메뉴 건너뛰기




Volumn 1437, Issue 3, 1999, Pages 301-316

Macrophage-targeted CTP:phosphocholine cytidylyltransferase (1-314) transgenic mice

Author keywords

CTP:phosphocholine cytidylyltransferase; Macrophage; Phosphatidylcholine biosynthesis; Transgenic mouse

Indexed keywords

3,3' DITHIOBIS(SUCCINIMIDYL PROPIONATE); CHOLESTEROL; CHOLINE; CHOLINE PHOSPHATE CYTIDYLYLTRANSFERASE; CYTIDINE; LIPOSOME; OLEIC ACID; PHOSPHATIDYLCHOLINE; PHOSPHORYLCHOLINE; TRITIUM;

EID: 0033602389     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1388-1981(99)00023-2     Document Type: Article
Times cited : (16)

References (46)
  • 1
    • 0025134479 scopus 로고
    • Phosphatidylcholine metabolism: Masochistic enzymology, metabolic regulation, and lipoprotein assembly
    • Vance D.E. Phosphatidylcholine metabolism: masochistic enzymology, metabolic regulation, and lipoprotein assembly. Biochem. Cell Biol. 68:1990;1151-1165.
    • (1990) Biochem. Cell Biol. , vol.68 , pp. 1151-1165
    • Vance, D.E.1
  • 2
    • 0025610139 scopus 로고
    • Regulation of phosphatidylcholine biosynthesis
    • Kent C. Regulation of phosphatidylcholine biosynthesis. Prog. Lipid Res. 29:1991;87-105.
    • (1991) Prog. Lipid Res. , vol.29 , pp. 87-105
    • Kent, C.1
  • 3
    • 0028067154 scopus 로고
    • Identification of the membrane-binding domain of rat liver CTP:phosphocholine cytidylyltransferase using chymotrypsin proteolysis
    • Craig L., Johnson J.E., Cornell R.B. Identification of the membrane-binding domain of rat liver CTP:phosphocholine cytidylyltransferase using chymotrypsin proteolysis. J. Biol. Chem. 269:1994;3311-3317.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3311-3317
    • Craig, L.1    Johnson, J.E.2    Cornell, R.B.3
  • 4
    • 0030983294 scopus 로고    scopus 로고
    • The structure of the gene for murine CTP:phosphocholine cytidylyltransferase, Ctpct. Relationship of exon structure to functional domains and identification of transcriptional start sites and potential upstream regulatory elements
    • Tang W., Keesler G.A., Tabas I. The structure of the gene for murine CTP:phosphocholine cytidylyltransferase, Ctpct. Relationship of exon structure to functional domains and identification of transcriptional start sites and potential upstream regulatory elements. J. Biol. Chem. 272:1997;13146-13151.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13146-13151
    • Tang, W.1    Keesler, G.A.2    Tabas, I.3
  • 5
    • 0024364943 scopus 로고
    • Chemical cross-linking reveals a dimeric structure for CTP: Phosphocholine cytidylyltransferase
    • Cornell R. Chemical cross-linking reveals a dimeric structure for CTP: phosphocholine cytidylyltransferase. J. Biol. Chem. 264:1989;9077-9082.
    • (1989) J. Biol. Chem. , vol.264 , pp. 9077-9082
    • Cornell, R.1
  • 6
    • 0027415175 scopus 로고
    • Nuclear localization of soluble CTP:phosphocholine cytidylyltransferase
    • Wang Y., Sweitzer T.D., Weinhold P.A., Kent C. Nuclear localization of soluble CTP:phosphocholine cytidylyltransferase. J. Biol. Chem. 268:1993;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
  • 7
    • 0029671241 scopus 로고    scopus 로고
    • CTP:phosphocholine cytidylyltransferase is both a nuclear and cytoplasmic protein in primary hepatocytes
    • Houweling M., Cui Z., Anfuso C.D., Bussière M., Chen M.H., Vance D.E. CTP:phosphocholine cytidylyltransferase is both a nuclear and cytoplasmic protein in primary hepatocytes. Eur. J. Cell Biol. 69:1996;55-63.
