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Volumn 280, Issue C, 2010, Pages 79-184

Membrane trafficking in protozoa: Snare proteins, H+-ATPase, actin, and other key players in ciliates

Author keywords

Actin; Ciliate; Membrane; Paramecium; SNAREs Tetrahymena; Trafficking

Indexed keywords

ACTIN; ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR; ADENOSINE TRIPHOSPHATASE INHIBITOR; BREFELDIN A; CALCIUM BINDING PROTEIN; CHAPERONE; F ACTIN; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATASE; LIPOCORTIN 2; N ETHYLMALEIMIDE SENSITIVE FACTOR; PHALLOIDIN; PROTEINASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; SNARE PROTEIN; SYNAPTOTAGMIN;

EID: 77957946461     PISSN: 19376448     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1937-6448(10)80003-6     Document Type: Article
Times cited : (34)

References (515)
  • 1
    • 3342913655 scopus 로고    scopus 로고
    • Synaptotagmins are trafficked to distinct subcellular domains including the postsynaptic compartment
    • Adolfsen, B., Saraswati, S., Yoshihara, M., Littleton, J.T., 2004. Synaptotagmins are trafficked to distinct subcellular domains including the postsynaptic compartment. J. Cell Biol. 166, 249-260.
    • (2004) J. Cell Biol. , vol.166 , pp. 249-260
    • Adolfsen, B.1    Saraswati, S.2    Yoshihara, M.3    Littleton, J.T.4
  • 2
    • 0025814879 scopus 로고
    • Microtubule diversity in ciliated cells: evidence for its generation by post-translational modification in the axonemes of Paramecium and quail oviduct cells
    • Adoutte, A., Delgado, P., Fleury, A., Levilliers, N., Lainé, M.-C., Marty, M.-C., et al., 1991. Microtubule diversity in ciliated cells: evidence for its generation by post-translational modification in the axonemes of Paramecium and quail oviduct cells. Biol. Cell 71, 227-245.
    • (1991) Biol. Cell , vol.71 , pp. 227-245
    • Adoutte, A.1    Delgado, P.2    Fleury, A.3    Levilliers, N.4    Lainé, M.-C.5    Marty, M.-C.6
  • 3
    • 33646112380 scopus 로고    scopus 로고
    • Synaptotagmin IV is necessary for the maturation of secretory granules in PC12 cells
    • Ahras, M., Otto, G.P., Tooze, S.A., 2006. Synaptotagmin IV is necessary for the maturation of secretory granules in PC12 cells. J. Cell Biol. 173, 241-251.
    • (2006) J. Cell Biol. , vol.173 , pp. 241-251
    • Ahras, M.1    Otto, G.P.2    Tooze, S.A.3
  • 4
    • 0002351563 scopus 로고
    • Cytology
    • Springer-Verlag, Görtz, H.-D. (Ed.), Berlin, Heidelberg, New York
    • Allen, R.D., 1988. Cytology. In: Görtz, H.-D. (Ed.), Paramecium. Springer-Verlag, Berlin, Heidelberg, New York, pp. 4-40.
    • (1988) Paramecium , pp. 4-40
    • Allen, R.D.1
  • 5
    • 0033777003 scopus 로고    scopus 로고
    • The contractile vacuole system and its membrane dynamics
    • Allen, R.D., 2000. The contractile vacuole system and its membrane dynamics. Bioessays 22, 1035-1042.
    • (2000) Bioessays , vol.22 , pp. 1035-1042
    • Allen, R.D.1
  • 6
    • 0019225464 scopus 로고
    • Membrane recycling and endocytosis in Paramecium confirmed by horseradish peroxidase pulse-chase studies
    • Allen, R.D., Fok, A.K., 1980. Membrane recycling and endocytosis in Paramecium confirmed by horseradish peroxidase pulse-chase studies. J. Cell Sci. 45, 131-145.
    • (1980) J. Cell Sci. , vol.45 , pp. 131-145
    • Allen, R.D.1    Fok, A.K.2
  • 7
    • 0020803834 scopus 로고
    • Nonlysosomal vesicles (acidosomes) are involved in phagosome acidification in Paramecium
    • Allen, R.D., Fok, A.K., 1983a. Nonlysosomal vesicles (acidosomes) are involved in phagosome acidification in Paramecium. J. Cell Biol. 97, 566-570.
    • (1983) J. Cell Biol. , vol.97 , pp. 566-570
    • Allen, R.D.1    Fok, A.K.2
  • 8
    • 0020640501 scopus 로고
    • Phagosome fusion vesicles of Paramecium. I. Thin-section morphology
    • Allen, R.D., Fok, A.K., 1983b. Phagosome fusion vesicles of Paramecium. I. Thin-section morphology. Eur. J. Cell Biol. 29, 150-158.
    • (1983) Eur. J. Cell Biol. , vol.29 , pp. 150-158
    • Allen, R.D.1    Fok, A.K.2
  • 9
    • 0021123418 scopus 로고
    • Membrane behavior of exocytic vesicles III. Flow of horseradish peroxidase labeled trichocyst membrane remnants in Paramecium
    • Allen, R.D., Fok, A.K., 1984a. Membrane behavior of exocytic vesicles. III. Flow of horseradish peroxidase labeled trichocyst membrane remnants in Paramecium. Eur. J. Cell Biol. 35, 27-34.
    • (1984) Eur. J. Cell Biol. , vol.35 , pp. 27-34
    • Allen, R.D.1    Fok, A.K.2
  • 10
    • 0021744617 scopus 로고
    • Retrieval of lysosomal membrane and acid phosphatase from phagolysosomes of Paramecium caudatum
    • Allen, R.D., Fok, A.K., 1984b. Retrieval of lysosomal membrane and acid phosphatase from phagolysosomes of Paramecium caudatum. J. Cell Biol. 99, 1955-1959.
    • (1984) J. Cell Biol. , vol.99 , pp. 1955-1959
    • Allen, R.D.1    Fok, A.K.2
  • 11
    • 0021811101 scopus 로고
    • Modulation of the digestive lysosomal system in Paramecium caudatum III. Morphological effects of cytochalasin B
    • Allen, R.D., Fok, A.K., 1985. Modulation of the digestive lysosomal system in Paramecium caudatum. III. Morphological effects of cytochalasin B. Eur. J. Cell Biol. 37, 35-43.
    • (1985) Eur. J. Cell Biol. , vol.37 , pp. 35-43
    • Allen, R.D.1    Fok, A.K.2
  • 12
    • 84986467014 scopus 로고
    • Membrane dynamics of the contractile vacuole complex of Paramecium
    • Allen, R.D., Fok, A.K., 1988. Membrane dynamics of the contractile vacuole complex of Paramecium. J. Protozool. 35, 63-71.
    • (1988) J. Protozool. , vol.35 , pp. 63-71
    • Allen, R.D.1    Fok, A.K.2
  • 13
    • 0027290618 scopus 로고
    • Nonclathrin vesicle coats and filament networks in the transition zone and trans-Golgi region of the Golgi complex of Paramecium
    • Allen, R.D., Fok, A.K., 1993. Nonclathrin vesicle coats and filament networks in the transition zone and trans-Golgi region of the Golgi complex of Paramecium. J. Struct. Biol. 110, 215-226.
    • (1993) J. Struct. Biol. , vol.110 , pp. 215-226
    • Allen, R.D.1    Fok, A.K.2
  • 14
    • 0034018279 scopus 로고    scopus 로고
    • Membrane trafficking and processing in Paramecium
    • Allen, R.D., Fok, A.K., 2000. Membrane trafficking and processing in Paramecium. Int. Rev. Cytol. 198, 277-317.
    • (2000) Int. Rev. Cytol. , vol.198 , pp. 277-317
    • Allen, R.D.1    Fok, A.K.2
  • 15
    • 0036204472 scopus 로고    scopus 로고
    • Osmoregulation and contractile vacuoles of protozoa
    • Allen, R.D., Naitoh, Y., 2002. Osmoregulation and contractile vacuoles of protozoa. Int. Rev. Cytol. 215, 351-394.
    • (2002) Int. Rev. Cytol. , vol.215 , pp. 351-394
    • Allen, R.D.1    Naitoh, Y.2
  • 16
    • 0016373673 scopus 로고
    • The cytoproct of Paramecium caudatum: structure and function, microtubules, and fate of food vacuole membranes
    • Allen, R.D., Wolf, R.W., 1974. The cytoproct of Paramecium caudatum: structure and function, microtubules, and fate of food vacuole membranes. J. Cell Sci. 14, 611-631.
    • (1974) J. Cell Sci. , vol.14 , pp. 611-631
    • Allen, R.D.1    Wolf, R.W.2
  • 17
    • 0024065235 scopus 로고
    • A survey of lectin binding in Paramecium
    • Allen, R.D., Ueno, M.S., Fok, A.K., 1988. A survey of lectin binding in Paramecium. J. Protozool. 35, 400-407.
    • (1988) J. Protozool. , vol.35 , pp. 400-407
    • Allen, R.D.1    Ueno, M.S.2    Fok, A.K.3
  • 18
    • 0024392222 scopus 로고
    • An investigation of mitochondrial inner membranes by rapid-freeze deep-etch techniques
    • Allen, R.D., Schroeder, C.C., Fok, A.K., 1989. An investigation of mitochondrial inner membranes by rapid-freeze deep-etch techniques. J. Cell Biol. 108, 2233-2240.
    • (1989) J. Cell Biol. , vol.108 , pp. 2233-2240
    • Allen, R.D.1    Schroeder, C.C.2    Fok, A.K.3
  • 19
    • 0026528046 scopus 로고
    • Endosomal system of Paramecium: coated pits to early endosomes
    • Allen, R.D., Schroeder, C.C., Fok, A.K., 1992. Endosomal system of Paramecium: coated pits to early endosomes. J. Cell Sci. 101, 449-461.
    • (1992) J. Cell Sci. , vol.101 , pp. 449-461
    • Allen, R.D.1    Schroeder, C.C.2    Fok, A.K.3
  • 20
    • 0027517907 scopus 로고
    • Acidosomes: recipients of multiple sources of membrane and cargo during development and maturation
    • Allen, R.D., Ma, L., Fok, A.K., 1993. Acidosomes: recipients of multiple sources of membrane and cargo during development and maturation. J. Cell Sci. 106, 411-422.
    • (1993) J. Cell Sci. , vol.106 , pp. 411-422
    • Allen, R.D.1    Ma, L.2    Fok, A.K.3
  • 21
    • 0028959551 scopus 로고
    • Rapid bulk replacement of acceptor membrane by donor membrane during phagosome to phagoacidosome transformation in Paramecium
    • Allen, R.D., Bala, N.P., Ali, R.F., Nishida, D.M., Aihara, M.S., Ishida, M., et al., 1995. Rapid bulk replacement of acceptor membrane by donor membrane during phagosome to phagoacidosome transformation in Paramecium. J. Cell Sci. 108, 1263-1274.
    • (1995) J. Cell Sci. , vol.108 , pp. 1263-1274
    • Allen, R.D.1    Bala, N.P.2    Ali, R.F.3    Nishida, D.M.4    Aihara, M.S.5    Ishida, M.6
  • 22
    • 55549089615 scopus 로고    scopus 로고
    • Large ARF guanine nucleotide exchange factors in membrane trafficking
    • Anders, N., Jürgens, G., 2008. Large ARF guanine nucleotide exchange factors in membrane trafficking. Cell. Mol. Life Sci. 65, 3433-3445.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 3433-3445
    • Anders, N.1    Jürgens, G.2
  • 23
    • 0027730175 scopus 로고
    • Cytoplasmsic dynein-dependent vesicular transport from early to late endosomes
    • Aniento, F., Emans, N., Griffiths, G., Gruenberg, J., 1993. Cytoplasmsic dynein-dependent vesicular transport from early to late endosomes. J. Cell Biol. 123, 1373-1387.
    • (1993) J. Cell Biol. , vol.123 , pp. 1373-1387
    • Aniento, F.1    Emans, N.2    Griffiths, G.3    Gruenberg, J.4
  • 24
    • 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 Acid Res. 35, D439-D444.
    • (2007) Nucleic Acid Res , vol.35
    • Arnaiz, O.1    Cain, S.2    Cohen, J.3    Sperling, L.4
  • 25
    • 0026353850 scopus 로고
    • Protein discharge from immature secretory granules displays both regulated and constitutive characteristics
    • Arvan, P., Kuliawa, R., Prabakaran, D., Zavacki, A.-M., Elahi, D., Wang, S., et al., 1991. Protein discharge from immature secretory granules displays both regulated and constitutive characteristics. J. Biol. Chem. 266, 14171-14174.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14171-14174
    • Arvan, P.1    Kuliawa, R.2    Prabakaran, D.3    Zavacki, A.-M.4    Elahi, D.5    Wang, S.6
  • 26
    • 0028285025 scopus 로고
    • The dynein genes of Paramecium tetraurelia Sequences adjacent to the catalytic P-loop identify cytoplasmic and axonemal heavy chain isoforms
    • Asai, D.J., Beckwith, S.M., Kandl, K.A., Keating, H.H., Tjandra, H., Forney, J.D., 1994. The dynein genes of Paramecium tetraurelia. Sequences adjacent to the catalytic P-loop identify cytoplasmic and axonemal heavy chain isoforms. J. Cell Sci. 107, 839-847.
    • (1994) J. Cell Sci. , vol.107 , pp. 839-847
    • Asai, D.J.1    Beckwith, S.M.2    Kandl, K.A.3    Keating, H.H.4    Tjandra, H.5    Forney, J.D.6
  • 27
    • 0017667987 scopus 로고
    • Saltatory motility of uninserted trichocysts and mitochondria in Paramecium tetraurelia
    • Aufderheide, K.J., 1977. Saltatory motility of uninserted trichocysts and mitochondria in Paramecium tetraurelia. Science 198, 299-300.
    • (1977) Science , vol.198 , pp. 299-300
    • Aufderheide, K.J.1
  • 28
    • 0031898609 scopus 로고    scopus 로고
    • Exocytosis in chromaffin cells of the adrenal medulla
    • Aunis, D., 1998. Exocytosis in chromaffin cells of the adrenal medulla. Int. Rev. Cytol. 181, 213-320.
    • (1998) Int. Rev. Cytol. , vol.181 , pp. 213-320
    • Aunis, D.1
  • 29
    • 33750858684 scopus 로고    scopus 로고
    • Global trends of whole genome duplications revealed by the genome sequence of the ciliate Paramecium tetraurelia
    • Aury, J.-M., Jaillon, O., Duret, L., Noel, B., Jubin, C., Porcel, B.M., et al., 2006. Global trends of whole genome duplications revealed by the genome sequence of 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    Porcel, B.M.6
  • 30
    • 0028298540 scopus 로고
    • Electron cryomicroscopy of Bacillus stearothermophilus 50 S ribosomal subunits crystallized on phospholipid monolayers
    • Avila-Sakar, A.J., Guan, T.-L., Arad, T., Schmid, M.F., Loke, T.W., Yonath, A., et al., 1994. Electron cryomicroscopy of Bacillus stearothermophilus 50 S ribosomal subunits crystallized on phospholipid monolayers. J. Mol. Biol. 239, 689-697.
    • (1994) J. Mol. Biol. , vol.239 , pp. 689-697
    • Avila-Sakar, A.J.1    Guan, T.-L.2    Arad, T.3    Schmid, M.F.4    Loke, T.W.5    Yonath, A.6
  • 32
    • 0029144561 scopus 로고
    • Glycosylinositolphosphoceramide in the free-living protozoan Paramecium primaurelia: modification of core glycans by mannosyl phosphate
    • Azzouz, N., Striepen, B., Gerold, P., Capdeville, Y., Schwarz, R.T., 1995. Glycosylinositolphosphoceramide in the free-living protozoan Paramecium primaurelia: modification of core glycans by mannosyl phosphate. EMBO J. 14, 4422-4433.
    • (1995) EMBO J , vol.14 , pp. 4422-4433
    • Azzouz, N.1    Striepen, B.2    Gerold, P.3    Capdeville, Y.4    Schwarz, R.T.5
  • 33
    • 0034838444 scopus 로고    scopus 로고
    • Regulation of Paramecium primaurelia glycosylphosphatidyl-inositol biosynthesis via dolichol phosphate mannose synthesis
    • Azzouz, N., Gerold, P., Kedees, M.H., Shams-Eldin, H., Werner, R., Capdeville, Y., et al., 2001. Regulation of Paramecium primaurelia glycosylphosphatidyl-inositol biosynthesis via dolichol phosphate mannose synthesis. Biochimie 83, 801-809.
    • (2001) Biochimie , vol.83 , pp. 801-809
    • Azzouz, N.1    Gerold, P.2    Kedees, M.H.3    Shams-Eldin, H.4    Werner, R.5    Capdeville, Y.6
  • 34
    • 0032101334 scopus 로고    scopus 로고
    • The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function
    • Babst, M., Wendland, B., Estepa, E.J., Emr, S.D., 1998. The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function. EMBO J. 17, 2982-2993.
    • (1998) EMBO J , vol.17 , pp. 2982-2993
    • Babst, M.1    Wendland, B.2    Estepa, E.J.3    Emr, S.D.4
  • 35
    • 0024811663 scopus 로고
    • The subcellular organization of Madin-Darby canine kidney cells during the formation of a polarized epithelium
    • Bacallao, R., Antony, C., Dotti, C., Karsenti, E., Stelzer, E.H.K., Simons, K., 1989. The subcellular organization of Madin-Darby canine kidney cells during the formation of a polarized epithelium. J. Cell Biol. 109, 2817-2832.
    • (1989) J. Cell Biol. , vol.109 , pp. 2817-2832
    • Bacallao, R.1    Antony, C.2    Dotti, C.3    Karsenti, E.4    Stelzer, E.H.K.5    Simons, K.6
  • 37
    • 56149112941 scopus 로고    scopus 로고
    • The outer segment serves as a default destination for the trafficking of membrane proteins in photoreceptors
    • Baker, S.A., Haeri, M., Yoo, P., Gospe, S.M., Skiba, N.P., Knox, B.E., et al., 2008. The outer segment serves as a default destination for the trafficking of membrane proteins in photoreceptors. J. Cell Biol. 183, 485-498.
    • (2008) J. Cell Biol. , vol.183 , pp. 485-498
    • Baker, S.A.1    Haeri, M.2    Yoo, P.3    Gospe, S.M.4    Skiba, N.P.5    Knox, B.E.6
  • 38
    • 0034602344 scopus 로고    scopus 로고
    • A kingdom-level phylogeny of eukaryotes based on combined protein data
    • Baldauf, S.L., Roger, A.J., Wenk-Siefert, I., Doolittle, W.F., 2000. A kingdom-level phylogeny of eukaryotes based on combined protein data. Science 290, 972-977.
    • (2000) Science , vol.290 , pp. 972-977
    • Baldauf, S.L.1    Roger, A.J.2    Wenk-Siefert, I.3    Doolittle, W.F.4
  • 40
    • 0027636429 scopus 로고
    • Processing and secretion of lysosomal acid aα-glucosidase in Tetrahymena wild type and secretiondeficient mutant cells
    • Banno, Y., Okano, Y., Furukawa, K., Tiedtke, A., Kobata, A., Nozawa, Y., 1993. Processing and secretion of lysosomal acid aα-glucosidase in Tetrahymena wild type and secretiondeficient mutant cells. J. Eukaryot. Microbiol. 40, 515-520.
    • (1993) J. Eukaryot. Microbiol. , vol.40 , pp. 515-520
    • Banno, Y.1    Okano, Y.2    Furukawa, K.3    Tiedtke, A.4    Kobata, A.5    Nozawa, Y.6
  • 41
    • 0020757679 scopus 로고
    • Mapping of highly ordered membrane domains in the plasma membrane of the ciliate Cyclidium glaucoma
    • Bardele, C.F., 1983. Mapping of highly ordered membrane domains in the plasma membrane of the ciliate Cyclidium glaucoma. J. Cell Sci. 61, 1-30.
    • (1983) J. Cell Sci. , vol.61 , pp. 1-30
    • Bardele, C.F.1
  • 42
    • 53749099016 scopus 로고    scopus 로고
    • SNAREs: Cogs and coordinators in signaling and development
    • Bassham, D.C., Blatt, M.R., 2008. SNAREs: Cogs and coordinators in signaling and development. Plant Physiol. 147, 1504-1515.
    • (2008) Plant Physiol , vol.147 , pp. 1504-1515
    • Bassham, D.C.1    Blatt, M.R.2
  • 46
    • 28444439900 scopus 로고    scopus 로고
    • Organelle identity and the signposts for membrane traffic
    • Behnia, R., Munro, S., 2005. Organelle identity and the signposts for membrane traffic. Nature 438, 597-604.
    • (2005) Nature , vol.438 , pp. 597-604
    • Behnia, R.1    Munro, S.2
  • 48
    • 0017293026 scopus 로고
    • Genetic analysis of membrane differentiation in Paramecium Freeze-fracture study of the trichocyst cycle in wild-type and mutant strains
    • Beisson, J., Lefort-Tran, M., Pouphile, M., Rossignol, M., Satir, B., 1976. Genetic analysis of membrane differentiation in Paramecium. Freeze-fracture study of the trichocyst cycle in wild-type and mutant strains. J. Cell Biol. 69, 126-143.
    • (1976) J. Cell Biol. , vol.69 , pp. 126-143
    • Beisson, J.1    Lefort-Tran, M.2    Pouphile, M.3    Rossignol, M.4    Satir, B.5
  • 49
    • 0018972314 scopus 로고
    • Control of membrane fusion in exocytosis. Physiological studies on a Paramecium mutant blocked in the final step of the trichocyst extrusion process
    • Beisson, J., Cohen, J., Lefort-Tran, M., Pouphile, M., Rossignol, M., 1980. Control of membrane fusion in exocytosis. Physiological studies on a Paramecium mutant blocked in the final step of the trichocyst extrusion process. J. Cell Biol. 85, 213-227.
    • (1980) J. Cell Biol. , vol.85 , pp. 213-227
    • Beisson, J.1    Cohen, J.2    Lefort-Tran, M.3    Pouphile, M.4    Rossignol, M.5
  • 50
    • 0344701076 scopus 로고    scopus 로고
    • The lipid moiety of the GPI-anchor of the major plasma membrane proteins in Paramecium primaurelia is a ceramide: variation of the amide-linked fatty acid composition as a function of growth
    • Benwakrim, A., Trémolière, A., Labarre, J., Capdeville, Y., 1998. The lipid moiety of the GPI-anchor of the major plasma membrane proteins in Paramecium primaurelia is a ceramide: variation of the amide-linked fatty acid composition as a function of growth. Protist 149, 39-50.
    • (1998) Protist , vol.149 , pp. 39-50
    • Benwakrim, A.1    Trémolière, A.2    Labarre, J.3    Capdeville, Y.4
  • 52
    • 34548448140 scopus 로고    scopus 로고
    • The specificity of SNARE pairing in biological membranes is mediated by both proof-reading and spatial segregation
    • Bethani, I., Lang, T., Geumann, U., Sieber, J.J., Jahn, R., Rizzoli, S.O., 2007. The specificity of SNARE pairing in biological membranes is mediated by both proof-reading and spatial segregation. EMBO J. 26, 3981-3992.
    • (2007) EMBO J , vol.26 , pp. 3981-3992
    • Bethani, I.1    Lang, T.2    Geumann, U.3    Sieber, J.J.4    Jahn, R.5    Rizzoli, S.O.6
  • 53
    • 33644935227 scopus 로고    scopus 로고
    • + ATPase: molecular structure and function, physiological roles and regulation
    • + ATPase: molecular structure and function, physiological roles and regulation. J. Exp. Biol. 209, 577-589.
    • (2006) J. Exp. Biol. , vol.209 , pp. 577-589
    • Beyenbach, K.W.1    Wieczorek, H.2
  • 55
    • 69449093833 scopus 로고    scopus 로고
    • Steric and not structure-specific factors dictate the endocytic mechanism of glycosylphosphatidylinositolanchored proteins
    • Bhagatji, P., Leventis, R., Comeau, J., Refaei, M., Silvius, J.R., 2009. Steric and not structure-specific factors dictate the endocytic mechanism of glycosylphosphatidylinositolanchored proteins. J. Cell Biol. 186, 615-628.
    • (2009) J. Cell Biol. , vol.186 , pp. 615-628
    • Bhagatji, P.1    Leventis, R.2    Comeau, J.3    Refaei, M.4    Silvius, J.R.5
  • 56
    • 65249117536 scopus 로고    scopus 로고
    • Myosin 2 maintains an open exocytic fusion pore in secretory epithelial cells
    • Bhat, P., Thorn, P., 2009. Myosin 2 maintains an open exocytic fusion pore in secretory epithelial cells. Mol. Biol. Cell 20, 1795-1803.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1795-1803
    • Bhat, P.1    Thorn, P.2
  • 57
    • 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
  • 58
    • 0015061012 scopus 로고
    • Formation of crystalline ribosomal arrays in cultured chick embryo dorsal root ganglia
    • Birks, R.I., Weldon, P.R., 1971. Formation of crystalline ribosomal arrays in cultured chick embryo dorsal root ganglia. J. Anat. 109, 143-156.
    • (1971) J. Anat. , vol.109 , pp. 143-156
    • Birks, R.I.1    Weldon, P.R.2
  • 60
    • 38449084158 scopus 로고    scopus 로고
    • Intraflagellar transport: from molecular characterisation to mechanism
    • Blacque, O.E., Cevik, S., Kaplan, O.I., 2008. Intraflagellar transport: from molecular characterisation to mechanism. Front. Biosci. 13, 2633-2652.
    • (2008) Front. Biosci. , vol.13 , pp. 2633-2652
    • Blacque, O.E.1    Cevik, S.2    Kaplan, O.I.3
  • 61
    • 0029954687 scopus 로고    scopus 로고
    • A new syntaxin family member implicated in targeting of intracellular transport vesicles
    • Bock, J.B., Scheller, R.H., 1996. A new syntaxin family member implicated in targeting of intracellular transport vesicles. J. Biol. Chem. 271, 17961-17965.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17961-17965
    • Bock, J.B.1    Scheller, R.H.2
  • 62
    • 70449127054 scopus 로고    scopus 로고
    • 1-ATPase structure revealed
    • 1-ATPase structure revealed. EMBO Rep. 10, 1211-1212.
