메뉴 건너뛰기




Volumn 72, Issue 20, 2015, Pages 3931-3952

DAG tales: The multiple faces of diacylglycerol - Stereochemistry, metabolism, and signaling

Author keywords

Acyltransferase; Hydrolase; Insulin; Kinase; Lipase

Indexed keywords

ACYLTRANSFERASE; DIACYLGLYCEROL; MESSENGER RNA; PROTEIN KINASE C; SPHINGOMYELIN; TRIACYLGLYCEROL LIPASE; INSULIN; PHOSPHOLIPASE C;

EID: 84942371067     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-015-1982-3     Document Type: Review
Times cited : (202)

References (242)
  • 1
    • 0020169638 scopus 로고
    • Basic principles of the CIP system and proposals for a revision
    • Prelog V, Helmchen G (1982) Basic principles of the CIP system and proposals for a revision. Angew Chemie, Int Ed english 21:567-583
    • (1982) Angew Chemie, Int Ed English , vol.21 , pp. 567-583
    • Prelog, V.1    Helmchen, G.2
  • 3
    • 0037113954 scopus 로고    scopus 로고
    • The surface of lipid droplets is a phospholipid monolayer with a unique fatty acid composition
    • 1:CAS:528:DC%2BD38Xos1akur8%3D 12221100
    • Tauchi-Sato K, Ozeki S, Houjou T et al (2002) The surface of lipid droplets is a phospholipid monolayer with a unique fatty acid composition. J Biol Chem 277:44507-44512
    • (2002) J Biol Chem , vol.277 , pp. 44507-44512
    • Tauchi-Sato, K.1    Ozeki, S.2    Houjou, T.3
  • 4
    • 0032911957 scopus 로고    scopus 로고
    • Mechanisms of lipid-body formation
    • 1:CAS:528:DyaK1MXkslSjtLk%3D 10203758
    • Murphy DJ, Vance J (1999) Mechanisms of lipid-body formation. Trends Biochem Sci 24:109-115
    • (1999) Trends Biochem Sci , vol.24 , pp. 109-115
    • Murphy, D.J.1    Vance, J.2
  • 5
    • 1442285086 scopus 로고    scopus 로고
    • Synthesis and function of hepatic very-low-density lipoprotein
    • 1:CAS:528:DC%2BD2cXisVGrtrc%3D 14748713
    • Gibbons GF, Wiggins D, Brown A-M, Hebbachi A-M (2004) Synthesis and function of hepatic very-low-density lipoprotein. Biochem Soc Trans 32:59-64
    • (2004) Biochem Soc Trans , vol.32 , pp. 59-64
    • Gibbons, G.F.1    Wiggins, D.2    Brown, A.-M.3    Hebbachi, A.-M.4
  • 6
    • 8844226709 scopus 로고    scopus 로고
    • Fat mobilization in adipose tissue is promoted by adipose triglyceride lipase
    • 1:CAS:528:DC%2BD2cXpvVektLw%3D 15550674
    • Zimmermann R, Strauss JG, Haemmerle G et al (2004) Fat mobilization in adipose tissue is promoted by adipose triglyceride lipase. Science 306:1383-1386
    • (2004) Science , vol.306 , pp. 1383-1386
    • Zimmermann, R.1    Strauss, J.G.2    Haemmerle, G.3
  • 7
    • 8744297386 scopus 로고    scopus 로고
    • Desnutrin, an adipocyte gene encoding a novel patatin domain-containing protein, is induced by fasting and glucocorticoids: Ectopic expression of desnutrin increases triglyceride hydrolysis
    • 1:CAS:528:DC%2BD2cXptFejsLc%3D 15337759
    • Villena JA, Roy S, Sarkadi-Nagy E et al (2004) Desnutrin, an adipocyte gene encoding a novel patatin domain-containing protein, is induced by fasting and glucocorticoids: ectopic expression of desnutrin increases triglyceride hydrolysis. J Biol Chem 279:47066-47075
    • (2004) J Biol Chem , vol.279 , pp. 47066-47075
    • Villena, J.A.1    Roy, S.2    Sarkadi-Nagy, E.3
  • 8
    • 10344262633 scopus 로고    scopus 로고
    • Identification, cloning, expression, and purification of three novel human calcium-independent phospholipase A2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities
    • 1:CAS:528:DC%2BD2cXpslKjsbo%3D 15364929
    • Jenkins CM, Mancuso DJ, Yan W et al (2004) Identification, cloning, expression, and purification of three novel human calcium-independent phospholipase A2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities. J Biol Chem 279:48968-48975
    • (2004) J Biol Chem , vol.279 , pp. 48968-48975
    • Jenkins, C.M.1    Mancuso, D.J.2    Yan, W.3
  • 9
    • 33748745960 scopus 로고    scopus 로고
    • Characterization of the human patatin-like phospholipase family
    • 1:CAS:528:DC%2BD28Xpt1Gjsrg%3D 16799181
    • Wilson PA, Gardner SD, Lambie NM et al (2006) Characterization of the human patatin-like phospholipase family. J Lipid Res 47:1940-1949
    • (2006) J Lipid Res , vol.47 , pp. 1940-1949
    • Wilson, P.A.1    Gardner, S.D.2    Lambie, N.M.3
  • 10
    • 0037984885 scopus 로고    scopus 로고
    • The crystal structure, mutagenesis, and activity studies reveal that patatin is a lipid acyl hydrolase with a Ser-Asp catalytic dyad
    • 1:CAS:528:DC%2BD3sXjsleisr4%3D 12779324
    • Rydel TJ, Williams JM, Krieger E et al (2003) The crystal structure, mutagenesis, and activity studies reveal that patatin is a lipid acyl hydrolase with a Ser-Asp catalytic dyad. Biochemistry 42:6696-6708
    • (2003) Biochemistry , vol.42 , pp. 6696-6708
    • Rydel, T.J.1    Williams, J.M.2    Krieger, E.3
  • 11
    • 0030118333 scopus 로고    scopus 로고
    • A cytosolic phospholipase A2 from potato tissues appears to be patatin
    • 1:CAS:528:DyaK28Xis12ksbg%3D 8673343
    • Senda K, Yoshioka H, Doke N, Kawakita K (1996) A cytosolic phospholipase A2 from potato tissues appears to be patatin. Plant Cell Physiol 37:347-353
    • (1996) Plant Cell Physiol , vol.37 , pp. 347-353
    • Senda, K.1    Yoshioka, H.2    Doke, N.3    Kawakita, K.4
  • 12
    • 34247168090 scopus 로고    scopus 로고
    • Analysis of lipolytic protein trafficking and interactions in adipocytes
    • 17189257
    • Granneman JG, Moore HP, Granneman RL et al (2006) Analysis of lipolytic protein trafficking and interactions in adipocytes. J Biol Chem 282:5726-5735
    • (2006) J Biol Chem , vol.282 , pp. 5726-5735
    • Granneman, J.G.1    Moore, H.P.2    Granneman, R.L.3
  • 13
    • 84925746640 scopus 로고    scopus 로고
    • Adipose triglyceride lipase is involved in the mobilization of triglyceride and retinoid stores of hepatic stellate cells
    • 1:CAS:528:DC%2BC2MXjslymtLs%3D
    • Taschler U, Schreiber R, Chitraju C et al (2015) Adipose triglyceride lipase is involved in the mobilization of triglyceride and retinoid stores of hepatic stellate cells. Biochim Biophys Acta Mol Cell Biol Lipids 1851:937-945
    • (2015) Biochim Biophys Acta Mol Cell Biol Lipids , vol.1851 , pp. 937-945
    • Taschler, U.1    Schreiber, R.2    Chitraju, C.3
  • 14
    • 34447094951 scopus 로고    scopus 로고
    • A comparative study of human GS2, its paralogues, and its rat orthologue
    • 1:CAS:528:DC%2BD2sXnslSqu70%3D 17603008
    • Gao JG, Simon M (2007) A comparative study of human GS2, its paralogues, and its rat orthologue. Biochem Biophys Res Commun 360:501-506
    • (2007) Biochem Biophys Res Commun , vol.360 , pp. 501-506
    • Gao, J.G.1    Simon, M.2
  • 15
    • 27444433258 scopus 로고    scopus 로고
    • Expression, regulation, and triglyceride hydrolase activity of Adiponutrin family members
    • 1:CAS:528:DC%2BD2MXhtF2iu7nP 16150821
    • Lake AC, Sun Y, Li JL et al (2005) Expression, regulation, and triglyceride hydrolase activity of Adiponutrin family members. J Lipid Res 46:2477-2487
    • (2005) J Lipid Res , vol.46 , pp. 2477-2487
    • Lake, A.C.1    Sun, Y.2    Li, J.L.3
  • 16
    • 37149052557 scopus 로고    scopus 로고
    • PPARgamma regulates adipose triglyceride lipase in adipocytes in vitro and in vivo
    • 2819189 1:CAS:528:DC%2BD2sXhsVGls7jJ 17848638
    • Kershaw EE, Schupp M, Guan HP et al (2007) PPARgamma regulates adipose triglyceride lipase in adipocytes in vitro and in vivo. Am J Physiol Endocrinol Metab 293:E1736-E1745
    • (2007) Am J Physiol Endocrinol Metab , vol.293 , pp. E1736-E1745
    • Kershaw, E.E.1    Schupp, M.2    Guan, H.P.3
  • 17
    • 23644436551 scopus 로고    scopus 로고
    • Isoproterenol, TNFalpha, and insulin downregulate adipose triglyceride lipase in 3T3-L1 adipocytes
    • 1:CAS:528:DC%2BD2MXnslymtbk%3D 16009485
    • Kralisch S, Klein J, Lossner U et al (2005) Isoproterenol, TNFalpha, and insulin downregulate adipose triglyceride lipase in 3T3-L1 adipocytes. Mol Cell Endocrinol 240:43-49
    • (2005) Mol Cell Endocrinol , vol.240 , pp. 43-49
    • Kralisch, S.1    Klein, J.2    Lossner, U.3
  • 18
    • 34347219137 scopus 로고    scopus 로고
    • Adipose triglyceride lipase and hormone-sensitive lipase protein expression is decreased in the obese insulin-resistant state
    • 1:CAS:528:DC%2BD2sXmslOgs7c%3D 17356053
    • Jocken JWE, Langin D, Smit E et al (2007) Adipose triglyceride lipase and hormone-sensitive lipase protein expression is decreased in the obese insulin-resistant state. J Clin Endocrinol Metab 92:2292-2299
    • (2007) J Clin Endocrinol Metab , vol.92 , pp. 2292-2299
    • Jocken, J.W.E.1    Langin, D.2    Smit, E.3
  • 19
    • 33646128723 scopus 로고    scopus 로고
    • Adipose triglyceride lipase-mediated lipolysis of cellular fat stores is activated by CGI-58 and defective in Chanarin-Dorfman Syndrome
    • 1:CAS:528:DC%2BD28XltF2isL0%3D 16679289
    • Lass A, Zimmermann R, Haemmerle G et al (2006) Adipose triglyceride lipase-mediated lipolysis of cellular fat stores is activated by CGI-58 and defective in Chanarin-Dorfman Syndrome. Cell Metab 3:309-319
    • (2006) Cell Metab , vol.3 , pp. 309-319
    • Lass, A.1    Zimmermann, R.2    Haemmerle, G.3
  • 20
    • 77249118270 scopus 로고    scopus 로고
    • The G(0)/G(1) switch gene 2 regulates adipose lipolysis through association with adipose triglyceride lipase
    • 3658843 1:CAS:528:DC%2BC3cXlsVajurc%3D 20197052
    • Yang X, Lu X, Lombes M et al (2010) The G(0)/G(1) switch gene 2 regulates adipose lipolysis through association with adipose triglyceride lipase. Cell Metab 11:194-205
    • (2010) Cell Metab , vol.11 , pp. 194-205
    • Yang, X.1    Lu, X.2    Lombes, M.3
  • 21
    • 84867364913 scopus 로고    scopus 로고
    • G0/G1 switch gene-2 regulates human adipocyte lipolysis by affecting activity and localization of adipose triglyceride lipase
    • 3466000 1:CAS:528:DC%2BC38XhsFClsrbK 22891293
    • Schweiger M, Paar M, Eder C et al (2012) G0/G1 switch gene-2 regulates human adipocyte lipolysis by affecting activity and localization of adipose triglyceride lipase. J Lipid Res 53:2307-2317
    • (2012) J Lipid Res , vol.53 , pp. 2307-2317
    • Schweiger, M.1    Paar, M.2    Eder, C.3
  • 22
    • 33646462136 scopus 로고    scopus 로고
    • Defective lipolysis and altered energy metabolism in mice lacking adipose triglyceride lipase
    • 1:CAS:528:DC%2BD28XktVGntL4%3D 16675698
    • Haemmerle G, Lass A, Zimmermann R et al (2006) Defective lipolysis and altered energy metabolism in mice lacking adipose triglyceride lipase. Science 312:734-737
    • (2006) Science , vol.312 , pp. 734-737
    • Haemmerle, G.1    Lass, A.2    Zimmermann, R.3
  • 23
    • 84870372459 scopus 로고    scopus 로고
    • Studies on the substrate and stereo/regioselectivity of adipose triglyceride lipase, hormone-sensitive lipase, and diacylglycerol-O-acyltransferase enzymes
    • 3510842 1:CAS:528:DC%2BC38XhslGjsL%2FE 23066022
    • Eichmann TO, Kumari M, Haas J et al (2012) Studies on the substrate and stereo/regioselectivity of adipose triglyceride lipase, hormone-sensitive lipase, and diacylglycerol-O-acyltransferase enzymes. J Biol Chem 287(49):41446-41457
    • (2012) J Biol Chem , vol.287 , Issue.49 , pp. 41446-41457
    • Eichmann, T.O.1    Kumari, M.2    Haas, J.3
  • 24
    • 85003154718 scopus 로고
    • The lipolytic response to corticotropin
    • 1:CAS:528:DyaF3MXntFGhuw%3D%3D 13715328
    • Hollenberg CH, Raben MS, Astwood EB (1961) The lipolytic response to corticotropin. Endocrinology 68:589-598
    • (1961) Endocrinology , vol.68 , pp. 589-598
    • Hollenberg, C.H.1    Raben, M.S.2    Astwood, E.B.3
  • 25
    • 78651164698 scopus 로고
    • Hormone-sensitive lipase and monoglyceride lipase activities in adipose tissue
    • 1:CAS:528:DyaF2cXisVKmtg%3D%3D 14169138
    • Vaughan M, Berger JE, Steinberg D (1964) Hormone-sensitive lipase and monoglyceride lipase activities in adipose tissue. J Biol Chem 239:401-409
    • (1964) J Biol Chem , vol.239 , pp. 401-409
    • Vaughan, M.1    Berger, J.E.2    Steinberg, D.3
  • 26
    • 0348049843 scopus 로고    scopus 로고
    • Molecular mechanisms regulating hormone-sensitive lipase and lipolysis
    • 1:CAS:528:DC%2BD3sXps1yqu74%3D 14641008
    • Holm C (2003) Molecular mechanisms regulating hormone-sensitive lipase and lipolysis. Biochem Soc Trans 31:1120-1124
    • (2003) Biochem Soc Trans , vol.31 , pp. 1120-1124
    • Holm, C.1
  • 27
    • 0028274779 scopus 로고
    • Regulation of hormone-sensitive lipase during fasting
    • 1:CAS:528:DyaK2cXitFGqs7s%3D 8141275
    • Sztalryd C, Kraemer FB (1994) Regulation of hormone-sensitive lipase during fasting. Am J Physiol 266:E179-E185
    • (1994) Am J Physiol , vol.266 , pp. E179-E185
    • Sztalryd, C.1    Kraemer, F.B.2
  • 28
    • 0029806454 scopus 로고    scopus 로고
    • Domain-structure analysis of recombinant rat hormone-sensitive lipase
    • 1217784 1:CAS:528:DyaK28XmsVKrsLw%3D 8912675
    • Osterlund T, Danielsson B, Degerman E et al (1996) Domain-structure analysis of recombinant rat hormone-sensitive lipase. Biochem J 319(Pt 2):411-420
    • (1996) Biochem J , vol.319 , pp. 411-420
    • Osterlund, T.1    Danielsson, B.2    Degerman, E.3
  • 29
    • 0033056941 scopus 로고    scopus 로고
    • Domain identification of hormone-sensitive lipase by circular dichroism and fluorescence spectroscopy, limited proteolysis, and mass spectrometry
    • 1:CAS:528:DyaK1MXjsV2gsrg%3D 10336425
