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Volumn 82, Issue 1, 2004, Pages 113-128

Phospholipid biosynthesis in mammalian cells

Author keywords

Biosynthesis; Phosphatidic acid; Phosphatidylcholine; Phosphatidylethanolamine; Phosphatidylserine

Indexed keywords

BIOSYNTHESIS; GENES; PROTEINS; PURIFICATION;

EID: 2342572271     PISSN: 08298211     EISSN: None     Source Type: Journal    
DOI: 10.1139/o03-073     Document Type: Review
Times cited : (287)

References (210)
  • 1
    • 0032840741 scopus 로고    scopus 로고
    • The unique acyl chain specificity of biliary phosphatidylcholines in mice is independent of their biosynthetic origin in the liver
    • Agellon, L.B., Walkey, C.J., Vance, D.E., Kuipers, F., and Verkade, H.J. 1999. The unique acyl chain specificity of biliary phosphatidylcholines in mice is independent of their biosynthetic origin in the liver. Hepatology, 30: 725-729.
    • (1999) Hepatology , vol.30 , pp. 725-729
    • Agellon, L.B.1    Walkey, C.J.2    Vance, D.E.3    Kuipers, F.4    Verkade, H.J.5
  • 2
    • 0032584511 scopus 로고    scopus 로고
    • Molecular cloning of mouse choline kinase and choline/ethanolamine kinase: Their sequence comparison to the respective rat homologs
    • Aoyama, C., Nakashima, K., and Ishidate, K. 1998. Molecular cloning of mouse choline kinase and choline/ethanolamine kinase: their sequence comparison to the respective rat homologs. Biochim. Biophys. Acta, 1393: 179-185.
    • (1998) Biochim. Biophys. Acta , vol.1393 , pp. 179-185
    • Aoyama, C.1    Nakashima, K.2    Ishidate, K.3
  • 3
    • 0034029156 scopus 로고    scopus 로고
    • Structure and characterization of the genes for murine choline/ethanolamine kinase isozymes alpha and beta
    • Aoyama, C., Yamazaki, N., Terada, H., and Ishidate, K. 2000. Structure and characterization of the genes for murine choline/ethanolamine kinase isozymes alpha and beta. J. Lipid Res. 41: 452-464.
    • (2000) J. Lipid Res. , vol.41 , pp. 452-464
    • Aoyama, C.1    Yamazaki, N.2    Terada, H.3    Ishidate, K.4
  • 4
    • 0036566473 scopus 로고    scopus 로고
    • Expression and characterization of the active molecular forms of choline/ethanolamine kinase-alpha and -beta in mouse tissues, including carbon tetrachloride-induced liver
    • Aoyama, C., Ohtani, A., and Ishidate, K. 2002. Expression and characterization of the active molecular forms of choline/ethanolamine kinase-alpha and -beta in mouse tissues, including carbon tetrachloride-induced liver. Biochem. J. 363: 777-784.
    • (2002) Biochem. J. , vol.363 , pp. 777-784
    • Aoyama, C.1    Ohtani, A.2    Ishidate, K.3
  • 6
    • 0030726780 scopus 로고    scopus 로고
    • Control of membrane phophatidylcholine biosynthesis by diacylglycerol levels in neuronal cells undergoing neunte outgrowth
    • Araki, W., and Wurtman, R.J. 1997. Control of membrane phophatidylcholine biosynthesis by diacylglycerol levels in neuronal cells undergoing neunte outgrowth. Proc. Natl. Acad. Sci. U.S.A. 94: 11 946 - 11 950.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 11946-11950
    • Araki, W.1    Wurtman, R.J.2
  • 7
    • 0025744261 scopus 로고
    • Involvement of contact sites in phosphatidylserine import into liver mitochondria
    • Ardail, D., Lerme, F., and Louisot, P. 1991. Involvement of contact sites in phosphatidylserine import into liver mitochondria. J. Biol. Chem. 266: 7978-7981.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7978-7981
    • Ardail, D.1    Lerme, F.2    Louisot, P.3
  • 8
    • 0026980156 scopus 로고
    • Phospholipid import into mitochondria: Possible regulation mediated through lipid polymorphism
    • Ardail, D., Lerme, F., and Louisot, P. 1992. Phospholipid import into mitochondria: possible regulation mediated through lipid polymorphism. Biochem. Biophys. Res. Commun. 186: 1384-1390.
    • (1992) Biochem. Biophys. Res. Commun. , vol.186 , pp. 1384-1390
    • Ardail, D.1    Lerme, F.2    Louisot, P.3
  • 9
    • 0032541025 scopus 로고    scopus 로고
    • CD95 (Fas/APO-1) induces an increased phosphatidylserine synthesis that preceded its externalization during programmed cell death
    • Aussel, C., Pelassy, C., and Breittmayer, J.P. 1998. CD95 (Fas/APO-1) induces an increased phosphatidylserine synthesis that preceded its externalization during programmed cell death. FEBS Lett. 431: 195-199.
    • (1998) FEBS Lett. , vol.431 , pp. 195-199
    • Aussel, C.1    Pelassy, C.2    Breittmayer, J.P.3
  • 10
    • 0033583584 scopus 로고    scopus 로고
    • Transcriptional activation of the murine CTP:phosphocholine cytidylyltransferase gene (Ctpct): Combined action of upstream stimulatory and inhibitory cis-acting elements
    • Bakovic, M., Waite, K., Tang, W., Tabas, I., and Vance, D.E. 1999. Transcriptional activation of the murine CTP:phosphocholine cytidylyltransferase gene (Ctpct): combined action of upstream stimulatory and inhibitory cis-acting elements. Biochim. Biophys. Acta, 1438: 147-165.
    • (1999) Biochim. Biophys. Acta , vol.1438 , pp. 147-165
    • Bakovic, M.1    Waite, K.2    Tang, W.3    Tabas, I.4    Vance, D.E.5
  • 11
    • 0033994314 scopus 로고    scopus 로고
    • Functional significance of Sp1, Sp2 and Sp3 transcription factors in regulation of the murine CTP:phosphocholine cytidylyltransferase a promoter
    • Bakovic, M., Waite, K.A., and Vance, D.E. 2000. Functional significance of Sp1, Sp2 and Sp3 transcription factors in regulation of the murine CTP:phosphocholine cytidylyltransferase a promoter. J. Lipid Res. 41: 583-594.
    • (2000) J. Lipid Res. , vol.41 , pp. 583-594
    • Bakovic, M.1    Waite, K.A.2    Vance, D.E.3
  • 12
    • 0038150362 scopus 로고    scopus 로고
    • Oncogenic Ha-Ras transformation modulates the transcription of the CTP:phosphocholine cytidylyltransferase alpha gene via p42/44MAPK and transcription factor Sp3
    • Bakovic, M., Waite, K., and Vance, D.E. 2003. Oncogenic Ha-Ras transformation modulates the transcription of the CTP:phosphocholine cytidylyltransferase alpha gene via p42/44MAPK and transcription factor Sp3. J. Biol. Chem. 278: 14 753 - 14 761.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14753-14761
    • Bakovic, M.1    Waite, K.2    Vance, D.E.3
  • 13
    • 0041355204 scopus 로고    scopus 로고
    • Activation of CTP:phosphocholine cytidylyltransferase alpha expression during the S phase of the cell cycle is mediated by the transcription factor Sp1
    • Banchio, C., Schang, L.M., and Vance, D.E. 2003. Activation of CTP:phosphocholine cytidylyltransferase alpha expression during the S phase of the cell cycle is mediated by the transcription factor Sp1. J. Biol. Chem. 278: 32 457 - 32 464.
    • (2003) J. Biol. Chem. , vol.278 , pp. 32457-32464
    • Banchio, C.1    Schang, L.M.2    Vance, D.E.3
  • 15
    • 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 (Lond.), 312: 315-321.
    • (1984) Nature (Lond.) , vol.312 , pp. 315-321
    • Berridge, M.J.1    Irvine, R.F.2
  • 16
    • 0000872680 scopus 로고
    • The effects of the components of lecithine upon deposition of fat in the liver
    • Best, C.H., and Huntsman, M.E. 1932. The effects of the components of lecithine upon deposition of fat in the liver. J. Physiol. 75: 405-412.
    • (1932) J. Physiol. , vol.75 , pp. 405-412
    • Best, C.H.1    Huntsman, M.E.2
  • 18
    • 15844379770 scopus 로고    scopus 로고
    • A phospholipid acts as a chaperone in assembly of a membrane transport protein
    • Bogdanov, M., Sun, J., Kaback, H.R., and Dowhan, W. 1996. A phospholipid acts as a chaperone in assembly of a membrane transport protein. J. Biol. Chem. 271: 11 615 - 11 618.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11615-11618
    • Bogdanov, M.1    Sun, J.2    Kaback, H.R.3    Dowhan, W.4
  • 19
    • 0033617356 scopus 로고    scopus 로고
    • Phospholipid-assisted refolding of an integral membrane protein. Minimum structural features for phosphatidylethanolamine to act as a molecular chaperone
    • Bogdanov, M., Umeda, M., and Dowhan, W. 1999. Phospholipid-assisted refolding of an integral membrane protein. Minimum structural features for phosphatidylethanolamine to act as a molecular chaperone. J. Biol. Chem. 274: 12 339 - 12 345.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12339-12345
    • Bogdanov, M.1    Umeda, M.2    Dowhan, W.3
  • 20
    • 0002360622 scopus 로고
    • Enzymatic formation and decarboxylation of phosphatidylserine
    • Borkenhagen, L.F., Kennedy, E.P., and Fielding, L. 1961. Enzymatic formation and decarboxylation of phosphatidylserine. J. Biol. Chem. 236: 28-32.
    • (1961) J. Biol. Chem. , vol.236 , pp. 28-32
    • Borkenhagen, L.F.1    Kennedy, E.P.2    Fielding, L.3
  • 21
    • 0000226495 scopus 로고
    • The biosynthesis of choline and its relation to phospholipid metabolism. Biochim
    • Bremer, J., Figard, P.H., and Greenberg, D.M. 1960. The biosynthesis of choline and its relation to phospholipid metabolism. Biochim. Biophys. Acta, 43: 477-488.
    • (1960) Biophys. Acta , vol.43 , pp. 477-488
    • Bremer, J.1    Figard, P.H.2    Greenberg, D.M.3
  • 22
    • 0015876764 scopus 로고
    • Membrane structure: Some general principles
    • Wash., D.C.
    • Bretscher, M.S. 1973. Membrane structure: some general principles. Science (Wash., D.C.), 181: 622-629.
    • (1973) Science , vol.181 , pp. 622-629
    • Bretscher, M.S.1
  • 23
    • 0034758197 scopus 로고    scopus 로고
    • Compartmentalization of choline and acetylcholine metabolism in cultured sympathetic neurons
    • Bussiere, M., Vance, J.E., Campenot, R.B., and Vance, D.E. 2001. Compartmentalization of choline and acetylcholine metabolism in cultured sympathetic neurons. J. Biochem. 130: 561-568.
    • (2001) J. Biochem. , vol.130 , pp. 561-568
    • Bussiere, M.1    Vance, J.E.2    Campenot, R.B.3    Vance, D.E.4
  • 24
    • 0242665710 scopus 로고    scopus 로고
    • Enhanced expression and activation of CTP:phosphocholine cytidylyltransferase beta 2 during neunte outgrowth
    • Carter, J.M., Waite, K.A., Campenot, R.B., Vance, J.E., and Vance, D.E. 2003. Enhanced expression and activation of CTP:phosphocholine cytidylyltransferase beta 2 during neunte outgrowth. J. Biol. Chem. 278: 44 988 - 44 994.
    • (2003) J. Biol. Chem. , vol.278 , pp. 44988-44994
    • Carter, J.M.1    Waite, K.A.2    Campenot, R.B.3    Vance, J.E.4    Vance, D.E.5
  • 25
    • 0017645120 scopus 로고
    • Phospholipid synthesis in isolated fat cells
    • Coleman, R.A., and Bell, R.M. 1977. Phospholipid synthesis in isolated fat cells. J. Biol. Chem. 252: 3050-3056.
    • (1977) J. Biol. Chem. , vol.252 , pp. 3050-3056
    • Coleman, R.A.1    Bell, R.M.2
  • 26
    • 0033826433 scopus 로고    scopus 로고
    • Physiological and nutritional regulation of enzymes of triacylglycerol synthesis
    • Coleman, R.A., Lewin, T.M., and Muoio, D.M. 2000. Physiological and nutritional regulation of enzymes of triacylglycerol synthesis. Annu. Rev. Nutr. 20: 77-103.
    • (2000) Annu. Rev. Nutr. , vol.20 , pp. 77-103
    • Coleman, R.A.1    Lewin, T.M.2    Muoio, D.M.3
  • 27
    • 0024364943 scopus 로고
    • Chemical cross-linking reveals a dimeric structure for CTP:phosphocholine cytidylyltransferase
    • Cornell, R. 1989. Chemical cross-linking reveals a dimeric structure for CTP:phosphocholine cytidylyltransferase. J. Biol. Chem. 264: 9077-9082.