    • (1996) Eur. J. Cell Biol. , vol.69 , pp. 55-63
    • Houweling, M.1    Cui, Z.2    Anfuso, C.D.3    Bussière, M.4    Chen, M.H.5    Vance, D.E.6
  • 8
    • 0028787406 scopus 로고
    • The association of lipid activators with the amphipathic helical domain of CTP:phosphocholine cytidylyltransferase accelerates catalysis by increasing the affinity of the enzyme for CTP
    • Yang W., Boggs K.P., Jackowski S. The association of lipid activators with the amphipathic helical domain of CTP:phosphocholine cytidylyltransferase accelerates catalysis by increasing the affinity of the enzyme for CTP. J. Biol. Chem. 270:1995;23951-23957.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23951-23957
    • Yang, W.1    Boggs, K.P.2    Jackowski, S.3
  • 9
    • 0029048350 scopus 로고
    • Effects of altered phosphorylation sites on the properties of CTP:phosphocholine cytidylyltransferase
    • Wang Y., Kent C. Effects of altered phosphorylation sites on the properties of CTP:phosphocholine cytidylyltransferase. J. Biol. Chem. 270:1995;17843-17849.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17843-17849
    • Wang, Y.1    Kent, C.2
  • 10
    • 0031010020 scopus 로고    scopus 로고
    • Binding of CTP:phosphocholine cytidylyltransferase to lipid vesicles: Diacylglycerol and enzyme dephosphorylation increase the affinity for negatively charged membranes
    • Arnold R.S., DePaoli-Roach A.A., Cornell R.B. Binding of CTP:phosphocholine cytidylyltransferase to lipid vesicles: diacylglycerol and enzyme dephosphorylation increase the affinity for negatively charged membranes. Biochemistry. 36:1997;6149-6156.
    • (1997) Biochemistry , vol.36 , pp. 6149-6156
    • Arnold, R.S.1    Depaoli-Roach, A.A.2    Cornell, R.B.3
  • 11
    • 0032577585 scopus 로고    scopus 로고
    • Cloning and characterization of a second human CTP:phosphocholine cytidylyltransferase
    • Lykidis A., Murti K.G., Jackowski S. Cloning and characterization of a second human CTP:phosphocholine cytidylyltransferase. J. Biol. Chem. 273:1998;14022-14029.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14022-14029
    • Lykidis, A.1    Murti, K.G.2    Jackowski, S.3
  • 12
    • 0019888255 scopus 로고
    • Thermolabile CDP-choline synthetase in an animal cell mutant defective in lecithin formation
    • Esko J.D., Wermuth M.M., Raetz C.R.H. Thermolabile CDP-choline synthetase in an animal cell mutant defective in lecithin formation. J. Biol. Chem. 256:1981;7388-7393.
    • (1981) J. Biol. Chem. , vol.256 , pp. 7388-7393
    • Esko, J.D.1    Wermuth, M.M.2    Raetz, C.R.H.3
  • 13
    • 0030775933 scopus 로고    scopus 로고
    • Phospholipid metabolism in cholesterol-loaded macrophages
    • Tabas I. Phospholipid metabolism in cholesterol-loaded macrophages. Curr. Opin. Lipidol. 8:1997;263-267.
