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Volumn 87, Issue 1, 2012, Pages 1-10

Enzymes in brain phospholipid docosahexaenoic acid accretion: A PL-ethora of potential PL-ayers

Author keywords

Acyl CoA synthetases; Acyl CoA:1 acyl sn glycerol 3 phosphate acyltransferases; Brain; Docosahexaenoic acid; Fatty acid transport proteins; Fatty acyl CoA reductase; Land's pathway; Lipid enzymes; Phospholipids; Plasmalogens; Transacylases

Indexed keywords

1 ALKYL 2 ACETYLGLYCEROPHOSPHOCHOLINE ESTERASE; 1 ALKYL 2 ACYLGLYCEROL 3 PHOSPHATE; 1 ALKYL ACYLGLYCEROL 3 PHOSPHOETHANOLAMINE PHOSPHOCHOLINE; 1 ALKYLGLYCEROL 3 PHOSPHATE; CD36 ANTIGEN; DOCOSAHEXAENOIC ACID; FATTY ACID; FATTY ACID TRANSPORTER; GLYCEROL 3 PHOSPHATE ACYLTRANSFERASE; LYSOPHOSPHATIDIC ACID; PHOSPHOLIPID; POLYUNSATURATED FATTY ACID; UNCLASSIFIED DRUG;

EID: 84864082331     PISSN: 09523278     EISSN: 15322823     Source Type: Journal    
DOI: 10.1016/j.plefa.2012.06.001     Document Type: Review
Times cited : (36)

References (88)
  • 1
    • 77951979020 scopus 로고    scopus 로고
    • Effects of long-chain polyunsaturated fatty acid supplementation on neurodevelopment in childhood: a review of human studies
    • Ryan A.S., Astwood J.D., Gautier S., Kuratko C.N., Nelson E.B., Salem N. Effects of long-chain polyunsaturated fatty acid supplementation on neurodevelopment in childhood: a review of human studies. Prostaglandins Leukot. Essent. Fatty Acids 2010, 82(4-6):305-314.
    • (2010) Prostaglandins Leukot. Essent. Fatty Acids , vol.82 , Issue.4-6 , pp. 305-314
    • Ryan, A.S.1    Astwood, J.D.2    Gautier, S.3    Kuratko, C.N.4    Nelson, E.B.5    Salem, N.6
  • 2
    • 79959973322 scopus 로고    scopus 로고
    • Omega-3 polyunsaturated fatty acids in Alzheimer's disease: key questions and partial answers
    • Calon F. Omega-3 polyunsaturated fatty acids in Alzheimer's disease: key questions and partial answers. Curr. Alzheimer Res. 2011, 8(5):470-478.
    • (2011) Curr. Alzheimer Res. , vol.8 , Issue.5 , pp. 470-478
    • Calon, F.1
  • 3
    • 77949673613 scopus 로고    scopus 로고
    • DHA may prevent age-related dementia
    • Cole G.M., Frautschy S.A. DHA may prevent age-related dementia. J. Nutr. 2010, 140(4):869-874.
    • (2010) J. Nutr. , vol.140 , Issue.4 , pp. 869-874
    • Cole, G.M.1    Frautschy, S.A.2
  • 5
    • 27644474967 scopus 로고    scopus 로고
    • An extraordinary degree of structural specificity is required in neural phospholipids for optimal brain function: n-6 docosapentaenoic acid substitution for docosahexaenoic acid leads to a loss in spatial task performance
    • Lim S.Y., Hoshiba J., Salem N. An extraordinary degree of structural specificity is required in neural phospholipids for optimal brain function: n-6 docosapentaenoic acid substitution for docosahexaenoic acid leads to a loss in spatial task performance. J. Neurochem. 2005, 95(3):848-857.
    • (2005) J. Neurochem. , vol.95 , Issue.3 , pp. 848-857
    • Lim, S.Y.1    Hoshiba, J.2    Salem, N.3
  • 6
    • 25444501242 scopus 로고    scopus 로고
    • N-3 fatty acid deficiency induced by a modified artificial rearing method leads to poorer performance in spatial learning tasks
    • Lim S.Y., Hoshiba J., Moriguchi T., Salem N. N-3 fatty acid deficiency induced by a modified artificial rearing method leads to poorer performance in spatial learning tasks. Pediatr. Res. 2005, 58(4):741-748.
    • (2005) Pediatr. Res. , vol.58 , Issue.4 , pp. 741-748
    • Lim, S.Y.1    Hoshiba, J.2    Moriguchi, T.3    Salem, N.4
  • 7
    • 35848939164 scopus 로고    scopus 로고
    • Artificial rearing with docosahexaenoic acid and n-6 docosapentaenoic acid alters rat tissue fatty acid composition
    • Stark K.D., Lim S.Y., Salem N. Artificial rearing with docosahexaenoic acid and n-6 docosapentaenoic acid alters rat tissue fatty acid composition. J. Lipid Res. 2007, 48(11):2471-2477.
    • (2007) J. Lipid Res. , vol.48 , Issue.11 , pp. 2471-2477
    • Stark, K.D.1    Lim, S.Y.2    Salem, N.3
  • 8
    • 35448999303 scopus 로고    scopus 로고
    • Membrane phospholipid composition may contribute to exceptional longevity of the naked mole-rat (Heterocephalus glaber): a comparative study using shotgun lipidomics
    • Mitchell T.W., Buffenstein R., Hulbert A.J. Membrane phospholipid composition may contribute to exceptional longevity of the naked mole-rat (Heterocephalus glaber): a comparative study using shotgun lipidomics. Exp. Gerontol. 2007, 42(11):1053-1062.
    • (2007) Exp. Gerontol. , vol.42 , Issue.11 , pp. 1053-1062
    • Mitchell, T.W.1    Buffenstein, R.2    Hulbert, A.J.3
  • 9
    • 0031980129 scopus 로고    scopus 로고
    • Chronic dietary n-3 polyunsaturated fatty acids deficiency affects the fatty acid composition of plasmenylethanolamine and phosphatidylethanolamine differently in rat frontal cortex, striatum, and cerebellum
    • Favreliere S., Barrier L., Durand G., Chalon S., Tallineau C. Chronic dietary n-3 polyunsaturated fatty acids deficiency affects the fatty acid composition of plasmenylethanolamine and phosphatidylethanolamine differently in rat frontal cortex, striatum, and cerebellum. Lipids 1998, 33(4):401-407.
