메뉴 건너뛰기




Volumn 232, Issue , 2003, Pages 185-216

Molecular Aspects of Membrane Trafficking in Paramecium

Author keywords

Ciliates; Membrane fusion; Membrane traffic; Membranes; Paramecium

Indexed keywords

ADAPTOR PROTEIN; ADENOSINE TRIPHOSPHATASE; CALCINEURIN; CALMODULIN; CLATHRIN HEAVY CHAIN; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANINE NUCLEOTIDE EXCHANGE FACTOR; SNARE PROTEIN;

EID: 0346256847     PISSN: 00747696     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0074-7696(03)32005-4     Document Type: Article
Times cited : (32)

References (180)
  • 1
    • 0002061701 scopus 로고
    • Exocytosis: Biogenesis, transport and secretion of trichocysts
    • (H. D. Görtz, Ed.) Springer-Verlag, Berlin
    • Adoutte, A. (1988). Exocytosis: Biogenesis, transport and secretion of trichocysts. In "Paramecium" (H. D. Görtz, Ed.), pp. 325-362. Springer-Verlag, Berlin.
    • (1988) Paramecium , pp. 325-362
    • Adoutte, A.1
  • 2
    • 0033777003 scopus 로고    scopus 로고
    • The contractile vacuole and its membrane dynamics
    • Allen, R. D. (2000). The contractile vacuole and its membrane dynamics. BioEssays 22, 1035-1042.
    • (2000) BioEssays , vol.22 , pp. 1035-1042
    • Allen, R.D.1
  • 3
    • 0002351563 scopus 로고
    • Cytology
    • (H. D. Görtz, Ed.) Springer-Verlag, Berlin
    • Allen, R. D. (1988). Cytology. In "Paramecium" (H. D. Görtz, Ed.), pp. 4-40. Springer-Verlag, Berlin.
    • (1988) Paramecium , pp. 4-40
    • Allen, R.D.1
  • 4
    • 0019225464 scopus 로고
    • Membrane recycling and endocytosis in Paramecium confirmed by horseradish peroxidase pulse-chase studies
    • Allen, R. D., and 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
  • 5
    • 0020803834 scopus 로고
    • Nonlysosomal vesicles (acidosomes) are involved in phagosome acidification in Paramecium
    • Allen, R. D., and Fok, A. K. (1983). 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
  • 6
    • 0021123418 scopus 로고
    • Membrane behavior of exocytic vesicles. III. Flow of horseradish peroxidase labeled trichocyst membrane remnants in Paramecium
    • Allen, R. D., and Fok, A. K. (1984). 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
  • 7
    • 0000856763 scopus 로고
    • Endosomal membrane traffic of ciliates
    • (H. Plattner, Ed.) JAI Press, Greenwich, CT
    • Allen, R. D., and Fok, A. K. (1993a). Endosomal membrane traffic of ciliates. In "Membrane Traffic in Protozoa" (H. Plattner, Ed.), pp. 283-309. JAI Press, Greenwich, CT.
    • (1993) Membrane Traffic in Protozoa , pp. 283-309
    • Allen, R.D.1    Fok, A.K.2
  • 8
    • 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., and Fok, A. K. (1993b). 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
  • 9
    • 0034018279 scopus 로고    scopus 로고
    • Membrane trafficking and processing in Paramecium
    • Allen, R. D., and 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
  • 10
    • 0036204472 scopus 로고    scopus 로고
    • Osmoregulation and contractile vacuoles of protozoa
    • Allen, R. D., and 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
  • 11
    • 0016373673 scopus 로고
    • The cytoproct of Paramecium caudatum: Structure and function, microtubules, and fate of food vacuole membranes
    • Allen, R. D., and 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
  • 12
    • 0026528046 scopus 로고
    • Endosomal system of Paramecium: Coated pits to early endosomes
    • Allen, R. D., Schroeder, C. C., and 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
  • 13
    • 0024492941 scopus 로고
    • Intracellular binding of wheat germ agglutinin by Golgi complexes, phagosomes and lysososmes in Paramecium multimicronucleatum
    • Allen, R. D., Schroeder, C. C., and Fok, A. K. (1989). Intracellular binding of wheat germ agglutinin by Golgi complexes, phagosomes and lysososmes in Paramecium multimicronucleatum. J. Histochem. Cytochem. 37, 195-202.
    • (1989) J. Histochem. Cytochem. , vol.37 , pp. 195-202
    • Allen, R.D.1    Schroeder, C.C.2    Fok, A.K.3
  • 14
    • 0024065235 scopus 로고
    • A survey of lectin binding in Paramecium
    • Allen, R. D., Ueno, M. S., and 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
  • 15
    • 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
  • 16
    • 0033067958 scopus 로고    scopus 로고
    • Reconstitution of regulated exocytosis in cell-free systems: A critical appraisal
    • Avery, J., Jahn, R., and Edwardson, J. M. (1999). Reconstitution of regulated exocytosis in cell-free systems: A critical appraisal. Annu. Rev. Physiol. 61, 777-807.
    • (1999) Annu. Rev. Physiol. , vol.61 , pp. 777-807
    • Avery, J.1    Jahn, R.2    Edwardson, J.M.3
  • 17
    • 0032526224 scopus 로고    scopus 로고
    • Sorting and storage during secretory granule biogenesis: Looking backward and looking forward
    • Avran, P., and Castle, D. (1998). Sorting and storage during secretory granule biogenesis: Looking backward and looking forward. Biochem. J. 332, 593-610.
