메뉴 건너뛰기




Volumn 1348, Issue 1-2, 1997, Pages 45-55

Phosphatidate phosphatases and diacylglycerol pyrophosphate phosphatases in Saccharomyces cerevisiae and Escherichia coli

Author keywords

Bacteria; Diacylglycerol; Diacylglycerol pyrophosphate; Phosphatase; Phosphatidate; Yeast

Indexed keywords

PHOSPHATASE; PHOSPHATIDATE PHOSPHATASE;

EID: 0031552935     PISSN: 00052760     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2760(97)00095-7     Document Type: Review
Times cited : (70)

References (58)
  • 1
    • 0000456009 scopus 로고
    • The enzymatic dephosphorylation of phosphatidic acids
    • Smith S.W., Weiss S.B., Kennedy E.P. The enzymatic dephosphorylation of phosphatidic acids. J. Biol. Chem. 228:1957;915-922.
    • (1957) J. Biol. Chem. , vol.228 , pp. 915-922
    • Smith, S.W.1    Weiss, S.B.2    Kennedy, E.P.3
  • 2
    • 0021770019 scopus 로고
    • Regulatory role of phosphatidate phosphatase in triacylglycerol synthesis of Saccharomyces cerevisiae
    • Hosaka K., Yamashita S. Regulatory role of phosphatidate phosphatase in triacylglycerol synthesis of Saccharomyces cerevisiae. Biochim. Biophys. Acta. 796:1984;110-117.
    • (1984) Biochim. Biophys. Acta , vol.796 , pp. 110-117
    • Hosaka, K.1    Yamashita, S.2
  • 3
    • 0021770023 scopus 로고
    • Partial purification and properties of phosphatidate phosphatase in Saccharomyces cerevisiae
    • Hosaka K., Yamashita S. Partial purification and properties of phosphatidate phosphatase in Saccharomyces cerevisiae. Biochim. Biophys. Acta. 796:1984;102-109.
    • (1984) Biochim. Biophys. Acta , vol.796 , pp. 102-109
    • Hosaka, K.1    Yamashita, S.2
  • 4
    • 0024058719 scopus 로고
    • Regulation of phosphatidate phosphatase activity by inositol in Saccharomyces cerevisiae
    • Morlock K.R., Lin Y.-P., Carman G.M. Regulation of phosphatidate phosphatase activity by inositol in Saccharomyces cerevisiae. J. Bacteriol. 170:1988;3561-3566.
    • (1988) J. Bacteriol. , vol.170 , pp. 3561-3566
    • Morlock, K.R.1    Lin, Y.-P.2    Carman, G.M.3
  • 5
    • 0002644373 scopus 로고
    • in: J.A.F. Op den Kamp, B. Roelofsen, B., K.W.A. Wirtz (Eds.) Elsevier Science Publishers B.V., Amsterdam
    • E.P. Kennedy, in: J.A.F. Op den Kamp, B. Roelofsen, B., K.W.A. Wirtz (Eds.), Lipids and Membranes: Past, Present and Future, Elsevier Science Publishers B.V., Amsterdam, 1986, pp. 171-206.
    • (1986) Lipids and Membranes: Past, Present and Future , pp. 171-206
    • E.P. Kennedy1
  • 6
    • 0029920267 scopus 로고    scopus 로고
    • Regulation of phospholipid biosynthesis in the yeast Saccharomyces cerevisiae
    • Carman G.M., Zeimetz G.M. Regulation of phospholipid biosynthesis in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 271:1996;13293-13296.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13293-13296
    • Carman, G.M.1    Zeimetz, G.M.2
  • 7
    • 0000749205 scopus 로고
    • The function of cytidine coenzyme in the biosynthesis of phospholipids
    • Kennedy E.P., Weiss S.B. The function of cytidine coenzyme in the biosynthesis of phospholipids. J. Biol. Chem. 222:1956;193-214.
