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Volumn 48, Issue 1, 2005, Pages 16-24

cDNA cloning and expression analysis of a CTP:phosphoethanolamine cytidylyltransferase from barley

Author keywords

Hordeum vulgare; Low temperature; Membrane; Phosphatidylethanolamine; Phospholipid

Indexed keywords

ANIMALIA; ARABIDOPSIS; ARABIDOPSIS THALIANA; HORDEUM VULGARE; HORDEUM VULGARE SUBSP. VULGARE;

EID: 20744446781     PISSN: 12269239     EISSN: None     Source Type: Journal    
DOI: 10.1007/bf03030560     Document Type: Article
Times cited : (1)

References (55)
  • 1
    • 0024512566 scopus 로고
    • PCR-based cDNA libraries at the level of a few cells
    • Belyavsky AT, Vinogradova T, Rajewsky K (1989) PCR-based cDNA libraries at the level of a few cells. Nucl Acids Res 17: 2919-2932
    • (1989) Nucl Acids Res , vol.17 , pp. 2919-2932
    • Belyavsky, A.T.1    Vinogradova, T.2    Rajewsky, K.3
  • 3
    • 0033213987 scopus 로고    scopus 로고
    • Cloning and expression of CTP:phosphoethanolamine cytidylyltransferase cDNA from rat liver
    • Bladergroen BA, Houweling M, Geelen MJH, van Golde LMG (1999) Cloning and expression of CTP:phosphoethanolamine cytidylyltransferase cDNA from rat liver. Biochem J 343: 107-114
    • (1999) Biochem J , vol.343 , pp. 107-114
    • Bladergroen, B.A.1    Houweling, M.2    Geelen, M.J.H.3    Van Golde, L.M.G.4
  • 5
    • 0033665923 scopus 로고    scopus 로고
    • Emerging physiological roles for N-acylphosphatidylethanolamine metabolism in plants: Signal transduction and membrane protection
    • Chapman KD (2000) Emerging physiological roles for N- acylphosphatidylethanolamine metabolism in plants: Signal transduction and membrane protection. Chem Phys Lipids 108: 221-230
    • (2000) Chem Phys Lipids , vol.108 , pp. 221-230
    • Chapman, K.D.1
  • 6
    • 0001495662 scopus 로고
    • Catalytic properties of a newly discovered acyltransferase that synthesizes N-acylphosphatidylethanolamine in cottonseed (Gossypium hirsutum L.) microsomes
    • Chapman KD, Moore TS (1993) Catalytic properties of a newly discovered acyltransferase that synthesizes N-acylphosphatidylethanolamine in cottonseed (Gossypium hirsutum L.) microsomes. Plant Physiol 102: 761-769
    • (1993) Plant Physiol , vol.102 , pp. 761-769
    • Chapman, K.D.1    Moore, T.S.2
  • 7
    • 0031588602 scopus 로고    scopus 로고
    • Cloning of CTP:phosphocholine cytidylyltransferase cDNA from Arabidopsis thaliana
    • Choi S-B, Lee K-W, Cho SH (1997) Cloning of CTP:phosphocholine cytidylyltransferase cDNA from Arabidopsis thaliana. Mol Cells 7: 58-63
    • (1997) Mol Cells , vol.7 , pp. 58-63
    • Choi, S.-B.1    Lee, K.-W.2    Cho, S.H.3
  • 8
    • 0033772127 scopus 로고    scopus 로고
    • cDNA cloning and expression of an aminoalcoholphosphotransferase isoform in Chinese cabbage
    • Choi YH, Lee JK, Lee C-H, Cho SH (2000) cDNA cloning and expression of an aminoalcoholphosphotransferase isoform in Chinese cabbage. Plant Cell Physiol 41: 1080-1084
    • (2000) Plant Cell Physiol , vol.41 , pp. 1080-1084
    • Choi, Y.H.1    Lee, J.K.2    Lee, C.-H.3    Cho, S.H.4
  • 9
    • 0017868338 scopus 로고
    • Empirical predictions of protein conformation
    • Chou PY, Fasman GD (1978) Empirical predictions of protein conformation. Annu Rev Biochem 47: 251-276
    • (1978) Annu Rev Biochem , vol.47 , pp. 251-276
    • Chou, P.Y.1    Fasman, G.D.2
  • 10
    • 0026757391 scopus 로고
    • Structure and biological effects of lipid modifications on proteins
