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Volumn 42, Issue 5, 2000, Pages 757-764

Cloning of Arabidopsis thaliana phosphatidylinositol synthase and functional expression in the yeast pis mutant

Author keywords

Arabidopsis thaliana; Molecular cloning; Phosphatidylinositol synthase; Signal transduction; Yeast complementation

Indexed keywords

AMINO ACID SEQUENCE; ATPIS1; COMPLEMENTARY DNA; CYTIDINE DIPHOSPHATE DIACYLGLYCEROL INOSITOL 3 PHOSPHATIDYLTRANSFERASE; LIPID METABOLISM; MUTANT; NUCLEOTIDE SEQUENCE; PROTEIN FUNCTION; SIGNAL TRANSDUCTION;

EID: 0034008304     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1006308909105     Document Type: Article
Times cited : (24)

References (54)
  • 2
    • 0029974122 scopus 로고    scopus 로고
    • Carbon source regulation of PIS1 gene expression in Saccharomyces cerevisiae involves the MCM1 gene and the two-component regulatory gene, SLN1
    • Anderson, M.S. and Lopes, J.M. 1996. Carbon source regulation of PIS1 gene expression in Saccharomyces cerevisiae involves the MCM1 gene and the two-component regulatory gene, SLN1. J. Biol. Chem. 271: 26596-26601.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26596-26601
    • Anderson, M.S.1    Lopes, J.M.2
  • 3
    • 0028040154 scopus 로고
    • Purification and characterization of phosphatidylinositol synthase from human placenta
    • Antonsson, B.E. 1994. Purification and characterization of phosphatidylinositol synthase from human placenta. Biochem. J. 297: 517-522.
    • (1994) Biochem. J. , vol.297 , pp. 517-522
    • Antonsson, B.E.1
  • 4
    • 0029890329 scopus 로고    scopus 로고
    • Candida albicans phosphatidylinositol synthase has common features with both Saccharomyces cerevisiae and mammalian phosphatidylinositol synthase
    • Antonsson, B.E. and Klig, L.S. 1996. Candida albicans phosphatidylinositol synthase has common features with both Saccharomyces cerevisiae and mammalian phosphatidylinositol synthase. Yeast 12: 449-456.
    • (1996) Yeast , vol.12 , pp. 449-456
    • Antonsson, B.E.1    Klig, L.S.2
  • 5
    • 0021915669 scopus 로고
    • Regulation and location of phosphatidylglycerol and phosphatidylinositol synthesis in type II cells isolated from fetal rat lung
    • Batenburg, J.J., Klazinga, W. and van Golde, L.M.G. 1985. Regulation and location of phosphatidylglycerol and phosphatidylinositol synthesis in type II cells isolated from fetal rat lung. Biochim. Biophys. Acta 833: 17-24.
    • (1985) Biochim. Biophys. Acta , vol.833 , pp. 17-24
    • Batenburg, J.J.1    Klazinga, W.2    Van Golde, L.M.G.3
  • 6
    • 0021750054 scopus 로고
    • Inositol trisphosphate, a novel second messenger in cellular signal transduction
    • Berridge, M.J. and Irvine, R.F. 1984. Inositol trisphosphate, a novel second messenger in cellular signal transduction. Nature 312: 315-321.
    • (1984) Nature , vol.312 , pp. 315-321
    • Berridge, M.J.1    Irvine, R.F.2
  • 7
    • 0021443856 scopus 로고
    • Inositol trisphosphate and diacylglycerol as second messengers
    • Berridge, M.J. 1984. Inositol trisphosphate and diacylglycerol as second messengers. Biochem. J. 220: 345-360.
    • (1984) Biochem. J. , vol.220 , pp. 345-360
    • Berridge, M.J.1
  • 8
    • 0022342956 scopus 로고
    • Subcellular sites of synthesis of phosphatidylglycerol and phosphatidylinositol in type II pneumonocytes
    • Bleasdale, J.E., Tyler, N.B. and Snyder, J.M. 1985. Subcellular sites of synthesis of phosphatidylglycerol and phosphatidylinositol in type II pneumonocytes. Lung 163: 345-359.
    • (1985) Lung , vol.163 , pp. 345-359
    • Bleasdale, J.E.1    Tyler, N.B.2    Snyder, J.M.3
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 10
    • 0029968296 scopus 로고    scopus 로고
    • Phosphoinositides as regulators in membrane traffic
    • DeCamilli, P., Emr, S.D., McPherson, P.S. and Novick, P. 1996. Phosphoinositides as regulators in membrane traffic. Science 271: 1533-1539.
