of syntaxin 7 and vti1b form three-helix bundles that differ in their ability to regulate SNARE complex assembly
    • Antonin W, Dulubova I, Arac D, Pabst S, Plitzner J, Rizo J, Jahn R. The N-terminal domains of syntaxin 7 and vti1b form three-helix bundles that differ in their ability to regulate SNARE complex assembly. J Biol Chem 2002; 277: 36449-36456.
    • (2002) J Biol Chem , vol.277 , pp. 36449-36456
    • Antonin, W.1    Dulubova, I.2    Arac, D.3    Pabst, S.4    Plitzner, J.5    Rizo, J.6    Jahn, R.7
  • 61
    • 20444467326 scopus 로고    scopus 로고
    • A dual function for Munc-18 in exocytosis of PC12 cells
    • Schütz D, Zilly F, Lang T, Jahn R, Bruns D. A dual function for Munc-18 in exocytosis of PC12 cells. Eur J Neurosci 2005; 21: 2419-2432.
    • (2005) Eur J Neurosci , vol.21 , pp. 2419-2432
    • Schütz, D.1    Zilly, F.2    Lang, T.3    Jahn, R.4    Bruns, D.5
  • 63
    • 0028815453 scopus 로고
    • The t-SNAREs syntaxin 1 and SNAP-25 are present on organelles that participate in synaptic vesicle recycling
    • Walch-Solimena C, Blasi J, Edelmann L, Chapman ER, von Mollard GF, Jahn R. The t-SNAREs syntaxin 1 and SNAP-25 are present on organelles that participate in synaptic vesicle recycling. J Cell Biol 1995; 128: 637-645.
    • (1995) J Cell Biol , vol.128 , pp. 637-645
    • Walch-Solimena, C.1    Blasi, J.2    Edelmann, L.3    Chapman, E.R.4    von Mollard, G.F.5    Jahn, R.6
  • 64
    • 25444483892 scopus 로고    scopus 로고
    • Localization of plasma membrane t-SNAREs syntaxin 2 and 3 in intracellular compartments
    • Band AM, Kuismanen E. Localization of plasma membrane t-SNAREs syntaxin 2 and 3 in intracellular compartments. BMC Cell Biol 2005; 6: 26.
    • (2005) BMC Cell Biol , vol.6 , pp. 26
    • Band, A.M.1    Kuismanen, E.2
  • 65
    • 0343230883 scopus 로고
    • Golgi apparatus in ciliates. Ultrastructure, with special reference to Paramecium
    • Esteve JC. [Golgi apparatus in ciliates. Ultrastructure, with special reference to Paramecium]. J Protozool 1972; 19: 609-618.
    • (1972) J Protozool , vol.19 , pp. 609-618
    • Esteve, J.C.1
  • 66
    • 0002351563 scopus 로고
    • Cytology
    • In: Görtz HD, editor. Berlin: Springer-Verlag
    • Allen RD. Cytology. In: Görtz HD, editor. Paramecium. Berlin: Springer-Verlag; 1988, pp. 4-40.
    • (1988) Paramecium , pp. 4-40
    • Allen, R.D.1
  • 67
    • 0032579295 scopus 로고    scopus 로고
    • Role of vesicle-associated syntaxin 5 in the assembly of pre-Golgi intermediates
    • Rowe T, Dascher C, Bannykh S, Plutner H, Balch WE. Role of vesicle-associated syntaxin 5 in the assembly of pre-Golgi intermediates. Science 1998; 279: 696-700.
    • (1998) Science , vol.279 , pp. 696-700
    • Rowe, T.1    Dascher, C.2    Bannykh, S.3    Plutner, H.4    Balch, W.E.5
  • 70
    • 4344599512 scopus 로고    scopus 로고
    • Participation of the syntaxin 5/Ykt6/GS28/GS15 SNARE complex in transport from the early/recycling endosome to the trans-Golgi network
    • Tai G, Lu L, Wang TL, Tang BL, Goud B, Johannes L, Hong W. Participation of the syntaxin 5/Ykt6/GS28/GS15 SNARE complex in transport from the early/recycling endosome to the trans-Golgi network. Mol Biol Cell 2004; 15: 4011-4022.
    • (2004) Mol Biol Cell , vol.15 , pp. 4011-4022
    • Tai, G.1    Lu, L.2    Wang, T.L.3    Tang, B.L.4    Goud, B.5    Johannes, L.6    Hong, W.7
  • 71
    • 0032489499 scopus 로고    scopus 로고
    • Syntaxin 5 is a common component of the NSF- and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro
    • Rabouille C, Kondo H, Newman R, Hui N, Freemont P, Warren G. Syntaxin 5 is a common component of the NSF- and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro. Cell 1998; 92: 603-610.
    • (1998) Cell , vol.92 , pp. 603-610
    • Rabouille, C.1    Kondo, H.2    Newman, R.3    Hui, N.4    Freemont, P.5    Warren, G.6
  • 72
    • 0035661728 scopus 로고    scopus 로고
    • Interactions between syntaxins identify at least five SNARE complexes within the Golgi/prevacuolar system of the Arabidopsis cell
    • Sanderfoot AA, Kovaleva V, Bassham DC, Raikhel NV. Interactions between syntaxins identify at least five SNARE complexes within the Golgi/ prevacuolar system of the Arabidopsis cell. Mol Biol Cell 2001; 12: 3733-3743.