    • Chow M, Der CJ, Buss JE (1992) Structure and biological effects of lipid modifications on proteins. Curr Opin Cell Biol 4: 629-636
    • (1992) Curr Opin Cell Biol , vol.4 , pp. 629-636
    • Chow, M.1    Der, C.J.2    Buss, J.E.3
  • 11
    • 0028067154 scopus 로고
    • Identification of the membrane-binding domain of rat liver CTP:phosphocholine cytidylyltransferase using chymotrypsin proteolysis
    • Craig L, Johnson JE, Cornell RB (1994) Identification of the membrane-binding domain of rat liver CTP:phosphocholine cytidylyltransferase using chymotrypsin proteolysis. J Biol Chem 269: 3311-3317
    • (1994) J Biol Chem , vol.269 , pp. 3311-3317
    • Craig, L.1    Johnson, J.E.2    Cornell, R.B.3
  • 12
    • 0028519926 scopus 로고
    • The AAPT1 gene of soybean complements a cholinephosphotransferase- deficient mutant of a yeast
    • Dewey RE, Wilson RF, Novitzky WP, Goode JH (1994) The AAPT1 gene of soybean complements a cholinephosphotransferase-deficient mutant of a yeast. Plant Cell 6: 1495-1507
    • (1994) Plant Cell , vol.6 , pp. 1495-1507
    • Dewey, R.E.1    Wilson, R.F.2    Novitzky, W.P.3    Goode, J.H.4
  • 13
    • 0024212067 scopus 로고
    • Rapid production of full-length cDNAs from rare transcripts: Amplification using a single gene-specific oligonucleotide primer
    • Frohman MA, Dush MK, Martin GR (1988) Rapid production of full-length cDNAs from rare transcripts: Amplification using a single gene-specific oligonucleotide primer. Proc Natl Acad Sci USA 85: 8998-9002
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 8998-9002
    • Frohman, M.A.1    Dush, M.K.2    Martin, G.R.3
  • 14
    • 13444294946 scopus 로고    scopus 로고
    • Lipids in cellular structures
    • Blackwell Science, Oxford
    • Gurr MI, Harwood JL, Frayn KN (2002) Lipids in cellular structures, In Lipid Biochemistry. Blackwell Science, Oxford, pp 215-266
    • (2002) Lipid Biochemistry , pp. 215-266
    • Gurr, M.I.1    Harwood, J.L.2    Frayn, K.N.3
  • 15
    • 0008555115 scopus 로고    scopus 로고
    • Environmental effects on plant lipid biochemistry
    • JL Harwood, ed, Cambridge University Press, Cambridge
    • Harwood JL (1998) Environmental effects on plant lipid biochemistry. In JL Harwood, ed, Plant Lipid Biosynthesis. Cambridge University Press, Cambridge, pp 305-347
    • (1998) Plant Lipid Biosynthesis , pp. 305-347
    • Harwood, J.L.1
  • 17
    • 0019882643 scopus 로고
    • Preferred conformation and molecular packing of phosphatidylethanolamine and phosphatidylcholine
    • Hauser H, Pascher I, Pearson RH, Sundell S (1981) Preferred conformation and molecular packing of phosphatidylethanolamine and phosphatidylcholine. Biochim Biophys Acta 650: 21-51
    • (1981) Biochim Biophys Acta , vol.650 , pp. 21-51
    • Hauser, H.1    Pascher, I.2    Pearson, R.H.3    Sundell, S.4
  • 19
    • 0019303179 scopus 로고
    • Choline transport in Saccharomyces cerevisiae
    • Hosaka K, Yamashita S (1980) Choline transport in Saccharomyces cerevisiae. J Bacteriol 143: 176-181
    • (1980) J Bacteriol , vol.143 , pp. 176-181
    • Hosaka, K.1    Yamashita, S.2
  • 22
    • 0036859482 scopus 로고    scopus 로고
    • Phosphatidylcholine biosynthesis at low temperature: Differential expression of CTP:phosphorylcholine cytidylyltransferase isogenes in Arabidopsis thaliana
    • Inatsugi R, Nakamura M, Nishida I (2002) Phosphatidylcholine biosynthesis at low temperature: Differential expression of CTP:phosphorylcholine cytidylyltransferase isogenes in Arabidopsis thaliana. Plant Cell Physiol 43: 1342-1350