    • (2009) EMBO Rep , vol.10 , pp. 1211-1212
    • Boesen, T.1    Nissen, P.2
  • 63
    • 0033030282 scopus 로고    scopus 로고
    • Transformation of Paramecium tetraurelia by electroporation or particle bombardment
    • Boileau, A.J., Kissmehl, R.A., Kanabarocki, J.A., Saimi, Y., 1999. Transformation of Paramecium tetraurelia by electroporation or particle bombardment. J. Eukaryot. Microbiol. 46, 56-65.
    • (1999) J. Eukaryot. Microbiol. , vol.46 , pp. 56-65
    • Boileau, A.J.1    Kissmehl, R.A.2    Kanabarocki, J.A.3    Saimi, Y.4
  • 64
    • 0842324801 scopus 로고    scopus 로고
    • The mechanisms of vesicle budding and fusion
    • Bonifacino, J.S., Glick, B.S., 2004. The mechanisms of vesicle budding and fusion. Cell 116, 153-166.
    • (2004) Cell , vol.116 , pp. 153-166
    • Bonifacino, J.S.1    Glick, B.S.2
  • 65
    • 0026537949 scopus 로고
    • Interactions between genes involved in exocytotic membrane fusion in Paramecium
    • Bonnemain, H., Gulik-Krzywicki, T., Grandchamp, C., Cohen, J., 1992. Interactions between genes involved in exocytotic membrane fusion in Paramecium. Genetics 130, 461-470.
    • (1992) Genetics , vol.130 , pp. 461-470
    • Bonnemain, H.1    Gulik-Krzywicki, T.2    Grandchamp, C.3    Cohen, J.4
  • 67
    • 0037207101 scopus 로고    scopus 로고
    • Mutational analysis of synaptobrevin transmembrane domain oligomerization
    • Bowen, M.E., Engelman, D.M., Brunger, A.T., 2002. Mutational analysis of synaptobrevin transmembrane domain oligomerization. Biochemistry 41, 15861-15866.
    • (2002) Biochemistry , vol.41 , pp. 15861-15866
    • Bowen, M.E.1    Engelman, D.M.2    Brunger, A.T.3
  • 68
    • 0035692148 scopus 로고    scopus 로고
    • Analysis of a mutant exhibiting conditional sorting to dense core secretory granules in Tetrahymena thermophila
    • Bowman, G.R., Turkewitz, A.P., 2001. Analysis of a mutant exhibiting conditional sorting to dense core secretory granules in Tetrahymena thermophila. Genetics 159, 1605-1616.
    • (2001) Genetics , vol.159 , pp. 1605-1616
    • Bowman, G.R.1    Turkewitz, A.P.2
  • 69
    • 15844398287 scopus 로고    scopus 로고
    • Core formation and the acquisition of fusion competence are linked during secretory granule maturation in Tetrahymena
    • Bowman, G.R., Elde, N.C., Morgan, G., Winey, M., Turkewitz, A.P., 2005a. Core formation and the acquisition of fusion competence are linked during secretory granule maturation in Tetrahymena. Traffic 6, 303-323.
    • (2005) Traffic , vol.6 , pp. 303-323
    • Bowman, G.R.1    Elde, N.C.2    Morgan, G.3    Winey, M.4    Turkewitz, A.P.5
  • 70
    • 27244452149 scopus 로고    scopus 로고
    • Genomic and proteomic evidence for a second family of dense core granule cargo proteins in Tetrahymena thermophila
    • Bowman, G.R., Smith, D.G.S., Siu, K.W.M., Pearlman, R.E., Turkewitz, A.P., 2005b. Genomic and proteomic evidence for a second family of dense core granule cargo proteins in Tetrahymena thermophila. J. Eukaryot. Microbiol. 52, 291-297.
    • (2005) J. Eukaryot. Microbiol. , vol.52 , pp. 291-297
    • Bowman, G.R.1    Smith, D.G.S.2    Siu, K.W.M.3    Pearlman, R.E.4    Turkewitz, A.P.5
  • 71
    • 0037423371 scopus 로고    scopus 로고
    • Proprotein processing within secretory dense core granules of Tetrahymena thermophila
    • Bradshaw, N.R., Chilcoat, N.D., Verbsky, J.W., Turkewitz, A.P., 2003. Proprotein processing within secretory dense core granules of Tetrahymena thermophila. J. Biol. Chem. 278, 4087-4095.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4087-4095
    • Bradshaw, N.R.1    Chilcoat, N.D.2    Verbsky, J.W.3    Turkewitz, A.P.4
  • 73
    • 33644785944 scopus 로고    scopus 로고
    • Linking exocytosis and endocytosis during phagocytosis
    • Braun, V., Niedergang, F., 2006. Linking exocytosis and endocytosis during phagocytosis. Biol. Cell 98, 195-201.
    • (2006) Biol. Cell , vol.98 , pp. 195-201
    • Braun, V.1    Niedergang, F.2
  • 74
    • 9144238779 scopus 로고    scopus 로고
    • TI-VAMP/VAMP7 is required for optimal phagocytosis of opsonised particles in macrophages
    • Braun, V., Fraisier, V., Raposo, G., Hurbain, I., Sibarita, J.-B., Chavrier, P., et al., 2004. TI-VAMP/VAMP7 is required for optimal phagocytosis of opsonised particles in macrophages. EMBO J. 23, 4166-4176.
    • (2004) EMBO J , vol.23 , pp. 4166-4176
    • Braun, V.1    Fraisier, V.2    Raposo, G.3    Hurbain, I.4    Sibarita, J.-B.5    Chavrier, P.6
  • 75
    • 0025606401 scopus 로고
    • Regulation of microtubule dynamics and nucleation during polarization in MDCK II cells
    • Bré, M.-H., Pepperkok, R., Hill, A.M., Levilliers, N., Ansorge, W., Stelzer, E.H.K., et al., 1990. Regulation of microtubule dynamics and nucleation during polarization in MDCK II cells. J. Cell Biol. 111, 3013-3021.
    • (1990) J. Cell Biol. , vol.111 , pp. 3013-3021
    • Bré, M.-H.1    Pepperkok, R.2    Hill, A.M.3    Levilliers, N.4    Ansorge, W.5    Stelzer, E.H.K.6
  • 76
    • 0023238873 scopus 로고
    • Currents through the fusion pore that forms during exocytosis of a secretory vesicle
    • Breckenridge, L.J., Almers, W., 1987. Currents through the fusion pore that forms during exocytosis of a secretory vesicle. Nature 328, 814-817.
    • (1987) Nature , vol.328 , pp. 814-817
    • Breckenridge, L.J.1    Almers, W.2
  • 77
  • 78
    • 66449088593 scopus 로고    scopus 로고
    • Regulation of the V-ATPase in kidney epithelial cells: dual role in acid-base homeostasis and vesicle trafficking
    • Brown, D., Paunescu, T.G., Breton, S., Marshansky, V., 2009. Regulation of the V-ATPase in kidney epithelial cells: dual role in acid-base homeostasis and vesicle trafficking. J. Exp. Biol. 212, 1762-1772.
    • (2009) J. Exp. Biol. , vol.212 , pp. 1762-1772
    • Brown, D.1    Paunescu, T.G.2    Breton, S.3    Marshansky, V.4
  • 79
    • 49249106612 scopus 로고    scopus 로고
    • Highly specific interactions between botulinum neurotoxins and synaptic vesicle proteins
    • Brunger, A.T., Jin, R., Breidenbach, M.A., 2008. Highly specific interactions between botulinum neurotoxins and synaptic vesicle proteins. Cell. Mol. Life Sci. 65, 2296-2306.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 2296-2306
    • Brunger, A.T.1    Jin, R.2    Breidenbach, M.A.3
  • 81
    • 0742272120 scopus 로고    scopus 로고
    • A complete set of SNAREs in yeast
    • Burri, L., Lithgow, T., 2004. A complete set of SNAREs in yeast. Traffic 5, 45-52.
    • (2004) Traffic , vol.5 , pp. 45-52
    • Burri, L.1    Lithgow, T.2
  • 82
    • 34247623568 scopus 로고    scopus 로고
    • Coats, tethers, Rabs, and SNAREs work together to mediate the intracellular destination of a transport vesicle
    • Cai, H., Reinisch, K., Ferro-Novick, S., 2007. Coats, tethers, Rabs, and SNAREs work together to mediate the intracellular destination of a transport vesicle. Dev. Cell 12, 671-682.
    • (2007) Dev. Cell , vol.12 , pp. 671-682
    • Cai, H.1    Reinisch, K.2    Ferro-Novick, S.3
  • 83
    • 13244295520 scopus 로고    scopus 로고
    • The highways and byways of prion protein trafficking
    • Campana, V., Sarnataro, D., Zurzolo, C., 2005. The highways and byways of prion protein trafficking. Trends Cell Biol. 15, 102-111.
    • (2005) Trends Cell Biol , vol.15 , pp. 102-111
    • Campana, V.1    Sarnataro, D.2    Zurzolo, C.3
  • 84
    • 18344381438 scopus 로고    scopus 로고
    • Actin and Arf1-dependent recruitment of a cortactin-dynamin complex to the Golgi regulates post-Golgi transport
    • Cao, H., Weller, S., Orth, J.D., Chen, J., Huang, B., Chen, J.-L., et al., 2005. Actin and Arf1-dependent recruitment of a cortactin-dynamin complex to the Golgi regulates post-Golgi transport. Nat. Cell Biol. 7, 483-492.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 483-492
    • Cao, H.1    Weller, S.2    Orth, J.D.3    Chen, J.4    Huang, B.5    Chen, J.-L.6
  • 85
    • 0033846583 scopus 로고    scopus 로고
    • Paramecium GPI proteins: variability of expression and localization
    • Capdeville, Y., 2000. Paramecium GPI proteins: variability of expression and localization. Protist 151, 161-169.
    • (2000) Protist , vol.151 , pp. 161-169
    • Capdeville, Y.1
  • 86
    • 14644391576 scopus 로고    scopus 로고
    • Calcium-a universal carrier of biological signals
    • Carafoli, E., 2005. Calcium-a universal carrier of biological signals. FEBS J. 272, 1073-1089.
    • (2005) FEBS J , vol.272 , pp. 1073-1089
    • Carafoli, E.1
  • 88
    • 0030898528 scopus 로고    scopus 로고
    • Germline and somatic transformation of mating Tetrahymena thermophila by particle bombardement
    • Cassidy-Hanley, D., Bowen, J., Lee, J.H., Cole, E., VerPlank, L.A., Gaertig, J., et al., 1997. Germline and somatic transformation of mating Tetrahymena thermophila by particle bombardement. Genetics 146, 135-147.
    • (1997) Genetics , vol.146 , pp. 135-147
    • Cassidy-Hanley, D.1    Bowen, J.2    Lee, J.H.3    Cole, E.4    VerPlank, L.A.5    Gaertig, J.6
  • 89
    • 0036208071 scopus 로고    scopus 로고
    • The phagotropic origin of eukaryotes and phylogenetic classification of protozoa
    • Cavalier-Smith, T., 2002. The phagotropic origin of eukaryotes and phylogenetic classification of protozoa. Int. J. Syst. Evol. Microbiol. 52, 297-354.
    • (2002) Int. J. Syst. Evol. Microbiol. , vol.52 , pp. 297-354
    • Cavalier-Smith, T.1
  • 90
    • 46449093538 scopus 로고    scopus 로고
    • How does synaptotagmin trigger neurotransmitter release?
    • Chapman, E.R., 2008. How does synaptotagmin trigger neurotransmitter release? Annu. Rev. Biochem. 77, 615-641.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 615-641
    • Chapman, E.R.1
  • 91
    • 0030478918 scopus 로고    scopus 로고
    • Granule lattice protein 1 (Grl1p), an acidic, calcium-binding protein in Tetrahymena thermophila dense core secretory granules, influences granule size, shape, content organization, and release but not protein sorting or condensation
    • Chilcoat, N.D., Melia, S.M., Haddad, A., Turkewitz, A.P., 1996. Granule lattice protein 1 (Grl1p), an acidic, calcium-binding protein in Tetrahymena thermophila dense core secretory granules, influences granule size, shape, content organization, and release but not protein sorting or condensation. J. Cell Biol. 135, 1775-1787.
    • (1996) J. Cell Biol. , vol.135 , pp. 1775-1787
    • Chilcoat, N.D.1    Melia, S.M.2    Haddad, A.3    Turkewitz, A.P.4
  • 92
    • 0035902470 scopus 로고    scopus 로고
    • An antisense approach to phenotypebased gene cloning in Tetrahymena
    • Chilcoat, N.D., Elde, N.C., Turkewitz, A.P., 2001. An antisense approach to phenotypebased gene cloning in Tetrahymena. Proc. Natl. Acad. Sci. USA 98, 8709-8713.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8709-8713
    • Chilcoat, N.D.1    Elde, N.C.2    Turkewitz, A.P.3
  • 93
    • 34547559208 scopus 로고    scopus 로고
    • SARA-regulated vesicular targeting underlies formation of the light-sensing organelle in mammalian rods
    • Chuang, J.-Z., Zhao, Y., Sung, C.-H., 2007. SARA-regulated vesicular targeting underlies formation of the light-sensing organelle in mammalian rods. Cell 130, 535-547.
    • (2007) Cell , vol.130 , pp. 535-547
    • Chuang, J.-Z.1    Zhao, Y.2    Sung, C.-H.3
  • 94
    • 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
  • 95
    • 0021665182 scopus 로고
    • Actin microfilaments in Paramecium: localization and role in intracellular movements
    • Cohen, J., Garreau De Loubresse, N., Beisson, J., 1984. Actin microfilaments in Paramecium: localization and role in intracellular movements. Cell Motil. 4, 443-468.
    • (1984) Cell Motil , vol.4 , pp. 443-468
    • Cohen, J.1    Garreau De Loubresse, N.2    Beisson, J.3
  • 96
    • 0019888460 scopus 로고
    • Post-translational cleavage of mucocyst precursors in Tetrahymena
    • Collins, T., Wilhelm, J.M., 1981. Post-translational cleavage of mucocyst precursors in Tetrahymena. J. Biol. Chem. 256, 10475-10484.
    • (1981) J. Biol. Chem. , vol.256 , pp. 10475-10484
    • Collins, T.1    Wilhelm, J.M.2
  • 97
    • 0035895981 scopus 로고    scopus 로고
    • Requirement for N-ethylmaleimide-sensitive factor activity at different stages of bacterial invasion and phagocytosis
    • Coppolino, M.G., Kong, C., Mohtashami, M., Schreiber, A.D., Brumell, J.H., Finlay, B.B., et al., 2001. Requirement for N-ethylmaleimide-sensitive factor activity at different stages of bacterial invasion and phagocytosis. J. Biol. Chem. 276, 4772-4780.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4772-4780
    • Coppolino, M.G.1    Kong, C.2    Mohtashami, M.3    Schreiber, A.D.4    Brumell, J.H.5    Finlay, B.B.6
  • 98
    • 24344486424 scopus 로고    scopus 로고
    • Genetic, genomic, and functional analysis of the granule lattice proteins in Tetrahymena secretory granules
    • Cowan, A.T., Bowman, G.R., Edwards, K.F., Emerson, J.J., Turkewitz, A.P., 2005. Genetic, genomic, and functional analysis of the granule lattice proteins in Tetrahymena secretory granules. Mol. Biol. Cell 16, 4046-4060.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4046-4060
    • Cowan, A.T.1    Bowman, G.R.2    Edwards, K.F.3    Emerson, J.J.4    Turkewitz, A.P.5
  • 99
    • 0034681147 scopus 로고    scopus 로고
    • A rab11-containing rapidly recycling compartment in macrophages that promotes phagocytosis
    • Cox, D., Lee, D.J., Dale, B.M., Calafat, J., Greenberg, S., 2000. A rab11-containing rapidly recycling compartment in macrophages that promotes phagocytosis. Proc. Natl. Acad. Sci. USA 97, 680-685.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 680-685
    • Cox, D.1    Lee, D.J.2    Dale, B.M.3    Calafat, J.4    Greenberg, S.5
  • 100
    • 58149307926 scopus 로고    scopus 로고
    • Refined annotation and assembly of the Tetrahymena thermophila genome sequence through EST analysis, comparative genomic hybridization, and targeted gap closure
    • doi:10.1186/1471-2164-9-562
    • Coyne, R.S., Thiagarajan, M., Jones, K.M., Wortman, J.R., Tallon, L.J., Haas, B.J., et al., 2008. Refined annotation and assembly of the Tetrahymena thermophila genome sequence through EST analysis, comparative genomic hybridization, and targeted gap closure. BMC Genomics 9, 562. doi:10.1186/1471-2164-9-562.
    • (2008) BMC Genomics , vol.9 , pp. 562
    • Coyne, R.S.1    Thiagarajan, M.2    Jones, K.M.3    Wortman, J.R.4    Tallon, L.J.5    Haas, B.J.6
  • 101
    • 34548648653 scopus 로고    scopus 로고
    • Evolutionary genomics of plant genes encoding N-terminal-TM-C2 domain proteins and the similar FAM62 genes and synaptotagmin genes of metazoans
    • doi:10.1186/1471-2164-8-259
    • Craxton, M., 2007. Evolutionary genomics of plant genes encoding N-terminal-TM-C2 domain proteins and the similar FAM62 genes and synaptotagmin genes of metazoans. BMC Genomics 8, 259 doi:10.1186/1471-2164-8-259.
    • (2007) BMC Genomics , vol.8 , pp. 259
    • Craxton, M.1
  • 102
    • 0031939689 scopus 로고    scopus 로고
    • The copines, a novel class of C2 domain-containing, calcium dependent, phospholipidbinding proteins conserved from Paramecium to humans
    • Creutz, C.E., Tomsig, J.L., Snyder, S.L., Gautier, M.-C., Skouri, F., Beisson, J., et al., 1998. The copines, a novel class of C2 domain-containing, calcium dependent, phospholipidbinding proteins conserved from Paramecium to humans. J. Biol. Chem. 273, 1393-1402.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1393-1402
    • Creutz, C.E.1    Tomsig, J.L.2    Snyder, S.L.3    Gautier, M.-C.4    Skouri, F.5    Beisson, J.6
  • 104
    • 34948835726 scopus 로고    scopus 로고
    • Evolution of the eukaryotic membrane-trafficking system: origin, tempo and mode
    • Dacks, J.B., Field, M.C., 2007. Evolution of the eukaryotic membrane-trafficking system: origin, tempo and mode. J. Cell Sci. 120, 2977-2985.
    • (2007) J. Cell Sci. , vol.120 , pp. 2977-2985
    • Dacks, J.B.1    Field, M.C.2
  • 105
    • 0042663808 scopus 로고    scopus 로고
    • Microfilaments and microtubules regulate recycling from phagosomes
    • Damiani, M.T., Colombo, M.I., 2003. Microfilaments and microtubules regulate recycling from phagosomes. Exp. Cell Res. 289, 152-161.
    • (2003) Exp. Cell Res. , vol.289 , pp. 152-161
    • Damiani, M.T.1    Colombo, M.I.2
  • 106
    • 33745800098 scopus 로고    scopus 로고
    • Structural determinants of synaptobrevin 2 function in synaptic vesicle fusion
    • Déak, F., Shin, O.-H., Kavalali, E.T., Südhof, T.C., 2006. Structural determinants of synaptobrevin 2 function in synaptic vesicle fusion. J. Neurosci. 26, 6668-6676.
    • (2006) J. Neurosci. , vol.26 , pp. 6668-6676
    • Déak, F.1    Shin, O.-H.2    Kavalali, E.T.3    Südhof, T.C.4
  • 107
    • 64749107397 scopus 로고    scopus 로고
    • Munc 18-1 binding to the neuronal SNARE complex controls synaptic vesicle priming
    • Déak, F., Xu, Y., Dulubova, I., Khvotchev, M., Liu, X., Südhof, T.C., et al., 2009. Munc 18-1 binding to the neuronal SNARE complex controls synaptic vesicle priming. J. Cell Biol. 184, 751-764.
    • (2009) J. Cell Biol. , vol.184 , pp. 751-764
    • Déak, F.1    Xu, Y.2    Dulubova, I.3    Khvotchev, M.4    Liu, X.5    Südhof, T.C.6
  • 109
    • 0025035566 scopus 로고
    • Microtubular systems of Paramecium in division: pattern of cytospindle assembly
    • Delgado, P., Romero, M.R., Torres, A., 1990. Microtubular systems of Paramecium in division: pattern of cytospindle assembly. J. Protozool. 37, 182-186.
    • (1990) J. Protozool. , vol.37 , pp. 182-186
    • Delgado, P.1    Romero, M.R.2    Torres, A.3
  • 111
    • 34247543907 scopus 로고    scopus 로고
    • Sending proteins to dense core secretory granules: still a lot to sort out
    • Dikeakos, J.D., Reudelhuber, T.L., 2007. Sending proteins to dense core secretory granules: still a lot to sort out. J. Cell Biol. 177, 191-196.
    • (2007) J. Cell Biol. , vol.177 , pp. 191-196
    • Dikeakos, J.D.1    Reudelhuber, T.L.2
  • 112
    • 67649616340 scopus 로고    scopus 로고
    • Structural insights into the calmodulin-Munc13 interaction obtained by crosslinking and mass spectrometry
    • Dimova, K., Kalkhof, S., Pottratz, I., Ihling, C., Rodriguez-Cataneda, F., Liepold, T., et al., 2009. Structural insights into the calmodulin-Munc13 interaction obtained by crosslinking and mass spectrometry. Biochemistry 48, 5908-5921.
    • (2009) Biochemistry , vol.48 , pp. 5908-5921
    • Dimova, K.1    Kalkhof, S.2    Pottratz, I.3    Ihling, C.4    Rodriguez-Cataneda, F.5    Liepold, T.6
  • 113
    • 33645796449 scopus 로고    scopus 로고
    • Catalytic and mechanical cycles in F-ATP synthases
    • Dimroth, P., Ballmos, C.v., Meier, T., 2006. Catalytic and mechanical cycles in F-ATP synthases. EMBO Rep. 7, 276-282.
    • (2006) EMBO Rep , vol.7 , pp. 276-282
    • Dimroth, P.1    Ballmos, C.v.2    Meier, T.3
  • 114
    • 33746627569 scopus 로고    scopus 로고
    • Factors regulating the abundance and localization of synaptobrevin in the plasma membrane
    • Dittman, J.S., Kaplan, J.M., 2006. Factors regulating the abundance and localization of synaptobrevin in the plasma membrane. Proc. Natl. Acad. Sci. USA 103, 11399-11404.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 11399-11404
    • Dittman, J.S.1    Kaplan, J.M.2
  • 115
    • 48249134102 scopus 로고    scopus 로고
    • Mediation, modulation, and consequences of membrane-cytoskeleton interactions
    • Doherty, G.J., McMahon, H.T., 2008. Mediation, modulation, and consequences of membrane-cytoskeleton interactions. Annu. Rev. Biophys. Biomol. Struct. 37, 65-95.
    • (2008) Annu. Rev. Biophys. Biomol. Struct. , vol.37 , pp. 65-95
    • Doherty, G.J.1    McMahon, H.T.2
  • 116
  • 117
    • 41649113803 scopus 로고    scopus 로고
    • Analysis of sequence variability in the macronuclear DNA of Paramecium tetraurelia: a somatic view of the germline
    • Duret, L., Cohen, J., Jubin, C., Dessen, P., Gout, J.-F., Mousset, S., et al., 2008. Analysis of sequence variability in the macronuclear DNA of Paramecium tetraurelia: a somatic view of the germline. Genome Res. 18, 585-596.
    • (2008) Genome Res , vol.18 , pp. 585-596
    • Duret, L.1    Cohen, J.2    Jubin, C.3    Dessen, P.4    Gout, J.-F.5    Mousset, S.6
  • 118
    • 4444224966 scopus 로고    scopus 로고
    • Endocytosis by random: initiation and stabilization of clathrin-coated pits
    • Ehrlich, M., Boll, W., Van Oijen, A., Hariharan, R., Chandran, K., Nibert, M.L., et al., 2004. Endocytosis by random: initiation and stabilization of clathrin-coated pits. Cell 118, 591-605.
    • (2004) Cell , vol.118 , pp. 591-605
    • Ehrlich, M.1    Boll, W.2    Van Oijen, A.3    Hariharan, R.4    Chandran, K.5    Nibert, M.L.6
  • 119
    • 33748598232 scopus 로고    scopus 로고
    • Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a model eukaryote
    • Eisen, J.A., Coyne, R.S., Wu, M., Wu, D., Thiagarajan, M., Wortman, J.R., et al., 2006. Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a model eukaryote. PLoS Biol. 4, 1620-1644 e286.
    • (2006) PLoS Biol , vol.4 , pp. 1620-1644
    • Eisen, J.A.1    Coyne, R.S.2    Wu, M.3    Wu, D.4    Thiagarajan, M.5    Wortman, J.R.6
  • 120
    • 0037135973 scopus 로고    scopus 로고
    • Remodeling of organelle-bound actin is required for yeast vacuole fusion
    • Eitzen, G., Wang, L., Thorngren, N., Wickner, W., 2002. Remodeling of organelle-bound actin is required for yeast vacuole fusion. J. Cell Biol. 158, 669-679.
    • (2002) J. Cell Biol. , vol.158 , pp. 669-679
    • Eitzen, G.1    Wang, L.2    Thorngren, N.3    Wickner, W.4
  • 121
    • 55449130503 scopus 로고    scopus 로고
    • Elucidation of clathrin-mediated endocytosis in Tetrahymena reveals an evolutionarily convergent recruitment of dynamin
    • doi.org/101371.Journal.pgen.0010052
    • 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, 514-526. doi.org/10.1371.Journal.pgen.0010052.
