메뉴 건너뛰기




Volumn 139, Issue 5, 1997, Pages 1197-1207

In vivo analysis of the major exocytosis-sensitive phosphoprotein in Tetrahymena

Author keywords

[No Author keywords available]

Indexed keywords

MUSCLE ENZYME; PHOSPHOGLUCOMUTASE; PHOSPHOPROTEIN;

EID: 0030774280     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.139.5.1197     Document Type: Article
Times cited : (28)

References (63)
  • 1
    • 0028260539 scopus 로고
    • The activity of parafusin is distinct from that of phosphoglucomutase in the unicellular eukaryote Paramecium
    • Andersen, A.P., E. Wyroba, M. Reichman, H. Zhao, and B.H. Satir. 1994. The activity of parafusin is distinct from that of phosphoglucomutase in the unicellular eukaryote Paramecium. Biochem. Biophys. Res. Com. 200:1353-1358.
    • (1994) Biochem. Biophys. Res. Com. , vol.200 , pp. 1353-1358
    • Andersen, A.P.1    Wyroba, E.2    Reichman, M.3    Zhao, H.4    Satir, B.H.5
  • 3
    • 0028126074 scopus 로고
    • A novel phosphoglucomutase-related protein is concentrated in adherens junctions of muscle and nonmuscle cells
    • Belkin, A.M., I.V. Klimanskaya, M.E. Lukashev, K. Lilley, D.R. Critchley, and V. E. Koteliansky. 1994. A novel phosphoglucomutase-related protein is concentrated in adherens junctions of muscle and nonmuscle cells. J. Cell Sci. 107:159-73.
    • (1994) J. Cell Sci. , vol.107 , pp. 159-173
    • Belkin, A.M.1    Klimanskaya, I.V.2    Lukashev, M.E.3    Lilley, K.4    Critchley, D.R.5    Koteliansky, V.E.6
  • 4
    • 0027404604 scopus 로고
    • The molecular machinery for secretion is conserved from yeast to neurons
    • Bennett, M.K., and R. H. Scheller. 1993. The molecular machinery for secretion is conserved from yeast to neurons. Proc. Natl. Acad. Sci. USA. 90:2559-2563.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2559-2563
    • Bennett, M.K.1    Scheller, R.H.2
  • 5
    • 0027976872 scopus 로고
    • A family of hexosephosphate mutases in Saccharomyces cerevisiae
    • Boles, E., W. Liebetrau, M. Hofmann, and F.K. Zimmermann. 1994. A family of hexosephosphate mutases in Saccharomyces cerevisiae. Eur. J. Biochem. 220:83-96.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 83-96
    • Boles, E.1    Liebetrau, W.2    Hofmann, M.3    Zimmermann, F.K.4
  • 6
    • 0002695208 scopus 로고
    • Genetic organization of Tetrahymena
    • J.G. Gall, editor. Academic Press, NY
    • Bruns, P.J. 1986. Genetic organization of Tetrahymena. In The Molecular Biology of Ciliated Protozoa. J.G. Gall, editor. Academic Press, NY. pp. 27-44.
    • (1986) The Molecular Biology of Ciliated Protozoa , pp. 27-44
    • Bruns, P.J.1
  • 7
    • 0024150623 scopus 로고
    • Focal adhesions: Transmembrane junctions between the extracelular matrix and the cytoskeleton
    • Burridge, K., K. Fath. T. Kelly, T. Nuckolls, and C. Turner. 1988. Focal adhesions: transmembrane junctions between the extracelular matrix and the cytoskeleton. Annu. Rev. Cell Biol. 4:487-525.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 487-525
    • Burridge, K.1    Fath, K.2    Kelly, T.3    Nuckolls, T.4    Turner, C.5
  • 8
    • 0030051050 scopus 로고    scopus 로고
    • Synaptic vesicle biogenesis, docking, and fusion: A molecular description
    • Calakos, N., and R.H. Scheller. 1996. Synaptic vesicle biogenesis, docking, and fusion: a molecular description. Physiol. Rev. 76:1-29.