    • (2002) Plant Cell Physiol , vol.43 , pp. 1342-1350
    • Inatsugi, R.1    Nakamura, M.2    Nishida, I.3
  • 24
    • 0023664776 scopus 로고
    • An inspection of the domain between putative TATA box and translation start site in 79 plant genes
    • Joshi CP (1987a) An inspection of the domain between putative TATA box and translation start site in 79 plant genes. Nucl Acids Res 15: 6643-6653
    • (1987) Nucl Acids Res , vol.15 , pp. 6643-6653
    • Joshi, C.P.1
  • 25
    • 0023650367 scopus 로고
    • Putative polyadenylation signals in nuclear genes of higher plants: A complication and analysis
    • Joshi CP (1987b) Putative polyadenylation signals in nuclear genes of higher plants: A complication and analysis. Nucl Acids Res 15: 9627-9640
    • (1987) Nucl Acids Res , vol.15 , pp. 9627-9640
    • Joshi, C.P.1
  • 26
    • 0002001690 scopus 로고
    • No discrimination by choline- and ethanolaminephosphotransferase from potato tuber microsomes in molecular species of endogenous diacylglycerols
    • Justin AM, Demandre C, Tremolieres A, Mazliak P (1985) No discrimination by choline- and ethanolaminephosphotransferase from potato tuber microsomes in molecular species of endogenous diacylglycerols. Biochim Biophys Acta 836: 1-7
    • (1985) Biochim Biophys Acta , vol.836 , pp. 1-7
    • Justin, A.M.1    Demandre, C.2    Tremolieres, A.3    Mazliak, P.4
  • 27
    • 0025030678 scopus 로고
    • Cloning and expression of rat liver CTP:phosphocholine cytidylyltransferase: An amphipathic protein that controls phosphatidylcholine synthesis
    • Kalmar GB, Kay RJ, LaChance A, Aebersold R, Cornell RB (1990) Cloning and expression of rat liver CTP:phosphocholine cytidylyltransferase: An amphipathic protein that controls phosphatidylcholine synthesis. Proc Natl Acad Sci USA 87: 6029-6033
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6029-6033
    • Kalmar, G.B.1    Kay, R.J.2    LaChance, A.3    Aebersold, R.4    Cornell, R.B.5
  • 28
    • 0000749205 scopus 로고
    • The function of cytidine coenzymes in the biosynthesis of phospholipids
    • Kennedy EP, Weiss SB (1956) The function of cytidine coenzymes in the biosynthesis of phospholipids. J Biol Chem 222: 193-214
    • (1956) J Biol Chem , vol.222 , pp. 193-214
    • Kennedy, E.P.1    Weiss, S.B.2
  • 29
    • 20744440566 scopus 로고    scopus 로고
    • Cloning and expression of a cDNA, AAPT3, encoding aminoalcoholphosphotransferase isoform from Chinese cabbage
    • Kim KS, Park JH, Cho SH (2004) Cloning and expression of a cDNA, AAPT3, encoding aminoalcoholphosphotransferase isoform from Chinese cabbage. Kor J Biol Sci 8: 105-109
    • (2004) Kor J Biol Sci , vol.8 , pp. 105-109
    • Kim, K.S.1    Park, J.H.2    Cho, S.H.3
  • 30
    • 85051570592 scopus 로고
    • Phospholipid head groups
    • TS Moore, ed, CRC, Boca Raton
    • Kinney AJ (1993) Phospholipid head groups. In TS Moore, ed, Lipid Metabolism in Plants. CRC, Boca Raton, pp 259-284
    • (1993) Lipid Metabolism in Plants , pp. 259-284
    • Kinney, A.J.1
  • 31
    • 0009503128 scopus 로고
    • Phospholipid metabolism and plasma membrane morphology of warm and cool rye roots
    • Kinney AJ, Clarkson DT, Loughman BC (1987) Phospholipid metabolism and plasma membrane morphology of warm and cool rye roots. Plant Physiol Biochem 25: 769-774
    • (1987) Plant Physiol Biochem , vol.25 , pp. 769-774
