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Volumn 53, Issue 6-8, 2008, Pages 382-388

Diacylglyceride lipase activity in rod outer segments depends on the illumination state of the retina

Author keywords

Diacylglyceride lipase; Diacylglycerol; Monoacylglycerol; Rod outer segments

Indexed keywords

CERAMIDE; CERAMIDE 1 PHOSPHATE; DIACYLGLYCEROL; LYSOPHOSPHATIDIC ACID; MONOACYLGLYCEROL; SPHINGOSINE; SPHINGOSINE 1 PHOSPHATE; TRIACYLGLYCEROL LIPASE;

EID: 56349116714     PISSN: 01970186     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuint.2008.09.007     Document Type: Article
Times cited : (8)

References (56)
  • 2
    • 0023111228 scopus 로고
    • A novel group of very long chain polyenoic fatty acids in dipolyunsaturated phosphatidylcholines from vertebrate retina
    • Aveldano M.I. A novel group of very long chain polyenoic fatty acids in dipolyunsaturated phosphatidylcholines from vertebrate retina. J. Biol. Chem. 262 (1987) 1172-1179
    • (1987) J. Biol. Chem. , vol.262 , pp. 1172-1179
    • Aveldano, M.I.1
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0023114097 scopus 로고
    • Diurnal expression of transducin mRNA and translocation of transducin in rods of rat retina
    • Brann M.R., and Cohen L.V. Diurnal expression of transducin mRNA and translocation of transducin in rods of rat retina. Science 235 (1987) 585-587
    • (1987) Science , vol.235 , pp. 585-587
    • Brann, M.R.1    Cohen, L.V.2
  • 6
    • 14844284989 scopus 로고    scopus 로고
    • Lipid phosphate phosphatases and related proteins: signaling functions in development, cell division, and cancer
    • Brindley D.N. Lipid phosphate phosphatases and related proteins: signaling functions in development, cell division, and cancer. J. Cell Biochem. 92 (2004) 900-912
    • (2004) J. Cell Biochem. , vol.92 , pp. 900-912
    • Brindley, D.N.1
  • 7
    • 0023090907 scopus 로고
    • Effect of light-adaptation on the binding of 48-kDa protein (S-antigen) to photoreceptor cell membranes
    • Broekhuyse R.M., Janssen A.P., and Tolhuizen E.F. Effect of light-adaptation on the binding of 48-kDa protein (S-antigen) to photoreceptor cell membranes. Curr. Eye Res. 6 (1987) 607-610
    • (1987) Curr. Eye Res. , vol.6 , pp. 607-610
    • Broekhuyse, R.M.1    Janssen, A.P.2    Tolhuizen, E.F.3
  • 8
    • 2942517752 scopus 로고    scopus 로고
    • Divergent and convergent signaling by the diacylglycerol second messenger pathway in mammals
    • Brose N., Betz A., and Wegmeyer H. Divergent and convergent signaling by the diacylglycerol second messenger pathway in mammals. Curr. Opin. Neurobiol. 14 (2004) 328-340
    • (2004) Curr. Opin. Neurobiol. , vol.14 , pp. 328-340
    • Brose, N.1    Betz, A.2    Wegmeyer, H.3
  • 9
    • 0034917522 scopus 로고    scopus 로고
    • Activation, deactivation, and adaptation in vertebrate photoreceptor cells
    • Burns M.E., and Baylor D.A. Activation, deactivation, and adaptation in vertebrate photoreceptor cells. Annu. Rev. Neurosci. 24 (2001) 779-805
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 779-805
    • Burns, M.E.1    Baylor, D.A.2
  • 10
    • 33845962013 scopus 로고    scopus 로고
    • Diacylglycerol, when simplicity becomes complex
    • Carrasco S., and Merida I. Diacylglycerol, when simplicity becomes complex. Trends Biochem. Sci. 32 (2007) 27-36
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 27-36
    • Carrasco, S.1    Merida, I.2
  • 11
    • 0027335535 scopus 로고
    • Properties of phospholipase A2 activity from bovine retinal rod outer segments
    • Castagnet P.I., and Giusto N.M. Properties of phospholipase A2 activity from bovine retinal rod outer segments. Exp. Eye Res. 56 (1993) 709-719