    • (1996) Physiol. Rev. , vol.76 , pp. 1-29
    • Calakos, N.1    Scheller, R.H.2
  • 9
    • 0030478918 scopus 로고    scopus 로고
    • 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., S.M. Melia, A. Haddad, and A.P. Turkewitz. 1996. 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
  • 10
    • 0028831997 scopus 로고
    • Calcium signaling
    • Clapham, D.E. 1995. Calcium signaling. Cell. 80:259-268.
    • (1995) Cell , vol.80 , pp. 259-268
    • Clapham, D.E.1
  • 11
    • 0026664620 scopus 로고
    • The crystal structure of muscle phosphoglucomutase refined at 2.7-angstrom resolution
    • Dai, J.B., Y. Liu, W.J. Ray, Jr., and M. Konno. 1992. The crystal structure of muscle phosphoglucomutase refined at 2.7-angstrom resolution. J. Biol. Chem. 267:6322-6337.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6322-6337
    • Dai, J.B.1    Liu, Y.2    Ray Jr., W.J.3    Konno, M.4
  • 12
    • 0029796798 scopus 로고    scopus 로고
    • Regulation of intracellular calcium is closely linked to glucose metabolism in J774 macrophages
    • Darbha, S., and R.B. Marchase. 1996. Regulation of intracellular calcium is closely linked to glucose metabolism in J774 macrophages. Cell Calcium. 20:361-371.
    • (1996) Cell Calcium , vol.20 , pp. 361-371
    • Darbha, S.1    Marchase, R.B.2
  • 13
    • 0028138630 scopus 로고
    • The glycosylation of phosphoglucomutase is modulated by carbon source and heat shock in Saccharomyces cerevisiae
    • Dey, N.B., P. Bounelis, T.A. Fritz, D.M. Bedwell, and R.B. Marchase. 1994. The glycosylation of phosphoglucomutase is modulated by carbon source and heat shock in Saccharomyces cerevisiae. J. Biol. Chem. 269:27143-27148.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27143-27148
    • Dey, N.B.1    Bounelis, P.2    Fritz, T.A.3    Bedwell, D.M.4    Marchase, R.B.5
  • 15
    • 0027298836 scopus 로고
    • Perspectives on tubulin isotype function and evolution based on the observation that Tetrahymena thermophila microtubules contain a single α- and β-tubulin
    • Gaertig, J., T.H. Thatcher, K.E. McGrath, R.C. Callahan, and M.A. Gorovsky. 1993. Perspectives on tubulin isotype function and evolution based on the observation that Tetrahymena thermophila microtubules contain a single α-and β-tubulin. Cell Motil. Cytoskel. 25:243-253.
    • (1993) Cell Motil. Cytoskel. , vol.25 , pp. 243-253
    • Gaertig, J.1    Thatcher, T.H.2    McGrath, K.E.3    Callahan, R.C.4    Gorovsky, M.A.5
  • 16
    • 0028661172 scopus 로고
    • High frequency vector-mediated transformation and gene replacement in Tetrahymena
    • Gaertig, J., L. Gu, B. Hai, and M.A. Gorovsky. 1994. High frequency vector-mediated transformation and gene replacement in Tetrahymena. Nucleic Acids Res. 22:5391-5398.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 5391-5398
    • Gaertig, J.1    Gu, L.2    Hai, B.3    Gorovsky, M.A.4
  • 17
    • 0029178017 scopus 로고
    • Gene transfer by electroporation of Tetrahymena
    • J.A. Nickoloff, editor. Humana Press, Totowa, NJ
    • Gaertig, J., T.H. Thatcher, and M.A. Gorovsky. 1995. Gene transfer by electroporation of Tetrahymena. In Electroporation Protocols for Microorganisms, J.A. Nickoloff, editor. Humana Press, Totowa, NJ. pp. 331-348.
