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Volumn 46, Issue 12, 2005, Pages 2706-2716

Substrate specificity of human ceramide kinase

Author keywords

Arachidonic acid; Ceramide 1 phosphate; Inflammation; Phospholipase A2; Prostaglandins

Indexed keywords

CERAMIDE 1 PHOSPHATE; CERAMIDE 3 PHOSPHATE; CERAMIDE DERIVATIVE; CERAMIDE KINASE; DIACYLGLYCEROL; HYDROGEN; HYDROXYL GROUP; PHOSPHOTRANSFERASE; SATURATED FATTY ACID; SPHINGOSINE; TRITON X 100; UNCLASSIFIED DRUG; UNSATURATED FATTY ACID;

EID: 30344439710     PISSN: 00222275     EISSN: 15397262     Source Type: Journal    
DOI: 10.1194/jlr.M500313-JLR200     Document Type: Article
Times cited : (63)

References (59)
  • 1
    • 0022974603 scopus 로고
    • Sphingosine inhibition of protein kinase C activity and of phorbol dibutyrate binding in vitro and in human platelets
    • Hannun, Y. A., C. R. Loomis, A. H. Merrill, Jr., and R. M. Bell. 1986. Sphingosine inhibition of protein kinase C activity and of phorbol dibutyrate binding in vitro and in human platelets. J. Biol. Chem. 261: 12604-12609.
    • (1986) J. Biol. Chem. , vol.261 , pp. 12604-12609
    • Hannun, Y.A.1    Loomis, C.R.2    Merrill Jr., A.H.3    Bell, R.M.4
  • 2
    • 0024795059 scopus 로고
    • Sphingomyelin turnover induced by vitamin D3 in HL-60 cells. Role in cell differentiation
    • Okazaki, T., R. M. Bell, and Y. A. Hannun. 1989. Sphingomyelin turnover induced by vitamin D3 in HL-60 cells. Role in cell differentiation. J. Biol. Chem. 264: 19076-19080.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19076-19080
    • Okazaki, T.1    Bell, R.M.2    Hannun, Y.A.3
  • 3
    • 0025889011 scopus 로고
    • Characterization of a ceramide-activated protein kinase: Stimulation by tumor necrosis factor alpha
    • Mathias, S., K. A. Dressler, and R. N. Kolesnick. 1991. Characterization of a ceramide-activated protein kinase: stimulation by tumor necrosis factor alpha. Proc. Natl. Acad. Sci. USA. 88: 10009-10013.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10009-10013
    • Mathias, S.1    Dressler, K.A.2    Kolesnick, R.N.3
  • 4
    • 0026560014 scopus 로고
    • Tumor necrosis factor-alpha activates the sphingomyelin signal transduction pathway in a cell-free system
    • Dressler, K. A., S. Mathias, and R. N. Kolesnick. 1992. Tumor necrosis factor-alpha activates the sphingomyelin signal transduction pathway in a cell-free system. Science. 255: 1715-1718.
    • (1992) Science , vol.255 , pp. 1715-1718
    • Dressler, K.A.1    Mathias, S.2    Kolesnick, R.N.3
  • 5
    • 0027994349 scopus 로고
    • The sphingomyelin cycle and the second messenger function of ceramide
    • Hannun, Y. A. 1994. The sphingomyelin cycle and the second messenger function of ceramide. J. Biol. Chem. 269: 3125-3128.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3125-3128
    • Hannun, Y.A.1
  • 6
    • 0028855405 scopus 로고
    • Ceramide: An intracellular signal for apoptosis
    • Hannun, Y. A., and L. M. Obeid. 1995. Ceramide: an intracellular signal for apoptosis. Trends Biochem. Sci. 20: 73-77.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 73-77
    • Hannun, Y.A.1    Obeid, L.M.2
  • 7
    • 0028297068 scopus 로고
    • The sphingomyelin pathway in tumor necrosis factor and interleukin-1 signaling