    • (1997) Curr. Opin. Lipidol. , vol.8 , pp. 263-267
    • Tabas, I.1
  • 14
    • 0028206482 scopus 로고
    • Free cholesterol loading of macrophages stimulates phosphatidylcholine biosynthesis and up-regulation of CTP:phosphocholine cytidylyltransferase
    • Shiratori Y., Okwu A.K., Tabas I. Free cholesterol loading of macrophages stimulates phosphatidylcholine biosynthesis and up-regulation of CTP:phosphocholine cytidylyltransferase. J. Biol. Chem. 269:1994;11337-11348.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11337-11348
    • Shiratori, Y.1    Okwu, A.K.2    Tabas, I.3
  • 15
    • 0029585368 scopus 로고
    • Stimulation of CTP:phosphocholine cytidylyltransferase by free cholesterol loading of macrophages involves signaling through protein dephosphorylation
    • Shiratori Y., Houweling M., Zha X., Tabas I. Stimulation of CTP:phosphocholine cytidylyltransferase by free cholesterol loading of macrophages involves signaling through protein dephosphorylation. J. Biol. Chem. 270:1995;29894-29903.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29894-29903
    • Shiratori, Y.1    Houweling, M.2    Zha, X.3    Tabas, I.4
  • 16
    • 0029787574 scopus 로고    scopus 로고
    • Evidence that the initial up-regulation of phosphatidylcholine biosynthesis in free cholesterol-loaded macrophages is an adaptive response that prevents cholesterol-induced cellular necrosis. Proposed role of an eventual failure of this response in foam cell necrosis in advanced atherosclerosis
    • Tabas I., Marathe S., Keesler G.A., Beatini N., Shiratori Y. Evidence that the initial up-regulation of phosphatidylcholine biosynthesis in free cholesterol-loaded macrophages is an adaptive response that prevents cholesterol-induced cellular necrosis. Proposed role of an eventual failure of this response in foam cell necrosis in advanced atherosclerosis. J. Biol. Chem. 271:1996;22773-22781.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22773-22781
    • Tabas, I.1    Marathe, S.2    Keesler, G.A.3    Beatini, N.4    Shiratori, Y.5
  • 17
    • 0030685812 scopus 로고    scopus 로고
    • Free cholesterol-induced cytotoxicity. A possible contributing factor to macrophage foam cell necrosis in advanced atherosclerotic lesions
    • Tabas I. Free cholesterol-induced cytotoxicity. A possible contributing factor to macrophage foam cell necrosis in advanced atherosclerotic lesions. Trends Cardiovasc. Med. 7:1997;256-263.
    • (1997) Trends Cardiovasc. Med. , vol.7 , pp. 256-263
    • Tabas, I.1
  • 18
    • 0028970042 scopus 로고
    • Cell biology of atherosclerosis
    • Ross R. Cell biology of atherosclerosis. Annu. Rev. Physiol. 57:1995;791-804.
    • (1995) Annu. Rev. Physiol. , vol.57 , pp. 791-804
    • Ross, R.1
  • 19
    • 0029079926 scopus 로고
    • Decreased atherosclerosis in mice deficient in both macrophage colony-stimulating factor (op) and apolipoprotein E
    • Smith J.D., Trogan E., Ginsberg M., Grigaux C., Tian J., Miyata M. Decreased atherosclerosis in mice deficient in both macrophage colony-stimulating factor (op) and apolipoprotein E. Proc. Natl. Acad. Sci. USA. 92:1995;8264-8268.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8264-8268
    • Smith, J.D.1    Trogan, E.2    Ginsberg, M.3    Grigaux, C.4    Tian, J.5    Miyata, M.6
  • 20
    • 0027376554 scopus 로고
    • The role of macrophages in atherogenesis
    • Libby P., Clinton S.K. The role of macrophages in atherogenesis. Curr. Opin. Lipidol. 4:1993;355-363.
    • (1993) Curr. Opin. Lipidol. , vol.4 , pp. 355-363
    • Libby, P.1    Clinton, S.K.2
  • 21
    • 0027125530 scopus 로고
    • The pathogenesis of coronary artery disease and the acute coronary syndromes
    • Fuster V., Badimon L., Badimon J.J., Chesebro J.H. The pathogenesis of coronary artery disease and the acute coronary syndromes. New Engl. J. Med. 326:1992;242-250.