    • (1996) Science , vol.271 , pp. 1533-1539
    • DeCamilli, P.1    Emr, S.D.2    McPherson, P.S.3    Novick, P.4
  • 11
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., Haeberli, P. and Smithies, O. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucl. Acids Res. 12: 387-395.
    • (1984) Nucl. Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 12
    • 0028883178 scopus 로고
    • Phospholipid signaling
    • Divecha, N. and Irvine, R.F. 1995. Phospholipid signaling. Cell 80: 269-278.
    • (1995) Cell , vol.80 , pp. 269-278
    • Divecha, N.1    Irvine, R.F.2
  • 13
    • 0025941361 scopus 로고
    • An efficient transformation procedure enabling long-term storage of competent cells of various yeast genera
    • Dohmen, R.J., Strasser, A.W.M., Hoener, C.B. and Hollenberg, C.P. 1991. An efficient transformation procedure enabling long-term storage of competent cells of various yeast genera. Yeast 7: 691-692.
    • (1991) Yeast , vol.7 , pp. 691-692
    • Dohmen, R.J.1    Strasser, A.W.M.2    Hoener, C.B.3    Hollenberg, C.P.4
  • 14
    • 0000247297 scopus 로고
    • Plant phosphoinositides and intracellular signaling
    • Drøbak, B.K. 1993. Plant phosphoinositides and intracellular signaling. Plant Physiol. 102: 705-709.
    • (1993) Plant Physiol. , vol.102 , pp. 705-709
    • Drøbak, B.K.1
  • 16
    • 0020539016 scopus 로고
    • Phosphatidylinositol biosynthesis in Saccharomyces cerevisiae: Purification and properties of microsome-associated phosphatidylinositol synthase
    • Fischl, A.S. and Carman, G.M. 1983. Phosphatidylinositol biosynthesis in Saccharomyces cerevisiae: purification and properties of microsome-associated phosphatidylinositol synthase. J. Bact. 154: 304-311.
    • (1983) J. Bact. , vol.154 , pp. 304-311
    • Fischl, A.S.1    Carman, G.M.2
  • 17
    • 0022974684 scopus 로고
    • Phosphatidylinositol synthase from Saccharomyces cerevisiae -reconstitution, characterization and regulation of activity
    • Fischl, A.S., Homann, M.J., Poole, M.A. and Carman, G.M. 1986. Phosphatidylinositol synthase from Saccharomyces cerevisiae -reconstitution, characterization and regulation of activity. J. Biol. Chem. 261: 3178-3183.
    • (1986) J. Biol. Chem. , vol.261 , pp. 3178-3183
    • Fischl, A.S.1    Homann, M.J.2    Poole, M.A.3    Carman, G.M.4
  • 18
    • 0024266139 scopus 로고
    • New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
    • Gietz, R.D. and Sugino, A. 1988. New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene 74: 527-534.
    • (1988) Gene , vol.74 , pp. 527-534
    • Gietz, R.D.1    Sugino, A.2
  • 19
    • 0031148808 scopus 로고    scopus 로고
    • At-PLC2, a gene encoding phosphoinositide-specific phospholipase C, is constitutively expressed in vegetative and floral tissues in Arabidopsis thaliana
    • Hirayama, T., Mitsukawa, N., Shibata, D. and Shinozaki, K. 1997. At-PLC2, a gene encoding phosphoinositide-specific phospholipase C, is constitutively expressed in vegetative and floral tissues in Arabidopsis thaliana. Plant Mol. Biol. 34: 175-180.