    • (1998) Biochem. J. , vol.332 , pp. 593-610
    • Avran, P.1    Castle, D.2
  • 18
    • 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., and 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
  • 19
    • 0027636429 scopus 로고
    • Processing and secretion of lysosomal acid α-glucosidase in Tetrahymena wild type and secretion-deficient mutant cells
    • Banno, Y., Okano, Y., Furukawa, K., Tiedtke, A., Kobata, A., and Nozawa, Y. (1993). Processing and secretion of lysosomal acid α-glucosidase in Tetrahymena wild type and secretion-deficient 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
  • 22
    • 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., and 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
  • 23
    • 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., and 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
  • 24
    • 0033030282 scopus 로고    scopus 로고
    • Transformation of Paramecium tetraurelia by electroporation or particle bombardement
    • Boileau, A. J., Kissmehl, R., Kanabrocki, J. A., and Saimi, Y. (1999). Transformation of Paramecium tetraurelia by electroporation or particle bombardement. J. Eukaryot. Microbiol. 46, 56-65.
    • (1999) J. Eukaryot. Microbiol. , vol.46 , pp. 56-65
    • Boileau, A.J.1    Kissmehl, R.2    Kanabrocki, J.A.3    Saimi, Y.4
  • 25
    • 0035692148 scopus 로고    scopus 로고
    • Analysis of a mutant exhibiting conditional sorting to dense core secretory granules in Tetrahymena thermophila
    • Bowman, G. R., and 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
  • 26
    • 0027317940 scopus 로고
    • SCAMP 37, a new marker within the general cell surface recycling system
    • Brand, S. H., and Castle, J. C. (1993). SCAMP 37, a new marker within the general cell surface recycling system. EMBO J. 12, 3753-3761.
    • (1993) EMBO J. , vol.12 , pp. 3753-3761
    • Brand, S.H.1    Castle, J.C.2
  • 28
    • 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
  • 29
    • 0002786389 scopus 로고
    • Ciliary and plasma membrane proteins in Paramecium: Description, localization, and intracellular transit
    • (H. Plattner, Ed.) JAI Press, Greenwich, CT
    • Capdeville, Y., Charret, R., Antony, C., Delorme, J., Nahon, P., and Adoutte, A. (1993). Ciliary and plasma membrane proteins in Paramecium: Description, localization, and intracellular transit. In "Membrane Traffic in Protozoa" (H. Plattner, Ed.), pp. 181-226. JAI Press, Greenwich, CT.
    • (1993) Membrane Traffic in Protozoa , pp. 181-226
    • Capdeville, Y.1    Charret, R.2    Antony, C.3    Delorme, J.4    Nahon, P.5    Adoutte, A.6
  • 30
    • 0035826727 scopus 로고    scopus 로고
    • SNARE proteins are highly enriched in lipid rafts in PC12 cells: Implications for the spatial control of exocytosis
    • Chamberlain, L. H., Burgoyne, R. D., and Gould, G. W. (2001). SNARE proteins are highly enriched in lipid rafts in PC12 cells: Implications for the spatial control of exocytosis. Proc. Natl. Acad. Sci. USA 98, 5619-5624.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5619-5624
    • Chamberlain, L.H.1    Burgoyne, R.D.2    Gould, G.W.3
  • 31
    • 0030478918 scopus 로고    scopus 로고
    • Granule lattice protein 1 (Grllp), 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., and Turkewitz, A. P. (1996). Granule lattice protein 1 (Grllp), 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
  • 32
    • 0034306013 scopus 로고    scopus 로고
    • Function of Rho family proteins in actin dynamics during phagocytosis and engulfment
    • Chimini, G., and Chavrier, P. (2000). Function of Rho family proteins in actin dynamics during phagocytosis and engulfment. Nature Cell Biol. 2, E191-E196.
    • (2000) Nature Cell Biol. , vol.2
    • Chimini, G.1    Chavrier, P.2
  • 33
    • 0032374044 scopus 로고    scopus 로고
    • Molecular aspects of the endocytic pathway
    • Clague, M. J. (1998). Molecular aspects of the endocytic pathway. Biochem. J. 336, 271-282.
    • (1998) Biochem. J. , vol.336 , pp. 271-282
    • Clague, M.J.1
  • 34
    • 0000629911 scopus 로고
    • The cytoskeleton
    • (H. D. Görtz, Ed.) Springer-Verlag, Berlin
    • Cohen, J., and Beisson, J. (1988). The cytoskeleton. In "Paramecium" (H. D. Görtz, Ed.), pp. 363-392. Springer-Verlag, Berlin.
    • (1988) Paramecium , pp. 363-392
    • Cohen, J.1    Beisson, J.2
  • 35
    • 0037422066 scopus 로고    scopus 로고
    • Regulated protals of entry into the cell
    • Conner, S. D., and Schmid, S. L. (2003). Regulated protals of entry into the cell. Nature 422, 37-44.
    • (2003) Nature , vol.422 , pp. 37-44
    • Conner, S.D.1    Schmid, S.L.2
  • 36
    • 0033230605 scopus 로고    scopus 로고
    • Distruption of Rab3-calmodulin interaction, but not other effector interactions, prevents Rab3 inhibition of exocytosis
    • Coppola, T., Perret-Manoud, V., Lüthi, S., Farnsworth, C. C., Glomset, J. A., and Regazzi, R. (1999). Distruption of Rab3-calmodulin interaction, but not other effector interactions, prevents Rab3 inhibition of exocytosis. EMBO J. 18, 5885-5891.
    • (1999) EMBO J. , vol.18 , pp. 5885-5891
    • Coppola, T.1    Perret-Manoud, V.2    Lüthi, S.3    Farnsworth, C.C.4    Glomset, J.A.5    Regazzi, R.6
  • 39
  • 41
    • 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
  • 42
    • 0032820595 scopus 로고    scopus 로고
    • The structure, biosynthesis and functions of glycosylphosphatidylinositol anchors, and the contributions of trypanosome research
    • Ferguson, M. A. J. (1999). The structure, biosynthesis and functions of glycosylphosphatidylinositol anchors, and the contributions of trypanosome research. J. Cell Sci. 112, 2799-2809.
    • (1999) J. Cell Sci. , vol.112 , pp. 2799-2809
    • Ferguson, M.A.J.1
  • 44
    • 0344428151 scopus 로고    scopus 로고
    • Immunolabeling analysis of biosynthetic and degradative pathways of cell surface components (glycocalyx) in Paramecium cells
    • Flötenmeyer, M., Momayezi, M., and Plattner, H. (1999). Immunolabeling analysis of biosynthetic and degradative pathways of cell surface components (glycocalyx) in Paramecium cells. Eur. J. Cell Biol 78, 67-77.