    • (1989) J. Biol. Chem. , vol.264 , pp. 9077-9082
    • Cornell, R.1
  • 28
    • 0034284083 scopus 로고    scopus 로고
    • Regulation of CTP:phosphocholine cytidylyltransferase by amphitropism and relocalization
    • Cornell, R.B., and Northwood, I.C. 2000. Regulation of CTP:phosphocholine cytidylyltransferase by amphitropism and relocalization. Trends Biochem. Sci. 25: 441-447.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 441-447
    • Cornell, R.B.1    Northwood, I.C.2
  • 29
    • 0027182769 scopus 로고
    • Cloning and expression of a novel phosphatidylethanolamine N-methyltransferase
    • Cui, Z., Vance, J.E., Chen, M.H., Voelker, D.R., and Vance, D.E. 1993. Cloning and expression of a novel phosphatidylethanolamine N-methyltransferase. J. Biol. Chem. 268: 16 655 - 16 663.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16655-16663
    • Cui, Z.1    Vance, J.E.2    Chen, M.H.3    Voelker, D.R.4    Vance, D.E.5
  • 30
    • 0029610552 scopus 로고
    • Expression of phosphatidylethanolamine N-methyltransferase-2 in McArdle-RH7777 hepatoma cells inhibits the CDP-choline pathway for phosphatidylcholine biosynthesis via decreased gene expression of CTP:phosphocholine cytidylyltransferase
    • Cui, Z., Houweling, M., and Vance, D.E. 1995. Expression of phosphatidylethanolamine N-methyltransferase-2 in McArdle-RH7777 hepatoma cells inhibits the CDP-choline pathway for phosphatidylcholine biosynthesis via decreased gene expression of CTP:phosphocholine cytidylyltransferase. Biochem. J. 312: 939-945.
    • (1995) Biochem. J. , vol.312 , pp. 939-945
    • Cui, Z.1    Houweling, M.2    Vance, D.E.3
  • 31
    • 0026713286 scopus 로고
    • Biosynthesis of glycerolipid precursors in rat liver peroxisomes and their transport and conversion to phosphatidate in the endoplamsic reticulum
    • Das, A.K., Hone, S., and Hajra, A.K. 1992. Biosynthesis of glycerolipid precursors in rat liver peroxisomes and their transport and conversion to phosphatidate in the endoplamsic reticulum. J. Biol. Chem. 267: 9724-9730.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9724-9730
    • Das, A.K.1    Hone, S.2    Hajra, A.K.3
  • 32
    • 0035807063 scopus 로고    scopus 로고
    • Regulation of CTP:phosphocholine cytidylyltransferase activity by the physical properties of lipid membranes: An important role for stored curvature strain energy
    • Davies, S.M., Epand, R.M., Kraayenhof, R., and Cornell, R.B. 2001. Regulation of CTP:phosphocholine cytidylyltransferase activity by the physical properties of lipid membranes: an important role for stored curvature strain energy. Biochemistry, 40: 10 522 - 10 531.
    • (2001) Biochemistry , vol.40 , pp. 10522-10531
    • Davies, S.M.1    Epand, R.M.2    Kraayenhof, R.3    Cornell, R.B.4
  • 33
    • 0033569752 scopus 로고    scopus 로고
    • Molecular distinction of phosphatidylcholine synthesis between the CDP-choline pathway and phosphatidylethanolamine methylation pathway
    • DeLong, C.J., Shen, Y.-J., Thomas, M.J., and Cui, Z. 1999. Molecular distinction of phosphatidylcholine synthesis between the CDP-choline pathway and phosphatidylethanolamine methylation pathway. J. Biol. Chem. 274: 29 683 - 29 688.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29683-29688
    • DeLong, C.J.1    Shen, Y.-J.2    Thomas, M.J.3    Cui, Z.4
  • 34
    • 0025876649 scopus 로고
    • Static and dynamic lipid asymmetry in cell membranes
    • Devaux, P.F. 1991. Static and dynamic lipid asymmetry in cell membranes. Biochemistry, 30: 1163-1173.
    • (1991) Biochemistry , vol.30 , pp. 1163-1173
    • Devaux, P.F.1
  • 35
    • 0031552990 scopus 로고    scopus 로고
    • Mammalian mitochondrial glycerol-3-phosphate acyltransferase
    • Dircks, L.K., and Sul, H.S. 1997. Mammalian mitochondrial glycerol-3-phosphate acyltransferase. Biochim. Biophys. Acta, 1348: 17-26.
    • (1997) Biochim. Biophys. Acta , vol.1348 , pp. 17-26
    • Dircks, L.K.1    Sul, H.S.2
  • 36
    • 0037012907 scopus 로고    scopus 로고
    • Regulation of SREBP processing and membrane lipid production by phospholipids in Drosophila
    • Wash., D.C.
    • Dobrosotskaya, I.Y., Seegmiller, A.C., Brown, M.S., Goldstein, J.L., and Rawson, R.B. 2002. Regulation of SREBP processing and membrane lipid production by phospholipids in Drosophila. Science (Wash., D.C.), 296: 879-883.
    • (2002) Science , vol.296 , pp. 879-883
    • Dobrosotskaya, I.Y.1    Seegmiller, A.C.2    Brown, M.S.3    Goldstein, J.L.4    Rawson, R.B.5
  • 37
    • 0030957823 scopus 로고    scopus 로고
    • Molecular basis for membrane phospholipid diversity: Why are there so many lipids?
    • Dowhan, W. 1997. Molecular basis for membrane phospholipid diversity: why are there so many lipids? Annu. Rev. Biochem. 66: 199-232.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 199-232
    • Dowhan, W.1
  • 38
    • 0038202541 scopus 로고    scopus 로고
    • Functional roles of lipids in membranes
    • Edited by D.E. Vance and J.E. Vance. Elsevier Science Publishers, Amsterdam, Netherlands
    • Dowhan, W., and Bogdanov, M. 2002. Functional roles of lipids in membranes. In Biochemistry of lipids, lipoproteins and membranes. 4th ed. Edited by D.E. Vance and J.E. Vance. Elsevier Science Publishers, Amsterdam, Netherlands.
    • (2002) Biochemistry of Lipids, Lipoproteins and Membranes. 4th Ed.
    • Dowhan, W.1    Bogdanov, M.2
  • 39
    • 0037136071 scopus 로고    scopus 로고
    • CTP:phosphocholine cytidylyltransferase and protein kinase C recognize different physical features of membranes: Differential responses to an oxidized phosphatidylcholine
    • Drobnies, A.E., Davies, S.M., Kraayenhof, R., Epand, R.F., Epand, R.M., and Cornell, R.B. 2002. CTP:phosphocholine cytidylyltransferase and protein kinase C recognize different physical features of membranes: differential responses to an oxidized phosphatidylcholine. Biochim. Biophys. Acta, 1564: 82-90.
    • (2002) Biochim. Biophys. Acta , vol.1564 , pp. 82-90
    • Drobnies, A.E.1    Davies, S.M.2    Kraayenhof, R.3    Epand, R.F.4    Epand, R.M.5    Cornell, R.B.6
  • 40
    • 0024546684 scopus 로고
    • Adriamycin, a drug interacting with acidic phospholipids, blocks import of precursor proteins by isolated yeast mitochondria
    • Eilers, M., Endo, T., and Schatz, G. 1989. Adriamycin, a drug interacting with acidic phospholipids, blocks import of precursor proteins by isolated yeast mitochondria. J. Biol. Chem. 264: 2945-2950.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2945-2950
    • Eilers, M.1    Endo, T.2    Schatz, G.3
  • 41
    • 0034640856 scopus 로고    scopus 로고
    • An essential role for a membrane lipid in cytokinesis: Regulation of contractile ring disassembly by redistribution of phosphatidylethanolamine
    • Emoto, K., and Umeda, M. 2000. An essential role for a membrane lipid in cytokinesis: regulation of contractile ring disassembly by redistribution of phosphatidylethanolamine. J. Cell Biol. 149: 1215-1224.
    • (2000) J. Cell Biol. , vol.149 , pp. 1215-1224
    • Emoto, K.1    Umeda, M.2
  • 42
    • 0029850318 scopus 로고    scopus 로고
    • Redistribution of phosphatidylethanolamine at the cleavage furrow of dividing cells during cytokinesis
    • Emoto, K., Kobayashi, T., Yamaji, A., Aizawa, H., Yahara, I., Inoue, K., and Umeda, M. 1996. Redistribution of phosphatidylethanolamine at the cleavage furrow of dividing cells during cytokinesis. Proc. Natl. Acad. Sci. U.S.A. 93: 12 867 - 12 872.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 12867-12872
    • Emoto, K.1    Kobayashi, T.2    Yamaji, A.3    Aizawa, H.4    Yahara, I.5    Inoue, K.6    Umeda, M.7
  • 43
    • 0033607230 scopus 로고    scopus 로고
    • Isolation of a Chinese hamster ovary cell mutant defective in intramitochondrial transport of phosphatidylserine
    • Emoto, K., Kuge, O., Nishijima, M., and Umeda, M. 1999. Isolation of a Chinese hamster ovary cell mutant defective in intramitochondrial transport of phosphatidylserine. Proc. Natl. Acad. Sci. U.S.A. 96: 12 400 - 12 405.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 12400-12405
    • Emoto, K.1    Kuge, O.2    Nishijima, M.3    Umeda, M.4
  • 44
    • 0026508561 scopus 로고
    • Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages
    • Fadok, V.A., Voelker, D.R., Campbell, P.A., Cohen, J.J., Bratton, D.L., and Henson, P.M. 1992. Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages. J. Immunol. 148: 2207-2216.
    • (1992) J. Immunol. , vol.148 , pp. 2207-2216
    • Fadok, V.A.1    Voelker, D.R.2    Campbell, P.A.3    Cohen, J.J.4    Bratton, D.L.5    Henson, P.M.6
  • 46
    • 0035846941 scopus 로고    scopus 로고
    • Loss of phospholipid asymmetry and surface exposure of phosphatidylserine is required for phagocytosis of apoptotic cells by macrophages and fibroblasts
    • Fadok, V.A., de Cathelineau, A., Daleke, D.L., Henson, P.M., and Bratton, D.L. 2001. Loss of phospholipid asymmetry and surface exposure of phosphatidylserine is required for phagocytosis of apoptotic cells by macrophages and fibroblasts. J. Biol. Chem. 276: 1071-1077.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1071-1077
    • Fadok, V.A.1    De Cathelineau, A.2    Daleke, D.L.3    Henson, P.M.4    Bratton, D.L.5
  • 47
    • 0015003654 scopus 로고
    • Outer mitochondrial membrane continuous with endoplasmic reticulum
    • Franke, W.W., and Kartenbeck, J. 1971. Outer mitochondrial membrane continuous with endoplasmic reticulum. Protoplasma, 73: 35-41.
    • (1971) Protoplasma , vol.73 , pp. 35-41
    • Franke, W.W.1    Kartenbeck, J.2
  • 48
    • 0035816002 scopus 로고    scopus 로고
    • Transport of choline and its relationship to the expression of the organic cation transporters in a rat brain microvessel endothelial cell line (RBE4)
    • Friedrich, A., George, R.L., Bridges, C.C., Prasad, P.D., and Ganapathy, V. 2001. Transport of choline and its relationship to the expression of the organic cation transporters in a rat brain microvessel endothelial cell line (RBE4). Biochim. Biophys. Acta, 1512: 299-307.
    • (2001) Biochim. Biophys. Acta , vol.1512 , pp. 299-307
    • Friedrich, A.1    George, R.L.2    Bridges, C.C.3    Prasad, P.D.4    Ganapathy, V.5
  • 49
    • 0035941277 scopus 로고    scopus 로고
    • Transcription of the CTP:phosphocholine cytidylyltransferase alpha gene is enhanced during the S phase of the cell cycle
    • Golfman, L.S., Bakovic, M., and Vance, D.E. 2001. Transcription of the CTP:phosphocholine cytidylyltransferase alpha gene is enhanced during the S phase of the cell cycle. J. Biol. Chem. 276: 43 688 - 43 692.
    • (2001) J. Biol. Chem. , vol.276 , pp. 43688-43692
    • Golfman, L.S.1    Bakovic, M.2    Vance, D.E.3
  • 51
    • 0028861713 scopus 로고
    • Cholecystokinin stimulates the down-regulation of CTP:phosphocholine cytidylyltransferase in pancreatic acinar cells
    • Groblewski, G.E., Wang, Y., Ernst, S.A., Kent, C., and Williams, J.A. 1995. Cholecystokinin stimulates the down-regulation of CTP:phosphocholine cytidylyltransferase in pancreatic acinar cells. J. Biol. Chem. 270: 1437-1442.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1437-1442
    • Groblewski, G.E.1    Wang, Y.2    Ernst, S.A.3    Kent, C.4    Williams, J.A.5
  • 52
    • 0032533314 scopus 로고    scopus 로고
    • Isolation and chromosomal localization of two human CDP-diacylglycerol synthase (CDS) genes
    • Halford, S., Dulai, K.S., Daw, S.C., Fitzgibbon, J., and Hunt, D.M. 1998. Isolation and chromosomal localization of two human CDP-diacylglycerol synthase (CDS) genes. Genomics, 54: 140-144.