    • (1956) J. Biol. Chem. , vol.222 , pp. 193-214
    • Kennedy, E.P.1    Weiss, S.B.2
  • 8
    • 0024339246 scopus 로고
    • Purification and characterization of phosphatidate phosphatase from Saccharomyces cerevisiae
    • Lin Y.-P., Carman G.M. Purification and characterization of phosphatidate phosphatase from Saccharomyces cerevisiae. J. Biol. Chem. 264:1989;8641-8645.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8641-8645
    • Lin, Y.-P.1    Carman, G.M.2
  • 9
    • 0025894167 scopus 로고
    • Phosphatidate phosphatase from Saccharomyces cerevisiae. Isolation of 45-kDa and 104-kDa forms of the enzyme that are differentially regulated by inositol
    • Morlock K.R., McLaughlin J.J., Lin Y.-P., Carman G.M. Phosphatidate phosphatase from Saccharomyces cerevisiae. Isolation of 45-kDa and 104-kDa forms of the enzyme that are differentially regulated by inositol. J. Biol. Chem. 266:1991;3586-3593.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3586-3593
    • Morlock, K.R.1    McLaughlin, J.J.2    Lin, Y.-P.3    Carman, G.M.4
  • 10
    • 0025162158 scopus 로고
    • Kinetic analysis of yeast phosphatidate phosphatase toward Triton X-100/phosphatidate mixed micelles
    • Lin Y.-P., Carman G.M. Kinetic analysis of yeast phosphatidate phosphatase toward Triton X-100/phosphatidate mixed micelles. J. Biol. Chem. 265:1990;166-170.
    • (1990) J. Biol. Chem. , vol.265 , pp. 166-170
    • Lin, Y.-P.1    Carman, G.M.2
  • 11
    • 0029130345 scopus 로고
    • Lipid signaling enzymes and surface dilution kinetics
    • Carman G.M., Deems R.A., Dennis E.A. Lipid signaling enzymes and surface dilution kinetics. J. Biol. Chem. 270:1995;18711-18714.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18711-18714
    • Carman, G.M.1    Deems, R.A.2    Dennis, E.A.3
  • 12
    • 0027192315 scopus 로고
    • Regulation of phosphatidate phosphatase activity from the yeast Saccharomyces cerevisiae by sphingoid bases
    • Wu W., Lin Y.-P., Wang E., Merrill A.H. Jr., Carman G.M. Regulation of phosphatidate phosphatase activity from the yeast Saccharomyces cerevisiae by sphingoid bases. J. Biol. Chem. 268:1993;13830-13837.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13830-13837
    • Wu, W.1    Lin, Y.-P.2    Wang, E.3    Merrill A.H., Jr.4    Carman, G.M.5
  • 13
    • 0025253769 scopus 로고
    • The function of RAS genes in Saccharomyces cerevisiae
    • Broach J.R., Deschenes R.J. The function of RAS genes in Saccharomyces cerevisiae. Adv. Cancer Res. 54:1990;79-139.
    • (1990) Adv. Cancer Res. , vol.54 , pp. 79-139
    • Broach, J.R.1    Deschenes, R.J.2
  • 14
    • 0026644415 scopus 로고
    • The 45-kDa and 104-kDa forms of phosphatidate phosphatase from Saccharomyces cerevisiae are regulated differentially by phosphorylation via cAMP-dependent protein kinase
    • Quinlan J.J., Nickels J.T. Jr., Wu W., Lin Y.-P., Broach J.R., Carman G.M. The 45-kDa and 104-kDa forms of phosphatidate phosphatase from Saccharomyces cerevisiae are regulated differentially by phosphorylation via cAMP-dependent protein kinase. J. Biol. Chem. 267:1992;18013-18020.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18013-18020
    • Quinlan, J.J.1    Nickels J.T., Jr.2    Wu, W.3    Lin, Y.-P.4    Broach, J.R.5    Carman, G.M.6
  • 15
    • 0025361043 scopus 로고
    • SRV2, a gene required for RAS activation of adenylate cyclase in yeast
    • Fedor-Chaiken M., Deschenes R.J., Broach J. SRV2, a gene required for RAS activation of adenylate cyclase in yeast. Cell. 61:1990;329-340.
    • (1990) Cell , vol.61 , pp. 329-340
    • Fedor-Chaiken, M.1    Deschenes, R.J.2    Broach, J.3
  • 16
    • 0028150667 scopus 로고
    • Regulation of phosphatidate phosphatase activity from the yeast Saccharomyces cerevisiae by nucleotides
    • Wu W.-I., Carman G.M. Regulation of phosphatidate phosphatase activity from the yeast Saccharomyces cerevisiae by nucleotides. J. Biol. Chem. 269:1994;29495-29501.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29495-29501
    • Wu, W.-I.1    Carman, G.M.2
  • 17
    • 0025829047 scopus 로고
    • Molecular insights into enzymes of membrane bilayer assembly
    • Hjelmstad R.H., Bell R.M. Molecular insights into enzymes of membrane bilayer assembly. Biochemistry. 30:1991;1731-1740.