    • (1993) Exp. Eye Res. , vol.56 , pp. 709-719
    • Castagnet, P.I.1    Giusto, N.M.2
  • 12
    • 27844517355 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate and ceramide 1-phosphate: expanding roles in cell signaling
    • Chalfant C.E., and Spiegel S. Sphingosine 1-phosphate and ceramide 1-phosphate: expanding roles in cell signaling. J. Cell Sci. 118 (2005) 4605-4612
    • (2005) J. Cell Sci. , vol.118 , pp. 4605-4612
    • Chalfant, C.E.1    Spiegel, S.2
  • 14
    • 70449158340 scopus 로고
    • A simple method for the isolation and purification of total lipids from animal tissues
    • Folch J., Lees M., and Sloane Stanley G.H. A simple method for the isolation and purification of total lipids from animal tissues. J. Biol. Chem. 226 (1957) 497-509
    • (1957) J. Biol. Chem. , vol.226 , pp. 497-509
    • Folch, J.1    Lees, M.2    Sloane Stanley, G.H.3
  • 15
    • 0024579662 scopus 로고
    • Diacylglycerol modulates action potential frequency in GH3 pituitary cells: correlative biochemical and electrophysiological studies
    • Gammon C.M., Oxford G.S., Allen A.C., McCarthy K.D., and Morell P. Diacylglycerol modulates action potential frequency in GH3 pituitary cells: correlative biochemical and electrophysiological studies. Brain Res. 479 (1989) 217-224
    • (1989) Brain Res. , vol.479 , pp. 217-224
    • Gammon, C.M.1    Oxford, G.S.2    Allen, A.C.3    McCarthy, K.D.4    Morell, P.5
  • 17
    • 0026757772 scopus 로고
    • Activation of bovine rod outer segment phospholipase C by arrestin
    • Ghalayini A.J., and Anderson R.E. Activation of bovine rod outer segment phospholipase C by arrestin. J. Biol. Chem. 267 (1992) 17977-17982
    • (1992) J. Biol. Chem. , vol.267 , pp. 17977-17982
    • Ghalayini, A.J.1    Anderson, R.E.2
  • 18
    • 0018666105 scopus 로고
    • 2 production from [14C]glycerol in the bovine retina: the effects of incubation time, oxygen and glucose
    • 2 production from [14C]glycerol in the bovine retina: the effects of incubation time, oxygen and glucose. Exp. Eye Res. 29 (1979) 155-168
    • (1979) Exp. Eye Res. , vol.29 , pp. 155-168
    • Giusto, N.M.1    Bazan, N.G.2
  • 20
    • 0029101993 scopus 로고
    • Diacylglycerol analogs inhibit the rod cGMP-gated channel by a phosphorylation-independent mechanism
    • Gordon S.E., Downing-Park J., Tam B., and Zimmerman A.L. Diacylglycerol analogs inhibit the rod cGMP-gated channel by a phosphorylation-independent mechanism. Biophys. J. 69 (1995) 409-417
    • (1995) Biophys. J. , vol.69 , pp. 409-417
    • Gordon, S.E.1    Downing-Park, J.2    Tam, B.3    Zimmerman, A.L.4
  • 21
    • 0036893646 scopus 로고    scopus 로고
    • The phospholipids sphingosine-1-phosphate and lysophosphatidic acid prevent apoptosis in osteoblastic cells via a signaling pathway involving G(i) proteins and phosphatidylinositol-3 kinase
    • Grey A., Chen Q., Callon K., Xu X., Reid I.R., and Cornish J. The phospholipids sphingosine-1-phosphate and lysophosphatidic acid prevent apoptosis in osteoblastic cells via a signaling pathway involving G(i) proteins and phosphatidylinositol-3 kinase. Endocrinology 143 (2002) 4755-4763
    • (2002) Endocrinology , vol.143 , pp. 4755-4763
    • Grey, A.1    Chen, Q.2    Callon, K.3    Xu, X.4    Reid, I.R.5    Cornish, J.6
  • 22
    • 0030758287 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase in bovine photoreceptor rod outer segments
    • Guo X., Ghalayini A.J., Chen H., and Anderson R.E. Phosphatidylinositol 3-kinase in bovine photoreceptor rod outer segments. Invest. Ophthalmol. Vis. Sci. 38 (1997) 1873-1882
    • (1997) Invest. Ophthalmol. Vis. Sci. , vol.38 , pp. 1873-1882