    • (1997) Plant Mol. Biol. , vol.34 , pp. 175-180
    • Hirayama, T.1    Mitsukawa, N.2    Shibata, D.3    Shinozaki, K.4
  • 20
    • 0029061510 scopus 로고
    • A gene encoding a phosphatidyl-specific phospholipase C is induced by dehydration and salt stress in Arabidopsis thaliana
    • Hirayama, T., Ohio, C., Mizoguchi, T. and Shinozaki, K. 1995. A gene encoding a phosphatidyl-specific phospholipase C is induced by dehydration and salt stress in Arabidopsis thaliana. Proc. Natl. Acad. Sci. USA 92: 3903-3907.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3903-3907
    • Hirayama, T.1    Ohio, C.2    Mizoguchi, T.3    Shinozaki, K.4
  • 21
    • 0025805689 scopus 로고
    • sn-1,2-Diacylglycerol choline- and ethanolamine phosphotransferases in Saccharomyces cerevisiae
    • Hjelmstad, R.H. and Bell, R.M. 1991. sn-1,2-Diacylglycerol choline- and ethanolamine phosphotransferases in Saccharomyces cerevisiae. J. Biol. Chem. 266: 5094-5103.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5094-5103
    • Hjelmstad, R.H.1    Bell, R.M.2
  • 22
    • 0025308303 scopus 로고
    • Repression of choline kinase by inositol and choline in Saccharomyces cerevisiae
    • Hosaka, K., Murakami, T., Kodaki, T., Nikawa, J. and Yamashita, S. 1990. Repression of choline kinase by inositol and choline in Saccharomyces cerevisiae. J. Bact. 172: 2005-2112.
    • (1990) J. Bact. , vol.172 , pp. 2005-2112
    • Hosaka, K.1    Murakami, T.2    Kodaki, T.3    Nikawa, J.4    Yamashita, S.5
  • 23
    • 0023105540 scopus 로고
    • Independent phosphatidylinositol synthesis in pituitary plasma membrane and endoplasmic reticulum
    • Imai, A. and Gershengorn, M.C. 1987. Independent phosphatidylinositol synthesis in pituitary plasma membrane and endoplasmic reticulum. Nature: 325: 726-728.
    • (1987) Nature , vol.325 , pp. 726-728
    • Imai, A.1    Gershengorn, M.C.2
  • 24
    • 0028919469 scopus 로고
    • Compared selectivities of the phosphatidylinositol-synthase from maize coleoptiles either in microsomal membranes or after solubilization
    • Justin, A.-M., Hmyene, A., Kader, J.-C. and Mazliak, P. 1995. Compared selectivities of the phosphatidylinositol-synthase from maize coleoptiles either in microsomal membranes or after solubilization. Biochim. Biophys. Acta 1255: 161-166.
    • (1995) Biochim. Biophys. Acta , vol.1255 , pp. 161-166
    • Justin, A.-M.1    Hmyene, A.2    Kader, J.-C.3    Mazliak, P.4
  • 25
    • 0031797656 scopus 로고    scopus 로고
    • Reduced inositol content and altered morphology in transgenic potato plants inhibited for ID-myo-inositol 3-phosphate synthase
    • Keller, R., Brearley, C.A., Trethewey, R.N. and Müller-Röber, B. 1998. Reduced inositol content and altered morphology in transgenic potato plants inhibited for ID-myo-inositol 3-phosphate synthase. Plant J. 16: 403-410.
    • (1998) Plant J. , vol.16 , pp. 403-410
    • Keller, R.1    Brearley, C.A.2    Trethewey, R.N.3    Müller-Röber, B.4
  • 26
    • 0027512155 scopus 로고
    • Characterization of reactions catalysed by yeast phosphatidylinositol synthase
    • Klezovitch, O., Brandenburger, Y., Geindre, M. and Deshusses, J. 1993. Characterization of reactions catalysed by yeast phosphatidylinositol synthase. FEBS Lett. 320: 256-260.
    • (1993) FEBS Lett. , vol.320 , pp. 256-260
    • Klezovitch, O.1    Brandenburger, Y.2    Geindre, M.3    Deshusses, J.4
  • 27
    • 0031105938 scopus 로고    scopus 로고
    • Complementary DNAs encoding eukaryotic-type cytidine-5′-diphosphate-diacylglycerol synthases of two plant species
    • Kopka, J., Ludewig, M. and Müller-Röber, B. 1997a. Complementary DNAs encoding eukaryotic-type cytidine-5′-diphosphate-diacylglycerol synthases of two plant species. Plant Physiol. 113: 997-1002.
    • (1997) Plant Physiol. , vol.113 , pp. 997-1002
    • Kopka, J.1    Ludewig, M.2    Müller-Röber, B.3
  • 28
    • 0031127339 scopus 로고    scopus 로고
    • Potato guard cells respond to drying soil by a complex change in the expression of genes related to carbon metabolism and turgor regulation
    • Kopka, J., Provart, N.J. and Müller-Röber, B. 1997b. Potato guard cells respond to drying soil by a complex change in the expression of genes related to carbon metabolism and turgor regulation. Plant J. 11: 871-882.