    • (1999) Eur. J. Cell Biol. , vol.78 , pp. 67-77
    • Flötenmeyer, M.1    Momayezi, M.2    Plattner, H.3
  • 45
    • 0000657252 scopus 로고
    • Membrane flow in the digestive cycle of Paramecium
    • (H. Plattner, Ed.) JAI Press, Greenwich, CT
    • Fok, A. K., and Allen, R. D. (1993). Membrane flow in the digestive cycle of Paramecium. In "Membrane Traffic in Protozoa" (H. Plattner, Ed.), pp. 311-337. JAI Press, Greenwich, CT.
    • (1993) Membrane Traffic in Protozoa , pp. 311-337
    • Fok, A.K.1    Allen, R.D.2
  • 46
    • 0036063275 scopus 로고    scopus 로고
    • The vacuolar-ATPase of Paramecium multimicronucleatum 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., and Allen, R. D. (2002). The vacuolar-ATPase of Paramecium multimicronucleatum 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, R.D.6
  • 47
    • 0028133493 scopus 로고
    • The identification of a complex family of low-molecular weight GTP-binding protein homologues from Paramecium tetraurelia by PCR cloning
    • Fraga, D., and Hinrichsen, R. D. (1994). The identification of a complex family of low-molecular weight 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
  • 48
    • 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., and 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
  • 49
    • 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., and 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
  • 50
    • 0036137143 scopus 로고    scopus 로고
    • RNA interference by feeding in Paramecium
    • Galvani, A., and 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
  • 51
    • 0035504570 scopus 로고    scopus 로고
    • Transgene-mediated post-transcriptional gene silencing is inhibited by 3′ non-coding sequences in Paramecium
    • Galvani, A., and Sperling, L. (2001). Transgene-mediated post-transcriptional gene silencing is inhibited by 3′ non-coding sequences in Paramecium. Nucleic Ac. Res. 29, 4387-4394.
    • (2001) Nucleic Ac. Res. , vol.29 , pp. 4387-4394
    • Galvani, A.1    Sperling, L.2
  • 53
    • 0002172130 scopus 로고
    • Early steps of the secretory pathway in Paramecium: Ultrastructural immunocytochemical and genetic analysis of trichocyst biogenesis
    • (H. Plattner, Ed.) JAI Press, Greenwich, CT
    • Garreau De Loubresse, N. (1993). Early steps of the secretory pathway in Paramecium: Ultrastructural immunocytochemical and genetic analysis of trichocyst biogenesis. In "Membrane Traffic in Protozoa" (H. Plattner, Ed.), pp. 27-59. JAI Press, Greenwich, CT.
    • (1993) Membrane Traffic in Protozoa , pp. 27-59
    • Garreau De Loubresse, N.1
  • 54
    • 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., and 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
  • 55
    • 0029971334 scopus 로고    scopus 로고
    • Cloning and sequence analysis of genes coding for Paramecium secretory granule (trichocyst) proteins: A unique protein fold for a family of polypeptides with different primary structures
    • Gautier, M. C., Sperling, L., and Madeddu, L. (1996). Cloning and sequence analysis of genes coding for Paramecium secretory granule (trichocyst) proteins: A unique protein fold for a family of polypeptides with different primary structures. J. Biol. Chem. 271, 10247-10255.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10247-10255
    • Gautier, M.C.1    Sperling, L.2    Madeddu, L.3
  • 56
    • 0033065245 scopus 로고    scopus 로고
    • SNAREs and SNARE regulators in membrane fusion and exocytosis
    • Gerst, J. E. (1999). SNAREs and SNARE regulators in membrane fusion and exocytosis. Cell. Mol. Life Sci. 55, 707-734.
    • (1999) Cell. Mol. Life Sci. , vol.55 , pp. 707-734
    • Gerst, J.E.1
  • 57
    • 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., and 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
  • 58
    • 84986426160 scopus 로고
    • Secretory proteins and glycoproteins from Paramecium cells
    • Glas-Albrecht, R., Németh, A., and 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    Németh, A.2    Plattner, H.3
  • 59
    • 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
  • 60
    • 0003948743 scopus 로고
    • Springer-Verlag, Berlin
    • Görtz, H. D. (1988). "Paramecium." Springer-Verlag, Berlin.
    • (1988) Paramecium
    • Görtz, H.D.1
  • 61
    • 0037237001 scopus 로고    scopus 로고
    • Synaptotagmin III is a critical factor for the formation of the perinuclear endocytic recycling compartment and determination of secretory granule size
    • Grimberg, E., Peng, Z., Hammel, I., and Sagi-Eisenberg, R. (2003). Synaptotagmin III is a critical factor for the formation of the perinuclear endocytic recycling compartment and determination of secretory granule size. J. Cell Sci. 116, 145-154.
    • (2003) J. Cell Sci. , vol.116 , pp. 145-154
    • Grimberg, E.1    Peng, Z.2    Hammel, I.3    Sagi-Eisenberg, R.4
  • 63
    • 0007587167 scopus 로고
    • Secretory lectins contained in trichocyst tips of Paramecium
    • Haacke-Bell, B., and 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
  • 64
    • 0034056289 scopus 로고    scopus 로고
    • Expression of the green fluorescent protein in Paramecium tetraurelia
    • Hauser, K., Haynes, W. J., Kung, C., Plattner, H., and Kissmehl, R. (2000). 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
  • 65
    • 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
  • 66
    • 0030307633 scopus 로고    scopus 로고
    • Toward cloning genes by complementation in Paramecium
    • Haynes, W. J., Ling, K. Y., Saimi, Y., and Kung, C. (1996). Toward cloning genes 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
  • 67
    • 0037351330 scopus 로고    scopus 로고
    • Changing directions: Clathrin-mediated transport between the Golgi and endosomes
    • Hinners, I., and Tooze, S. A. (2003). Changing directions: Clathrin-mediated transport between the Golgi and endosomes. J. Cell Sci. 116, 763-771.