    • (1995) Electroporation Protocols for Microorganisms , pp. 331-348
    • Gaertig, J.1    Thatcher, T.H.2    Gorovsky, M.A.3
  • 18
    • 0020356743 scopus 로고
    • Protein phosphorylation/dephosphorylation and stimulus-secretion coupling in wild type and mutant Paramecium
    • Gilligan, D.M., and B.H. Satir. 1982. Protein phosphorylation/dephosphorylation and stimulus-secretion coupling in wild type and mutant Paramecium. J. Biol. Chem. 257:13903-13906.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13903-13906
    • Gilligan, D.M.1    Satir, B.H.2
  • 19
    • 0026643637 scopus 로고
    • Genetic characterization of Tetrahymena thermophila mutants unable to secrete capsules
    • Gutierrez, J.C., and E. Orias. 1992. Genetic characterization of Tetrahymena thermophila mutants unable to secrete capsules. Dev. Genet. 13:160-166.
    • (1992) Dev. Genet. , vol.13 , pp. 160-166
    • Gutierrez, J.C.1    Orias, E.2
  • 20
    • 0000537609 scopus 로고
    • A starchless mutant of Nicotiana sylvestris containing a modified plastid phosphoglucomutase
    • Hanson, K.R., and N.A. McHale. 1988. A starchless mutant of Nicotiana sylvestris containing a modified plastid phosphoglucomutase. Plant Physiol. 88: 838-844.
    • (1988) Plant Physiol. , vol.88 , pp. 838-844
    • Hanson, K.R.1    McHale, N.A.2
  • 21
    • 84989617462 scopus 로고
    • Defensive function of trichocysts in Paramecium
    • Harumoto, T., and A. Miyake. 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
  • 22
    • 0030908946 scopus 로고    scopus 로고
    • Identification of isoforms of the exocytosis-sensitive phosphoprotein PP63/parafusin in Paramecium tetraurelia and demonstration of phosphoglucomutase activity
    • Hauser, K., R. Kissmehl, J. Linder, J.E. Schultz, F. Lottspeich, and H. Plattner. 1997. Identification of isoforms of the exocytosis-sensitive phosphoprotein PP63/parafusin in Paramecium tetraurelia and demonstration of phosphoglucomutase activity. Biochem. J. 323:289-296.
    • (1997) Biochem. J. , vol.323 , pp. 289-296
    • Hauser, K.1    Kissmehl, R.2    Linder, J.3    Schultz, J.E.4    Lottspeich, F.5    Plattner, H.6
  • 23
    • 0028271352 scopus 로고
    • Characterization of the essential yeast gene encoding N-acetylglucosamine-phosphate mutase
    • Hofmann, M., E. Boles, and F.K. Zimmermann. 1994. Characterization of the essential yeast gene encoding N-acetylglucosamine-phosphate mutase. Euro. J. Biochem. 221:741-747.
    • (1994) Euro. J. Biochem. , vol.221 , pp. 741-747
    • Hofmann, M.1    Boles, E.2    Zimmermann, F.K.3
  • 24
    • 0026646436 scopus 로고
    • A cortical phosphoprotein ('PP63') sensitive to exocytosis triggering in Paramecium
    • Höhne-Zell, B., G. Knoll, U. Riedel-Gras, W. Hofer, and H. Plattner/ 1992. A cortical phosphoprotein ('PP63') sensitive to exocytosis triggering in Paramecium. Biochem. J. 286:843-849.
    • (1992) Biochem. J. , vol.286 , pp. 843-849
    • Höhne-Zell, B.1    Knoll, G.2    Riedel-Gras, U.3    Hofer, W.4    Plattner, H.5
  • 25
    • 0023651625 scopus 로고
    • Unusual features of transcribed and translated regions of the histone H4 gene family of Tetrahymena thermophila
    • Horowitz, S., J.K. Bowen, G.A. Bannon, and M.A. Gorovsky. 1987. Unusual features of transcribed and translated regions of the histone H4 gene family of Tetrahymena thermophila. Nucleic Acids Res. 15:141-160.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 141-160
    • Horowitz, S.1    Bowen, J.K.2    Bannon, G.A.3    Gorovsky, M.A.4
  • 26
    • 0020347803 scopus 로고
    • Phosphoglucomutase from yeast
    • Joshi, J.G. 1982. Phosphoglucomutase from yeast. Methods Enzymol. 89:599-605.