    • (2005) PLoS Genet , vol.1 , pp. 514-526
    • Elde, N.C.1    Morgan, G.2    Winey, M.3    Sperling, L.4    Turkewitz, A.P.5
  • 122
    • 33947726724 scopus 로고    scopus 로고
    • A role for convergent evolution in the secretory life of cells
    • Elde, N.C., Long, M., Turkewitz, A.P., 2007. A role for convergent evolution in the secretory life of cells. Trends Cell Biol. 17, 157-164.
    • (2007) Trends Cell Biol , vol.17 , pp. 157-164
    • Elde, N.C.1    Long, M.2    Turkewitz, A.P.3
  • 123
    • 58149094424 scopus 로고    scopus 로고
    • Characterization of SNAREs determines the absence of a typical Golgi apparatus in the ancient eukaryote Giardia lamblia
    • Elias, E.V., Quiroga, R., Gottig, N., Nakanishi, H., Nash, T.E., Neiman, A., et al., 2008. Characterization of SNAREs determines the absence of a typical Golgi apparatus in the ancient eukaryote Giardia lamblia. J. Biol. Chem. 283, 35996-36010.
    • (2008) J. Biol. Chem. , vol.283 , pp. 35996-36010
    • Elias, E.V.1    Quiroga, R.2    Gottig, N.3    Nakanishi, H.4    Nash, T.E.5    Neiman, A.6
  • 124
    • 66949128729 scopus 로고    scopus 로고
    • Identification of a palmitoyl acyltransferase required for protein sorting to the flagellar membrane
    • Emmer, B.T., Souther, C., Toriello, K.M., Olson, C.L., Epting, C.L., Engman, D.M., 2009. Identification of a palmitoyl acyltransferase required for protein sorting to the flagellar membrane. J. Cell Sci. 122, 867-874.
    • (2009) J. Cell Sci. , vol.122 , pp. 867-874
    • Emmer, B.T.1    Souther, C.2    Toriello, K.M.3    Olson, C.L.4    Epting, C.L.5    Engman, D.M.6
  • 125
    • 0343230883 scopus 로고
    • L'appareil de Golgi des ciliés. Ultrastructure, particulièrement chez Paramecium
    • Estève, J.C., 1972. L'appareil de Golgi des ciliés. Ultrastructure, particulièrement chez Paramecium. J. Protozool. 19, 609-618.
    • (1972) J. Protozool. , vol.19 , pp. 609-618
    • Estève, J.C.1
  • 126
    • 55749113538 scopus 로고    scopus 로고
    • The role of the C+ terminus of the SNARE protein SNAP-25 in fusion pore opening and a model for fusion pore mechanics
    • Fang, Q., Berberian, K., Gong, L.-W., Hafez, I., Sorensen, J.B., Lindau, M., 2008. The role of the C terminus of the SNARE protein SNAP-25 in fusion pore opening and a model for fusion pore mechanics. Proc. Natl. Acad. Sci. USA 105, 15388-15392.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 15388-15392
    • Fang, Q.1    Berberian, K.2    Gong, L.-W.3    Hafez, I.4    Sorensen, J.B.5    Lindau, M.6
  • 127
    • 0032430423 scopus 로고    scopus 로고
    • Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Qand R-SNAREs
    • Fasshauer, D., Sutton, R.B., Brunger, A.T., Jahn, R., 1998. Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Qand R-SNAREs. Proc. Natl. Acad. Sci. USA 95, 15781-15786.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15781-15786
    • Fasshauer, D.1    Sutton, R.B.2    Brunger, A.T.3    Jahn, R.4
  • 128
    • 67349242412 scopus 로고    scopus 로고
    • Actin and dynamin recruitment and the lack thereof at exoand endocytotic sites in PC12 cells
    • Felmy, F., 2009. Actin and dynamin recruitment and the lack thereof at exoand endocytotic sites in PC12 cells. Pflugers Arch. Eur. J. Physiol. 458, 403-417.
    • (2009) Pflugers Arch. Eur. J. Physiol. , vol.458 , pp. 403-417
    • Felmy, F.1
  • 130
    • 0344428151 scopus 로고    scopus 로고
    • Immuno-labeling analysis of biogenetic and degradative pathways of cell surface components (glycocalyx) in Paramecium cells
    • Flötenmeyer, M., Momayezi, M., Plattner, H., 1999. Immuno-labeling analysis of biogenetic 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
  • 131
    • 62149148157 scopus 로고    scopus 로고
    • A VAMP7/Vti1a SNARE complex distinguishes a non-conventional traffic route to the cell surface used by KchlP1 and Kv4 potassium channels
    • Flowerdew, S.E., Burgoyne, R.D., 2009. A VAMP7/Vti1a SNARE complex distinguishes a non-conventional traffic route to the cell surface used by KchlP1 and Kv4 potassium channels. Biochem. J. 418, 529-540.
    • (2009) Biochem. J. , vol.418 , pp. 529-540
    • Flowerdew, S.E.1    Burgoyne, R.D.2
  • 132
    • 0003122529 scopus 로고
    • The lysosomal system
    • Goertz, H.D. (Ed.), Springer-Verlag, Berlin, Heidelberg, New York
    • Fok, A.K., Allen, R.D., 1988. The lysosomal system. In: Goertz, H.D. (Ed.), Paramecium. Springer-Verlag, Berlin, Heidelberg, New York, pp. 301-324.
    • (1988) Paramecium , pp. 301-324
    • Fok, A.K.1    Allen, R.D.2
  • 133
    • 0025643091 scopus 로고
    • The phagosome-lysosome membrane system and its regulation in Paramecium
    • Fok, A.K., Allen, R.D., 1990. The phagosome-lysosome membrane system and its regulation in Paramecium. Int. Rev. Cytol. 123, 61-94.
    • (1990) Int. Rev. Cytol. , vol.123 , pp. 61-94
    • Fok, A.K.1    Allen, R.D.2
  • 134
    • 0020137079 scopus 로고
    • Lysosomal enzymes of Paramecium caudatum and Paramecium tetraurelia
    • Fok, A.K., Paeste, R.M., 1982. Lysosomal enzymes of Paramecium caudatum and Paramecium tetraurelia. Exp. Cell Res. 139, 159-169.
    • (1982) Exp. Cell Res. , vol.139 , pp. 159-169
    • Fok, A.K.1    Paeste, R.M.2
  • 135
    • 84985044169 scopus 로고
    • The correlation of digestive vacuole pH and size with the digestive cycle in Paramecium caudatum
    • Fok, A.K., Lee, Y., Allen, R.D., 1982. The correlation of digestive vacuole pH and size with the digestive cycle in Paramecium caudatum. J. Protozool. 29, 409-414.
    • (1982) J. Protozool. , vol.29 , pp. 409-414
    • Fok, A.K.1    Lee, Y.2    Allen, R.D.3
  • 136
    • 0021893207 scopus 로고
    • Modulation of the digestive lysosomal system in Paramecium caudatum. II. Physiological effects of cytochalasin B, colchicine and trifluoperazine
    • Fok, A.K., Leung, S.S.-K., Chun, D.P., Allen, R.D., 1985. Modulation of the digestive lysosomal system in Paramecium caudatum. II. Physiological effects of cytochalasin B, colchicine and trifluoperazine. Eur. J. Cell Biol. 37, 27-34.
    • (1985) Eur. J. Cell Biol. , vol.37 , pp. 27-34
    • Fok, A.K.1    Leung, S.-K.2    Chun, D.P.3    Allen, R.D.4
  • 137
    • 0023356339 scopus 로고
    • Phagosomal acidification in Paramecium: effects on lysosomal fusion
    • Fok, A.K., Ueno, M.S., Azada, E.A., Allen, R.D., 1987. Phagosomal acidification in Paramecium: effects on lysosomal fusion. Eur. J. Cell Biol. 43, 412-420.
    • (1987) Eur. J. Cell Biol. , vol.43 , pp. 412-420
    • Fok, A.K.1    Ueno, M.S.2    Azada, E.A.3    Allen, R.D.4
  • 138
    • 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
  • 139
    • 0036063275 scopus 로고    scopus 로고
    • The vacuolar-ATPase of Paramecium multimicronuleatum gene structure of the B subunit and the dynamics of the V-ATPase-rich osmoregulatory membranes
    • Fok, A.K., Yamauchi, K., Ishihara, A., Aihara, M.S., Ishida, M., Allen, A.R., 2002. The vacuolar-ATPase of Paramecium multimicronuleatum gene structure of the B subunit and the dynamics of the V-ATPase-rich osmoregulatory membranes. J. Eukaryot. Microbiol. 49, 185-196.
    • (2002) J. Eukaryot. Microbiol. , vol.49 , pp. 185-196
    • Fok, A.K.1    Yamauchi, K.2    Ishihara, A.3    Aihara, M.S.4    Ishida, M.5    Allen, A.R.6
  • 140
    • 57749181967 scopus 로고    scopus 로고
    • Calmodulin localization and its effects on endocytotic and phagocytotic membrane trafficking in Paramecium multimicronucleatum
    • Fok, A.K., Aihara, M.S., Ishida, M., Allen, R.D., 2008. Calmodulin localization and its effects on endocytotic and phagocytotic membrane trafficking in Paramecium multimicronucleatum. J. Eukaryot. Microbiol. 55, 481-491.
    • (2008) J. Eukaryot. Microbiol. , vol.55 , pp. 481-491
    • Fok, A.K.1    Aihara, M.S.2    Ishida, M.3    Allen, R.D.4
  • 141
    • 33748327050 scopus 로고    scopus 로고
    • The intraflagellar transport protein IFT20 is associated with the Golgi complex and is required for cilia assembly
    • Follit, J.A., Tuft, R.A., Fogarty, K.E., Pazour, G.J., 2006. The intraflagellar transport protein IFT20 is associated with the Golgi complex and is required for cilia assembly. Mol. Biol. Cell 17, 3781-3792.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3781-3792
    • Follit, J.A.1    Tuft, R.A.2    Fogarty, K.E.3    Pazour, G.J.4
  • 142
    • 51849157397 scopus 로고    scopus 로고
    • Intermediate organelles of the plant secretory pathway: identity and function
    • Foresti, O., Denecke, J., 2008. Intermediate organelles of the plant secretory pathway: identity and function. Traffic 9, 1599-1612.
    • (2008) Traffic , vol.9 , pp. 1599-1612
    • Foresti, O.1    Denecke, J.2
  • 143
    • 35448946098 scopus 로고    scopus 로고
    • Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology
    • Forgac, M., 2007. Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology. Nat. Rev. Mol. Cell Biol. 8, 917-929.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 917-929
    • Forgac, M.1
  • 144
    • 0028133493 scopus 로고
    • The identification of a complex family of low-molecularweight GTP-binding protein homologues from Paramecium tetraurelia by PCR cloning
    • Fraga, D., Hinrichsen, R.D., 1994. The identification of a complex family of low-molecularweight GTP-binding protein homologues from Paramecium tetraurelia by PCR cloning. Gene 147, 145-148.
    • (1994) Gene , vol.147 , pp. 145-148
    • Fraga, D.1    Hinrichsen, R.D.2
  • 146
    • 0033989699 scopus 로고    scopus 로고
    • Cell biology of Tetrahymena thermophila
    • Frankel, J., 2000. Cell biology of Tetrahymena thermophila. Methods Cell Biol. 62, 27-125.
    • (2000) Methods Cell Biol , vol.62 , pp. 27-125
    • Frankel, J.1
  • 147
    • 34250851923 scopus 로고    scopus 로고
    • Coassembly of flotillins induces formation of membrane microdomains, membrane curvature, and vesicle budding
    • Frick, M., Bright, N.A., Riento, K., Bray, A., Merrifield, C., Nichols, B.J., 2007. Coassembly of flotillins induces formation of membrane microdomains, membrane curvature, and vesicle budding. Curr. Biol. 17, 1151-1156.
    • (2007) Curr. Biol. , vol.17 , pp. 1151-1156
    • Frick, M.1    Bright, N.A.2    Riento, K.3    Bray, A.4    Merrifield, C.5    Nichols, B.J.6
  • 148
    • 0035105036 scopus 로고    scopus 로고
    • ND9P, a novel protein with armadillo-like repeats involved in exocytosis: physiological studies using allelic mutants in Paramecium
    • Froissard, M., Keller, A.M., Cohen, J., 2001. ND9P, a novel protein with armadillo-like repeats involved in exocytosis: physiological studies using allelic mutants in Paramecium. Genetics 157, 611-620.
    • (2001) Genetics , vol.157 , pp. 611-620
    • Froissard, M.1    Keller, A.M.2    Cohen, J.3
  • 149
    • 0035989389 scopus 로고    scopus 로고
    • N-Ethylmaleimide-sensitive factor is required to organize functional exocytotic microdomains in Paramecium
    • Froissard, M., Kissmehl, R., Dedieu, J.-C., Gulik-Krzywicki, T., Plattner, H., Cohen, J., 2002. N-Ethylmaleimide-sensitive factor is required to organize functional exocytotic microdomains in Paramecium. Genetics 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
  • 150
    • 3142683683 scopus 로고    scopus 로고
    • Novel secretory vesicle proteins essential for membrane fusion display extracellular-matrix domains
    • Froissard, M., Keller, A.-M., Dedieu, J.-C., Cohen, J., 2004. Novel secretory vesicle proteins essential for membrane fusion display extracellular-matrix domains. Traffic 5, 493-502.
    • (2004) Traffic , vol.5 , pp. 493-502
    • Froissard, M.1    Keller, A.-M.2    Dedieu, J.-C.3    Cohen, J.4
  • 151
    • 0034648771 scopus 로고    scopus 로고
    • Functional architecture of an intracellular membrane t-SNARE
    • Fukuda, R., McNew, J.A., Weber, T., Parlati, F., Engel, T., Nickel, W., et al., 2000. Functional architecture of an intracellular membrane t-SNARE. Nature 407, 198-202.
    • (2000) Nature , vol.407 , pp. 198-202
    • Fukuda, R.1    McNew, J.A.2    Weber, T.3    Parlati, F.4    Engel, T.5    Nickel, W.6
  • 152
    • 0034118251 scopus 로고    scopus 로고
    • Molecular mechanisms of microtubular organelle assembly in Tetrahymena
    • Gaertig, J., 2000. Molecular mechanisms of microtubular organelle assembly in Tetrahymena. J. Eukaryot. Microbiol. 47, 185-190.
    • (2000) J. Eukaryot. Microbiol. , vol.47 , pp. 185-190
    • Gaertig, J.1
  • 153
    • 0028661172 scopus 로고
    • High frequency vector-mediated transformation and gene replacement in Tetrahymena
    • Gaertig, J., Gu, L., Hai, B., Gorovsky, M.A., 1994. High frequency vector-mediated transformation and gene replacement in Tetrahymena. Nucleic Acid Res. 22, 5391-5398.
    • (1994) Nucleic Acid Res , vol.22 , pp. 5391-5398
    • Gaertig, J.1    Gu, L.2    Hai, B.3    Gorovsky, M.A.4
  • 154
    • 0033836520 scopus 로고    scopus 로고
    • The recycling endosome of Madin-Darby canine kidney cells is a mildly acidic compartment rich in raft components
    • Gagescu, R., Demaurex, N., Parton, R.G., Hunziker, W., Huber, L.A., Gruenberg, J., 2000. The recycling endosome of Madin-Darby canine kidney cells is a mildly acidic compartment rich in raft components. Mol. Biol. Cell 11, 2775-2791.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2775-2791
    • Gagescu, R.1    Demaurex, N.2    Parton, R.G.3    Hunziker, W.4    Huber, L.A.5    Gruenberg, J.6
  • 155
    • 60749098725 scopus 로고    scopus 로고
    • Actin and endocytosis: mechanisms and phylogeny
    • Galletta, B.J., Cooper, J.A., 2009. Actin and endocytosis: mechanisms and phylogeny. Curr. Opin. Cell Biol. 21, 20-27.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 20-27
    • Galletta, B.J.1    Cooper, J.A.2
  • 156
    • 85031257012 scopus 로고    scopus 로고
    • VAMP7. UCSD Nat. Mol. Pages. 10. 1038/mp.a003510.01
    • Galli, T., D'Esposito, M., Sotirakis, E., 2006. VAMP7. UCSD Nat. Mol. Pages. 10.1038/mp.a003510.01.
    • (2006)
    • Galli, T.1    D'Esposito, M.2    Sotirakis, E.3
  • 158
    • 0036137143 scopus 로고    scopus 로고
    • RNA interference by feeding in Paramecium
    • Galvani, A., Sperling, L., 2002. RNA interference by feeding in Paramecium. Trends Genet. 18, 11-12.
    • (2002) Trends Genet , vol.18 , pp. 11-12
    • Galvani, A.1    Sperling, L.2
  • 160
    • 4344648254 scopus 로고    scopus 로고
    • RNA-mediated programming of developmental genome rearrangements in Paramecium tetraurelia
    • Garnier, O., Serrano, V., Duharcourt, S., Meyer, E., 2004. RNA-mediated programming of developmental genome rearrangements in Paramecium tetraurelia. Mol. Cell. Biol. 24, 7370-7379.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 7370-7379
    • Garnier, O.1    Serrano, V.2    Duharcourt, S.3    Meyer, E.4
  • 162
    • 0028672211 scopus 로고
    • Immature secretory granules are not acidic in Paramecium: implications for sorting to the regulated pathway
    • Garreau De Loubresse, N., Gautier, M.-C., Sperling, L., 1994. Immature secretory granules are not acidic in Paramecium: implications for sorting to the regulated pathway. Biol. Cell 82, 139-147.
    • (1994) Biol. Cell , vol.82 , pp. 139-147
    • Garreau De Loubresse, N.1    Gautier, M.-C.2    Sperling, L.3
  • 163
    • 0016331513 scopus 로고
    • Observations of a naturally-occurring latice array of ribosomes in ultrathin section of Ajellomyces dermatitidis
    • Garrison, R.G., Boyd, K.S., 1974. Observations of a naturally-occurring latice array of ribosomes in ultrathin section of Ajellomyces dermatitidis. Mycopathol. Mycol. Appl. 54, 335-339.
    • (1974) Mycopathol. Mycol. Appl. , vol.54 , pp. 335-339
    • Garrison, R.G.1    Boyd, K.S.2
  • 164
    • 23444441760 scopus 로고
    • Evidence for defects in membrane traffic in Paramecium secretory mutants unable to produce functional storage granules
    • Gautier, M.-C., Garreau De Loubresse, N., Madeddu, L., Sperling, L., 1994. Evidence for defects in membrane traffic in Paramecium secretory mutants unable to produce functional storage granules. J. Cell Biol. 124, 893-902.
    • (1994) J. Cell Biol. , vol.124 , pp. 893-902
    • Gautier, M.-C.1    Garreau De Loubresse, N.2    Madeddu, L.3    Sperling, L.4
  • 166
    • 34247255039 scopus 로고    scopus 로고
    • Vesicle movements are governed by the size and dynamics of F-actin cytoskeletal structures in bovine chromaffin cells
    • Giner, D., López, I., Villanueva, J., Torres, V., Viniegra, S., Gutiérrez, L.M., 2007. Vesicle movements are governed by the size and dynamics of F-actin cytoskeletal structures in bovine chromaffin cells. Neuroscience 146, 659-669.
    • (2007) Neuroscience , vol.146 , pp. 659-669
    • Giner, D.1    López, I.2    Villanueva, J.3    Torres, V.4    Viniegra, S.5    Gutiérrez, L.M.6
  • 167
    • 84986426160 scopus 로고
    • Secretory proteins and glycoproteins from Paramecium cells
    • Glas-Albrecht, R., Nemeth, A., Plattner, H., 1990. Secretory proteins and glycoproteins from Paramecium cells. Eur. J. Protistol. 26, 149-159.
    • (1990) Eur. J. Protistol. , vol.26 , pp. 149-159
    • Glas-Albrecht, R.1    Nemeth, A.2    Plattner, H.3
  • 168
    • 0025734584 scopus 로고
    • Synchronised secretory organelle docking in Paramecium Saltatory movement along microtubules transiently formed from ciliary basal bodies and selective exclusion of microinjected heterologous organelles
    • Glas-Albrecht, R., Kaesberg, B., Knoll, G., Allmann, K., Pape, R., Plattner, H., 1991. Synchronised secretory organelle docking in Paramecium. Saltatory movement along microtubules transiently formed from ciliary basal bodies and selective exclusion of microinjected heterologous organelles. J. Cell Sci. 100, 45-54.
    • (1991) J. Cell Sci. , vol.100 , pp. 45-54
    • Glas-Albrecht, R.1    Kaesberg, B.2    Knoll, G.3    Allmann, K.4    Pape, R.5    Plattner, H.6
  • 170
    • 29144458972 scopus 로고    scopus 로고
    • ND6P, a novel protein with RCC1-like domains involved in exocytosis in Paramecium
    • Gogendeau, D., Keller, A.M., Yanagi, A., Cohen, J., 2005. ND6P, a novel protein with RCC1-like domains involved in exocytosis in Paramecium. Eukaryot. Cell 4, 2129-2139.
    • (2005) Eukaryot. Cell , vol.4 , pp. 2129-2139
    • Gogendeau, D.1    Keller, A.M.2    Yanagi, A.3    Cohen, J.4
  • 171
    • 0034353225 scopus 로고    scopus 로고
    • 2+/calmodulin-binding proteins are involved in Tetrahymena thermophila phagocytosis
    • 2+/calmodulin-binding proteins are involved in Tetrahymena thermophila phagocytosis. Cell Struct. Funct. 25, 243-251.
    • (2000) Cell Struct. Funct. , vol.25 , pp. 243-251
    • Gonda, K.1    Komatsu, M.2    Numata, O.3
  • 172
    • 0031952838 scopus 로고    scopus 로고
    • SNAP-25 palmitoylation and plasma membrane targeting require a functional secretory pathway
    • Gonzalo, S., Linder, M.E., 1998. SNAP-25 palmitoylation and plasma membrane targeting require a functional secretory pathway. Mol. Biol. Cell 9, 585-597.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 585-597
    • Gonzalo, S.1    Linder, M.E.2
  • 173
    • 17444393115 scopus 로고    scopus 로고
    • Identification of functionally interacting SNAREs by using complementary substitution in the conserved '0' layer
    • Graf, C.T., Riedel, D., Schmitt, H.D., Jahn, R., 2005. Identification of functionally interacting SNAREs by using complementary substitution in the conserved '0' layer. Mol. Biol. Cell 16, 2263-2274.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2263-2274
    • Graf, C.T.1    Riedel, D.2    Schmitt, H.D.3    Jahn, R.4
  • 174
    • 56349114911 scopus 로고    scopus 로고
    • SNAREs-molecular governors in signalling and development
    • Grefen, C., Blatt, M.R., 2008. SNAREs-molecular governors in signalling and development. Curr. Opin. Plant Biol. 11, 600-609.
    • (2008) Curr. Opin. Plant Biol. , vol.11 , pp. 600-609
    • Grefen, C.1    Blatt, M.R.2
  • 175
    • 0032577562 scopus 로고    scopus 로고
    • Sec6/8 complex is recruited to cell-cell contacts and specific transport vesicle delivery to the basal-lateral membrane in epithelial cells
    • Grindstaff, K.K., Yeaman, C., Anandasabapathy, N., Hsu, S.-C., Rodriguez-Boulan, E., Scheller, R.H., et al., 1998. Sec6/8 complex is recruited to cell-cell contacts and specific transport vesicle delivery to the basal-lateral membrane in epithelial cells. Cell 93, 731-740.
    • (1998) Cell , vol.93 , pp. 731-740
    • Grindstaff, K.K.1    Yeaman, C.2    Anandasabapathy, N.3    Hsu, S.-C.4    Rodriguez-Boulan, E.5    Scheller, R.H.6
  • 176
    • 0036023244 scopus 로고    scopus 로고
    • In the polymorphic ciliate Tetrahymena vorax, the non-selective phagocytosis seen in microstomes changes to a highly selective process in macrostomes
    • Gronlien, H.K., Berg, T., Lovlie, A.M., 2002a. In the polymorphic ciliate Tetrahymena vorax, the non-selective phagocytosis seen in microstomes changes to a highly selective process in macrostomes. J. Exp. Biol. 205, 2089-2097.
    • (2002) J. Exp. Biol. , vol.205 , pp. 2089-2097
    • Gronlien, H.K.1    Berg, T.2    Lovlie, A.M.3
  • 177
    • 0036033743 scopus 로고    scopus 로고
    • Relationship between the membrane potential of the contractile vacuole complex and its osmoregulatory activity in Paramecium multimicronucleatum
    • Gronlien, H.K., Stock, C., Aihara, M.S., Allen, R.D., Naitoh, Y., 2002b. Relationship between the membrane potential of the contractile vacuole complex and its osmoregulatory activity in Paramecium multimicronucleatum. J. Exp. Biol. 205, 3261-3270.
    • (2002) J. Exp. Biol. , vol.205 , pp. 3261-3270
    • Gronlien, H.K.1    Stock, C.2    Aihara, M.S.3    Allen, R.D.4    Naitoh, Y.5
  • 178
    • 33747066132 scopus 로고    scopus 로고
    • Rabs and their effectors: achieving specificity in membrane traffic
    • Grosshans, B.L., Ortiz, D., Novick, P., 2006. Rabs and their effectors: achieving specificity in membrane traffic. Proc. Natl. Acad. Sci. USA 103, 11821-11827.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 11821-11827
    • Grosshans, B.L.1    Ortiz, D.2    Novick, P.3
  • 179
    • 0034675978 scopus 로고    scopus 로고
    • Geranylgeranylated SNAREs are dominant inhibitors of membrane fusion
    • Grote, E., Baba, M., Ohsumi, Y., Novick, P.J., 2000. Geranylgeranylated SNAREs are dominant inhibitors of membrane fusion. J. Cell Biol. 151, 453-465.