    • Kinney, A.J.1    Clarkson, D.T.2    Loughman, B.C.3
  • 32
    • 0023665902 scopus 로고
    • An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs
    • Kozak M (1987a) An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs. Nucl Acids Res 15: 8125-8148
    • (1987) Nucl Acids Res , vol.15 , pp. 8125-8148
    • Kozak, M.1
  • 33
    • 0023425901 scopus 로고
    • Effects of intercistronic length on the efficiency of reinitiation by eucaryotic ribosomes
    • Kozak M (1987b) Effects of intercistronic length on the efficiency of reinitiation by eucaryotic ribosomes. Mol Cell Biol 7: 3438-3445
    • (1987) Mol Cell Biol , vol.7 , pp. 3438-3445
    • Kozak, M.1
  • 34
    • 0020475449 scopus 로고
    • A simple method displaying the hydropathic character of a protein
    • Kyte J, Doolittle RF (1982) A simple method displaying the hydropathic character of a protein. J Mol Biol 157: 105-132
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 35
    • 20744447408 scopus 로고    scopus 로고
    • Cloning and expression of a cDNA encoding aminoalcoholphosphotransferase from Pimpinella brachycarpa
    • Lee JK, Choi YH, Bae YG, Lee WS, Cho SH (2001) Cloning and expression of a cDNA encoding aminoalcoholphosphotransferase from Pimpinella brachycarpa. J Plant Biol 44: 27-32
    • (2001) J Plant Biol , vol.44 , pp. 27-32
    • Lee, J.K.1    Choi, Y.H.2    Bae, Y.G.3    Lee, W.S.4    Cho, S.H.5
  • 36
    • 0016824492 scopus 로고
    • Evidence that phosphatidylcholine and phosphatidylethanolamine are synthesized by a single enzyme present in the endoplasmic reticulum of castor bean endosperm
    • Lord JM (1975) Evidence that phosphatidylcholine and phosphatidylethanolamine are synthesized by a single enzyme present in the endoplasmic reticulum of castor bean endosperm. Biochem J 151: 451-453
    • (1975) Biochem J , vol.151 , pp. 451-453
    • Lord, J.M.1
  • 37
    • 0000679931 scopus 로고
    • Plasma membrane lipid alterations associated with cold acclimation of winter rye seedlings (Secale cereale L. cv. Puma)
    • Lynch DV, Steponkus PL (1987) Plasma membrane lipid alterations associated with cold acclimation of winter rye seedlings (Secale cereale L. cv. Puma). Plant Physiol 83: 761-767
    • (1987) Plant Physiol , vol.83 , pp. 761-767
    • Lynch, D.V.1    Steponkus, P.L.2
  • 38
    • 0007581195 scopus 로고
    • Biosynthesis of phosphatidylethanolamine by enzyme preparations from plant tissues
    • Macher BA, Mudd JB (1974) Biosynthesis of phosphatidylethanolamine by enzyme preparations from plant tissues. Plant Physiol 53: 171-175
    • (1974) Plant Physiol , vol.53 , pp. 171-175
    • Macher, B.A.1    Mudd, J.B.2
  • 39
    • 0026664217 scopus 로고
    • Phosphatidylethanolamine is the donor of the ethanolamine residue linking a glycosylphosphatidylinositol anchor to protein
    • Menon AK, Stevens VL (1992) Phosphatidylethanolamine is the donor of the ethanolamine residue linking a glycosylphosphatidylinositol anchor to protein. J Biol Chem 267: 15277-15280
    • (1992) J Biol Chem , vol.267 , pp. 15277-15280
    • Menon, A.K.1    Stevens, V.L.2
  • 40
    • 20744435983 scopus 로고    scopus 로고
    • A study of the physiological function of phosphatidylethanolamine in Arabidopsis
    • N Murata, M Yamada, I Nishida, H Okuyama, J Sekiya, H Wada, eds, Kluwer Academic Publishers, Dordrecht
    • Mizoi J, Nakamura M, Nishida I (2003) A study of the physiological function of phosphatidylethanolamine in Arabidopsis. In N Murata, M Yamada, I Nishida, H Okuyama, J Sekiya, H Wada, eds, Advanced Research on Plant Lipids. Kluwer Academic Publishers, Dordrecht, pp 377-380