    • (1998) Lipids , vol.33 , Issue.4 , pp. 401-407
    • Favreliere, S.1    Barrier, L.2    Durand, G.3    Chalon, S.4    Tallineau, C.5
  • 10
    • 0030808624 scopus 로고    scopus 로고
    • Dietary alpha-linolenic acid increases the biosynthesis of the choline glycerophospholipids from [14C]CDPcholine in rat liver and kidney but not in brain
    • Kim K.S., Park E.J., Lee C.W., Joo H.T., Yeo Y.K. Dietary alpha-linolenic acid increases the biosynthesis of the choline glycerophospholipids from [14C]CDPcholine in rat liver and kidney but not in brain. Neurochem. Res. 1997, 22(10):1291-1297.
    • (1997) Neurochem. Res. , vol.22 , Issue.10 , pp. 1291-1297
    • Kim, K.S.1    Park, E.J.2    Lee, C.W.3    Joo, H.T.4    Yeo, Y.K.5
  • 11
    • 0021260660 scopus 로고
    • Studies on ether phospholipids. II. Comparative composition of various tissues from human, rat and guinea pig
    • Diagne A., Fauvel J., Record M., Chap H., Douste-Blazy L. Studies on ether phospholipids. II. Comparative composition of various tissues from human, rat and guinea pig. Biochim. Biophys. Acta 1984, 793(2):221-231.
    • (1984) Biochim. Biophys. Acta , vol.793 , Issue.2 , pp. 221-231
    • Diagne, A.1    Fauvel, J.2    Record, M.3    Chap, H.4    Douste-Blazy, L.5
  • 12
    • 0035887367 scopus 로고    scopus 로고
    • Separation and quantitation of phospholipids and their ether analogues by high-performance liquid chromatography
    • Guan Z., Grunler J., Piao S., Sindelar P.J. Separation and quantitation of phospholipids and their ether analogues by high-performance liquid chromatography. Anal. Biochem. 2001, 297(2):137-143.
    • (2001) Anal. Biochem. , vol.297 , Issue.2 , pp. 137-143
    • Guan, Z.1    Grunler, J.2    Piao, S.3    Sindelar, P.J.4
  • 13
    • 0032770167 scopus 로고    scopus 로고
    • Decrease and structural modifications of phosphatidylethanolamine plasmalogen in the brain with Alzheimer disease
    • Guan Z., Wang Y., Cairns N.J., Lantos P.L., Dallner G., Sindelar P.J. Decrease and structural modifications of phosphatidylethanolamine plasmalogen in the brain with Alzheimer disease. J. Neuropathol. Exp. Neurol. 1999, 58(7):740-747.
    • (1999) J. Neuropathol. Exp. Neurol. , vol.58 , Issue.7 , pp. 740-747
    • Guan, Z.1    Wang, Y.2    Cairns, N.J.3    Lantos, P.L.4    Dallner, G.5    Sindelar, P.J.6
  • 14
  • 15
    • 23844432885 scopus 로고    scopus 로고
    • Alpha-linolenic acid does not contribute appreciably to docosahexaenoic acid within brain phospholipids of adult rats fed a diet enriched in docosahexaenoic acid
    • DeMar J.C., Ma K., Chang L., Bell J.M., Rapoport S.I. Alpha-linolenic acid does not contribute appreciably to docosahexaenoic acid within brain phospholipids of adult rats fed a diet enriched in docosahexaenoic acid. J. Neurochem. 2005, 94(4):1063-1076.
    • (2005) J. Neurochem. , vol.94 , Issue.4 , pp. 1063-1076
    • DeMar, J.C.1    Ma, K.2    Chang, L.3    Bell, J.M.4    Rapoport, S.I.5
  • 16
    • 35348852575 scopus 로고    scopus 로고
    • A model for fatty acid transport into the brain
    • Hamilton J.A., Brunaldi K. A model for fatty acid transport into the brain. J. Mol. Neurosci. 2007, 33(1):12-17.
    • (2007) J. Mol. Neurosci. , vol.33 , Issue.1 , pp. 12-17
    • Hamilton, J.A.1    Brunaldi, K.2
  • 17
    • 38049098106 scopus 로고    scopus 로고
    • The low density lipoprotein receptor is not necessary for maintaining mouse brain polyunsaturated fatty acid concentrations
    • Chen C.T., Ma D.W., Kim J.H., Mount H.T., Bazinet R.P. The low density lipoprotein receptor is not necessary for maintaining mouse brain polyunsaturated fatty acid concentrations. J. Lipid Res. 2008, 49(1):147-152.
    • (2008) J. Lipid Res. , vol.49 , Issue.1 , pp. 147-152
    • Chen, C.T.1    Ma, D.W.2    Kim, J.H.3    Mount, H.T.4    Bazinet, R.P.5
  • 18
    • 77953287047 scopus 로고    scopus 로고
    • Genetic ablation of CD36 does not alter mouse brain polyunsaturated fatty acid concentrations
    • Song B.J., Elbert A., Rahman T., Orr S.K., Chen C.T., Febbraio M., Bazinet R.P. Genetic ablation of CD36 does not alter mouse brain polyunsaturated fatty acid concentrations. Lipids 2010, 45(4):291-299.
    • (2010) Lipids , vol.45 , Issue.4 , pp. 291-299
    • Song, B.J.1    Elbert, A.2    Rahman, T.3    Orr, S.K.4    Chen, C.T.5    Febbraio, M.6    Bazinet, R.P.7
  • 19
    • 77951630116 scopus 로고    scopus 로고
    • The very low density lipoprotein receptor is not necessary for maintaining brain polyunsaturated fatty acid concentrations
    • Rahman T., Taha A.Y., Song B.J., Orr S.K., Liu Z., Chen C.T., Bazinet R.P. The very low density lipoprotein receptor is not necessary for maintaining brain polyunsaturated fatty acid concentrations. Prostaglandins Leukot. Essent. Fatty Acids 2010, 82(2-3):141-145.
    • (2010) Prostaglandins Leukot. Essent. Fatty Acids , vol.82 , Issue.2-3 , pp. 141-145
    • Rahman, T.1    Taha, A.Y.2    Song, B.J.3    Orr, S.K.4    Liu, Z.5    Chen, C.T.6    Bazinet, R.P.7
  • 20
    • 0028152492 scopus 로고
    • Expression cloning and characterization of a novel adipocyte long chain fatty acid transport protein
    • Schaffer J.E., Lodish H.F. Expression cloning and characterization of a novel adipocyte long chain fatty acid transport protein. Cell 1994, 79(3):427-436.