    • Osterlund T, Beussman DJ, Julenius K et al (1999) Domain identification of hormone-sensitive lipase by circular dichroism and fluorescence spectroscopy, limited proteolysis, and mass spectrometry. J Biol Chem 274:15382-15388
    • (1999) J Biol Chem , vol.274 , pp. 15382-15388
    • Osterlund, T.1    Beussman, D.J.2    Julenius, K.3
  • 30
    • 0031041639 scopus 로고    scopus 로고
    • Identification of essential aspartic acid and histidine residues of hormone-sensitive lipase: Apparent residues of the catalytic triad
    • 1:CAS:528:DyaK2sXhtlyisLY%3D 9091313
    • Osterlund T, Contreras JA, Holm C (1997) Identification of essential aspartic acid and histidine residues of hormone-sensitive lipase: apparent residues of the catalytic triad. FEBS Lett 403:259-262
    • (1997) FEBS Lett , vol.403 , pp. 259-262
    • Osterlund, T.1    Contreras, J.A.2    Holm, C.3
  • 31
    • 0027198857 scopus 로고
    • Gene organization and primary structure of human hormone-sensitive lipase: Possible significance of a sequence homology with a lipase of Moraxella TA144, an antarctic bacterium
    • 46620 1:CAS:528:DyaK3sXks1Kmsbc%3D 8506334
    • Langin D, Laurell H, Holst LS et al (1993) Gene organization and primary structure of human hormone-sensitive lipase: possible significance of a sequence homology with a lipase of Moraxella TA144, an antarctic bacterium. Proc Natl Acad Sci USA 90:4897-4901
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 4897-4901
    • Langin, D.1    Laurell, H.2    Holst, L.S.3
  • 32
    • 0034059932 scopus 로고    scopus 로고
    • Hormone-sensitive lipase functions as an oligomer
    • 1:CAS:528:DC%2BD3cXpsVKksw%3D%3D 10694408
    • Shen WJ, Patel S, Hong R, Kraemer FB (2000) Hormone-sensitive lipase functions as an oligomer. Biochemistry 39:2392-2398
    • (2000) Biochemistry , vol.39 , pp. 2392-2398
    • Shen, W.J.1    Patel, S.2    Hong, R.3    Kraemer, F.B.4
  • 33
    • 0021069165 scopus 로고
    • Phosphorylation of hormone-sensitive lipase by cyclic AMP-dependent protein kinase
    • 1:STN:280:DyaL2c%2Fosl2iuw%3D%3D 6317686
    • Stralfors P, Belfrage P (1983) Phosphorylation of hormone-sensitive lipase by cyclic AMP-dependent protein kinase. J Biol Chem 258:15146-15152
    • (1983) J Biol Chem , vol.258 , pp. 15146-15152
    • Stralfors, P.1    Belfrage, P.2
  • 34
    • 0032560615 scopus 로고    scopus 로고
    • Mutational analysis of structural features of rat hormone-sensitive lipase
    • 1:CAS:528:DyaK1cXjsFegurc%3D 9636039
    • Shen WJ, Patel S, Natu V, Kraemer FB (1998) Mutational analysis of structural features of rat hormone-sensitive lipase. Biochemistry 37:8973-8979
    • (1998) Biochemistry , vol.37 , pp. 8973-8979
    • Shen, W.J.1    Patel, S.2    Natu, V.3    Kraemer, F.B.4
  • 35
    • 2642614548 scopus 로고    scopus 로고
    • Identification of novel phosphorylation sites in hormone-sensitive lipase that are phosphorylated in response to isoproterenol and govern activation properties in vitro
    • 1:CAS:528:DyaK1cXjvFSgsA%3D%3D 9417067
    • Anthonsen MW, Ronnstrand L, Wernstedt C et al (1998) Identification of novel phosphorylation sites in hormone-sensitive lipase that are phosphorylated in response to isoproterenol and govern activation properties in vitro. J Biol Chem 273:215-221
    • (1998) J Biol Chem , vol.273 , pp. 215-221
    • Anthonsen, M.W.1    Ronnstrand, L.2    Wernstedt, C.3
  • 36
    • 0021309466 scopus 로고
    • Regulation of adipose tissue lipolysis through reversible phosphorylation of hormone-sensitive lipase
    • 1:CAS:528:DyaL2cXktlehtrk%3D 6328925
    • Belfrage P, Fredrikson G, Olsson H, Stralfors P (1984) Regulation of adipose tissue lipolysis through reversible phosphorylation of hormone-sensitive lipase. Adv Cyclic Nucleotide Protein Phosphorylation Res 17:351-359
    • (1984) Adv Cyclic Nucleotide Protein Phosphorylation Res , vol.17 , pp. 351-359
    • Belfrage, P.1    Fredrikson, G.2    Olsson, H.3    Stralfors, P.4
  • 37
    • 0019847943 scopus 로고
    • Regulation of adipose-tissue lipolysis by phosphorylation of hormone-sensitive lipase
    • 1:CAS:528:DyaL38XhtlGqs7c%3D 6274818
    • Belfrage P, Fredrikson G, Nilsson NO, Stralfors P (1981) Regulation of adipose-tissue lipolysis by phosphorylation of hormone-sensitive lipase. Int J Obes 5:635-641
    • (1981) Int J Obes , vol.5 , pp. 635-641
    • Belfrage, P.1    Fredrikson, G.2    Nilsson, N.O.3    Stralfors, P.4
  • 38
    • 0011682519 scopus 로고
    • Hormonal regulation of hormone-sensitive lipase in intact adipocytes: Identification of phosphorylated sites and effects on the phosphorylation by lipolytic hormones and insulin
    • 345498 1:STN:280:DyaL2c3itF2msg%3D%3D 6374655
    • Stralfors P, Bjorgell P, Belfrage P (1984) Hormonal regulation of hormone-sensitive lipase in intact adipocytes: identification of phosphorylated sites and effects on the phosphorylation by lipolytic hormones and insulin. Proc Natl Acad Sci USA 81:3317-3321
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 3317-3321
    • Stralfors, P.1    Bjorgell, P.2    Belfrage, P.3
  • 39
    • 0025330929 scopus 로고
    • Identification and role of the basal phosphorylation site on hormone-sensitive lipase
    • 1:CAS:528:DyaK3cXksleks7w%3D 2165906
    • Garton AJ, Yeaman SJ (1990) Identification and role of the basal phosphorylation site on hormone-sensitive lipase. Eur J Biochem 191:245-250
    • (1990) Eur J Biochem , vol.191 , pp. 245-250
    • Garton, A.J.1    Yeaman, S.J.2
  • 40
    • 0029069574 scopus 로고
    • Perilipin is located on the surface layer of intracellular lipid droplets in adipocytes
    • 1:CAS:528:DyaK2MXms1Cntbo%3D 7665999
    • Blanchette-Mackie EJ, Dwyer NK, Barber T et al (1995) Perilipin is located on the surface layer of intracellular lipid droplets in adipocytes. J Lipid Res 36:1211-1226
    • (1995) J Lipid Res , vol.36 , pp. 1211-1226
    • Blanchette-Mackie, E.J.1    Dwyer, N.K.2    Barber, T.3
  • 41
    • 0034623950 scopus 로고    scopus 로고
    • Perilipin A increases triacylglycerol storage by decreasing the rate of triacylglycerol hydrolysis
    • 1:CAS:528:DC%2BD3cXoslymtrk%3D 10948207
    • Brasaemle DL, Rubin B, Harten IA et al (2000) Perilipin A increases triacylglycerol storage by decreasing the rate of triacylglycerol hydrolysis. J Biol Chem 275:38486-38493
    • (2000) J Biol Chem , vol.275 , pp. 38486-38493
    • Brasaemle, D.L.1    Rubin, B.2    Harten, I.A.3
  • 42
    • 33847714769 scopus 로고    scopus 로고
    • Control of adipose triglyceride lipase action by serine 517 of perilipin A globally regulates protein kinase A-stimulated lipolysis in adipocytes
    • 1:CAS:528:DC%2BD2sXit1OhsA%3D%3D 17114792
    • Miyoshi H, Perfield JW 2nd, Souza SC et al (2007) Control of adipose triglyceride lipase action by serine 517 of perilipin A globally regulates protein kinase A-stimulated lipolysis in adipocytes. J Biol Chem 282:996-1002
    • (2007) J Biol Chem , vol.282 , pp. 996-1002
    • Miyoshi, H.1    Perfield, J.W.2    Souza, S.C.3
  • 43
    • 33744944318 scopus 로고    scopus 로고
    • Perilipin promotes HSL-mediated adipocyte lipolysis via phosphorylation-dependent and independent mechanisms
    • 1:CAS:528:DC%2BD28Xlt1CktLk%3D 16595669
    • Miyoshi H, Souza SC, Zhang HH et al (2006) Perilipin promotes HSL-mediated adipocyte lipolysis via phosphorylation-dependent and independent mechanisms. J Biol Chem 281(23):15837-15844
    • (2006) J Biol Chem , vol.281 , Issue.23 , pp. 15837-15844
    • Miyoshi, H.1    Souza, S.C.2    Zhang, H.H.3
  • 44
    • 0037424252 scopus 로고    scopus 로고
    • Functional studies on native and mutated forms of perilipins. A role in protein kinase A-mediated lipolysis of triacylglycerols
    • 1:CAS:528:DC%2BD3sXhsF2hsbw%3D 12477720
    • Tansey JT, Huml AM, Vogt R et al (2003) Functional studies on native and mutated forms of perilipins. A role in protein kinase A-mediated lipolysis of triacylglycerols. J Biol Chem 278:8401-8406
    • (2003) J Biol Chem , vol.278 , pp. 8401-8406
    • Tansey, J.T.1    Huml, A.M.2    Vogt, R.3
  • 45
    • 0037477829 scopus 로고    scopus 로고
    • Perilipin A is essential for the translocation of hormone-sensitive lipase during lipolytic activation
    • 2172984 1:CAS:528:DC%2BD3sXkvFCmsr0%3D 12810697
    • Sztalryd C, Xu G, Dorward H et al (2003) Perilipin A is essential for the translocation of hormone-sensitive lipase during lipolytic activation. J Cell Biol 161:1093-1103
    • (2003) J Cell Biol , vol.161 , pp. 1093-1103
    • Sztalryd, C.1    Xu, G.2    Dorward, H.3
  • 46
    • 0026783771 scopus 로고
    • Mechanism of hormone-stimulated lipolysis in adipocytes: Translocation of hormone-sensitive lipase to the lipid storage droplet
    • 49955 1:CAS:528:DyaK38XmtV2ksbw%3D 1528859
    • Egan JJ, Greenberg AS, Chang MK et al (1992) Mechanism of hormone-stimulated lipolysis in adipocytes: translocation of hormone-sensitive lipase to the lipid storage droplet. Proc Natl Acad Sci USA 89:8537-8541
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 8537-8541
    • Egan, J.J.1    Greenberg, A.S.2    Chang, M.K.3
  • 47
    • 0242290249 scopus 로고    scopus 로고
    • Mutational analysis of the hormone-sensitive lipase translocation reaction in adipocytes
    • 1:CAS:528:DC%2BD3sXosFSrsbs%3D 12832420
    • Su CL, Sztalryd C, Contreras JA et al (2003) Mutational analysis of the hormone-sensitive lipase translocation reaction in adipocytes. J Biol Chem 278:43615-43619
    • (2003) J Biol Chem , vol.278 , pp. 43615-43619
    • Su, C.L.1    Sztalryd, C.2    Contreras, J.A.3
  • 48
    • 12944335303 scopus 로고    scopus 로고
    • Targeted disruption of hormone-sensitive lipase results in male sterility and adipocyte hypertrophy, but not in obesity
    • 15409 1:CAS:528:DC%2BD3cXot1ansQ%3D%3D 10639158
    • Osuga J, Ishibashi S, Oka T et al (2000) Targeted disruption of hormone-sensitive lipase results in male sterility and adipocyte hypertrophy, but not in obesity. Proc Natl Acad Sci USA 97:787-792
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 787-792
    • Osuga, J.1    Ishibashi, S.2    Oka, T.3
  • 49
    • 0344896634 scopus 로고    scopus 로고
    • Resistance to high-fat diet-induced obesity and altered expression of adipose-specific genes in HSL-deficient mice
    • 1:CAS:528:DC%2BD2cXhtFCmuw%3D%3D 12954598
    • Harada K, Shen WJ, Patel S et al (2003) Resistance to high-fat diet-induced obesity and altered expression of adipose-specific genes in HSL-deficient mice. Am J Physiol Endocrinol Metab 285:E1182-E1195
    • (2003) Am J Physiol Endocrinol Metab , vol.285 , pp. E1182-E1195
    • Harada, K.1    Shen, W.J.2    Patel, S.3
  • 50
    • 0344667491 scopus 로고    scopus 로고
    • Decreased fatty acid esterification compensates for the reduced lipolytic activity in hormone-sensitive lipase-deficient white adipose tissue
    • 1:CAS:528:DC%2BD3sXpslensbY%3D 12923228
    • Zimmermann R, Haemmerle G, Wagner EM et al (2003) Decreased fatty acid esterification compensates for the reduced lipolytic activity in hormone-sensitive lipase-deficient white adipose tissue. J Lipid Res 44:2089-2099
    • (2003) J Lipid Res , vol.44 , pp. 2089-2099
    • Zimmermann, R.1    Haemmerle, G.2    Wagner, E.M.3
  • 51
    • 0037085450 scopus 로고    scopus 로고
    • Hormone-sensitive lipase deficiency in mice causes diglyceride accumulation in adipose tissue, muscle, and testis
    • 1:CAS:528:DC%2BD38XhsFeqtLo%3D 11717312
    • Haemmerle G, Zimmermann R, Hayn M et al (2002) Hormone-sensitive lipase deficiency in mice causes diglyceride accumulation in adipose tissue, muscle, and testis. J Biol Chem 277:4806-4815
    • (2002) J Biol Chem , vol.277 , pp. 4806-4815
    • Haemmerle, G.1    Zimmermann, R.2    Hayn, M.3
  • 52
    • 0035257508 scopus 로고    scopus 로고
    • The adipose tissue phenotype of hormone-sensitive lipase deficiency in mice
    • 1:CAS:528:DC%2BD3MXkt1Kqsr8%3D 11316346
    • Wang SP, Laurin N, Himms-Hagen J et al (2001) The adipose tissue phenotype of hormone-sensitive lipase deficiency in mice. Obes Res 9:119-128
    • (2001) Obes Res , vol.9 , pp. 119-128
    • Wang, S.P.1    Laurin, N.2    Himms-Hagen, J.3
  • 53
    • 0019481108 scopus 로고
    • Hormone-sensitive lipase of rat adipose tissue. Purification and some properties
    • 1:CAS:528:DyaL3MXkt1Sgsrc%3D 7240206
    • Fredrikson G, Stralfors P, Nilsson NO, Belfrage P (1981) Hormone-sensitive lipase of rat adipose tissue. Purification and some properties. J Biol Chem 256:6311-6320
    • (1981) J Biol Chem , vol.256 , pp. 6311-6320
    • Fredrikson, G.1    Stralfors, P.2    Nilsson, N.O.3    Belfrage, P.4
  • 54
    • 0030983554 scopus 로고    scopus 로고
    • Retinyl ester hydrolysis and retinol efflux from BFC-1beta adipocytes
    • 1:CAS:528:DyaK2sXjsFOjurc%3D 9162045
    • Wei S, Lai K, Patel S et al (1997) Retinyl ester hydrolysis and retinol efflux from BFC-1beta adipocytes. J Biol Chem 272:14159-14165
    • (1997) J Biol Chem , vol.272 , pp. 14159-14165
    • Wei, S.1    Lai, K.2    Patel, S.3
  • 55
    • 0024386843 scopus 로고
    • P-nitrophenyl butyrate hydrolyzing activity of hormone-Sensitive lipase from bovine adipose tissue
    • 1:CAS:528:DyaL1MXkvFalur4%3D 2794798
    • Tsujita T, Ninomiya H, Okuda H (1989) P-nitrophenyl butyrate hydrolyzing activity of hormone-Sensitive lipase from bovine adipose tissue. J Lipid Res 30:997-1004
    • (1989) J Lipid Res , vol.30 , pp. 997-1004
    • Tsujita, T.1    Ninomiya, H.2    Okuda, H.3
  • 56
    • 0021016694 scopus 로고
    • Positional specificity of hormone-sensitive lipase from rat adipose tissue