    • (1991) Biochemistry , vol.30 , pp. 1731-1740
    • Hjelmstad, R.H.1    Bell, R.M.2
  • 18
    • 0029897877 scopus 로고    scopus 로고
    • Regulation of phosphatidate phosphatase activity from the yeast Saccharomyces cerevisiae by phospholipids
    • Wu W.-I., Carman G.M. Regulation of phosphatidate phosphatase activity from the yeast Saccharomyces cerevisiae by phospholipids. Biochemistry. 35:1996;3790-3796.
    • (1996) Biochemistry , vol.35 , pp. 3790-3796
    • Wu, W.-I.1    Carman, G.M.2
  • 19
    • 0024541436 scopus 로고
    • Function of sphingolipids and sphingolipid breakdown in cellular regulation
    • Hannun Y.A., Bell R.M. Function of sphingolipids and sphingolipid breakdown in cellular regulation. Science. 243:1989;500-507.
    • (1989) Science , vol.243 , pp. 500-507
    • Hannun, Y.A.1    Bell, R.M.2
  • 20
    • 0026022563 scopus 로고
    • Cell regulation by sphingosine and more complex sphingolipids
    • Merrill A.H. Jr. Cell regulation by sphingosine and more complex sphingolipids. J. Bioenerg. Biomembr. 23:1991;83-104.
    • (1991) J. Bioenerg. Biomembr. , vol.23 , pp. 83-104
    • Merrill A.H., Jr.1
  • 21
    • 0028296793 scopus 로고
    • Phosphatidylcholine breakdown and signal transduction
    • Exton J.H. Phosphatidylcholine breakdown and signal transduction. Biochim. Biophys. Acta. 1212:1994;26-42.
    • (1994) Biochim. Biophys. Acta , vol.1212 , pp. 26-42
    • Exton, J.H.1
  • 22
    • 0018651858 scopus 로고
    • Triacylglycerol metabolism in Saccharomyces cerevisiae relation to phospholipid synthesis
    • Taylor F.R., Parks L.W. Triacylglycerol metabolism in Saccharomyces cerevisiae relation to phospholipid synthesis. Biochim. Biophys. Acta. 575:1979;204-214.
    • (1979) Biochim. Biophys. Acta , vol.575 , pp. 204-214
    • Taylor, F.R.1    Parks, L.W.2
  • 23
    • 0022998293 scopus 로고
    • Regulation of phosphatidylserine synthase from Saccharomyces cerevisiae by phospholipid precursors
    • Poole M.A., Homann M.J., Bae-Lee M., Carman G.M. Regulation of phosphatidylserine synthase from Saccharomyces cerevisiae by phospholipid precursors. J. Bacteriol. 168:1986;668-672.
    • (1986) J. Bacteriol. , vol.168 , pp. 668-672
    • Poole, M.A.1    Homann, M.J.2    Bae-Lee, M.3    Carman, G.M.4
  • 24
    • 0023073676 scopus 로고
    • The membrane-associated enzyme phosphatidylserine synthase of yeast is regulated at the level of mRNA abundance
    • Bailis A.M., Poole M.A., Carman G.M., Henry S.A. The membrane-associated enzyme phosphatidylserine synthase of yeast is regulated at the level of mRNA abundance. Mol. Cell. Biol. 7:1987;167-176.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 167-176
    • Bailis, A.M.1    Poole, M.A.2    Carman, G.M.3    Henry, S.A.4
  • 25
    • 0023768355 scopus 로고
    • Phosphorylation of yeast phosphatidylserine synthase in vivo and in vitro by cyclic AMP-dependent protein kinase
    • Kinney A.J., Carman G.M. Phosphorylation of yeast phosphatidylserine synthase in vivo and in vitro by cyclic AMP-dependent protein kinase. Proc. Natl. Acad. Sci. USA. 85:1988;7962-7966.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7962-7966
    • Kinney, A.J.1    Carman, G.M.2
  • 26
    • 0025344428 scopus 로고
    • Regulation of yeast phosphatidylserine synthase and phosphatidylinositol synthase activities by phospholipids in Triton X-100/phospholipid mixed micelles
    • Bae-Lee M., Carman G.M. Regulation of yeast phosphatidylserine synthase and phosphatidylinositol synthase activities by phospholipids in Triton X-100/phospholipid mixed micelles. J. Biol. Chem. 265:1990;7221-7226.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7221-7226
    • Bae-Lee, M.1    Carman, G.M.2
  • 27
    • 0027507073 scopus 로고
    • Diacylglycerol pyrophosphate, a novel phospholipid compound
    • Wissing J.B., Behrbohm H. Diacylglycerol pyrophosphate, a novel phospholipid compound. FEBS Lett. 315:1993;95-99.