    • (2003) J. Cell Sci. , vol.116 , pp. 763-771
    • Hinners, I.1    Tooze, S.A.2
  • 68
    • 0034526495 scopus 로고    scopus 로고
    • Dynamin and its role in membrane fission
    • Hinshaw, J. E. (2000). Dynamin and its role in membrane fission. Annu. Rev. Cell Dev. Biol. 16, 483-519.
    • (2000) Annu. Rev. Cell Dev. Biol. , vol.16 , pp. 483-519
    • Hinshaw, J.E.1
  • 69
    • 0037168529 scopus 로고    scopus 로고
    • Imaging direct, dynamin-dependent recapture of fusing secretory granules on plasma membrane lawns from PC12 cells
    • Holroyd, P., Lang, T., Wenzel, D., DeCamilli, P., and Jahn, R. (2002). Imaging direct, dynamin-dependent recapture of fusing secretory granules on plasma membrane lawns from PC12 cells. Proc. Natl. Acad. Sci. USA 99, 16806-16811.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16806-16811
    • Holroyd, P.1    Lang, T.2    Wenzel, D.3    DeCamilli, P.4    Jahn, R.5
  • 72
    • 0032836484 scopus 로고    scopus 로고
    • Membrane fusion and exocytosis
    • Jahn, R., and Südhof, T. C. (1999). Membrane fusion and exocytosis. Annu. Rev. Biochem. 68, 863-911.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 863-911
    • Jahn, R.1    Südhof, T.C.2
  • 73
    • 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., and 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
  • 74
    • 0033957134 scopus 로고    scopus 로고
    • An indexed genomic library for Paramecium complementation cloning
    • Keller, A. M., and 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
  • 75
    • 0022402201 scopus 로고
    • Pathways of protein secretion in eukaryotes
    • Kelly, R. B. (1985). Pathways of protein secretion in eukaryotes. Science 230, 25-32.
    • (1985) Science , vol.230 , pp. 25-32
    • Kelly, R.B.1
  • 76
    • 0027184405 scopus 로고
    • Calmodulin is essential for assembling links necessary for exocytotic membrane fusion in Paramecium
    • Kerboeuf, D., Leberre, A., Dedieu, J. C., and Cohen, J. (1993). Calmodulin is essential for assembling links necessary for exocytotic membrane fusion in Paramecium. EMBO J. 12, 3385-3390.
    • (1993) EMBO J. , vol.12 , pp. 3385-3390
    • Kerboeuf, D.1    Leberre, A.2    Dedieu, J.C.3    Cohen, J.4
  • 77
    • 0022650710 scopus 로고
    • Filamentous actin in Paramecium cells: Mapping by phalloidin affinity labeling in vivo and in vitro
    • Kersken, H., Vilmart-Seuwen, J., Momayezi, M., and Plattner, H. (1986). Filamentous actin in Paramecium cells: Mapping by phalloidin affinity labeling in vivo and in vitro. J. Histochem. Cytochem. 34, 443-454.
    • (1986) J. Histochem. Cytochem. , vol.34 , pp. 443-454
    • Kersken, H.1    Vilmart-Seuwen, J.2    Momayezi, M.3    Plattner, H.4
  • 79
    • 0037107589 scopus 로고    scopus 로고
    • NSF regulates membrane traffic along multiple pathways in Paramecium
    • Kissmehl, R., Froissard, M., Plattner, H., Momayezi, M., and 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
  • 80
    • 0031571648 scopus 로고    scopus 로고
    • Occurrence of a paranitrophenyl phosphate-phosphatase with calcineurin-like characteristics in Paramecium tetraurelia
    • Kissmehl, R., Treptau, T., Kottwitz, B., and Plattner, H. (1997). Occurrence of a paranitrophenyl phosphate-phosphatase with calcineurin-like characteristics in Paramecium tetraurelia. Arch. Biochem. Biophys. 344, 260-270.
    • (1997) Arch. Biochem. Biophys. , vol.344 , pp. 260-270
    • Kissmehl, R.1    Treptau, T.2    Kottwitz, B.3    Plattner, H.4
  • 81
    • 0027336746 scopus 로고
    • Three pools of lysosomal enzymes in Tetrahymena thermophila
    • Kiy, T., Vosskühler, C., Rasmussen, L., and Tiedtke, A. (1993). Three pools of lysosomal enzymes in Tetrahymena thermophila. Exp. Cell Res. 205, 286-292.
    • (1993) Exp. Cell Res. , vol.205 , pp. 286-292
    • Kiy, T.1    Vosskühler, C.2    Rasmussen, L.3    Tiedtke, A.4
  • 82
    • 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., and 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
  • 83
    • 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., and 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
  • 84
    • 0032577483 scopus 로고    scopus 로고
    • Regulation of the calmodulin-stimulated protein phosphatase, calcineurin
    • Klee, C. B., Ren, H., and Wang, X. (1998). Regulation of the calmodulin-stimulated protein phosphatase, calcineurin. J. Biol. Chem. 273, 13367-13370.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13367-13370
    • Klee, C.B.1    Ren, H.2    Wang, X.3
  • 86
    • 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., and Plattner, H. (1991). Quenched flow analysis of exocytosis in Paramecium cells: Time course, changes in membrane structure, and calcium requirements revealed after rapid mixing and rapid freezing of intact cells. J. Cell Biol. 113, 1295-1304.
    • (1991) J. Cell Biol. , vol.113 , pp. 1295-1304
    • Knoll, G.1    Braun, C.2    Plattner, H.3
  • 88
    • 0027351866 scopus 로고
    • The Golgi apparatus of Tetrahymena thermophila
    • Kurz, S., and 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
  • 89
    • 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., and Jahn, R. (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    Jahn, R.7
  • 90
    • 0037119465 scopus 로고    scopus 로고
    • Localization of the lectin, ERp57, and polypeptide binding sites of calnexin and calreticulin
    • Leach, M. R., Cohen-Doyle, M. F., Thomas, D. Y., and Williams, D. B. (2002). Localization of the lectin, ERp57, and polypeptide binding sites of calnexin and calreticulin. J. Biol. Chem. 277, 29686-29697.