    • 1:CAS:528:DyaL3sXmtVyltbo%3D 6643478
    • Fredrikson G, Belfrage P (1983) Positional specificity of hormone-sensitive lipase from rat adipose tissue. J Biol Chem 258:14253-14256
    • (1983) J Biol Chem , vol.258 , pp. 14253-14256
    • Fredrikson, G.1    Belfrage, P.2
  • 57
    • 71549120401 scopus 로고    scopus 로고
    • In vitro stereoselective hydrolysis of diacylglycerols by hormone-sensitive lipase
    • 1:CAS:528:DC%2BD1MXhsV2msrnF 19800417
    • Rodriguez JA, Ben Ali Y, Abdelkafi S et al (2010) In vitro stereoselective hydrolysis of diacylglycerols by hormone-sensitive lipase. Biochim Biophys Acta 1801:77-83
    • (2010) Biochim Biophys Acta , vol.1801 , pp. 77-83
    • Rodriguez, J.A.1    Ben, A.Y.2    Abdelkafi, S.3
  • 58
    • 0027080211 scopus 로고
    • Adipose hormone-sensitive lipase preferentially releases polyunsaturated fatty acids from triglycerides
    • 1:CAS:528:DyaK3sXls1yrtA%3D%3D 1362594
    • Gavino VC, Gavino GR (1992) Adipose hormone-sensitive lipase preferentially releases polyunsaturated fatty acids from triglycerides. Lipids 27:950-954
    • (1992) Lipids , vol.27 , pp. 950-954
    • Gavino, V.C.1    Gavino, G.R.2
  • 59
    • 33846029180 scopus 로고    scopus 로고
    • Adipose triglyceride lipase and hormone-sensitive lipase are the major enzymes in adipose tissue triacylglycerol catabolism
    • 1:CAS:528:DC%2BD28XhtlCrt7zE 17074755
    • Schweiger M, Schreiber R, Haemmerle G et al (2006) Adipose triglyceride lipase and hormone-sensitive lipase are the major enzymes in adipose tissue triacylglycerol catabolism. J Biol Chem 281:40236-40241
    • (2006) J Biol Chem , vol.281 , pp. 40236-40241
    • Schweiger, M.1    Schreiber, R.2    Haemmerle, G.3
  • 60
    • 0031019790 scopus 로고    scopus 로고
    • Purification and characterization of a porcine liver microsomal triacylglycerol hydrolase
    • 1:CAS:528:DyaK2sXps1yhsQ%3D%3D 9048571
    • Lehner R, Verger R (1997) Purification and characterization of a porcine liver microsomal triacylglycerol hydrolase. Biochemistry 36:1861-1868
    • (1997) Biochemistry , vol.36 , pp. 1861-1868
    • Lehner, R.1    Verger, R.2
  • 61
    • 0026040248 scopus 로고
    • The nucleotide and deduced amino acid sequences of porcine liver proline- beta-naphthylamidase. Evidence for the identity with carboxylesterase
    • 1:CAS:528:DyaK3sXjsFShtQ%3D%3D 1959668
    • Matsushima M, Inoue H, Ichinose M et al (1991) The nucleotide and deduced amino acid sequences of porcine liver proline- beta-naphthylamidase. Evidence for the identity with carboxylesterase. FEBS Lett 293:37-41
    • (1991) FEBS Lett , vol.293 , pp. 37-41
    • Matsushima, M.1    Inoue, H.2    Ichinose, M.3
  • 62
    • 0026575834 scopus 로고
    • Synthesis and secretion of wild-type and mutant human plasma cholesteryl ester transfer protein in baculovirus-transfected insect cells: The carboxyl-terminal region is required for both lipoprotein binding and catalysis of transfer
    • 525639 1:CAS:528:DyaK38XlsVGmt7g%3D 1570336
    • Au-Young J, Fielding CJ (1992) Synthesis and secretion of wild-type and mutant human plasma cholesteryl ester transfer protein in baculovirus-transfected insect cells: the carboxyl-terminal region is required for both lipoprotein binding and catalysis of transfer. Proc Natl Acad Sci USA 89:4094-4098
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 4094-4098
    • Au-Young, J.1    Fielding, C.J.2
  • 63
    • 0023251539 scopus 로고
    • Cloning and sequencing of human cholesteryl ester transfer protein cDNA
    • 1:CAS:528:DyaL2sXmtFaksbc%3D 3600759
    • Drayna D, Jarnagin AS, McLean J et al (1987) Cloning and sequencing of human cholesteryl ester transfer protein cDNA. Nature 327:632-634
    • (1987) Nature , vol.327 , pp. 632-634
    • Drayna, D.1    Jarnagin, A.S.2    McLean, J.3
  • 64
    • 0025757377 scopus 로고
    • The COOH terminus of several liver carboxylesterases targets these enzymes to the lumen of the endoplasmic reticulum
    • 1:CAS:528:DyaK3MXlslyitro%3D 1939102
    • Robbi M, Beaufay H (1991) The COOH terminus of several liver carboxylesterases targets these enzymes to the lumen of the endoplasmic reticulum. J Biol Chem 266:20498-20503
    • (1991) J Biol Chem , vol.266 , pp. 20498-20503
    • Robbi, M.1    Beaufay, H.2
  • 65
    • 0031800635 scopus 로고    scopus 로고
    • The mammalian carboxylesterases: From molecules to functions
    • 1:CAS:528:DyaK1cXivF2itLc%3D 9597156
    • Satoh T, Hosokawa M (1998) The mammalian carboxylesterases: from molecules to functions. Annu Rev Pharmacol Toxicol 38:257-288
    • (1998) Annu Rev Pharmacol Toxicol , vol.38 , pp. 257-288
    • Satoh, T.1    Hosokawa, M.2
  • 66
    • 0035967790 scopus 로고    scopus 로고
    • The cloning and expression of a murine triacylglycerol hydrolase cDNA and the structure of its corresponding gene
    • 1:CAS:528:DC%2BD3MXlt1Sksbg%3D 11470237
    • Dolinsky VW, Sipione S, Lehner R, Vance DE (2001) The cloning and expression of a murine triacylglycerol hydrolase cDNA and the structure of its corresponding gene. Biochim Biophys Acta 1532:162-172
    • (2001) Biochim Biophys Acta , vol.1532 , pp. 162-172
    • Dolinsky, V.W.1    Sipione, S.2    Lehner, R.3    Vance, D.E.4
  • 67
    • 0037188395 scopus 로고    scopus 로고
    • Structure-function analysis of human triacylglycerol hydrolase by site-directed mutagenesis: Identification of the catalytic triad and a glycosylation site
    • 1:CAS:528:DC%2BD38XjtFGmsLc%3D 12022871
    • Alam M, Vance DE, Lehner R (2002) Structure-function analysis of human triacylglycerol hydrolase by site-directed mutagenesis: identification of the catalytic triad and a glycosylation site. Biochemistry 41:6679-6687
    • (2002) Biochemistry , vol.41 , pp. 6679-6687
    • Alam, M.1    Vance, D.E.2    Lehner, R.3
  • 68
    • 3242656203 scopus 로고    scopus 로고
    • Triacylglycerol hydrolase: Role in intracellular lipid metabolism
    • 1:CAS:528:DC%2BD2cXntlCktbk%3D 15224187
    • Dolinsky VW, Gilham D, Alam M et al (2004) Triacylglycerol hydrolase: role in intracellular lipid metabolism. Cell Mol Life Sci 61:1633-1651
    • (2004) Cell Mol Life Sci , vol.61 , pp. 1633-1651
    • Dolinsky, V.W.1    Gilham, D.2    Alam, M.3
  • 69
    • 1642545652 scopus 로고    scopus 로고
    • Regulation of the enzymes of hepatic microsomal triacylglycerol lipolysis and re-esterification by the glucocorticoid dexamethasone
    • 1224021 1:CAS:528:DC%2BD2cXisVyktbg%3D 14662008
    • Dolinsky VW, Douglas DN, Lehner R, Vance DE (2004) Regulation of the enzymes of hepatic microsomal triacylglycerol lipolysis and re-esterification by the glucocorticoid dexamethasone. Biochem J 378:967-974
    • (2004) Biochem J , vol.378 , pp. 967-974
    • Dolinsky, V.W.1    Douglas, D.N.2    Lehner, R.3    Vance, D.E.4
  • 70
    • 77953523654 scopus 로고    scopus 로고
    • Altered lipid droplet dynamics in hepatocytes lacking triacylglycerol hydrolase expression
    • 2883943 1:CAS:528:DC%2BC3cXpsFCqtbo%3D 20410140
    • Wang H, Wei E, Quiroga AD et al (2010) Altered lipid droplet dynamics in hepatocytes lacking triacylglycerol hydrolase expression. Mol Biol Cell 21:1991-2000
    • (2010) Mol Biol Cell , vol.21 , pp. 1991-2000
    • Wang, H.1    Wei, E.2    Quiroga, A.D.3
  • 71
    • 77249149984 scopus 로고    scopus 로고
    • Loss of TGH/Ces3 in mice decreases blood lipids, improves glucose tolerance, and increases energy expenditure
    • 1:CAS:528:DC%2BC3cXlsVajurY%3D 20197051
    • Wei E, Ben Ali Y, Lyon J et al (2010) Loss of TGH/Ces3 in mice decreases blood lipids, improves glucose tolerance, and increases energy expenditure. Cell Metab 11:183-193
    • (2010) Cell Metab , vol.11 , pp. 183-193
    • Wei, E.1    Ben, A.Y.2    Lyon, J.3
  • 72
    • 0037192385 scopus 로고    scopus 로고
    • A novel phospholipase A1 with sequence homology to a mammalian Sec23p-interacting protein, p125
    • 1:CAS:528:DC%2BD38Xis1KgsLw%3D 11788596
    • Nakajima KI, Sonoda H, Mizoguchi T et al (2002) A novel phospholipase A1 with sequence homology to a mammalian Sec23p-interacting protein, p125. J Biol Chem 277:11329-11335
    • (2002) J Biol Chem , vol.277 , pp. 11329-11335
    • Nakajima, K.I.1    Sonoda, H.2    Mizoguchi, T.3
  • 73
    • 84907892277 scopus 로고    scopus 로고
    • The hereditary spastic paraplegia-related enzyme DDHD2 is a principal brain triglyceride lipase
    • 4205627 1:CAS:528:DC%2BC2cXhs1Cht77E 25267624
    • Inloes JM, Hsu K-L, Dix MM et al (2014) The hereditary spastic paraplegia-related enzyme DDHD2 is a principal brain triglyceride lipase. Proc Natl Acad Sci 111:14924-14929
    • (2014) Proc Natl Acad Sci , vol.111 , pp. 14924-14929
    • Inloes, J.M.1    Hsu, K.-L.2    Dix, M.M.3
  • 74
    • 33747072385 scopus 로고    scopus 로고
    • Identification of a novel member of the carboxylesterase family that hydrolyzes triacylglycerol: A potential role in adipocyte lipolysis
    • 1:CAS:528:DC%2BD28XmvVChtLY%3D 16804080
    • Okazaki H, Igarashi M, Nishi M et al (2006) Identification of a novel member of the carboxylesterase family that hydrolyzes triacylglycerol: a potential role in adipocyte lipolysis. Diabetes 55:2091-2097
    • (2006) Diabetes , vol.55 , pp. 2091-2097
    • Okazaki, H.1    Igarashi, M.2    Nishi, M.3
  • 75
    • 0028071435 scopus 로고
    • Isolation of a new gene GS2 (DXS1283E) from a CpG island between STS and KAL1 on Xp22.3
    • 1:CAS:528:DyaK2MXksVygsA%3D%3D 7806223
    • Lee WC, Salido E, Yen PH (1994) Isolation of a new gene GS2 (DXS1283E) from a CpG island between STS and KAL1 on Xp22.3. Genomics 22:372-376
    • (1994) Genomics , vol.22 , pp. 372-376
    • Lee, W.C.1    Salido, E.2    Yen, P.H.3
  • 76
    • 20544442848 scopus 로고    scopus 로고
    • Identification of a novel keratinocyte retinyl ester hydrolase as a transacylase and lipase
    • 1:CAS:528:DC%2BD2MXlvF2ktL4%3D 15955102
    • Gao J, Simon M (2005) Identification of a novel keratinocyte retinyl ester hydrolase as a transacylase and lipase. J Invest Dermatol 124:1259-1266
    • (2005) J Invest Dermatol , vol.124 , pp. 1259-1266
    • Gao, J.1    Simon, M.2
  • 77
    • 0035823621 scopus 로고    scopus 로고
    • Adiponutrin, a transmembrane protein corresponding to a novel dietary- and obesity-linked mRNA specifically expressed in the adipose lineage
    • 1:CAS:528:DC%2BD3MXmslymurk%3D 11431482
    • Baulande S, Lasnier F, Lucas M, Pairault J (2001) Adiponutrin, a transmembrane protein corresponding to a novel dietary- and obesity-linked mRNA specifically expressed in the adipose lineage. J Biol Chem 276:33336-33344
    • (2001) J Biol Chem , vol.276 , pp. 33336-33344
    • Baulande, S.1    Lasnier, F.2    Lucas, M.3    Pairault, J.4
  • 78
    • 77952409634 scopus 로고    scopus 로고
    • A feed-forward loop amplifies nutritional regulation of PNPLA3
    • 2867902 1:CAS:528:DC%2BC3cXlsFynt7w%3D 20385813
    • Huang Y, He S, Li JZ et al (2010) A feed-forward loop amplifies nutritional regulation of PNPLA3. Proc Natl Acad Sci USA 107:7892-7897
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 7892-7897
    • Huang, Y.1    He, S.2    Li, J.Z.3
  • 79
    • 77949895032 scopus 로고    scopus 로고
    • A sequence variation (I148M) in PNPLA3 associated with nonalcoholic fatty liver disease disrupts triglyceride hydrolysis
    • 2825465 1:CAS:528:DC%2BC3cXit1aitrg%3D 20034933
    • He S, McPhaul C, Li JZ et al (2010) A sequence variation (I148M) in PNPLA3 associated with nonalcoholic fatty liver disease disrupts triglyceride hydrolysis. J Biol Chem 285:6706-6715
    • (2010) J Biol Chem , vol.285 , pp. 6706-6715
    • He, S.1    McPhaul, C.2    Li, J.Z.3
  • 80
    • 33644764922 scopus 로고    scopus 로고
    • Adipose triglyceride lipase: Function, regulation by insulin, and comparison with adiponutrin
    • 2819178 1:CAS:528:DC%2BD28XlvVSlug%3D%3D 16380488
    • Kershaw EE, Hamm JK, Verhagen LA et al (2006) Adipose triglyceride lipase: function, regulation by insulin, and comparison with adiponutrin. Diabetes 55:148-157
    • (2006) Diabetes , vol.55 , pp. 148-157
    • Kershaw, E.E.1    Hamm, J.K.2    Verhagen, L.A.3
  • 81
    • 84903996547 scopus 로고    scopus 로고
    • PNPLA3 has retinyl-palmitate lipase activity in human hepatic stellate cells
    • 4082369 1:CAS:528:DC%2BC2cXhtFeitbjM 24670599
    • Pirazzi C, Valenti L, Motta BM et al (2014) PNPLA3 has retinyl-palmitate lipase activity in human hepatic stellate cells. Hum Mol Genet 23:4077-4085
    • (2014) Hum Mol Genet , vol.23 , pp. 4077-4085
    • Pirazzi, C.1    Valenti, L.2    Motta, B.M.3
  • 82
    • 80054806707 scopus 로고    scopus 로고
    • Expression and characterization of a PNPLA3 protein isoform (I148M) associated with nonalcoholic fatty liver disease
    • 3199456 1:CAS:528:DC%2BC3MXhtlGns7fM 21878620
    • Huang Y, Cohen JC, Hobbs HH (2011) Expression and characterization of a PNPLA3 protein isoform (I148M) associated with nonalcoholic fatty liver disease. J Biol Chem 286:37085-37093
    • (2011) J Biol Chem , vol.286 , pp. 37085-37093
    • Huang, Y.1    Cohen, J.C.2    Hobbs, H.H.3
  • 83
    • 78751489992 scopus 로고    scopus 로고
    • Pnpla3/Adiponutrin deficiency in mice does not contribute to fatty liver disease or metabolic syndrome
    • 3023552 1:CAS:528:DC%2BC3MXht1alurY%3D 21068004
    • Basantani MK, Sitnick MT, Cai L et al (2011) Pnpla3/Adiponutrin deficiency in mice does not contribute to fatty liver disease or metabolic syndrome. J Lipid Res 52:318-329