    • (1992) New Engl. J. Med. , vol.326 , pp. 242-250
    • Fuster, V.1    Badimon, L.2    Badimon, J.J.3    Chesebro, J.H.4
  • 22
    • 0028291124 scopus 로고
    • Expression of wild-type and mutant rat liver CTP:phosphocholine cytidylyltransferase in a cytidylyltransferase-deficient Chinese hamster ovary cell line
    • Sweitzer T.D., Kent C. Expression of wild-type and mutant rat liver CTP:phosphocholine cytidylyltransferase in a cytidylyltransferase-deficient Chinese hamster ovary cell line. Arch. Biochem. Biophys. 311:1994;107-116.
    • (1994) Arch. Biochem. Biophys. , vol.311 , pp. 107-116
    • Sweitzer, T.D.1    Kent, C.2
  • 23
    • 0027992029 scopus 로고
    • Overexpression of rat liver CTP:phosphocholine cytidylyltransferase accelerates phosphatidylcholine synthesis and degradation
    • Walkey C.J., Kalmar G.B., Cornell R.B. Overexpression of rat liver CTP:phosphocholine cytidylyltransferase accelerates phosphatidylcholine synthesis and degradation. J. Biol. Chem. 269:1994;5742-5749.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5742-5749
    • Walkey, C.J.1    Kalmar, G.B.2    Cornell, R.B.3
  • 24
    • 0029033139 scopus 로고
    • Identification of an inhibitory domain of CTP:phosphocholine cytidylyltransferase
    • Wang Y., Kent C. Identification of an inhibitory domain of CTP:phosphocholine cytidylyltransferase. J. Biol. Chem. 270:1995;18948-18952.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18948-18952
    • Wang, Y.1    Kent, C.2
  • 25
    • 0029009415 scopus 로고
    • Scavenger receptor A gene regulatory elements target gene expression to macrophages and to foam cells of atherosclerotic lesions
    • Horvai A., Palinski W., Wu H., Moulton K.S., Kalla K., Glass C.K. Scavenger receptor A gene regulatory elements target gene expression to macrophages and to foam cells of atherosclerotic lesions. Proc. Natl. Acad. Sci. USA. 92:1995;5391-5395.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5391-5395
    • Horvai, A.1    Palinski, W.2    Wu, H.3    Moulton, K.S.4    Kalla, K.5    Glass, C.K.6
  • 26
    • 0344247088 scopus 로고
    • Identification of an inhibitory domain of CTP:phosphocholine cytidylyltransferase
    • Wang Y., Kent C. Identification of an inhibitory domain of CTP:phosphocholine cytidylyltransferase. Anal. Biochem. 208:1995;283-287.
    • (1995) Anal. Biochem. , vol.208 , pp. 283-287
    • Wang, Y.1    Kent, C.2
  • 27
    • 0026713830 scopus 로고
    • Immunolocalization of membrane-associated CTP:phosphocholine cytidylyltransferase in phosphatidylcholine-deficient Chinese hamster ovary cells
    • Watkins J.D., Kent C. Immunolocalization of membrane-associated CTP:phosphocholine cytidylyltransferase in phosphatidylcholine-deficient Chinese hamster ovary cells. J. Biol. Chem. 267:1992;5686-5692.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5686-5692
    • Watkins, J.D.1    Kent, C.2
  • 28
    • 0021320894 scopus 로고
    • Selective inhibition of acyl coenzyme A:cholesterol acyltransferase by compound 58-035
    • Ross A.C., Go K.J., Heider J.G., Rothblat G.H. Selective inhibition of acyl coenzyme A:cholesterol acyltransferase by compound 58-035. J. Biol. Chem. 259:1984;815-819.
    • (1984) J. Biol. Chem. , vol.259 , pp. 815-819
    • Ross, A.C.1    Go, K.J.2    Heider, J.G.3    Rothblat, G.H.4
  • 29
    • 0024592946 scopus 로고
    • High levels of human apolipoprotein A-I in transgenic mice result in increased plasma levels of small high density lipoprotein (HDL) particles comparable to human HDL3
    • Walsh A., Ito Y., Breslow J.L. High levels of human apolipoprotein A-I in transgenic mice result in increased plasma levels of small high density lipoprotein (HDL) particles comparable to human HDL3. J. Biol. Chem. 264:1989;6488-6494.