    • (1998) Genomics , vol.54 , pp. 140-144
    • Halford, S.1    Dulai, K.S.2    Daw, S.C.3    Fitzgibbon, J.4    Hunt, D.M.5
  • 53
    • 0036889152 scopus 로고    scopus 로고
    • Mitochondrial glycerol-3-phosphate acyltransferase-deficient mice have reduced weight and liver triacylglycerol content and altered glycerolipid fatty acid composition
    • Hammond, L.E., Gallagher, P.A., Wang, S., Hiller, S., Kluckman, K.D., Posey-Marcos, E.L., Maeda, N., and Coleman, R.A. 2002. Mitochondrial glycerol-3-phosphate acyltransferase-deficient mice have reduced weight and liver triacylglycerol content and altered glycerolipid fatty acid composition. Mol. Cell. Biol. 22: 8204-8214.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8204-8214
    • Hammond, L.E.1    Gallagher, P.A.2    Wang, S.3    Hiller, S.4    Kluckman, K.D.5    Posey-Marcos, E.L.6    Maeda, N.7    Coleman, R.A.8
  • 54
    • 0024473409 scopus 로고
    • Isolation and characterization of a Chinese hamster ovary cell mutant with altered regulation of phosphatidylserine biosynthesis
    • Hasegawa, K., Kuge, O., Nishijima, M., and Akamatsu, Y. 1989. Isolation and characterization of a Chinese hamster ovary cell mutant with altered regulation of phosphatidylserine biosynthesis. J. Biol. Chem. 264: 19 887 - 19 892.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19887-19892
    • Hasegawa, K.1    Kuge, O.2    Nishijima, M.3    Akamatsu, Y.4
  • 55
    • 0029819084 scopus 로고    scopus 로고
    • Cloning of CDP-diacylglycerol synthase from a human neuronal cell line
    • Heacock, A.M., Uhler, M.D., and Agranoff, B.W. 1996. Cloning of CDP-diacylglycerol synthase from a human neuronal cell line. J. Neurochem. 67: 2200-2203.
    • (1996) J. Neurochem. , vol.67 , pp. 2200-2203
    • Heacock, A.M.1    Uhler, M.D.2    Agranoff, B.W.3
  • 56
    • 0033561020 scopus 로고    scopus 로고
    • Cloning and expression of a human choline/ethanolaminephosphotransferase: Synthesis of phosphatidylcholine and phosphatidyethanolamine
    • Henneberry, A.L., and McMaster, C.R. 1999. Cloning and expression of a human choline/ethanolaminephosphotransferase: synthesis of phosphatidylcholine and phosphatidyethanolamine. Biochem. J. 339: 291-298.
    • (1999) Biochem. J. , vol.339 , pp. 291-298
    • Henneberry, A.L.1    McMaster, C.R.2
  • 57
    • 0034703103 scopus 로고    scopus 로고
    • Cloning, genomic organization, and characterization of a human cholinephosphotransferase
    • In process citation
    • Henneberry, A.L., Wistow, G., and McMaster, C.R. 2000. Cloning, genomic organization, and characterization of a human cholinephosphotransferase [In process citation]. J. Biol. Chem. 275: 29 808 - 29 815.
    • (2000) J. Biol. Chem. , vol.275 , pp. 29808-29815
    • Henneberry, A.L.1    Wistow, G.2    McMaster, C.R.3
  • 58
    • 0028121377 scopus 로고
    • Increased expression of CTP:phosphocholine cytidylyltransferase in maturing type II cells
    • Hogan, M., Zimmermann, L.J., Wang, J., Kuliszewski, M., Liu, J., and Post, M. 1994. Increased expression of CTP:phosphocholine cytidylyltransferase in maturing type II cells. Am. J. Physiol. 267: L25-L32.
    • (1994) Am. J. Physiol. , vol.267
    • Hogan, M.1    Zimmermann, L.J.2    Wang, J.3    Kuliszewski, M.4    Liu, J.5    Post, M.6
  • 59
    • 0026545179 scopus 로고
    • Phosphatidylethanolamine metabolism in rat liver after partial hepatectomy
    • Houweling, M., Tijburg, L.B., Vaartjes, W.J., and van Golde, L.M.G. 1992. Phosphatidylethanolamine metabolism in rat liver after partial hepatectomy. Biochem. J. 283: 55-61.
    • (1992) Biochem. J. , vol.283 , pp. 55-61
    • Houweling, M.1    Tijburg, L.B.2    Vaartjes, W.J.3    Van Golde, L.M.G.4
  • 60
    • 0028174960 scopus 로고
    • Dephosphorylation of CTP-phosphocholine cytidylyltransferase is not required for binding to membranes
    • Houweling, M., Jamil, H., Hatch, G.M., and Vance, D.E. 1994. Dephosphorylation of CTP-phosphocholine cytidylyltransferase is not required for binding to membranes. J. Biol. Chem. 269: 7544-7551.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7544-7551
    • Houweling, M.1    Jamil, H.2    Hatch, G.M.3    Vance, D.E.4
  • 61
    • 0029671241 scopus 로고    scopus 로고
    • CTP:phosphocholine cytidylyltransferase in both a nuclear and cytoplasmic protein in primary hepatocytes
    • Houweling, M., Cui, Z., Anfuso, C.D., Bussiere, M., Chen, M.H., and Vance, D.E. 1996. CTP:phosphocholine cytidylyltransferase in both a nuclear and cytoplasmic protein in primary hepatocytes. Eur. J. Cell Biol. 69: 55-63.
    • (1996) Eur. J. Cell Biol. , vol.69 , pp. 55-63
    • Houweling, M.1    Cui, Z.2    Anfuso, C.D.3    Bussiere, M.4    Chen, M.H.5    Vance, D.E.6
  • 62
    • 0031576034 scopus 로고    scopus 로고
    • Induction of hepatocyte proliferation after partial hepatectomy is accompanied by a markedly reduced expression of phosphatidylethanolamine N-methyltransferase-2
    • Houweling, M., Cui, Z., Tessitore, L., and Vance, D.E. 1997. Induction of hepatocyte proliferation after partial hepatectomy is accompanied by a markedly reduced expression of phosphatidylethanolamine N-methyltransferase-2. Biochim. Biophys. Acta, 1346: 1-9.
    • (1997) Biochim. Biophys. Acta , vol.1346 , pp. 1-9
    • Houweling, M.1    Cui, Z.2    Tessitore, L.3    Vance, D.E.4
  • 63
    • 0035834709 scopus 로고    scopus 로고
    • Mitochondrial glycerol phosphate acyltransferase directs the incorporation of exogenous fatty acids into triacylglycerol
    • Igal, R.A., Wang, S., Gonzalez-Baro, M., and Coleman, R.A. 2001. Mitochondrial glycerol phosphate acyltransferase directs the incorporation of exogenous fatty acids into triacylglycerol. J. Biol. Chem. 276: 42 205 - 42 212.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42205-42212
    • Igal, R.A.1    Wang, S.2    Gonzalez-Baro, M.3    Coleman, R.A.4
  • 64
    • 0031552993 scopus 로고    scopus 로고
    • Choline/ethanolamine kinase from mammalian tissues
    • Ishidate, K. 1997. Choline/ethanolamine kinase from mammalian tissues. Biochim. Biophys. Acta, 1348: 70-78.
    • (1997) Biochim. Biophys. Acta , vol.1348 , pp. 70-78
    • Ishidate, K.1
  • 65
    • 0021678131 scopus 로고
    • Complete purification of choline kinase from rat kidney and preparation of rabbit antibody against rat kidney choline kinase
    • Ishidate, K., Nakagomi, K., and Nakazawa, Y. 1984. Complete purification of choline kinase from rat kidney and preparation of rabbit antibody against rat kidney choline kinase. J. Biol. Chem. 259: 14 706 - 14 710.
    • (1984) J. Biol. Chem. , vol.259 , pp. 14706-14710
    • Ishidate, K.1    Nakagomi, K.2    Nakazawa, Y.3
  • 66
    • 0022363386 scopus 로고
    • Complete co-purification of choline kinase and ethanolamine kinase from rat kidney and immunological evidence for both kinase activities residing on the same enzyme protein(s) in rat tissues
    • Ishidate, K., Furusawa, K.-i., and Nakazawa, Y. 1985. Complete co-purification of choline kinase and ethanolamine kinase from rat kidney and immunological evidence for both kinase activities residing on the same enzyme protein(s) in rat tissues. Biochim. Biophys. Acta, 836: 119-124.
    • (1985) Biochim. Biophys. Acta , vol.836 , pp. 119-124
    • Ishidate, K.1    Furusawa, K.-I.2    Nakazawa, Y.3
  • 67
    • 0025184422 scopus 로고
    • Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum
    • Jackson, M.R., Nilsson, T., and Peterson, P.A. 1990. Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum. EMBO J. 9: 3153-3162.
    • (1990) EMBO J. , vol.9 , pp. 3153-3162
    • Jackson, M.R.1    Nilsson, T.2    Peterson, P.A.3
  • 68
    • 0026500225 scopus 로고
    • Evidence that cyclic AMP induced inhibition of phosphatidylcholine biosynthesis is caused by a decrease in cellular diacylglycerol levels in cultured rat hepatocytes
    • Jamil, H., Utal, A.K., and Vance, D.E. 1992. Evidence that cyclic AMP induced inhibition of phosphatidylcholine biosynthesis is caused by a decrease in cellular diacylglycerol levels in cultured rat hepatocytes. J. Biol. Chem. 267: 1752-1760.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1752-1760
    • Jamil, H.1    Utal, A.K.2    Vance, D.E.3
  • 69
    • 0018265533 scopus 로고
    • Distribution of phospholipid biosynthetic enzymes among cell components of rat liver
    • Jelsema, C.J., and Morré, D.J. 1978. Distribution of phospholipid biosynthetic enzymes among cell components of rat liver. J. Biol. Chem. 253: 7960-7971.
    • (1978) J. Biol. Chem. , vol.253 , pp. 7960-7971
    • Jelsema, C.J.1    Morré, D.J.2
  • 70
    • 0037414807 scopus 로고    scopus 로고
    • Both acidic and basic amino acids in an amphitropic enzyme, CTP:phosphocholine cytidylyltransferase, dictate its selectivity for anionic membranes
    • Johnson, J.E., Xie, M., Singh, L.M., Edge, R., and Cornell, R.B. 2003. Both acidic and basic amino acids in an amphitropic enzyme, CTP:phosphocholine cytidylyltransferase, dictate its selectivity for anionic membranes. J. Biol. Chem. 278: 514-522.
    • (2003) J. Biol. Chem. , vol.278 , pp. 514-522
    • Johnson, J.E.1    Xie, M.2    Singh, L.M.3    Edge, R.4    Cornell, R.B.5
  • 71
    • 0027053153 scopus 로고
    • Lipid composition of subcellular membranes from larvae and prepupae of Drosophila melanogaster
    • Jones, H.E., Harwood, J.L., Bowen, I.D., and Griffiths, G. 1992. Lipid composition of subcellular membranes from larvae and prepupae of Drosophila melanogaster. Lipids, 27: 984-987.
    • (1992) Lipids , vol.27 , pp. 984-987
    • Jones, H.E.1    Harwood, J.L.2    Bowen, I.D.3    Griffiths, G.4
  • 72
    • 0025030678 scopus 로고
    • Cloning and expression of rat liver CTP:phosphocholine cytidylyltransferase: An amphipatnic protein that controls phosphatidylcholine synthesis
    • Kalmar, G.B., Kay, R.J., Lachance, A., Aebersold, R., and Cornell, R.B. 1990. Cloning and expression of rat liver CTP:phosphocholine cytidylyltransferase: an amphipatnic protein that controls phosphatidylcholine synthesis. Proc. Natl. Acad. Sci. U.S.A. 87: 6029-6033.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 6029-6033
    • Kalmar, G.B.1    Kay, R.J.2    Lachance, A.3    Aebersold, R.4    Cornell, R.B.5
  • 73
    • 0001590175 scopus 로고
    • Metabolism and function of bacterial lipids. II. Biosynthesis of lipids in Escherichia coli
    • Kanfer, J.N., and Kennedy, E.P. 1964. Metabolism and function of bacterial lipids. II. Biosynthesis of lipids in Escherichia coli. J. Biol. Chem. 239: 1720-1726.
    • (1964) J. Biol. Chem. , vol.239 , pp. 1720-1726
    • Kanfer, J.N.1    Kennedy, E.P.2
  • 75
    • 0020559431 scopus 로고
    • Phosphatidylethanolamine synthesis in ethanolamine-responsive and nonresponsive cells in culture
    • Kano-Sueoka, T., Errick, J.E., King, D., and Walsh, L.A. 1983. Phosphatidylethanolamine synthesis in ethanolamine-responsive and nonresponsive cells in culture. J. Cell. Physiol. 117: 109-115.
    • (1983) J. Cell. Physiol. , vol.117 , pp. 109-115
    • Kano-Sueoka, T.1    Errick, J.E.2    King, D.3    Walsh, L.A.4
  • 76
    • 0037783979 scopus 로고    scopus 로고
    • Gene structure, expression and identification of a new CTP:phosphocholine cytidylyltransferase beta isoform
    • Karim, M., Jackson, P., and Jackowski, S. 2003. Gene structure, expression and identification of a new CTP:phosphocholine cytidylyltransferase beta isoform. Biochim. Biophys. Acta, 1633: 1-12.
    • (2003) Biochim. Biophys. Acta , vol.1633 , pp. 1-12
    • Karim, M.1    Jackson, P.2    Jackowski, S.3
  • 77
    • 0034879757 scopus 로고    scopus 로고
    • CTP:phosphocholine cytidylyltransferase, a new sterol- and SREBP-responsive gene
    • Kast, H.R., Nguyen, C.M., Ainsfeld, A.M., Ericsson, J., and Edwards, P.A. 2001. CTP:phosphocholine cytidylyltransferase, a new sterol- and SREBP-responsive gene. J. Lipid Res. 42: 1266-1272.