    • Guo, X.1    Ghalayini, A.J.2    Chen, H.3    Anderson, R.E.4
  • 23
    • 0037135626 scopus 로고    scopus 로고
    • The Ceramide-centric universe of lipid-mediated cell regulation: stress encounters of the lipid kind
    • Hannun Y.A., and Obeid L.M. The Ceramide-centric universe of lipid-mediated cell regulation: stress encounters of the lipid kind. J. Biol. Chem. 277 (2002) 25847-25850
    • (2002) J. Biol. Chem. , vol.277 , pp. 25847-25850
    • Hannun, Y.A.1    Obeid, L.M.2
  • 24
    • 0016368896 scopus 로고
    • Purification of a plasma membrane-bound adenosine triphosphatase from plant roots
    • Hodges T.K., and Leonard R.T. Purification of a plasma membrane-bound adenosine triphosphatase from plant roots. Methods Enzymol. 32 (1974) 392-406
    • (1974) Methods Enzymol. , vol.32 , pp. 392-406
    • Hodges, T.K.1    Leonard, R.T.2
  • 25
    • 0032496366 scopus 로고    scopus 로고
    • Identification of a novel human phosphatidic acid phosphatase type 2 isoform
    • Hooks S.B., Ragan S.P., and Lynch K.R. Identification of a novel human phosphatidic acid phosphatase type 2 isoform. FEBS Lett. 427 (1998) 188-192
    • (1998) FEBS Lett. , vol.427 , pp. 188-192
    • Hooks, S.B.1    Ragan, S.P.2    Lynch, K.R.3
  • 26
    • 0034131372 scopus 로고    scopus 로고
    • Light-mediated activation of diacylglycerol kinase in rat and bovine rod outer segments
    • Huang Z., Ghalayini A., Guo X.X., Alvarez K.M., and Anderson R.E. Light-mediated activation of diacylglycerol kinase in rat and bovine rod outer segments. J. Neurochem. 75 (2000) 355-362
    • (2000) J. Neurochem. , vol.75 , pp. 355-362
    • Huang, Z.1    Ghalayini, A.2    Guo, X.X.3    Alvarez, K.M.4    Anderson, R.E.5
  • 27
    • 4344684533 scopus 로고    scopus 로고
    • Different expression strategy: multiple intronic gene clusters of box H/ACA snoRNA in Drosophila melanogaster
    • Huang Z.P., Zhou H., Liang D., and Qu L.H. Different expression strategy: multiple intronic gene clusters of box H/ACA snoRNA in Drosophila melanogaster. J. Mol. Biol. 341 (2004) 669-683
    • (2004) J. Mol. Biol. , vol.341 , pp. 669-683
    • Huang, Z.P.1    Zhou, H.2    Liang, D.3    Qu, L.H.4
  • 28
    • 0025268427 scopus 로고
    • Diacylglycerol generated in the phospholipid vesicles by phospholipase C is effectively utilized by diacylglycerol lipase in rat liver cytosol
    • Ide H., Koyama S., and Nakazawa Y. Diacylglycerol generated in the phospholipid vesicles by phospholipase C is effectively utilized by diacylglycerol lipase in rat liver cytosol. Biochim. Biophys. Acta 1044 (1990) 179-186
    • (1990) Biochim. Biophys. Acta , vol.1044 , pp. 179-186
    • Ide, H.1    Koyama, S.2    Nakazawa, Y.3
  • 30
    • 28844501202 scopus 로고    scopus 로고
    • Transducin activation state controls its light-dependent translocation in rod photoreceptors
    • Kerov V., Chen D., Moussaif M., Chen Y.J., Chen C.K., and Artemyev N.O. Transducin activation state controls its light-dependent translocation in rod photoreceptors. J. Biol. Chem. 280 (2005) 41069-41076
    • (2005) J. Biol. Chem. , vol.280 , pp. 41069-41076
    • Kerov, V.1    Chen, D.2    Moussaif, M.3    Chen, Y.J.4    Chen, C.K.5    Artemyev, N.O.6
  • 31
    • 0020018797 scopus 로고
    • Light-regulated binding of proteins to photoreceptor membranes and its use for the purification of several rod cell proteins
    • Kuhn H. Light-regulated binding of proteins to photoreceptor membranes and its use for the purification of several rod cell proteins. Methods Enzymol. 81 (1982) 556-564
    • (1982) Methods Enzymol. , vol.81 , pp. 556-564
    • Kuhn, H.1
  • 32