    • (2011) J Lipid Res , vol.52 , pp. 318-329
    • Basantani, M.K.1    Sitnick, M.T.2    Cai, L.3
  • 84
    • 84868609657 scopus 로고    scopus 로고
    • Chronic overexpression of PNPLA3I148M in mouse liver causes hepatic steatosis
    • 3484461 1:CAS:528:DC%2BC38Xhs1CisL%2FK 23023705
    • Li JZ, Huang Y, Karaman R et al (2012) Chronic overexpression of PNPLA3I148M in mouse liver causes hepatic steatosis. J Clin Invest 122:4130-4144
    • (2012) J Clin Invest , vol.122 , pp. 4130-4144
    • Li, J.Z.1    Huang, Y.2    Karaman, R.3
  • 85
    • 79960729651 scopus 로고    scopus 로고
    • Mouse patatin-like phospholipase domain-containing 3 influences systemic lipid and glucose homeostasis
    • 1:CAS:528:DC%2BC3MXpt1yju7k%3D 21547936
    • Qiao A, Liang J, Ke Y et al (2011) Mouse patatin-like phospholipase domain-containing 3 influences systemic lipid and glucose homeostasis. Hepatology 54:509-521
    • (2011) Hepatology , vol.54 , pp. 509-521
    • Qiao, A.1    Liang, J.2    Ke, Y.3
  • 86
    • 84920955177 scopus 로고    scopus 로고
    • Pnpla3I148M knockin mice accumulate PNPLA3 on lipid droplets and develop hepatic steatosis
    • 4262735 24917523
    • Smagris E, BasuRay S, Li J et al (2014) Pnpla3I148M knockin mice accumulate PNPLA3 on lipid droplets and develop hepatic steatosis. Hepatology 61:108-118
    • (2014) Hepatology , vol.61 , pp. 108-118
    • Smagris, E.1    BasuRay, S.2    Li, J.3
  • 87
    • 84860465005 scopus 로고    scopus 로고
    • Adiponutrin functions as a nutritionally regulated lysophosphatidic acid acyltransferase
    • 3361708 1:CAS:528:DC%2BC38XmsVequrc%3D 22560221
    • Kumari M, Schoiswohl G, Chitraju C et al (2012) Adiponutrin functions as a nutritionally regulated lysophosphatidic acid acyltransferase. Cell Metab 15:691-702
    • (2012) Cell Metab , vol.15 , pp. 691-702
    • Kumari, M.1    Schoiswohl, G.2    Chitraju, C.3
  • 88
    • 79960081490 scopus 로고    scopus 로고
    • Targeting phosphatidylcholine-specific phospholipase C for atherogenesis therapy
    • 1:CAS:528:DC%2BC3MXoslWhtro%3D 21742273
    • Li H, Zhang L, Yin D et al (2010) Targeting phosphatidylcholine-specific phospholipase C for atherogenesis therapy. Trends Cardiovasc Med 20:172-176
    • (2010) Trends Cardiovasc Med , vol.20 , pp. 172-176
    • Li, H.1    Zhang, L.2    Yin, D.3
  • 89
    • 4444370177 scopus 로고    scopus 로고
    • Phosphatidylcholine-specific phospholipase C in mitogen-stimulated fibroblasts
    • 1:CAS:528:DC%2BD2cXntlOhsL8%3D 15350536
    • Ramoni C, Spadaro F, Barletta B et al (2004) Phosphatidylcholine-specific phospholipase C in mitogen-stimulated fibroblasts. Exp Cell Res 299:370-382
    • (2004) Exp Cell Res , vol.299 , pp. 370-382
    • Ramoni, C.1    Spadaro, F.2    Barletta, B.3
  • 90
    • 0034927336 scopus 로고    scopus 로고
    • Regulation of phosphoinositide-specific phospholipase C
    • 1:CAS:528:DC%2BD3MXlsVeht7s%3D 11395409
    • Rhee SG (2001) Regulation of phosphoinositide-specific phospholipase C. Annu Rev Biochem 70:281-312
    • (2001) Annu Rev Biochem , vol.70 , pp. 281-312
    • Rhee, S.G.1
  • 91
    • 30944456676 scopus 로고    scopus 로고
    • The latest phospholipase C, PLCeta, is implicated in neuronal function
    • 1:CAS:528:DC%2BD28XosFKkuw%3D%3D 16310357
    • Cockcroft S (2006) The latest phospholipase C, PLCeta, is implicated in neuronal function. Trends Biochem Sci 31:4-7
    • (2006) Trends Biochem Sci , vol.31 , pp. 4-7
    • Cockcroft, S.1
  • 92
    • 33751315308 scopus 로고    scopus 로고
    • Phospholipase C epsilon: Linking second messengers and small GTPases
    • 1:CAS:528:DC%2BD28Xht1OhtLjF 17085049
    • Bunney TD, Katan M (2006) Phospholipase C epsilon: linking second messengers and small GTPases. Trends Cell Biol 16:640-648
    • (2006) Trends Cell Biol , vol.16 , pp. 640-648
    • Bunney, T.D.1    Katan, M.2
  • 93
    • 46249091922 scopus 로고    scopus 로고
    • Multiple roles of phosphoinositide-specific phospholipase C isozymes
    • 1:CAS:528:DC%2BD1cXosVKkurc%3D 18593525
    • Suh PG, Park JI, Manzoli L et al (2008) Multiple roles of phosphoinositide-specific phospholipase C isozymes. BMB Rep 41:415-434
    • (2008) BMB Rep , vol.41 , pp. 415-434
    • Suh, P.G.1    Park, J.I.2    Manzoli, L.3
  • 94
    • 77956392921 scopus 로고    scopus 로고
    • Phospholipase C is a key enzyme regulating intracellular calcium and modulating the phosphoinositide balance
    • 1:CAS:528:DC%2BC3cXhtFWqsLjK 20553968
    • Fukami K, Inanobe S, Kanemaru K, Nakamura Y (2010) Phospholipase C is a key enzyme regulating intracellular calcium and modulating the phosphoinositide balance. Prog Lipid Res 49:429-437
    • (2010) Prog Lipid Res , vol.49 , pp. 429-437
    • Fukami, K.1    Inanobe, S.2    Kanemaru, K.3    Nakamura, Y.4
  • 95
    • 0015987808 scopus 로고
    • The enzymatic formation of sphingomyelin from ceramide and lecithin in mouse liver
    • 1:CAS:528:DyaE2cXhsVWqtbk%3D 4817756
    • Ullman MD, Radin NS (1974) The enzymatic formation of sphingomyelin from ceramide and lecithin in mouse liver. J Biol Chem 249:1506-1512
    • (1974) J Biol Chem , vol.249 , pp. 1506-1512
    • Ullman, M.D.1    Radin, N.S.2
  • 96
    • 0020287371 scopus 로고
    • Cellular and enzymic synthesis of sphingomyelin
    • 1:CAS:528:DyaL38XitFCru7s%3D 7093220
    • Voelker DR, Kennedy EP (1982) Cellular and enzymic synthesis of sphingomyelin. Biochemistry 21:2753-2759
    • (1982) Biochemistry , vol.21 , pp. 2753-2759
    • Voelker, D.R.1    Kennedy, E.P.2
  • 97
    • 0842263750 scopus 로고    scopus 로고
    • Identification of a family of animal sphingomyelin synthases
    • 1271672 1:CAS:528:DC%2BD2cXhtVequr4%3D 14685263
    • Huitema K, van den Dikkenberg J, Brouwers JFHM, Holthuis JCM (2004) Identification of a family of animal sphingomyelin synthases. EMBO J 23:33-44
    • (2004) EMBO J , vol.23 , pp. 33-44
    • Huitema, K.1    Van Den Dikkenberg, J.2    Brouwers, J.3    Holthuis, J.C.M.4
  • 98
    • 33749576963 scopus 로고    scopus 로고
    • The multigenic sphingomyelin synthase family
    • 1:CAS:528:DC%2BD28XhtVahsLnF 16905542
    • Tafesse FG, Ternes P, Holthuis JCM (2006) The multigenic sphingomyelin synthase family. J Biol Chem 281:29421-29425
    • (2006) J Biol Chem , vol.281 , pp. 29421-29425
    • Tafesse, F.G.1    Ternes, P.2    Holthuis, J.C.M.3
  • 99
    • 33947371349 scopus 로고    scopus 로고
    • Cellular localization of sphingomyelin synthase 2 in the seminiferous epithelium of adult rat testes
    • 1:CAS:528:DC%2BD2sXktlKqtL0%3D 17210739
    • Lee NPY, Mruk DD, Xia W, Cheng CY (2007) Cellular localization of sphingomyelin synthase 2 in the seminiferous epithelium of adult rat testes. J Endocrinol 192:17-32
    • (2007) J Endocrinol , vol.192 , pp. 17-32
    • Lee, N.P.Y.1    Mruk, D.D.2    Xia, W.3    Cheng, C.Y.4
  • 100
    • 0037059451 scopus 로고    scopus 로고
    • Role of diacylglycerol in PKD recruitment to the TGN and protein transport to the plasma membrane
    • 1:CAS:528:DC%2BD38Xkt1Kmsw%3D%3D 11729268
    • Baron CL, Malhotra V (2002) Role of diacylglycerol in PKD recruitment to the TGN and protein transport to the plasma membrane. Science 295:325-328
    • (2002) Science , vol.295 , pp. 325-328
    • Baron, C.L.1    Malhotra, V.2
  • 101
    • 1642602671 scopus 로고    scopus 로고
    • Protein kinase D regulates basolateral membrane protein exit from trans-Golgi network
    • 3372901 1:CAS:528:DC%2BD2cXosFShsw%3D%3D 14743217
    • Yeaman C, Ayala MI, Wright JR et al (2004) Protein kinase D regulates basolateral membrane protein exit from trans-Golgi network. Nat Cell Biol 6:106-112
    • (2004) Nat Cell Biol , vol.6 , pp. 106-112
    • Yeaman, C.1    Ayala, M.I.2    Wright, J.R.3
  • 102
    • 34547110137 scopus 로고    scopus 로고
    • Both sphingomyelin synthases SMS1 and SMS2 are required for sphingomyelin homeostasis and growth in human HeLa cells
    • 1:CAS:528:DC%2BD2sXmt1ektLc%3D 17449912
    • Tafesse FG, Huitema K, Hermansson M et al (2007) Both sphingomyelin synthases SMS1 and SMS2 are required for sphingomyelin homeostasis and growth in human HeLa cells. J Biol Chem 282:17537-17547
    • (2007) J Biol Chem , vol.282 , pp. 17537-17547
    • Tafesse, F.G.1    Huitema, K.2    Hermansson, M.3
  • 103
    • 67449147119 scopus 로고    scopus 로고
    • Sphingomyelin synthase-related protein SMSr controls ceramide homeostasis in the ER
    • 2711605 1:CAS:528:DC%2BD1MXnsF2rsro%3D 19506037
    • Vacaru AM, Tafesse FG, Ternes P et al (2009) Sphingomyelin synthase-related protein SMSr controls ceramide homeostasis in the ER. J Cell Biol 185:1013-1027
    • (2009) J Cell Biol , vol.185 , pp. 1013-1027
    • Vacaru, A.M.1    Tafesse, F.G.2    Ternes, P.3
  • 104
    • 70350383478 scopus 로고    scopus 로고
    • Sphingomyelin synthase SMS2 displays dual activity as ceramide phosphoethanolamine synthase
    • 2759833 1:CAS:528:DC%2BD1MXhtlShur%2FE 19454763
    • Ternes P, Brouwers JFHM, van den Dikkenberg J, Holthuis JCM (2009) Sphingomyelin synthase SMS2 displays dual activity as ceramide phosphoethanolamine synthase. J Lipid Res 50:2270-2277
    • (2009) J Lipid Res , vol.50 , pp. 2270-2277
    • Ternes, P.1    Brouwers, J.2    Van Den Dikkenberg, J.3    Holthuis, J.C.M.4
  • 105
    • 0018846846 scopus 로고
    • Enzymes of glycerolipid synthesis in eukaryotes
    • 1:CAS:528:DyaL3cXks1ChtL8%3D 6250446
    • Bell RM, Coleman RA (1980) Enzymes of glycerolipid synthesis in eukaryotes. Annu Rev Biochem 49:459-487
    • (1980) Annu Rev Biochem , vol.49 , pp. 459-487
    • Bell, R.M.1    Coleman, R.A.2
  • 106
    • 0345171460 scopus 로고    scopus 로고
    • Enzymes of triacylglycerol synthesis and their regulation
    • 1:CAS:528:DC%2BD3sXptlyhtbs%3D 14654091
    • Coleman RA, Lee DP (2004) Enzymes of triacylglycerol synthesis and their regulation. Prog Lipid Res 43:134-176
    • (2004) Prog Lipid Res , vol.43 , pp. 134-176
    • Coleman, R.A.1    Lee, D.P.2
  • 107
    • 80054057662 scopus 로고    scopus 로고
    • Mammalian triacylglycerol metabolism: Synthesis, lipolysis, and signaling
    • 3181269 1:CAS:528:DC%2BC3MXmvFChsbY%3D 21627334
    • Coleman RA, Mashek DG (2011) Mammalian triacylglycerol metabolism: synthesis, lipolysis, and signaling. Chem Rev 111:6359-6386
    • (2011) Chem Rev , vol.111 , pp. 6359-6386
    • Coleman, R.A.1    Mashek, D.G.2
  • 108
    • 0001031875 scopus 로고
    • Enzymatic esterification of alpha-glycerophosphate by long chain fatty acids
    • 1:CAS:528:DyaG3sXntlWhsA%3D%3D 13084606
    • Kornberg A, Pricer WE (1953) Enzymatic esterification of alpha-glycerophosphate by long chain fatty acids. J Biol Chem 204:345
    • (1953) J Biol Chem , vol.204 , pp. 345
    • Kornberg, A.1    Pricer, W.E.2
  • 109
    • 0001644335 scopus 로고
    • Synthesis of phosphatidates in isolated mitochondria
    • Burblitz C, Kennedy EP (1954) Synthesis of phosphatidates in isolated mitochondria. J Biol Chem 211:951
    • (1954) J Biol Chem , vol.211 , pp. 951
    • Burblitz, C.1    Kennedy, E.P.2
  • 110
    • 0014935325 scopus 로고
    • The utilization of the alpha-glycerophosphate and monoglyceride pathways for phosphatidyl choline biosynthesis in the intestine
    • 1:CAS:528:DyaE3MXkvFyhtw%3D%3D 5473485
    • Johnston M, Schultz D, Schiller M (1970) The utilization of the alpha-glycerophosphate and monoglyceride pathways for phosphatidyl choline biosynthesis in the intestine. Biochim Biophys Acta 218:124-133
    • (1970) Biochim Biophys Acta , vol.218 , pp. 124-133
    • Johnston, M.1    Schultz, D.2    Schiller, M.3
  • 111
    • 0035289931 scopus 로고    scopus 로고
    • Intestinal lipid absorption and transport
    • 1:CAS:528:DC%2BD3MXjtFakur4%3D 11229876
    • Phan CT, Tso P (2001) Intestinal lipid absorption and transport. Front Biosci 6:D299-D319
    • (2001) Front Biosci , vol.6 , pp. D299-D319
    • Phan, C.T.1    Tso, P.2
  • 112
    • 0015897117 scopus 로고
    • Regulation of triglyceride biosynthesis in adipose and intestinal tissue
    • 1:CAS:528:DyaE3sXks1ertrc%3D 4715324
    • Polheim D, David JS, Schultz FM et al (1973) Regulation of triglyceride biosynthesis in adipose and intestinal tissue. J Lipid Res 14:415-421
    • (1973) J Lipid Res , vol.14 , pp. 415-421
    • Polheim, D.1    David, J.S.2    Schultz, F.M.3
  • 113
    • 36949090283 scopus 로고
    • New synthesis of lecithin in an isolated enzyme system
    • 1:STN:280:DyaG2s%2FhsFGlug%3D%3D 13369471
    • Kennedy EP, Smith SW, Weiss SB (1956) New synthesis of lecithin in an isolated enzyme system. Nature 178:594-595
    • (1956) Nature , vol.178 , pp. 594-595
    • Kennedy, E.P.1    Smith, S.W.2    Weiss, S.B.3
  • 114
    • 9444267788 scopus 로고
    • Biosynthesis of phospholipids
    • 1:CAS:528:DyaG1cXhtFGitQ%3D%3D 13480372
    • Kennedy EP (1957) Biosynthesis of phospholipids. Fed Proc 16:847-853
    • (1957) Fed Proc , vol.16 , pp. 847-853
    • Kennedy, E.P.1
  • 115
    • 77953591461 scopus 로고    scopus 로고
    • The Kennedy pathway-De novo synthesis of phosphatidylethanolamine and phosphatidylcholine
    • 1:CAS:528:DC%2BC3cXmsVGhtLk%3D 20503434
    • Gibellini F, Smith TK (2010) The Kennedy pathway-De novo synthesis of phosphatidylethanolamine and phosphatidylcholine. IUBMB Life 62:414-428
    • (2010) IUBMB Life , vol.62 , pp. 414-428
    • Gibellini, F.1    Smith, T.K.2
  • 116
    • 0035163850 scopus 로고    scopus 로고
    • Lipodystrophy in the fld mouse results from mutation of a new gene encoding a nuclear protein, lipin
    • 1:CAS:528:DC%2BD3MXis1yrug%3D%3D 11138012