    • (2001) J. Lipid Res. , vol.42 , pp. 1266-1272
    • Kast, H.R.1    Nguyen, C.M.2    Ainsfeld, A.M.3    Ericsson, J.4    Edwards, P.A.5
  • 78
    • 0000749205 scopus 로고
    • The function of cytidine coenzymes in the biosynthesis of phospholipides
    • Kennedy, E.P., and Weiss, S.B. 1956. The function of cytidine coenzymes in the biosynthesis of phospholipides. J. Biol. Chem. 222: 193-214.
    • (1956) J. Biol. Chem. , vol.222 , pp. 193-214
    • Kennedy, E.P.1    Weiss, S.B.2
  • 79
    • 0031553042 scopus 로고    scopus 로고
    • CTP:phosphocholine cytidylyltransferase
    • Kent, C. 1997. CTP:phosphocholine cytidylyltransferase. Biochim. Biophys. Acta, 1348: 79-90.
    • (1997) Biochim. Biophys. Acta , vol.1348 , pp. 79-90
    • Kent, C.1
  • 80
    • 0035816590 scopus 로고    scopus 로고
    • Expression and characterization of recombinant rat Acyl-CoA synthetases 1, 4, and 5. Selective inhibition by triacsin C and thiazolidinediones
    • Kim, J.H., Lewin, T.M., and Coleman, R.A. 2001. Expression and characterization of recombinant rat Acyl-CoA synthetases 1, 4, and 5. Selective inhibition by triacsin C and thiazolidinediones. J. Biol. Chem. 276: 24 667 - 24 673.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24667-24673
    • Kim, J.H.1    Lewin, T.M.2    Coleman, R.A.3
  • 81
    • 0031553017 scopus 로고    scopus 로고
    • Phosphatidylserine synthase I and II of mammalian cells
    • Kuge, O., and Nishijima, M. 1997. Phosphatidylserine synthase I and II of mammalian cells. Biochim. Biophys. Acta, 1348: 151-158.
    • (1997) Biochim. Biophys. Acta , vol.1348 , pp. 151-158
    • Kuge, O.1    Nishijima, M.2
  • 82
    • 0021846710 scopus 로고
    • Isolation of a somatic cell mutant defective in phosphatidylserine biosynthesis
    • Kuge, O., Nishijima, M., and Akamatsu, Y. 1985. Isolation of a somatic cell mutant defective in phosphatidylserine biosynthesis. Proc. Natl. Acad. Sci. U.S.A. 82: 1926-1930.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 1926-1930
    • Kuge, O.1    Nishijima, M.2    Akamatsu, Y.3
  • 83
    • 0023010680 scopus 로고
    • Phosphatidylserine biosynthesis in cultured chinese hamster ovary cells. II. Isolation and characterization of phosphatidylserine auxotrophs
    • Kuge, O., Nishijima, M., and Akamatsu, Y. 1986. Phosphatidylserine biosynthesis in cultured chinese hamster ovary cells. II. Isolation and characterization of phosphatidylserine auxotrophs. J. Biol. Chem. 261: 5790-5794.
    • (1986) J. Biol. Chem. , vol.261 , pp. 5790-5794
    • Kuge, O.1    Nishijima, M.2    Akamatsu, Y.3
  • 84
    • 0026337977 scopus 로고
    • A Chinese hamster cDNA encoding a protein essential for phosphatidylserine synthase I activity
    • Kuge, O., Nishijima, M., and Akamatsu, Y. 1991a. A Chinese hamster cDNA encoding a protein essential for phosphatidylserine synthase I activity. J. Biol. Chem. 266: 24 184 - 24 189.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24184-24189
    • Kuge, O.1    Nishijima, M.2    Akamatsu, Y.3
  • 85
    • 0025822140 scopus 로고
    • A cloned gene encoding phosphatidylserine decarboxylase complements the phosphatidylserine biosynthetic defect of a Chinese hamster ovary cell mutant
    • Kuge, O., Nishijima, M., and Akamatsu, Y. 1991b. A cloned gene encoding phosphatidylserine decarboxylase complements the phosphatidylserine biosynthetic defect of a Chinese hamster ovary cell mutant. J. Biol. Chem. 266: 6370-6376.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6370-6376
    • Kuge, O.1    Nishijima, M.2    Akamatsu, Y.3
  • 86
    • 0030814763 scopus 로고    scopus 로고
    • Cloning of a Chinese hamster ovary (CHO) cDNA encoding phosphatidylserine synthase (PSS) II, overexpression of which suppresses the phosphatidylserine biosynthetic defect of a PSS I-lacking mutant of CHO-K1 cells
    • Kuge, O., Saito, K., and Nishijima, M. 1997. Cloning of a Chinese hamster ovary (CHO) cDNA encoding phosphatidylserine synthase (PSS) II, overexpression of which suppresses the phosphatidylserine biosynthetic defect of a PSS I-lacking mutant of CHO-K1 cells. J. Biol. Chem. 272: 19 133 - 19 139.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19133-19139
    • Kuge, O.1    Saito, K.2    Nishijima, M.3
  • 87
    • 0032516053 scopus 로고    scopus 로고
    • Control of phosphatidylserine biosynthesis through phosphatidylserine - Mediated inhibition of phosphatidylserine synthase I in Chinese hamster ovary cells
    • Kuge, O., Hasegawa, K., Saito, K., and Nishijima, M. 1998. Control of phosphatidylserine biosynthesis through phosphatidylserine - mediated inhibition of phosphatidylserine synthase I in Chinese hamster ovary cells. Proc. Natl. Acad. Sci. U.S.A. 95: 4199-4203.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 4199-4203
    • Kuge, O.1    Hasegawa, K.2    Saito, K.3    Nishijima, M.4
  • 88
    • 0033588336 scopus 로고    scopus 로고
    • Control of phosphatidylserine synthase II activity in Chinese hamster ovary cells
    • Kuge, O., Saito, K., and Nishijima, M. 1999. Control of phosphatidylserine synthase II activity in Chinese hamster ovary cells. J. Biol. Chem. 274: 23 844 - 23 849.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23844-23849
    • Kuge, O.1    Saito, K.2    Nishijima, M.3
  • 89
    • 0035968290 scopus 로고    scopus 로고
    • Enhancement of transport-dependent decarboxylation of phosphatidylserine by S100B protein in permeabilized Chinese hamster ovary cells
    • Kuge, O., Yamakawa, Y., and Nishijima, M. 2001. Enhancement of transport-dependent decarboxylation of phosphatidylserine by S100B protein in permeabilized Chinese hamster ovary cells. J. Biol. Chem. 276: 23 700 - 23 706.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23700-23706
    • Kuge, O.1    Yamakawa, Y.2    Nishijima, M.3
  • 90
    • 0142180059 scopus 로고    scopus 로고
    • Purification and characterization of Chinese hamster phosphatidylserine synthase 2
    • Kuge, O., Hasegawa, K., Ohsawa, T., Saito, K., and Nishijima, M. 2003. Purification and characterization of Chinese hamster phosphatidylserine synthase 2. J. Biol. Chem. 278: 42 692 - 42 698.
    • (2003) J. Biol. Chem. , vol.278 , pp. 42692-42698
    • Kuge, O.1    Hasegawa, K.2    Ohsawa, T.3    Saito, K.4    Nishijima, M.5
  • 91
    • 0017811284 scopus 로고
    • Sodium-dependent, high affinity choline uptake
    • Kuhar, M.J., and Murrin, L.C. 1978. Sodium-dependent, high affinity choline uptake. J. Neurochem. 30: 15-21.
    • (1978) J. Neurochem. , vol.30 , pp. 15-21
    • Kuhar, M.J.1    Murrin, L.C.2
  • 92
    • 0015578427 scopus 로고
    • Choline: Selective accumulation by central cholinergic neurons
    • Kuhar, M.J., Sethy, V.H., Roth, R.H., and Agfajanian, G.K. 1973. Choline: selective accumulation by central cholinergic neurons. J. Neurochem. 20: 581-593.
    • (1973) J. Neurochem. , vol.20 , pp. 581-593
    • Kuhar, M.J.1    Sethy, V.H.2    Roth, R.H.3    Agfajanian, G.K.4
  • 93
    • 0034640297 scopus 로고    scopus 로고
    • Regulation of phosphatidylcholine metabolism in Chinese hamster ovary cells by the sterol regulatory element-binding protein (SREBP)/SREBP cleavage-activating protein pathway
    • Lagace, T.A., Storey, M.K., and Ridgway, N.D. 2000. Regulation of phosphatidylcholine metabolism in Chinese hamster ovary cells by the sterol regulatory element-binding protein (SREBP)/SREBP cleavage-activating protein pathway. J. Biol. Chem. 275: 14 367 - 14 374.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14367-14374
    • Lagace, T.A.1    Storey, M.K.2    Ridgway, N.D.3
  • 94
    • 0025295176 scopus 로고
    • Regulation of the synthesis of platelet-activating factor and its inactive storage precursor (1-alkyl-2-acyl-sn-glycero-3-phosphocholine) from 1-alkyl-2-acetyl-sn-glycerol by rabbit platelets
    • Lee, T.C., Malone, B., Blank, M.L., Fitzgerald, V., and Snyder, F. 1990. Regulation of the synthesis of platelet-activating factor and its inactive storage precursor (1-alkyl-2-acyl-sn-glycero-3-phosphocholine) from 1-alkyl-2-acetyl-sn-glycerol by rabbit platelets. J. Biol. Chem. 265: 9181-9187.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9181-9187
    • Lee, T.C.1    Malone, B.2    Blank, M.L.3    Fitzgerald, V.4    Snyder, F.5
  • 95
    • 0021089013 scopus 로고
    • Isolation of the yeast structural gene for the membrane-associated enzyme phosphatidylserine synthase
    • Letts, V.A., Klig, L.S., Bae-Lee, M., Carman, G.M., and Henry, S.A. 1983. Isolation of the yeast structural gene for the membrane-associated enzyme phosphatidylserine synthase. Proc. Natl. Acad. Sci. U.S.A. 80: 7279-7283.
    • (1983) Proc. Natl. Acad. Sci. U.S.A. , vol.80 , pp. 7279-7283
    • Letts, V.A.1    Klig, L.S.2    Bae-Lee, M.3    Carman, G.M.4    Henry, S.A.5
  • 96
    • 0035816532 scopus 로고    scopus 로고
    • Acyl-CoA synthetase isoforms 1, 4, and 5 are present in different subcellular membranes in rat liver and can be inhibited independently
    • Lewin, T.M., Kim, J.H., Granger, D.A., Vance, J.E., and Coleman, R.A. 2001. Acyl-CoA synthetase isoforms 1, 4, and 5 are present in different subcellular membranes in rat liver and can be inhibited independently. J. Biol. Chem. 276: 24 674 - 24 679.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24674-24679
    • Lewin, T.M.1    Kim, J.H.2    Granger, D.A.3    Vance, J.E.4    Coleman, R.A.5
  • 97
    • 0023762589 scopus 로고
    • Structural characterization of Escherichia coli phosphatidylserine decarboxylase
    • Li, Q.-X., and Dowhan, W. 1988. Structural characterization of Escherichia coli phosphatidylserine decarboxylase. J. Biol. Chem. 263: 11 516 - 11 512.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11516-111512
    • Li, Q.-X.1    Dowhan, W.2
  • 98
    • 0031455170 scopus 로고    scopus 로고
    • The role of CDP-diacylglycerol synthetase and phosphatidylinositol synthase activity levels in the regulation of cellular phosphatidylinositol content
    • Lykidis, A., Jackson, P.D., Rock, C.O., and Jackowski, S. 1997. The role of CDP-diacylglycerol synthetase and phosphatidylinositol synthase activity levels in the regulation of cellular phosphatidylinositol content. J. Biol. Chem. 272: 33 402 - 33 409.
    • (1997) J. Biol. Chem. , vol.272 , pp. 33402-33409
    • Lykidis, A.1    Jackson, P.D.2    Rock, C.O.3    Jackowski, S.4
  • 99
    • 0032577585 scopus 로고    scopus 로고
    • Cloning and characterization of a second human CTP:phosphocholine cytidylyltransferase
    • Lykidis, A., Murti, K.G., and Jackowski, S. 1998. Cloning and characterization of a second human CTP:phosphocholine cytidylyltransferase. J. Biol. Chem. 273: 14 022 - 14 029.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14022-14029
    • Lykidis, A.1    Murti, K.G.2    Jackowski, S.3
  • 100
    • 0033578749 scopus 로고    scopus 로고
    • Distribution of CTP:phosphocholine cytidylyltransferase (CCT) isoforms: Identification of a new CCTβ splice variant
    • Lykidis, A., Baburina, I., and Jackowski, S. 1999. Distribution of CTP:phosphocholine cytidylyltransferase (CCT) isoforms: identification of a new CCTβ splice variant. J. Biol. Chem. 274: 26 992 - 27 001.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26992-27001
    • Lykidis, A.1    Baburina, I.2    Jackowski, S.3
  • 101
    • 0035910413 scopus 로고    scopus 로고
    • Overexpression of a mammalian ethanolamine-specific kinase accelerates the CDP-ethanolamine pathway
    • Lykidis, A., Wang, J., Karim, M.A., and Jackowski, S. 2001. Overexpression of a mammalian ethanolamine-specific kinase accelerates the CDP-ethanolamine pathway. J. Biol. Chem. 276: 2174-2179.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2174-2179
    • Lykidis, A.1    Wang, J.2    Karim, M.A.3    Jackowski, S.4
  • 102
    • 0028308709 scopus 로고
    • Identification of phosphorylation sites in rat liver CTP:phosphocholine cytidylyltransferase
    • MacDonald, I., and Kent, C. 1994. Identification of phosphorylation sites in rat liver CTP:phosphocholine cytidylyltransferase. J. Biol. Chem. 269: 10 529 - 10 537.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10529-10537
    • MacDonald, I.1    Kent, C.2
  • 103
    • 0037083890 scopus 로고    scopus 로고
    • Lipid deprivation increases surfactant phosphatidylcholine synthesis via a sterol-sensitive regulatory element within the CTP:phosphocholine cytidylyltransferase promoter
    • Mallampalli, R.K., Ryan, A.J., Carroll, J.L., Osborne, T.F., and Thomas, C.P. 2002. Lipid deprivation increases surfactant phosphatidylcholine synthesis via a sterol-sensitive regulatory element within the CTP:phosphocholine cytidylyltransferase promoter. Biochem. J. 362: 81-88.