    • (1982) Methods Enzymol. , vol.89 , pp. 599-605
    • Joshi, J.G.1
  • 27
    • 0029891406 scopus 로고    scopus 로고
    • Protein phosphatase and kinase activities possibly involved in exocytosis regulation in Paramecium tetraurelia
    • Kissmehl, R., T. Treptau, H.W. Hofer, and H. Plattner. 1996. Protein phosphatase and kinase activities possibly involved in exocytosis regulation in Paramecium tetraurelia. Biochem. J. 317:65-76.
    • (1996) Biochem. J. , vol.317 , pp. 65-76
    • Kissmehl, R.1    Treptau, T.2    Hofer, H.W.3    Plattner, H.4
  • 28
    • 0031041882 scopus 로고    scopus 로고
    • A novel, calcium-inhibitable casein kinase in Paramecium cells
    • Kissmehl, R., T. Treptau, K. Hauser, and H. Plattner. 1997. A novel, calcium-inhibitable casein kinase in Paramecium cells. FEBS Lett. 402:227-235.
    • (1997) FEBS Lett. , vol.402 , pp. 227-235
    • Kissmehl, R.1    Treptau, T.2    Hauser, K.3    Plattner, H.4
  • 29
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. 1991. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24:946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 30
    • 0026657595 scopus 로고
    • Purification, characterization, and molecular cloning of a 60-kD phosphoprotein in rabbit skeletal sarcoplasmic reticulum which is an isoform of phosphoglucomutase
    • Lee, Y.S., A.R. Marks, N. Gureckas, R. Lacro, B. Nadal-Ginard, and D.H. Kim. 1992. Purification, characterization, and molecular cloning of a 60-kD phosphoprotein in rabbit skeletal sarcoplasmic reticulum which is an isoform of phosphoglucomutase. J. Biol. Chem. 267:21080-21088.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21080-21088
    • Lee, Y.S.1    Marks, A.R.2    Gureckas, N.3    Lacro, R.4    Nadal-Ginard, B.5    Kim, D.H.6
  • 31
    • 0028148056 scopus 로고
    • Molecular cloning and characterization of the pgm gene encoding phosphoglucomutase of Escherichia coli
    • Lu, M., and N. Kleckner. 1994. Molecular cloning and characterization of the pgm gene encoding phosphoglucomutase of Escherichia coli. J. Bacteriol. 176:5847-5851.
    • (1994) J. Bacteriol. , vol.176 , pp. 5847-5851
    • Lu, M.1    Kleckner, N.2
  • 32
    • 0029019520 scopus 로고
    • A large multigenic family codes for the polypeptides of the crystalline trichocyst matrix in Paramecium
    • Madeddu, L., M.-C. Gautier, L. Vayssié, A. Houari, and L. Sperling. 1995. A large multigenic family codes for the polypeptides of the crystalline trichocyst matrix in Paramecium. Mol. Biol. Cell. 6:649-659.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 649-659
    • Madeddu, L.1    Gautier, M.-C.2    Vayssié, L.3    Houari, A.4    Sperling, L.5
  • 33
    • 0022272135 scopus 로고
    • Protein secretion in Tetrahymena thermophila: Characterization of the secretory mutant strain SB281
    • Maihle, N.J., and B.H. Satir. 1985. Protein secretion in Tetrahymena thermophila: characterization of the secretory mutant strain SB281. J. Cell Sci. 78:49-65.
    • (1985) J. Cell Sci. , vol.78 , pp. 49-65
    • Maihle, N.J.1    Satir, B.H.2
  • 34
    • 0023666011 scopus 로고
    • 32P]thioate analogue of UDP-GLC is efficiently utilized by the glucose phosphotransferase and is relatively resistant to hydrolytic degradation
    • 32P]thioate analogue of UDP-GLC is efficiently utilized by the glucose phosphotransferase and is relatively resistant to hydrolytic degradation. Biochim. Biophys. Acta. 916:157-162.