    • (1989) J. Biol. Chem. , vol.264 , pp. 6488-6494
    • Walsh, A.1    Ito, Y.2    Breslow, J.L.3
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 0026590767 scopus 로고
    • Choline-phosphate cytidylyltransferase
    • Weinhold P.A., Feldman D.A. Choline-phosphate cytidylyltransferase. Methods Enzymol. 209:1992;248-258.
    • (1992) Methods Enzymol. , vol.209 , pp. 248-258
    • Weinhold, P.A.1    Feldman, D.A.2
  • 33
    • 33845261493 scopus 로고
    • A rapid method for total lipid extraction and purification
    • Bligh E.G., Dyer W.J. A rapid method for total lipid extraction and purification. Can. J. Biochem. Physiol. 37:1959;911-917.
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 34
    • 0019407287 scopus 로고
    • Choline metabolism and phosphatidylcholine biosynthesis in cultured rat hepatocytes
    • Pritchard P.H., Vance D.E. Choline metabolism and phosphatidylcholine biosynthesis in cultured rat hepatocytes. Biochem. J. 196:1981;261-267.
    • (1981) Biochem. J. , vol.196 , pp. 261-267
    • Pritchard, P.H.1    Vance, D.E.2
  • 35
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
    • Dignam J.D., Lebovitz R.M., Roeder R.G. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11:1983;1475-1489.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 1475-1489
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.G.3
  • 36
    • 0020488632 scopus 로고
    • Cross-linking studies of the protein topography of rat liver microsomes
    • Baskin L.S., Yang C.S. Cross-linking studies of the protein topography of rat liver microsomes. Biochim. Biophys. Acta. 684:1982;263-271.
    • (1982) Biochim. Biophys. Acta , vol.684 , pp. 263-271
    • Baskin, L.S.1    Yang, C.S.2
  • 37
    • 0021206880 scopus 로고
    • Membrane-bound CTP:phosphocholine cytidylyltransferase regulates the rate of phosphatidylcholine synthesis in HeLa cells treated with unsaturated fatty acids
    • Pelech S.L., Cook H.W., Paddon H.B., Vance D.E. Membrane-bound CTP:phosphocholine cytidylyltransferase regulates the rate of phosphatidylcholine synthesis in HeLa cells treated with unsaturated fatty acids. Biochim. Biophys. Acta. 795:1984;433-440.
    • (1984) Biochim. Biophys. Acta , vol.795 , pp. 433-440
    • Pelech, S.L.1    Cook, H.W.2    Paddon, H.B.3    Vance, D.E.4
  • 38
    • 0028835448 scopus 로고
    • Effect of cytidine on membrane phospholipid synthesis in rat striatal slices
    • Savci V., Wurtman R.J. Effect of cytidine on membrane phospholipid synthesis in rat striatal slices. J. Neurochem. 64:1995;378-384.
    • (1995) J. Neurochem. , vol.64 , pp. 378-384
    • Savci, V.1    Wurtman, R.J.2
  • 39
    • 0026637566 scopus 로고
    • Enhancement by cytidine of membrane phospholipid synthesis
    • Coviella I.L.G., Wurtman R.J. Enhancement by cytidine of membrane phospholipid synthesis. J. Neurochem. 59:1992;338-343.
    • (1992) J. Neurochem. , vol.59 , pp. 338-343
    • Coviella, I.L.G.1    Wurtman, R.J.2
  • 40
    • 0032557153 scopus 로고    scopus 로고
    • Studies on the regulation of CTP:phosphocholine cytidylyltransferase using permeabilized HEP G2 cells: Evidence that both active and inactive enzyme are membrane-bound
    • Weinhold P.A., Barrett D. Studies on the regulation of CTP:phosphocholine cytidylyltransferase using permeabilized HEP G2 cells: evidence that both active and inactive enzyme are membrane-bound. Biochim. Biophys. Acta. 1391:1998;307-319.