    • (2002) Biochem. J. , vol.362 , pp. 81-88
    • Mallampalli, R.K.1    Ryan, A.J.2    Carroll, J.L.3    Osborne, T.F.4    Thomas, C.P.5
  • 105
    • 0035158274 scopus 로고    scopus 로고
    • Inhibin B in male reproduction: Pathophysiology and clinical relevance
    • Meachem, S.J., Nieschlag, E., and Simoni, M. 2001. Inhibin B in male reproduction: pathophysiology and clinical relevance. Eur. J. Endocrinol. 145: 561-571.
    • (2001) Eur. J. Endocrinol. , vol.145 , pp. 561-571
    • Meachem, S.J.1    Nieschlag, E.2    Simoni, M.3
  • 106
    • 0026664217 scopus 로고
    • Phosphatidylethanolamine is the donor of the ethanolamine residue linking a glycosylphosphatidylinositol anchor to protein
    • Menon, A.K., and Stevens, V.L. 1992. Phosphatidylethanolamine is the donor of the ethanolamine residue linking a glycosylphosphatidylinositol anchor to protein. J. Biol. Chem. 267: 15 277 - 15 280.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15277-15280
    • Menon, A.K.1    Stevens, V.L.2
  • 107
    • 0023025855 scopus 로고
    • Characterization of the pathways for phosphatidylethanolamine biosynthesis in Chinese hamster ovary mutant and parental cell lines
    • Miller, M.A., and Kent, C. 1986. Characterization of the pathways for phosphatidylethanolamine biosynthesis in Chinese hamster ovary mutant and parental cell lines. J. Biol. Chem. 261: 9753-9761.
    • (1986) J. Biol. Chem. , vol.261 , pp. 9753-9761
    • Miller, M.A.1    Kent, C.2
  • 108
    • 0014994920 scopus 로고
    • Connections between mitochondria and endoplasmic reticulum in rat liver and and onion stem
    • Morré, D.J., Merritt, W.D., and Lembi, C.A. 1971. Connections between mitochondria and endoplasmic reticulum in rat liver and and onion stem. Protoplasma, 73: 43-49.
    • (1971) Protoplasma , vol.73 , pp. 43-49
    • Morré, D.J.1    Merritt, W.D.2    Lembi, C.A.3
  • 109
    • 0033635489 scopus 로고    scopus 로고
    • Acyl-CoAs are functionally channeled in liver: Potential role of acyl-CoA synthetase
    • Muoio, D.M., Lewin, T., Wiedmer, P., and Coleman, R.A. 2000. Acyl-CoAs are functionally channeled in liver: potential role of acyl-CoA synthetase. Am. J. Physiol. Endocrinol. Metab. 279: E1366-E1373.
    • (2000) Am. J. Physiol. Endocrinol. Metab. , vol.279
    • Muoio, D.M.1    Lewin, T.2    Wiedmer, P.3    Coleman, R.A.4
  • 110
    • 0030975483 scopus 로고    scopus 로고
    • Cloning of a human cDNA for CTP-phosphoethanolamine cytidylyltransferase by complementation in vivo of a yeast mutant
    • Nakashima, A., Hosaka, K., and Nikawa, J.-I. 1997. Cloning of a human cDNA for CTP-phosphoethanolamine cytidylyltransferase by complementation in vivo of a yeast mutant. J. Biol. Chem. 272: 9567-9572.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9567-9572
    • Nakashima, A.1    Hosaka, K.2    Nikawa, J.-I.3
  • 111
    • 0023658449 scopus 로고
    • Nucleotide sequence and characterization of the yeast PSS gene encoding phosphatidylserine synthase
    • Nikawa, J.-i., Tsukagoshi, Y., Kodaki, T., and Yamashita, S. 1987. Nucleotide sequence and characterization of the yeast PSS gene encoding phosphatidylserine synthase. Eur. J. Biochem. 167: 7-12.
    • (1987) Eur. J. Biochem. , vol.167 , pp. 7-12
    • Nikawa, J.-I.1    Tsukagoshi, Y.2    Kodaki, T.3    Yamashita, S.4
  • 112
    • 0022980698 scopus 로고
    • Phosphatidylserine biosynthesis in cultured Chinese hamster ovary cells. I. Inhibition of de novo phosphatidylserine biosynthesis by exogenous phosphatidylserine and its efficient incorporation
    • Nishijima, M., Kuge, O., and Akamatsu, Y. 1986. Phosphatidylserine biosynthesis in cultured Chinese hamster ovary cells. I. Inhibition of de novo phosphatidylserine biosynthesis by exogenous phosphatidylserine and its efficient incorporation. J. Biol. Chem. 261: 5784-5789.
    • (1986) J. Biol. Chem. , vol.261 , pp. 5784-5789
    • Nishijima, M.1    Kuge, O.2    Akamatsu, Y.3
  • 113
    • 0023052241 scopus 로고
    • Studies and perspectives of protein kinase C
    • Wash., D.C.
    • Nishizuka, Y. 1986. Studies and perspectives of protein kinase C. Science (Wash., D.C.), 233: 305-312.
    • (1986) Science , vol.233 , pp. 305-312
    • Nishizuka, Y.1
  • 114
    • 0242385311 scopus 로고    scopus 로고
    • Insights into the requirement of phosphatidylcholine synthesis for liver function in mice
    • Noga, A.A., and Vance, D.E. 2003a. Insights into the requirement of phosphatidylcholine synthesis for liver function in mice. J. Lipid Res. 44: 1998-2005.
    • (2003) J. Lipid Res. , vol.44 , pp. 1998-2005
    • Noga, A.A.1    Vance, D.E.2
  • 115
    • 0038159461 scopus 로고    scopus 로고
    • A gender-specific role for phosphatidylethanolamine N-methyltransferase- derived phosphatidylcholine in the regulation of plasma high density and very low density lipoproteins in mice
    • Noga, A.A., and Vance, D.E. 2003b. A gender-specific role for phosphatidylethanolamine N-methyltransferase-derived phosphatidylcholine in the regulation of plasma high density and very low density lipoproteins in mice. J. Biol. Chem. 278: 21 851 - 21 859.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21851-21859
    • Noga, A.A.1    Vance, D.E.2
  • 116
    • 0036829872 scopus 로고    scopus 로고
    • An unexpected requirement for phosphatidylethanolamine N-methyltransferase in the secretion of very low density lipoproteins
    • Noga, A.A., Zhao, Y., and Vance, D.E. 2002. An unexpected requirement for phosphatidylethanolamine N-methyltransferase in the secretion of very low density lipoproteins. J. Biol. Chem. 277: 42 358 - 42 365.
    • (2002) J. Biol. Chem. , vol.277 , pp. 42358-42365
    • Noga, A.A.1    Zhao, Y.2    Vance, D.E.3
  • 118
    • 0033543697 scopus 로고    scopus 로고
    • Shuttling of CTP:phosphocholine cytidylyltransferase between the nucleus and endoplasmic reticulum accompanies the wave of phosphatidylcholine synthesis during the G0-G1 transition
    • Northwood, I.C., Tong, A.H.Y., Crawford, B., Drobnies, A.E., and Cornell, R.B. 1999. Shuttling of CTP:phosphocholine cytidylyltransferase between the nucleus and endoplasmic reticulum accompanies the wave of phosphatidylcholine synthesis during the G0-G1 transition. J. Biol. Chem. 274: 26 340 - 26 248.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26340-126248
    • Northwood, I.C.1    Tong, A.H.Y.2    Crawford, B.3    Drobnies, A.E.4    Cornell, R.B.5
  • 119
    • 0027984012 scopus 로고
    • Cloning, sequencing and expression in Escherichia coli of the Bacillus subtilis gene for phosphatidylserine synthase
    • Okada, M., Matsuzaki, H., Shibuya, I., and Matsumoto, K. 1994. Cloning, sequencing and expression in Escherichia coli of the Bacillus subtilis gene for phosphatidylserine synthase. J. Bacteriol. 176: 7456-7461.
    • (1994) J. Bacteriol. , vol.176 , pp. 7456-7461
    • Okada, M.1    Matsuzaki, H.2    Shibuya, I.3    Matsumoto, K.4
  • 120
    • 0037160130 scopus 로고    scopus 로고
    • Single nucleotide polymorphism of the human high affinity choline transporter alters transport rate
    • Okuda, T., Okamura, M., Kaitsuka, C., Haga, T., and Gurwitz, D. 2002. Single nucleotide polymorphism of the human high affinity choline transporter alters transport rate. J. Biol. Chem. 277: 45 315 - 45 322.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45315-45322
    • Okuda, T.1    Okamura, M.2    Kaitsuka, C.3    Haga, T.4    Gurwitz, D.5
  • 121
    • 0142039652 scopus 로고    scopus 로고
    • The crystal structure of choline kinase reveals a eukaryotic protein kinase fold
    • Camb.
    • Peisach, D., Gee, P., Kent, C., and Xu, Z. 2003. The crystal structure of choline kinase reveals a eukaryotic protein kinase fold. Structure (Camb.), 11: 703-713.
    • (2003) Structure , vol.11 , pp. 703-713
    • Peisach, D.1    Gee, P.2    Kent, C.3    Xu, Z.4
  • 122
    • 0347419431 scopus 로고    scopus 로고
    • Genomic organization and differential splicing of the mouse and human Pcyt2 genes
    • Poloumienko, A., Cote, A., Quee, A.-T., Zhu, L., and Bakovic, M. 2003. Genomic organization and differential splicing of the mouse and human Pcyt2 genes. Gene, 325: 145-155.
    • (2003) Gene , vol.325 , pp. 145-155
    • Poloumienko, A.1    Cote, A.2    Quee, A.-T.3    Zhu, L.4    Bakovic, M.5
  • 123
    • 0017483927 scopus 로고
    • Gene cloning for the isolation of enzymes of membrane lipid synthesis: Phosphatidylserine synthase overproduction in Eschericia coli
    • Raetz, C.R.H., Larson, T.J., and Dowhan, W. 1977. Gene cloning for the isolation of enzymes of membrane lipid synthesis: phosphatidylserine synthase overproduction in Eschericia coli. Proc. Natl. Acad. Sci. U.S.A. 74: 1412-1416.
    • (1977) Proc. Natl. Acad. Sci. U.S.A. , vol.74 , pp. 1412-1416
    • Raetz, C.R.H.1    Larson, T.J.2    Dowhan, W.3
  • 124
    • 0037186623 scopus 로고    scopus 로고
    • Kinetic analyses of liver phosphatidylcholine and phosphatidylethanolamine biosynthesis using (13)C NMR spectroscopy
    • Reo, N.V., Adinehzadeh, M., and Foy, B.D. 2002. Kinetic analyses of liver phosphatidylcholine and phosphatidylethanolamine biosynthesis using (13)C NMR spectroscopy. Biochim. Biophys. Acta, 1580: 171-188.
    • (2002) Biochim. Biophys. Acta , vol.1580 , pp. 171-188
    • Reo, N.V.1    Adinehzadeh, M.2    Foy, B.D.3
  • 125
    • 0037929506 scopus 로고    scopus 로고
    • Regulation of the CDP-choline pathway by sterol regulatory element binding proteins involves transcriptional and post-transcriptional mechanisms
    • Ridgway, N.D., and Lagace, T.A. 2003. Regulation of the CDP-choline pathway by sterol regulatory element binding proteins involves transcriptional and post-transcriptional mechanisms. Biochem. J. 372: 811-819.
    • (2003) Biochem. J. , vol.372 , pp. 811-819
    • Ridgway, N.D.1    Lagace, T.A.2
  • 126
    • 0023657097 scopus 로고
    • Purification of phosphatidylethanolamine N-methyltransferase from rat liver
    • Ridgway, N.D., and Vance, D.E. 1987. Purification of phosphatidylethanolamine N-methyltransferase from rat liver. J. Biol. Chem. 262: 17 231 - 17 239.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17231-17239
    • Ridgway, N.D.1    Vance, D.E.2
  • 127
    • 0023744186 scopus 로고
    • Kinetic mechanism of phosphatidylethanolamine N-methyltransferase
    • Ridgway, N.D., and Vance, D.E. 1988. Kinetic mechanism of phosphatidylethanolamine N-methyltransferase. J. Biol. Chem. 263: 16 864 - 16 871.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16864-16871
    • Ridgway, N.D.1    Vance, D.E.2
  • 128
    • 0035966013 scopus 로고    scopus 로고
    • CTP:phosphocholine cytidylyltransferase alpha is a cytosolic protein in pulmonary epithelial cells and tissues
    • Ridsdale, R., Tseu, I., Wang, J., and Post, M. 2001. CTP:phosphocholine cytidylyltransferase alpha is a cytosolic protein in pulmonary epithelial cells and tissues. J. Biol. Chem. 276: 49 148 - 49 155.