    • (1987) Biochim. Biophys. Acta. , vol.916 , pp. 157-162
    • Marchase, R.B.1    Sounders, A.M.2    Rivera, A.A.3    Cook, J.M.4
  • 36
    • 0024490176 scopus 로고
    • Codon usage in Tetrahymena and other ciliates
    • Martindale, D.W. 1989. Codon usage in Tetrahymena and other ciliates. J. Protozool. 36:29-34.
    • (1989) J. Protozool. , vol.36 , pp. 29-34
    • Martindale, D.W.1
  • 38
    • 0030021413 scopus 로고    scopus 로고
    • A novel dystrophin/utrophin-associated protein is an enzymatically inactive member of the phosphoglucomutase superfamily
    • Moiseeva, E.P., A. M. Belkin, N.K. Spurr, V.E. Koteliansky, and D.R. Critchley. 1996. A novel dystrophin/utrophin-associated protein is an enzymatically inactive member of the phosphoglucomutase superfamily. Eur. J. Biochem. 235:103-113.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 103-113
    • Moiseeva, E.P.1    Belkin, A.M.2    Spurr, N.K.3    Koteliansky, V.E.4    Critchley, D.R.5
  • 39
    • 0023376810 scopus 로고
    • Exocytosis induction in Parameciuim tetraurelia cells by exogenous phosphoprotein phosphatases in vivo and in vitro: Possible involvement of calcineurin in exocytotic membrane fusion
    • Momayezi, M., C. Lumpert, H. Kersken, U. Gras, H. Plattner, M. Krinks, and C.B. Klee. 1987. Exocytosis induction in Parameciuim tetraurelia cells by exogenous phosphoprotein phosphatases in vivo and in vitro: possible involvement of calcineurin in exocytotic membrane fusion. J. Cell Biol. 105:181-189.
    • (1987) J. Cell Biol. , vol.105 , pp. 181-189
    • Momayezi, M.1    Lumpert, C.2    Kersken, H.3    Gras, U.4    Plattner, H.5    Krinks, M.6    Klee, C.B.7
  • 41
    • 0023691425 scopus 로고
    • Genetic applications of an inverse polymerase chain reaction
    • Ochman, H., A.S. Gerber, and D.L. Hartl. 1988. Genetic applications of an inverse polymerase chain reaction. Genetics. 120:621-623.
    • (1988) Genetics , vol.120 , pp. 621-623
    • Ochman, H.1    Gerber, A.S.2    Hartl, D.L.3
  • 42
    • 0025234499 scopus 로고
    • Transcription of a yeast phosphoglucomutase isozyme gene is galactose inducible and glucose repressible
    • Oh, D., and J.E. Hopper. 1990. Transcription of a yeast phosphoglucomutase isozyme gene is galactose inducible and glucose repressible. Mol. Cell. Biol. 10:1415-1422.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 1415-1422
    • Oh, D.1    Hopper, J.E.2
  • 44
    • 0030965369 scopus 로고    scopus 로고
    • Regulation of calcium-induced exocytosis from gastric chief cells by protein phosphatase-2B (calcineurin)
    • Raufman, J.P., R. Malhotra, and R.D. Raffaniello. 1997. Regulation of calcium-induced exocytosis from gastric chief cells by protein phosphatase-2B (calcineurin). Biochim. Biophys. Acta. 1357:73-80.
    • (1997) Biochim. Biophys. Acta. , vol.1357 , pp. 73-80
    • Raufman, J.P.1    Malhotra, R.2    Raffaniello, R.D.3
  • 45
  • 46
    • 0024996651 scopus 로고
    • Parafusin, an exocytic-sensitive phosphoprotein, is the primary acceptor for the glucosylphosphotransferase in Paramecium tetraurelia and rat liver
    • Satir, B.H., C. Srisomsap, M. Reichman, and R.B. Marchase. 1990. Parafusin, an exocytic-sensitive phosphoprotein, is the primary acceptor for the glucosylphosphotransferase in Paramecium tetraurelia and rat liver. J. Cell Biol. 111:901-907.