    • (1994) Cell , vol.79 , Issue.3 , pp. 427-436
    • Schaffer, J.E.1    Lodish, H.F.2
  • 21
    • 0141566277 scopus 로고    scopus 로고
    • Transmembrane movement of exogenous long-chain fatty acids: proteins, enzymes, and vectorial esterification
    • table
    • Black P.N., DiRusso C.C. Transmembrane movement of exogenous long-chain fatty acids: proteins, enzymes, and vectorial esterification. Microbiol. Mol. Biol. Rev. 2003, 67(3):454-472. table.
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , Issue.3 , pp. 454-472
    • Black, P.N.1    DiRusso, C.C.2
  • 22
    • 0033579432 scopus 로고    scopus 로고
    • The fatty acid transport protein (FATP1) is a very long chain acyl-CoA synthetase
    • Coe N.R., Smith A.J., Frohnert B.I., Watkins P.A., Bernlohr D.A. The fatty acid transport protein (FATP1) is a very long chain acyl-CoA synthetase. J. Biol. Chem. 1999, 274(51):36300-36304.
    • (1999) J. Biol. Chem. , vol.274 , Issue.51 , pp. 36300-36304
    • Coe, N.R.1    Smith, A.J.2    Frohnert, B.I.3    Watkins, P.A.4    Bernlohr, D.A.5
  • 23
    • 79954988524 scopus 로고    scopus 로고
    • Fatty acid transport protein expression in human brain and potential role in fatty acid transport across human brain microvessel endothelial cells
    • Mitchell R.W., On N.H., Del Bigio M.R., Miller D.W., Hatch G.M. Fatty acid transport protein expression in human brain and potential role in fatty acid transport across human brain microvessel endothelial cells. J. Neurochem. 2011, 117(4):735-746.
    • (2011) J. Neurochem. , vol.117 , Issue.4 , pp. 735-746
    • Mitchell, R.W.1    On, N.H.2    Del Bigio, M.R.3    Miller, D.W.4    Hatch, G.M.5
  • 24
    • 33847170487 scopus 로고    scopus 로고
    • Placental transfer of long-chain polyunsaturated fatty acids (LC-PUFA)
    • Koletzko B., Larque E., Demmelmair H. Placental transfer of long-chain polyunsaturated fatty acids (LC-PUFA). J. Perinat. Med. 2007, 35(Suppl 1):S5-11.
    • (2007) J. Perinat. Med. , vol.35 , Issue.SUPPL. 1
    • Koletzko, B.1    Larque, E.2    Demmelmair, H.3
  • 25
    • 0035972814 scopus 로고    scopus 로고
    • Mouse fatty acid transport protein 4 (FATP4): characterization of the gene and functional assessment as a very long chain acyl-CoA synthetase
    • Herrmann T., Buchkremer F., Gosch I., Hall A.M., Bernlohr D.A., Stremmel W. Mouse fatty acid transport protein 4 (FATP4): characterization of the gene and functional assessment as a very long chain acyl-CoA synthetase. Gene 2001, 270(1-2):31-40.
    • (2001) Gene , vol.270 , Issue.1-2 , pp. 31-40
    • Herrmann, T.1    Buchkremer, F.2    Gosch, I.3    Hall, A.M.4    Bernlohr, D.A.5    Stremmel, W.6
  • 26
    • 0037119475 scopus 로고    scopus 로고
    • Functional role of fatty acyl-coenzyme A synthetase in the transmembrane movement and activation of exogenous long-chain fatty acids. Amino acid residues within the ATP/AMP signature motif of Escherichia coli FadD are required for enzyme activity and fatty acid transport
    • Weimar J.D., DiRusso C.C., Delio R., Black P.N. Functional role of fatty acyl-coenzyme A synthetase in the transmembrane movement and activation of exogenous long-chain fatty acids. Amino acid residues within the ATP/AMP signature motif of Escherichia coli FadD are required for enzyme activity and fatty acid transport. J. Biol. Chem. 2002, 277(33):29369-29376.
    • (2002) J. Biol. Chem. , vol.277 , Issue.33 , pp. 29369-29376
    • Weimar, J.D.1    DiRusso, C.C.2    Delio, R.3    Black, P.N.4
  • 27
    • 37249092959 scopus 로고    scopus 로고
    • Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human genome
    • Watkins P.A., Maiguel D., Jia Z., Pevsner J. Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human genome. J. Lipid Res. 2007, 48(12):2736-2750.
    • (2007) J. Lipid Res. , vol.48 , Issue.12 , pp. 2736-2750
    • Watkins, P.A.1    Maiguel, D.2    Jia, Z.3    Pevsner, J.4
  • 28
    • 33748752324 scopus 로고    scopus 로고
    • Rat long-chain acyl-CoA synthetase mRNA, protein, and activity vary in tissue distribution and in response to diet
    • Mashek D.G., Li L.O., Coleman R.A. Rat long-chain acyl-CoA synthetase mRNA, protein, and activity vary in tissue distribution and in response to diet. J. Lipid Res. 2006, 47(9):2004-2010.
    • (2006) J. Lipid Res. , vol.47 , Issue.9 , pp. 2004-2010
    • Mashek, D.G.1    Li, L.O.2    Coleman, R.A.3
  • 29
    • 0026528995 scopus 로고
    • Cloning and functional expression of a novel long-chain acyl-CoA synthetase expressed in brain
    • Fujino T., Yamamoto T. Cloning and functional expression of a novel long-chain acyl-CoA synthetase expressed in brain. J. Biochem. 1992, 111(2):197-203.
    • (1992) J. Biochem. , vol.111 , Issue.2 , pp. 197-203
    • Fujino, T.1    Yamamoto, T.2
  • 30
    • 15444373653 scopus 로고    scopus 로고
    • Long-chain acyl-CoA synthetase 6 preferentially promotes DHA metabolism
    • Marszalek J.R., Kitidis C., DiRusso C.C., Lodish H.F. Long-chain acyl-CoA synthetase 6 preferentially promotes DHA metabolism. J. Biol. Chem. 2005, 280(11):10817-10826.