    • (1998) Biochim. Biophys. Acta , vol.1391 , pp. 307-319
    • Weinhold, P.A.1    Barrett, D.2
  • 41
    • 0031973259 scopus 로고    scopus 로고
    • Cytidylyltransferase-binding protein is identical to transcytosis-associated protein (TAP/p115) and enhances the lipid activation of cytidylyltransferase
    • Feldman D.A., Weinhold P.A. Cytidylyltransferase-binding protein is identical to transcytosis-associated protein (TAP/p115) and enhances the lipid activation of cytidylyltransferase. J. Biol. Chem. 273:1998;102-109.
    • (1998) J. Biol. Chem. , vol.273 , pp. 102-109
    • Feldman, D.A.1    Weinhold, P.A.2
  • 42
    • 0025334244 scopus 로고
    • Sphingosine inhibits the activity of rat liver CTP: Phosphocholine cytidylyltransferase
    • Sohal P.S., Cornell R.B. Sphingosine inhibits the activity of rat liver CTP: phosphocholine cytidylyltransferase. J. Biol. Chem. 265:1990;11746-11750.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11746-11750
    • Sohal, P.S.1    Cornell, R.B.2
  • 43
    • 0028987154 scopus 로고
    • Lysophosphatidylcholine and 1-O-octadecyl-2-O-methyl-rac-glycero-3-phosphocholine inhibit the CDP-choline pathway of phosphatidylcholine synthesis at the CTP:phosphocholine cytidylyltransferase step
    • Boggs K.P., Rock C.O., Jackowski S. Lysophosphatidylcholine and 1-O-octadecyl-2-O-methyl-rac-glycero-3-phosphocholine inhibit the CDP-choline pathway of phosphatidylcholine synthesis at the CTP:phosphocholine cytidylyltransferase step. J. Biol. Chem. 270:1995;7757-7764.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7757-7764
    • Boggs, K.P.1    Rock, C.O.2    Jackowski, S.3
  • 44
    • 0032484590 scopus 로고    scopus 로고
    • The antiproliferative effect of hexadecylphosphocholine toward HL60 cells is prevented by exogenous lysophosphatidylcholine
    • Boggs K., Rock C.O., Jackowski S. The antiproliferative effect of hexadecylphosphocholine toward HL60 cells is prevented by exogenous lysophosphatidylcholine. Biochim. Biophys. Acta. 1389:1998;1-12.
    • (1998) Biochim. Biophys. Acta , vol.1389 , pp. 1-12
    • Boggs, K.1    Rock, C.O.2    Jackowski, S.3
  • 45
    • 0031892176 scopus 로고    scopus 로고
    • Apoptosis triggered by 1-O-octadecyl-2-O-methyl-rac-glycero-3-phosphocholine is prevented by increased expression of CTP:phosphocholine cytidylyltransferase
    • Baburina I., Jackowski S. Apoptosis triggered by 1-O-octadecyl-2-O-methyl-rac-glycero-3-phosphocholine is prevented by increased expression of CTP:phosphocholine cytidylyltransferase. J. Biol. Chem. 273:1998;2169-2173.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2169-2173
    • Baburina, I.1    Jackowski, S.2
  • 46
    • 0023657208 scopus 로고
    • Molecular cloning and characterization of the gene encoding cholinephosphate cytidylyltransferase in Saccharomyces cerevisiae
    • Tsukagoshi Y., Nikawa J., Yamashita S. Molecular cloning and characterization of the gene encoding cholinephosphate cytidylyltransferase in Saccharomyces cerevisiae. Eur. J. Biochem. 169:1987;477-486.
    • (1987) Eur. J. Biochem. , vol.169 , pp. 477-486
    • Tsukagoshi, Y.1    Nikawa, J.2    Yamashita, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.