    • (2001) J. Biol. Chem. , vol.276 , pp. 49148-49155
    • Ridsdale, R.1    Tseu, I.2    Wang, J.3    Post, M.4
  • 130
    • 0038572727 scopus 로고    scopus 로고
    • Homocysteine and coronary artery disease
    • Edited by R. Carmel and D.W. Jacobsne. Cambridge University Press, Cambridge, U.K.
    • Robinson, K. 2001. Homocysteine and coronary artery disease. In Homocysteine in health and disease. Edited by R. Carmel and D.W. Jacobsne. Cambridge University Press, Cambridge, U.K.
    • (2001) Homocysteine in Health and Disease
    • Robinson, K.1
  • 131
  • 132
    • 0033847579 scopus 로고    scopus 로고
    • Lipoprotein deprivation stimulates transcription of the CTP:phosphocholine cytidylyltransferase gene
    • Ryan, A.J., McCoy, D.M., Mathur, S.N., Field, F.J., and Mallampalli, R.K. 2000. Lipoprotein deprivation stimulates transcription of the CTP:phosphocholine cytidylyltransferase gene. J. Lipid Res. 41: 1268-1277.
    • (2000) J. Lipid Res. , vol.41 , pp. 1268-1277
    • Ryan, A.J.1    McCoy, D.M.2    Mathur, S.N.3    Field, F.J.4    Mallampalli, R.K.5
  • 133
    • 0030597170 scopus 로고    scopus 로고
    • Immunochemical identification of the pssA gene product as phosphatidylserine synthase I of Chinese hamster ovary cells
    • Saito, K., Kuge, O., Akamatsu, Y., and Nishijima, M. 1997. Immunochemical identification of the pssA gene product as phosphatidylserine synthase I of Chinese hamster ovary cells. FEBS Lett. 395: 262-266.
    • (1997) FEBS Lett. , vol.395 , pp. 262-266
    • Saito, K.1    Kuge, O.2    Akamatsu, Y.3    Nishijima, M.4
  • 134
    • 0031002921 scopus 로고    scopus 로고
    • Gene cloning and characterization of CDP-diacylglycerol synthase from rat brain
    • Saito, S., Goto, K., Tonosaki, A., and Kondo, H. 1997. Gene cloning and characterization of CDP-diacylglycerol synthase from rat brain. J. Biol. Chem. 272: 9503-9509.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9503-9509
    • Saito, S.1    Goto, K.2    Tonosaki, A.3    Kondo, H.4
  • 135
    • 0032479436 scopus 로고    scopus 로고
    • Genetic evidence that phosphatidylserine synthase II catalyzes the conversion of phosphatidylethanolamine to phosphatidylserine in Chinese hamster ovary cells
    • Saito, K., Nishijima, M., and Kuge, O. 1998. Genetic evidence that phosphatidylserine synthase II catalyzes the conversion of phosphatidylethanolamine to phosphatidylserine in Chinese hamster ovary cells. J. Biol. Chem. 273: 17 199 - 17 205.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17199-17205
    • Saito, K.1    Nishijima, M.2    Kuge, O.3
  • 136
    • 0030844278 scopus 로고    scopus 로고
    • Ethanolamine modulates the rate of rat hepatocyte proliferation in vitro and in vivo
    • Sasaki, H., Kume, H., Nemoto, A., Narisawa, S., and Takahashi, N. 1997. Ethanolamine modulates the rate of rat hepatocyte proliferation in vitro and in vivo. Proc. Natl. Acad. Sci. U.S.A. 94: 7320-7325.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 7320-7325
    • Sasaki, H.1    Kume, H.2    Nemoto, A.3    Narisawa, S.4    Takahashi, N.5
  • 137
    • 0026423662 scopus 로고
    • Transbilayer movement of phospholipids in red cell and platelet membranes
    • Schroit, A.J., and Zwaal, R.F.A. 1991. Transbilayer movement of phospholipids in red cell and platelet membranes. Biochim. Biophys. Acta, 1071: 313-329.
    • (1991) Biochim. Biophys. Acta , vol.1071 , pp. 313-329
    • Schroit, A.J.1    Zwaal, R.F.A.2
  • 138
    • 0037185026 scopus 로고    scopus 로고
    • Phosphatidylserine transport to the mitochondria is regulated by ubiquitination
    • Schumacher, M.M., Choi, J.Y., and Voelker, D.R. 2002. Phosphatidylserine transport to the mitochondria is regulated by ubiquitination. J. Biol. Chem. 277: 51 033 - 51 042.
    • (2002) J. Biol. Chem. , vol.277 , pp. 51033-51042
    • Schumacher, M.M.1    Choi, J.Y.2    Voelker, D.R.3
  • 139
    • 0028349810 scopus 로고
    • An N-terminal double-arginine motif maintains type II membrane proteins in the endoplasmic reticulum
    • Schutze, M.-P., Peterson, P.A., and Jackson, M.R. 1994. An N-terminal double-arginine motif maintains type II membrane proteins in the endoplasmic reticulum. EMBO J. 13: 1696-1705.
    • (1994) EMBO J. , vol.13 , pp. 1696-1705
    • Schutze, M.-P.1    Peterson, P.A.2    Jackson, M.R.3
  • 141
    • 12444341903 scopus 로고    scopus 로고
    • Localization of the phosphatidylethanolamine methylation pathway and scavenger receptor class B type I to the canalicular membrane: Evidence for apical phosphatidylcholine biosynthesis that may promote biliary excretion of phospholipid and cholesterol
    • Sehayek, E., Wang, R., Ono, J.G., Zinchuk, V.S., Duncan, E.M., Shefer, S., Vance, D.E., Ananthanarayanan, M., Chait, B.T., and Breslow, J.L. 2003. Localization of the phosphatidylethanolamine methylation pathway and scavenger receptor class B type I to the canalicular membrane: evidence for apical phosphatidylcholine biosynthesis that may promote biliary excretion of phospholipid and cholesterol. J. Lipid Res. 44: 1605-1613.
    • (2003) J. Lipid Res. , vol.44 , pp. 1605-1613
    • Sehayek, E.1    Wang, R.2    Ono, J.G.3    Zinchuk, V.S.4    Duncan, E.M.5    Shefer, S.6    Vance, D.E.7    Ananthanarayanan, M.8    Chait, B.T.9    Breslow, J.L.10
  • 142
    • 0029055754 scopus 로고
    • Evidence that phosphatidylserine is imported into mitochondria via a mitochondria-associated membrane and that the majority of mitochondrial phosphatidylethanolamine is derived from decarboxylation of phosphatidylserine
    • Shiao, Y.-J., Lupo, G., and Vance, J.E. 1995. Evidence that phosphatidylserine is imported into mitochondria via a mitochondria-associated membrane and that the majority of mitochondrial phosphatidylethanolamine is derived from decarboxylation of phosphatidylserine. J. Biol. Chem. 270: 11 190 - 11 198.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11190-11198
    • Shiao, Y.-J.1    Lupo, G.2    Vance, J.E.3
  • 143
    • 0032055479 scopus 로고    scopus 로고
    • A mitochondrial membrane protein is required for translocation of phosphatidylserine from mitochondria-associated membranes to mitochondria
    • Shiao, Y.-J., Balcerzak, B., and Vance, J.E. 1998. A mitochondrial membrane protein is required for translocation of phosphatidylserine from mitochondria-associated membranes to mitochondria. Biochem. J. 331: 217-223.
    • (1998) Biochem. J. , vol.331 , pp. 217-223
    • Shiao, Y.-J.1    Balcerzak, B.2    Vance, J.E.3
  • 144
    • 0035978412 scopus 로고    scopus 로고
    • Structure, expression profile and alternative processing of the human phosphatidylethanolamine N-methyltransferase (PEMT) gene
    • Shields, D.J., Agellon, L.B., and Vance, D.E. 2001. Structure, expression profile and alternative processing of the human phosphatidylethanolamine N-methyltransferase (PEMT) gene. Biochim. Biophys. Acta, 1532: 105-114.
    • (2001) Biochim. Biophys. Acta , vol.1532 , pp. 105-114
    • Shields, D.J.1    Agellon, L.B.2    Vance, D.E.3
  • 145
    • 0037474254 scopus 로고    scopus 로고
    • Membrane topography of human phosphatidylethanolamine N-methyltransferase
    • Shields, D.J., Lehner, R., Agellon, L.B., and Vance, D.E. 2003a. Membrane topography of human phosphatidylethanolamine N-methyltransferase. J. Biol. Chem. 278: 2956-2962.
    • (2003) J. Biol. Chem. , vol.278 , pp. 2956-2962
    • Shields, D.J.1    Lehner, R.2    Agellon, L.B.3    Vance, D.E.4
  • 146
    • 0041315473 scopus 로고    scopus 로고
    • Molecular dissection of the AdoMet binding site of phosphatidylethanolamine N-methyltransferase
    • Shields, D.J., Altarejos, J.Y., Wang, X., Agellon, L.B., and Vance, D.E. 2003b. Molecular dissection of the AdoMet binding site of phosphatidylethanolamine N-methyltransferase. J. Biol. Chem. 278: 35 826 - 35 836.
    • (2003) J. Biol. Chem. , vol.278 , pp. 35826-35836
    • Shields, D.J.1    Altarejos, J.Y.2    Wang, X.3    Agellon, L.B.4    Vance, D.E.5
  • 147
    • 0017325162 scopus 로고
    • Two fractions of rough endoplasmic reticulum from rat liver
    • Shore, G.G., and Tata, J.R. 1977. Two fractions of rough endoplasmic reticulum from rat liver. J. Cell Biol. 72: 714-725.
    • (1977) J. Cell Biol. , vol.72 , pp. 714-725
    • Shore, G.G.1    Tata, J.R.2
  • 148
    • 0033741374 scopus 로고    scopus 로고
    • Gene trapping methods for the identification and functional analysis of cell surface proteins in mice
    • Skarnes, W.C. 2000. Gene trapping methods for the identification and functional analysis of cell surface proteins in mice. Methods Enzymol. 328: 592-615.
    • (2000) Methods Enzymol. , vol.328 , pp. 592-615
    • Skarnes, W.C.1
  • 149
    • 0029023713 scopus 로고
    • Capturing genes encoding membrane and secreted proteins important for mouse development
    • Skarnes, W.C., Moss, J.E., Hurtley, S.M., Beddington, R.S. 1995. Capturing genes encoding membrane and secreted proteins important for mouse development. Proc. Natl. Acad. Sci. U.S.A. 92: 6592-6596.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 6592-6596
    • Skarnes, W.C.1    Moss, J.E.2    Hurtley, S.M.3    Beddington, R.S.4
  • 150
    • 0019127792 scopus 로고
    • Regulation of phosphatidylcholine biosynthesis in cultured chick embryonic muscle treated with phospholipase C
    • Sleight, R., and Kent, C. 1980. Regulation of phosphatidylcholine biosynthesis in cultured chick embryonic muscle treated with phospholipase C. J. Biol. Chem. 255: 10 644 - 10 650.
    • (1980) J. Biol. Chem. , vol.255 , pp. 10644-10650
    • Sleight, R.1    Kent, C.2
  • 152
    • 0017403288 scopus 로고
    • Pyruvate-containing enzymes
    • Snell, E.E. 1977. Pyruvate-containing enzymes. Trends Biochem. Sci. 2: 131-135.
    • (1977) Trends Biochem. Sci. , vol.2 , pp. 131-135
    • Snell, E.E.1
  • 153
    • 0033567415 scopus 로고    scopus 로고
    • Cloning and expression of murine liver phosphatidylserine synthase (PSS)-2: Differential regulation of phospholipid metabolism by PSS1 and PSS2
    • Stone, S.J., and Vance, J.E. 1999. Cloning and expression of murine liver phosphatidylserine synthase (PSS)-2: differential regulation of phospholipid metabolism by PSS1 and PSS2. Biochem. J. 342: 57-64.