    • (2005) J. Biol. Chem. , vol.280 , Issue.11 , pp. 10817-10826
    • Marszalek, J.R.1    Kitidis, C.2    DiRusso, C.C.3    Lodish, H.F.4
  • 31
    • 2642562066 scopus 로고    scopus 로고
    • Acyl-CoA synthetase 2 overexpression enhances fatty acid internalization and neurite outgrowth
    • Marszalek J.R., Kitidis C., Dararutana A., Lodish H.F. Acyl-CoA synthetase 2 overexpression enhances fatty acid internalization and neurite outgrowth. J. Biol. Chem. 2004, 279(23):23882-23891.
    • (2004) J. Biol. Chem. , vol.279 , Issue.23 , pp. 23882-23891
    • Marszalek, J.R.1    Kitidis, C.2    Dararutana, A.3    Lodish, H.F.4
  • 32
    • 0029953175 scopus 로고    scopus 로고
    • Molecular characterization and expression of rat acyl-CoA synthetase 3
    • Fujino T., Kang M.J., Suzuki H., Iijima H., Yamamoto T. Molecular characterization and expression of rat acyl-CoA synthetase 3. J. Biol. Chem. 1996, 271(28):16748-16752.
    • (1996) J. Biol. Chem. , vol.271 , Issue.28 , pp. 16748-16752
    • Fujino, T.1    Kang, M.J.2    Suzuki, H.3    Iijima, H.4    Yamamoto, T.5
  • 33
    • 13444306413 scopus 로고    scopus 로고
    • Characterization of recombinant long-chain rat acyl-CoA synthetase isoforms 3 and 6: identification of a novel variant of isoform 6
    • Van Horn C.G., Caviglia J.M., Li L.O., Wang S., Granger D.A., Coleman R.A. Characterization of recombinant long-chain rat acyl-CoA synthetase isoforms 3 and 6: identification of a novel variant of isoform 6. Biochemistry 2005, 44(5):1635-1642.
    • (2005) Biochemistry , vol.44 , Issue.5 , pp. 1635-1642
    • Van Horn, C.G.1    Caviglia, J.M.2    Li, L.O.3    Wang, S.4    Granger, D.A.5    Coleman, R.A.6
  • 34
    • 78651374376 scopus 로고    scopus 로고
    • Valproate uncompetitively inhibits arachidonic acid acylation by rat acyl-CoA synthetase 4: relevance to valproate's efficacy against bipolar disorder
    • Shimshoni J.A., Basselin M., Li L.O., Coleman R.A., Rapoport S.I., Modi H.R. Valproate uncompetitively inhibits arachidonic acid acylation by rat acyl-CoA synthetase 4: relevance to valproate's efficacy against bipolar disorder. Biochim. Biophys. Acta 2011, 1811(3):163-169.
    • (2011) Biochim. Biophys. Acta , vol.1811 , Issue.3 , pp. 163-169
    • Shimshoni, J.A.1    Basselin, M.2    Li, L.O.3    Coleman, R.A.4    Rapoport, S.I.5    Modi, H.R.6
  • 35
    • 0345171460 scopus 로고    scopus 로고
    • Enzymes of triacylglycerol synthesis and their regulation
    • Coleman R.A., Lee D.P. Enzymes of triacylglycerol synthesis and their regulation. Prog. Lipid Res. 2004, 43(2):134-176.
    • (2004) Prog. Lipid Res. , vol.43 , Issue.2 , pp. 134-176
    • Coleman, R.A.1    Lee, D.P.2
  • 36
    • 0014938124 scopus 로고
    • Initial incorporation into rat liver glycerolipids of intraportally injected (3H)glycerol
    • Akesson B., Elovson J., Arvidson G. Initial incorporation into rat liver glycerolipids of intraportally injected (3H)glycerol. Biochim. Biophys. Acta 1970, 210(1):15-27.
    • (1970) Biochim. Biophys. Acta , vol.210 , Issue.1 , pp. 15-27
    • Akesson, B.1    Elovson, J.2    Arvidson, G.3
  • 37
    • 0031589572 scopus 로고    scopus 로고
    • CDNA cloning and expression of murine 1-acyl-sn-glycerol-3-phosphate acyltransferase
    • Kume K., Shimizu T. cDNA cloning and expression of murine 1-acyl-sn-glycerol-3-phosphate acyltransferase. Biochem. Biophys. Res. Commun. 1997, 237(3):663-666.
    • (1997) Biochem. Biophys. Res. Commun. , vol.237 , Issue.3 , pp. 663-666
    • Kume, K.1    Shimizu, T.2
  • 38
  • 39
    • 12844249385 scopus 로고    scopus 로고
    • Cloning and characterization of murine 1-acyl-sn-glycerol 3-phosphate acyltransferases and their regulation by PPARalpha in murine heart
    • Lu B., Jiang Y.J., Zhou Y., Xu F.Y., Hatch G.M., Choy P.C. Cloning and characterization of murine 1-acyl-sn-glycerol 3-phosphate acyltransferases and their regulation by PPARalpha in murine heart. Biochem. J. 2005, 385(Pt 2):469-477.
    • (2005) Biochem. J. , vol.385 , Issue.PART 2 , pp. 469-477
    • Lu, B.1    Jiang, Y.J.2    Zhou, Y.3    Xu, F.Y.4    Hatch, G.M.5    Choy, P.C.6
  • 40
    • 0032512848 scopus 로고    scopus 로고
    • Characterization of a human lysophosphatidic acid acyltransferase that is encoded by a gene located in the class III region of the human major histocompatibility complex
    • Aguado B., Campbell R.D. Characterization of a human lysophosphatidic acid acyltransferase that is encoded by a gene located in the class III region of the human major histocompatibility complex. J. Biol. Chem. 1998, 273(7):4096-4105.
    • (1998) J. Biol. Chem. , vol.273 , Issue.7 , pp. 4096-4105
    • Aguado, B.1    Campbell, R.D.2
  • 42
    • 0030925549 scopus 로고    scopus 로고
    • Cloning and expression of two human lysophosphatidic acid acyltransferase cDNAs that enhance cytokine-induced signaling responses in cells
    • West J., Tompkins C.K., Balantac N., Nudelman E., Meengs B., White T., Bursten S., Coleman J., Kumar A., et al. Cloning and expression of two human lysophosphatidic acid acyltransferase cDNAs that enhance cytokine-induced signaling responses in cells. DNA Cell Biol. 1997, 16(6):691-701.