    • (1990) J. Cell Biol. , vol.111 , pp. 901-907
    • Satir, B.H.1    Srisomsap, C.2    Reichman, M.3    Marchase, R.B.4
  • 47
    • 77956835775 scopus 로고
    • Methods in Paramecium research
    • D.M. Prescott, editor. Academic Press, New York
    • Sonneborn, T.M. 1970. Methods in Paramecium research. In Methods in Cell Physiology. D.M. Prescott, editor. Academic Press, New York. pp. 241-339.
    • (1970) Methods in Cell Physiology , pp. 241-339
    • Sonneborn, T.M.1
  • 48
    • 0023659744 scopus 로고
    • Involvement of a 65 kD phosphoprotein in the regulation of membrane fusion during exocytosis in Paramecium cells
    • Stecher, B., B. Hohne, U. Gras, M. Momayezi, R. Glas-Albrecht, and H. Plattner. 1987. Involvement of a 65 kD phosphoprotein in the regulation of membrane fusion during exocytosis in Paramecium cells. FEBS Lett. 223:25-32.
    • (1987) FEBS Lett. , vol.223 , pp. 25-32
    • Stecher, B.1    Hohne, B.2    Gras, U.3    Momayezi, M.4    Glas-Albrecht, R.5    Plattner, H.6
  • 50
    • 0028148299 scopus 로고
    • Cloning and sequencing of parafusin, a calcium-dependent exocytosis-related phosphoglycoprotein
    • Subramanian, S.V., E. Wyroba, A.P. Andersen, and B.H. Satir. 1994. Cloning and sequencing of parafusin, a calcium-dependent exocytosis-related phosphoglycoprotein. Proc. Natl. Acad. Sci. USA. 91:9832-9836.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9832-9836
    • Subramanian, S.V.1    Wyroba, E.2    Andersen, A.P.3    Satir, B.H.4
  • 51
    • 0025828234 scopus 로고
    • Proteins of synaptic vesicles involved in exocytosis and membrane recycling
    • Sudhof, T. C., and R. Jahn. 1991. Proteins of synaptic vesicles involved in exocytosis and membrane recycling. Neuron. 6: 665-677.
    • (1991) Neuron , vol.6 , pp. 665-677
    • Sudhof, T.C.1    Jahn, R.2
  • 52
    • 0016924064 scopus 로고
    • Capsule shedding in Tetrahymena
    • Tiedtke, A. 1976. Capsule shedding in Tetrahymena. Naturwissenschaften. 63: 93-94.
    • (1976) Naturwissenschaften , vol.63 , pp. 93-94
    • Tiedtke, A.1
  • 53
    • 0026643635 scopus 로고
    • Immunocytochemical analysis of secretion mutants of Tetrahymena using a mucocyst-specific monoclonal antibody
    • Turkewitz, A.P., and R.B. Kelly. 1992. Immunocytochemical analysis of secretion mutants of Tetrahymena using a mucocyst-specific monoclonal antibody. Dev. Genet. 13:151-159.
    • (1992) Dev. Genet. , vol.13 , pp. 151-159
    • Turkewitz, A.P.1    Kelly, R.B.2
  • 54
    • 0025815320 scopus 로고
    • Maturation of dense core granules in wild type and mutant Tetrahymena thermophila
    • Turkewitz, A.P., L. Madeddu, and R.B. Kelly. 1991. Maturation of dense core granules in wild type and mutant Tetrahymena thermophila. EMBO (Eur. Mol. Biol. Organ.) J. 10:1979-1987.
    • (1991) EMBO (Eur. Mol. Biol. Organ.) J. , vol.10 , pp. 1979-1987
    • Turkewitz, A.P.1    Madeddu, L.2    Kelly, R.B.3
  • 56
    • 0027979755 scopus 로고
    • The addition of glucose-1-phosphate to the cytoplasmic glycoprotein phosphoglucomutase is modulated by intracellular calcium in PC12 cells and rat cortical synaptosomes
    • Veyna, N.A., J.C. Jay, C. Srisomsap, P. Bounelis, and R. B. Marchase. 1994. The addition of glucose-1-phosphate to the cytoplasmic glycoprotein phosphoglucomutase is modulated by intracellular calcium in PC12 cells and rat cortical synaptosomes. J. Neurochem. 62:456-64.