    • (1999) Biochem. J. , vol.342 , pp. 57-64
    • Stone, S.J.1    Vance, J.E.2
  • 154
    • 0034602158 scopus 로고    scopus 로고
    • Phosphatidylserine synthase-1 and -2 are localized to mitochondria-associated membranes
    • Stone, S.J., and Vance, J.E. 2000. Phosphatidylserine synthase-1 and -2 are localized to mitochondria-associated membranes. J. Biol. Chem. 275: 34 534 - 34 540.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34534-34540
    • Stone, S.J.1    Vance, J.E.2
  • 155
    • 0032571291 scopus 로고    scopus 로고
    • Cloning and expression of mouse liver phosphatidylserine synthase-1 cDNA: Overexpression in rat hepatoma cells inhibits the CDP-ethanolamine pathway for phosphatidylethanolamine biosynthesis
    • Stone, S.J., Cui, Z., and Vance, J.E. 1998. Cloning and expression of mouse liver phosphatidylserine synthase-1 cDNA: overexpression in rat hepatoma cells inhibits the CDP-ethanolamine pathway for phosphatidylethanolamine biosynthesis. J. Biol. Chem. 273: 7293-7302.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7293-7302
    • Stone, S.J.1    Cui, Z.2    Vance, J.E.3
  • 156
    • 0035896540 scopus 로고    scopus 로고
    • Structure and expression of the murine phosphatidylserine synthase-1 gene
    • Sturbois-Balcerzak, B., Stone, S.J., Sreenivas, A., and Vance, J.E. 2001. Structure and expression of the murine phosphatidylserine synthase-1 gene. J. Biol. Chem. 276: 8205-8212.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8205-8212
    • Sturbois-Balcerzak, B.1    Stone, S.J.2    Sreenivas, A.3    Vance, J.E.4
  • 157
    • 0035853680 scopus 로고    scopus 로고
    • Identification of transcriptional enhancer factor-4 as a transcriptional modulator of CTP:phosphotholine cytidylyltransferase α
    • Sugimoto, H., Bakovic, M., Yamashita, S., and Vance, D.E. 2001. Identification of transcriptional enhancer factor-4 as a transcriptional modulator of CTP:phosphotholine cytidylyltransferase α. J. Biol. Chem. 276: 12 338 - 12 344.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12338-12344
    • Sugimoto, H.1    Bakovic, M.2    Yamashita, S.3    Vance, D.E.4
  • 158
    • 0037490195 scopus 로고    scopus 로고
    • Identification of Ets-1 as an important transcriptional activator of CTP:phosphocholine cytidylyltransferase alpha in COS-7 cells and co-activation with transcriptional enhancer factor-4
    • Sugimoto, H., Sugimoto, S., Tatei, K., Obinata, H., Bakovic, M., Izumi, T., and Vance, D.E. 2003. Identification of Ets-1 as an important transcriptional activator of CTP:phosphocholine cytidylyltransferase alpha in COS-7 cells and co-activation with transcriptional enhancer factor-4. J. Biol. Chem. 278: 19 716 - 19 722.
    • (2003) J. Biol. Chem. , vol.278 , pp. 19716-19722
    • Sugimoto, H.1    Sugimoto, S.2    Tatei, K.3    Obinata, H.4    Bakovic, M.5    Izumi, T.6    Vance, D.E.7
  • 159
    • 0016609166 scopus 로고
    • Biosynthesis of phosphatidylethanolamines and phosphatidylcholines from ethanolamine and choline in rat liver
    • Sundler, R., and Akesson, B. 1975a. Biosynthesis of phosphatidylethanolamines and phosphatidylcholines from ethanolamine and choline in rat liver. Biochem. J. 146: 309-315.
    • (1975) Biochem. J. , vol.146 , pp. 309-315
    • Sundler, R.1    Akesson, B.2
  • 160
    • 0016761879 scopus 로고
    • Regulation of phospholipid biosynthesis in isolated rat hepatocytes. Effect of different substrates
    • Sundler, R., and Akesson, B. 1975b. Regulation of phospholipid biosynthesis in isolated rat hepatocytes. Effect of different substrates. J. Biol. Chem. 250: 3359-3367.
    • (1975) J. Biol. Chem. , vol.250 , pp. 3359-3367
    • Sundler, R.1    Akesson, B.2
  • 161
    • 0016188231 scopus 로고
    • Quantitative role of base exchange in phosphatidylethanolamine synthesis in isolated rat hepatocytes
    • Sundler, R., Akesson, B., and Nilsson, A. 1974. Quantitative role of base exchange in phosphatidylethanolamine synthesis in isolated rat hepatocytes. FEBS Lett. 43: 303-307.
    • (1974) FEBS Lett. , vol.43 , pp. 303-307
    • Sundler, R.1    Akesson, B.2    Nilsson, A.3
  • 162
    • 0021962054 scopus 로고
    • Purification and properties of an ethanolamine-serine base exchange
    • Suzuki, T.T., and Kanfer, J.N. 1985. Purification and properties of an ethanolamine-serine base exchange enzyme of rat brain microsomes. J. Biol. Chem. 260: 1394-1399.
    • (1985) J. Biol. Chem. , vol.260 , pp. 1394-1399
    • Suzuki, T.T.1    Kanfer, J.N.2
  • 163
    • 0030983294 scopus 로고    scopus 로고
    • The structure of the gene for murine CTP:phosphocholine cytidylyltransferase, Ctpct
    • Tang, W., Keesler, G.A., and Tabas, I. 1997. The structure of the gene for murine CTP:phosphocholine cytidylyltransferase, Ctpct. J. Biol. Chem. 272: 13 146 - 13 151.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13146-13151
    • Tang, W.1    Keesler, G.A.2    Tabas, I.3
  • 164
    • 0033602389 scopus 로고    scopus 로고
    • Macrophage-targeted CTP:phosphocholine cytidylyltransferase (1-314) transgenic mice
    • Tang, W., Walsh, A., and Tabas, I. 1999. Macrophage-targeted CTP:phosphocholine cytidylyltransferase (1-314) transgenic mice. Biochim. Biophys. Acta, 1437: 301-316.
    • (1999) Biochim. Biophys. Acta , vol.1437 , pp. 301-316
    • Tang, W.1    Walsh, A.2    Tabas, I.3
  • 165
    • 0025951209 scopus 로고
    • Colony-stimulating factor 1 regulates CTP:phosphocholine cytidylyltransferase mRNA levels
    • Tessner, T.G., Rock, C.O., Kalmar, G.B., Cornell, R.B., and Jackowski, S. 1991. Colony-stimulating factor 1 regulates CTP:phosphocholine cytidylyltransferase mRNA levels. J. Biol. Chem. 266: 16 261 - 16 264.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16261-16264
    • Tessner, T.G.1    Rock, C.O.2    Kalmar, G.B.3    Cornell, R.B.4    Jackowski, S.5
  • 166
    • 0024401051 scopus 로고
    • Biosynthesis of phosphatidylethanolamine via the CDP-ethanolamine route is an important pathway in isolated rat hepatocytes
    • Tijburg, L.B.M., Geelen, M.J.H., and van Golde, L.M.G. 1989a. Biosynthesis of phosphatidylethanolamine via the CDP-ethanolamine route is an important pathway in isolated rat hepatocytes. Biochem. Biophys. Res. Commun. 160: 1275-1280.
    • (1989) Biochem. Biophys. Res. Commun. , vol.160 , pp. 1275-1280
    • Tijburg, L.B.M.1    Geelen, M.J.H.2    Van Golde, L.M.G.3
  • 167
    • 0024312193 scopus 로고
    • Regulation of the biosynthesis of triacylglycerol, phosphatidylcholine and phosphatidylethanolamine in the liver
    • Tijburg, L.B.M., Geelen, M.J.H., and van Golde, L.M.G. 1989b. Regulation of the biosynthesis of triacylglycerol, phosphatidylcholine and phosphatidylethanolamine in the liver. Biochim. Biophys. Acta, 1004: 1-19.
    • (1989) Biochim. Biophys. Acta , vol.1004 , pp. 1-19
    • Tijburg, L.B.M.1    Geelen, M.J.H.2    Van Golde, L.M.G.3
  • 168
    • 0028924622 scopus 로고
    • Phosphatidylserine decarboxylase 2 of Saccharomyces cerevisiae. Cloning and mapping of the gene, heterologous expression and creation of the null allele
    • Trotter, P.J., Pedretti, J., Yates, R., and Voelker, D.R. 1995. Phosphatidylserine decarboxylase 2 of Saccharomyces cerevisiae. Cloning and mapping of the gene, heterologous expression and creation of the null allele. J. Biol. Chem. 270: 6071-6080.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6071-6080
    • Trotter, P.J.1    Pedretti, J.2    Yates, R.3    Voelker, D.R.4
  • 170
    • 0026346995 scopus 로고
    • Diacylglycerol signals the translocation of CTP:choline-phosphate cytidylyltransferase in HeLa cells treated with 12-O-tetradecanoylphorbol-13- acetate
    • Utal, A.K., Jamil, H., and Vance, D.E. 1991. Diacylglycerol signals the translocation of CTP:choline-phosphate cytidylyltransferase in HeLa cells treated with 12-O-tetradecanoylphorbol-13-acetate. J. Biol. Chem. 266: 24 084 - 24 091.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24084-24091
    • Utal, A.K.1    Jamil, H.2    Vance, D.E.3
  • 172
    • 0025253338 scopus 로고
    • Chinese hamster ovary cells deficient in peroxisomes lack the nonspecific lipid transfer protein (sterol carrier protein 2)
    • van Heusden, G.P.H., Bos, K., Raetz, C.R.H., and Wirtz, K.W.A. 1990. Chinese hamster ovary cells deficient in peroxisomes lack the nonspecific lipid transfer protein (sterol carrier protein 2). J. Biol. Chem. 265: 4105-4110.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4105-4110
    • Van Heusden, G.P.H.1    Bos, K.2    Raetz, C.R.H.3    Wirtz, K.W.A.4
  • 173
    • 0034721549 scopus 로고    scopus 로고
    • Human sphingosine-1-phosphate lyase: cDNA cloning, functional expression studies and mapping to chromosome 10q22(1)
    • Van Veldhoven, P.P., Gijsbers, S., Mannaerts, G.P., Vermeesch, J.R., and Brys, V. 2000. Human sphingosine-1-phosphate lyase: cDNA cloning, functional expression studies and mapping to chromosome 10q22(1). Biochim. Biophys. Acta, 1487: 128-134.
    • (2000) Biochim. Biophys. Acta , vol.1487 , pp. 128-134
    • Van Veldhoven, P.P.1    Gijsbers, S.2    Mannaerts, G.P.3    Vermeesch, J.R.4    Brys, V.5
  • 174
    • 0025134479 scopus 로고
    • Phosphatidylcholine metabolism: Masochistic enzymology, metabolic regulation, and lipoprotein assembly
    • Vance, D.E. 1990. Phosphatidylcholine metabolism: masochistic enzymology, metabolic regulation, and lipoprotein assembly. Biochem. Cell Biol. 68: 1151-1165.
    • (1990) Biochem. Cell Biol. , vol.68 , pp. 1151-1165
    • Vance, D.E.1
  • 175
    • 35448953520 scopus 로고    scopus 로고
    • Phospholipid biosynthesis in eukaryotes
    • Edited by D.E.Vance and J.E. Vance. Elsevier Science Publishers, Amsterdam, Netherlands
    • Vance, D.E. 2002. Phospholipid biosynthesis in eukaryotes. In Biochemistry of lipids, lipoproteins and membranes. 4th ed. Edited by D.E.Vance and J.E. Vance. Elsevier Science Publishers, Amsterdam, Netherlands. pp. 205-232.
    • (2002) Biochemistry of Lipids, Lipoproteins and Membranes. 4th Ed. , pp. 205-232
    • Vance, D.E.1
  • 176
    • 0018429122 scopus 로고
    • How is phosphatidylcholine biosynthesis regulated?
    • Vance, D.E., and Choy, P.C. 1979. How is phosphatidylcholine biosynthesis regulated? Trends Biochem. Sci. 4: 145-148.
    • (1979) Trends Biochem. Sci. , vol.4 , pp. 145-148
    • Vance, D.E.1    Choy, P.C.2
  • 177
    • 0040448196 scopus 로고
    • Enzyme translocation in the regulation of phosphatidylcholine biosynthesis
    • Vance, D.E., and Pelech, S.L. 1984. Enzyme translocation in the regulation of phosphatidylcholine biosynthesis. Trends Biochem. Sci. 9: 17-20.
    • (1984) Trends Biochem. Sci. , vol.9 , pp. 17-20
    • Vance, D.E.1    Pelech, S.L.2
  • 178
    • 0025273937 scopus 로고
    • Phospholipid synthesis in a membrane fraction associated with mitochondria
    • Vance, J.E. 1990. Phospholipid synthesis in a membrane fraction associated with mitochondria. J. Biol. Chem. 265: 7248-7256.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7248-7256
    • Vance, J.E.1
  • 179
    • 0026088027 scopus 로고
    • Newly made phosphatidylserine and phosphatidylethanolamine are preferentially translocated between rat liver mitochondria and endoplasmic reticulum
    • Vance, J.E. 1991. Newly made phosphatidylserine and phosphatidylethanolamine are preferentially translocated between rat liver mitochondria and endoplasmic reticulum. J. Biol. Chem. 266: 89-97.
    • (1991) J. Biol. Chem. , vol.266 , pp. 89-97
    • Vance, J.E.1
  • 180
    • 0031738656 scopus 로고    scopus 로고
    • Eukaryotic lipid-biosynthetic enzymes: The same but not the same
    • Vance, J.E. 1998. Eukaryotic lipid-biosynthetic enzymes: the same but not the same. Trends Biochem. Sci. 23: 423-428.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 423-428
    • Vance, J.E.1
  • 181
    • 1542465944 scopus 로고    scopus 로고
    • The molecular and cell biology of phosphatidylserine and phospahtidylethanolamine
    • Vance, J.E. 2003. The molecular and cell biology of phosphatidylserine and phospahtidylethanolamine. Prog. Nucleic Acid Res. Mol. Biol. 75: 69-111.
    • (2003) Prog. Nucleic Acid Res. Mol. Biol. , vol.75 , pp. 69-111
    • Vance, J.E.1
  • 182
    • 0023903699 scopus 로고
    • Does rat liver Golgi have the capacity to synthesize phospholipids for lipoprotein secretion?
    • Vance, J.E., and Vance, D.E. 1988. Does rat liver Golgi have the capacity to synthesize phospholipids for lipoprotein secretion? J. Biol. Chem. 263: 5898-5908.