    • (2003) Advanced Research on Plant Lipids , pp. 377-380
    • Mizoi, J.1    Nakamura, M.2    Nishida, I.3
  • 41
    • 0034459468 scopus 로고    scopus 로고
    • Upstream open reading frames as regulators of mRNA translation
    • Morris DR, Geballe AP (2000) Upstream open reading frames as regulators of mRNA translation. Mol Cell Biol 20: 8635-8642
    • (2000) Mol Cell Biol , vol.20 , pp. 8635-8642
    • Morris, D.R.1    Geballe, A.P.2
  • 42
    • 0029658809 scopus 로고    scopus 로고
    • Protein kinase C is a major mediator of the stimulatory effect of phorbol ester on phospholipase D-mediated hydrolysis of phosphatidylethanolamine
    • Mukherjee JJ, Chung T, Ways DK, Kiss Z (1996) Protein kinase C is a major mediator of the stimulatory effect of phorbol ester on phospholipase D-mediated hydrolysis of phosphatidylethanolamine. J Biol Chem 271: 28912-28917
    • (1996) J Biol Chem , vol.271 , pp. 28912-28917
    • Mukherjee, J.J.1    Chung, T.2    Ways, D.K.3    Kiss, Z.4
  • 43
    • 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, Nikawa J (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.3
  • 44
    • 0030152042 scopus 로고    scopus 로고
    • Cloning of Brassica napus CTP:phosphocholine cytidylyltransferase cDNAs by complementation in a yeast cct mutant
    • Nishida I, Swinhoe R, Slabas AR, Murata N (1996) Cloning of Brassica napus CTP:phosphocholine cytidylyltransferase cDNAs by complementation in a yeast cct mutant. Plant Mol Biol 31: 205-211
    • (1996) Plant Mol Biol , vol.31 , pp. 205-211
    • Nishida, I.1    Swinhoe, R.2    Slabas, A.R.3    Murata, N.4
  • 45
    • 0001519162 scopus 로고    scopus 로고
    • Identification of functional conserved residues of CTP:glycerol-3- phosphate cytidylyltransferase: Role of histidines in the conserved HXGH in catalysis
    • Park YS, Gee P, Sanker S, Schurter EJ, Zuiderweg ER, Kent C (1997) Identification of functional conserved residues of CTP:glycerol-3-phosphate cytidylyltransferase: Role of histidines in the conserved HXGH in catalysis. J Biol Chem 272: 15161-15166
    • (1997) J Biol Chem , vol.272 , pp. 15161-15166
    • Park, Y.S.1    Gee, P.2    Sanker, S.3    Schurter, E.J.4    Zuiderweg, E.R.5    Kent, C.6
  • 46
    • 0015454947 scopus 로고
    • Differences between conformations of lecithin and phosphatidylethanolamine polar groups and their effects on interactions of phospholipid bilayer membranes
    • Phillips MC, Finer EG, Hauser H (1972) Differences between conformations of lecithin and phosphatidylethanolamine polar groups and their effects on interactions of phospholipid bilayer membranes. Biochim Biophys Acta 290: 397-402
    • (1972) Biochim Biophys Acta , vol.290 , pp. 397-402
    • Phillips, M.C.1    Finer, E.G.2    Hauser, H.3
  • 47
    • 0042352498 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of an aminoalcoholphosphotransferase (AAPT1) from Brassica napus: Effects of low temperature and abscisic acid treatments on AAPT expression in Arabidopsis plants and effects of over-expression of BnAAPT1 in transgenic Arabidopsis
    • Qi Q, Huang YF, Cutler AJ, Abrams SR, Taylor DC (2003) Molecular and biochemical characterization of an aminoalcoholphosphotransferase (AAPT1) from Brassica napus: Effects of low temperature and abscisic acid treatments on AAPT expression in Arabidopsis plants and effects of over-expression of BnAAPT1 in transgenic Arabidopsis. Planta 217: 547-558