    • (2002) J. Biol. Chem. , vol.277 , pp. 29686-29697
    • Leach, M.R.1    Cohen-Doyle, M.F.2    Thomas, D.Y.3    Williams, D.B.4
  • 92
    • 0036906581 scopus 로고    scopus 로고
    • Role of secretory carrier membrane protein SCAMP2 in granule exocytosis
    • Liu, L., Guo, Z., Tieu, Q., Castle, A., and Castle, D. (2002). Role of secretory carrier membrane protein SCAMP2 in granule exocytosis. Mol. Biol. Cell 13, 4266-4278.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4266-4278
    • Liu, L.1    Guo, Z.2    Tieu, Q.3    Castle, A.4    Castle, D.5
  • 93
    • 0022965674 scopus 로고
    • Lectin binding sites in Paramecium tetraurelia cells. I. Labeling analysis predominantly of secretory components
    • Lüthe, N., Plattner, H., Haacke, B., Walther, W., and 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, N.1    Plattner, H.2    Haacke, B.3    Walther, W.4    Müller, M.5
  • 94
    • 0032899307 scopus 로고    scopus 로고
    • Biochemical analysis of membrane proteins from an early maturation stage of phagosomes
    • Maicher, M. T., and 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
  • 95
    • 0037164807 scopus 로고    scopus 로고
    • Concentrative sorting of secretory cargo proteins into COPII-coated vesicles
    • Malkus, P., Jiang, F., and Schekman, R. (2002). Concentrative sorting of secretory cargo proteins into COPII-coated vesicles. J. Cell Biol. 159, 915-921.
    • (2002) J. Cell Biol. , vol.159 , pp. 915-921
    • Malkus, P.1    Jiang, F.2    Schekman, R.3
  • 96
    • 0032543766 scopus 로고    scopus 로고
    • Calcium triggers calcineurin-dependent synaptic vesicle recycling in mammalian nerve terminals
    • Marks, B., and McMahon, H. T. (1998). Calcium triggers calcineurin-dependent synaptic vesicle recycling in mammalian nerve terminals. Curr. Biol. 8, 740-749.
    • (1998) Curr. Biol. , vol.8 , pp. 740-749
    • Marks, B.1    McMahon, H.T.2
  • 97
    • 0033538576 scopus 로고    scopus 로고
    • The structural era of endocytosis
    • Marsh, M., and McMahon, H. T. (1999). The structural era of endocytosis. Science 285, 215-220.
    • (1999) Science , vol.285 , pp. 215-220
    • Marsh, M.1    McMahon, H.T.2
  • 98
    • 0037187635 scopus 로고    scopus 로고
    • Prime movers of synaptic vesicle exocytosis
    • Martin, T. F. J. (2002). Prime movers of synaptic vesicle exocytosis. Neuron 34, 9-12.
    • (2002) Neuron , vol.34 , pp. 9-12
    • Martin, T.F.J.1
  • 99
    • 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
  • 100
    • 0035663883 scopus 로고    scopus 로고
    • What drives membrane fusion in eukaryotes?
    • Mayer, A. (2001). What drives membrane fusion in eukaryotes? Trends Biochem. Sci. 26, 717-723.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 717-723
    • Mayer, A.1
  • 102
    • 0031985394 scopus 로고    scopus 로고
    • Mutational analysis of regulated exocytosis in Tetrahymena
    • Melia, S. M., Cole, E. S., and 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
  • 103
    • 0036714223 scopus 로고    scopus 로고
    • Imaging actin and dynamin recruitment during invagination of single clathrin-coated pits
    • Merrifield, C. J., Feldman, M. E., Wan, L., and Almers, W. (2002). Imaging actin and dynamin recruitment during invagination of single clathrin-coated pits. Nature Cell Biol. 4, 691-698.
    • (2002) Nature Cell Biol. , vol.4 , pp. 691-698
    • Merrifield, C.J.1    Feldman, M.E.2    Wan, L.3    Almers, W.4
  • 104
    • 0031729619 scopus 로고    scopus 로고
    • Maturation of phagosomes is accompanied by specific patterns of small GTPases
    • Meyer, M., Mayer, T., and 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
  • 106
    • 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., and 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
  • 107
    • 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., and 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
  • 108
    • 0033852346 scopus 로고    scopus 로고
    • Quantitative immunogold localization of protein phosphatase 2B (calcineurin) in Paramecium cells
    • Momayezi, M., Kissmehl, R., and 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
  • 109
    • 0026022461 scopus 로고
    • Detection with monoclonal antibodies of a 15-kDa proteolipid in both presynaptic plasma membranes and synaptic vesicles in Torpedo electric organ
    • Morel, N., Synguelakis, M., and LeGal LaSalle, G. (1991). Detection with monoclonal antibodies of a 15-kDa proteolipid in both presynaptic plasma membranes and synaptic vesicles in Torpedo electric organ. J. Neurochem. 56, 1401-1408.
    • (1991) J. Neurochem. , vol.56 , pp. 1401-1408
    • Morel, N.1    Synguelakis, M.2    LeGal LaSalle, G.3
  • 111
    • 0036851186 scopus 로고    scopus 로고
    • Brefeldin A: Deciphering an enigmatic inhibitor of secretion
    • Nebenführ, A., Ritzenthaler, C., and Robinson, D. G. (2002). Brefeldin A: Deciphering an enigmatic inhibitor of secretion. Plant Physiol. 130, 1102-1108.
    • (2002) Plant Physiol. , vol.130 , pp. 1102-1108
    • Nebenführ, A.1    Ritzenthaler, C.2    Robinson, D.G.3
  • 112
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald, A. F., Aravind, L., Spouge, J. L., and Koonin, E. V. (1999). AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9, 27-43.