    • (1988) J. Biol. Chem. , vol.263 , pp. 5898-5908
    • Vance, J.E.1    Vance, D.E.2
  • 183
    • 0026342158 scopus 로고
    • Biosynthesis of membrane lipids in rat axons
    • Vance, I.E., Pan, D., Vance, D.E., and Campenot, R.B. 1991. Biosynthesis of membrane lipids in rat axons. J. Cell Biol. 115: 1061-1068.
    • (1991) J. Cell Biol. , vol.115 , pp. 1061-1068
    • Vance, I.E.1    Pan, D.2    Vance, D.E.3    Campenot, R.B.4
  • 184
    • 0027954891 scopus 로고
    • Evidence that the major membrane lipids, except cholesterol, are made in axons of cultured rat sympathetic neurons
    • Vance, J.E., Pan, D., Campenot, R.B., Bussiere, M., and Vance, D.E. 1994. Evidence that the major membrane lipids, except cholesterol, are made in axons of cultured rat sympathetic neurons. J. Neurochem. 62: 329-337.
    • (1994) J. Neurochem. , vol.62 , pp. 329-337
    • Vance, J.E.1    Pan, D.2    Campenot, R.B.3    Bussiere, M.4    Vance, D.E.5
  • 185
    • 0002845059 scopus 로고
    • Phosphatidylserine functions as the major precursor of phosphatidylethanolamine in cultured BHK-21 cells
    • Voelker, D.R. 1984. Phosphatidylserine functions as the major precursor of phosphatidylethanolamine in cultured BHK-21 cells. Proc. Natl. Acad. Sci. U.S.A. 81: 2669-2673.
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 2669-2673
    • Voelker, D.R.1
  • 186
    • 0024847351 scopus 로고
    • Phosphatidylserine translocation to the mitochondrion is an ATP-dependent process in permeabilized animal cells
    • Voelker, D.R. 1989a. Phosphatidylserine translocation to the mitochondrion is an ATP-dependent process in permeabilized animal cells. Proc. Natl. Acad. Sci. U.S.A. 86: 9921-9925.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 9921-9925
    • Voelker, D.R.1
  • 187
    • 0024321167 scopus 로고
    • Reconstitution of phosphatidylserine import into rat liver mitochondria
    • Voelker, D.R. 1989b. Reconstitution of phosphatidylserine import into rat liver mitochondria. J. Biol. Chem. 264: 8019-8025.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8019-8025
    • Voelker, D.R.1
  • 188
    • 0025128087 scopus 로고
    • Characterization of phosphatidylserine synthesis and translocation in permeabilized animal cells
    • Voelker, D.R. 1990. Characterization of phosphatidylserine synthesis and translocation in permeabilized animal cells. J. Biol. Chem. 265: 14 340 - 14 346.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14340-14346
    • Voelker, D.R.1
  • 189
    • 0025912667 scopus 로고
    • Adriamycin disrupts phosphatidylserine import into the mitochondria of permeabilized CHO-K1 cells
    • Voelker, D.R. 1991. Adriamycin disrupts phosphatidylserine import into the mitochondria of permeabilized CHO-K1 cells. J. Biol. Chem. 266: 12 185 - 12 188.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12185-12188
    • Voelker, D.R.1
  • 190
    • 0027405015 scopus 로고
    • The ATP-dependent translocation of phosphatidylserine to the mitochondria is a process that is restricted to the autologous organelle
    • Voelker, D.R. 1993. The ATP-dependent translocation of phosphatidylserine to the mitochondria is a process that is restricted to the autologous organelle. J. Biol. Chem. 268: 7069-7074.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7069-7074
    • Voelker, D.R.1
  • 191
    • 0031553041 scopus 로고    scopus 로고
    • Phosphatidylserine decarboxylase
    • Voelker, D.R. 1997. Phosphatidylserine decarboxylase. Biochim. Biophys. Acta, 1348: 236-244.
    • (1997) Biochim. Biophys. Acta , vol.1348 , pp. 236-244
    • Voelker, D.R.1
  • 192
    • 0003580743 scopus 로고    scopus 로고
    • Lipid assembly into cell membranes
    • Edited by D.E. Vance and J.E. Vance. Elsevier Science Publishers, Amsterdam, Netherlands
    • Voelker, D.R. 2002. Lipid assembly into cell membranes. In Biochemistry of lipids, lipoproteins and membranes. 4th ed. Edited by D.E. Vance and J.E. Vance. Elsevier Science Publishers, Amsterdam, Netherlands, pp. 459-463.
    • (2002) Biochemistry of Lipids, Lipoproteins and Membranes. 4th Ed. , pp. 459-463
    • Voelker, D.R.1
  • 193
    • 0038620481 scopus 로고    scopus 로고
    • New perspectives on the regulation of intermembrane glycerophospholipid traffic
    • Voelker, D.R. 2003. New perspectives on the regulation of intermembrane glycerophospholipid traffic. J. Lipid Res. 44: 441-449.
    • (2003) J. Lipid Res. , vol.44 , pp. 441-449
    • Voelker, D.R.1
  • 194
    • 0022636810 scopus 로고
    • Isolation and characterization of a Chinese hamster ovary cell line requiring ethanolamine or phosphatidylserine for growth and exhibiting defective phosphatidylserine synthase activity
    • Voelker, D.R., and Frazier, J.L. 1986. Isolation and characterization of a Chinese hamster ovary cell line requiring ethanolamine or phosphatidylserine for growth and exhibiting defective phosphatidylserine synthase activity. J. Biol. Chem. 261: 1002-1008.
    • (1986) J. Biol. Chem. , vol.261 , pp. 1002-1008
    • Voelker, D.R.1    Frazier, J.L.2
  • 195
    • 0030465190 scopus 로고    scopus 로고
    • Characterization of the murine phosphatidylethanolamine N-methyltransferase-2 gene
    • Walkey, C.J., Cui, Z., Agellon, L.B., and Vance, D.E. 1996. Characterization of the murine phosphatidylethanolamine N-methyltransferase-2 gene. J. Lipid Res. 37: 2341-2350.
    • (1996) J. Lipid Res. , vol.37 , pp. 2341-2350
    • Walkey, C.J.1    Cui, Z.2    Agellon, L.B.3    Vance, D.E.4
  • 197
    • 0032538421 scopus 로고    scopus 로고
    • Biochemical and evolutionary significance of phospholipid methylation
    • Walkey, C.J., Yu, L., Agellon, L.B., and Vance, D.E. 1998. Biochemical and evolutionary significance of phospholipid methylation. J. Biol. Chem. 273: 27 043 - 27 046.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27043-27046
    • Walkey, C.J.1    Yu, L.2    Agellon, L.B.3    Vance, D.E.4
  • 198
    • 0033521716 scopus 로고    scopus 로고
    • Identification of three novel cDNAs for human phosphatidylethanolamine N-methyltransferase and localization of the human gene on chromosome 17p11.2
    • Walkey, C.J., Shields, D.J., and Vance, D.E. 1999. Identification of three novel cDNAs for human phosphatidylethanolamine N-methyltransferase and localization of the human gene on chromosome 17p11.2. Biochim. Biophys. Acta, 1436: 405-412.
    • (1999) Biochim. Biophys. Acta , vol.1436 , pp. 405-412
    • Walkey, C.J.1    Shields, D.J.2    Vance, D.E.3
  • 199
    • 0027415175 scopus 로고
    • Nuclear localization of soluble CTP:phosphocholine cytidylyltransferase
    • Wang, Y., Sweitzer, T.D., Weinhold, P.A., and Kent, C. 1993. Nuclear localization of soluble CTP:phosphocholine cytidylyltransferase. J. Biol. Chem. 268: 5899-5904.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5899-5904
    • Wang, Y.1    Sweitzer, T.D.2    Weinhold, P.A.3    Kent, C.4
  • 200
    • 0026713830 scopus 로고
    • Immunolocalization of membrane-associated CTP:phosphocholine cytidylyltransferase in phosphatidylcholine-deficient Chinese hamster ovary cells
    • Watkins, J.D., and Kent, C. 1992. Immunolocalization of membrane-associated CTP:phosphocholine cytidylyltransferase in phosphatidylcholine-deficient Chinese hamster ovary cells. J. Biol. Chem. 267: 5686-5692.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5686-5692
    • Watkins, J.D.1    Kent, C.2
  • 201
    • 0022972322 scopus 로고
    • The purification and characterization of CTP:phosphorylcholine cytidylyltransferase from rat liver
    • Weinhold, P.A., Rounsifer, M.E., and Feldman, D.A. 1986. The purification and characterization of CTP:phosphorylcholine cytidylyltransferase from rat liver. J. Biol. Chem. 261: 5104-5110.
    • (1986) J. Biol. Chem. , vol.261 , pp. 5104-5110
    • Weinhold, P.A.1    Rounsifer, M.E.2    Feldman, D.A.3
  • 203
    • 0015501875 scopus 로고
    • Choline: High affinity up-take by rat brain synaptosomes
    • Wash., D.C.
    • Yamamura, H.I., and Snyder, S.H. 1972. Choline: high affinity up-take by rat brain synaptosomes. Science (Wash., D.C.), 178: 626-628.
    • (1972) Science , vol.178 , pp. 626-628
    • Yamamura, H.I.1    Snyder, S.H.2
  • 204
    • 0027383706 scopus 로고
    • Expression and identification of p90 as the murine mitochondrial glycerol-3-phosphate acyltransferase
    • Yet, S.F., Lee, S., Hahm, Y.T., and Sul, H.S. 1993. Expression and identification of p90 as the murine mitochondrial glycerol-3-phosphate acyltransferase. Biochemistry, 32: 9486-9491.
    • (1993) Biochemistry , vol.32 , pp. 9486-9491
    • Yet, S.F.1    Lee, S.2    Hahm, Y.T.3    Sul, H.S.4
  • 205
    • 0034721547 scopus 로고    scopus 로고
    • Preferential externalization of newly synthesized phosphatidylserine in apoptotic U937 cells is dependent on caspase-mediated pathways
    • Yu, A.Y., Byers, D.M., Ridgway, N.D., McMaster, C.R., and Cook, H.W. 2000. Preferential externalization of newly synthesized phosphatidylserine in apoptotic U937 cells is dependent on caspase-mediated pathways. Biochim. Biophys. Acta, 1487: 296-308.
    • (2000) Biochim. Biophys. Acta , vol.1487 , pp. 296-308
    • Yu, A.Y.1    Byers, D.M.2    Ridgway, N.D.3    McMaster, C.R.4    Cook, H.W.5
  • 206
    • 0038660732 scopus 로고    scopus 로고
    • Stimulation of phosphatidylserine biosynthesis and facilitation of UV-induced apoptosis in Chinese hamster overy cells over-expressing phospholipid scramblase 1
    • Yu, A., McMaster, C.R., Byers, D.M., Ridgway, N.D., and Cook, H.W. 2003. Stimulation of phosphatidylserine biosynthesis and facilitation of UV-induced apoptosis in Chinese hamster overy cells over-expressing phospholipid scramblase 1. J. Biol. Chem. 278: 9706-9714.
    • (2003) J. Biol. Chem. , vol.278 , pp. 9706-9714
    • Yu, A.1    McMaster, C.R.2    Byers, D.M.3    Ridgway, N.D.4    Cook, H.W.5
  • 207
    • 0020597859 scopus 로고
    • Phosphatidylserine decarboxylase is located on the external side of the inner mitochondrial membrane
    • Zborowski, J., Dygas, A., and Wojtczak, L. 1983. Phosphatidylserine decarboxylase is located on the external side of the inner mitochondrial membrane. FEBS Lett. 157: 179-182.
    • (1983) FEBS Lett. , vol.157 , pp. 179-182
    • Zborowski, J.1    Dygas, A.2    Wojtczak, L.3
  • 208
    • 0020442447 scopus 로고
    • Phosphatidylethanolamine biosynthesis in isolated hamster heart
    • Zelinski, T.A., and Choy, P.C. 1982. Phosphatidylethanolamine biosynthesis in isolated hamster heart. Can. J. Biochem. 60: 817-823.
    • (1982) Can. J. Biochem. , vol.60 , pp. 817-823
    • Zelinski, T.A.1    Choy, P.C.2
  • 209
    • 0034634673 scopus 로고    scopus 로고
    • Macrophages deficient in CTP:phosphocholine cytidylyltransferase-a are viable under normal culture conditions but are highly susceptible to free cholesterol-induced death
    • Zhang, D., Tang, W., Yao, P.M., Yang, C., Xie, B., Jackowski, S., and Tabas, I. 2000. Macrophages deficient in CTP:phosphocholine cytidylyltransferase-a are viable under normal culture conditions but are highly susceptible to free cholesterol-induced death. J. Biol. Chem. 275: 35 368 - 35 376.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35368-35376
    • Zhang, D.1    Tang, W.2    Yao, P.M.3    Yang, C.4    Xie, B.5    Jackowski, S.6    Tabas, I.7
  • 210
    • 0032567648 scopus 로고    scopus 로고
    • Identification of the first mammalian sphingosine phosphate lyase gene and its functional expression in yeast
    • Zhou, J., and Saba, J.D. 1998. Identification of the first mammalian sphingosine phosphate lyase gene and its functional expression in yeast. Biochem. Biophys. Res. Commun. 242: 502-507.
    • (1998) Biochem. Biophys. Res. Commun. , vol.242 , pp. 502-507
    • Zhou, J.1    Saba, J.D.2


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