    • Peterfy M, Phan J, Xu P, Reue K (2001) Lipodystrophy in the fld mouse results from mutation of a new gene encoding a nuclear protein, lipin. Nat Genet 27:121-124
    • (2001) Nat Genet , vol.27 , pp. 121-124
    • Peterfy, M.1    Phan, J.2    Xu, P.3    Reue, K.4
  • 117
    • 33947542353 scopus 로고    scopus 로고
    • Three mammalian lipins act as phosphatidate phosphatases with distinct tissue expression patterns
    • 1:CAS:528:DC%2BD2sXht1Krur0%3D 17158099
    • Donkor J, Sariahmetoglu M, Dewald J et al (2007) Three mammalian lipins act as phosphatidate phosphatases with distinct tissue expression patterns. J Biol Chem 282:3450-3457
    • (2007) J Biol Chem , vol.282 , pp. 3450-3457
    • Donkor, J.1    Sariahmetoglu, M.2    Dewald, J.3
  • 118
    • 33846975789 scopus 로고    scopus 로고
    • Insulin controls subcellular localization and multisite phosphorylation of the phosphatidic acid phosphatase, lipin 1
    • 1:CAS:528:DC%2BD2sXks1yk 17105729
    • Harris TE, Huffman TA, Chi A et al (2007) Insulin controls subcellular localization and multisite phosphorylation of the phosphatidic acid phosphatase, lipin 1. J Biol Chem 282:277-286
    • (2007) J Biol Chem , vol.282 , pp. 277-286
    • Harris, T.E.1    Huffman, T.A.2    Chi, A.3
  • 119
    • 0021354540 scopus 로고
    • Oleic acid promotes the activation and translocation of phosphatidate phosphohydrolase from the cytosol to particulate fractions of isolated rat hepatocytes
    • 1153561 1:CAS:528:DyaL2cXktVCms7w%3D 6331400
    • Cascales C, Mangiapane EH, Brindley DN (1984) Oleic acid promotes the activation and translocation of phosphatidate phosphohydrolase from the cytosol to particulate fractions of isolated rat hepatocytes. Biochem J 219:911-916
    • (1984) Biochem J , vol.219 , pp. 911-916
    • Cascales, C.1    Mangiapane, E.H.2    Brindley, D.N.3
  • 120
    • 15944375261 scopus 로고    scopus 로고
    • Lipin, a lipodystrophy and obesity gene
    • 1:CAS:528:DC%2BD2MXhtlaqs7s%3D 16054046
    • Phan J, Reue K (2005) Lipin, a lipodystrophy and obesity gene. Cell Metab 1:73-83
    • (2005) Cell Metab , vol.1 , pp. 73-83
    • Phan, J.1    Reue, K.2
  • 121
    • 0037790713 scopus 로고    scopus 로고
    • MGAT2, a monoacylglycerol acyltransferase expressed in the small intestine
    • 1:CAS:528:DC%2BD3sXjs1Kht7w%3D 12621063
    • Yen CL Jr, Farese RV (2003) MGAT2, a monoacylglycerol acyltransferase expressed in the small intestine. J Biol Chem 278:18532-18537
    • (2003) J Biol Chem , vol.278 , pp. 18532-18537
    • Yen, C.L.1    Farese, R.V.2
  • 122
    • 0037172964 scopus 로고    scopus 로고
    • Identification of a gene encoding MGAT1, a monoacylglycerol acyltransferase
    • 124292 1:CAS:528:DC%2BD38XltF2hsr4%3D 12077311
    • Yen CL, Stone SJ, Cases S et al (2002) Identification of a gene encoding MGAT1, a monoacylglycerol acyltransferase. Proc Natl Acad Sci USA 99:8512-8517
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 8512-8517
    • Yen, C.L.1    Stone, S.J.2    Cases, S.3
  • 123
    • 0038075340 scopus 로고    scopus 로고
    • Identification of acyl coenzyme A:monoacylglycerol acyltransferase 3, an intestinal specific enzyme implicated in dietary fat absorption
    • 1:CAS:528:DC%2BD3sXjtVSisb8%3D 12618427
    • Cheng D, Nelson TC, Chen J et al (2003) Identification of acyl coenzyme A:monoacylglycerol acyltransferase 3, an intestinal specific enzyme implicated in dietary fat absorption. J Biol Chem 278:13611-13614
    • (2003) J Biol Chem , vol.278 , pp. 13611-13614
    • Cheng, D.1    Nelson, T.C.2    Chen, J.3
  • 124
    • 0035914356 scopus 로고    scopus 로고
    • Cloning of DGAT2, a second mammalian diacylglycerol acyltransferase, and related family members
    • 1:CAS:528:DC%2BD3MXnvVenur8%3D 11481335
    • Cases S, Stone SJ, Zhou P et al (2001) Cloning of DGAT2, a second mammalian diacylglycerol acyltransferase, and related family members. J Biol Chem 276:38870-38876
    • (2001) J Biol Chem , vol.276 , pp. 38870-38876
    • Cases, S.1    Stone, S.J.2    Zhou, P.3
  • 125
    • 0038751862 scopus 로고    scopus 로고
    • Cloning and functional characterization of a mouse intestinal acyl-CoA:monoacylglycerol acyltransferase, MGAT2
    • 1:CAS:528:DC%2BD3sXjtVSitLo%3D 12576479
    • Cao J, Lockwood J, Burn P, Shi Y (2003) Cloning and functional characterization of a mouse intestinal acyl-CoA:monoacylglycerol acyltransferase, MGAT2. J Biol Chem 278:13860-13866
    • (2003) J Biol Chem , vol.278 , pp. 13860-13866
    • Cao, J.1    Lockwood, J.2    Burn, P.3    Shi, Y.4
  • 126
    • 0037477454 scopus 로고    scopus 로고
    • Properties of the mouse intestinal acyl-CoA:monoacylglycerol acyltransferase, MGAT2
    • 1:CAS:528:DC%2BD3sXlt1Cmu7c%3D 12730219
    • Cao J, Burn P, Shi Y (2003) Properties of the mouse intestinal acyl-CoA:monoacylglycerol acyltransferase, MGAT2. J Biol Chem 278:25657-25663
    • (2003) J Biol Chem , vol.278 , pp. 25657-25663
    • Cao, J.1    Burn, P.2    Shi, Y.3
  • 127
    • 33947104623 scopus 로고    scopus 로고
    • Catalytic properties of MGAT3, a putative triacylgycerol synthase
    • 1:CAS:528:DC%2BD2sXis1yqt7g%3D 17170429
    • Cao J, Cheng L, Shi Y (2007) Catalytic properties of MGAT3, a putative triacylgycerol synthase. J Lipid Res 48:583-591
    • (2007) J Lipid Res , vol.48 , pp. 583-591
    • Cao, J.1    Cheng, L.2    Shi, Y.3
  • 128
    • 0014004998 scopus 로고
    • The effect of chain length on the activation and subsequent incorporation of fatty acids into glycerides by the small intestinal mucosa
    • 1:CAS:528:DyaF28Xktlaitr0%3D 5968597
    • Brindley DN, Hubscher G (1966) The effect of chain length on the activation and subsequent incorporation of fatty acids into glycerides by the small intestinal mucosa. Biochim Biophys Acta 125:92-105
    • (1966) Biochim Biophys Acta , vol.125 , pp. 92-105
    • Brindley, D.N.1    Hubscher, G.2
  • 129
    • 0031081552 scopus 로고    scopus 로고
    • In vivo and in vitro studies on the stereoselective hydrolysis of tri- and diglycerides by gastric and pancreatic lipases
    • 1:CAS:528:DyaK2sXhsVKhs7g%3D 9061207
    • Carriere F, Rogalska E, Cudrey C et al (1997) In vivo and in vitro studies on the stereoselective hydrolysis of tri- and diglycerides by gastric and pancreatic lipases. Bioorg Med Chem 5:429-435
    • (1997) Bioorg Med Chem , vol.5 , pp. 429-435
    • Carriere, F.1    Rogalska, E.2    Cudrey, C.3
  • 130
    • 0028806511 scopus 로고
    • Rat GP-3 is a pancreatic lipase with kinetic properties that differ from colipase-dependent pancreatic lipase
    • 1:CAS:528:DyaK2MXpslGit7k%3D 8656075
    • Jennens ML, Lowe ME (1995) Rat GP-3 is a pancreatic lipase with kinetic properties that differ from colipase-dependent pancreatic lipase. J Lipid Res 36:2374-2382
    • (1995) J Lipid Res , vol.36 , pp. 2374-2382
    • Jennens, M.L.1    Lowe, M.E.2
  • 131
    • 0028279834 scopus 로고
    • Evidence for a pancreatic lipase subfamily with new kinetic properties
    • 1:CAS:528:DyaK2cXhvVKjs7o%3D 8130186
    • Thirstrup K, Verger R, Carrière F (1994) Evidence for a pancreatic lipase subfamily with new kinetic properties. Biochemistry 33:2748-2756
    • (1994) Biochemistry , vol.33 , pp. 2748-2756
    • Thirstrup, K.1    Verger, R.2    Carrière, F.3
  • 132
    • 0033610799 scopus 로고    scopus 로고
    • Structure and activity of rat pancreatic lipase-related protein 2
    • 1:CAS:528:DyaK1cXnvVeltb8%3D 9822688
    • Roussel A, Yang Y, Ferrato F et al (1998) Structure and activity of rat pancreatic lipase-related protein 2. J Biol Chem 273:32121-32128
    • (1998) J Biol Chem , vol.273 , pp. 32121-32128
    • Roussel, A.1    Yang, Y.2    Ferrato, F.3
  • 133
    • 0026671201 scopus 로고
    • Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2
    • 1:CAS:528:DyaK3sXkt1emtrc%3D 1379598
    • Giller T, Buchwald P, Blum-Kaelin D et al (1992) Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. J Biol Chem 267:16509-16516
    • (1992) J Biol Chem , vol.267 , pp. 16509-16516
    • Giller, T.1    Buchwald, P.2    Blum-Kaelin, D.3
  • 134
    • 0027475881 scopus 로고
    • Controlling lipase stereoselectivity via the surface pressure
    • 1:CAS:528:DyaK3sXlsV2jtQ%3D%3D 8419355
    • Rogalska E, Ransac S, Verger R (1993) Controlling lipase stereoselectivity via the surface pressure. J Biol Chem 268:792-794
    • (1993) J Biol Chem , vol.268 , pp. 792-794
    • Rogalska, E.1    Ransac, S.2    Verger, R.3
  • 135
    • 0027506517 scopus 로고
    • Stereoselective hydrolysis of triglycerides by animal and microbial lipases
    • 1:CAS:528:DyaK3sXkvV2ksL0%3D 8448074
    • Rogalska E, Cudrey C, Ferrato F, Verger R (1993) Stereoselective hydrolysis of triglycerides by animal and microbial lipases. Chirality 5:24-30
    • (1993) Chirality , vol.5 , pp. 24-30
    • Rogalska, E.1    Cudrey, C.2    Ferrato, F.3    Verger, R.4
  • 136
    • 0015964339 scopus 로고
    • Stereospecificity of lipases. Enzymic hydrolysis of enantiomeric alkyl diacylglycerols by lipoprotein lipase, lingual lipase and pancreatic lipase
    • 1:CAS:528:DyaE2cXksF2qtr8%3D 4854401
    • Paltauf F, Esfandi F, Holasek A (1974) Stereospecificity of lipases. Enzymic hydrolysis of enantiomeric alkyl diacylglycerols by lipoprotein lipase, lingual lipase and pancreatic lipase. FEBS Lett 40:119-123
    • (1974) FEBS Lett , vol.40 , pp. 119-123
    • Paltauf, F.1    Esfandi, F.2    Holasek, A.3
  • 137
    • 0020174483 scopus 로고
    • Stereospecificity of premature human infant lingual lipase
    • 1:CAS:528:DyaL38XlsFylsL0%3D 7132587
    • Jensen RG, DeJong FA, Clark RM et al (1982) Stereospecificity of premature human infant lingual lipase. Lipids 17:570-572
    • (1982) Lipids , vol.17 , pp. 570-572
    • Jensen, R.G.1    DeJong, F.A.2    Clark, R.M.3
  • 138
    • 0020966216 scopus 로고
    • Studies on the substrate specificity of purified human milk bile salt-activated lipase
    • 1:CAS:528:DyaL3sXltlKjsr8%3D 6874684
    • Wang CS, Kuksis A, Manganaro F et al (1983) Studies on the substrate specificity of purified human milk bile salt-activated lipase. J Biol Chem 258:9197-9202
    • (1983) J Biol Chem , vol.258 , pp. 9197-9202
    • Wang, C.S.1    Kuksis, A.2    Manganaro, F.3
  • 139
    • 0015523805 scopus 로고
    • Positional specificity of lipoprotein lipase
    • 1:CAS:528:DyaE3sXhsVCj 5076762
    • Morley N, Kuksis A (1972) Positional specificity of lipoprotein lipase. J Biol Chem 247:6389-6393
    • (1972) J Biol Chem , vol.247 , pp. 6389-6393
    • Morley, N.1    Kuksis, A.2
  • 140
    • 0017053460 scopus 로고
    • Stereospecificity of hepatic lipases
    • 1:CAS:528:DyaE2sXjvFaqtA%3D%3D 12007
    • Akesson B, Gronowitz S, Herslof B (1976) Stereospecificity of hepatic lipases. FEBS Lett 71:241-244
    • (1976) FEBS Lett , vol.71 , pp. 241-244
    • Akesson, B.1    Gronowitz, S.2    Herslof, B.3
  • 141
    • 0029012014 scopus 로고
    • Identification of an endogenous 2-monoglyceride, present in canine gut, that binds to cannabinoid receptors
    • 1:CAS:528:DyaK2MXmsl2ks7Y%3D 7605349
    • Mechoulam R, Ben-Shabat S, Hanus L et al (1995) Identification of an endogenous 2-monoglyceride, present in canine gut, that binds to cannabinoid receptors. Biochem Pharmacol 50:83-90
    • (1995) Biochem Pharmacol , vol.50 , pp. 83-90
    • Mechoulam, R.1    Ben-Shabat, S.2    Hanus, L.3
  • 142
    • 0028970517 scopus 로고
    • 2-Arachidonoylglycerol: A possible endogenous cannabinoid receptor ligand in brain
    • 1:CAS:528:DyaK2MXosVyqtLk%3D 7575630
    • Sugiura T, Kondo S, Sukagawa A et al (1995) 2-Arachidonoylglycerol: a possible endogenous cannabinoid receptor ligand in brain. Biochem Biophys Res Commun 215:89-97
    • (1995) Biochem Biophys Res Commun , vol.215 , pp. 89-97
    • Sugiura, T.1    Kondo, S.2    Sukagawa, A.3
  • 143
    • 84896131810 scopus 로고    scopus 로고
    • Cannabis finds its way into treatment of Crohn's disease
    • 4076530 1:CAS:528:DC%2BC2cXktVSmt7s%3D 24356243
    • Schicho R, Storr M (2014) Cannabis finds its way into treatment of Crohn's disease. Pharmacology 93:1-3
    • (2014) Pharmacology , vol.93 , pp. 1-3
    • Schicho, R.1    Storr, M.2
  • 144
    • 84930196343 scopus 로고    scopus 로고
    • Inhibiting endocannabinoid biosynthesis: A novel approach to the treatment of constipation
    • 1:CAS:528:DC%2BC2MXhtVent7rM 25684407
    • Bashashati M, Nasser Y, Keenan C et al (2015) Inhibiting endocannabinoid biosynthesis: a novel approach to the treatment of constipation. Br J Pharmacol 172(12):3099-3111
    • (2015) Br J Pharmacol , vol.172 , Issue.12 , pp. 3099-3111
    • Bashashati, M.1    Nasser, Y.2    Keenan, C.3
  • 145
    • 84938749877 scopus 로고    scopus 로고
    • Monoglyceride lipase-deficiency causes desensitization of intestinal cannabinoid receptor type 1 and increased colonic μ-opioid receptor sensitivity
    • [Epub ahead of print]
    • Taschler U, Eichmann TO, Radner FPW et al (2015) Monoglyceride lipase-deficiency causes desensitization of intestinal cannabinoid receptor type 1 and increased colonic μ-opioid receptor sensitivity. Br J Pharmacol [Epub ahead of print]
    • (2015) Br J Pharmacol
    • Taschler, U.1    Eichmann, T.O.2    Radner, F.P.W.3    Al, E.4
  • 146
    • 13144281703 scopus 로고    scopus 로고
    • Identification of a gene encoding an acyl CoA:diacylglycerol acyltransferase, a key enzyme in triacylglycerol synthesis
    • 23692 1:CAS:528:DyaK1cXntFWktbg%3D 9789033