    • (1999) Genome Res. , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 113
    • 0030800703 scopus 로고    scopus 로고
    • Biogenesis of COPI-coated transport vesicles
    • Nickel, W., and Wieland, F. T. (1997). Biogenesis of COPI-coated transport vesicles. FEBS Lett. 413, 395-400.
    • (1997) FEBS Lett. , vol.413 , pp. 395-400
    • Nickel, W.1    Wieland, F.T.2
  • 114
    • 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., and 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
  • 115
    • 0020827145 scopus 로고
    • Coated pits and pinocytosis in Tetrahymena
    • Nilsson, J. R., and VanDeurs, B. (1983). Coated pits and pinocytosis in Tetrahymena. J. Cell Sci. 63, 209-222.
    • (1983) J. Cell Sci. , vol.63 , pp. 209-222
    • Nilsson, J.R.1    VanDeurs, B.2
  • 116
    • 0020855138 scopus 로고
    • Isolation and ultrastructural characterization of secretory mutants of Tetrahymena thermophila
    • Orias, E., Flacks, M., and 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
  • 117
    • 0031916766 scopus 로고    scopus 로고
    • Vesicle recycling revisited: Rapid endocytosis may be the first step
    • Palfrey, H. C., and Artalejo, C. R. (1998). Vesicle recycling revisited: Rapid endocytosis may be the first step. Neuroscience 83, 969-989.
    • (1998) Neuroscience , vol.83 , pp. 969-989
    • Palfrey, H.C.1    Artalejo, C.R.2
  • 118
    • 0021989409 scopus 로고
    • Synchronous exocytosis in Paramecium cells. V. Ultrastructural adaptation phenomena during re-insertion of secretory organelles
    • Pape, R., and Plattner, H. (1985). Synchronous exocytosis in Paramecium cells. V. Ultrastructural adaptation phenomena during re-insertion of secretory organelles. Eur. J. Cell Biol. 36, 38-47.
    • (1985) Eur. J. Cell Biol. , vol.36 , pp. 38-47
    • Pape, R.1    Plattner, H.2
  • 119
    • 0025610466 scopus 로고
    • Secretory organelle docking at the cell membrane of Paramecium cells: Dedocking and synchronized redocking of trichocysts
    • Pape, R., and Plattner, H. (1990). Secretory organelle docking at the cell membrane of 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
  • 120
    • 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., and Mayer, A. (2001). Transcomplex formation by proteolipid channels in the terminal phase of membrane fusion. Nature 409, 581-583.
    • (2001) Nature , vol.409 , pp. 581-583
    • Peters, C.1    Bayer, M.J.2    Bühler, S.3    Andersen, J.S.4    Mann, M.5    Mayer, A.6
  • 121
    • 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
  • 122
    • 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
  • 123
    • 0035996801 scopus 로고    scopus 로고
    • My favorite cell - Paramecium
    • Plattner, H. (2002). My favorite cell - Paramecium. BioEssays 24, 649-658.
    • (2002) BioEssays , vol.24 , pp. 649-658
    • Plattner, H.1
  • 125
    • 0001857542 scopus 로고
    • Synchronous exocytosis in Paramecium cells
    • (A. E. Sowers, Ed.) Plenum Press, New York
    • Plattner, H. (1987). Synchronous exocytosis in Paramecium cells. In "Cell Fusion" (A. E. Sowers, Ed.), pp. 69-98. Plenum Press, New York.
    • (1987) Cell Fusion , pp. 69-98
    • Plattner, H.1
  • 126
    • 0041659178 scopus 로고    scopus 로고
    • Dense-core secretory vesicle docking and exocytotic membrane fusion in Paramecium cells
    • Plattner, H., and Kissmehl, R. (2003). Dense-core secretory vesicle docking and exocytotic membrane fusion in Paramecium cells. Biochim. Biophys. Acta. 1641, 185-193.
    • (2003) Biochim. Biophys. Acta , vol.1641 , pp. 185-193
    • Plattner, H.1    Kissmehl, R.2
  • 127
    • 0033781424 scopus 로고    scopus 로고
    • Calcium in ciliated protozoa: Sources, regulation, and calcium regulated functions
    • Plattner, H., and Klauke, N. (2001). Calcium in ciliated protozoa: Sources, regulation, and calcium regulated functions. Int. Rev. Cytol. 201, 115-208.
    • (2001) Int. Rev. Cytol. , vol.201 , pp. 115-208
    • Plattner, H.1    Klauke, N.2
  • 128
    • 0030801106 scopus 로고    scopus 로고
    • Facilitation of membrane fusion during exocytosis and exocytosis-coupled endocytosis and acceleration of "ghost" detachment in Paramecium by extracellular calcium: A quenched-flow/freeze-fracture analysis
    • Plattner, H., Braun, C., and Hentschel, J. (1997). Facilitation of membrane fusion during exocytosis and exocytosis-coupled endocytosis and acceleration of "ghost" detachment in Paramecium by extracellular calcium: A quenched-flow/freeze-fracture analysis J. Membr. Biol. 158, 197-208.
    • (1997) J. Membr. Biol. , vol.158 , pp. 197-208
    • Plattner, H.1    Braun, C.2    Hentschel, J.3
  • 129
    • 0030971213 scopus 로고    scopus 로고
    • Differential distribution of calcium stores in Paramecium cells: Occurrence of a subplasmalemmal store with a calsequestrin-like protein
    • Plattner, H., Haberrmann, A., Kissmehl, R., Klauke, N., Majoul, I., and Söling, H. D. (1997). Differential distribution of calcium stores in Paramecium cells: Occurrence of a subplasmalemmal store with a calsequestrin-like protein. Eur. J. Cell Biol. 72, 297-306.