    • (1997) Plant J. , vol.11 , pp. 871-882
    • Kopka, J.1    Provart, N.J.2    Müller-Röber, B.3
  • 29
    • 0031788164 scopus 로고    scopus 로고
    • Molecular and enzymatic characterization of three phosphoinositide-specific phospholipase C isoforms from potato
    • Kopka, J., Pical, C., Gray, J.E. and Müller-Röber, B. 1998. Molecular and enzymatic characterization of three phosphoinositide-specific phospholipase C isoforms from potato. Plant Physiol. 116: 239-250.
    • (1998) Plant Physiol. , vol.116 , pp. 239-250
    • Kopka, J.1    Pical, C.2    Gray, J.E.3    Müller-Röber, B.4
  • 30
    • 0028894710 scopus 로고
    • Functional analysis of mutations in the PIS gene, which encodes Saccharomyces cerevisiae phosphatidylinositol synthase
    • Kumano, Y. and Nikawa, J. 1995. Functional analysis of mutations in the PIS gene, which encodes Saccharomyces cerevisiae phosphatidylinositol synthase. FEMS Microbiol. Lett. 126: 81-84.
    • (1995) FEMS Microbiol. Lett. , vol.126 , pp. 81-84
    • Kumano, Y.1    Nikawa, J.2
  • 31
    • 0029588457 scopus 로고
    • Phospholipidsynthesizing enzymes in Golgi membranes of the yeast, Saccharomyces cerevisiae
    • Leber, A., Hrastnik, C. and Daum, G. 1995. Phospholipidsynthesizing enzymes in Golgi membranes of the yeast, Saccharomyces cerevisiae. FEBS Lett. 377: 271-274.
    • (1995) FEBS Lett. , vol.377 , pp. 271-274
    • Leber, A.1    Hrastnik, C.2    Daum, G.3
  • 32
    • 0023654956 scopus 로고
    • Improved method for the isolation of RNA from plant tissues
    • Logemann, J., Schell, J. and Willmitzer, L. 1987. Improved method for the isolation of RNA from plant tissues. Anal. Biochem. 163: 21-26.
    • (1987) Anal. Biochem. , vol.163 , pp. 21-26
    • Logemann, J.1    Schell, J.2    Willmitzer, L.3
  • 33
    • 0031455170 scopus 로고    scopus 로고
    • The role of CDP-diacylglycerol synthase and phosphatidylinositol synthase activity levels in the regulation of cellular phosphatidylinositol content
    • Lykidis, A.D., Jackson, P.D., Rock, C.O. and Jackowski, S. 1997. The role of CDP-diacylglycerol synthase and phosphatidylinositol synthase activity levels in the regulation of cellular phosphatidylinositol content. J. Biol. Chem. 272: 33402-33409.
    • (1997) J. Biol. Chem. , vol.272 , pp. 33402-33409
    • Lykidis, A.D.1    Jackson, P.D.2    Rock, C.O.3    Jackowski, S.4
  • 34
    • 0032143402 scopus 로고    scopus 로고
    • A gene encoding phosphatidylinositol-4-phosphate 5-kinase is induced by water stress and abscisic acid in Arabidopsis thaliana
    • Mikami, K., Katagiri, T., Iuchi, S., Yamaguchi-Shinozaki, K. and Shinozaki, K. 1998. A gene encoding phosphatidylinositol-4-phosphate 5-kinase is induced by water stress and abscisic acid in Arabidopsis thaliana. Plant J. 15: 563-568.
    • (1998) Plant J. , vol.15 , pp. 563-568
    • Mikami, K.1    Katagiri, T.2    Iuchi, S.3    Yamaguchi-Shinozaki, K.4    Shinozaki, K.5
  • 35
    • 0027984472 scopus 로고
    • Identification of rat liver phosphatidylinositol synthase as a 21 kDa protein
    • Monaco, M.E., Feldman, M. and Kleinberg, D.L. 1994. Identification of rat liver phosphatidylinositol synthase as a 21 kDa protein. Biochem. J. 304: 301-305.
    • (1994) Biochem. J. , vol.304 , pp. 301-305
    • Monaco, M.E.1    Feldman, M.2    Kleinberg, D.L.3
  • 37
    • 0019980518 scopus 로고
    • Yeast mutant defective in synthesis of phosphatidylinositol
    • Nikawa, J. and Yamashita, S. 1982. Yeast mutant defective in synthesis of phosphatidylinositol. Eur. J. Biochem. 125: 445-451.