    • (2000) J. Cell Biol. , vol.151 , pp. 453-465
    • Grote, E.1    Baba, M.2    Ohsumi, Y.3    Novick, P.J.4
  • 180
    • 84934440674 scopus 로고    scopus 로고
    • An evolutionary perspective on eukaryotic membrane trafficking
    • Gurkan, C., Koulov, A.V., Balch, W.E., 2007. An evolutionary perspective on eukaryotic membrane trafficking. Adv. Exp. Med. Biol. 607, 73-83.
    • (2007) Adv. Exp. Med. Biol. , vol.607 , pp. 73-83
    • Gurkan, C.1    Koulov, A.V.2    Balch, W.E.3
  • 181
    • 0026643637 scopus 로고
    • Genetic characterization of Tetrahymena thermophila mutants unable to secrete capsules
    • Gutiérrez, J.C., Orias, E., 1992. Genetic characterization of Tetrahymena thermophila mutants unable to secrete capsules. Dev. Genet. 13, 160-166.
    • (1992) Dev. Genet. , vol.13 , pp. 160-166
    • Gutiérrez, J.C.1    Orias, E.2
  • 182
    • 0007587167 scopus 로고
    • Secretory lectins contained in trichocyst tips of Paramecium
    • Haacke-Bell, B., Plattner, H., 1987. Secretory lectins contained in trichocyst tips of Paramecium. Eur. J. Cell Biol. 44, 1-9.
    • (1987) Eur. J. Cell Biol. , vol.44 , pp. 1-9
    • Haacke-Bell, B.1    Plattner, H.2
  • 183
    • 33947194392 scopus 로고    scopus 로고
    • The phagosome: compartment with a license to kill
    • Haas, A., 2007. The phagosome: compartment with a license to kill. Traffic 8, 311-330.
    • (2007) Traffic , vol.8 , pp. 311-330
    • Haas, A.1
  • 186
    • 33748696966 scopus 로고    scopus 로고
    • Use of HAPPY mapping for the higher order assembly of the Tetrahymena genome
    • Hamilton, E.P., Dear, P.H., Rowland, T., Saks, K., Eisen, J.A., Orias, E., 2006. Use of HAPPY mapping for the higher order assembly of the Tetrahymena genome. Genomics 88, 443-451.
    • (2006) Genomics , vol.88 , pp. 443-451
    • Hamilton, E.P.1    Dear, P.H.2    Rowland, T.3    Saks, K.4    Eisen, J.A.5    Orias, E.6
  • 189
    • 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
  • 190
    • 0036965646 scopus 로고    scopus 로고
    • Phagocytosis and the microtubule cytoskeleton
    • Harrison, R.E., Grinstein, S., 2002. Phagocytosis and the microtubule cytoskeleton. Biochem. Cell Biol. 80, 509-515.
    • (2002) Biochem. Cell Biol. , vol.80 , pp. 509-515
    • Harrison, R.E.1    Grinstein, S.2
  • 191
    • 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
  • 192
    • 0034056289 scopus 로고    scopus 로고
    • Expression of the green fluorescent protein in Paramecium tetraurelia
    • Hauser, K., Haynes, W.J., Kung, C., Plattner, H., Kissmehl, R., 2000a. Expression of the green fluorescent protein in Paramecium tetraurelia. Eur. J. Cell Biol. 79, 144-149.
    • (2000) Eur. J. Cell Biol. , vol.79 , pp. 144-149
    • Hauser, K.1    Haynes, W.J.2    Kung, C.3    Plattner, H.4    Kissmehl, R.5
  • 193
    • 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
  • 194
    • 33847388051 scopus 로고    scopus 로고
    • Calcium: a fundamental regulator of intracellular membrane fusion?
    • Hay, J.C., 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
  • 195
    • 0030307633 scopus 로고    scopus 로고
    • Toward cloning by complementation in Paramecium
    • Haynes, W.J., Ling, K.-Y., Saimi, Y., Kung, C., 1996. Toward cloning by complementation in Paramecium. J. Neurogenet. 11, 81-98.
    • (1996) J. Neurogenet. , vol.11 , pp. 81-98
    • Haynes, W.J.1    Ling, K.-Y.2    Saimi, Y.3    Kung, C.4
  • 196
    • 0343627752 scopus 로고    scopus 로고
    • The cloning and molecular analysis of pawn-B in Paramecium tetraurelia
    • Haynes, W.J., Ling, K.-Y., Preston, R.R., Saimi, Y., Kung, C., 2000. The cloning and molecular analysis of pawn-B in Paramecium tetraurelia. Genetics 155, 1105-1117.
    • (2000) Genetics , vol.155 , pp. 1105-1117
    • Haynes, W.J.1    Ling, K.-Y.2    Preston, R.R.3    Saimi, Y.4    Kung, C.5
  • 198
    • 0028000081 scopus 로고
    • 2+
    • Heinemann, C., Chow, R.H., Neher, E., Zucker, R.S., 1994. Kinetics of the secretory response in bovine chromaffin cells following flash photolysis of caged Ca2+. Biophys.J. 67, 2546-2557.
    • (1994) Biophys. J. , vol.67 , pp. 2546-2557
    • Heinemann, C.1    Chow, R.H.2    Neher, E.3    Zucker, R.S.4
  • 199
    • 0030176313 scopus 로고    scopus 로고
    • Fasts steps in exocytosis and endocytosis studied by capacitance measurements
    • Henkel, A.W., Almers, W., 1996. Fasts steps in exocytosis and endocytosis studied by capacitance measurements. Curr. Opin. Neurobiol. 6, 350-357.
    • (1996) Curr. Opin. Neurobiol. , vol.6 , pp. 350-357
    • Henkel, A.W.1    Almers, W.2
  • 200
    • 0030010317 scopus 로고    scopus 로고
    • FM1-43 dye ultrastructural localization in and release from frog motor nerve terminals
    • Henkel, A.W., Lübke, J., Betz, W.J., 1996. FM1-43 dye ultrastructural localization in and release from frog motor nerve terminals. Proc. Natl. Acad. Sci. USA 93, 1918-1923.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1918-1923
    • Henkel, A.W.1    Lübke, J.2    Betz, W.J.3
  • 201
    • 33645019692 scopus 로고    scopus 로고
    • Biochemical and molecular characterisation of Tetrahymena thermophila extracellular cysteine proteases
    • doi:10.1186/1471-2180-6-19
    • Herrmann, L., Erkelenz, M., Aldag, I., Tiedtke, A., Hartmann, M.W.W., 2006. Biochemical and molecular characterisation of Tetrahymena thermophila extracellular cysteine proteases. BMC Microbiol. 6, 19. doi:10.1186/1471-2180-6-19.
    • (2006) BMC Microbiol , vol.6 , pp. 19
    • Herrmann, L.1    Erkelenz, M.2    Aldag, I.3    Tiedtke, A.4    Hartmann, M.W.W.5
  • 202
    • 0018746093 scopus 로고
    • Synaptic vesicle exocytosis captured by quick freezing and correlated with quantal transmitter release
    • Heuser, J.E., Reese, T.S., Dennis, M.J., Jan, Y., Jan, L., Evans, L., 1979. Synaptic vesicle exocytosis captured by quick freezing and correlated with quantal transmitter release. J. Cell Biol. 81, 275-300.
    • (1979) J. Cell Biol. , vol.81 , pp. 275-300
    • Heuser, J.E.1    Reese, T.S.2    Dennis, M.J.3    Jan, Y.4    Jan, L.5    Evans, L.6
  • 203
    • 62149142874 scopus 로고    scopus 로고
    • V-ATPase functions in normal and disease processes
    • Hinton, A., Bond, S., Forgac, M., 2009. V-ATPase functions in normal and disease processes. Eur. J. Physiol. 457, 589-598.
    • (2009) Eur. J. Physiol. , vol.457 , pp. 589-598
    • Hinton, A.1    Bond, S.2    Forgac, M.3
  • 204
    • 14844331501 scopus 로고    scopus 로고
    • Molecular motors and mechanisms of directional transport in neurons
    • Hirokawa, N., Takemura, R., 2005. Molecular motors and mechanisms of directional transport in neurons. Nat. Rev. Neurosci. 6, 201-214.
    • (2005) Nat. Rev. Neurosci. , vol.6 , pp. 201-214
    • Hirokawa, N.1    Takemura, R.2
  • 205
    • 0032517767 scopus 로고    scopus 로고
    • Kinetic analysis of secretory protein traffic and characterization of Golgi to plasma membrane transport intermediates in living cells
    • Hirschberg, K., Miller, C.M., Ellenberg, J., Presley, J.F., Siggia, E.D., Phair, R.D., et al., 1998. Kinetic analysis of secretory protein traffic and characterization of Golgi to plasma membrane transport intermediates in living cells. J. Cell Biol. 143, 1485-1503.
    • (1998) J. Cell Biol. , vol.143 , pp. 1485-1503
    • Hirschberg, K.1    Miller, C.M.2    Ellenberg, J.3    Presley, J.F.4    Siggia, E.D.5    Phair, R.D.6
  • 206
    • 18044376595 scopus 로고    scopus 로고
    • Directed motility of phagosomes in Tetrahymena thermophila requires actin and myo1p, a novel unconventional myosin
    • Hosein, R.E., Williams, S.A., Gavin, R.H., 2005. Directed motility of phagosomes in Tetrahymena thermophila requires actin and myo1p, a novel unconventional myosin. Cell Motil. Cytoskeleton 61, 49-60.
    • (2005) Cell Motil. Cytoskeleton , vol.61 , pp. 49-60
    • Hosein, R.E.1    Williams, S.A.2    Gavin, R.H.3
  • 207
    • 33845203703 scopus 로고    scopus 로고
    • Induction of gene silencing by hairpin RNA expression in Tetrahymena thermophila reveals a second small RNA pathway
    • Howard-Till, R.A., Yao, M.-C., 2006. Induction of gene silencing by hairpin RNA expression in Tetrahymena thermophila reveals a second small RNA pathway. Mol. Cell. Biol. 26, 8731-8742.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 8731-8742
    • Howard-Till, R.A.1    Yao, M.-C.2
  • 208
    • 33645152194 scopus 로고    scopus 로고
    • V-ATPase interacts with ARNO and Arf6 in early endosomes and regulates the protein degradative pathway
    • Hurtado-Lorenzo, A., Skinner, L., El Annan, J., Futai, M., Sun-Wada, G.-H., Bourgoin, S., et al., 2006. V-ATPase interacts with ARNO and Arf6 in early endosomes and regulates the protein degradative pathway. Nat. Cell Biol. 8, 124-136.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 124-136
    • Hurtado-Lorenzo, A.1    Skinner, L.2    El Annan, J.3    Futai, M.4    Sun-Wada, G.-H.5    Bourgoin, S.6
  • 209
    • 0030928572 scopus 로고    scopus 로고
    • Tetrahymena: the key to the genetic analysis of the regulated pathway of polypeptide secretion?
    • Hutton, J.C., 1997. Tetrahymena: the key to the genetic analysis of the regulated pathway of polypeptide secretion? Proc. Natl. Acad. Sci. USA 94, 10490-10492.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10490-10492
    • Hutton, J.C.1
  • 210
    • 37149030670 scopus 로고    scopus 로고
    • Fusion, fission, and secretion during phagocytosis
    • Huynh, K.K., Kay, J.G., Stow, J.L., Grinstein, S., 2007. Fusion, fission, and secretion during phagocytosis. Physiology 22, 366-372.
    • (2007) Physiology , vol.22 , pp. 366-372
    • Huynh, K.K.1    Kay, J.G.2    Stow, J.L.3    Grinstein, S.4
  • 211
    • 0033969088 scopus 로고    scopus 로고
    • Synaptotagmin IV is present at the Golgi and distal parts of neurites
    • Ibata, K., Fukuda, M., Hamada, T., Kabayama, H., Mikoshiba, K., 2000. Synaptotagmin IV is present at the Golgi and distal parts of neurites. J. Neurochem. 74, 518-526.
    • (2000) J. Neurochem. , vol.74 , pp. 518-526
    • Ibata, K.1    Fukuda, M.2    Hamada, T.3    Kabayama, H.4    Mikoshiba, K.5
  • 212
    • 0024595678 scopus 로고
    • Development of surface pattern during division in Paramecium I. Mapping of duplication and reorganization of cortical cytoskeletal structures in the wild-type
    • Iftode, F., Cohen, J., Ruiz, F., Torres-Rueda, A., Chen-Shan, L., Adoutte, A., et al., 1989. Development of surface pattern during division in Paramecium. I. Mapping of duplication and reorganization of cortical cytoskeletal structures in the wild-type. Development 105, 191-211.
    • (1989) Development , vol.105 , pp. 191-211
    • Iftode, F.1    Cohen, J.2    Ruiz, F.3    Torres-Rueda, A.4    Chen-Shan, L.5    Adoutte, A.6
  • 213
    • 66349093877 scopus 로고    scopus 로고
    • Role of syntaxin 18 in the organization of endoplasmic reticulum subdomains
    • Iinuma, T., Aoki, T., Arasaki, K., Hirose, H., Yamamoto, A., Samata, R., et al., 2009. Role of syntaxin 18 in the organization of endoplasmic reticulum subdomains. J. Cell Sci. 122, 1680-1690.
    • (2009) J. Cell Sci. , vol.122 , pp. 1680-1690
    • Iinuma, T.1    Aoki, T.2    Arasaki, K.3    Hirose, H.4    Yamamoto, A.5    Samata, R.6
  • 214
    • 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, R.D., Fok, A.K., 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
  • 215
    • 0035192612 scopus 로고    scopus 로고
    • Autophagosome requires specific early Sec proteins for its formation and NSF/SNARE for vacuolar fusion
    • Ishihara, N., Hamasaki, M., Yokota, S., Suzuki, K., Kamada, Y., Kihara, A., et al., 2001. Autophagosome requires specific early Sec proteins for its formation and NSF/SNARE for vacuolar fusion. Mol. Biol. Cell 12, 3690-3702.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3690-3702
    • Ishihara, N.1    Hamasaki, M.2    Yokota, S.3    Suzuki, K.4    Kamada, Y.5    Kihara, A.6
  • 218
    • 0025365264 scopus 로고
    • Cytosolic free calcium elevation mediates the phagosome-lysosome fusion during phagocytosis in human neutrophils
    • Jaconi, M.E.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.E.1    Lew, D.P.2    Carpentier, J.-L.3    Magnusson, K.E.4    Sjögren, M.5    Stendahl, O.6
  • 220
    • 0037459076 scopus 로고    scopus 로고
    • Membrane fusion
    • Jahn, R., Lang, T., Südhof, T.C., 2003. Membrane fusion. Cell 112, 519-533.
    • (2003) Cell , vol.112 , pp. 519-533
    • Jahn, R.1    Lang, T.2    Südhof, T.C.3
  • 221
    • 67549134810 scopus 로고    scopus 로고
    • Exocytosis of post-Golgi vesicles is regulated by components of the endocytic machinery
    • Jaiswal, J.K., Rivera, V.M., Simon, S.M., 2009. Exocytosis of post-Golgi vesicles is regulated by components of the endocytic machinery. Cell 137, 1308-1319.
    • (2009) Cell , vol.137 , pp. 1308-1319
    • Jaiswal, J.K.1    Rivera, V.M.2    Simon, S.M.3
  • 222
    • 27744520682 scopus 로고    scopus 로고
    • Rab proteins, connecting transport and vesicle fusion
    • Jordens, I., Marsman, M., Kuijl, C., Neefjes, J., 2005. Rab proteins, connecting transport and vesicle fusion. Traffic 6, 1070-1077.
    • (2005) Traffic , vol.6 , pp. 1070-1077
    • Jordens, I.1    Marsman, M.2    Kuijl, C.3    Neefjes, J.4
  • 223
    • 0028828226 scopus 로고
    • Defective recycling of synaptic vesicles in synaptotagmin mutants of Caenorhabditis elegans
    • Jorgensen, E.M., Hartwieg, E., Schuske, K., Nonet, M.L., Jin, Y., Horvitz, H.R., 1995. Defective recycling of synaptic vesicles in synaptotagmin mutants of Caenorhabditis elegans. Nature 378, 196-199.
    • (1995) Nature , vol.378 , pp. 196-199
    • Jorgensen, E.M.1    Hartwieg, E.2    Schuske, K.3    Nonet, M.L.4    Jin, Y.5    Horvitz, H.R.6
  • 225
    • 33745767358 scopus 로고    scopus 로고
    • Harnessing actin dynamics for clathrinmediated endocytosis
    • Kaksonen, M., Toret, C.P., Drubin, D.G., 2006. Harnessing actin dynamics for clathrinmediated endocytosis. Nat. Rev. Mol. Cell Biol. 7, 404-414.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 404-414
    • Kaksonen, M.1    Toret, C.P.2    Drubin, D.G.3
  • 226
    • 0036499901 scopus 로고    scopus 로고
    • Interaction of syncollin with GP-2, the major membrane protein of pancreatic zymogen granules, and association with lipid microdomains
    • Kalus, I., Hodel, A., Koch, A., Kleene, R., Edwardson, J.M., Schrader, M., 2002. Interaction of syncollin with GP-2, the major membrane protein of pancreatic zymogen granules, and association with lipid microdomains. Biochem.J. 362, 433-442.
    • (2002) Biochem. J. , vol.362 , pp. 433-442
    • Kalus, I.1    Hodel, A.2    Koch, A.3    Kleene, R.4    Edwardson, J.M.5    Schrader, M.6
  • 227
    • 0033068160 scopus 로고    scopus 로고
    • 2+ -dependent exocytosis: implications of kinetic diversity for secretory function
    • 2+ -dependent exocytosis: implications of kinetic diversity for secretory function. Trends Neurosci. 22, 88-93.
    • (1999) Trends Neurosci , vol.22 , pp. 88-93
    • Kasai, H.1
  • 228
  • 229
    • 0035861664 scopus 로고    scopus 로고
    • The aminoterminal domain of the vacuolar proton-translocating ATPase a subunit controls targeting and in vivo dissociation, and the carboxyl-terminal domain affects coupling of proton transport and ATP hydrolysis
    • Kawasaki-Nishi, S., Bowers, K., Nishi, T., Forgac, M., Stevens, T.H., 2001. The aminoterminal domain of the vacuolar proton-translocating ATPase a subunit controls targeting and in vivo dissociation, and the carboxyl-terminal domain affects coupling of proton transport and ATP hydrolysis. J. Biol. Chem. 276, 47411-47420.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47411-47420
    • Kawasaki-Nishi, S.1    Bowers, K.2    Nishi, T.3    Forgac, M.4    Stevens, T.H.5
  • 230
    • 0033957134 scopus 로고    scopus 로고
    • An indexed genomic library for Paramecium complementation cloning
    • Keller, A.-M., Cohen, J., 2000. An indexed genomic library for Paramecium complementation cloning. J. Eukaryot. Microbiol. 47, 1-6.
    • (2000) J. Eukaryot. Microbiol. , vol.47 , pp. 1-6
    • Keller, A.-M.1    Cohen, J.2
  • 231
    • 0027184405 scopus 로고
    • Calmodulin is essential for assembling links necessary for exocytotic membrane fusion in Paramecium
    • Kerboeuf, D., LeBerre, A., Dedieu, J.C., Cohen, J., 1993. Calmodulin is essential for assembling links necessary for exocytotic membrane fusion in Paramecium.EMBOJ.12, 3385-3390.
    • (1993) EMBOJ. , vol.12 , pp. 3385-3390
    • Kerboeuf, D.1    LeBerre, A.2    Dedieu, J.C.3    Cohen, J.4
  • 232
    • 0022621312 scopus 로고
    • Filamentous actin in Paramecium cells: functional and structural changes correlated with phalloidin affinity labeling in vivo
    • Kersken, H., Momayezi, M., Braun, C., Plattner, H., 1986. Filamentous actin in Paramecium cells: functional and structural changes correlated with phalloidin affinity labeling in vivo. J. Histochem. Cytochem. 34, 455-465.
    • (1986) J. Histochem. Cytochem. , vol.34 , pp. 455-465
    • Kersken, H.1    Momayezi, M.2    Braun, C.3    Plattner, H.4
  • 234
    • 34547772739 scopus 로고    scopus 로고
    • Microtubules regulate PI-3K activity and recruitment to the phagocytic cup during Fcg receptor-mediated phagocytosis in nonelicited macrophages
    • Khandani, A., Eng, E., Jongstra-Bilen, J., Schreiber, A.D., Douda, D., SamavarchiTehrani, P., et al., 2007. Microtubules regulate PI-3K activity and recruitment to the phagocytic cup during Fcg receptor-mediated phagocytosis in nonelicited macrophages. J. Leukoc. Biol. 82, 417-428.
    • (2007) J. Leukoc. Biol. , vol.82 , pp. 417-428
    • Khandani, A.1    Eng, E.2    Jongstra-Bilen, J.3    Schreiber, A.D.4    Douda, D.5    SamavarchiTehrani, P.6
  • 235
    • 1942440993 scopus 로고    scopus 로고
    • Highly divergent actins from karyorelictean, heterotrich, and litostome ciliates
    • Kim, O.T.P., Yura, K., Gob, N., Harumoto, T., 2004. Highly divergent actins from karyorelictean, heterotrich, and litostome ciliates. J. Eukaryot. Microbiol. 51, 227-233.
    • (2004) J. Eukaryot. Microbiol. , vol.51 , pp. 227-233
    • Kim, O.T.P.1    Yura, K.2    Gob, N.3    Harumoto, T.4
  • 236
    • 24944523300 scopus 로고    scopus 로고
    • Clathrin-independent endocytosis: new insights into caveolae and non-caveolar lipid raft carriers
    • Kirkham, M., Parton, R.G., 2005. Clathrin-independent endocytosis: new insights into caveolae and non-caveolar lipid raft carriers. Biochim. Biophys. Acta Mol. Cell Res. 1745, 273-286.
    • (2005) Biochim. Biophys. Acta Mol. Cell Res. , vol.1745 , pp. 273-286
    • Kirkham, M.1    Parton, R.G.2
  • 237
    • 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
  • 239
    • 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., Nühse, K., Lutter, 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    Nühse, K.5    Lutter, K.6
  • 240
    • 9144269720 scopus 로고    scopus 로고
    • Fusion between phagosomes, early and late endosomes: a role for actin in fusion between late, but not early endocytic organelles
    • Kjeken, R., Egeberg, M., Habermann, A., Kuehnel, M., Peyron, P., Floetenmeyer, M., et al., 2004. Fusion between phagosomes, early and late endosomes: a role for actin in fusion between late, but not early endocytic organelles. Mol. Biol. Cell 15, 345-358.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 345-358
    • Kjeken, R.1    Egeberg, M.2    Habermann, A.3    Kuehnel, M.4    Peyron, P.5    Floetenmeyer, M.6
  • 241
    • 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
  • 242
    • 0033848055 scopus 로고    scopus 로고
    • "Frustrated exocytosis"-a novel phenomenon: membrane fusion without contents release, followed by detachment and reattachment of dense core vesicles in Paramecium cells
    • Klauke, N., Plattner, H., 2000. "Frustrated exocytosis"-a novel phenomenon: membrane fusion without contents release, followed by detachment and reattachment of dense core vesicles in Paramecium cells. J. Membr. Biol. 176, 237-248.
    • (2000) J. Membr. Biol. , vol.176 , pp. 237-248
    • Klauke, N.1    Plattner, H.2
  • 243
    • 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
  • 245
    • 0034537290 scopus 로고    scopus 로고
    • Autophagy as a regulated pathway of cellular degradation
    • Klionsky, D.J., Emr, S.D., 2000. Autophagy as a regulated pathway of cellular degradation. Science 290, 1717-1721.
    • (2000) Science , vol.290 , pp. 1717-1721
    • Klionsky, D.J.1    Emr, S.D.2
  • 246
    • 34548515059 scopus 로고    scopus 로고
    • An elaborate classification of SNARE proteins sheds light on the conservation of the eukaryotic endomembrane system
    • Kloepper, T.H., Kienle, C.N., Fasshauer, D., 2007. An elaborate classification of SNARE proteins sheds light on the conservation of the eukaryotic endomembrane system. Mol. Biol. Cell 18, 3463-3471.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3463-3471
    • Kloepper, T.H.1    Kienle, C.N.2    Fasshauer, D.3
  • 247
    • 49749133839 scopus 로고    scopus 로고
    • SNAREing the basis of multicellularity: consequences of protein family expansion during evolution
    • Kloepper, T.H., Kienle, C.N., Fasshauer, D., 2008. SNAREing the basis of multicellularity: consequences of protein family expansion during evolution. Mol. Biol. Evol. 25, 2055-2068.
    • (2008) Mol. Biol. Evol. , vol.25 , pp. 2055-2068
    • Kloepper, T.H.1    Kienle, C.N.2    Fasshauer, D.3
  • 248
    • 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
  • 250
    • 0011228521 scopus 로고
    • Ultrastructural analysis of biological membrane fusion and a tentative correlation with biochemical and biophysical aspects
    • Plattner, H. (Ed.) CRC Press, Boca Raton (FL, USA)
    • Knoll, G., Plattner, H., 1989. Ultrastructural analysis of biological membrane fusion and a tentative correlation with biochemical and biophysical aspects. In: Plattner, H. (Ed.), Electron Microscopy of Subcellular Dynamics. CRC Press, Boca Raton (FL, USA), pp. 95-117.
    • (1989) Electron Microscopy of Subcellular Dynamics , pp. 95-117
    • Knoll, G.1    Plattner, H.2
  • 251
    • 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
  • 252
    • 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
  • 253
    • 11144245626 scopus 로고    scopus 로고
    • The role of autophagy during the early neonatal starvation period
    • Kuma, A., Hatano, M., Matsui, M., Yamamoto, A., Nakaya, H., Yoshimori, T., et al., 2004. The role of autophagy during the early neonatal starvation period. Nature 432, 1032-1036.