    • (1997) DNA Cell Biol. , vol.16 , Issue.6 , pp. 691-701
    • West, J.1    Tompkins, C.K.2    Balantac, N.3    Nudelman, E.4    Meengs, B.5    White, T.6    Bursten, S.7    Coleman, J.8    Kumar, A.9
  • 43
    • 0035145685 scopus 로고    scopus 로고
    • Overexpression of 1-acyl-glycerol-3-phosphate acyltransferase-alpha enhances lipid storage in cellular models of adipose tissue and skeletal muscle
    • Ruan H., Pownall H.J. Overexpression of 1-acyl-glycerol-3-phosphate acyltransferase-alpha enhances lipid storage in cellular models of adipose tissue and skeletal muscle. Diabetes 2001, 50(2):233-240.
    • (2001) Diabetes , vol.50 , Issue.2 , pp. 233-240
    • Ruan, H.1    Pownall, H.J.2
  • 44
    • 79953231189 scopus 로고    scopus 로고
    • Enzymatic activities of the human AGPAT isoform 3 and isoform 5: localization of AGPAT5 to mitochondria
    • Prasad S.S., Garg A., Agarwal A.K. Enzymatic activities of the human AGPAT isoform 3 and isoform 5: localization of AGPAT5 to mitochondria. J. Lipid Res. 2011, 52(3):451-462.
    • (2011) J. Lipid Res. , vol.52 , Issue.3 , pp. 451-462
    • Prasad, S.S.1    Garg, A.2    Agarwal, A.K.3
  • 45
    • 34447104351 scopus 로고    scopus 로고
    • Functional characterization of human 1-acylglycerol-3-phosphate-O-acyltransferase isoform 9: cloning, tissue distribution, gene structure, and enzymatic activity
    • Agarwal A.K., Sukumaran S., Bartz R., Barnes R.I., Garg A. Functional characterization of human 1-acylglycerol-3-phosphate-O-acyltransferase isoform 9: cloning, tissue distribution, gene structure, and enzymatic activity. J. Endocrinol. 2007, 193(3):445-457.
    • (2007) J. Endocrinol. , vol.193 , Issue.3 , pp. 445-457
    • Agarwal, A.K.1    Sukumaran, S.2    Bartz, R.3    Barnes, R.I.4    Garg, A.5
  • 46
    • 77956858262 scopus 로고    scopus 로고
    • Enzymatic activity of the human 1-acylglycerol-3-phosphate-O-acyltransferase isoform 11: upregulated in breast and cervical cancers
    • Agarwal A.K., Garg A. Enzymatic activity of the human 1-acylglycerol-3-phosphate-O-acyltransferase isoform 11: upregulated in breast and cervical cancers. J. Lipid Res. 2010, 51(8):2143-2152.
    • (2010) J. Lipid Res. , vol.51 , Issue.8 , pp. 2143-2152
    • Agarwal, A.K.1    Garg, A.2
  • 48
    • 0034465086 scopus 로고    scopus 로고
    • CDNA cloning, expression and chromosomal localization of two human lysophosphatidic acid acyltransferases
    • Eberhardt C., Gray P.W., Tjoelker L.W. cDNA cloning, expression and chromosomal localization of two human lysophosphatidic acid acyltransferases. Adv. Exp. Med. Biol. 1999, 469:351-356.
    • (1999) Adv. Exp. Med. Biol. , vol.469 , pp. 351-356
    • Eberhardt, C.1    Gray, P.W.2    Tjoelker, L.W.3
  • 49
    • 67649421649 scopus 로고    scopus 로고
    • Functional characterization of the human 1-acylglycerol-3-phosphate-O-acyltransferase isoform 10/glycerol-3-phosphate acyltransferase isoform 3
    • Sukumaran S., Barnes R.I., Garg A., Agarwal A.K. Functional characterization of the human 1-acylglycerol-3-phosphate-O-acyltransferase isoform 10/glycerol-3-phosphate acyltransferase isoform 3. J. Mol. Endocrinol. 2009, 42(6):469-478.
    • (2009) J. Mol. Endocrinol. , vol.42 , Issue.6 , pp. 469-478
    • Sukumaran, S.1    Barnes, R.I.2    Garg, A.3    Agarwal, A.K.4
  • 51
    • 49649090149 scopus 로고    scopus 로고
    • Molecular identification of a novel mammalian brain isoform of acyl-CoA:lysophospholipid acyltransferase with prominent ethanolamine lysophospholipid acylating activity, LPEAT2
    • Cao J., Shan D., Revett T., Li D., Wu L., Liu W., Tobin J.F., Gimeno R.E. Molecular identification of a novel mammalian brain isoform of acyl-CoA:lysophospholipid acyltransferase with prominent ethanolamine lysophospholipid acylating activity, LPEAT2. J. Biol. Chem. 2008, 283(27):19049-19057.
    • (2008) J. Biol. Chem. , vol.283 , Issue.27 , pp. 19049-19057
    • Cao, J.1    Shan, D.2    Revett, T.3    Li, D.4    Wu, L.5    Liu, W.6    Tobin, J.F.7    Gimeno, R.E.8
  • 52
    • 33646145315 scopus 로고    scopus 로고
    • Functional characterization of human 1-acylglycerol-3-phosphate acyltransferase isoform 8: cloning, tissue distribution, gene structure, and enzymatic activity
    • Agarwal A.K., Barnes R.I., Garg A. Functional characterization of human 1-acylglycerol-3-phosphate acyltransferase isoform 8: cloning, tissue distribution, gene structure, and enzymatic activity. Arch. Biochem. Biophys. 2006, 449(1-2):64-76.
    • (2006) Arch. Biochem. Biophys. , vol.449 , Issue.1-2 , pp. 64-76
    • Agarwal, A.K.1    Barnes, R.I.2    Garg, A.3
  • 53
    • 0030844660 scopus 로고    scopus 로고
    • Acyltransferases and transacylases involved in fatty acid remodeling of phospholipids and metabolism of bioactive lipids in mammalian cells
    • Yamashita A., Sugiura T., Waku K. Acyltransferases and transacylases involved in fatty acid remodeling of phospholipids and metabolism of bioactive lipids in mammalian cells. J. Biochem. 1997, 122(1):1-16.