    • (1982) Eur. J. Biochem. , vol.125 , pp. 445-451
    • Nikawa, J.1    Yamashita, S.2
  • 38
    • 0021754350 scopus 로고
    • Molecular cloning of the gene encoding CDPdiacylglycerol-inositol 3-phosphatidyl transferase in Saccharomyces cerevisiae
    • Nikawa, J. and Yamashita, S. 1984. Molecular cloning of the gene encoding CDPdiacylglycerol-inositol 3-phosphatidyl transferase in Saccharomyces cerevisiae. Eur. J. Biochem. 143: 251-256.
    • (1984) Eur. J. Biochem. , vol.143 , pp. 251-256
    • Nikawa, J.1    Yamashita, S.2
  • 39
    • 0023214019 scopus 로고
    • Primary structure and disruption of the phosphatidylinositol synthase gene of Saccharomyces cerevisiae
    • Nikawa, J., Kodaki, T. and Yamashita, S. 1987. Primary structure and disruption of the phosphatidylinositol synthase gene of Saccharomyces cerevisiae. J. Biol. Chem. 262: 4876-4881.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4876-4881
    • Nikawa, J.1    Kodaki, T.2    Yamashita, S.3
  • 40
    • 0024095856 scopus 로고
    • Expression of the Saccharomyces cerevisiae PIS gene and synthesis of phosphatidylinositol in Escherichia coli
    • Nikawa, J., Kodaki, T. and Yamashita, S. 1988. Expression of the Saccharomyces cerevisiae PIS gene and synthesis of phosphatidylinositol in Escherichia coli. J. Bact. 170: 4727-4731.
    • (1988) J. Bact. , vol.170 , pp. 4727-4731
    • Nikawa, J.1    Kodaki, T.2    Yamashita, S.3
  • 41
    • 0021770867 scopus 로고
    • Phosphatidylinositol synthase from canine pancreas: Solubilization by n-octyl gulcopyranoside and stabilization by manganese
    • Parries, G. and Hokin-Neaverson, M 1984. Phosphatidylinositol synthase from canine pancreas: solubilization by n-octyl gulcopyranoside and stabilization by manganese. Biochemistry 23: 4785-4791.
    • (1984) Biochemistry , vol.23 , pp. 4785-4791
    • Parries, G.1    Hokin-Neaverson, M.2
  • 42
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson, W.R. and Lipman, D.J. 1988. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA 85: 2444-2448.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 43
    • 0025015267 scopus 로고
    • Role of phosphoinositides in transmembrane signaling
    • Rana, R.S. and Hokin, L.E. 1990. Role of phosphoinositides in transmembrane signaling. Physiol. Rev. 70: 115-164.
    • (1990) Physiol. Rev. , vol.70 , pp. 115-164
    • Rana, R.S.1    Hokin, L.E.2
  • 45
    • 0000336167 scopus 로고    scopus 로고
    • An Arabidopsis phosphatidylinositol-4-phosphate 5-kinase homolog with seven novel repeats rich in aromatic and glycine residues
    • PGR 97-150
    • Satterlee, J.S. and Sussman, M.R. 1997. An Arabidopsis phosphatidylinositol-4-phosphate 5-kinase homolog with seven novel repeats rich in aromatic and glycine residues. Plant Physiol. 115: 864 (PGR 97-150).
    • (1997) Plant Physiol. , vol.115 , pp. 864
    • Satterlee, J.S.1    Sussman, M.R.2
  • 46
    • 0029360601 scopus 로고
    • Characterization of a plasma membrane-associated phosphoinositide-specific phospholipase C from soybean
    • Shi, J., Gonzales, R.A. and Bhattacharyya, M.K. 1995. Characterization of a plasma membrane-associated phosphoinositide-specific phospholipase C from soybean. Plant J. 8: 381-390.
    • (1995) Plant J. , vol.8 , pp. 381-390
    • Shi, J.1    Gonzales, R.A.2    Bhattacharyya, M.K.3
  • 47
    • 0017664467 scopus 로고
    • CDP-diglyceride: Inositol transferase from rat liver
    • Takenawa, T. and Egawa, K. 1977. CDP-diglyceride: inositol transferase from rat liver. J. Biol. Chem. 252: 5419-5423.