    • (2004) Nature , vol.432 , pp. 1032-1036
    • Kuma, A.1    Hatano, M.2    Matsui, M.3    Yamamoto, A.4    Nakaya, H.5    Yoshimori, T.6
  • 254
    • 38349098186 scopus 로고    scopus 로고
    • Photolysis of a caged peptide reveals rapid action of N-ethylmaleimide sensitive factor before neurotransmitter release
    • Kuner, T., Li, Y., Gee, K.R., Bonewald, L.F., Augustine, G.J., 2008. Photolysis of a caged peptide reveals rapid action of N-ethylmaleimide sensitive factor before neurotransmitter release. Proc. Natl. Acad. Sci. USA 105, 347-352.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 347-352
    • Kuner, T.1    Li, Y.2    Gee, K.R.3    Bonewald, L.F.4    Augustine, G.J.5
  • 255
    • 0020010461 scopus 로고
    • The physiological basis of taxes in Paramecium
    • Kung, C., Saimi, Y., 1982. The physiological basis of taxes in Paramecium. Annu. Rev. Physiol. 44, 519-534.
    • (1982) Annu. Rev. Physiol. , vol.44 , pp. 519-534
    • Kung, C.1    Saimi, Y.2
  • 256
    • 33745392345 scopus 로고    scopus 로고
    • Identification of a novel actin-related protein in Tetrahymena cilia
    • Kuribara, S., Kato, M., Kato-Minoura, T., Numata, O., 2006. Identification of a novel actin-related protein in Tetrahymena cilia. Cell Motil. Cytoskeleton 63, 437-446.
    • (2006) Cell Motil. Cytoskeleton , vol.63 , pp. 437-446
    • Kuribara, S.1    Kato, M.2    Kato-Minoura, T.3    Numata, O.4
  • 257
    • 0027351866 scopus 로고
    • The Golgi apparatus of Tetrahymena thermophila
    • Kurz, S., Tiedtke, A., 1993. The Golgi apparatus of Tetrahymena thermophila. J. Eukaryot. Microbiol. 40, 10-13.
    • (1993) J. Eukaryot. Microbiol. , vol.40 , pp. 10-13
    • Kurz, S.1    Tiedtke, A.2
  • 258
    • 0016734447 scopus 로고
    • Endocrine secretory mechanisms
    • Lacy, P.E., 1975. Endocrine secretory mechanisms. A review. Am. J. Pathol. 79, 170-187.
    • (1975) A review. Am. J. Pathol. , vol.79 , pp. 170-187
    • Lacy, P.E.1
  • 261
    • 34247383535 scopus 로고    scopus 로고
    • Modification of a hydrophobic layer by a point mutation in syntaxin 1A regulates the rate of synaptic vesicle fusion
    • Lagow, R.D., Bao, H., Cohen, E.N., Daniels, R.W., Zuzek, A., Williams, W.H., et al., 2007. Modification of a hydrophobic layer by a point mutation in syntaxin 1A regulates the rate of synaptic vesicle fusion. PLoS Biol. 5, 800-817.
    • (2007) PLoS Biol , vol.5 , pp. 800-817
    • Lagow, R.D.1    Bao, H.2    Cohen, E.N.3    Daniels, R.W.4    Zuzek, A.5    Williams, W.H.6
  • 262
    • 0035341309 scopus 로고    scopus 로고
    • SNAREs are concentrated in cholesterol-dependent clusters that define docking and fusion sites for exocytosis
    • Lang, T., Bruns, D., Wenzel, D., Riedel, D., Holroyd, P., Thiele, C., et al., 2001. SNAREs are concentrated in cholesterol-dependent clusters that define docking and fusion sites for exocytosis. EMBO J. 20, 2202-2213.
    • (2001) EMBO J , vol.20 , pp. 2202-2213
    • Lang, T.1    Bruns, D.2    Wenzel, D.3    Riedel, D.4    Holroyd, P.5    Thiele, C.6
  • 263
    • 27144543784 scopus 로고    scopus 로고
    • Scaffolding microdomains and beyond: the function of reggie/flotillin proteins
    • Langhorst, M.F., Reuter, A., Stuermer, C.A.O., 2005. Scaffolding microdomains and beyond: the function of reggie/flotillin proteins. Cell. Mol. Life Sci. 62, 2228-2240.
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 2228-2240
    • Langhorst, M.F.1    Reuter, A.2    Stuermer, C.A.O.3
  • 265
    • 34548508978 scopus 로고    scopus 로고
    • Dynamic regulation of the large exocytotic fusion pore in pancreatic acinar cells
    • Larina, O., Dhat, P., Pickett, J.A., Laukinonis, B.S., Shah, A., Kruger, W.A., et al., 2007. Dynamic regulation of the large exocytotic fusion pore in pancreatic acinar cells. Mol. Biol. Cell 18, 3502-3511.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3502-3511
    • Larina, O.1    Dhat, P.2    Pickett, J.A.3    Laukinonis, B.S.4    Shah, A.5    Kruger, W.A.6
  • 266
    • 62149115148 scopus 로고    scopus 로고
    • 2+ compartments, microdomains and the many facets of Ca signalling
    • 2+ compartments, microdomains and the many facets of Ca signalling. FEBS J. 276, 1800-1816.
    • (2009) FEBS J , vol.276 , pp. 1800-1816
    • Laude, A.J.1    Simpson, A.W.M.2
  • 267
    • 0032963084 scopus 로고    scopus 로고
    • Gene knockouts reveal separate functions for two cytoplasmic dyneins in Tetrahymena thermophila
    • Lee, S., Wisniewski, J.C., Dentler, W.L., Asai, D.J., 1999. Gene knockouts reveal separate functions for two cytoplasmic dyneins in Tetrahymena thermophila. Mol. Biol. Cell 10, 771-784.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 771-784
    • Lee, S.1    Wisniewski, J.C.2    Dentler, W.L.3    Asai, D.J.4
  • 268
    • 0019454972 scopus 로고
    • Control of exocytotic processes: cytological and physiological studies of trichocyst mutants in Paramecium tetraurelia
    • Lefort-Tran, M., Aufderheide, K., Pouphile, M., Rossignol, M., Beisson, J., 1981. Control of exocytotic processes: cytological and physiological studies of trichocyst mutants in Paramecium tetraurelia. J. Cell Biol. 88, 301-311.
    • (1981) J. Cell Biol. , vol.88 , pp. 301-311
    • Lefort-Tran, M.1    Aufderheide, K.2    Pouphile, M.3    Rossignol, M.4    Beisson, J.5
  • 269
    • 24944474829 scopus 로고    scopus 로고
    • D-3 phosphoinositides of the ciliate Tetrahymena: characterization and study of their regulatory role in lysosomal enzyme secretion
    • Leonaritis, G., Tiedtke, A., Galanopoulou, D., 2005. D-3 phosphoinositides of the ciliate Tetrahymena: characterization and study of their regulatory role in lysosomal enzyme secretion. Biochim. Biophys. Acta Mol. Cell Res. 1745, 330-341.
    • (2005) Biochim. Biophys. Acta Mol. Cell Res. , vol.1745 , pp. 330-341
    • Leonaritis, G.1    Tiedtke, A.2    Galanopoulou, D.3
  • 270
    • 35348946444 scopus 로고    scopus 로고
    • + channels: tuning β-cell excitability with syntaxin-1A and other exocytotic proteins
    • + channels: tuning β-cell excitability with syntaxin-1A and other exocytotic proteins. Endocr. Rev. 28, 653-663.
    • (2007) Endocr. Rev. , vol.28 , pp. 653-663
    • Leung, Y.M.1    Kwan, E.P.2    Ng, B.3    Kang, Y.4    Gaisano, H.Y.5
  • 272
    • 33744478902 scopus 로고    scopus 로고
    • Multiple tubulin forms in ciliate protozoan Tetrahymena and Paramecium species
    • Libusóva, L., Dráber, P., 2006. Multiple tubulin forms in ciliate protozoan Tetrahymena and Paramecium species. Protoplasma 227, 65-76.
    • (2006) Protoplasma , vol.227 , pp. 65-76
    • Libusóva, L.1    Dráber, P.2
  • 273
    • 70350005334 scopus 로고    scopus 로고
    • Transient assembly of F-actin by phagosomes delays phagosome fusion with lysosomes in cargo-overloaded macrophages
    • Liebl, D., Griffiths, G., 2009. Transient assembly of F-actin by phagosomes delays phagosome fusion with lysosomes in cargo-overloaded macrophages. J. Cell Sci. 122, 2935-2945.
    • (2009) J. Cell Sci. , vol.122 , pp. 2935-2945
    • Liebl, D.1    Griffiths, G.2
  • 274
    • 0030807735 scopus 로고    scopus 로고
    • Structural organization of the synaptic exocytosis core complex
    • Lin, R.C., Scheller, R.H., 1997. Structural organization of the synaptic exocytosis core complex. Neuron 19, 1087-1094.
    • (1997) Neuron , vol.19 , pp. 1087-1094
    • Lin, R.C.1    Scheller, R.H.2
  • 275
    • 24944547589 scopus 로고    scopus 로고
    • Microtubule actin crosslinking factor 1b: a novel plakin that localizes to the Golgi complex
    • Lin, C.-M., Chen, H.-J., Leung, C.L., Parry, D.A.D., Liem, R.K.H., 2005. Microtubule actin crosslinking factor 1b: a novel plakin that localizes to the Golgi complex. J. Cell Sci. 118, 3727-3738.
    • (2005) J. Cell Sci. , vol.118 , pp. 3727-3738
    • Lin, C.-M.1    Chen, H.-J.2    Leung, C.L.3    Parry, D.A.D.4    Liem, R.K.H.5
  • 277
    • 35649028253 scopus 로고    scopus 로고
    • SNARE-ware: the role of SNARE-domain proteins in plant cells
    • Lipka, V., Kwon, C., Panstruga, R., 2007. SNARE-ware: the role of SNARE-domain proteins in plant cells. Annu. Rev. Cell Dev. Biol. 23, 147-174.
    • (2007) Annu. Rev. Cell Dev. Biol. , vol.23 , pp. 147-174
    • Lipka, V.1    Kwon, C.2    Panstruga, R.3
  • 279
    • 3042542941 scopus 로고    scopus 로고
    • Sec22p export from the endoplasmic reticulum is independent of SNARE pairing
    • Liu, Y., Flanagan, J.J., Barlowe, C., 2004. Sec22p export from the endoplasmic reticulum is independent of SNARE pairing. J. Biol. Chem. 279, 27225-27232.
    • (2004) J. Biol. Chem. , vol.279 , pp. 27225-27232
    • Liu, Y.1    Flanagan, J.J.2    Barlowe, C.3
  • 281
    • 0038329315 scopus 로고    scopus 로고
    • Syntaxin 2 and endobrevin are required for the terminal step of cytokinesis in mammalian cells
    • Low, S.H., Li, X., Miura, M., Kudo, N., Quinones, B., Weimbs, T., 2003. Syntaxin 2 and endobrevin are required for the terminal step of cytokinesis in mammalian cells. Dev. Cell 4, 753-759.
    • (2003) Dev. Cell , vol.4 , pp. 753-759
    • Low, S.H.1    Li, X.2    Miura, M.3    Kudo, N.4    Quinones, B.5    Weimbs, T.6
  • 282
    • 46449090904 scopus 로고    scopus 로고
    • Supramolecular SNARE assembly precedes hemifusion in SNARE-mediated membrane fusion
    • Lu, X., Zhang, Y., Shin, Y.-K., 2008. Supramolecular SNARE assembly precedes hemifusion in SNARE-mediated membrane fusion. Nat. Struct. Mol. Biol. 15, 700-706.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 700-706
    • Lu, X.1    Zhang, Y.2    Shin, Y.-K.3
  • 283
    • 0026586401 scopus 로고
    • Secretory organelles of Paramecium cells (trichocysts) are not remarkably acidic compartments
    • Lumpert, C.J., Glas-Albrecht, R., Eisenmann, E., Plattner, H., 1992. Secretory organelles of Paramecium cells (trichocysts) are not remarkably acidic compartments. J. Histochem. Cytochem. 40, 153-160.
    • (1992) J. Histochem. Cytochem. , vol.40 , pp. 153-160
    • Lumpert, C.J.1    Glas-Albrecht, R.2    Eisenmann, E.3    Plattner, H.4
  • 284
    • 0022965674 scopus 로고
    • Lectin binding sites in Paramecium tetraurelia cells I. Labeling analysis predominantly of secretory components
    • Lüthe, H., Plattner, H., Haacke, B., Walther, P., Müller, M., 1986. Lectin binding sites in Paramecium tetraurelia cells. I. Labeling analysis predominantly of secretory components. Histochemistry 85, 365-376.
    • (1986) Histochemistry , vol.85 , pp. 365-376
    • Lüthe, H.1    Plattner, H.2    Haacke, B.3    Walther, P.4    Müller, M.5
  • 287
    • 0000017069 scopus 로고
    • Electrophysiology
    • Görtz, H.-D. (Ed.), SpringerVerlag, Berlin, Heidelberg, New York
    • Machemer, H., 1988. Electrophysiology. In: Görtz, H.-D. (Ed.), Paramecium. SpringerVerlag, Berlin, Heidelberg, New York, pp. 185-215.
    • (1988) Paramecium , pp. 185-215
    • Machemer, H.1
  • 289
    • 15044352445 scopus 로고    scopus 로고
    • Fatty acylation and prenylation of proteins: what's hot in a fat
    • Magee, T., Seabra, M.C., 2005. Fatty acylation and prenylation of proteins: what's hot in a fat. Curr. Opin. Cell Biol. 17, 190-196.
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 190-196
    • Magee, T.1    Seabra, M.C.2
  • 290
    • 0032899307 scopus 로고    scopus 로고
    • Biochemical analysis of membrane proteins from an early maturation stage of phagosomes
    • Maicher, M.T., Tiedtke, A., 1999. Biochemical analysis of membrane proteins from an early maturation stage of phagosomes. Electrophoresis 20, 1011-1016.
    • (1999) Electrophoresis , vol.20 , pp. 1011-1016
    • Maicher, M.T.1    Tiedtke, A.2
  • 291
    • 6344272891 scopus 로고    scopus 로고
    • Role of Vma21p in assembly and transport of the yeast vacuolar ATPase
    • Malkus, P., Graham, L.A., Stevens, T.H., Schekman, R., 2004. Role of Vma21p in assembly and transport of the yeast vacuolar ATPase. Mol. Biol. Cell 15, 5075-5091.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5075-5091
    • Malkus, P.1    Graham, L.A.2    Stevens, T.H.3    Schekman, R.4
  • 293
    • 34247579058 scopus 로고    scopus 로고
    • The transport signal on Sec22 for packaging into COPII-coated vesicles is a conformational epitope
    • Mancias, J.D., Goldberg, J., 2007. The transport signal on Sec22 for packaging into COPII-coated vesicles is a conformational epitope. Mol. Cell 26, 403-414.
    • (2007) Mol. Cell , vol.26 , pp. 403-414
    • Mancias, J.D.1    Goldberg, J.2
  • 294
    • 0035947648 scopus 로고    scopus 로고
    • Intra-endosomal pH-sensitive recruitment of the Arf-nucleotide exchange factor ARNO and Arf6 from cytoplasm to proximal tubule endosomes
    • Maranda, B., Brown, D., Bourgoin, S., Casanova, J.E., Vinay, P., Ausiello, D.A., et al., 2001. Intra-endosomal pH-sensitive recruitment of the Arf-nucleotide exchange factor ARNO and Arf6 from cytoplasm to proximal tubule endosomes. J. Biol. Chem. 276, 18540-18550.
    • (2001) J. Biol. Chem. , vol.276 , pp. 18540-18550
    • Maranda, B.1    Brown, D.2    Bourgoin, S.3    Casanova, J.E.4    Vinay, P.5    Ausiello, D.A.6
  • 295
    • 47349120492 scopus 로고    scopus 로고
    • +-ATPase in vesicular trafficking: targeting, regulation and function
    • +-ATPase in vesicular trafficking: targeting, regulation and function. Curr. Opin. Cell Biol. 20, 415-426.
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 415-426
    • Marshansky, V.1    Futai, M.2
  • 296
    • 45849152550 scopus 로고    scopus 로고
    • Mechanisms of membrane fusion: disparate players and common principles
    • Martens, S., McMahon, H.T., 2008. Mechanisms of membrane fusion: disparate players and common principles. Nat. Rev. Mol. Cell Biol. 9, 543-556.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 543-556
    • Martens, S.1    McMahon, H.T.2
  • 297
    • 34249933061 scopus 로고    scopus 로고
    • How synaptotagmin promotes membrane fusion
    • Martens, S., Kozlov, M.M., McMahon, H.T., 2007. How synaptotagmin promotes membrane fusion. Science 316, 1205-1208.
    • (2007) Science , vol.316 , pp. 1205-1208
    • Martens, S.1    Kozlov, M.M.2    McMahon, H.T.3
  • 298
    • 0023576902 scopus 로고
    • Translocation and clustering of endosomes and lysosomes depends on microtubules
    • Matteoni, R., Kreis, T.E., 1987. Translocation and clustering of endosomes and lysosomes depends on microtubules. J. Cell Biol. 105, 1253-1265.
    • (1987) J. Cell Biol. , vol.105 , pp. 1253-1265
    • Matteoni, R.1    Kreis, T.E.2
  • 299
    • 0019851385 scopus 로고
    • Identification of a synaptic vesiclespecific membrane protein with a wide distribution in neuronal and neurosecretory tissue
    • Matthew, W.D., Tsavaler, L., Reichardt, L.F., 1981. Identification of a synaptic vesiclespecific membrane protein with a wide distribution in neuronal and neurosecretory tissue. J. Cell Biol. 91, 257-269.
    • (1981) J. Cell Biol. , vol.91 , pp. 257-269
    • Matthew, W.D.1    Tsavaler, L.2    Reichardt, L.F.3
  • 300
    • 0035067475 scopus 로고    scopus 로고
    • Phagocytosis and the actin cytoskeleton
    • May, R., Machesky, L.M., 2001. Phagocytosis and the actin cytoskeleton. J. Cell Sci. 114, 1061-1077.
    • (2001) J. Cell Sci. , vol.114 , pp. 1061-1077
    • May, R.1    Machesky, L.M.2
  • 301
    • 0036437326 scopus 로고    scopus 로고
    • Membrane fusion in eukaryotic cells
    • Mayer, A., 2002. Membrane fusion in eukaryotic cells. Annu. Rev. Cell Dev. Biol. 18, 289-314.
    • (2002) Annu. Rev. Cell Dev. Biol. , vol.18 , pp. 289-314
    • Mayer, A.1
  • 302
    • 34547114456 scopus 로고    scopus 로고
    • Pathways of clathrin-independent endocytosis
    • Mayor, S., Pagano, R.E., 2007. Pathways of clathrin-independent endocytosis. Nat. Rev. Mol. Cell Biol. 8, 603-612.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 603-612
    • Mayor, S.1    Pagano, R.E.2
  • 304
    • 59649128407 scopus 로고    scopus 로고
    • Ciliary targeting motif VxPx directs assembly of a trafficking module through Arf4
    • Mazelova, J., Astuto-Gribble, L., Inoue, H., Tam, B.M., Schonteich, E., Prekeris, R., et al., 2009a. Ciliary targeting motif VxPx directs assembly of a trafficking module through Arf4. EMBO J. 28, 183-192.
    • (2009) EMBO J , vol.28 , pp. 183-192
    • Mazelova, J.1    Astuto-Gribble, L.2    Inoue, H.3    Tam, B.M.4    Schonteich, E.5    Prekeris, R.6
  • 305
    • 68949189407 scopus 로고    scopus 로고
    • Syntaxin 3 and SNAP-25 pairing regulated by omega-3 docosahexaenoic acid, controls the delivery of rhodopsin for the biogenesis of cilia-derived sensory organelles, the rod outer segments
    • Mazelova, J., Ransom, N., Astuto-Gribble, L., Wilson, M.C., Deretic, D., 2009b. Syntaxin 3 and SNAP-25 pairing regulated by omega-3 docosahexaenoic acid, controls the delivery of rhodopsin for the biogenesis of cilia-derived sensory organelles, the rod outer segments. J. Cell Sci. 122, 2003-2013.
    • (2009) J. Cell Sci. , vol.122 , pp. 2003-2013
    • Mazelova, J.1    Ransom, N.2    Astuto-Gribble, L.3    Wilson, M.C.4    Deretic, D.5
  • 306
    • 0034648836 scopus 로고    scopus 로고
    • Compartmental specificity of cellular membrane fusion encoded in SNARE proteins
    • McNew, J.A., Parlati, F., Fukuda, R., Johnston, R.J., Paz, K., Paumet, F., et al., 2000. Compartmental specificity of cellular membrane fusion encoded in SNARE proteins. Nature 407, 153-159.
    • (2000) Nature , vol.407 , pp. 153-159
    • McNew, J.A.1    Parlati, F.2    Fukuda, R.3    Johnston, R.J.4    Paz, K.5    Paumet, F.6
  • 307
    • 38349018454 scopus 로고    scopus 로고
    • Munc 18-1 prevents the formation of ectopic SNARE complexes in living cells
    • Medine, C.N., Rickman, C., Chamberlain, L.H., Duncan, R.R., 2007. Munc 18-1 prevents the formation of ectopic SNARE complexes in living cells. J. Cell Sci. 120, 4407-4415.
    • (2007) J. Cell Sci. , vol.120 , pp. 4407-4415
    • Medine, C.N.1    Rickman, C.2    Chamberlain, L.H.3    Duncan, R.R.4
  • 308
    • 0031985394 scopus 로고    scopus 로고
    • Mutational analysis of regulated exocytosis in Tetrahymena
    • Melia, S.M., Cole, E.S., Turkewitz, A.P., 1998. Mutational analysis of regulated exocytosis in Tetrahymena. J. Cell Sci. 111, 131-140.
    • (1998) J. Cell Sci. , vol.111 , pp. 131-140
    • Melia, S.M.1    Cole, E.S.2    Turkewitz, A.P.3
  • 309
    • 0037008962 scopus 로고    scopus 로고
    • Regulation of membrane fusion by the membrane-proximal coil of the t-SNARE during zippering of SNAREpins
    • Melia, T.J., Weber, T., McNew, J.A., Fisher, L.E., Johnston, R.J., Parlati, F., et al., 2002. Regulation of membrane fusion by the membrane-proximal coil of the t-SNARE during zippering of SNAREpins. J. Cell Biol. 158, 929-940.
    • (2002) J. Cell Biol. , vol.158 , pp. 929-940
    • Melia, T.J.1    Weber, T.2    McNew, J.A.3    Fisher, L.E.4    Johnston, R.J.5    Parlati, F.6
  • 310
    • 0033084780 scopus 로고    scopus 로고
    • Paramecium molecular genetics: functional complementation and homology-dependent gene inactivation
    • Meyer, E., Cohen, J., 1999. Paramecium molecular genetics: functional complementation and homology-dependent gene inactivation. Protist 150, 11-16.
    • (1999) Protist , vol.150 , pp. 11-16
    • Meyer, E.1    Cohen, J.2
  • 311
    • 0031729619 scopus 로고    scopus 로고
    • Maturation of phagosomes is accompanied by specific patterns of small GTPases
    • Meyer, M., Mayer, T., Tiedtke, A., 1998. Maturation of phagosomes is accompanied by specific patterns of small GTPases. Electrophoresis 19, 2528-2535.
    • (1998) Electrophoresis , vol.19 , pp. 2528-2535
    • Meyer, M.1    Mayer, T.2    Tiedtke, A.3
  • 312
    • 38349064976 scopus 로고    scopus 로고
    • Mechanisms and functions of endocytosis
    • Miaczynska, M., Stenmark, H., 2008. Mechanisms and functions of endocytosis. J. Cell Biol. 180, 7-11.
    • (2008) J. Cell Biol. , vol.180 , pp. 7-11
    • Miaczynska, M.1    Stenmark, H.2
  • 313
    • 57349129589 scopus 로고    scopus 로고
    • Primary granule exocytosis in human neutrophils is regulated by Rac-dependent actin remodeling
    • Mitchell, T., Lo, A., Logan, M.R., Lacy, P., Eitzen, G., 2008. Primary granule exocytosis in human neutrophils is regulated by Rac-dependent actin remodeling. Am. J. Physiol. Cell Physiol. 295, C1344-C1365.
    • (2008) Am. J. Physiol. Cell Physiol. , vol.295
    • Mitchell, T.1    Lo, A.2    Logan, M.R.3    Lacy, P.4    Eitzen, G.5
  • 315
    • 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
  • 316
    • 0027436835 scopus 로고
    • Ultrastructural and antigenic preservation of a delicate structure by cryopreparation: Identification and immunogold localization during biogenesis of a secretory component (membrane-matrix connection) in Paramecium trichocysts
    • Momayezi, M., Habermann, A.W., Sokolova, J.J., Kissmehl, R., Plattner, H., 1993. Ultrastructural and antigenic preservation of a delicate structure by cryopreparation: Identification and immunogold localization during biogenesis of a secretory component (membrane-matrix connection) in Paramecium trichocysts. J. Histochem. Cytochem. 41, 1669-1677.
    • (1993) J. Histochem. Cytochem. , vol.41 , pp. 1669-1677
    • Momayezi, M.1    Habermann, A.W.2    Sokolova, J.J.3    Kissmehl, R.4    Plattner, H.5
  • 317
    • 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
  • 318
    • 0029613765 scopus 로고
    • Structure and function of tetanus and botulinum neurotoxins
    • Montecucco, C., Schiavo, G., 1995. Structure and function of tetanus and botulinum neurotoxins. Q. Rev. Biophys. 28, 423-472.
    • (1995) Q. Rev. Biophys. , vol.28 , pp. 423-472
    • Montecucco, C.1    Schiavo, G.2
  • 319
    • 21744457054 scopus 로고    scopus 로고
    • SNARE complexes and neuroexocytosis: how many, how close?
    • Montecucco, C., Schiavo, G., Pantano, S., 2005. SNARE complexes and neuroexocytosis: how many, how close? Trends Biochem. Sci. 30, 367-372.