    • (1997) Eur. J. Cell Biol. , vol.72 , pp. 297-306
    • Plattner, H.1    Haberrmann, A.2    Kissmehl, R.3    Klauke, N.4    Majoul, I.5    Söling, H.D.6
  • 130
    • 0001930854 scopus 로고
    • Synchronization of different steps of the secretory cycle in Paramecium tetraurelia: Trichocyst exocytosis, exocytosis-coupled endocytosis, and intracellular transport
    • (H. Plattner, Ed.) JAI Press, Greenwich, CT
    • Plattner, H., Knoll, G., and Pape, R. (1993). Synchronization of different steps of the secretory cycle in Paramecium tetraurelia: Trichocyst exocytosis, exocytosis-coupled endocytosis, and intracellular transport. In "Membrane Traffic in Protozoa" (H. Plattner, Ed.), pp. 123-148. JAI Press, Greenwich, CT.
    • (1993) Membrane Traffic in Protozoa , pp. 123-148
    • Plattner, H.1    Knoll, G.2    Pape, R.3
  • 131
    • 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., and Kersken, H. (1985). 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
  • 133
    • 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., and 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
  • 134
    • 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
  • 135
    • 0001188280 scopus 로고
    • Genetic dissection of the morphogenesis and dynamics of exocytosis sites in Paramecium
    • Pouphile, M., Lefort-Tran, M., Plattner, H., Rossignol, M., and Beisson, J. (1986). Genetic dissection of the morphogenesis and dynamics 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
  • 137
    • 0037350449 scopus 로고    scopus 로고
    • Real-time analysis of clathrin-mediated endocytosis during cell migration
    • Rappoport, J. Z., and Simon, S. M. (2003). Real-time analysis of clathrin-mediated endocytosis during cell migration. J. Cell Sci. 116, 847-855.
    • (2003) J. Cell Sci. , vol.116 , pp. 847-855
    • Rappoport, J.Z.1    Simon, S.M.2
  • 138
    • 0031693296 scopus 로고    scopus 로고
    • Mechanics of membrane fusion
    • Rizo, J., and Südhof, T. C. (1998). Mechanics of membrane fusion. Nature Struct. Biol. 5, 839-842.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 839-842
    • Rizo, J.1    Südhof, T.C.2
  • 139
    • 1842414864 scopus 로고    scopus 로고
    • Throttles and dampers: Controlling the engine of membrane fusion
    • Rothman, J. E., and Söllner, T. H. (1997). Throttles and dampers: Controlling the engine of membrane fusion. Science 276, 1212-1213.
    • (1997) Science , vol.276 , pp. 1212-1213
    • Rothman, J.E.1    Söllner, T.H.2
  • 140
    • 0032905628 scopus 로고    scopus 로고
    • Basal body duplication in Paramecium requires γ-tubulin
    • Ruiz, F., Beisson, J., Rossier, J., and Dupuis-Williams, P. (1999). Basal body duplication in Paramecium requires γ-tubulin. Curr. Biol. 9, 43-46.
    • (1999) Curr. Biol. , vol.9 , pp. 43-46
    • Ruiz, F.1    Beisson, J.2    Rossier, J.3    Dupuis-Williams, P.4
  • 142
    • 0033786834 scopus 로고    scopus 로고
    • Real-time measurements of vesicle-SNARE recycling in synapses of the central nervous system
    • Sankaranarayanan, S., and Ryan, T. A. (2000). Real-time measurements of vesicle-SNARE recycling in synapses of the central nervous system. Nature Cell Biol. 2, 197-204.
    • (2000) Nature Cell Biol. , vol.2 , pp. 197-204
    • Sankaranarayanan, S.1    Ryan, T.A.2
  • 143
    • 0035146137 scopus 로고    scopus 로고
    • Calcium accelerates endocytosis of vSNAREs at hippocampal synapses
    • Sankaranarayanan, S., and Ryan, T. A. (2001). Calcium accelerates endocytosis of vSNAREs at hippocampal synapses. Nature Neurosci. 4, 129-136.
    • (2001) Nature Neurosci. , vol.4 , pp. 129-136
    • Sankaranarayanan, S.1    Ryan, T.A.2
  • 144
    • 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., and 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
  • 147
    • 0025663441 scopus 로고
    • Vesicle transport along microtubular ribbons and isolation of cytoplasmic dynein from Paramecium
    • Schroeder, C. C., Fok, A. K., and 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
  • 148
    • 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
  • 149
    • 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., and 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
  • 150
    • 0028287470 scopus 로고
    • Neurotransmission: Harnessing fusion machinery at the synapse
    • Söllner, T., and Rothman, J. E. (1994). Neurotransmission: Harnessing fusion machinery at the synapse. Trends Neurosci. 17, 344-348.
    • (1994) Trends Neurosci. , vol.17 , pp. 344-348
    • Söllner, T.1    Rothman, J.E.2
  • 151
    • 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., and Rothman, J. E. (1993). 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
  • 153
    • 0034496237 scopus 로고    scopus 로고
    • The endocytosis machinery
    • Sorkin, A. (2000). The endocytosis machinery. J. Cell Sci. 113, 4375-4376.
    • (2000) J. Cell Sci. , vol.113 , pp. 4375-4376
    • Sorkin, A.1
  • 157
    • 0022377781 scopus 로고
    • Carbohydrates of lysosomal enzymes secreted by Tetrahymena pyriformis
    • Taniguchi, T., Mizuochi, T., Banno, Y., Nozawa, Y., and 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
  • 158
    • 0007496640 scopus 로고
    • Pathways of lysosomal enzyme secretion in Tetrahymena
    • (H. Plattner, Ed.) JAI Press, Greenwich, CT
    • Tiedtke, A., Kiy, T., Vosskühler, C., and Rasmussen, L. (1993). Pathways of lysosomal enzyme secretion in Tetrahymena. In "Membrane Tarffic in Protozoa" (H. Plattner, Ed.), pp. 99-122. JAI Press, Greenwich, CT.
    • (1993) Membrane Tarffic in Protozoa , pp. 99-122
    • Tiedtke, A.1    Kiy, T.2    Vosskühler, C.3    Rasmussen, L.4
  • 159
    • 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., and Naitoh, Y. (1998). 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
  • 160
    • 0035280141 scopus 로고    scopus 로고
    • Secretory granule biogenesis: Rafting to the SNARE
    • Tooze, S. A., Martens, G. J. M., and Huttner, W. B. (2001). Secretory granule biogenesis: Rafting to the SNARE. Trends Cell Biol. 11, 116-122.