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 0033784615 scopus 로고    scopus 로고
    • Protein machines and lipid assemblies: current views of cell membrane fusion
    • Lentz B.R., Malinin V., Haque M.E., and Evans K. Protein machines and lipid assemblies: current views of cell membrane fusion. Curr. Opin. Struct. Biol. 10 (2000) 607-615
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 607-615
    • Lentz, B.R.1    Malinin, V.2    Haque, M.E.3    Evans, K.4
  • 34
    • 33645997388 scopus 로고    scopus 로고
    • Insights on TRP channels from in vivo studies in Drosophila
    • Minke B., and Parnas M. Insights on TRP channels from in vivo studies in Drosophila. Annu. Rev. Physiol. 68 (2006) 649-684
    • (2006) Annu. Rev. Physiol. , vol.68 , pp. 649-684
    • Minke, B.1    Parnas, M.2
  • 35
    • 0021918091 scopus 로고
    • Phosphorylation, transbilayer movement, and facilitated intracellular transport of diacylglycerol are involved in the uptake of a fluorescent analog of phosphatidic acid by cultured fibroblasts
    • Pagano R.E., and Longmuir K.J. Phosphorylation, transbilayer movement, and facilitated intracellular transport of diacylglycerol are involved in the uptake of a fluorescent analog of phosphatidic acid by cultured fibroblasts. J. Biol. Chem. 260 (1985) 1909-1916
    • (1985) J. Biol. Chem. , vol.260 , pp. 1909-1916
    • Pagano, R.E.1    Longmuir, K.J.2
  • 36
    • 0022571825 scopus 로고
    • Phosphatidate phosphatase activity in isolated rod outer segment from bovine retina
    • Pasquare de Garcia S.J., and Giusto N.M. Phosphatidate phosphatase activity in isolated rod outer segment from bovine retina. Biochim. Biophys. Acta 875 (1986) 195-202
    • (1986) Biochim. Biophys. Acta , vol.875 , pp. 195-202
    • Pasquare de Garcia, S.J.1    Giusto, N.M.2
  • 37
    • 0027458961 scopus 로고
    • Differential properties of phosphatidate phosphohydrolase and diacylglyceride lipase activities in retinal subcellular fractions and rod outer segments
    • Pasquare S.J., and Giusto N.M. Differential properties of phosphatidate phosphohydrolase and diacylglyceride lipase activities in retinal subcellular fractions and rod outer segments. Comp. Biochem. Physiol. B 104 (1993) 141-148
    • (1993) Comp. Biochem. Physiol. B , vol.104 , pp. 141-148
    • Pasquare, S.J.1    Giusto, N.M.2
  • 38
    • 44549086416 scopus 로고    scopus 로고
    • Involvement of lysophosphatidic acid, sphingosine 1-phosphate and ceramide 1-phosphate in the metabolization of phosphatidic acid by lipid phosphate phosphatases in bovine rod outer segments
    • Pasquare S.J., Salvador G.A., and Giusto N.M. Involvement of lysophosphatidic acid, sphingosine 1-phosphate and ceramide 1-phosphate in the metabolization of phosphatidic acid by lipid phosphate phosphatases in bovine rod outer segments. Neurochem. Res. 33 (2008) 1205-1215
    • (2008) Neurochem. Res. , vol.33 , pp. 1205-1215
    • Pasquare, S.J.1    Salvador, G.A.2    Giusto, N.M.3
  • 39
    • 0034661394 scopus 로고    scopus 로고
    • Effect of light on phosphatidate phosphohydrolase activity of retina rod outer segments: the role of transducin
    • Pasquare S.J., Salvador G.A., Roque M.E., and Giusto N.M. Effect of light on phosphatidate phosphohydrolase activity of retina rod outer segments: the role of transducin. Arch. Biochem. Biophys. 379 (2000) 299-306
    • (2000) Arch. Biochem. Biophys. , vol.379 , pp. 299-306
    • Pasquare, S.J.1    Salvador, G.A.2    Roque, M.E.3    Giusto, N.M.4
  • 40
    • 0031936890 scopus 로고    scopus 로고
    • Can phosphorylation and dephosphorylation of rod outer segment membranes affect phosphatidate phosphohydrolase and diacylglycerol lipase activities?