    • Kolesnick, R., and D. W. Golde. 1994. The sphingomyelin pathway in tumor necrosis factor and interleukin-1 signaling. Cell. 77: 325-328.
    • (1994) Cell , vol.77 , pp. 325-328
    • Kolesnick, R.1    Golde, D.W.2
  • 9
    • 0032489435 scopus 로고    scopus 로고
    • Modulation of cell signalling by ceramides
    • Gomez-Munoz, A. 1998. Modulation of cell signalling by ceramides. Biochim. Biophys. Acta. 1391: 92-109.
    • (1998) Biochim. Biophys. Acta , vol.1391 , pp. 92-109
    • Gomez-Munoz, A.1
  • 10
    • 0025185675 scopus 로고
    • Characterization of a ceramide kinase activity from human leukemia (HL-60) cells. Separation from diacylglycerol kinase activity
    • Kolesnick, R. N., and M. R. Hemer. 1990. Characterization of a ceramide kinase activity from human leukemia (HL-60) cells. Separation from diacylglycerol kinase activity. J. Biol. Chem. 265: 18803-18808.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18803-18808
    • Kolesnick, R.N.1    Hemer, M.R.2
  • 11
    • 0027428283 scopus 로고
    • Ceramide-activated protein phosphatase: Partial purification and relationship to protein phosphatase 2A
    • Dobrowsky, R. T., and Y. A. Hannun. 1993. Ceramide-activated protein phosphatase: partial purification and relationship to protein phosphatase 2A. Adv. Lipid Res. 25: 91-104.
    • (1993) Adv. Lipid Res. , vol.25 , pp. 91-104
    • Dobrowsky, R.T.1    Hannun, Y.A.2
  • 12
    • 0027965006 scopus 로고
    • Protein kinase C zeta isoform is critical for kappa B-dependent promoter activation by sphingomyelinase
    • Lozano, J., E. Berra, M. M. Municio, M. T. Diaz-Meco, I. Dominguez, L. Sanz, and J. Moscat. 1994. Protein kinase C zeta isoform is critical for kappa B-dependent promoter activation by sphingomyelinase. J. Biol. Chem. 269: 19200-19202.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19200-19202
    • Lozano, J.1    Berra, E.2    Municio, M.M.3    Diaz-Meco, M.T.4    Dominguez, I.5    Sanz, L.6    Moscat, J.7
  • 15
    • 0028838235 scopus 로고
    • Phosphorylation of Raf by ceramide-activated protein kinase
    • Yao, B., Y. Zhang, S. Delikat, S. Mathias, S. Basu, and R. Kolesnick. 1995. Phosphorylation of Raf by ceramide-activated protein kinase. Nature. 378: 307-310.
    • (1995) Nature , vol.378 , pp. 307-310
    • Yao, B.1    Zhang, Y.2    Delikat, S.3    Mathias, S.4    Basu, S.5    Kolesnick, R.6
  • 16
    • 0029996139 scopus 로고    scopus 로고
    • Signal transduction through lipid second messengers
    • Spiegel, S., D. Foster, and R. Kolesnick. 1996. Signal transduction through lipid second messengers. Curr. Opin. Cell Biol. 8: 159-167.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 159-167
    • Spiegel, S.1    Foster, D.2    Kolesnick, R.3
  • 17
    • 0029890361 scopus 로고    scopus 로고
    • Role of ceramide in stimulation of the transcription of cytosolic phospholipase A2 and cyclooxygenase 2
    • Hayakawa, M., S. Jayadev, M. Tsujimoto, Y. A. Hannun, and F. Ito. 1996. Role of ceramide in stimulation of the transcription of cytosolic phospholipase A2 and cyclooxygenase 2. Biochem. Biophys. Res. Commun. 220: 681-686.
    • (1996) Biochem. Biophys. Res. Commun. , vol.220 , pp. 681-686