    • (1997) J. Biochem. , vol.122 , Issue.1 , pp. 1-16
    • Yamashita, A.1    Sugiura, T.2    Waku, K.3
  • 54
    • 0016666155 scopus 로고
    • Substrate-selectivity of rat liver microsomal 1,2-diacylglycerol: CDP-choline(ethanolamine) choline(ethanolamine)phosphotransferase in utilizing endogenous substrates
    • Kanoh H., Ohno K. Substrate-selectivity of rat liver microsomal 1,2-diacylglycerol: CDP-choline(ethanolamine) choline(ethanolamine)phosphotransferase in utilizing endogenous substrates. Biochim. Biophys. Acta 1975, 380(2):199-207.
    • (1975) Biochim. Biophys. Acta , vol.380 , Issue.2 , pp. 199-207
    • Kanoh, H.1    Ohno, K.2
  • 55
    • 0017842211 scopus 로고
    • Differential utilization of 1-palmitoyl and 1-stearoyl homologues of various unsaturated 1,2-diacyl-sn-glycerols for phosphatidylcholine and phosphatidylethanolamine synthesis in rat liver microsomes
    • Holub B.J. Differential utilization of 1-palmitoyl and 1-stearoyl homologues of various unsaturated 1,2-diacyl-sn-glycerols for phosphatidylcholine and phosphatidylethanolamine synthesis in rat liver microsomes. J. Biol. Chem. 1978, 253(3):691-696.
    • (1978) J. Biol. Chem. , vol.253 , Issue.3 , pp. 691-696
    • Holub, B.J.1
  • 56
    • 2342572271 scopus 로고    scopus 로고
    • Phospholipid biosynthesis in mammalian cells
    • Vance J.E., Vance D.E. Phospholipid biosynthesis in mammalian cells. Biochem. Cell Biol. 2004, 82(1):113-128.
    • (2004) Biochem. Cell Biol. , vol.82 , Issue.1 , pp. 113-128
    • Vance, J.E.1    Vance, D.E.2
  • 57
    • 34547131318 scopus 로고    scopus 로고
    • Novel metabolism of docosahexaenoic acid in neural cells
    • Kim H.Y. Novel metabolism of docosahexaenoic acid in neural cells. J. Biol. Chem. 2007, 282(26):18661-18665.
    • (2007) J. Biol. Chem. , vol.282 , Issue.26 , pp. 18661-18665
    • Kim, H.Y.1
  • 58
    • 0942279701 scopus 로고    scopus 로고
    • Substrate preference in phosphatidylserine biosynthesis for docosahexaenoic acid containing species
    • Kim H.Y., Bigelow J., Kevala J.H. Substrate preference in phosphatidylserine biosynthesis for docosahexaenoic acid containing species. Biochemistry 2004, 43(4):1030-1036.
    • (2004) Biochemistry , vol.43 , Issue.4 , pp. 1030-1036
    • Kim, H.Y.1    Bigelow, J.2    Kevala, J.H.3
  • 59
  • 60
    • 0035914356 scopus 로고    scopus 로고
    • Cloning of DGAT2, a second mammalian diacylglycerol acyltransferase, and related family members
    • Cases S., Stone S.J., Zhou P., Yen E., Tow B., Lardizabal K.D., Voelker T., Farese R.V. Cloning of DGAT2, a second mammalian diacylglycerol acyltransferase, and related family members. J. Biol. Chem. 2001, 276(42):38870-38876.
    • (2001) J. Biol. Chem. , vol.276 , Issue.42 , pp. 38870-38876
    • Cases, S.1    Stone, S.J.2    Zhou, P.3    Yen, E.4    Tow, B.5    Lardizabal, K.D.6    Voelker, T.7    Farese, R.V.8
  • 61
    • 0016268661 scopus 로고
    • Effect of different fatty acids on glycerolipid synthesis in isolated rat hepatocytes
    • Sundler R., Akesson B., Nilsson A. Effect of different fatty acids on glycerolipid synthesis in isolated rat hepatocytes. J. Biol. Chem. 1974, 249(16):5102-5107.
    • (1974) J. Biol. Chem. , vol.249 , Issue.16 , pp. 5102-5107
    • Sundler, R.1    Akesson, B.2    Nilsson, A.3
  • 62
    • 35348922263 scopus 로고    scopus 로고
    • Neuronal specific increase of phosphatidylserine by docosahexaenoic acid
    • Guo M., Stockert L., Akbar M., Kim H.Y. Neuronal specific increase of phosphatidylserine by docosahexaenoic acid. J. Mol. Neurosci. 2007, 33(1):67-73.
    • (2007) J. Mol. Neurosci. , vol.33 , Issue.1 , pp. 67-73
    • Guo, M.1    Stockert, L.2    Akbar, M.3    Kim, H.Y.4
  • 63
    • 4444258170 scopus 로고    scopus 로고
    • Mammalian wax biosynthesis. I. Identification of two fatty acyl-Coenzyme A reductases with different substrate specificities and tissue distributions
    • Cheng J.B., Russell D.W. Mammalian wax biosynthesis. I. Identification of two fatty acyl-Coenzyme A reductases with different substrate specificities and tissue distributions. J. Biol. Chem. 2004, 279(36):37789-37797.
    • (2004) J. Biol. Chem. , vol.279 , Issue.36 , pp. 37789-37797
    • Cheng, J.B.1    Russell, D.W.2
  • 64
    • 0025371616 scopus 로고
    • Purification and properties of acyl/alkyl dihydroxyacetone-phosphate reductase from guinea pig liver peroxisomes
    • Datta S.C., Ghosh M.K., Hajra A.K. Purification and properties of acyl/alkyl dihydroxyacetone-phosphate reductase from guinea pig liver peroxisomes. J. Biol. Chem. 1990, 265(14):8268-8274.
    • (1990) J. Biol. Chem. , vol.265 , Issue.14 , pp. 8268-8274
    • Datta, S.C.1    Ghosh, M.K.2    Hajra, A.K.3
  • 65
    • 0035102918 scopus 로고    scopus 로고
    • Plasmalogens: biosynthesis and functions
    • Nagan N., Zoeller R.A. Plasmalogens: biosynthesis and functions. Prog. Lipid Res. 2001, 40(3):199-229.
    • (2001) Prog. Lipid Res. , vol.40 , Issue.3 , pp. 199-229
    • Nagan, N.1    Zoeller, R.A.2
  • 66
    • 0017357108 scopus 로고
    • 1-Alkyl-sn-glycero-3-phosphate: acyl-CoA acyltransferase in rat brain microsomes
    • Fleming P.J., Hajra A.K. 1-Alkyl-sn-glycero-3-phosphate: acyl-CoA acyltransferase in rat brain microsomes. J. Biol. Chem. 1977, 252(5):1663-1672.