    • (1977) J. Biol. Chem. , vol.252 , pp. 5419-5423
    • Takenawa, T.1    Egawa, K.2
  • 48
    • 0028286689 scopus 로고
    • Cloning of a cDNa encoding a second phosphatidylinositol transfer protein of rat brain by complementation of the yeast sec14 mutation
    • Tanaka, S. and Hosaka, K. 1994. Cloning of a cDNA encoding a second phosphatidylinositol transfer protein of rat brain by complementation of the yeast sec14 mutation. J. Biochem. 115: 981-984.
    • (1994) J. Biochem. , vol.115 , pp. 981-984
    • Tanaka, S.1    Hosaka, K.2
  • 49
    • 0030576913 scopus 로고    scopus 로고
    • Molecular cloning of rat phosphatidylinositol synthase cDNA by functional complementation of the yeast Saccharomyces cerevisiae pis mutation
    • Tanaka, S., Nikawa, J., Imai, H., Yamashita, S. and Hosaka, K. 1996. Molecular cloning of rat phosphatidylinositol synthase cDNA by functional complementation of the yeast Saccharomyces cerevisiae pis mutation. FEBS Lett. 393: 89-92.
    • (1996) FEBS Lett. , vol.393 , pp. 89-92
    • Tanaka, S.1    Nikawa, J.2    Imai, H.3    Yamashita, S.4    Hosaka, K.5
  • 50
    • 0032577480 scopus 로고    scopus 로고
    • Scanning alanine mutagenesis of the CDP-alcohol phosphotransferase motif of Saccharomyces cerevisiae cholinephosphotransferase
    • Williams, J.G. and McMaster, C.R. 1998. Scanning alanine mutagenesis of the CDP-alcohol phosphotransferase motif of Saccharomyces cerevisiae cholinephosphotransferase. J. Biol. Chem. 273: 13482-13487.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13482-13487
    • Williams, J.G.1    McMaster, C.R.2
  • 51
    • 0001909299 scopus 로고
    • Plasma membrane preparations from suspension cultured plant cells contain the enzymes for the recycling of phosphatidic acid and diacylglycerol
    • Wissing, J.B., Grabowski, L., Drewitz, E., Hanenberg, A., Wylegalla, C. and Wagner, K.G. 1992. Plasma membrane preparations from suspension cultured plant cells contain the enzymes for the recycling of phosphatidic acid and diacylglycerol. Plant Sci. 87: 29-37.
    • (1992) Plant Sci. , vol.87 , pp. 29-37
    • Wissing, J.B.1    Grabowski, L.2    Drewitz, E.3    Hanenberg, A.4    Wylegalla, C.5    Wagner, K.G.6
  • 52
    • 0028812325 scopus 로고
    • Regulation of PLC-mediated signalling in vivo by CDP-diacylglycerol synthase
    • Wu, L., Niemeyer, B., Colley, N., Socolich, M. and Zucker, C.S. 1995. Regulation of PLC-mediated signalling in vivo by CDP-diacylglycerol synthase. Nature 373: 216-222.
    • (1995) Nature , vol.373 , pp. 216-222
    • Wu, L.1    Niemeyer, B.2    Colley, N.3    Socolich, M.4    Zucker, C.S.5
  • 53
    • 0033605257 scopus 로고    scopus 로고
    • A plant 126-kDa phosphatidylinositol 4-kinase with a novel repeat structure: Cloning and functional expression in baculovirus-infected insect cells
    • Xue, H.-W., Pical, C., Brearley, C., Elge, S. and Müller-Röber, B. 1999. A plant 126-kDa phosphatidylinositol 4-kinase with a novel repeat structure: cloning and functional expression in baculovirus-infected insect cells. J. Biol. Chem. 274: 5738-5745.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5738-5745
    • Xue, H.-W.1    Pical, C.2    Brearley, C.3    Elge, S.4    Müller-Röber, B.5
  • 54
    • 0018902403 scopus 로고
    • Regulation of phosphatidylethanolamine methyltransferase level by myo-inositol in Saccharomyces cerevisiae
    • Yamashita, S. and Oshima, A. 1980. Regulation of phosphatidylethanolamine methyltransferase level by myo-inositol in Saccharomyces cerevisiae. Eur. J. Biochem. 104: 611-616.
    • (1980) Eur. J. Biochem. , vol.104 , pp. 611-616
    • Yamashita, S.1    Oshima, A.2


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