    • Hayakawa, M.1    Jayadev, S.2    Tsujimoto, M.3    Hannun, Y.A.4    Ito, F.5
  • 18
    • 0028825719 scopus 로고
    • Interaction of ceramides, sphingosine, and sphingosine 1-phosphate in regulating DNA synthesis and phospholipase D activity
    • Gomez-Munoz, A., D. W. Waggoner, L. O'Brien, and D. N. Brindley. 1995. Interaction of ceramides, sphingosine, and sphingosine 1-phosphate in regulating DNA synthesis and phospholipase D activity. J. Biol. Chem. 270: 26318-26325.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26318-26325
    • Gomez-Munoz, A.1    Waggoner, D.W.2    O'Brien, L.3    Brindley, D.N.4
  • 19
    • 0028339322 scopus 로고
    • Cell-permeable ceramides inhibit the stimulation of DNA synthesis and phospholipase D activity by phosphatidate and lysophosphatidate in rat fibroblasts
    • Gomez-Munoz, A., A. Martin, L. O'Brien, and D. N. Brindley. 1994. Cell-permeable ceramides inhibit the stimulation of DNA synthesis and phospholipase D activity by phosphatidate and lysophosphatidate in rat fibroblasts. J. Biol. Chem. 269: 8937-8943.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8937-8943
    • Gomez-Munoz, A.1    Martin, A.2    O'Brien, L.3    Brindley, D.N.4
  • 20
    • 0036479251 scopus 로고    scopus 로고
    • Ceramide-induced inhibition of Akt is mediated through protein kinase Czeta: Implications for growth arrest
    • Bourbon, N. A., L. Sandirasegarane, and M. Kester. 2002. Ceramide-induced inhibition of Akt is mediated through protein kinase Czeta: implications for growth arrest. J. Biol. Chem. 277: 3286-3292.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3286-3292
    • Bourbon, N.A.1    Sandirasegarane, L.2    Kester, M.3
  • 21
    • 0034607914 scopus 로고    scopus 로고
    • Ceramide inhibits protein kinase B/Akt by promoting dephosphorylation of serine 473
    • Schubert, K. M., M. P. Scheid, and V. Duronio. 2000. Ceramide inhibits protein kinase B/Akt by promoting dephosphorylation of serine 473. J. Biol. Chem. 275: 13330-13335.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13330-13335
    • Schubert, K.M.1    Scheid, M.P.2    Duronio, V.3
  • 22
    • 0024373904 scopus 로고
    • Synaptic vesicle ceramide kinase. A calcium-stimulated lipid kinase that co-purifies with brain synaptic vesicles
    • Bajjalieh, S. M., T. F. Martin, and E. Floor. 1989. Synaptic vesicle ceramide kinase. A calcium-stimulated lipid kinase that co-purifies with brain synaptic vesicles. J. Biol. Chem. 264: 14354-14360.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14354-14360
    • Bajjalieh, S.M.1    Martin, T.F.2    Floor, E.3
  • 23
    • 0037189475 scopus 로고    scopus 로고
    • Ceramide kinase, a novel lipid kinase. Molecular cloning and functional characterization
    • Sugiura, M., K. Kono, H. Liu, T. Shimizugawa, H. Minekura, S. Spiegel, and T. Kohama. 2002. Ceramide kinase, a novel lipid kinase. Molecular cloning and functional characterization. J. Biol. Chem. 277: 23294-23300.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23294-23300
    • Sugiura, M.1    Kono, K.2    Liu, H.3    Shimizugawa, T.4    Minekura, H.5    Spiegel, S.6    Kohama, T.7
  • 24
    • 0025168334 scopus 로고
    • Ceramide 1-phosphate, a novel phospholipid in human leukemia (HL-60) cells. Synthesis via ceramide from sphingomyelin