    • Cases S, Smith SJ, Zheng YW et al (1998) Identification of a gene encoding an acyl CoA:diacylglycerol acyltransferase, a key enzyme in triacylglycerol synthesis. Proc Natl Acad Sci USA 95:13018-13023
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 13018-13023
    • Cases, S.1    Smith, S.J.2    Zheng, Y.W.3
  • 147
    • 0034161499 scopus 로고    scopus 로고
    • A superfamily of membrane-bound O-acyltransferases with implications for wnt signaling
    • 1:CAS:528:DC%2BD3cXhsFOisro%3D 10694878
    • Hofmann K (2000) A superfamily of membrane-bound O-acyltransferases with implications for wnt signaling. Trends Biochem Sci 25:111-112
    • (2000) Trends Biochem Sci , vol.25 , pp. 111-112
    • Hofmann, K.1
  • 148
    • 58149457426 scopus 로고    scopus 로고
    • Thematic review series: Glycerolipids. DGAT enzymes and triacylglycerol biosynthesis
    • 3837458 1:CAS:528:DC%2BD1cXht12it7rI 18757836
    • Yen CL, Stone SJ, Koliwad S et al (2008) Thematic review series: glycerolipids. DGAT enzymes and triacylglycerol biosynthesis. J Lipid Res 49:2283-2301
    • (2008) J Lipid Res , vol.49 , pp. 2283-2301
    • Yen, C.L.1    Stone, S.J.2    Koliwad, S.3
  • 149
    • 64149132208 scopus 로고    scopus 로고
    • The endoplasmic reticulum enzyme DGAT2 is found in mitochondria-associated membranes and has a mitochondrial targeting signal that promotes its association with mitochondria
    • 2643492 1:CAS:528:DC%2BD1MXhvVSntLk%3D 19049983
    • Stone SJ, Levin MC, Zhou P et al (2009) The endoplasmic reticulum enzyme DGAT2 is found in mitochondria-associated membranes and has a mitochondrial targeting signal that promotes its association with mitochondria. J Biol Chem 284:5352-5361
    • (2009) J Biol Chem , vol.284 , pp. 5352-5361
    • Stone, S.J.1    Levin, M.C.2    Zhou, P.3
  • 150
    • 78549270833 scopus 로고    scopus 로고
    • Topological orientation of acyl-CoA:diacylglycerol acyltransferase-1 (DGAT1) and identification of a putative active site histidine and the role of the n terminus in dimer/tetramer formation
    • 2988343 1:CAS:528:DC%2BC3cXhsVCrt77J 20876538
    • McFie PJ, Stone SL, Banman SL, Stone SJ (2010) Topological orientation of acyl-CoA:diacylglycerol acyltransferase-1 (DGAT1) and identification of a putative active site histidine and the role of the n terminus in dimer/tetramer formation. J Biol Chem 285:37377-37387
    • (2010) J Biol Chem , vol.285 , pp. 37377-37387
    • McFie, P.J.1    Stone, S.L.2    Banman, S.L.3    Stone, S.J.4
  • 151
    • 47249093611 scopus 로고    scopus 로고
    • An N-terminal fragment of mouse DGAT1 binds different acyl-CoAs with varying affinity
    • 1:CAS:528:DC%2BD1cXoslGmtbo%3D 18571500
    • Siloto RMP, Madhavji M, Wiehler WB et al (2008) An N-terminal fragment of mouse DGAT1 binds different acyl-CoAs with varying affinity. Biochem Biophys Res Commun 373:350-354
    • (2008) Biochem Biophys Res Commun , vol.373 , pp. 350-354
    • Siloto, R.M.P.1    Madhavji, M.2    Wiehler, W.B.3
  • 152
    • 0035503969 scopus 로고    scopus 로고
    • Human acyl-CoA:diacylglycerol acyltransferase is a tetrameric protein
    • 1222193 1:CAS:528:DC%2BD3MXovVSisbc%3D 11672446
    • Cheng D, Meegalla RL, He B et al (2001) Human acyl-CoA:diacylglycerol acyltransferase is a tetrameric protein. Biochem J 359:707-714
    • (2001) Biochem J , vol.359 , pp. 707-714
    • Cheng, D.1    Meegalla, R.L.2    He, B.3
  • 153
    • 0030957455 scopus 로고    scopus 로고
    • Overt and latent activities of diacylglycerol acyltransferase in rat liver microsomes: Possible roles in very-low-density lipoprotein triacylglycerol secretion
    • 1218291 1:CAS:528:DyaK2sXisVygurc%3D 9173878
    • Owen MR, Corstorphine CC, Zammit VA (1997) Overt and latent activities of diacylglycerol acyltransferase in rat liver microsomes: possible roles in very-low-density lipoprotein triacylglycerol secretion. Biochem J 323(1):17-21
    • (1997) Biochem J , vol.323 , Issue.1 , pp. 17-21
    • Owen, M.R.1    Corstorphine, C.C.2    Zammit, V.A.3
  • 154
    • 80054678271 scopus 로고    scopus 로고
    • Evidence that diacylglycerol acyltransferase 1 (DGAT1) has dual membrane topology in the endoplasmic reticulum of HepG2 cells
    • 3196132 1:CAS:528:DC%2BC3MXhtlSqt7bK 21846726
    • Wurie HR, Bucketts L, Zammit VA (2011) Evidence that diacylglycerol acyltransferase 1 (DGAT1) has dual membrane topology in the endoplasmic reticulum of HepG2 cells. J Biol Chem 286:36238-36247
    • (2011) J Biol Chem , vol.286 , pp. 36238-36247
    • Wurie, H.R.1    Bucketts, L.2    Zammit, V.A.3
  • 155
    • 24744443740 scopus 로고    scopus 로고
    • The triacylglycerol synthesis enzyme DGAT1 also catalyzes the synthesis of diacylglycerols, waxes, and retinyl esters
    • 1:CAS:528:DC%2BD2MXmtFKksbk%3D 15834126
    • Yen CL, Monetti M, Burri BJ Jr, Farese RV (2005) The triacylglycerol synthesis enzyme DGAT1 also catalyzes the synthesis of diacylglycerols, waxes, and retinyl esters. J Lipid Res 46:1502-1511
    • (2005) J Lipid Res , vol.46 , pp. 1502-1511
    • Yen, C.L.1    Monetti, M.2    Burri, B.J.3    Farese, R.V.4
  • 156
    • 0035914412 scopus 로고    scopus 로고
    • DGAT2 is a new diacylglycerol acyltransferase gene family: Purification, cloning, and expression in insect cells of two polypeptides from Mortierella ramanniana with diacylglycerol acyltransferase activity
    • 1:CAS:528:DC%2BD3MXnvVenur4%3D 11481333
    • Lardizabal KD, Mai JT, Wagner NW et al (2001) DGAT2 is a new diacylglycerol acyltransferase gene family: purification, cloning, and expression in insect cells of two polypeptides from Mortierella ramanniana with diacylglycerol acyltransferase activity. J Biol Chem 276:38862-38869
    • (2001) J Biol Chem , vol.276 , pp. 38862-38869
    • Lardizabal, K.D.1    Mai, J.T.2    Wagner, N.W.3
  • 157
    • 33845977414 scopus 로고    scopus 로고
    • Membrane topology and identification of key functional amino acid residues of murine acyl-CoA:diacylglycerol acyltransferase-2
    • 1:CAS:528:DC%2BD28XhtlCrt73O 17035227
    • Stone SJ, Levin MC Jr, Farese RV (2006) Membrane topology and identification of key functional amino acid residues of murine acyl-CoA:diacylglycerol acyltransferase-2. J Biol Chem 281:40273-40282
    • (2006) J Biol Chem , vol.281 , pp. 40273-40282
    • Stone, S.J.1    Levin, M.C.2    Farese, R.V.3
  • 158
    • 33244496395 scopus 로고    scopus 로고
    • Mutation of F417 but not of L418 or L420 in the lipid binding domain decreases the activity of triacylglycerol hydrolase
    • 1:CAS:528:DC%2BD28Xhtlaitb0%3D 16282638
    • Alam M, Gilham D, Vance DE, Lehner R (2006) Mutation of F417 but not of L418 or L420 in the lipid binding domain decreases the activity of triacylglycerol hydrolase. J Lipid Res 47:375-383
    • (2006) J Lipid Res , vol.47 , pp. 375-383
    • Alam, M.1    Gilham, D.2    Vance, D.E.3    Lehner, R.4
  • 159
    • 38849096602 scopus 로고    scopus 로고
    • Imaging of lipid biosynthesis: How a neutral lipid enters lipid droplets
    • 1:CAS:528:DC%2BD1cXisVakur4%3D 18088320
    • Kuerschner L, Moessinger C, Thiele C (2008) Imaging of lipid biosynthesis: how a neutral lipid enters lipid droplets. Traffic 9:338-352
    • (2008) Traffic , vol.9 , pp. 338-352
    • Kuerschner, L.1    Moessinger, C.2    Thiele, C.3
  • 160
    • 80051522307 scopus 로고    scopus 로고
    • Murine diacylglycerol acyltransferase-2 (DGAT2) can catalyze triacylglycerol synthesis and promote lipid droplet formation independent of its localization to the endoplasmic reticulum
    • 3151068 1:CAS:528:DC%2BC3MXpsl2ms7Y%3D 21680734
    • McFie PJ, Banman SL, Kary S, Stone SJ (2011) Murine diacylglycerol acyltransferase-2 (DGAT2) can catalyze triacylglycerol synthesis and promote lipid droplet formation independent of its localization to the endoplasmic reticulum. J Biol Chem 286:28235-28246
    • (2011) J Biol Chem , vol.286 , pp. 28235-28246
    • McFie, P.J.1    Banman, S.L.2    Kary, S.3    Stone, S.J.4
  • 161
    • 1642523683 scopus 로고    scopus 로고
    • Lipopenia and skin barrier abnormalities in DGAT2-deficient mice
    • 1:CAS:528:DC%2BD2cXitFyhu78%3D 14668353
    • Stone SJ, Myers HM, Watkins SM et al (2004) Lipopenia and skin barrier abnormalities in DGAT2-deficient mice. J Biol Chem 279:11767-11776
    • (2004) J Biol Chem , vol.279 , pp. 11767-11776
    • Stone, S.J.1    Myers, H.M.2    Watkins, S.M.3
  • 162
    • 80053499230 scopus 로고    scopus 로고
    • Characterization of acyl-coenzyme A: Diacylglycerol acyltransferase (DGAT) enzyme of human small intestine
    • 1:CAS:528:DC%2BC3MXmtl2ns70%3D 21369919
    • Hiramine Y, Tanabe T (2011) Characterization of acyl-coenzyme A: diacylglycerol acyltransferase (DGAT) enzyme of human small intestine. J Physiol Biochem 67:259-264
    • (2011) J Physiol Biochem , vol.67 , pp. 259-264
    • Hiramine, Y.1    Tanabe, T.2
  • 163
    • 0034103658 scopus 로고    scopus 로고
    • Obesity resistance and multiple mechanisms of triglyceride synthesis in mice lacking Dgat
    • 1:CAS:528:DC%2BD3cXjtFSlt78%3D 10802663
    • Smith SJ, Cases S, Jensen DR et al (2000) Obesity resistance and multiple mechanisms of triglyceride synthesis in mice lacking Dgat. Nat Genet 25:87-90
    • (2000) Nat Genet , vol.25 , pp. 87-90
    • Smith, S.J.1    Cases, S.2    Jensen, D.R.3
  • 164
    • 84865227832 scopus 로고    scopus 로고
    • Diacylglycerol acyltransferase 2 (DGAT2) acts upstream of DGAT1, and utilises nascent diglycerides and de novo synthesised fatty acids in HepG2 cells
    • 1:CAS:528:DC%2BC38Xht1ahu7fJ 22748069
    • Wurie HR, Buckett L, Zammit VA (2012) Diacylglycerol acyltransferase 2 (DGAT2) acts upstream of DGAT1, and utilises nascent diglycerides and de novo synthesised fatty acids in HepG2 cells. FEBS J 279(17):3033-3047
    • (2012) FEBS J , vol.279 , Issue.17 , pp. 3033-3047
    • Wurie, H.R.1    Buckett, L.2    Zammit, V.A.3
  • 165
    • 84861425644 scopus 로고    scopus 로고
    • The use of stable isotope-labeled glycerol and oleic acid to differentiate the hepatic functions of DGAT1 and -2
    • 3351817 1:CAS:528:DC%2BC38Xns1emtbk%3D 22493088
    • Qi J, Lang W, Geisler JG et al (2012) The use of stable isotope-labeled glycerol and oleic acid to differentiate the hepatic functions of DGAT1 and -2. J Lipid Res 53:1106-1116
    • (2012) J Lipid Res , vol.53 , pp. 1106-1116
    • Qi, J.1    Lang, W.2    Geisler, J.G.3
  • 166
    • 10744229235 scopus 로고    scopus 로고
    • Cloning of the first sn1-DAG lipases points to the spatial and temporal regulation of endocannabinoid signaling in the brain
    • 2173631 1:CAS:528:DC%2BD3sXovFCnur8%3D 14610053
    • Bisogno T, Howell F, Williams G et al (2003) Cloning of the first sn1-DAG lipases points to the spatial and temporal regulation of endocannabinoid signaling in the brain. J Cell Biol 163:463-468
    • (2003) J Cell Biol , vol.163 , pp. 463-468
    • Bisogno, T.1    Howell, F.2    Williams, G.3
  • 167
    • 76649137560 scopus 로고    scopus 로고
    • Loss of retrograde endocannabinoid signaling and reduced adult neurogenesis in diacylglycerol lipase knock-out mice
    • 1:CAS:528:DC%2BC3cXkt12ltr0%3D 20147530
    • Gao Y, Vasilyev DV, Goncalves MB et al (2010) Loss of retrograde endocannabinoid signaling and reduced adult neurogenesis in diacylglycerol lipase knock-out mice. J Neurosci 30:2017-2024
    • (2010) J Neurosci , vol.30 , pp. 2017-2024
    • Gao, Y.1    Vasilyev, D.V.2    Goncalves, M.B.3
  • 168
    • 79959291986 scopus 로고    scopus 로고
    • Diacylglycerol lipase-alpha and -beta control neurite outgrowth in neuro-2a cells through distinct molecular mechanisms
    • 3127538 1:CAS:528:DC%2BC3MXosFajtro%3D 21493725
    • Jung K, Astarita G, Thongkham D, Piomelli D (2011) Diacylglycerol lipase-alpha and -beta control neurite outgrowth in neuro-2a cells through distinct molecular mechanisms. Mol Pharmacol 80:60-67
    • (2011) Mol Pharmacol , vol.80 , pp. 60-67
    • Jung, K.1    Astarita, G.2    Thongkham, D.3    Piomelli, D.4
  • 169
    • 0014629493 scopus 로고
    • Structural analyses of rat liver phosphoglycerides
    • 1:CAS:528:DyaE3cXjvFSnsA%3D%3D 4312070
    • Wood R, Harlow RD (1969) Structural analyses of rat liver phosphoglycerides. Arch Biochem Biophys 135:272-281
    • (1969) Arch Biochem Biophys , vol.135 , pp. 272-281
    • Wood, R.1    Harlow, R.D.2
  • 170
    • 0014478824 scopus 로고
    • Molecular species of lecithins from erythrocytes and plasma of man
    • 1:CAS:528:DyaF1MXktVSiur0%3D 5782351
    • Marai L, Kuksis A (1969) Molecular species of lecithins from erythrocytes and plasma of man. J Lipid Res 10:141-152
    • (1969) J Lipid Res , vol.10 , pp. 141-152
    • Marai, L.1    Kuksis, A.2
  • 171
    • 67649886200 scopus 로고    scopus 로고
    • From endocannabinoid profiling to "endocannabinoid therapeutics"
    • 1:CAS:528:DC%2BD1MXosVWlurs%3D 19497779
    • Ligresti A, Petrosino S, Di Marzo V (2009) From endocannabinoid profiling to "endocannabinoid therapeutics". Curr Opin Chem Biol 13:321-331
    • (2009) Curr Opin Chem Biol , vol.13 , pp. 321-331
    • Ligresti, A.1    Petrosino, S.2    Di Marzo, V.3
  • 172
    • 38149018650 scopus 로고    scopus 로고
    • Diacylglycerol kinases: At the hub of cell signalling
    • 1:CAS:528:DC%2BD2sXhsVantLbF 18062770
    • Merida I, Avila-Flores A, Merino E (2008) Diacylglycerol kinases: at the hub of cell signalling. Biochem J 409:1-18
    • (2008) Biochem J , vol.409 , pp. 1-18
    • Merida, I.1    Avila-Flores, A.2    Merino, E.3
  • 173
    • 34249995516 scopus 로고    scopus 로고
    • Diacylglycerol kinases: Why so many of them?