    • (1977) J. Biol. Chem. , vol.252 , Issue.5 , pp. 1663-1672
    • Fleming, P.J.1    Hajra, A.K.2
  • 67
    • 0014429578 scopus 로고
    • Acyl coenzyme A:1-alkenyl-glycero-3-phosphorylcholine acyltransferase action in plasmalogen biosynthesis
    • Waku K., Lands W.E. Acyl coenzyme A:1-alkenyl-glycero-3-phosphorylcholine acyltransferase action in plasmalogen biosynthesis. J. Biol. Chem. 1968, 243(10):2654-2659.
    • (1968) J. Biol. Chem. , vol.243 , Issue.10 , pp. 2654-2659
    • Waku, K.1    Lands, W.E.2
  • 68
    • 0014861970 scopus 로고
    • Acyltransferase activity to 1-O-alkyl-glycero-3-phosphorylcholine in sarcoplasmic reticulum
    • Waku K., Nakazawa Y. Acyltransferase activity to 1-O-alkyl-glycero-3-phosphorylcholine in sarcoplasmic reticulum. J. Biochem. 1970, 68(4):459-466.
    • (1970) J. Biochem. , vol.68 , Issue.4 , pp. 459-466
    • Waku, K.1    Nakazawa, Y.2
  • 69
    • 0017708075 scopus 로고
    • Regulation of the fatty acid composition of alkyl ether phospholipid in Ehrlich ascites tumor cells. The substrate specificities of 1-O-alkylglycerol 3-phosphate and 1-O-alkylglycero-3-phosphocholine acyltransferases
    • Waku K., Nakazawa Y. Regulation of the fatty acid composition of alkyl ether phospholipid in Ehrlich ascites tumor cells. The substrate specificities of 1-O-alkylglycerol 3-phosphate and 1-O-alkylglycero-3-phosphocholine acyltransferases. J. Biochem. 1977, 82(6):1779-1784.
    • (1977) J. Biochem. , vol.82 , Issue.6 , pp. 1779-1784
    • Waku, K.1    Nakazawa, Y.2
  • 70
    • 0019841316 scopus 로고
    • The synthesis of choline plasmalogen by the methylation pathway in rat brain
    • Mozzi R., Siepi D., Andreoli V., Porcellati G. The synthesis of choline plasmalogen by the methylation pathway in rat brain. FEBS Lett. 1981, 131(1):115-118.
    • (1981) FEBS Lett. , vol.131 , Issue.1 , pp. 115-118
    • Mozzi, R.1    Siepi, D.2    Andreoli, V.3    Porcellati, G.4
  • 72
    • 34548214548 scopus 로고    scopus 로고
    • Prostaglandin synthesis in rat brain astrocytes is under the control of the n-3 docosahexaenoic acid, released by group VIB calcium-independent phospholipase A2
    • Strokin M., Sergeeva M., Reiser G. Prostaglandin synthesis in rat brain astrocytes is under the control of the n-3 docosahexaenoic acid, released by group VIB calcium-independent phospholipase A2. J. Neurochem. 2007, 102(6):1771-1782.
    • (2007) J. Neurochem. , vol.102 , Issue.6 , pp. 1771-1782
    • Strokin, M.1    Sergeeva, M.2    Reiser, G.3
  • 74
    • 27944499029 scopus 로고    scopus 로고
    • Plasmalogen metabolism-related enzymes in rat brain during aging: influence of n-3 fatty acid intake
    • Andre A., Juaneda P., Sebedio J.L., Chardigny J.M. Plasmalogen metabolism-related enzymes in rat brain during aging: influence of n-3 fatty acid intake. Biochimie 2006, 88(1):103-111.
    • (2006) Biochimie , vol.88 , Issue.1 , pp. 103-111
    • Andre, A.1    Juaneda, P.2    Sebedio, J.L.3    Chardigny, J.M.4
  • 75
    • 66349088254 scopus 로고    scopus 로고
    • Recent progress on acyl CoA: lysophospholipid acyltransferase research
    • Shindou H., Hishikawa D., Harayama T., Yuki K., Shimizu T. Recent progress on acyl CoA: lysophospholipid acyltransferase research. J. Lipid Res. 2009, 50:S46-S51. Suppl.
    • (2009) J. Lipid Res. , vol.50 , Issue.SUPPL.
    • Shindou, H.1    Hishikawa, D.2    Harayama, T.3    Yuki, K.4    Shimizu, T.5
  • 76
    • 33745976120 scopus 로고    scopus 로고
    • Cloning and characterization of mouse lung-type acyl-CoA:lysophosphatidylcholine acyltransferase 1 (LPCAT1). Expression in alveolar type II cells and possible involvement in surfactant production
    • Nakanishi H., Shindou H., Hishikawa D., Harayama T., Ogasawara R., Suwabe A., Taguchi R., Shimizu T. Cloning and characterization of mouse lung-type acyl-CoA:lysophosphatidylcholine acyltransferase 1 (LPCAT1). Expression in alveolar type II cells and possible involvement in surfactant production. J. Biol. Chem. 2006, 281(29):20140-20147.
    • (2006) J. Biol. Chem. , vol.281 , Issue.29 , pp. 20140-20147
    • Nakanishi, H.1    Shindou, H.2    Hishikawa, D.3    Harayama, T.4    Ogasawara, R.5    Suwabe, A.6    Taguchi, R.7    Shimizu, T.8
  • 77
    • 33746781022 scopus 로고    scopus 로고
    • Identification and characterization of a lysophosphatidylcholine acyltransferase in alveolar type II cells
    • Chen X., Hyatt B.A., Mucenski M.L., Mason R.J., Shannon J.M. Identification and characterization of a lysophosphatidylcholine acyltransferase in alveolar type II cells. Proc. Natl. Acad. Sci. USA 2006, 103(31):11724-11729.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , Issue.31 , pp. 11724-11729
    • Chen, X.1    Hyatt, B.A.2    Mucenski, M.L.3    Mason, R.J.4    Shannon, J.M.5
  • 78
    • 34250343830 scopus 로고    scopus 로고
    • A single enzyme catalyzes both platelet-activating factor production and membrane biogenesis of inflammatory cells. Cloning and characterization of acetyl-CoA:LYSO-PAF acetyltransferase
    • Shindou H., Hishikawa D., Nakanishi H., Harayama T., Ishii S., Taguchi R., Shimizu T. A single enzyme catalyzes both platelet-activating factor production and membrane biogenesis of inflammatory cells. Cloning and characterization of acetyl-CoA:LYSO-PAF acetyltransferase. J. Biol. Chem. 2007, 282(9):6532-6539.