    • (1993) FEBS Lett. , vol.315 , pp. 95-99
    • Wissing, J.B.1    Behrbohm, H.2
  • 28
    • 0030800717 scopus 로고    scopus 로고
    • Metabolism of diacylglycerol pyrophosphate by suspension cultured Catharanthus roseus cells.
    • Identification and characterization of diacylglycerol pyrophosphatase phosphatase in plants in press.
    • B. Riedel, M. Morr, W.-I. Wu, G.M. Carman, J.B. Wissing, Metabolism of diacylglycerol pyrophosphate by suspension cultured Catharanthus roseus cells. Identification and characterization of diacylglycerol pyrophosphatase phosphatase in plants, Plant Sci. (1997) in press.
    • (1997) Plant Sci.
    • B. Riedel1    M. Morr2    W.-I. Wu3    G.M. Carman4    J.B. Wissing5
  • 29
    • 0030032698 scopus 로고    scopus 로고
    • Purification and characterization of diacylglycerol pyrophosphate phosphatase from Saccharomyces cerevisiae
    • Wu W.-I., Liu Y., Riedel B., Wissing J.B., Fischl A.S., Carman G.M. Purification and characterization of diacylglycerol pyrophosphate phosphatase from Saccharomyces cerevisiae. J. Biol. Chem. 271:1996;1868-1876.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1868-1876
    • Wu, W.-I.1    Liu, Y.2    Riedel, B.3    Wissing, J.B.4    Fischl, A.S.5    Carman, G.M.6
  • 30
    • 0001512621 scopus 로고
    • Fatty acyl-CoA and fatty acyl-acyl carrier protein as acyl donors in the synthesis of lyso-phosphatidate and phosphatidate in Escherichia coli
    • Van den Bosch H., Vagelos P.R. Fatty acyl-CoA and fatty acyl-acyl carrier protein as acyl donors in the synthesis of lyso-phosphatidate and phosphatidate in Escherichia coli. Biochim. Biophys. Acta. 218:1970;233-248.
    • (1970) Biochim. Biophys. Acta , vol.218 , pp. 233-248
    • Van den Bosch, H.1    Vagelos, P.R.2
  • 31
    • 0020657183 scopus 로고
    • Multiple genes for membrane-bound phosphatases in Escherichia coli and their action on phospholipid precursors
    • Icho T., Raetz C.R.H. Multiple genes for membrane-bound phosphatases in Escherichia coli and their action on phospholipid precursors. J. Bacteriol. 153:1983;722-730.
    • (1983) J. Bacteriol. , vol.153 , pp. 722-730
    • Icho, T.1    Raetz, C.R.H.2
  • 32
    • 0024110267 scopus 로고
    • Membrane-bound phosphatases in Escherichia coli: Sequence of the pgpB gene and dual subcellular localization of the pgpB product
    • Icho T. Membrane-bound phosphatases in Escherichia coli: Sequence of the pgpB gene and dual subcellular localization of the pgpB product. J. Bacteriol. 170:1988;5117-5124.
    • (1988) J. Bacteriol. , vol.170 , pp. 5117-5124
    • Icho, T.1
  • 33
    • 0026597155 scopus 로고
    • The pgpA and pgpB genes of Escherichia coli are not essential: Evidence for a third phosphatidylglycerophosphate phosphatase
    • Funk C.R., Zimniak L., Dowhan W. The pgpA and pgpB genes of Escherichia coli are not essential: Evidence for a third phosphatidylglycerophosphate phosphatase. J. Bacteriol. 174:1992;205-213.
    • (1992) J. Bacteriol. , vol.174 , pp. 205-213
    • Funk, C.R.1    Zimniak, L.2    Dowhan, W.3
  • 34
    • 0029828862 scopus 로고    scopus 로고
    • The Escherichia coli pgpB gene encodes for a diacylglycerol pyrophosphate phosphatase activity
    • Dillon D.A., Wu W.-I., Riedel B., Wissing J.B., Dowhan W., Carman G.M. The Escherichia coli pgpB gene encodes for a diacylglycerol pyrophosphate phosphatase activity. J. Biol. Chem. 271:1996;30548-30553.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30548-30553
    • Dillon, D.A.1    Wu, W.-I.2    Riedel, B.3    Wissing, J.B.4    Dowhan, W.5    Carman, G.M.6
  • 36
    • 0031048876 scopus 로고    scopus 로고
    • Identification of a novel phosphatase sequence motif
    • Stukey J., Carman G.M. Identification of a novel phosphatase sequence motif. Protein Sci. 6:1997;1-4.