    • (2003) Planta , vol.217 , pp. 547-558
    • Qi, Q.1    Huang, Y.F.2    Cutler, A.J.3    Abrams, S.R.4    Taylor, D.C.5
  • 48
    • 0029840156 scopus 로고    scopus 로고
    • Isolation and characterization of ECT1 gene encoding CTP: phosphoethanolamine cytidylyltransferase of Saccharomyces cerevisiae
    • Rho M-S, Kawamata Y, Nakamura H, Ohta A, Takagi M (1996) Isolation and characterization of ECT1 gene encoding CTP:phosphoethanolamine cytidylyltransferase of Saccharomyces cerevisiae. J Biochem 120: 1040-1047
    • (1996) J Biochem , vol.120 , pp. 1040-1047
    • Rho, M.-S.1    Kawamata, Y.2    Nakamura, H.3    Ohta, A.4    Takagi, M.5
  • 49
    • 11944252359 scopus 로고
    • Membrane bilayer distribution of phosphatidylethanolamine synthesized by the ethanolaminephosphotransferase and ethanolamine exchange reactions
    • Shin S, Moore TS (1990) Membrane bilayer distribution of phosphatidylethanolamine synthesized by the ethanolaminephosphotransferase and ethanolamine exchange reactions. Plant Physiol 93: 154-159
    • (1990) Plant Physiol , vol.93 , pp. 154-159
    • Shin, S.1    Moore, T.S.2
  • 50
    • 0001064239 scopus 로고
    • Phosphatidylethanolamine synthesis in castor bean endosperm
    • Sparace SA, Wagner LK, Moore TS (1981) Phosphatidylethanolamine synthesis in castor bean endosperm. Plant Physiol 67: 922-925
    • (1981) Plant Physiol , vol.67 , pp. 922-925
    • Sparace, S.A.1    Wagner, L.K.2    Moore, T.S.3
  • 51
    • 0016753096 scopus 로고
    • Ethanolaminephosphate cytidylyltransferase: Purification and characterization of the enzyme from rat liver
    • Sundler R (1975) Ethanolaminephosphate cytidylyltransferase: Purification and characterization of the enzyme from rat liver. J Biol Chem 250: 8585-8590
    • (1975) J Biol Chem , vol.250 , pp. 8585-8590
    • Sundler, R.1
  • 53
    • 0032125864 scopus 로고    scopus 로고
    • The role of histidine residues in the HXGH site of CTP:phosphocholine cytidylyltransferase in CTP binding and catalysis
    • Veitch DP, Gilham D, Cornell RB (1998) The role of histidine residues in the HXGH site of CTP:phosphocholine cytidylyltransferase in CTP binding and catalysis. Eur J Biochem 255: 227-234
    • (1998) Eur J Biochem , vol.255 , pp. 227-234
    • Veitch, D.P.1    Gilham, D.2    Cornell, R.B.3
  • 54
    • 0025876221 scopus 로고
    • Phosphatidylethanolamine synthesis by castor bean endosperm: Intracellular distribution and characteristics of CTP:ethanolaminephosphate cytidylyltransferase
    • Wang X, Moore TS (1991) Phosphatidylethanolamine synthesis by castor bean endosperm: Intracellular distribution and characteristics of CTP:ethanolaminephosphate cytidylyltransferase. J Biol Chem 266: 19981-19987
    • (1991) J Biol Chem , vol.266 , pp. 19981-19987
    • Wang, X.1    Moore, T.S.2
  • 55
    • 4344625375 scopus 로고    scopus 로고
    • Membrane lipid biosynthesis in Chlamydomonas reinhardtii. Expression and characterization of CTP:phosphoethanolamine cytidylyltransferase
    • Yang W, Mason CB, Pollock SV, Lavezzi T, Moroney JV, Moore TS (2004) Membrane lipid biosynthesis in Chlamydomonas reinhardtii. Expression and characterization of CTP:phosphoethanolamine cytidylyltransferase. Biochem J 382: 51-57
    • (2004) Biochem J , vol.382 , pp. 51-57
    • Yang, W.1    Mason, C.B.2    Pollock, S.V.3    Lavezzi, T.4    Moroney, J.V.5    Moore, T.S.6


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