    • (1994) J. Neurochem. , vol.62 , pp. 456-464
    • Veyna, N.A.1    Jay, J.C.2    Srisomsap, C.3    Bounelis, P.4    Marchase, R.B.5
  • 58
    • 0023648790 scopus 로고
    • The enzyme lactate dehydrogenase is a strucutral protein in avian and crocodilian lenses
    • Wistow, G.J., J.W.M. Mulders, and W.W. Jong. 1987. The enzyme lactate dehydrogenase is a strucutral protein in avian and crocodilian lenses. Nature. 326: 622-624.
    • (1987) Nature , vol.326 , pp. 622-624
    • Wistow, G.J.1    Mulders, J.W.M.2    Jong, W.W.3
  • 59
    • 0031407579 scopus 로고    scopus 로고
    • Maximum ages of ciliate lineages estimated using a small subunit rRNa molecular clock: Crown eukaryotes date back to the Paleoproterozoic
    • In press
    • Wright, A.-D., and D.H. Lynn. 1997. Maximum ages of ciliate lineages estimated using a small subunit rRNA molecular clock: crown eukaryotes date back to the Paleoproterozoic. Arch. Protistenkd. In press.
    • (1997) Arch. Protistenkd.
    • Wright, A.-D.1    Lynn, D.H.2
  • 60
    • 0029559869 scopus 로고
    • Mammalian homologue of the calcium-sensitive phosphoglycoprotein, parafusin
    • Wyroba, E., A. Widding Hoyer, P. Storgaard, and B.H. Satir. 1995. Mammalian homologue of the calcium-sensitive phosphoglycoprotein, parafusin. Eur. J. Cell Biol. 68:419-426.
    • (1995) Eur. J. Cell Biol. , vol.68 , pp. 419-426
    • Wyroba, E.1    Widding Hoyer, A.2    Storgaard, P.3    Satir, B.H.4
  • 61
    • 0016202011 scopus 로고
    • Comparison of the sequence of macro- and micronuclear DNA of Tetrahymena pyriformis
    • Yao, M.-C., and M. Gorovsky. 1974. Comparison of the sequence of macro-and micronuclear DNA of Tetrahymena pyriformis. Proc. Natl. Acad. Sci. USA. 48:1-18.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.48 , pp. 1-18
    • Yao, M.-C.1    Gorovsky, M.2
  • 62
    • 0028310423 scopus 로고
    • Lipooligosaccharide biosynthesis in pathogenic Neisseria. Cloning, identification, and characterization of the phosphoglucomutase gene
    • Zhou, D., D.S. Stephens, B.W. Gibson, J.J. Engstrom, C.F. McAllister, F.K. Lee, and M.A. Apicella. 1994. Lipooligosaccharide biosynthesis in pathogenic Neisseria. Cloning, identification, and characterization of the phosphoglucomutase gene. J. Biol. Chem. 269:11162-11169.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11162-11169
    • Zhou, D.1    Stephens, D.S.2    Gibson, B.W.3    Engstrom, J.J.4    McAllister, C.F.5    Lee, F.K.6    Apicella, M.A.7
  • 63
    • 0022392704 scopus 로고
    • Synchronous exocytosis in Paramecium cells involves very rapid (<1 s) reversible dephosphorylation of a 65-kD phosphoprotein in exocytosis-competent strains
    • Zieseniss, E., and H. Plattner. 1985. Synchronous exocytosis in Paramecium cells involves very rapid (<1 s) reversible dephosphorylation of a 65-kD phosphoprotein in exocytosis-competent strains. J. Cell Biol. 101:2028-2035.
    • (1985) J. Cell Biol. , vol.101 , pp. 2028-2035
    • Zieseniss, E.1    Plattner, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.