    • 1:CAS:528:DC%2BD2sXmsFCmtro%3D 17512245
    • Sakane F, Imai S, Kai M et al (2007) Diacylglycerol kinases: why so many of them? Biochim Biophys Acta 1771:793-806
    • (2007) Biochim Biophys Acta , vol.1771 , pp. 793-806
    • Sakane, F.1    Imai, S.2    Kai, M.3
  • 174
    • 67349142556 scopus 로고    scopus 로고
    • Mammalian diacylglycerol kinases: Molecular interactions and biological functions of selected isoforms
    • 2744455 1:CAS:528:DC%2BD1MXmvFGhtro%3D 19364481
    • Topham MK, Epand RM (2009) Mammalian diacylglycerol kinases: molecular interactions and biological functions of selected isoforms. Biochim Biophys Acta 1790:416-424
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 416-424
    • Topham, M.K.1    Epand, R.M.2
  • 175
    • 0033597338 scopus 로고    scopus 로고
    • Mammalian diacylglycerol kinases, a family of lipid kinases with signaling functions
    • 1:CAS:528:DyaK1MXislGmtLs%3D 10206945
    • Topham MK, Prescott SM (1999) Mammalian diacylglycerol kinases, a family of lipid kinases with signaling functions. J Biol Chem 274:11447-11450
    • (1999) J Biol Chem , vol.274 , pp. 11447-11450
    • Topham, M.K.1    Prescott, S.M.2
  • 176
    • 41949141028 scopus 로고    scopus 로고
    • Lipid messenger, diacylglycerol, and its regulator, diacylglycerol kinase, in cells, organs, and animals: History and perspective
    • 1:CAS:528:DC%2BD1cXkt1Wgs7Y%3D 18323690
    • Goto K, Hozumi Y, Nakano T et al (2008) Lipid messenger, diacylglycerol, and its regulator, diacylglycerol kinase, in cells, organs, and animals: history and perspective. Tohoku J Exp Med 214:199-212
    • (2008) Tohoku J Exp Med , vol.214 , pp. 199-212
    • Goto, K.1    Hozumi, Y.2    Nakano, T.3
  • 177
    • 80054080494 scopus 로고    scopus 로고
    • Regulation and functions of diacylglycerol kinases
    • 1:CAS:528:DC%2BC3MXpsFSktbo%3D 21800853
    • Shulga YV, Topham MK, Epand RM (2011) Regulation and functions of diacylglycerol kinases. Chem Rev 111:6186-6208
    • (2011) Chem Rev , vol.111 , pp. 6186-6208
    • Shulga, Y.V.1    Topham, M.K.2    Epand, R.M.3
  • 178
    • 0022243876 scopus 로고
    • The nature of protein kinase C activation by physically defined phospholipid vesicles and diacylglycerols
    • 1:CAS:528:DyaL2MXlsFKgsrY%3D 3161882
    • Boni LT, Rando RR (1985) The nature of protein kinase C activation by physically defined phospholipid vesicles and diacylglycerols. J Biol Chem 260:10819-10825
    • (1985) J Biol Chem , vol.260 , pp. 10819-10825
    • Boni, L.T.1    Rando, R.R.2
  • 179
    • 0021774491 scopus 로고
    • The stereospecific activation of protein kinase C
    • 1:CAS:528:DyaL2cXltVKnsrw%3D
    • Rando RR, Young N (1984) The stereospecific activation of protein kinase C. Biochem Biophys Res 122:818-823
    • (1984) Biochem Biophys Res , vol.122 , pp. 818-823
    • Rando, R.R.1    Young, N.2
  • 180
    • 0022930403 scopus 로고
    • Stereospecificity of diacylglycerol for stimulus-response coupling in platelets
    • 1:CAS:528:DyaL2sXjtVKjsQ%3D%3D 3778485
    • Nomura H, Ase K, Sekiguchi K et al (1986) Stereospecificity of diacylglycerol for stimulus-response coupling in platelets. Biochem Biophys Res Commun 140:1143-1151
    • (1986) Biochem Biophys Res Commun , vol.140 , pp. 1143-1151
    • Nomura, H.1    Ase, K.2    Sekiguchi, K.3
  • 181
    • 37149021094 scopus 로고    scopus 로고
    • Substrate chirality and specificity of diacylglycerol kinases and the multisubstrate lipid kinase
    • 1:CAS:528:DC%2BD2sXhtlSkurfK 18004883
    • Epand RM, Shulga YV, Timmons HC et al (2007) Substrate chirality and specificity of diacylglycerol kinases and the multisubstrate lipid kinase. Biochemistry 46:14225-14231
    • (2007) Biochemistry , vol.46 , pp. 14225-14231
    • Epand, R.M.1    Shulga, Y.V.2    Timmons, H.C.3
  • 182
    • 0029998639 scopus 로고    scopus 로고
    • Molecular cloning of a novel human diacylglycerol kinase highly selective for arachidonate-containing substrates
    • 1:CAS:528:DyaK28XisFKjs7s%3D 8626589
    • Tang W, Bunting M, Zimmerman GA et al (1996) Molecular cloning of a novel human diacylglycerol kinase highly selective for arachidonate-containing substrates. J Biol Chem 271:10237-10241
    • (1996) J Biol Chem , vol.271 , pp. 10237-10241
    • Tang, W.1    Bunting, M.2    Zimmerman, G.A.3
  • 183
    • 71449090748 scopus 로고    scopus 로고
    • Diacylglycerol kinase ε is selective for both acyl chains of phosphatidic acid or diacylglycerol
    • 2781506 1:CAS:528:DC%2BD1MXhtlequ7bP 19744926
    • Lung M, Shulga YV, Ivanova PT et al (2009) Diacylglycerol kinase ε is selective for both acyl chains of phosphatidic acid or diacylglycerol. J Biol Chem 284:31062-31073
    • (2009) J Biol Chem , vol.284 , pp. 31062-31073
    • Lung, M.1    Shulga, Y.V.2    Ivanova, P.T.3
  • 184
    • 0035836345 scopus 로고    scopus 로고
    • Diacylglycerol kinase epsilon regulates seizure susceptibility and long-term potentiation through arachidonoyl- inositol lipid signaling
    • De Turco EBR, Tang W, Topham MK et al (2001) Diacylglycerol kinase epsilon regulates seizure susceptibility and long-term potentiation through arachidonoyl- inositol lipid signaling. Proc Natl Acad Sci USA 98:4740-4745
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 4740-4745
    • De Turco, E.B.R.1    Tang, W.2    Topham, M.K.3
  • 185
    • 0033561020 scopus 로고    scopus 로고
    • Cloning and expression of a human choline/ethanolaminephosphotransferase: Synthesis of phosphatidylcholine and phosphatidylethanolamine
    • 1220157 1:CAS:528:DyaK1MXjtVakt70%3D 10191259
    • Henneberry AL, McMaster CR (1999) Cloning and expression of a human choline/ethanolaminephosphotransferase: synthesis of phosphatidylcholine and phosphatidylethanolamine. Biochem J 339(Pt 2):291-298
    • (1999) Biochem J , vol.339 , pp. 291-298
    • Henneberry, A.L.1    McMaster, C.R.2
  • 186
    • 0034703103 scopus 로고    scopus 로고
    • Cloning, genomic organization, and characterization of a human cholinephosphotransferase
    • 1:CAS:528:DC%2BD3cXmvFKjtLY%3D 10893425
    • Henneberry AL, Wistow G, McMaster CR (2000) Cloning, genomic organization, and characterization of a human cholinephosphotransferase. J Biol Chem 275:29808-29815
    • (2000) J Biol Chem , vol.275 , pp. 29808-29815
    • Henneberry, A.L.1    Wistow, G.2    McMaster, C.R.3
  • 187
    • 0036734611 scopus 로고    scopus 로고
    • The major sites of cellular phospholipid synthesis and molecular determinants of Fatty Acid and lipid head group specificity
    • 124149 1:CAS:528:DC%2BD38XntlGis7k%3D 12221122
    • Henneberry AL, Wright MM, McMaster CR (2002) The major sites of cellular phospholipid synthesis and molecular determinants of Fatty Acid and lipid head group specificity. Mol Biol Cell 13:3148-3161
    • (2002) Mol Biol Cell , vol.13 , pp. 3148-3161
    • Henneberry, A.L.1    Wright, M.M.2    McMaster, C.R.3
  • 188
    • 0031552997 scopus 로고    scopus 로고
    • CDP-choline:1,2-diacylglycerol cholinephosphotransferase
    • 9370321
    • McMaster CR, Bell RM (1997) CDP-choline:1,2-diacylglycerol cholinephosphotransferase. Biochim Biophys Acta 1348:100-110
    • (1997) Biochim Biophys Acta , vol.1348 , pp. 100-110
    • McMaster, C.R.1    Bell, R.M.2
  • 189
    • 0028146323 scopus 로고
    • Chimeric enzymes. Structure-function analysis of segments of sn-1,2-diacylglycerol choline- and ethanolaminephosphotransferases
    • 1:CAS:528:DyaK2cXlvF2nsbw%3D 8063717
    • Hjelmstad RH, Morash SC, McMaster CR, Bell RM (1994) Chimeric enzymes. Structure-function analysis of segments of sn-1,2-diacylglycerol choline- and ethanolaminephosphotransferases. J Biol Chem 269:20995-21002
    • (1994) J Biol Chem , vol.269 , pp. 20995-21002
    • Hjelmstad, R.H.1    Morash, S.C.2    McMaster, C.R.3    Bell, R.M.4
  • 190
    • 0031552956 scopus 로고    scopus 로고
    • CDP-ethanolamine:1,2-diacylglycerol ethanolaminephosphotransferase
    • 1:CAS:528:DyaK2sXmtFKhtbw%3D 9370323
    • McMaster CR, Bell RM (1997) CDP-ethanolamine:1,2-diacylglycerol ethanolaminephosphotransferase. Biochim Biophys Acta 1348:117-123
    • (1997) Biochim Biophys Acta , vol.1348 , pp. 117-123
    • McMaster, C.R.1    Bell, R.M.2
  • 191
    • 0028077593 scopus 로고
    • Phosphatidylcholine biosynthesis in Saccharomyces cerevisiae. Regulatory insights from studies employing null and chimeric sn-1,2-diacylglycerol choline- and ethanolaminephosphotransferases
    • 1:CAS:528:DyaK2cXmsFSqs7c%3D 7961735
    • McMaster CR, Bell RM (1994) Phosphatidylcholine biosynthesis in Saccharomyces cerevisiae. Regulatory insights from studies employing null and chimeric sn-1,2-diacylglycerol choline- and ethanolaminephosphotransferases. J Biol Chem 269:28010-28016
    • (1994) J Biol Chem , vol.269 , pp. 28010-28016
    • McMaster, C.R.1    Bell, R.M.2
  • 192
    • 0028035256 scopus 로고
    • Functional redundancy of CDP-ethanolamine and CDP-choline pathway enzymes in phospholipid biosynthesis: Ethanolamine-dependent effects on steady-state membrane phospholipid composition in Saccharomyces cerevisiae
    • 197054 1:CAS:528:DyaK2cXmvFKru7w%3D 7961445
    • McGee TP, Skinner HB, Bankaitis VA (1994) Functional redundancy of CDP-ethanolamine and CDP-choline pathway enzymes in phospholipid biosynthesis: ethanolamine-dependent effects on steady-state membrane phospholipid composition in Saccharomyces cerevisiae. J Bacteriol 176:6861-6868
    • (1994) J Bacteriol , vol.176 , pp. 6861-6868
    • McGee, T.P.1    Skinner, H.B.2    Bankaitis, V.A.3
  • 193
    • 0025028993 scopus 로고
    • Evidence that only newly made phosphatidylethanolamine is methylated to phosphatidylcholine and that phosphatidylethanolamine is not significantly deacylated-reacylated in rat hepatocytes
    • 1:CAS:528:DyaK3MXitFelsg%3D%3D 2211705
    • Samborski RW, Ridgway ND, Vance DE (1990) Evidence that only newly made phosphatidylethanolamine is methylated to phosphatidylcholine and that phosphatidylethanolamine is not significantly deacylated-reacylated in rat hepatocytes. J Biol Chem 265:18322-18329
    • (1990) J Biol Chem , vol.265 , pp. 18322-18329
    • Samborski, R.W.1    Ridgway, N.D.2    Vance, D.E.3
  • 194
    • 26444514142 scopus 로고    scopus 로고
    • The diacylglycerol-sensitive TRPC3/6/7 subfamily of cation channels: Functional characterization and physiological relevance
    • 1:CAS:528:DC%2BD2MXhtVKqu7rL
    • Dietrich A, Kalwa H, Rost BR, Gudermann T (2005) The diacylglycerol-sensitive TRPC3/6/7 subfamily of cation channels: functional characterization and physiological relevance. Pflugers Arch Eur J Physiol 451:72-80
    • (2005) Pflugers Arch Eur J Physiol , vol.451 , pp. 72-80
    • Dietrich, A.1    Kalwa, H.2    Rost, B.R.3    Gudermann, T.4
  • 195
    • 77953897740 scopus 로고    scopus 로고
    • On the potential role of source and species of diacylglycerol in phospholipase-dependent regulation of TRPC3 channels
    • 1:CAS:528:DC%2BC3cXhtlKrt77E
    • Vazquez G, Tano JY, Smedlund K (2010) On the potential role of source and species of diacylglycerol in phospholipase-dependent regulation of TRPC3 channels. Channels (Austin) 4:232-240
    • (2010) Channels (Austin) , vol.4 , pp. 232-240
    • Vazquez, G.1    Tano, J.Y.2    Smedlund, K.3
  • 196
    • 55949109631 scopus 로고    scopus 로고
    • Structural basis of protein kinase C isoform function
    • 2899688 1:CAS:528:DC%2BD1cXhtlGgtbnJ 18923184
    • Steinberg SF (2008) Structural basis of protein kinase C isoform function. Physiol Rev 88:1341-1378
    • (2008) Physiol Rev , vol.88 , pp. 1341-1378
    • Steinberg, S.F.1
  • 197
    • 78651376861 scopus 로고    scopus 로고
    • Protein kinase C isoforms: Mediators of reactive lipid metabolites in the development of insulin resistance
    • 1:CAS:528:DC%2BC3MXnsFWnsg%3D%3D 21176778
    • Turban S, Hajduch E (2011) Protein kinase C isoforms: mediators of reactive lipid metabolites in the development of insulin resistance. FEBS Lett 585:269-274
    • (2011) FEBS Lett , vol.585 , pp. 269-274
    • Turban, S.1    Hajduch, E.2
  • 198
    • 0035413601 scopus 로고    scopus 로고
    • Protein kinase C: Structural and spatial regulation by phosphorylation, cofactors, and macromolecular interactions
    • 1:CAS:528:DC%2BD3MXkslCju7g%3D 11749377
    • Newton AC (2001) Protein kinase C: structural and spatial regulation by phosphorylation, cofactors, and macromolecular interactions. Chem Rev 101:2353-2364
    • (2001) Chem Rev , vol.101 , pp. 2353-2364
    • Newton, A.C.1
  • 199
    • 0038754049 scopus 로고    scopus 로고
    • Phorbol esters and neurotransmitter release: More than just protein kinase C?
    • 1573789 1:CAS:528:DC%2BD3sXjsFGitbg%3D 12711617
    • Silinsky EM, Searl TJ (2003) Phorbol esters and neurotransmitter release: more than just protein kinase C? Br J Pharmacol 138:1191-1201
    • (2003) Br J Pharmacol , vol.138 , pp. 1191-1201
    • Silinsky, E.M.1    Searl, T.J.2
  • 200
    • 0036905264 scopus 로고    scopus 로고
    • Move over protein kinase C, you've got company: Alternative cellular effectors of diacylglycerol and phorbol esters
    • 1:CAS:528:DC%2BD38XpvVSqt7k%3D 12414987
    • Brose N, Rosenmund C (2002) Move over protein kinase C, you've got company: alternative cellular effectors of diacylglycerol and phorbol esters. J Cell Sci 115:4399-4411
    • (2002) J Cell Sci , vol.115 , pp. 4399-4411
    • Brose, N.1    Rosenmund, C.2
  • 201
    • 0036209077 scopus 로고    scopus 로고
    • Novel "nonkinase" phorbol ester receptors: The C1 domain connection
    • 1:CAS:528:DC%2BD38Xis1Ogurw%3D 11901214
    • Kazanietz MG (2002) Novel "nonkinase" phorbol ester receptors: the C1 domain connection. Mol Pharmacol 61:759-767
    • (2002) Mol Pharmacol , vol.61 , pp. 759-767
    • Kazanietz, M.G.1
  • 202
    • 0034025493 scopus 로고    scopus 로고
    • Eyes, wide shut: Protein kinase C isozymes are not the only receptors for the phorbol ester tumor promoters
    • 1:CAS:528:DC%2BD3cXjtFSjsL8%3D 10820483
    • Kazanietz MG (2000) Eyes, wide shut: protein kinase C isozymes are not the only receptors for the phorbol ester tumor promoters. Mol Carcinog 28:5-11
    • (2000) Mol Carcinog , vol.28 , pp. 5-11
    • Kazanietz, M.G.1
  • 203
    • 0032849088 scopus 로고    scopus 로고
    • New insights into the regulation of protein kinase C and novel phorbol ester receptors
    • 1:CAS:528:DyaK1MXms1Oiu7g%3D 10506570
    • Ron D, Kazanietz MG (1999) New insights into the regulation of protein kinase C and novel phorbol ester receptors. FASEB J 13:1658-1676
    • (1999) FASEB J , vol.13 , pp. 1658-1676
    • Ron, D.1    Kazanietz, M.G.2
  • 205
    • 0242321186 scopus 로고    scopus 로고
    • Divergence and complexities in DAG signaling: Looking beyond PKC
    • 1:CAS:528:DC%2BD3sXos12ks7k%3D 14607084
    • Yang C, Kazanietz MG (2003) Divergence and complexities in DAG signaling: looking beyond PKC. Trends Pharmacol Sci 24:602-608
    • (2003) Trends Pharmacol Sci , vol.24 , pp. 602-608
    • Yang, C.1    Kazanietz, M.G.2
  • 206
    • 0028649465 scopus 로고
    • Expression of alpha 1-chimaerin (rac-1 GAP) alters the cytoskeletal and adhesive properties of fibroblasts
    • 1:CAS:528:DyaK2MXislSqt70%3D 7534315
    • Herrera R, Shivers BD (1994) Expression of alpha 1-chimaerin (rac-1 GAP) alters the cytoskeletal and adhesive properties of fibroblasts. J Cell Biochem 56:582-591
    • (1994) J Cell Biochem , vol.56 , pp. 582-591
    • Herrera, R.1    Shivers, B.D.2
  • 207
    • 0034644772 scopus 로고    scopus 로고
    • Characterization of RasGRP2, a plasma membrane-targeted, dual specificity Ras/Rap exchange factor
    • 1:CAS:528:DC%2BD3cXnsFejtL0%3D 10918068
    • Clyde-Smith J, Silins G, Gartside M et al (2000) Characterization of RasGRP2, a plasma membrane-targeted, dual specificity Ras/Rap exchange factor. J Biol Chem 275:32260-32267
    • (2000) J Biol Chem , vol.275 , pp. 32260-32267
    • Clyde-Smith, J.1    Silins, G.2    Gartside, M.3
  • 208
    • 0035853782 scopus 로고    scopus 로고
    • Activation of the Rap1 guanine nucleotide exchange gene, CalDAG-GEF I, in BXH-2 murine myeloid leukemia
    • 1:CAS:528:DC%2BD3MXjtFylsL8%3D 11278453