    • (1997) Protein Sci. , vol.6 , pp. 1-4
    • Stukey, J.1    Carman, G.M.2
  • 37
    • 0029744530 scopus 로고    scopus 로고
    • 2-inducible hic53 clone yielded the cDNA encoding phosphatidic acid phosphatase
    • 2-inducible hic53 clone yielded the cDNA encoding phosphatidic acid phosphatase. J. Biol. Chem. 271:1996;18931-18938.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18931-18938
    • Kai, M.1    Wada, I.2    Imai, S.3    Sakane, F.4    Kanoh, H.5
  • 38
    • 0021566523 scopus 로고
    • Intracellular translocation of phosphatidate phosphohydrolase and its possible role in the control of glycerolipid synthesis
    • Brindley D.N. Intracellular translocation of phosphatidate phosphohydrolase and its possible role in the control of glycerolipid synthesis. Prog. Lipid Res. 23:1984;115-133.
    • (1984) Prog. Lipid Res. , vol.23 , pp. 115-133
    • Brindley, D.N.1
  • 39
    • 0029835107 scopus 로고    scopus 로고
    • Phosphatidate phosphatases of mammals, yeast, and higher plants
    • Kocsis M.G., Weselake R.J. Phosphatidate phosphatases of mammals, yeast, and higher plants. Lipids. 31:1996;785-802.
    • (1996) Lipids , vol.31 , pp. 785-802
    • Kocsis, M.G.1    Weselake, R.J.2
  • 41
    • 0025774977 scopus 로고
    • Plasma membrane fractions from rat liver contain a phosphatidate phosphohydrolase distinct from that in the endoplasmic reticulum and cytosol
    • Jamal Z., Martin A., Gomez-Munoz A., Brindley D.N. Plasma membrane fractions from rat liver contain a phosphatidate phosphohydrolase distinct from that in the endoplasmic reticulum and cytosol. J. Biol. Chem. 266:1991;2988-2996.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2988-2996
    • Jamal, Z.1    Martin, A.2    Gomez-Munoz, A.3    Brindley, D.N.4
  • 42
    • 0029888864 scopus 로고    scopus 로고
    • Phosphatidate phosphohydrolase and signal transduction
    • Brindley D.N., Waggoner D.W. Phosphatidate phosphohydrolase and signal transduction. Chem. Phys. Lipids. 80:1996;45-57.
    • (1996) Chem. Phys. Lipids , vol.80 , pp. 45-57
    • Brindley, D.N.1    Waggoner, D.W.2
  • 43
    • 0029127249 scopus 로고
    • Purification and characterization of a novel plasma membrane phosphatidate phosphohydrolase from rat liver
    • Waggoner D.W., Martin A., Dewald J., Gomez-Munoz A., Brindley D.N. Purification and characterization of a novel plasma membrane phosphatidate phosphohydrolase from rat liver. J. Biol. Chem. 270:1995;19422-19429.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19422-19429
    • Waggoner, D.W.1    Martin, A.2    Dewald, J.3    Gomez-Munoz, A.4    Brindley, D.N.5
  • 44
    • 0029024743 scopus 로고
    • Purification and characterization of N-ethylmaleimide-insensitive phosphatidic acid phosphohydrolase (PAP2) from rat liver
    • Fleming I.N., Yeaman S.J. Purification and characterization of N-ethylmaleimide-insensitive phosphatidic acid phosphohydrolase (PAP2) from rat liver. Biochem. J. 308:1995;983-989.
    • (1995) Biochem. J. , vol.308 , pp. 983-989
    • Fleming, I.N.1    Yeaman, S.J.2
  • 45
    • 0030012094 scopus 로고    scopus 로고
    • Identification of phosphatidate phosphohydrolase purified from rat liver membranes on SDS-polyacrylamide gel electrophoresis
    • Siess E.A., Hofstetter M.M. Identification of phosphatidate phosphohydrolase purified from rat liver membranes on SDS-polyacrylamide gel electrophoresis. FEBS Lett. 381:1996;169-173.