    • (2005) Trends Biochem. Sci , vol.30 , pp. 367-372
    • Montecucco, C.1    Schiavo, G.2    Pantano, S.3
  • 320
    • 61749095982 scopus 로고    scopus 로고
    • Annexin A2-dependent polymerization of actin mediates endosome biogenesis
    • Morel, E., Parton, R.G., Gruenberg, J., 2009. Annexin A2-dependent polymerization of actin mediates endosome biogenesis. Dev. Cell 16, 445-457.
    • (2009) Dev. Cell , vol.16 , pp. 445-457
    • Morel, E.1    Parton, R.G.2    Gruenberg, J.3
  • 321
    • 0035166819 scopus 로고    scopus 로고
    • Mutant rab8 impairs docking and fusion of rhodopsin-bearing post-Golgi membranes and causes cell death of transgenic Xenopus rods
    • Moritz, O.L., Tam, B.M., Hurd, L.L., Peränen, J., Deretic, D., Papermaster, D.S., 2001. Mutant rab8 impairs docking and fusion of rhodopsin-bearing post-Golgi membranes and causes cell death of transgenic Xenopus rods. Mol. Biol. Cell 12, 2341-2351.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2341-2351
    • Moritz, O.L.1    Tam, B.M.2    Hurd, L.L.3    Peränen, J.4    Deretic, D.5    Papermaster, D.S.6
  • 322
    • 0043029286 scopus 로고    scopus 로고
    • SNARE selectivity of the COPII coat
    • Mossessova, E., Bickford, L.C., Goldberg, J., 2003. SNARE selectivity of the COPII coat. Cell 114, 483-495.
    • (2003) Cell , vol.114 , pp. 483-495
    • Mossessova, E.1    Bickford, L.C.2    Goldberg, J.3
  • 323
    • 22044439908 scopus 로고    scopus 로고
    • The domain architecture of large guanine nucleotide exchange factors for the small GTP-binding protein Arf
    • doi:10.1186/1471-2164-6-20
    • Mouratou, B., Biou, V., Joubert, A., Cohen, J., Shields, D.J., Geldner, N., et al., 2005. The domain architecture of large guanine nucleotide exchange factors for the small GTP-binding protein Arf. MBC Genomics 6, 20. doi:10.1186/1471-2164-6-20.
    • (2005) MBC Genomics , vol.6 , pp. 20
    • Mouratou, B.1    Biou, V.2    Joubert, A.3    Cohen, J.4    Shields, D.J.5    Geldner, N.6
  • 324
    • 0035951401 scopus 로고    scopus 로고
    • Protein sorting upon exit from the endoplasmic reticulum
    • Muniz, M., Morsomme, P., Riezman, H., 2001. Protein sorting upon exit from the endoplasmic reticulum. Cell 104, 313-320.
    • (2001) Cell , vol.104 , pp. 313-320
    • Muniz, M.1    Morsomme, P.2    Riezman, H.3
  • 325
    • 66349122907 scopus 로고    scopus 로고
    • Clustering of syntaxin-1A in model membranes is modulated by phosphatidylinositol 4, 5-bisphosphate and cholesterol
    • Murray, D.H., Tamm, L.K., 2009. Clustering of syntaxin-1A in model membranes is modulated by phosphatidylinositol 4, 5-bisphosphate and cholesterol. Biochemistry 48, 4617-4625.
    • (2009) Biochemistry , vol.48 , pp. 4617-4625
    • Murray, D.H.1    Tamm, L.K.2
  • 326
    • 34250012834 scopus 로고    scopus 로고
    • A core complex of BBS proteins cooperates with the GTPase Rab8 to promote ciliary membrane biogenesis
    • Nachury, M.V., Loktev, A.V., Zhang, Q., Westlake, C.J., Peränen, J., Merdes, A., et al., 2007. A core complex of BBS proteins cooperates with the GTPase Rab8 to promote ciliary membrane biogenesis. Cell 129, 1201-1213.
    • (2007) Cell , vol.129 , pp. 1201-1213
    • Nachury, M.V.1    Loktev, A.V.2    Zhang, Q.3    Westlake, C.J.4    Peränen, J.5    Merdes, A.6
  • 328
    • 0032995292 scopus 로고    scopus 로고
    • A Sec7-related protein in Paramecium
    • Nair, S., Guerra, C., Satir, P., 1999. A Sec7-related protein in Paramecium. FASEB J. 13, 1249-1257.
    • (1999) FASEB J. , vol.13 , pp. 1249-1257
    • Nair, S.1    Guerra, C.2    Satir, P.3
  • 329
    • 0032008553 scopus 로고    scopus 로고
    • 2+ microdomains: new tools for understanding their roles in neurotransmitter release
    • 2+ microdomains: new tools for understanding their roles in neurotransmitter release. Neuron 20, 389-399.
    • (1998) Neuron , vol.20 , pp. 389-399
    • Neher, E.1
  • 330
    • 0013657423 scopus 로고
    • Discrete changes of cell membrane capacitance observed under conditions of enhanced secretion in bovine adrenal chromaffin cells
    • Neher, E., Marty, A., 1982. Discrete changes of cell membrane capacitance observed under conditions of enhanced secretion in bovine adrenal chromaffin cells. Proc. Natl. Acad. Sci. USA 79, 6712-6716.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 6712-6716
    • Neher, E.1    Marty, A.2
  • 331
    • 9344268267 scopus 로고    scopus 로고
    • Kinetic efficiency of endocytosis at mammalian CNS synapses requires synaptotagmin I
    • Nicholson-Tomishima, K., Ryan, T.A., 2004. Kinetic efficiency of endocytosis at mammalian CNS synapses requires synaptotagmin I. Proc. Natl. Acad. Sci. USA 101, 16648-16652.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 16648-16652
    • Nicholson-Tomishima, K.1    Ryan, T.A.2
  • 332
    • 0033607182 scopus 로고    scopus 로고
    • Content mixing and membrane integrity during membrane fusion driven by pairing of isolated v-SNAREs and t-SNAREs
    • Nickel, W., Weber, T., McNew, J.A., Parlati, F., Söllner, T.H., Rothman, J.E., 1999. Content mixing and membrane integrity during membrane fusion driven by pairing of isolated v-SNAREs and t-SNAREs. Proc. Natl. Acad. Sci. USA 96, 12571-12576.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12571-12576
    • Nickel, W.1    Weber, T.2    McNew, J.A.3    Parlati, F.4    Söllner, T.H.5    Rothman, J.E.6
  • 333
    • 0037477712 scopus 로고    scopus 로고
    • ADP ribosylation factor 6 is activated and controls membrane delivery during phagocytosis in macrophages
    • Niedergang, F., Colucci-Guyon, E., Dubois, T., Raposo, G., Chavrier, P., 2003. ADP ribosylation factor 6 is activated and controls membrane delivery during phagocytosis in macrophages. J. Cell Biol. 161, 1143-1150.
    • (2003) J. Cell Biol. , vol.161 , pp. 1143-1150
    • Niedergang, F.1    Colucci-Guyon, E.2    Dubois, T.3    Raposo, G.4    Chavrier, P.5
  • 335
    • 0028268948 scopus 로고
    • Clostridial neurotoxins: new tools for dissecting exocytosis
    • Niemann, H., Blasi, J., Jahn, R., 1994. Clostridial neurotoxins: new tools for dissecting exocytosis. Trends Cell Biol. 4, 179-185.
    • (1994) Trends Cell Biol , vol.4 , pp. 179-185
    • Niemann, H.1    Blasi, J.2    Jahn, R.3
  • 336
    • 0020827145 scopus 로고
    • Coated pits with pinocytosis in Tetrahymena
    • Nilsson, J.R., Van Deurs, B., 1983. Coated pits with pinocytosis in Tetrahymena. J. Cell Sci. 63, 209-222.
    • (1983) J. Cell Sci. , vol.63 , pp. 209-222
    • Nilsson, J.R.1    Van Deurs, B.2
  • 338
    • 0030860083 scopus 로고    scopus 로고
    • The diversity of Rab proteins in vesicle transport
    • Novick, P., Zerial, M., 1997. The diversity of Rab proteins in vesicle transport. Curr. Opin. Cell Biol. 9, 496-504.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 496-504
    • Novick, P.1    Zerial, M.2
  • 339
    • 67649470529 scopus 로고    scopus 로고
    • Reconstitution of Rab-and SNARE-dependent membrane fusion by synthetic endosomes
    • Ohya, T., Miaczynska, M., Coskun, Ü., Lommer, B., Runge, A., Drechsel, D., et al., 2009. Reconstitution of Rab-and SNARE-dependent membrane fusion by synthetic endosomes. Nature 459, 1091-1097.
    • (2009) Nature , vol.459 , pp. 1091-1097
    • Ohya, T.1    Miaczynska, M.2    Coskun, Ü.3    Lommer, B.4    Runge, A.5    Drechsel, D.6
  • 340
    • 0031935639 scopus 로고    scopus 로고
    • Mapping the germ-line and somatic genomes of a ciliated protozoan Tetrahymena thermophila
    • Orias, E., 1998. Mapping the germ-line and somatic genomes of a ciliated protozoan, Tetrahymena thermophila. Genome Res. 8, 91-99.
    • (1998) Genome Res , vol.8 , pp. 91-99
    • Orias, E.1
  • 341
    • 0020855138 scopus 로고
    • Isolation and ultrastructural characterization of secretory mutants of Tetrahymena thermophila
    • Orias, E., Flacks, M., Satir, B.H., 1983. Isolation and ultrastructural characterization of secretory mutants of Tetrahymena thermophila. J. Cell Sci. 64, 49-67.
    • (1983) J. Cell Sci. , vol.64 , pp. 49-67
    • Orias, E.1    Flacks, M.2    Satir, B.H.3
  • 342
    • 0034669052 scopus 로고    scopus 로고
    • Exocytosis requires asymmetry in the central layer of the SNARE complex
    • Ossig, R., Schmitt, H.D., De Groot, B., Riedel, D., Keränen, S., Ronne, H., et al., 2000. Exocytosis requires asymmetry in the central layer of the SNARE complex. EMBO J. 19, 6000-6010.
    • (2000) EMBO J , vol.19 , pp. 6000-6010
    • Ossig, R.1    Schmitt, H.D.2    De Groot, B.3    Riedel, D.4    Keränen, S.5    Ronne, H.6
  • 343
    • 3843103801 scopus 로고    scopus 로고
    • Endocytosis, membrane recycling and sorting of GPI-anchored proteins: Trypanosoma brucei as a model system
    • Overath, P., Engstler, M., 2004. Endocytosis, membrane recycling and sorting of GPI-anchored proteins: Trypanosoma brucei as a model system. Mol. Microbiol. 53, 735-744.
    • (2004) Mol. Microbiol. , vol.53 , pp. 735-744
    • Overath, P.1    Engstler, M.2
  • 344
    • 50549084252 scopus 로고    scopus 로고
    • 2+ -dependent, phopholipid-binding residues of synaptotagmin are critical for excitation-secretion coupling in vivo
    • 2+ -dependent, phopholipid-binding residues of synaptotagmin are critical for excitation-secretion coupling in vivo. J. Neurosci. 28, 7458-7466.
    • (2008) J. Neurosci. , vol.28 , pp. 7458-7466
    • Paddock, B.E.1    Striegel, A.R.2    Hui, E.3    Chapman, E.R.4    Reist, N.E.5
  • 345
    • 0025610466 scopus 로고
    • Secretory organelle docking at the cell membrane in Paramecium cells: dedocking and synchronized redocking of trichocysts
    • Pape, R., Plattner, H., 1990. Secretory organelle docking at the cell membrane in Paramecium cells: dedocking and synchronized redocking of trichocysts. Exp. Cell Res. 191, 263-272.
    • (1990) Exp. Cell Res. , vol.191 , pp. 263-272
    • Pape, R.1    Plattner, H.2
  • 346
    • 85005628586 scopus 로고
    • Effects of anti-microtubule agents on Paramecium cell culture growth
    • Pape, R., Kissmehl, R., Glas-Albrecht, R., Plattner, H., 1991. Effects of anti-microtubule agents on Paramecium cell culture growth. Eur. J. Protistol. 27, 283-289.
    • (1991) Eur. J. Protistol. , vol.27 , pp. 283-289
    • Pape, R.1    Kissmehl, R.2    Glas-Albrecht, R.3    Plattner, H.4
  • 347
    • 0037117610 scopus 로고    scopus 로고
    • Distinct SNARE complexes mediating membrane fusion in Golgi transport based on combinatorial specificity
    • Parlati, F., Varlamov, O., Paz, K., McNew, J.A., Hurtado, D., Söllner, T.H., et al., 2002. Distinct SNARE complexes mediating membrane fusion in Golgi transport based on combinatorial specificity. Proc. Natl. Acad. Sci. USA 99, 5424-5429.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5424-5429
    • Parlati, F.1    Varlamov, O.2    Paz, K.3    McNew, J.A.4    Hurtado, D.5    Söllner, T.H.6
  • 348
    • 0031973716 scopus 로고    scopus 로고
    • The AAA team: related ATPases with diverse functions
    • Patel, S., Latterich, M., 1998. The AAA team: related ATPases with diverse functions. Trends Cell Biol. 8, 65-71.
    • (1998) Trends Cell Biol , vol.8 , pp. 65-71
    • Patel, S.1    Latterich, M.2
  • 349
    • 0018101264 scopus 로고
    • Membranous sacs associated with cilia of Paramecium
    • Patterson, D.J., 1978. Membranous sacs associated with cilia of Paramecium. Cytobiology 17, 107-113.
    • (1978) Cytobiology , vol.17 , pp. 107-113
    • Patterson, D.J.1
  • 350
    • 1542409030 scopus 로고    scopus 로고
    • The specificity of SNARE-dependent fusion is encoded in the SNARE motif
    • Paumet, F., Rahimian, V., Rothman, J.E., 2004. The specificity of SNARE-dependent fusion is encoded in the SNARE motif. Proc. Natl. Acad. Sci. USA 101, 3376-3380.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3376-3380
    • Paumet, F.1    Rahimian, V.2    Rothman, J.E.3
  • 352
    • 0026029035 scopus 로고
    • Multiple a-tubulin isoforms in cilia and cytoskeleton of Tetrahymena pyriformis generated by post-translational modifications Studies during reciliation
    • Penque, D., Galego, L., Rodrigues-Pousada, C., 1991. Multiple a-tubulin isoforms in cilia and cytoskeleton of Tetrahymena pyriformis generated by post-translational modifications. Studies during reciliation. Eur. J. Biochem. 195, 487-494.
    • (1991) Eur. J. Biochem. , vol.195 , pp. 487-494
    • Penque, D.1    Galego, L.2    Rodrigues-Pousada, C.3
  • 353
    • 0026088029 scopus 로고
    • Structural and functional conservation of synaptotagmin (p65) in Drosophila and humans
    • Perin, M.S., Johnston, P.A., Özcelik, T., Jahn, R., Francke, U., Südhof, T.C., 1991. Structural and functional conservation of synaptotagmin (p65) in Drosophila and humans. J. Biol. Chem. 266, 615-622.
    • (1991) J. Biol. Chem. , vol.266 , pp. 615-622
    • Perin, M.S.1    Johnston, P.A.2    Özcelik, T.3    Jahn, R.4    Francke, U.5    Südhof, T.C.6
  • 354
    • 0032506349 scopus 로고    scopus 로고
    • 2+/calmodulin signals the completion of docking and triggers a late step of vacuole fusion
    • 2+/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
  • 355
    • 0035252348 scopus 로고    scopus 로고
    • Transcomplex formation by proteolipid channels in the terminal phase of membrane fusion
    • Peters, C., Bayer, M.J., Bühler, S., Andersen, J.S., Mann, M., Mayer, A., 2001. Transcomplex formation by proteolipid channels in the terminal phase of membrane fusion. Nature 409, 581-588.
    • (2001) Nature , vol.409 , pp. 581-588
    • Peters, C.1    Bayer, M.J.2    Bühler, S.3    Andersen, J.S.4    Mann, M.5    Mayer, A.6
  • 356
    • 0026228127 scopus 로고
    • Small GTP-binding proteins associated with secretory vesicles of Paramecium
    • Peterson, J.B., 1991. Small GTP-binding proteins associated with secretory vesicles of Paramecium. J. Protozool. 38, 495-501.
    • (1991) J. Protozool. , vol.38 , pp. 495-501
    • Peterson, J.B.1
  • 357
    • 34548625556 scopus 로고    scopus 로고
    • Unsolved mysteries in membrane traffic
    • Pfeffer, S.R., 2007. Unsolved mysteries in membrane traffic. Annu. Rev. Biochem. 76, 629-645.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 629-645
    • Pfeffer, S.R.1
  • 358
    • 0016136026 scopus 로고
    • Intramembraneous changes on cationophore-triggered exocytosis in Paramecium
    • Plattner, H., 1974. Intramembraneous changes on cationophore-triggered exocytosis in Paramecium. Nature 252, 722-724.
    • (1974) Nature , vol.252 , pp. 722-724
    • Plattner, H.1
  • 359
    • 0019828157 scopus 로고
    • Membrane behaviour during exocytosis
    • Plattner, H., 1981. Membrane behaviour during exocytosis. Cell Biol. Int. Rep. 5, 435-459.
    • (1981) Cell Biol. Int. Rep. , vol.5 , pp. 435-459
    • Plattner, H.1
  • 360
    • 0001857542 scopus 로고
    • Synchronous exocytosis in Paramecium cells
    • Sowers, A.E. (Ed.), Plenum Press, New York
    • Plattner, H., 1987. Synchronous exocytosis in Paramecium cells. In: Sowers, A.E. (Ed.), Cell Fusion. Plenum Press, New York, pp. 69-98.
    • (1987) Cell Fusion , pp. 69-98
    • Plattner, H.1
  • 361
    • 0024909111 scopus 로고
    • Regulation of membrane fusion during exocytosis
    • Plattner, H., 1989. Regulation of membrane fusion during exocytosis. Int. Rev. Cytol. 119, 197-286.
    • (1989) Int. Rev. Cytol. , vol.119 , pp. 197-286
    • Plattner, H.1
  • 362
    • 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
  • 363
    • 0346256847 scopus 로고    scopus 로고
    • Molecular aspects of membrane trafficking in Paramecium
    • Plattner, H., Kissmehl, R., 2003a. 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
  • 364
    • 0041659178 scopus 로고    scopus 로고
    • Dense-core secretory vesicle docking and exocytotic membrane fusion in Paramecium cells
    • Plattner, H., Kissmehl, R., 2003b. Dense-core secretory vesicle docking and exocytotic membrane fusion in Paramecium cells. Biochim. Biophys. Acta Mol. Cell Res. 1641, 183-193.
    • (2003) Biochim. Biophys. Acta Mol. Cell Res. , vol.1641 , pp. 183-193
    • Plattner, H.1    Kissmehl, R.2
  • 365
    • 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
  • 366
    • 0002485261 scopus 로고
    • The "focal membrane fusion" model revisited: toward a unifying structural concept of biological membrane fusion
    • O'Day, D.H. (Ed.), Academic Press, New York
    • Plattner, H., Knoll, G., 1993. The "focal membrane fusion" model revisited: toward a unifying structural concept of biological membrane fusion. In: O'Day, D.H. (Ed.), Signal Transduction During Biomembrane Fusion. Academic Press, New York, pp. 19-46.
    • (1993) Signal Transduction During Biomembrane Fusion , pp. 19-46
    • Plattner, H.1    Knoll, G.2
  • 367
    • 0015846192 scopus 로고
    • Membrane specializations in the form of regular membrane-to-membrane attachment sites in Paramecium A correlated freezeetching and ultrathin-sectioning analysis
    • Plattner, H., Miller, F., Bachmann, L., 1973. Membrane specializations in the form of regular membrane-to-membrane attachment sites in Paramecium. A correlated freezeetching and ultrathin-sectioning analysis. J. Cell Sci. 13, 687-719.
    • (1973) J. Cell Sci. , vol.13 , pp. 687-719
    • Plattner, H.1    Miller, F.2    Bachmann, L.3
  • 368
    • 0020093799 scopus 로고
    • Cytoskeleton-secretory vesicle interactions during the docking of secretory vesicles at the cell membrane in Paramecium tetraurelia cells
    • Plattner, H., Westphal, C., Tiggemann, R., 1982. Cytoskeleton-secretory vesicle interactions during the docking of secretory vesicles at the cell membrane in Paramecium tetraurelia cells. J. Cell Biol. 92, 368-377.
    • (1982) J. Cell Biol. , vol.92 , pp. 368-377
    • Plattner, H.1    Westphal, C.2    Tiggemann, R.3
  • 369
    • 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
  • 370
    • 0022269152 scopus 로고
    • Synchronous exocytosis in Paramecium cells. VI. Ultrastructural analysis of membrane resealing and retrieval
    • Plattner, H., Pape, R., Haacke, B., Olbricht, K., Westphal, C., Kersken, H., 1985a. Synchronous exocytosis in Paramecium cells. VI. Ultrastructural analysis of membrane resealing and retrieval. J. Cell Sci. 77, 1-17.
    • (1985) J. Cell Sci. , vol.77 , pp. 1-17
    • Plattner, H.1    Pape, R.2    Haacke, B.3    Olbricht, K.4    Westphal, C.5    Kersken, H.6
  • 371
    • 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., 1985b. 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
  • 372
    • 0027057592 scopus 로고
    • The mechanics of biological membrane fusion Merger of aspects from electron microscopy and patch-clamp analysis
    • Plattner, H., Knoll, G., Erxleben, C., 1992. The mechanics of biological membrane fusion. Merger of aspects from electron microscopy and patch-clamp analysis. J. Cell Sci. 103, 613-618.
    • (1992) J. Cell Sci. , vol.103 , pp. 613-618
    • Plattner, H.1    Knoll, G.2    Erxleben, C.3
  • 373
    • 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
    • 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, pp. 123-148.
    • (1993) Membrane Traffic in Protozoa , pp. 123-148
    • Plattner, H.1    Knoll, G.2    Pape, R.3
  • 374
    • 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
    • Plattner, H., Braun, C., Hentschel, J., 1997. Facilitation of membrane fusion during exocytosis and exocytosis-coupled endocytosis and acceleration of "ghost" detachment in Paramecium by extracellular calcium. J. Membr. Biol. 158, 197-208.
    • (1997) J. Membr. Biol. , vol.158 , pp. 197-208
    • Plattner, H.1    Braun, C.2    Hentschel, J.3
  • 375
    • 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
  • 376
    • 33746915109 scopus 로고    scopus 로고
    • N to C-terminal SNARE complex assembly promotes rapid membrane fusion
    • Pobbati, A.V., Stein, A., Fasshauer, D., 2006. N to C-terminal SNARE complex assembly promotes rapid membrane fusion. Science 313, 673-676.
    • (2006) Science , vol.313 , pp. 673-676
    • Pobbati, A.V.1    Stein, A.2    Fasshauer, D.3
  • 377
    • 35548970161 scopus 로고    scopus 로고
    • Distinct v-SNAREs regulate direct and indirect apical delivery in polarized epithelia cells
    • Pocard, T., LeBivic, A., Galli, T., Zurzolo, C., 2007. Distinct v-SNAREs regulate direct and indirect apical delivery in polarized epithelia cells. J. Cell Sci. 120, 3309-3320.
    • (2007) J. Cell Sci. , vol.120 , pp. 3309-3320
    • Pocard, T.1    LeBivic, A.2    Galli, T.3    Zurzolo, C.4
  • 378
    • 0016257034 scopus 로고
    • Mutations affecting the trichocysts in Paramecium aurelia. I. Morphology and description of the mutants
    • Pollack, S., 1974. Mutations affecting the trichocysts in Paramecium aurelia. I. Morphology and description of the mutants. J. Protozool. 21, 352-362.
    • (1974) J. Protozool. , vol.21 , pp. 352-362
    • Pollack, S.1
  • 379
    • 0035865464 scopus 로고    scopus 로고
    • Genomics, the cytoskeleton and motility
    • Pollard, T.D., 2001. Genomics, the cytoskeleton and motility. Nature 409, 842-843.
    • (2001) Nature , vol.409 , pp. 842-843
    • Pollard, T.D.1
  • 380
    • 56349166631 scopus 로고    scopus 로고
    • Vesicular transport: EnSNAREd by GAPs
    • Poon, P.P., Spang, A., 2008. Vesicular transport: EnSNAREd by GAPs. Curr. Biol. 18, R1053-R1054.
    • (2008) Curr. Biol. , vol.18
    • Poon, P.P.1    Spang, A.2
  • 381
    • 0346874341 scopus 로고    scopus 로고
    • Synaptotagmin I is necessary for compensatory synaptic vesicle endocytosis in vivo
    • Poskanzer, K.E., Marek, K.W., Sweeney, S.T., Davis, G.W., 2003. Synaptotagmin I is necessary for compensatory synaptic vesicle endocytosis in vivo. Nature 426, 559-563.
    • (2003) Nature , vol.426 , pp. 559-563
    • Poskanzer, K.E.1    Marek, K.W.2    Sweeney, S.T.3    Davis, G.W.4
  • 382
    • 0001188280 scopus 로고
    • Genetic dissection of the morphogenesis of exocytosis sites in Paramecium
    • Pouphile, M., Lefort-Tran, M., Plattner, H., Rossignol, M., Beisson, J., 1986. Genetic dissection of the morphogenesis of exocytosis sites in Paramecium. Biol. Cell 56, 151-162.
    • (1986) Biol. Cell , vol.56 , pp. 151-162
    • Pouphile, M.1    Lefort-Tran, M.2    Plattner, H.3    Rossignol, M.4    Beisson, J.5
  • 383
    • 43049180250 scopus 로고    scopus 로고
    • 2+- buffering in prion-null mice: association with reduced afterhyperpolarizations in CA1 hippocampal neurons
    • 2+- buffering in prion-null mice: association with reduced afterhyperpolarizations in CA1 hippocampal neurons. J. Neurosci. 28, 3877-3886.