    • (2001) Mol Biol Cell , vol.12 , pp. 3733-3743
    • Sanderfoot, A.A.1    Kovaleva, V.2    Bassham, D.C.3    Raikhel, N.V.4
  • 73
    • 0029949540 scopus 로고    scopus 로고
    • Characterization and subcellular localization of target membrane soluble NSF attachment protein receptors (t-SNAREs) in macrophages. Syntaxins 2, 3, and 4 are present on phagosomal membranes
    • Hackam DJ, Rotstein OD, Bennett MK, Klip A, Grinstein S, Manolson MF. Characterization and subcellular localization of target membrane soluble NSF attachment protein receptors (t-SNAREs) in macrophages. Syntaxins 2, 3, and 4 are present on phagosomal membranes. J Immunol 1996; 156: 4377-4383.
    • (1996) J Immunol , vol.156 , pp. 4377-4383
    • Hackam, D.J.1    Rotstein, O.D.2    Bennett, M.K.3    Klip, A.4    Grinstein, S.5    Manolson, M.F.6
  • 74
  • 75
    • 0033001625 scopus 로고    scopus 로고
    • A possible role of di-leucine-based motifs in targeting and sorting of the syntaxin family of proteins
    • Tang BL, Hong W. A possible role of di-leucine-based motifs in targeting and sorting of the syntaxin family of proteins. FEBS Lett 1999; 446: 211-212.
    • (1999) FEBS Lett , vol.446 , pp. 211-212
    • Tang, B.L.1    Hong, W.2
  • 76
    • 0034793911 scopus 로고    scopus 로고
    • Roles of the cytoplasmic and transmembrane domains of syntaxins in intracellular localization and trafficking
    • Kasai K, Akagawa K. Roles of the cytoplasmic and transmembrane domains of syntaxins in intracellular localization and trafficking. J Cell Sci 2001; 114: 3115-3124.
    • (2001) J Cell Sci , vol.114 , pp. 3115-3124
    • Kasai, K.1    Akagawa, K.2
  • 77
    • 0034805876 scopus 로고    scopus 로고
    • Transmembrane domain length determines intracellular membrane compartment localization of syntaxins 3, 4, and 5
    • Watson RT, Pessin JE. Transmembrane domain length determines intracellular membrane compartment localization of syntaxins 3, 4, and 5. Am J Physiol Cell Physiol 2001; 281: C215-C223.
    • (2001) Am J Physiol Cell Physiol , vol.281
    • Watson, R.T.1    Pessin, J.E.2
  • 78
    • 0000225464 scopus 로고
    • Paramecium aurelia
    • In: Kung RC, editor. New York: Plenum Press
    • Sonneborn TM. Paramecium aurelia. In: Kung RC, editor. Handbook of Genetics. New York: Plenum Press; 1974, pp. 469-594.
    • (1974) Handbook of Genetics , pp. 469-594
    • Sonneborn, T.M.1
  • 84
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones DT. Protein secondary structure prediction based on position-specific scoring matrices. J Mol Biol 1999; 292: 195-202.
    • (1999) J Mol Biol , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 85
    • 0028211273 scopus 로고
    • A model recognition approach to the prediction of all-helical membrane protein structure and topology
    • Jones DT, Taylor WR, Thornton JM. A model recognition approach to the prediction of all-helical membrane protein structure and topology. Biochemistry 1994; 33: 3038-3049.
    • (1994) Biochemistry , vol.33 , pp. 3038-3049
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 86
    • 0032570779 scopus 로고    scopus 로고
    • Do transmembrane protein superfolds exist?
    • Jones DT. Do transmembrane protein superfolds exist? FEBS Lett 1998; 423: 281-285.
    • (1998) FEBS Lett , vol.423 , pp. 281-285
    • Jones, D.T.1
  • 87
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin LJ, Bryson K, Jones DT. The PSIPRED protein structure prediction server. Bioinformatics 2000; 16: 404-405.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 88
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: Integrated software for Molecular Evolutionary Genetics Analysis and sequence alignment
    • Kumar S, Tamura K, Nei M. MEGA3: Integrated software for Molecular Evolutionary Genetics Analysis and sequence alignment. Brief Bioinform 2004; 5: 150-163.
    • (2004) Brief Bioinform , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 90
    • 0031778402 scopus 로고    scopus 로고
    • The cloning by complementation of the pawn-A gene in Paramecium
    • Haynes WJ, Vaillant B, Preston RR, Saimi Y, Kung C. The cloning by complementation of the pawn-A gene in Paramecium. Genetics 1998; 149: 947-957.