    • (2001) Trends Cell Biol. , vol.11 , pp. 116-122
    • Tooze, S.A.1    Martens, G.J.M.2    Huttner, W.B.3
  • 161
    • 0028956745 scopus 로고
    • Different domains of the AP-1 adaptor complex are required for Golgi membrane binding and clathrin recruitment
    • Traub, L. M., Kornfeld, S., and Ungewickell, E. (1995). Different domains of the AP-1 adaptor complex are required for Golgi membrane binding and clathrin recruitment. J. Biol. Chem. 270, 4933-4942.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4933-4942
    • Traub, L.M.1    Kornfeld, S.2    Ungewickell, E.3
  • 162
    • 0037474290 scopus 로고    scopus 로고
    • Differential role of actin, clathrin, and dynamin in Fcγ receptor-mediated endocytosis and phagocytosis
    • Tse, S. M. L., Furuya, W., Gold, E., Schreiber, A. D., Sandvig, K., Inman, R. D., and Grinstein, S. (2003). Differential role of actin, clathrin, and dynamin in Fcγ receptor-mediated endocytosis and phagocytosis. J. Biol. Chem. 278, 3331-3338.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3331-3338
    • Tse, S.M.L.1    Furuya, W.2    Gold, E.3    Schreiber, A.D.4    Sandvig, K.5    Inman, R.D.6    Grinstein, S.7
  • 164
    • 0025815320 scopus 로고
    • Maturation of dense core granules in wild type and mutant Tetrahymena thermophila
    • Turkewitz, A. P., Madeddu, L., and 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
  • 165
    • 0036138203 scopus 로고    scopus 로고
    • Functional genomics: The coming of age for Tetrahymena thermophila
    • Turkewitz, A. P., Orias, E., and 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
  • 167
    • 0030759249 scopus 로고    scopus 로고
    • Formation of secretory vesicles in the biosynthetic pathway
    • Urbé, S., Tooze, S. A., and Barr, F. A. (1997). Formation of secretory vesicles in the biosynthetic pathway. Biochim. Biophys. Acta 1358, 6-22.
    • (1997) Biochim. Biophys. Acta , vol.1358 , pp. 6-22
    • Urbé, S.1    Tooze, S.A.2    Barr, F.A.3
  • 168
    • 0034122147 scopus 로고    scopus 로고
    • Molecular genetics of regulated secretion in Paramecium
    • Vayssié, L., Skouri, F., Sperling, L., and 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
  • 169
    • 0029943482 scopus 로고    scopus 로고
    • Poisson-distributed active fusion complexes underlie the control of the rate and extent of exocytosis by calcium
    • Vogel, S. S., Blank, P. S., and Zimmerberg, J. (1996). Poisson-distributed active fusion complexes underlie the control of the rate and extent of exocytosis by calcium. J. Cell Biol. 134, 329-338.
    • (1996) J. Cell Biol. , vol.134 , pp. 329-338
    • Vogel, S.S.1    Blank, P.S.2    Zimmerberg, J.3
  • 170
    • 0027772671 scopus 로고
    • A Ca-dependent early step in the release of catecholamines from adrenal chromaffin cells
    • Von Rueden, L., and Neher, E. (1993). A Ca-dependent early step in the release of catecholamines from adrenal chromaffin cells. Science 262, 1061-1065.
    • (1993) Science , vol.262 , pp. 1061-1065
    • Von Rueden, L.1    Neher, E.2
  • 171
    • 84987576613 scopus 로고
    • Magneticseparation of phagosomes of defined age from Tetrahymena thermophila
    • Vosskühler, C., and Tiedtke, A. (1993). Magneticseparation 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
  • 172
  • 173
    • 0001792655 scopus 로고    scopus 로고
    • Genetic characterization of the secretory mutants in Paramecium caudatum
    • Watanabe, T., and 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
  • 175
    • 0035003581 scopus 로고    scopus 로고
    • N-Ethylmaleimide sensitive factor (NSF) structure and function
    • Whiteheart, S. W., Schraw, T., and 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
  • 176
    • 0035753543 scopus 로고    scopus 로고
    • Structure of the vacuolar adenosine triphosphatases
    • Wilkens, S. (2001). Structure of the vacuolar adenosine triphosphatases. Cell Biochem. Biophys. 34, 191-208.
    • (2001) Cell Biochem. Biophys. , vol.34 , pp. 191-208
    • Wilkens, S.1
  • 177
    • 0037109072 scopus 로고    scopus 로고
    • Do SNARE proteins confer specificity for vesicle fusion?
    • Xue, M., and Zhang, B. (2002). Do SNARE proteins confer specificity for vesicle fusion? Proc. Natl. Acad. Sci. USA 99, 13359-13361.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13359-13361
    • Xue, M.1    Zhang, B.2
  • 178
    • 0037078331 scopus 로고    scopus 로고
    • ARFGAP1 promotes the formation of COPI vesicles, suggesting function as a component of the coat
    • Yang, J. S., Lee, S. Y., Gao, M., Bourgoin, S., Randazzo, P. A., Premont, R. T., and Hsu, V. W. (2002). ARFGAP1 promotes the formation of COPI vesicles, suggesting function as a component of the coat. J. Cell Biol. 159, 69-78.
    • (2002) J. Cell Biol. , vol.159 , pp. 69-78
    • Yang, J.S.1    Lee, S.Y.2    Gao, M.3    Bourgoin, S.4    Randazzo, P.A.5    Premont, R.T.6    Hsu, V.W.7
  • 180
    • 0035371723 scopus 로고    scopus 로고
    • How can proteolipids be central players in membrane fusion?
    • Zimmerberg, J. (2001). How can proteolipids be central players in membrane fusion? Trends Cell Biol. 11, 233-234.
    • (2001) Trends Cell Biol. , vol.11 , pp. 233-234
    • Zimmerberg, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.