    • (2008) J. Neurosci. , vol.28 , pp. 3877-3886
    • Powell, A.D.1    Toescu, E.C.2    Collinge, J.3    Jefferys, J.G.R.4
  • 384
    • 50549086057 scopus 로고    scopus 로고
    • Molecular basis for the sorting of the SNARE VAMP7 into endocytic clathrincoated vesicles by the ArfGAP Hrb
    • Pryor, P.R., Jackson, L., Gray, S.R., Edeling, M.A., Thompson, A., Sanderson, C.M., et al., 2008. Molecular basis for the sorting of the SNARE VAMP7 into endocytic clathrincoated vesicles by the ArfGAP Hrb. Cell 134, 817-827.
    • (2008) Cell , vol.134 , pp. 817-827
    • Pryor, P.R.1    Jackson, L.2    Gray, S.R.3    Edeling, M.A.4    Thompson, A.5    Sanderson, C.M.6
  • 385
    • 34548319580 scopus 로고    scopus 로고
    • Cellular environment is important in controlling V-ATPase dissociation and its dependence on activity
    • Qi, J., Forgac, M., 2007. Cellular environment is important in controlling V-ATPase dissociation and its dependence on activity. J. Biol. Chem. 282, 24743-24751.
    • (2007) J. Biol. Chem. , vol.282 , pp. 24743-24751
    • Qi, J.1    Forgac, M.2
  • 386
    • 0036683087 scopus 로고    scopus 로고
    • Calmodulin and lipid binding to synaptobrevin regulates calcium-dependent exocytosis
    • Quetlas, S., Iborra, C., Sasakawa, N., De Haro, L., Kumakura, K., Sato, K., et al., 2002. Calmodulin and lipid binding to synaptobrevin regulates calcium-dependent exocytosis. EMBO J. 21, 3970-3979.
    • (2002) EMBO J , vol.21 , pp. 3970-3979
    • Quetlas, S.1    Iborra, C.2    Sasakawa, N.3    De Haro, L.4    Kumakura, K.5    Sato, K.6
  • 387
    • 70349696856 scopus 로고    scopus 로고
    • Independent transport and sorting of functionally distinct protein families in Tetrahymena thermophila dense core secretory granules
    • Rahaman, A., Miao, W., Turkewitz, A.P., 2009. Independent transport and sorting of functionally distinct protein families in Tetrahymena thermophila dense core secretory granules. Eukaryot. Cell 8, 1575-1583.
    • (2009) Eukaryot. Cell , vol.8 , pp. 1575-1583
    • Rahaman, A.1    Miao, W.2    Turkewitz, A.P.3
  • 389
    • 0034833877 scopus 로고    scopus 로고
    • Fluid phase and receptor-mediated endocytosis in Paramecium primaurelia by fluorescence confocal laser scanning microscopy
    • Ramoino, P., Fronte, P., Fato, M., Beltrame, F., Robello, M., Diaspro, A., 2001. Fluid phase and receptor-mediated endocytosis in Paramecium primaurelia by fluorescence confocal laser scanning microscopy. Eur. Biophys. J. 30, 305-312.
    • (2001) Eur. Biophys. J. , vol.30 , pp. 305-312
    • Ramoino, P.1    Fronte, P.2    Fato, M.3    Beltrame, F.4    Robello, M.5    Diaspro, A.6
  • 390
    • 33645158483 scopus 로고    scopus 로고
    • V-ATPase: a potential pH sensor
    • Recchi, C., Chavrier, P., 2006. V-ATPase: a potential pH sensor. Nat. Cell Biol. 8, 107-109.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 107-109
    • Recchi, C.1    Chavrier, P.2
  • 391
    • 0036673069 scopus 로고    scopus 로고
    • Snares and munc 18 in synaptic vesicle fusion
    • Rizo, J., Südhof, T.C., 2002. Snares and munc 18 in synaptic vesicle fusion. Nat. Rev. Neurosci. 3, 641-653.
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 641-653
    • Rizo, J.1    Südhof, T.C.2
  • 392
    • 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
  • 393
    • 53749091460 scopus 로고    scopus 로고
    • What is moving in the secretory pathway of plants?
    • Rojo, E., Denecke, J., 2008. What is moving in the secretory pathway of plants? Plant Physiol. 147, 1493-1503.
    • (2008) Plant Physiol , vol.147 , pp. 1493-1503
    • Rojo, E.1    Denecke, J.2
  • 395
    • 0028261177 scopus 로고
    • Exo-endocytosis and closing of the fission pore during endocytosis in single pituitary nerve terminals internally perfused with high calcium concentrations
    • Rosenboom, H., Lindau, M., 1994. Exo-endocytosis and closing of the fission pore during endocytosis in single pituitary nerve terminals internally perfused with high calcium concentrations. Proc. Natl. Acad. Sci. USA 91, 5267-5271.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5267-5271
    • Rosenboom, H.1    Lindau, M.2
  • 397
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman, J.E., 1994. Mechanisms of intracellular protein transport. Nature 372, 55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 398
    • 0028385277 scopus 로고
    • Implications of the SNARE hypothesis for intracellular membrane topology and dynamics
    • Rothman, J.E., Warren, G., 1994. Implications of the SNARE hypothesis for intracellular membrane topology and dynamics. Curr. Biol. 4, 220-233.
    • (1994) Curr. Biol. , vol.4 , pp. 220-233
    • Rothman, J.E.1    Warren, G.2
  • 399
    • 0028892429 scopus 로고
    • Proteolytic processing mechanisms in the biosynthesis of neuroendocrine peptides: the subtilisin-like proprotein convertases
    • Rouillé, Y., Duguay, S.J., Lund, K., Furuta, M., Gong, Q., Lipkind, G., et al., 1995. Proteolytic processing mechanisms in the biosynthesis of neuroendocrine peptides: the subtilisin-like proprotein convertases. Front. Neuroendocrinol. 16, 322-361.
    • (1995) Front. Neuroendocrinol. , vol.16 , pp. 322-361
    • Rouillé, Y.1    Duguay, S.J.2    Lund, K.3    Furuta, M.4    Gong, Q.5    Lipkind, G.6
  • 400
    • 57649167478 scopus 로고    scopus 로고
    • The long and short of membrane fission
    • Roux, A., Antonny, B., 2008. The long and short of membrane fission. Cell 135, 1163-1165.
    • (2008) Cell , vol.135 , pp. 1163-1165
    • Roux, A.1    Antonny, B.2
  • 402
    • 0033563810 scopus 로고    scopus 로고
    • 3H]scyllo-inositol by Tetrahymena: incorporation into phosphatidylinositol, phosphatidylinositol-linked glycans, and polyphosphoinositols
    • 3H]scyllo-inositol by Tetrahymena: incorporation into phosphatidylinositol, phosphatidylinositol-linked glycans, and polyphosphoinositols. Arch. Biochem. Biophys. 366, 261-266.
    • (1999) Arch. Biochem. Biophys. , vol.366 , pp. 261-266
    • Ryals, P.E.1    Kersting, M.C.2
  • 403
    • 59449088040 scopus 로고    scopus 로고
    • Voa1p functions in V-ATPase assembly in the yeast endoplasmic reticulum
    • Ryan, M., Graham, L.A., Stevens, T.H., 2008. Voa1p functions in V-ATPase assembly in the yeast endoplasmic reticulum. Mol. Biol. Cell 19, 5131-5142.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 5131-5142
    • Ryan, M.1    Graham, L.A.2    Stevens, T.H.3
  • 405
    • 55949104921 scopus 로고    scopus 로고
    • Membrane microdomain switching: a regulatory mechanism of amyloid precursor protein processing
    • Sakurai, T., Kaneko, K., Okuno, M., Wada, K., Kashiyama, T., Shimizu, H., et al., 2008. Membrane microdomain switching: a regulatory mechanism of amyloid precursor protein processing. J. Cell Biol. 183, 339-352.
    • (2008) J. Cell Biol. , vol.183 , pp. 339-352
    • Sakurai, T.1    Kaneko, K.2    Okuno, M.3    Wada, K.4    Kashiyama, T.5    Shimizu, H.6
  • 406
    • 34250682971 scopus 로고    scopus 로고
    • Increases in the number of SNARE genes parallels the rise of multicellularity among the green plants
    • Sanderfoot, A., 2007. Increases in the number of SNARE genes parallels the rise of multicellularity among the green plants. Plant Physiol. 144, 6-17.
    • (2007) Plant Physiol , vol.144 , pp. 6-17
    • Sanderfoot, A.1
  • 407
    • 0029257210 scopus 로고
    • Conjugation rescue of exocytosis mutants in Tetrahymena thermophila indicates the presence of functional intermediates in the regulated secretory pathway
    • Sauer, M.K., Kelly, R.B., 1995. Conjugation rescue of exocytosis mutants in Tetrahymena thermophila indicates the presence of functional intermediates in the regulated secretory pathway. J. Eukaryot. Microbiol. 42, 173-183.
    • (1995) J. Eukaryot. Microbiol. , vol.42 , pp. 173-183
    • Sauer, M.K.1    Kelly, R.B.2
  • 408
    • 62549102934 scopus 로고    scopus 로고
    • Arabidopsis synaptotagmin 1 is required for the maintenance of plasma membrane integrity and cell viability
    • Schapire, A.L., Voigt, B., Jasik, J., Rosado, A., Lopez-Cobollo, R., Menzel, D., et al., 2008. Arabidopsis synaptotagmin 1 is required for the maintenance of plasma membrane integrity and cell viability. Plant Cell 20, 3374-3388.
    • (2008) Plant Cell , vol.20 , pp. 3374-3388
    • Schapire, A.L.1    Voigt, B.2    Jasik, J.3    Rosado, A.4    Lopez-Cobollo, R.5    Menzel, D.6
  • 410
    • 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
  • 411
    • 48949084738 scopus 로고    scopus 로고
    • Molecular identification of a SNAP-25-like SNARE protein in Paramecium
    • Schilde, C., Lutter, K., Kissmehl, R., Plattner, H., 2008. Molecular identification of a SNAP-25-like SNARE protein in Paramecium. Eukaryot. Cell 7, 1387-1402.
    • (2008) Eukaryot. Cell , vol.7 , pp. 1387-1402
    • Schilde, C.1    Lutter, K.2    Kissmehl, R.3    Plattner, H.4
  • 412
    • 75849116774 scopus 로고    scopus 로고
    • Distinct subcellular localization of a group of synaptobrevin-like SNAREs in Paramecium tetraurelia and effects of silencing of the SNARE-specific chaperone, NSF
    • Schilde, C., Schönemann, B., Sehring, I.M., Plattner, H., 2010. Distinct subcellular localization of a group of synaptobrevin-like SNAREs in Paramecium tetraurelia and effects of silencing of the SNARE-specific chaperone, NSF. Eukaryot. Cell 9, 288-305.
    • (2010) Eukaryot. Cell , vol.9 , pp. 288-305
    • Schilde, C.1    Schönemann, B.2    Sehring, I.M.3    Plattner, H.4
  • 413
    • 33646461205 scopus 로고    scopus 로고
    • The structure of the mammalian signal recognition particle (SRP) receptor as prototype for the interaction of small GTPases with longin domains
    • Schlenker, O., Hendricks, A., Sinning, I., Wild, K., 2006. The structure of the mammalian signal recognition particle (SRP) receptor as prototype for the interaction of small GTPases with longin domains. J. Biol. Chem. 281, 8898-8906.
    • (2006) J. Biol. Chem. , vol.281 , pp. 8898-8906
    • Schlenker, O.1    Hendricks, A.2    Sinning, I.3    Wild, K.4
  • 415
    • 0025663441 scopus 로고
    • Vesicle transport along microtubular ribbons and isolation of cytoplasmic dynein from Paramecium
    • Schroeder, C.C., Fok, A.K., Allen, R.D., 1990. Vesicle transport along microtubular ribbons and isolation of cytoplasmic dynein from Paramecium. J. Cell Biol. 111, 2553-2562.
    • (1990) J. Cell Biol. , vol.111 , pp. 2553-2562
    • Schroeder, C.C.1    Fok, A.K.2    Allen, R.D.3
  • 417
    • 9344268278 scopus 로고    scopus 로고
    • Synaptotagmin promotes both vesicle fusion and recycling
    • Schwartz, T.L., 2004. Synaptotagmin promotes both vesicle fusion and recycling. Proc. Natl. Acad. Sci. USA 101, 16401-16402.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 16401-16402
    • Schwartz, T.L.1
  • 418
    • 65649153795 scopus 로고    scopus 로고
    • Capture and release of partially zipped trans-SNARE complexes on intact organelles
    • Schwartz, M.L., Merz, A.J., 2009. Capture and release of partially zipped trans-SNARE complexes on intact organelles. J. Cell Biol. 185, 535-549.
    • (2009) J. Cell Biol. , vol.185 , pp. 535-549
    • Schwartz, M.L.1    Merz, A.J.2
  • 420
    • 36248977639 scopus 로고    scopus 로고
    • + -ATPase in the targeting of proton pump-coated vesicles to collecting duct cell apical membrane
    • + -ATPase in the targeting of proton pump-coated vesicles to collecting duct cell apical membrane. Kidney Int. 72, 1310-1315.
    • (2007) Kidney Int , vol.72 , pp. 1310-1315
    • Schwartz, J.H.1    Li, G.2    Suri, V.3    Ross, J.J.4    Alexander, E.A.5
  • 422
    • 33846804142 scopus 로고    scopus 로고
    • A broad spectrum of actin paralogs in Paramecium tetraurelia cells display differential localization and function
    • Sehring, I.M., Reiner, C., Mansfeld, J., Plattner, H., Kissmehl, R., 2007b. 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
  • 423
    • 77952009906 scopus 로고    scopus 로고
    • The actin subfamily PtAct4, out of many subfamilies, is differentially localized for specific local functions in Paramecium tetraurelia cells
    • (in press)
    • Sehring, I.M., Reiner, C., Plattner, H., 2010. The actin subfamily PtAct4, out of many subfamilies, is differentially localized for specific local functions in Paramecium tetraurelia cells. Eur. J. Cell Biol. (in press).
    • (2010) Eur. J. Cell Biol.
    • Sehring, I.M.1    Reiner, C.2    Plattner, H.3
  • 424
    • 0037133578 scopus 로고    scopus 로고
    • A robust inducible-repressible promoter greatly facilitates gene knockouts, conditional expression, and overexpression of homologous and heterologous genes in Tetrahymena thermophila
    • Shang, Y., Song, X., Bowen, J., Corstanje, R., Gao, Y., Gaertig, J., et al., 2002. A robust inducible-repressible promoter greatly facilitates gene knockouts, conditional expression, and overexpression of homologous and heterologous genes in Tetrahymena thermophila. Proc. Natl. Acad. Sci. USA 99, 3734-3739.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 3734-3739
    • Shang, Y.1    Song, X.2    Bowen, J.3    Corstanje, R.4    Gao, Y.5    Gaertig, J.6
  • 426
    • 33646202286 scopus 로고    scopus 로고
    • The SNARE motif is essential for the formation of syntaxin clusters in the plasma membrane
    • Sieber, J.J., Willig, K.I., Heintzmann, R., Hell, S.W., Lang, T., 2006. The SNARE motif is essential for the formation of syntaxin clusters in the plasma membrane. Biophys. J. 90, 2843-2851.
    • (2006) Biophys. J. , vol.90 , pp. 2843-2851
    • Sieber, J.J.1    Willig, K.I.2    Heintzmann, R.3    Hell, S.W.4    Lang, T.5
  • 428
    • 0002637639 scopus 로고
    • Cytoplasmic streaming in Paramecium
    • Sikora, J., 1981. Cytoplasmic streaming in Paramecium. Protoplasma 109, 57-77.
    • (1981) Protoplasma , vol.109 , pp. 57-77
    • Sikora, J.1
  • 429
    • 0030997642 scopus 로고    scopus 로고
    • Genetic approach to regulated exocytosis using functional complementation in Paramecium: identification of the ND7 gene required for membrane fusion
    • Skouri, F., Cohen, J., 1997. Genetic approach to regulated exocytosis using functional complementation in Paramecium: identification of the ND7 gene required for membrane fusion. Mol. Biol. Cell 8, 1063-1071.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1063-1071
    • Skouri, F.1    Cohen, J.2
  • 430
  • 431
    • 33845315084 scopus 로고    scopus 로고
    • Powering membrane traffic in endocytosis and recycling
    • Soldati, T., Schliwa, M., 2006. Powering membrane traffic in endocytosis and recycling. Nat. Rev. Mol. Cell Biol. 7, 897-908.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 897-908
    • Soldati, T.1    Schliwa, M.2
  • 432
    • 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, M.K., Whiteheart, S.W., Scheller, R.H., Rothman, J.E., 1993a. A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion. Cell 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
  • 434
    • 23944501982 scopus 로고    scopus 로고
    • SNARE complexes prepare for membrane fusion
    • Sorensen, J.B., 2005. SNARE complexes prepare for membrane fusion. Trends Neurosci. 28, 453-455.
    • (2005) Trends Neurosci , vol.28 , pp. 453-455
    • Sorensen, J.B.1
  • 435
    • 33644852285 scopus 로고    scopus 로고
    • Sequential N to C-terminal SNARE complex assembly drives priming and fusion of secretory vesicles
    • Sorensen, J.B., Wiederhold, K., Müller, E.M., Milosevic, I., Nagy, G., De Groot, B.L., et al., 2006. Sequential N to C-terminal SNARE complex assembly drives priming and fusion of secretory vesicles. EMBO J. 25, 955-966.
    • (2006) EMBO J , vol.25 , pp. 955-966
    • Sorensen, J.B.1    Wiederhold, K.2    Müller, E.M.3    Milosevic, I.4    Nagy, G.5    De Groot, B.L.6
  • 436
    • 67949124784 scopus 로고    scopus 로고
    • On vesicle formation and tethering in the ER-Golgi shuttle
    • Spang, A., 2009. On vesicle formation and tethering in the ER-Golgi shuttle. Curr. Opin. Cell Biol. 21, 531-536.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 531-536
    • Spang, A.1
  • 437
    • 64849095076 scopus 로고    scopus 로고
    • Grab a Golgi: laser trapping of Golgi bodies reveals in vivo interactions with the endoplasmic reticulum
    • Sparkes, I.A., Ketelaar, T., De Ruijter, N.C.A., Hawes, C., 2009. Grab a Golgi: laser trapping of Golgi bodies reveals in vivo interactions with the endoplasmic reticulum. Traffic 10, 567-571.
    • (2009) Traffic , vol.10 , pp. 567-571
    • Sparkes, I.A.1    Ketelaar, T.2    De Ruijter, N.C.A.3    Hawes, C.4
  • 438
    • 0023428178 scopus 로고
    • The crystal lattice of Paramecium trichocysts before and after exocytosis by X-ray diffraction and freeze-fracture electron microscopy
    • Sperling, L., Tardieu, A., Gulik-Krzywicki, T., 1987. The crystal lattice of Paramecium trichocysts before and after exocytosis by X-ray diffraction and freeze-fracture electron microscopy. J. Cell Biol. 105, 1649-1662.
    • (1987) J. Cell Biol. , vol.105 , pp. 1649-1662
    • Sperling, L.1    Tardieu, A.2    Gulik-Krzywicki, T.3
  • 440
    • 0032584717 scopus 로고    scopus 로고
    • Nucleation of COPII vesicular coat complex by endoplasmic reticulum to Golgi vesicle SNAREs
    • Springer, S., Schekman, R., 1998. Nucleation of COPII vesicular coat complex by endoplasmic reticulum to Golgi vesicle SNAREs. Science 281, 698-700.
    • (1998) Science , vol.281 , pp. 698-700
    • Springer, S.1    Schekman, R.2
  • 441
    • 36749083072 scopus 로고    scopus 로고
    • Phagosomal alcidification: measurement, manipulation and functional consequences
    • Steinberg, B.E., Huynh, K.K., Grinstein, S., 2007. Phagosomal alcidification: measurement, manipulation and functional consequences. Biochem. Soc. Trans. 35, 1083-1087.
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 1083-1087
    • Steinberg, B.E.1    Huynh, K.K.2    Grinstein, S.3
  • 442
    • 0025876729 scopus 로고
    • Cortical alveoli of Paramecium: a vast submembranous calcium storage compartment
    • Stelly, N., Mauger, J.P., Kéryer, G., 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    Kéryer, G.3    Claret, M.4    Adoutte, A.5
  • 443
    • 41949123425 scopus 로고    scopus 로고
    • Dimer ribbons of ATP synthase shape the inner mitochondrial membrane
    • Strauss, M., Hofhaus, G., Schröder, R.R., Kühlbrandt, W., 2008. Dimer ribbons of ATP synthase shape the inner mitochondrial membrane. EMBO J. 27, 1154-1160.
    • (2008) EMBO J , vol.27 , pp. 1154-1160
    • Strauss, M.1    Hofhaus, G.2    Schröder, R.R.3    Kühlbrandt, W.4
  • 444
    • 0024634937 scopus 로고
    • The inositol lipids of Paramecium tetraurelia and preliminary characterizations of phosphoinositide kinase activity in the ciliary membrane
    • Suchard, S.J., Rhoads, D.E., Kaneshiro, E.S., 1989. The inositol lipids of Paramecium tetraurelia and preliminary characterizations of phosphoinositide kinase activity in the ciliary membrane. J. Protozool. 36, 185-190.
    • (1989) J. Protozool. , vol.36 , pp. 185-190
    • Suchard, S.J.1    Rhoads, D.E.2    Kaneshiro, E.S.3
  • 445
    • 35348897753 scopus 로고    scopus 로고
    • Membrane fusion as a team effort
    • Südhof, T.C., 2007. Membrane fusion as a team effort. Proc. Natl. Acad. Sci. USA 104, 13541-13542.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 13541-13542
    • Südhof, T.C.1
  • 447
    • 67650150253 scopus 로고    scopus 로고
    • The roles of actin cytoskeleton and microtubules for membrane recycling of a food vacuole in Tetrahymena thermophila
    • Sugita, M., Nakano, K., Sato, M., Toyooka, K., Numata, O., 2009. The roles of actin cytoskeleton and microtubules for membrane recycling of a food vacuole in Tetrahymena thermophila. Cell Motil. Cytoskeleton 66, 371-377.
    • (2009) Cell Motil. Cytoskeleton , vol.66 , pp. 371-377
    • Sugita, M.1    Nakano, K.2    Sato, M.3    Toyooka, K.4    Numata, O.5
  • 448
    • 33751511196 scopus 로고    scopus 로고
    • The a3 isoform of V-ATPase regulates insulin secretion from pancreatic beta cells
    • Sun-Wada, G.-H., Toyomura, T., Murata, Y., Yamamoto, A., Futai, M., Wada, Y., 2006. The a3 isoform of V-ATPase regulates insulin secretion from pancreatic beta cells. J. Cell Sci. 119, 4531-4540.
    • (2006) J. Cell Sci. , vol.119 , pp. 4531-4540
    • Sun-Wada, G.-H.1    Toyomura, T.2    Murata, Y.3    Yamamoto, A.4    Futai, M.5    Wada, Y.6
  • 450
    • 33645240221 scopus 로고    scopus 로고
    • Cloning of two genes encoding Rab7 in Paramecium
    • Surmacz, L., Wiejak, J., Wyroba, E., 2006. Cloning of two genes encoding Rab7 in Paramecium. Acta Biochim. Pol. 53, 149-156.
    • (2006) Acta Biochim. Pol. , vol.53 , pp. 149-156
    • Surmacz, L.1    Wiejak, J.2    Wyroba, E.3
  • 451
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2 4 Å resolution
    • Sutton, R.B., Fasshauer, D., Jahn, R., Brunger, A.T., 1998. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution. Nature 395, 347-353.
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 452
    • 0022377781 scopus 로고
    • Carbohydrates of lysosomal enzymes secreted by Tetrahymena pyriformis
    • Taniguchi, T., Mizuochi, T., Banno, Y., Nozawa, Y., Kobata, A., 1985. Carbohydrates of lysosomal enzymes secreted by Tetrahymena pyriformis. J. Biol. Chem. 260, 13941-13946.
    • (1985) J. Biol. Chem. , vol.260 , pp. 13941-13946
    • Taniguchi, T.1    Mizuochi, T.2    Banno, Y.3    Nozawa, Y.4    Kobata, A.5
  • 453
    • 0029843493 scopus 로고    scopus 로고
    • The exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae
    • Terbush, D.R., Maurice, T., Roth, D., Novick, P., 1996. The exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae. EMBO J. 15, 6483-6494.
    • (1996) EMBO J , vol.15 , pp. 6483-6494
    • Terbush, D.R.1    Maurice, T.2    Roth, D.3    Novick, P.4
  • 454
    • 3542999933 scopus 로고    scopus 로고
    • A soluble SNARE drives rapid docking, bypassing ATP and Sec17/18p for vacuole fusion
    • Thorngren, N., Collins, K.M., Fratti, R.A., Wickner, W., Merz, A.J., 2004. A soluble SNARE drives rapid docking, bypassing ATP and Sec17/18p for vacuole fusion. EMBO J. 23, 2765-2776.
    • (2004) EMBO J , vol.23 , pp. 2765-2776
    • Thorngren, N.1    Collins, K.M.2    Fratti, R.A.3    Wickner, W.4    Merz, A.J.5
  • 455
    • 0024741693 scopus 로고
    • Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite Listeria monocytogenes
    • Tilney, L.G., Portnoy, D.A., 1989. Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite, Listeria monocytogenes. J. Cell Biol. 109, 1597-1608.
    • (1989) J. Cell Biol. , vol.109 , pp. 1597-1608
    • Tilney, L.G.1    Portnoy, D.A.2
  • 456
    • 0022917578 scopus 로고
    • Selection of chemical spacers to improve isoelectric focussing resolving power: implications for use in two-dimensional electrophoresis
    • Tindall, S.H., 1986. Selection of chemical spacers to improve isoelectric focussing resolving power: implications for use in two-dimensional electrophoresis. Anal. Biochem. 159, 287-294.