    • (2007) J. Biol. Chem. , vol.282 , Issue.9 , pp. 6532-6539
    • Shindou, H.1    Hishikawa, D.2    Nakanishi, H.3    Harayama, T.4    Ishii, S.5    Taguchi, R.6    Shimizu, T.7
  • 79
    • 42949095543 scopus 로고    scopus 로고
    • Discovery of a lysophospholipid acyltransferase family essential for membrane asymmetry and diversity
    • Hishikawa D., Shindou H., Kobayashi S., Nakanishi H., Taguchi R., Shimizu T. Discovery of a lysophospholipid acyltransferase family essential for membrane asymmetry and diversity. Proc. Natl. Acad. Sci. USA 2008, 105(8):2830-2835.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , Issue.8 , pp. 2830-2835
    • Hishikawa, D.1    Shindou, H.2    Kobayashi, S.3    Nakanishi, H.4    Taguchi, R.5    Shimizu, T.6
  • 80
    • 0024419559 scopus 로고
    • Selective acyl transfer in the reacylation of brain glycerophospholipids. Comparison of three acylation systems for 1-alk-1'-enylglycero-3-phosphoethanolamine, 1-acylglycero-3-phosphoethanolamine and 1-acylglycero-3-phosphocholine in rat brain microsomes
    • Masuzawa Y., Sugiura T., Sprecher H., Waku K. Selective acyl transfer in the reacylation of brain glycerophospholipids. Comparison of three acylation systems for 1-alk-1'-enylglycero-3-phosphoethanolamine, 1-acylglycero-3-phosphoethanolamine and 1-acylglycero-3-phosphocholine in rat brain microsomes. Biochim. Biophys. Acta 1989, 1005(1):1-12.
    • (1989) Biochim. Biophys. Acta , vol.1005 , Issue.1 , pp. 1-12
    • Masuzawa, Y.1    Sugiura, T.2    Sprecher, H.3    Waku, K.4
  • 81
    • 0023279772 scopus 로고
    • Selective transacylation of 1-O-alkylglycerophosphoethanolamine by docosahexaenoate and arachidonate in rat brain microsomes
    • Ojima A., Nakagawa Y., Sugiura T., Masuzawa Y., Waku K. Selective transacylation of 1-O-alkylglycerophosphoethanolamine by docosahexaenoate and arachidonate in rat brain microsomes. J. Neurochem. 1987, 48(5):1403-1410.
    • (1987) J. Neurochem. , vol.48 , Issue.5 , pp. 1403-1410
    • Ojima, A.1    Nakagawa, Y.2    Sugiura, T.3    Masuzawa, Y.4    Waku, K.5
  • 82
    • 0025312564 scopus 로고
    • Phospholipid synthesis by extracellular phospholipase A2 in organic solvents
    • Pernas P., Olivier J.L., Legoy M.D., Bereziat G. Phospholipid synthesis by extracellular phospholipase A2 in organic solvents. Biochem. Biophys. Res. Commun. 1990, 168(2):644-650.
    • (1990) Biochem. Biophys. Res. Commun. , vol.168 , Issue.2 , pp. 644-650
    • Pernas, P.1    Olivier, J.L.2    Legoy, M.D.3    Bereziat, G.4
  • 83
    • 0023154711 scopus 로고
    • Transacylation of lyso platelet-activating factor and other lysophospholipids by macrophage microsomes. Distinct donor and acceptor selectivities
    • Sugiura T., Masuzawa Y., Nakagawa Y., Waku K. Transacylation of lyso platelet-activating factor and other lysophospholipids by macrophage microsomes. Distinct donor and acceptor selectivities. J. Biol. Chem. 1987, 262(3):1199-1205.
    • (1987) J. Biol. Chem. , vol.262 , Issue.3 , pp. 1199-1205
    • Sugiura, T.1    Masuzawa, Y.2    Nakagawa, Y.3    Waku, K.4
  • 84
    • 0021089326 scopus 로고
    • Arachidonoyl transacylase in human platelets. Coenzyme A-independent transfer of arachidonate from phosphatidylcholine to lysoplasmenylethanolamine
    • Kramer R.M., Deykin D. Arachidonoyl transacylase in human platelets. Coenzyme A-independent transfer of arachidonate from phosphatidylcholine to lysoplasmenylethanolamine. J. Biol. Chem. 1983, 258(22):13806-13811.
    • (1983) J. Biol. Chem. , vol.258 , Issue.22 , pp. 13806-13811
    • Kramer, R.M.1    Deykin, D.2
  • 85
    • 0024297324 scopus 로고
    • Coenzyme A-dependent transacylation system in rabbit liver microsomes
    • Sugiura T., Masuzawa Y., Waku K. Coenzyme A-dependent transacylation system in rabbit liver microsomes. J. Biol. Chem. 1988, 263(33):17490-17498.
    • (1988) J. Biol. Chem. , vol.263 , Issue.33 , pp. 17490-17498
    • Sugiura, T.1    Masuzawa, Y.2    Waku, K.3
  • 86
    • 0028104966 scopus 로고
    • Purification and characterization of glycerophosphate acyltransferase from rat liver mitochondria
    • Vancura A., Haldar D. Purification and characterization of glycerophosphate acyltransferase from rat liver mitochondria. J. Biol. Chem. 1994, 269(44):27209-27215.
    • (1994) J. Biol. Chem. , vol.269 , Issue.44 , pp. 27209-27215
    • Vancura, A.1    Haldar, D.2
  • 88
    • 33845941190 scopus 로고    scopus 로고
    • Molecular identification of microsomal acyl-CoA:glycerol-3-phosphate acyltransferase, a key enzyme in de novo triacylglycerol synthesis
    • Cao J., Li J.L., Li D., Tobin J.F., Gimeno R.E. Molecular identification of microsomal acyl-CoA:glycerol-3-phosphate acyltransferase, a key enzyme in de novo triacylglycerol synthesis. Proc. Natl. Acad. Sci. USA 2006, 103(52):19695-19700.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , Issue.52 , pp. 19695-19700
    • Cao, J.1    Li, J.L.2    Li, D.3    Tobin, J.F.4    Gimeno, R.E.5


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