    • Perez Roque M.E., Pasquare S.J., Castagnet P.I., and Giusto N.M. Can phosphorylation and dephosphorylation of rod outer segment membranes affect phosphatidate phosphohydrolase and diacylglycerol lipase activities?. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 119 (1998) 85-93
    • (1998) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.119 , pp. 85-93
    • Perez Roque, M.E.1    Pasquare, S.J.2    Castagnet, P.I.3    Giusto, N.M.4
  • 41
    • 0023650261 scopus 로고
    • Light-stimulated protein movement in rod photoreceptor cells of the rat retina
    • Philp N.J., Chang W., and Long K. Light-stimulated protein movement in rod photoreceptor cells of the rat retina. FEBS Lett. 225 (1987) 127-132
    • (1987) FEBS Lett. , vol.225 , pp. 127-132
    • Philp, N.J.1    Chang, W.2    Long, K.3
  • 42
    • 28844452498 scopus 로고    scopus 로고
    • Lipid phosphate phosphatases and lipid phosphate signalling
    • Pyne S., Long J.S., Ktistakis N.T., and Pyne N.J. Lipid phosphate phosphatases and lipid phosphate signalling. Biochem. Soc. Trans. 33 (2005) 1370-1374
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 1370-1374
    • Pyne, S.1    Long, J.S.2    Ktistakis, N.T.3    Pyne, N.J.4
  • 43
    • 0037044798 scopus 로고    scopus 로고
    • In vivo regulation of phosphoinositide 3-kinase in retina through light-induced tyrosine phosphorylation of the insulin receptor beta-subunit
    • Rajala R.V., McClellan M.E., Ash J.D., and Anderson R.E. In vivo regulation of phosphoinositide 3-kinase in retina through light-induced tyrosine phosphorylation of the insulin receptor beta-subunit. J. Biol. Chem. 277 (2002) 43319-43326
    • (2002) J. Biol. Chem. , vol.277 , pp. 43319-43326
    • Rajala, R.V.1    McClellan, M.E.2    Ash, J.D.3    Anderson, R.E.4
  • 44
    • 0032555608 scopus 로고    scopus 로고
    • Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform
    • Roberts R., Sciorra V.A., and Morris A.J. Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform. J. Biol. Chem. 273 (1998) 22059-22067
    • (1998) J. Biol. Chem. , vol.273 , pp. 22059-22067
    • Roberts, R.1    Sciorra, V.A.2    Morris, A.J.3
  • 45
    • 0029058254 scopus 로고
    • Phosphatidylethanolamine N-methyltransferase activity in isolated rod outer segments from bovine retina
    • Roque M.E., and Giusto N.M. Phosphatidylethanolamine N-methyltransferase activity in isolated rod outer segments from bovine retina. Exp. Eye Res. 60 (1995) 631-643
    • (1995) Exp. Eye Res. , vol.60 , pp. 631-643
    • Roque, M.E.1    Giusto, N.M.2
  • 46
    • 0032754777 scopus 로고    scopus 로고
    • Light activation of phosphatidylethanolamine N-methyltransferase in rod outer segments and its modulation by association states of transducin
    • Roque M.E., Salvador G.A., and Giusto N.M. Light activation of phosphatidylethanolamine N-methyltransferase in rod outer segments and its modulation by association states of transducin. Exp. Eye Res. 69 (1999) 555-562
    • (1999) Exp. Eye Res. , vol.69 , pp. 555-562
    • Roque, M.E.1    Salvador, G.A.2    Giusto, N.M.3
  • 47
    • 34247550248 scopus 로고    scopus 로고
    • Bovine brain diacylglycerol lipase: substrate specificity and activation by cyclic AMP-dependent protein kinase
    • Rosenberger T.A., Farooqui A.A., and Horrocks L.A. Bovine brain diacylglycerol lipase: substrate specificity and activation by cyclic AMP-dependent protein kinase. Lipids 42 (2007) 187-195
    • (2007) Lipids , vol.42 , pp. 187-195
    • Rosenberger, T.A.1    Farooqui, A.A.2    Horrocks, L.A.3