    • (1986) Anal. Biochem. , vol.159 , pp. 287-294
    • Tindall, S.H.1
  • 457
    • 0001522582 scopus 로고    scopus 로고
    • Electrophysiology of the in situ contractile vacuole complex of Paramecium reveals its membrane dynamics and electrogenic site during osmoregulatory activity
    • Tominaga, T., Allen, R.D., Naitoh, Y., 1998a. Electrophysiology of the in situ contractile vacuole complex of Paramecium reveals its membrane dynamics and electrogenic site during osmoregulatory activity. J. Exp. Biol. 201, 451-460.
    • (1998) J. Exp. Biol. , vol.201 , pp. 451-460
    • Tominaga, T.1    Allen, R.D.2    Naitoh, Y.3
  • 458
    • 0031734823 scopus 로고    scopus 로고
    • Cyclic changes in the tension of the contractile vacuole complex membrane control its exocytotic cycle
    • Tominaga, T., Allen, R.D., Naitoh, Y., 1998b. Cyclic changes in the tension of the contractile vacuole complex membrane control its exocytotic cycle. J. Exp. Biol. 201, 2647-2658.
    • (1998) J. Exp. Biol. , vol.201 , pp. 2647-2658
    • Tominaga, T.1    Allen, R.D.2    Naitoh, Y.3
  • 460
    • 0038532315 scopus 로고    scopus 로고
    • Identification of targets for calcium signaling through the copine family of proteins
    • Tomsig, J.L., Snyder, S.L., Creutz, C.E., 2003. Identification of targets for calcium signaling through the copine family of proteins. J. Biol. Chem. 278, 10048-10054.
    • (2003) J. Biol. Chem. , vol.278 , pp. 10048-10054
    • Tomsig, J.L.1    Snyder, S.L.2    Creutz, C.E.3
  • 461
    • 1942520207 scopus 로고    scopus 로고
    • 2+ -regulated membrane fusion by synaptotagmin and SNAREs
    • 2+ -regulated membrane fusion by synaptotagmin and SNAREs. Science 304, 435-438.
    • (2004) Science , vol.304 , pp. 435-438
    • Tucker, W.C.1    Weber, T.2    Chapman, E.R.3
  • 462
    • 1042268889 scopus 로고    scopus 로고
    • Out with a bang! Tetrahymena as a model system to study secretory granule biogenesis
    • Turkewitz, A.P., 2004. Out with a bang! Tetrahymena as a model system to study secretory granule biogenesis. Traffic 5, 63-68.
    • (2004) Traffic , vol.5 , pp. 63-68
    • Turkewitz, A.P.1
  • 463
    • 0025815320 scopus 로고
    • Maturation of dense core granules in wild type and mutant Tetrahymena thermophila
    • Turkewitz, A.P., Madeddu, L., Kelly, R.B., 1991. Maturation of dense core granules in wild type and mutant Tetrahymena thermophila. EMBO J. 10, 1979-1987.
    • (1991) EMBO J , vol.10 , pp. 1979-1987
    • Turkewitz, A.P.1    Madeddu, L.2    Kelly, R.B.3
  • 465
    • 0036138203 scopus 로고    scopus 로고
    • Functional genomics: the coming of age for Tetrahymena thermophila
    • Turkewitz, A.P., Orias, E., Kapler, G., 2002. Functional genomics: the coming of age for Tetrahymena thermophila. Trends Genet. 18, 35-40.
    • (2002) Trends Genet , vol.18 , pp. 35-40
    • Turkewitz, A.P.1    Orias, E.2    Kapler, G.3
  • 466
    • 19444384136 scopus 로고    scopus 로고
    • The longin domain regulates subcellular targeting of VAMP7 in Arabidopsis thaliana
    • Uemura, T., Sato, M.H., Takeyasu, K., 2005. The longin domain regulates subcellular targeting of VAMP7 in Arabidopsis thaliana. FEBS Lett. 579, 2842-2846.
    • (2005) FEBS Lett , vol.579 , pp. 2842-2846
    • Uemura, T.1    Sato, M.H.2    Takeyasu, K.3
  • 467
    • 0029850677 scopus 로고    scopus 로고
    • Rab11 regulates recycling through the pericentriolar recycling endosome
    • Ullrich, O., Reinsch, S., Urbé, S., Zerial, M., Parton, R.G., 1996. Rab11 regulates recycling through the pericentriolar recycling endosome. J. Cell Biol. 135, 913-924.
    • (1996) J. Cell Biol. , vol.135 , pp. 913-924
    • Ullrich, O.1    Reinsch, S.2    Urbé, S.3    Zerial, M.4    Parton, R.G.5
  • 468
    • 26244457213 scopus 로고    scopus 로고
    • Functions of SNAREs in intracellular membrane fusion and lipid bilayer mixing
    • Ungermann, C., Langosch, D., 2005. Functions of SNAREs in intracellular membrane fusion and lipid bilayer mixing. J. Cell Sci. 118, 3819-3828.
    • (2005) J. Cell Sci. , vol.118 , pp. 3819-3828
    • Ungermann, C.1    Langosch, D.2
  • 469
    • 0032576576 scopus 로고    scopus 로고
    • Homotypic fusion of immature secretory granules during maturation in a cell-free assay
    • Urbé, S., Page, L.J., Tooze, S.A., 1998. Homotypic fusion of immature secretory granules during maturation in a cell-free assay. J. Cell Biol. 143, 1831-1844.
    • (1998) J. Cell Biol. , vol.143 , pp. 1831-1844
    • Urbé, S.1    Page, L.J.2    Tooze, S.A.3
  • 470
    • 0842333851 scopus 로고    scopus 로고
    • Dynein: an ancient motor protein involved in multiple modes of transport
    • Vallee, R.B., Williams, J.C., Varma, D., Barnhart, L.E., 2004. Dynein: an ancient motor protein involved in multiple modes of transport. J. Neurobiol. 58, 189-200.
    • (2004) J. Neurobiol. , vol.58 , pp. 189-200
    • Vallee, R.B.1    Williams, J.C.2    Varma, D.3    Barnhart, L.E.4
  • 471
    • 0346492581 scopus 로고    scopus 로고
    • i-SNAREs: inhibitory SNAREs that fine-tune the specificity of membrane fusion
    • Varlamov, O., Volchuk, A., Rahimian, V., Doege, C.A., Paumet, F., Eng, W.S., et al., 2004. i-SNAREs: inhibitory SNAREs that fine-tune the specificity of membrane fusion. J. Cell Biol. 164, 79-88.
    • (2004) J. Cell Biol. , vol.164 , pp. 79-88
    • Varlamov, O.1    Volchuk, A.2    Rahimian, V.3    Doege, C.A.4    Paumet, F.5    Eng, W.S.6
  • 472
    • 0034122147 scopus 로고    scopus 로고
    • Molecular genetics of regulated secretion in Paramecium
    • Vayssié, L., Skouri, F., Sperling, L., Cohen, J., 2000. Molecular genetics of regulated secretion in Paramecium. Biochimie 82, 269-288.
    • (2000) Biochimie , vol.82 , pp. 269-288
    • Vayssié, L.1    Skouri, F.2    Sperling, L.3    Cohen, J.4
  • 473
    • 0035065377 scopus 로고    scopus 로고
    • Growth and form of secretory granules involves stepwise assembly but not differential sorting of a family of secretory proteins in Paramecium
    • Vayssié, L., Garreau De Loubresse, N., Sperling, L., 2001. Growth and form of secretory granules involves stepwise assembly but not differential sorting of a family of secretory proteins in Paramecium. J. Cell Sci. 114, 875-886.
    • (2001) J. Cell Sci. , vol.114 , pp. 875-886
    • Vayssié, L.1    Garreau De Loubresse, N.2    Sperling, L.3
  • 474
    • 18244432240 scopus 로고    scopus 로고
    • Multiple palmitoylation of synaptotagmin and the t-SNARE SNAP-25
    • Veit, M., Söllner, T.H., Rothman, J.E., 1996. Multiple palmitoylation of synaptotagmin and the t-SNARE SNAP-25. FEBS Lett. 385, 119-123.
    • (1996) FEBS Lett , vol.385 , pp. 119-123
    • Veit, M.1    Söllner, T.H.2    Rothman, J.E.3
  • 475
    • 0031594225 scopus 로고    scopus 로고
    • 2+-binding activity of dense-core vesicle polypeptides in Tetrahymena
    • 2+-binding activity of dense-core vesicle polypeptides in Tetrahymena. Mol. Biol. Cell 9, 497-511.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 497-511
    • Verbsky, J.W.1    Turkewitz, A.P.2
  • 476
    • 0018784027 scopus 로고
    • Fusion of phospholipid vesicles in association with the appearance of lipidic particles as visualized by freeze-fracturing
    • Verkleij, A.J., Mombers, C., Gerritsen, W.J., Leunissen-Bijvelt, L., Cullis, P.R., 1979. Fusion of phospholipid vesicles in association with the appearance of lipidic particles as visualized by freeze-fracturing. Biochim. Biophys. Acta 555, 358-361.
    • (1979) Biochim. Biophys. Acta , vol.555 , pp. 358-361
    • Verkleij, A.J.1    Mombers, C.2    Gerritsen, W.J.3    Leunissen-Bijvelt, L.4    Cullis, P.R.5
  • 477
    • 0020513776 scopus 로고
    • Membrane-integrated proteins at preformed exocytosis sites
    • Vilmart, J., Plattner, H., 1983. Membrane-integrated proteins at preformed exocytosis sites. J. Histochem. Cytochem. 31, 626-632.
    • (1983) J. Histochem. Cytochem. , vol.31 , pp. 626-632
    • Vilmart, J.1    Plattner, H.2
  • 478
    • 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
  • 479
    • 54049128127 scopus 로고    scopus 로고
    • The exocytosis regulator synaptotagmin V controls phagocytosis in macrophages
    • Vinet, A.F., 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
  • 480
    • 0037078319 scopus 로고    scopus 로고
    • Calcium-regulated exocytosis of dense-core vesicles requires the activation of ADP-ribosylation factor (ARF)6 by ARF nucleotide binding site opener at the plasma membrane
    • Vitale, N., ChasserotGolaz, S., Bailly, Y., Morinaga, N., Frohman, M.A., Bader, M.F., 2002. Calcium-regulated exocytosis of dense-core vesicles requires the activation of ADP-ribosylation factor (ARF)6 by ARF nucleotide binding site opener at the plasma membrane. J. Cell Biol. 159, 79-89.
    • (2002) J. Cell Biol. , vol.159 , pp. 79-89
    • Vitale, N.1    ChasserotGolaz, S.2    Bailly, Y.3    Morinaga, N.4    Frohman, M.A.5    Bader, M.F.6
  • 481
    • 51249118719 scopus 로고    scopus 로고
    • Heterotypic tubular connections at the endoplasmic reticulum-Golgi complex interface
    • Vivero-Salmerón, G., Ballesta, J., Martínez-Menárguez, J.A., 2008. Heterotypic tubular connections at the endoplasmic reticulum-Golgi complex interface. Histochem. Cell Biol. 130, 709-717.
    • (2008) Histochem. Cell Biol. , vol.130 , pp. 709-717
    • Vivero-Salmerón, G.1    Ballesta, J.2    Martínez-Menárguez, J.A.3
  • 482
    • 0033622509 scopus 로고    scopus 로고
    • 2+ -dependent steps leading to secretion in chromaffin cells from mouse adrenal slices
    • 2+ -dependent steps leading to secretion in chromaffin cells from mouse adrenal slices. Neuron 28, 537-545.
    • (2000) Neuron , vol.28 , pp. 537-545
    • Voets, T.1
  • 483
    • 84987576613 scopus 로고
    • Magnetic separation of phagosomes of defined age from Tetrahymena thermophila
    • Vosskühler, C., Tiedtke, A., 1993. Magnetic separation of phagosomes of defined age from Tetrahymena thermophila. J. Eukaryot. Microbiol. 40, 556-562.
    • (1993) J. Eukaryot. Microbiol. , vol.40 , pp. 556-562
    • Vosskühler, C.1    Tiedtke, A.2
  • 484
    • 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
  • 485
    • 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
  • 486
  • 487
    • 0001792655 scopus 로고    scopus 로고
    • Genetic characterization of the secretory mutants in Paramecium caudatum
    • Watanabe, T., Haga, N., 1996. Genetic characterization of the secretory mutants in Paramecium caudatum. Protoplasma 192, 11-19.
    • (1996) Protoplasma , vol.192 , pp. 11-19
    • Watanabe, T.1    Haga, N.2
  • 488
    • 0033963378 scopus 로고    scopus 로고
    • Functional cooperation of two independent targeting domains in syntaxin 6 is required for its efficient localization in the trans-Golgi network of 3T3L1 adipocytes
    • Watson, R.T., Pessin, J.E., 2000. Functional cooperation of two independent targeting domains in syntaxin 6 is required for its efficient localization in the trans-Golgi network of 3T3L1 adipocytes. J. Biol. Chem. 275, 1261-1268.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1261-1268
    • Watson, R.T.1    Pessin, J.E.2
  • 489
    • 0034805876 scopus 로고    scopus 로고
    • Transmembrane domain length determines intracellular membrane compartment localization of syntaxins 3, 4, and 5
    • Watson, R.T., Pessin, J.E., 2001. Transmembrane domain length determines intracellular membrane compartment localization of syntaxins 3, 4, and 5. Am. J. Physiol. Cell Physiol. 281, C215-C223.
    • (2001) Am. J. Physiol. Cell Physiol. , vol.281
    • Watson, R.T.1    Pessin, J.E.2
  • 490
    • 0034839484 scopus 로고    scopus 로고
    • Syntaxin 6 the promiscuous behaviour of a SNARE protein
    • Wendler, F., Tooze, S., 2001. Syntaxin 6: the promiscuous behaviour of a SNARE protein. Traffic 2, 606-611.
    • (2001) Traffic , vol.2 , pp. 606-611
    • Wendler, F.1    Tooze, S.2
  • 491
    • 38949211822 scopus 로고    scopus 로고
    • Accessory proteins stabilize the acceptor complex for synaptobrevin, the 1:1 syntaxin/SNAP-25 complex
    • Weninger, K., Bowen, M., Choi, U.B., Chu, S., Brunger, A.T., 2008. Accessory proteins stabilize the acceptor complex for synaptobrevin, the 1:1 syntaxin/SNAP-25 complex. Structure 16, 308-320.
    • (2008) Structure , vol.16 , pp. 308-320
    • Weninger, K.1    Bowen, M.2    Choi, U.B.3    Chu, S.4    Brunger, A.T.5
  • 492
    • 0345169048 scopus 로고    scopus 로고
    • Post-translational modifications regulate microtubule function
    • Westermann, S., Weber, K., 2003. Post-translational modifications regulate microtubule function. Nat. Rev. Mol. Cell Biol. 4, 938-947.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 938-947
    • Westermann, S.1    Weber, K.2
  • 493
    • 0035003581 scopus 로고    scopus 로고
    • N-Ethylmaleimide sensitive factor (NSF) structure and function
    • Whiteheart, S.W., Schraw, T., Matveeva, E.A., 2001. N-Ethylmaleimide sensitive factor (NSF) structure and function. Int. Rev. Cytol. 207, 71-112.
    • (2001) Int. Rev. Cytol. , vol.207 , pp. 71-112
    • Whiteheart, S.W.1    Schraw, T.2    Matveeva, E.A.3
  • 494
    • 9244252581 scopus 로고    scopus 로고
    • Dynamin and clathrin-dependent endocytic pathway in unicellular eukaryote Paramecium
    • Wiejak, J., Surmacz, L., Wyroba, E., 2004. Dynamin and clathrin-dependent endocytic pathway in unicellular eukaryote Paramecium. Biochem. Cell Biol. 82, 547-558.
    • (2004) Biochem. Cell Biol. , vol.82 , pp. 547-558
    • Wiejak, J.1    Surmacz, L.2    Wyroba, E.3
  • 495
    • 41449086954 scopus 로고    scopus 로고
    • Twenty-five dyneins in Tetrahymena: a re-examination of the multidynein hypothesis
    • Wilkes, D.E., Watson, H.E., Mitchell, D.R., Asai, D.J., 2008. Twenty-five dyneins in Tetrahymena: a re-examination of the multidynein hypothesis. Cell Motil. Cytoskeleton 65, 342-351.
    • (2008) Cell Motil. Cytoskeleton , vol.65 , pp. 342-351
    • Wilkes, D.E.1    Watson, H.E.2    Mitchell, D.R.3    Asai, D.J.4
  • 496
    • 33645076501 scopus 로고    scopus 로고
    • The actin gene ACT1 is required for phagocytosis, motility, and cell separation of Tetrahymena thermophila
    • Williams, N.E., Tsao, C.-C., Bowen, J., Hehman, G.L., Williams, R.J., Frankel, J., 2006. The actin gene ACT1 is required for phagocytosis, motility, and cell separation of Tetrahymena thermophila. Eukaryot. Cell 5, 555-567.
    • (2006) Eukaryot. Cell , vol.5 , pp. 555-567
    • Williams, N.E.1    Tsao, C.-C.2    Bowen, J.3    Hehman, G.L.4    Williams, R.J.5    Frankel, J.6
  • 497
    • 48949092559 scopus 로고    scopus 로고
    • Glutamylation on aα-tubulin is not essential but affects the assembly and functions of a subset of microtubules in Tetrahymena thermophila
    • Wloga, D., Rogowski, K., Sharma, N., Van Dijk, J., Janke, C., Eddé, B., et al., 2008. Glutamylation on aα-tubulin is not essential but affects the assembly and functions of a subset of microtubules in Tetrahymena thermophila. Eukaryot. Cell 7, 1362-1372.
    • (2008) Eukaryot. Cell , vol.7 , pp. 1362-1372
    • Wloga, D.1    Rogowski, K.2    Sharma, N.3    Van Dijk, J.4    Janke, C.5    Eddé, B.6
  • 498
    • 68149171755 scopus 로고    scopus 로고
    • 2+ and calmodulin initiate all forms of endocytosis during depolarization at a nerve terminal
    • 2+ and calmodulin initiate all forms of endocytosis during depolarization at a nerve terminal. Nat. Neurosci. 12, 1003-1010.
    • (2009) Nat. Neurosci. , vol.12 , pp. 1003-1010
    • Wu, X.-S.1    McNeil, B.D.2    Xu, J.3    Fan, J.4    Xue, L.5    Melicoff, E.6
  • 499
    • 34250857340 scopus 로고    scopus 로고
    • Regulation of membrane fusion in synaptic excitation-secretion coupling: speed and accuracy matter
    • Wojcik, S.M., Brose, N., 2007. Regulation of membrane fusion in synaptic excitation-secretion coupling: speed and accuracy matter. Neuron 55, 11-24.
    • (2007) Neuron , vol.55 , pp. 11-24
    • Wojcik, S.M.1    Brose, N.2
  • 500
    • 35748984673 scopus 로고    scopus 로고
    • Phagosome maturation in unicellular eukaryote Paramecium: the presence of RILP Rab7 and Lamp-2
    • Wyroba, E., Surmacz, L., Osinska, M., Wiejak, J., 2007. Phagosome maturation in unicellular eukaryote Paramecium: the presence of RILP, Rab7 and Lamp-2. Eur. J. Histochem. 51, 163-172.
    • (2007) Eur. J. Histochem. , vol.51 , pp. 163-172
    • Wyroba, E.1    Surmacz, L.2    Osinska, M.3    Wiejak, J.4
  • 501
    • 0033564814 scopus 로고    scopus 로고
    • Early requirement for a-SNAP and NSF in the secretory cascade in chromaffin cells
    • Xu, T., Ashery, U., Burgoyne, R.D., Neher, E., 1999. Early requirement for a-SNAP and NSF in the secretory cascade in chromaffin cells. EMBO J. 18, 3293-3304.
    • (1999) EMBO J , vol.18 , pp. 3293-3304
    • Xu, T.1    Ashery, U.2    Burgoyne, R.D.3    Neher, E.4
  • 502
    • 9444242125 scopus 로고    scopus 로고
    • Repeated cycles of rapid actin assembly and disassembly on epithelia cell phagosomes
    • Yam, P.T., Thériot, J.A., 2004. Repeated cycles of rapid actin assembly and disassembly on epithelia cell phagosomes. Mol. Biol. Cell 15, 5647-5658.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5647-5658
    • Yam, P.T.1    Thériot, J.A.2
  • 503
    • 33744949741 scopus 로고    scopus 로고
    • Domain requirement for the membrane trafficking and targeting of syntaxin 1A
    • Yang, X., Xu, P., Xiao, Y., Xiong, X., Xu, T., 2006. Domain requirement for the membrane trafficking and targeting of syntaxin 1A. J. Biol. Chem. 281, 15457-15463.
    • (2006) J. Biol. Chem. , vol.281 , pp. 15457-15463
    • Yang, X.1    Xu, P.2    Xiao, Y.3    Xiong, X.4    Xu, T.5
  • 504
    • 0035969243 scopus 로고    scopus 로고
    • Sec6/8 complexes on trans-Golgi network and plasma membrane regulate late stages of exocytosis in mammalian cells
    • Yeaman, C., Grindstaff, K.K., Wright, J.R., Nelson, W.J., 2001. Sec6/8 complexes on trans-Golgi network and plasma membrane regulate late stages of exocytosis in mammalian cells. J. Cell Biol. 155, 593-604.
    • (2001) J. Cell Biol. , vol.155 , pp. 593-604
    • Yeaman, C.1    Grindstaff, K.K.2    Wright, J.R.3    Nelson, W.J.4
  • 505
    • 33745761913 scopus 로고    scopus 로고
    • Extracting sequence motifs and the phylogenetic features of SNARE-dependent membrane traffic
    • Yoshizawa, A.C., Kawashima, S., Okuda, S., Fujita, M., Itoh, M., Moriya, Y., et al., 2006. Extracting sequence motifs and the phylogenetic features of SNARE-dependent membrane traffic. Traffic 7, 1104-1118.
    • (2006) Traffic , vol.7 , pp. 1104-1118
    • Yoshizawa, A.C.1    Kawashima, S.2    Okuda, S.3    Fujita, M.4    Itoh, M.5    Moriya, Y.6
  • 506
    • 0031926942 scopus 로고    scopus 로고
    • Relative potencies of different cytochalasins for the inhibition of phagocytosis in ciliates
    • Zackroff, R.V., Hufnagel, L.A., 1998. Relative potencies of different cytochalasins for the inhibition of phagocytosis in ciliates. J. Eukaryot. Microbiol. 45, 397-403.
    • (1998) J. Eukaryot. Microbiol. , vol.45 , pp. 397-403
    • Zackroff, R.V.1    Hufnagel, L.A.2
  • 507
    • 4143067041 scopus 로고    scopus 로고
    • High coding density on the largest Paramecium tetraurelia somatic chromosome
    • Zagulski, M., Nowak, J.K., LeMouel, A., Nowacki, M., Migdalski, A., Gromadka, R., 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    LeMouel, A.3    Nowacki, M.4    Migdalski, A.5    Gromadka, R.6
  • 510
    • 34547859121 scopus 로고    scopus 로고
    • The role for HNF-1β-targeted collectrin in maintenance of primary cilia and cell polarity in collecting duct cells
    • e414. doi:10.1371/journal.pone.0000414
    • Zhang, Y., Wada, J., Yasuhara, A., Iseda, I., Eguchi, J., Fukui, K., et al., 2007. The role for HNF-1β-targeted collectrin in maintenance of primary cilia and cell polarity in collecting duct cells. PLoS One 5, e414. doi:10.1371/journal.pone.0000414, pp. 1-15.
    • (2007) PLoS One , vol.5 , pp. 1-15
    • Zhang, Y.1    Wada, J.2    Yasuhara, A.3    Iseda, I.4    Eguchi, J.5    Fukui, K.6
  • 511
    • 69949175597 scopus 로고    scopus 로고
    • A link between ER tethering and COP-I vesicle uncoating
    • Zink, S., Wenzel, D., Wurm, C.A., Schmitt, H.D., 2009. A link between ER tethering and COP-I vesicle uncoating. Dev. Cell 17, 403-416.
    • (2009) Dev. Cell , vol.17 , pp. 403-416
    • Zink, S.1    Wenzel, D.2    Wurm, C.A.3    Schmitt, H.D.4
  • 512
    • 33748136805 scopus 로고    scopus 로고
    • Genome architecture drives protein evolution in ciliates
    • Zufall, R.A., McGrath, C.L., Muse, S.V., Katz, L.A., 2006. Genome architecture drives protein evolution in ciliates. Mol. Biol. Evol. 23, 1681-1687.
    • (2006) Mol. Biol. Evol. , vol.23 , pp. 1681-1687
    • Zufall, R.A.1    McGrath, C.L.2    Muse, S.V.3    Katz, L.A.4
  • 514
    • 66249115336 scopus 로고    scopus 로고
    • The exocyst protein Sec 10 is necessary for primary ciliogenesis and cytogenesis in vitro
    • Zuo, X., Guo, W., Lipschutz, J.H., 2009. The exocyst protein Sec 10 is necessary for primary ciliogenesis and cytogenesis in vitro. Mol. Biol. Cell 20, 2522-2529.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 2522-2529
    • Zuo, X.1    Guo, W.2    Lipschutz, J.H.3
  • 515
    • 66749102168 scopus 로고    scopus 로고
    • Nested genes CDA12 and CDA13 encode proteins associated with membrane trafficking in the ciliate Tetrahymena thermophila
    • Zweifel, E., Smith, J., Romero, D., Giddings, T.H., Winey, M., Honts, J., et al., 2009. Nested genes CDA12 and CDA13 encode proteins associated with membrane trafficking in the ciliate Tetrahymena thermophila. Eukaryot. Cell 8, 899-912.
    • (2009) Eukaryot. Cell , vol.8 , pp. 899-912
    • Zweifel, E.1    Smith, J.2    Romero, D.3    Giddings, T.H.4    Winey, M.5    Honts, J.6


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