    • (1996) FEBS Lett. , vol.381 , pp. 169-173
    • Siess, E.A.1    Hofstetter, M.M.2
  • 46
    • 0026483490 scopus 로고
    • Purification and properties of phosphatidic acid phosphatase from porcine thymus membranes
    • Kanoh H., Imai S., Yamada K., Sakane F. Purification and properties of phosphatidic acid phosphatase from porcine thymus membranes. J. Biol. Chem. 267:1992;25809-25814.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25809-25814
    • Kanoh, H.1    Imai, S.2    Yamada, K.3    Sakane, F.4
  • 48
    • 0000394735 scopus 로고
    • Phosphatidate kinase, a novel enzyme in phospholipid metabolism. Purification, subcellular localization, and occurrence in the plant kingdom
    • Wissing J.B., Behrbohm H. Phosphatidate kinase, a novel enzyme in phospholipid metabolism. Purification, subcellular localization, and occurrence in the plant kingdom. Plant Physiol. 102:1993;1243-1249.
    • (1993) Plant Physiol. , vol.102 , pp. 1243-1249
    • Wissing, J.B.1    Behrbohm, H.2
  • 49
    • 0029899903 scopus 로고    scopus 로고
    • Identification of diacylglycerol pyrophosphate as a novel metabolic product of phosphatidic acid during G-protein activation in plants
    • Munnik T., de Vrije T., Irvine R.F., Musgrave A. Identification of diacylglycerol pyrophosphate as a novel metabolic product of phosphatidic acid during G-protein activation in plants. J. Biol. Chem. 271:1996;15708-15715.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15708-15715
    • Munnik, T.1    De Vrije, T.2    Irvine, R.F.3    Musgrave, A.4
  • 50
    • 0026702008 scopus 로고
    • Inositol lipids in cellular signalling mechanisms
    • Michell R.H. Inositol lipids in cellular signalling mechanisms. Trends Biochem. Sci. 17:1992;274-276.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 274-276
    • Michell, R.H.1
  • 51
    • 0023112474 scopus 로고
    • Inositol lipids and cell proliferation
    • Berridge M.J. Inositol lipids and cell proliferation. Biochim. Biophys. Acta. 907:1987;33-45.
    • (1987) Biochim. Biophys. Acta , vol.907 , pp. 33-45
    • Berridge, M.J.1
  • 53
    • 0025187787 scopus 로고
    • Myo-Inositol metabolites as cellular signals
    • Downes C.P., Macphee C.H. myo-Inositol metabolites as cellular signals. Eur. J. Biochem. 193:1990;1-18.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 1-18
    • Downes, C.P.1    Macphee, C.H.2
  • 54
    • 0028883178 scopus 로고
    • Phospholipid Signal.
    • Divecha N., Irvine R.F. Phospholipid Signal. Cell. 80:1995;269-278.
    • (1995) Cell , vol.80 , pp. 269-278
    • Divecha, N.1    Irvine, R.F.2
  • 56
    • 0030221928 scopus 로고    scopus 로고
    • Phosphatidic acid: A lipid messenger involved in intracellular and extracellular signalling
    • English D. Phosphatidic acid: A lipid messenger involved in intracellular and extracellular signalling. Cell. Signal. 8:1996;341-347.
    • (1996) Cell. Signal , vol.8 , pp. 341-347
    • English, D.1
  • 57
    • 0031021247 scopus 로고    scopus 로고
    • The Drosophila protein Wunen repels migrating germ cells
    • Zhang N., Zhang J., Purcell K., Chen Y., Howard K. The Drosophila protein Wunen repels migrating germ cells. Nature. 385:1997;64-67.
    • (1997) Nature , vol.385 , pp. 64-67
    • Zhang, N.1    Zhang, J.2    Purcell, K.3    Chen, Y.4    Howard, K.5
  • 58
    • 0029910301 scopus 로고    scopus 로고
    • The Dri 42 gene, whose expression is up-regulated during epithelial differentiation, encodes a novel endoplasmic reticulum resident transmembrane protein
    • Barila D., Plateroti M., Nobili F., Muda A.O., Xie Y., Morimoto T., Perozzi G. The Dri 42 gene, whose expression is up-regulated during epithelial differentiation, encodes a novel endoplasmic reticulum resident transmembrane protein. J. Biol. Chem. 271:1996;29928-29936.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29928-29936
    • Barila, D.1    Plateroti, M.2    Nobili, F.3    Muda, A.O.4    Xie, Y.5    Morimoto, T.6    Perozzi, G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.