  • 48
    • 0014779155 scopus 로고
    • Two dimensional then layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots
    • Rouser G., Fkeischer S., and Yamamoto A. Two dimensional then layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots. Lipids 5 (1970) 494-496
    • (1970) Lipids , vol.5 , pp. 494-496
    • Rouser, G.1    Fkeischer, S.2    Yamamoto, A.3
  • 49
    • 33646879410 scopus 로고    scopus 로고
    • Phospholipase D from photoreceptor rod outer segments is a downstream effector of RhoA: evidence of a light-dependent mechanism
    • Salvador G.A., and Giusto N.M. Phospholipase D from photoreceptor rod outer segments is a downstream effector of RhoA: evidence of a light-dependent mechanism. Exp. Eye Res. 83 (2006) 202-211
    • (2006) Exp. Eye Res. , vol.83 , pp. 202-211
    • Salvador, G.A.1    Giusto, N.M.2
  • 51
    • 0037187644 scopus 로고    scopus 로고
    • Massive light-driven translocation of transducin between the two major compartments of rod cells: a novel mechanism of light adaptation
    • Sokolov M., Lyubarsky A.L., Strissel K.J., Savchenko A.B., Govardovskii V.I., Pugh Jr. E.N., and Arshavsky V.Y. Massive light-driven translocation of transducin between the two major compartments of rod cells: a novel mechanism of light adaptation. Neuron 34 (2002) 95-106
    • (2002) Neuron , vol.34 , pp. 95-106
    • Sokolov, M.1    Lyubarsky, A.L.2    Strissel, K.J.3    Savchenko, A.B.4    Govardovskii, V.I.5    Pugh Jr., E.N.6    Arshavsky, V.Y.7
  • 53
    • 0036019386 scopus 로고    scopus 로고
    • Biosynthesis and degradation of anandamide and 2-arachidonoylglycerol and their possible physiological significance
    • Sugiura T., Kobayashi Y., Oka S., and Waku K. Biosynthesis and degradation of anandamide and 2-arachidonoylglycerol and their possible physiological significance. Prostaglandins Leukot. Essent. Fatty Acids 66 (2002) 173-192
    • (2002) Prostaglandins Leukot. Essent. Fatty Acids , vol.66 , pp. 173-192
    • Sugiura, T.1    Kobayashi, Y.2    Oka, S.3    Waku, K.4
  • 54
    • 0023697234 scopus 로고
    • Light-dependent subcellular movement of photoreceptor proteins
    • Whelan J.P., and McGinnis J.F. Light-dependent subcellular movement of photoreceptor proteins. J. Neurosci. Res. 20 (1988) 263-270
    • (1988) J. Neurosci. Res. , vol.20 , pp. 263-270
    • Whelan, J.P.1    McGinnis, J.F.2
  • 55
    • 0242321186 scopus 로고    scopus 로고
    • Divergence and complexities in DAG signaling: looking beyond PKC
    • Yang C., and Kazanietz M.G. Divergence and complexities in DAG signaling: looking beyond PKC. Trends Pharmacol. Sci. 24 (2003) 602-608
    • (2003) Trends Pharmacol. Sci. , vol.24 , pp. 602-608
    • Yang, C.1    Kazanietz, M.G.2
  • 56
    • 33646932964 scopus 로고    scopus 로고
    • Localization of diacylglycerol lipase-alpha around postsynaptic spine suggests close proximity between production site of an endocannabinoid, 2-arachidonoyl-glycerol, and presynaptic cannabinoid CB1 receptor
    • Yoshida T., Fukaya M., Uchigashima M., Miura E., Kamiya H., Kano M., and Watanabe M. Localization of diacylglycerol lipase-alpha around postsynaptic spine suggests close proximity between production site of an endocannabinoid, 2-arachidonoyl-glycerol, and presynaptic cannabinoid CB1 receptor. J. Neurosci. 26 (2006) 4740-4751
    • (2006) J. Neurosci. , vol.26 , pp. 4740-4751
    • Yoshida, T.1    Fukaya, M.2    Uchigashima, M.3    Miura, E.4    Kamiya, H.5    Kano, M.6    Watanabe, M.7


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