    • (1998) Genetics , vol.149 , pp. 947-957
    • Haynes, W.J.1    Vaillant, B.2    Preston, R.R.3    Saimi, Y.4    Kung, C.5
  • 91
    • 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. The vacuolar proton-ATPase plays a major role in several membrane-bounded organelles in Paramecium. J Cell Sci 2005; 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
  • 93
    • 0029201538 scopus 로고
    • Induction of antibiotic resistance in Paramecium tetraurelia by the bacterial gene APH-3′-II
    • Haynes WJ, Ling KY, Saimi Y, Kung C. Induction of antibiotic resistance in Paramecium tetraurelia by the bacterial gene APH-3′-II. J Eukaryot Microbiol 1995; 42: 83-91.
    • (1995) J Eukaryot Microbiol , vol.42 , pp. 83-91
    • Haynes, W.J.1    Ling, K.Y.2    Saimi, Y.3    Kung, C.4
  • 94
    • 0002305048 scopus 로고
    • Effect of adaptation to the environment on chemotaxis of Paramecium caudatum
    • Dryl S. Effect of adaptation to the environment on chemotaxis of Paramecium caudatum. Acta Biol Exp 1959; 19: 83-93.
    • (1959) Acta Biol Exp , vol.19 , pp. 83-93
    • Dryl, S.1
  • 95
    • 0035941485 scopus 로고    scopus 로고
    • Ingestion of bacterially expressed dsRNAs can produce specific and potent genetic interference in Caenorhabditis elegans
    • Timmons L, Court DL, Fire A. Ingestion of bacterially expressed dsRNAs can produce specific and potent genetic interference in Caenorhabditis elegans. Gene 2001; 263: 103-112.
    • (2001) Gene , vol.263 , pp. 103-112
    • Timmons, L.1    Court, D.L.2    Fire, A.3
  • 96
    • 0016257034 scopus 로고
    • Mutations affecting the trichocysts in Paramecium aurelia. I. Morphology and description of the mutants
    • Pollack S. Mutations affecting the trichocysts in Paramecium aurelia. I. Morphology and description of the mutants. J Protozool 1974; 21: 352-362.
    • (1974) J Protozool , vol.21 , pp. 352-362
    • Pollack, S.1
  • 97
    • 0000063837 scopus 로고
    • Use of polymerase chain reaction for the rapid construction of synthetic genes
    • Dillon PJ, Rosen CA. Use of polymerase chain reaction for the rapid construction of synthetic genes. Methods Mol Biol 1993; 15: 263-s269.
    • (1993) Methods Mol Biol , vol.15
    • Dillon, P.J.1    Rosen, C.A.2
  • 98
    • 8744300794 scopus 로고    scopus 로고
    • Cloning of β-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. Cloning of β-tubulin and succinate dehydrogenase genes from Uromyces fabae and establishing selection conditions for their use in transformation. Eur J Plant Pathol 2004; 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
  • 99
    • 0029891406 scopus 로고    scopus 로고
    • Protein phosphatase and kinase activities possibly involved in exocytosis regulation in Paramecium tetraurelia
    • Kissmehl R, Treptau T, Hofer HW, Plattner H. Protein phosphatase and kinase activities possibly involved in exocytosis regulation in Paramecium tetraurelia. Biochem J 1996; 317: 65-76.
    • (1996) Biochem J , vol.317 , pp. 65-76
    • Kissmehl, R.1    Treptau, T.2    Hofer, H.W.3    Plattner, H.4
  • 100
    • 0025286727 scopus 로고
    • Cell surface complexes ('cortices') isolated from Paramecium tetraurelia cells as a model system for analysing exocytosis in vitro in conjunction with microinjection studies
    • Lumpert CJ, Kersken H, Plattner H. Cell surface complexes ('cortices') isolated from Paramecium tetraurelia cells as a model system for analysing exocytosis in vitro in conjunction with microinjection studies. Biochem J 1990; 269: 639-645.
    • (1990) Biochem J , vol.269 , pp. 639-645
    • Lumpert, C.J.1    Kersken, H.2    Plattner, H.3
  • 101
    • 0031773844 scopus 로고    scopus 로고
    • Subplasmalemmal Ca-stores in Paramecium tetraurelia. Identification and characterisation of a sarco(endo)plasmic reticulum-like Ca (2+) -ATPase by phosphoenzyme intermediate formation and its inhibition by caffeine
    • Kissmehl R, Huber S, Kottwitz B, Hauser K, Plattner H. Subplasmalemmal Ca-stores in Paramecium tetraurelia. Identification and characterisation of a sarco(endo)plasmic reticulum-like Ca (2+) -ATPase by phosphoenzyme intermediate formation and its inhibition by caffeine. Cell Calcium 1998; 24: 193-203.
    • (1998) Cell Calcium , vol.24 , pp. 193-203
    • Kissmehl, R.1    Huber, S.2    Kottwitz, B.3    Hauser, K.4    Plattner, H.5
  • 102
    • 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. Seventeen a-subunit isoforms of Paramecium V-ATPase provide high specialization in localization and function. Mol Biol Cell 2006; 17: 917-930.
    • (2006) Mol Biol Cell , vol.17 , pp. 917-930
    • Wassmer, T.1    Kissmehl, R.2    Cohen, J.3    Plattner, H.4


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