    • Dupuy AJ, Morgan K, Von Lintig FC et al (2001) Activation of the Rap1 guanine nucleotide exchange gene, CalDAG-GEF I, in BXH-2 murine myeloid leukemia. J Biol Chem 276:11804-11811
    • (2001) J Biol Chem , vol.276 , pp. 11804-11811
    • Dupuy, A.J.1    Morgan, K.2    Von Lintig, F.C.3
  • 209
    • 0033084096 scopus 로고    scopus 로고
    • Differential expression of two novel Munc13 proteins in rat brain
    • 1219986 1:CAS:528:DyaK1MXhsFykurw%3D 9895278
    • Augustin I, Betz A, Herrmann C et al (1999) Differential expression of two novel Munc13 proteins in rat brain. Biochem J 337(Pt 3):363-371
    • (1999) Biochem J , vol.337 , pp. 363-371
    • Augustin, I.1    Betz, A.2    Herrmann, C.3
  • 210
    • 0033615054 scopus 로고    scopus 로고
    • Munc13-1 is essential for fusion competence of glutamatergic synaptic vesicles
    • 1:CAS:528:DyaK1MXltVGmt7o%3D 10440375
    • Augustin I, Rosenmund C, Südhof TC, Brose N (1999) Munc13-1 is essential for fusion competence of glutamatergic synaptic vesicles. Nature 400:457-461
    • (1999) Nature , vol.400 , pp. 457-461
    • Augustin, I.1    Rosenmund, C.2    Südhof, T.C.3    Brose, N.4
  • 211
    • 0033352861 scopus 로고    scopus 로고
    • Drosophila UNC-13 is essential for synaptic transmission
    • 1:CAS:528:DyaK1MXmvFGlsrw%3D 10526334
    • Aravamudan B, Fergestad T, Davis WS et al (1999) Drosophila UNC-13 is essential for synaptic transmission. Nat Neurosci 2:965-971
    • (1999) Nat Neurosci , vol.2 , pp. 965-971
    • Aravamudan, B.1    Fergestad, T.2    Davis, W.S.3
  • 212
    • 0034679721 scopus 로고    scopus 로고
    • Munc13-1 acts as a priming factor for large dense-core vesicles in bovine chromaffin cells
    • 313963 1:CAS:528:DC%2BD3cXmtlegsrs%3D 10899113
    • Ashery U, Varoqueaux F, Voets T et al (2000) Munc13-1 acts as a priming factor for large dense-core vesicles in bovine chromaffin cells. EMBO J 19:3586-3596
    • (2000) EMBO J , vol.19 , pp. 3586-3596
    • Ashery, U.1    Varoqueaux, F.2    Voets, T.3
  • 213
    • 0033538345 scopus 로고    scopus 로고
    • Gbetagamma-mediated regulation of Golgi organization is through the direct activation of protein kinase D
    • 1:CAS:528:DyaK1MXks1Kktr4%3D 10412981
    • Jamora C, Yamanouye N, Van Lint J et al (1999) Gbetagamma-mediated regulation of Golgi organization is through the direct activation of protein kinase D. Cell 98:59-68
    • (1999) Cell , vol.98 , pp. 59-68
    • Jamora, C.1    Yamanouye, N.2    Van Lint, J.3
  • 214
    • 0035830496 scopus 로고    scopus 로고
    • Protein kinase D regulates the fission of cell surface destined transport carriers from the trans-Golgi network
    • 1:CAS:528:DC%2BD3MXis1ejsb8%3D 11239398
    • Liljedahl M, Maeda Y, Colanzi A et al (2001) Protein kinase D regulates the fission of cell surface destined transport carriers from the trans-Golgi network. Cell 104:409-420
    • (2001) Cell , vol.104 , pp. 409-420
    • Liljedahl, M.1    Maeda, Y.2    Colanzi, A.3
  • 215
    • 0034792872 scopus 로고    scopus 로고
    • Intracellular signalling mechanisms regulating glucose transport in insulin-sensitive tissues (review)
    • 1:CAS:528:DC%2BD3MXnslGqsbY%3D 11681786
    • Litherland GJ, Hajduch E, Hundal HS (2001) Intracellular signalling mechanisms regulating glucose transport in insulin-sensitive tissues (review). Mol Membr Biol 18:195-204
    • (2001) Mol Membr Biol , vol.18 , pp. 195-204
    • Litherland, G.J.1    Hajduch, E.2    Hundal, H.S.3
  • 216
    • 72949093349 scopus 로고    scopus 로고
    • The nuts and bolts of AGC protein kinases
    • 1:CAS:528:DC%2BD1MXhsFymt7bI 20027184
    • Pearce LR, Komander D, Alessi DR (2010) The nuts and bolts of AGC protein kinases. Nat Rev Mol Cell Biol 11:9-22
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 9-22
    • Pearce, L.R.1    Komander, D.2    Alessi, D.R.3
  • 217
    • 0037677096 scopus 로고    scopus 로고
    • Insulin-stimulated phosphorylation of a Rab GTPase-activating protein regulates GLUT4 translocation
    • 1:CAS:528:DC%2BD3sXjtVCmt7w%3D 12637568
    • Sano H, Kane S, Sano E et al (2003) Insulin-stimulated phosphorylation of a Rab GTPase-activating protein regulates GLUT4 translocation. J Biol Chem 278:14599-14602
    • (2003) J Biol Chem , vol.278 , pp. 14599-14602
    • Sano, H.1    Kane, S.2    Sano, E.3
  • 218
    • 77953868236 scopus 로고    scopus 로고
    • Lipid-induced insulin resistance: Unravelling the mechanism
    • 2995547 1:CAS:528:DC%2BC3cXotVagtrk%3D 20609972
    • Samuel VT, Petersen KF, Shulman GI (2010) Lipid-induced insulin resistance: unravelling the mechanism. Lancet 375:2267-2277
    • (2010) Lancet , vol.375 , pp. 2267-2277
    • Samuel, V.T.1    Petersen, K.F.2    Shulman, G.I.3
  • 219
    • 33847404482 scopus 로고    scopus 로고
    • Inhibition of protein kinase Cepsilon prevents hepatic insulin resistance in nonalcoholic fatty liver disease
    • 1797607 1:CAS:528:DC%2BD2sXis12htLo%3D 17318260
    • Samuel VT, Liu ZX, Wang A et al (2007) Inhibition of protein kinase Cepsilon prevents hepatic insulin resistance in nonalcoholic fatty liver disease. J Clin Invest 117:739-745
    • (2007) J Clin Invest , vol.117 , pp. 739-745
    • Samuel, V.T.1    Liu, Z.X.2    Wang, A.3
  • 220
    • 8544233570 scopus 로고    scopus 로고
    • Protein kinase C Theta inhibits insulin signaling by phosphorylating IRS1 at Ser(1101)
    • 1:CAS:528:DC%2BD2cXovVCgtbs%3D 15364919
    • Li Y, Soos TJ, Li X et al (2004) Protein kinase C Theta inhibits insulin signaling by phosphorylating IRS1 at Ser(1101). J Biol Chem 279:45304-45307
    • (2004) J Biol Chem , vol.279 , pp. 45304-45307
    • Li, Y.1    Soos, T.J.2    Li, X.3
  • 221
    • 34347238724 scopus 로고    scopus 로고
    • Hepatic overexpression of glycerol-sn-3-phosphate acyltransferase 1 in rats causes insulin resistance
    • 2819346 1:CAS:528:DC%2BD2sXltFemtbo%3D 17389595
    • Nagle CA, An J, Shiota M et al (2007) Hepatic overexpression of glycerol-sn-3-phosphate acyltransferase 1 in rats causes insulin resistance. J Biol Chem 282:14807-14815
    • (2007) J Biol Chem , vol.282 , pp. 14807-14815
    • Nagle, C.A.1    An, J.2    Shiota, M.3
  • 222
    • 0025123408 scopus 로고
    • 1,2-Diacylglycerol and ceramide levels in insulin-resistant tissues of the rat in vivo
    • 1:CAS:528:DyaK3cXlvV2isLc%3D 2211599
    • Turinsky J, O'Sullivan DM, Bayly BP (1990) 1,2-Diacylglycerol and ceramide levels in insulin-resistant tissues of the rat in vivo. J Biol Chem 265:16880-16885
    • (1990) J Biol Chem , vol.265 , pp. 16880-16885
    • Turinsky, J.1    O'Sullivan, D.M.2    Bayly, B.P.3
  • 223
    • 78349242167 scopus 로고    scopus 로고
    • A high-fat, ketogenic diet causes hepatic insulin resistance in mice, despite increasing energy expenditure and preventing weight gain
    • 1:CAS:528:DC%2BC3cXhsFSgu7fO
    • Jornayvaz FR, Jurczak MJ, Lee HY et al (2010) A high-fat, ketogenic diet causes hepatic insulin resistance in mice, despite increasing energy expenditure and preventing weight gain. Am J Physiol Metab 299:E808-E815
    • (2010) Am J Physiol Metab , vol.299 , pp. E808-E815
    • Jornayvaz, F.R.1    Jurczak, M.J.2    Lee, H.Y.3
  • 224
    • 34347235098 scopus 로고    scopus 로고
    • Dissociation of hepatic steatosis and insulin resistance in mice overexpressing DGAT in the liver
    • 1:CAS:528:DC%2BD2sXotlCitLg%3D 17618857
    • Monetti M, Levin MC, Watt MJ et al (2007) Dissociation of hepatic steatosis and insulin resistance in mice overexpressing DGAT in the liver. Cell Metab 6:69-78
    • (2007) Cell Metab , vol.6 , pp. 69-78
    • Monetti, M.1    Levin, M.C.2    Watt, M.J.3
  • 225
    • 79954996869 scopus 로고    scopus 로고
    • Hepatic insulin resistance in mice with hepatic overexpression of diacylglycerol acyltransferase 2
    • 3078388 1:CAS:528:DC%2BC3MXkvVChtr0%3D 21436037
    • Jornayvaz FR, Birkenfeld AL, Jurczak MJ et al (2011) Hepatic insulin resistance in mice with hepatic overexpression of diacylglycerol acyltransferase 2. Proc Natl Acad Sci USA 108:5748-5752
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 5748-5752
    • Jornayvaz, F.R.1    Birkenfeld, A.L.2    Jurczak, M.J.3
  • 226
    • 84860497397 scopus 로고    scopus 로고
    • Diacylglycerol activation of protein kinase Cepsilon and hepatic insulin resistance
    • Jornayvaza F, Shulman GI, Jornayvaz FR, Shulman GI (2012) Diacylglycerol activation of protein kinase Cepsilon and hepatic insulin resistance. Cell Metab 15:574-584
    • (2012) Cell Metab , vol.15 , pp. 574-584
    • Jornayvaza, F.1    Shulman, G.I.2    Jornayvaz, F.R.3    Shulman, G.I.4
  • 227
    • 80053627289 scopus 로고    scopus 로고
    • Cellular mechanism of insulin resistance in nonalcoholic fatty liver disease
    • 3182681 1:CAS:528:DC%2BC3MXht1Kmtb3I 21930939
    • Kumashiro N, Erion DM, Zhang D et al (2011) Cellular mechanism of insulin resistance in nonalcoholic fatty liver disease. Proc Natl Acad Sci USA 108:16381-16385
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 16381-16385
    • Kumashiro, N.1    Erion, D.M.2    Zhang, D.3
  • 228
    • 0141480969 scopus 로고    scopus 로고
    • Hormone-sensitive lipase null mice exhibit signs of impaired insulin sensitivity whereas insulin secretion is intact
    • 1:CAS:528:DC%2BD3sXnt1ejsLw%3D 12835327
    • Mulder H, Sorhede-Winzell M, Contreras JA et al (2003) Hormone-sensitive lipase null mice exhibit signs of impaired insulin sensitivity whereas insulin secretion is intact. J Biol Chem 278:36380-36388
    • (2003) J Biol Chem , vol.278 , pp. 36380-36388
    • Mulder, H.1    Sorhede-Winzell, M.2    Contreras, J.A.3
  • 229
    • 0035461405 scopus 로고    scopus 로고
    • A role for hormone-sensitive lipase in glucose-stimulated insulin secretion: A study in hormone-sensitive lipase-deficient mice
    • 1:CAS:528:DC%2BD3MXmsFKnsrw%3D 11522661
    • Roduit R, Masiello P, Wang SP et al (2001) A role for hormone-sensitive lipase in glucose-stimulated insulin secretion: a study in hormone-sensitive lipase-deficient mice. Diabetes 50:1970-1975
    • (2001) Diabetes , vol.50 , pp. 1970-1975
    • Roduit, R.1    Masiello, P.2    Wang, S.P.3
  • 230
    • 0041314066 scopus 로고    scopus 로고
    • Increased hepatic insulin sensitivity together with decreased hepatic triglyceride stores in hormone-sensitive lipase-deficient mice
    • 1:CAS:528:DC%2BD3sXlslGjtr8%3D 12865325
    • Voshol PJ, Haemmerle G, Ouwens DM et al (2003) Increased hepatic insulin sensitivity together with decreased hepatic triglyceride stores in hormone-sensitive lipase-deficient mice. Endocrinology 144:3456-3462
    • (2003) Endocrinology , vol.144 , pp. 3456-3462
    • Voshol, P.J.1    Haemmerle, G.2    Ouwens, D.M.3
  • 231
    • 20544449419 scopus 로고    scopus 로고
    • Hormone-sensitive lipase knockout mice have increased hepatic insulin sensitivity and are protected from short-term diet-induced insulin resistance in skeletal muscle and heart
    • 1:CAS:528:DC%2BD2MXmvVertbg%3D
    • Park SY, Kim HJ, Wang S et al (2005) Hormone-sensitive lipase knockout mice have increased hepatic insulin sensitivity and are protected from short-term diet-induced insulin resistance in skeletal muscle and heart. Am J Physiol Metab 289:E30-E39
    • (2005) Am J Physiol Metab , vol.289 , pp. E30-E39
    • Park, S.Y.1    Kim, H.J.2    Wang, S.3
  • 232
    • 84902159389 scopus 로고    scopus 로고
    • Null mutation in hormone-sensitive lipase gene and risk of type 2 diabetes
    • 4096982 24848981
    • Albert JS, Yerges-Armstrong LM, Horenstein RB et al (2014) Null mutation in hormone-sensitive lipase gene and risk of type 2 diabetes. N Engl J Med 370:2307-2315
    • (2014) N Engl J Med , vol.370 , pp. 2307-2315
    • Albert, J.S.1    Yerges-Armstrong, L.M.2    Horenstein, R.B.3
  • 233
    • 78149346457 scopus 로고    scopus 로고
    • CGI-58 knockdown in mice causes hepatic steatosis, but prevents diet-induced obesity and glucose intolerance
    • 2952571 1:CAS:528:DC%2BC3cXhsVWgt7vO 20802159
    • Brown JM, Betters JL, Lord C et al (2010) CGI-58 knockdown in mice causes hepatic steatosis, but prevents diet-induced obesity and glucose intolerance. J Lipid Res 51:3306-3315
    • (2010) J Lipid Res , vol.51 , pp. 3306-3315
    • Brown, J.M.1    Betters, J.L.2    Lord, C.3
  • 234
    • 84873178604 scopus 로고    scopus 로고
    • CGI-58 knockdown sequesters diacylglycerols in lipid droplets/ER-preventing diacylglycerol-mediated hepatic insulin resistance
    • 3562813 1:CAS:528:DC%2BC3sXisl2nsL4%3D 23302688
    • Cantley JL, Yoshimura T, Camporez JPG et al (2013) CGI-58 knockdown sequesters diacylglycerols in lipid droplets/ER-preventing diacylglycerol-mediated hepatic insulin resistance. Proc Natl Acad Sci USA 110:1869-1874
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 1869-1874
    • Cantley, J.L.1    Yoshimura, T.2    Camporez, J.P.G.3
  • 235
    • 79959387473 scopus 로고    scopus 로고
    • Altered skeletal muscle lipase expression and activity contribute to insulin resistance in humans
    • 3114384 1:CAS:528:DC%2BC3MXnvFeqtbk%3D 21498783
    • Badin PM, Louche K, Mairal A et al (2011) Altered skeletal muscle lipase expression and activity contribute to insulin resistance in humans. Diabetes 60:1734-1742
    • (2011) Diabetes , vol.60 , pp. 1734-1742
    • Badin, P.M.1    Louche, K.2    Mairal, A.3
  • 236
    • 64649096897 scopus 로고    scopus 로고
    • Adipose overexpression of desnutrin promotes fatty acid use and attenuates diet-induced obesity
    • 2661591 1:CAS:528:DC%2BD1MXktleiurw%3D 19136649
    • Ahmadian M, Duncan RE, Varady KA et al (2009) Adipose overexpression of desnutrin promotes fatty acid use and attenuates diet-induced obesity. Diabetes 58:855-866
    • (2009) Diabetes , vol.58 , pp. 855-866
    • Ahmadian, M.1    Duncan, R.E.2    Varady, K.A.3
  • 237
    • 33748998746 scopus 로고    scopus 로고
    • Imaging diacylglycerol dynamics at organelle membranes
    • 1:CAS:528:DC%2BD28XpvVCmtLc%3D 16990811
    • Sato M, Ueda Y, Umezawa Y (2006) Imaging diacylglycerol dynamics at organelle membranes. Nat Methods 3:797-799
    • (2006) Nat Methods , vol.3 , pp. 797-799
    • Sato, M.1    Ueda, Y.2    Umezawa, Y.3
  • 238
    • 77954941774 scopus 로고    scopus 로고
    • Calcium transduces plasma membrane receptor signals to produce diacylglycerol at golgi membranes
    • 2906264 1:CAS:528:DC%2BC3cXovFenu7c%3D 20519514
    • Kunkel MT, Newton AC (2010) Calcium transduces plasma membrane receptor signals to produce diacylglycerol at golgi membranes. J Biol Chem 285:22748-22752
    • (2010) J Biol Chem , vol.285 , pp. 22748-22752
    • Kunkel, M.T.1    Newton, A.C.2
  • 239
    • 84881157822 scopus 로고    scopus 로고
    • Sphingomyelin regulates the transbilayer movement of diacylglycerol in the plasma membrane of Madin-Darby canine kidney cells
    • 1:CAS:528:DC%2BC3sXht1OgtLnJ 23682124
    • Ueda Y, Makino A, Murase-Tamada K et al (2013) Sphingomyelin regulates the transbilayer movement of diacylglycerol in the plasma membrane of Madin-Darby canine kidney cells. FASEB J 27:3284-3297
    • (2013) FASEB J , vol.27 , pp. 3284-3297
    • Ueda, Y.1    Makino, A.2    Murase-Tamada, K.3
  • 240
    • 0032497838 scopus 로고    scopus 로고
    • Diacylglycerol: When is it an intracellular messenger?
    • 1:CAS:528:DyaK1cXns1Klur4%3D
    • Wakelam MJO (1998) Diacylglycerol: when is it an intracellular messenger? Biochim Biophys Acta Mol Cell Biol Lipids 1436:117-126
    • (1998) Biochim Biophys Acta Mol Cell Biol Lipids , vol.1436 , pp. 117-126
    • Wakelam, M.J.O.1
  • 241
    • 68049083133 scopus 로고    scopus 로고
    • Bioactive Lipids
    • Nicolaou A, Kokotos G (eds)
    • Becker KB, Hannun YA (2012) Bioactive Lipids. In: Nicolaou A, Kokotos G (eds) Bioact Lipids. p 37-61
    • (2012) Bioact Lipids , pp. 37-61
    • Becker, K.B.1    Hannun, Y.A.2
  • 242
    • 33845962013 scopus 로고    scopus 로고
    • Diacylglycerol, when simplicity becomes complex
    • 1:CAS:528:DC%2BD2sXisVSqsg%3D%3D 17157506
    • Carrasco S, Mérida I (2007) Diacylglycerol, when simplicity becomes complex. Trends Biochem Sci 32:27-36
    • (2007) Trends Biochem Sci , vol.32 , pp. 27-36
    • Carrasco, S.1    Mérida, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.