    • Dressler, K. A., and R. N. Kolesnick. 1990. Ceramide 1-phosphate, a novel phospholipid in human leukemia (HL-60) cells. Synthesis via ceramide from sphingomyelin. J. Biol. Chem. 265: 14917-14921.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14917-14921
    • Dressler, K.A.1    Kolesnick, R.N.2
  • 25
  • 26
    • 0037219462 scopus 로고    scopus 로고
    • Ceramide 1-phosphate formation in neutrophils
    • Rile, G., Y. Yatomi, T. Takafuta, and Y. Ozaki. 2003. Ceramide 1-phosphate formation in neutrophils. Acta Haematol. 109: 76-83.
    • (2003) Acta Haematol. , vol.109 , pp. 76-83
    • Rile, G.1    Yatomi, Y.2    Takafuta, T.3    Ozaki, Y.4
  • 27
    • 0036695440 scopus 로고    scopus 로고
    • Metabolic formation of ceramide-1-phosphate in cerebellar granule cells: Evidence for the phosphorylation of ceramide by different metabolic pathways
    • Riboni, L., R. Bassi, V. Anelli, and P. Viani. 2002. Metabolic formation of ceramide-1-phosphate in cerebellar granule cells: evidence for the phosphorylation of ceramide by different metabolic pathways. Neurochem. Res. 27: 711-716.
    • (2002) Neurochem. Res. , vol.27 , pp. 711-716
    • Riboni, L.1    Bassi, R.2    Anelli, V.3    Viani, P.4
  • 28
    • 0141755365 scopus 로고    scopus 로고
    • Ceramide kinase mediates cytokine- And calcium ionophore-induced arachidonic acid release
    • Pettus, B. J., A. Bielawska, S. Spiegel, P. Roddy, Y. A. Hannun, and C. E. Chalfant. 2003. Ceramide kinase mediates cytokine- and calcium ionophore-induced arachidonic acid release. J. Biol. Chem. 278: 38206-38213.
    • (2003) J. Biol. Chem. , vol.278 , pp. 38206-38213
    • Pettus, B.J.1    Bielawska, A.2    Spiegel, S.3    Roddy, P.4    Hannun, Y.A.5    Chalfant, C.E.6
  • 29
    • 0029014026 scopus 로고
    • Short-chain ceramide-1-phosphates are novel stimulators of DNA synthesis and cell division: Antagonism by cell-permeable ceramides
    • Gomez-Munoz, A., P. A. Duffy, A. Martin, L. O'Brien, H. S. Byun, R. Bittman, and D. N. Brindley. 1995. Short-chain ceramide-1-phosphates are novel stimulators of DNA synthesis and cell division: antagonism by cell-permeable ceramides. Mol. Pharmacol. 47: 833-839.
    • (1995) Mol. Pharmacol. , vol.47 , pp. 833-839
    • Gomez-Munoz, A.1    Duffy, P.A.2    Martin, A.3    O'Brien, L.4    Byun, H.S.5    Bittman, R.6    Brindley, D.N.7
  • 30
    • 0842282983 scopus 로고    scopus 로고
    • Ceramide-1-phosphate blocks apoptosis through inhibition of acid sphingomyelinase in macrophages
    • Gomez-Munoz, A., J. Y. Kong, B. Salh, and U. P. Steinbrecher. 2004. Ceramide-1-phosphate blocks apoptosis through inhibition of acid sphingomyelinase in macrophages. J. Lipid Res. 45: 99-105.
    • (2004) J. Lipid Res. , vol.45 , pp. 99-105
    • Gomez-Munoz, A.1    Kong, J.Y.2    Salh, B.3    Steinbrecher, U.P.4
  • 33
    • 20444371635 scopus 로고    scopus 로고
    • Ceramide 1-phosphate acts as a positive allosteric activator of group IVA cytosolic phospholipase A2alpha and enhances the interaction of the enzyme with phosphatidylcholine
    • Subramanian, P., R. V. Stahelin, Z. Szulc, A. Bielawska, W. Cho, and C. E. Chalfant. 2005. Ceramide 1-phosphate acts as a positive allosteric activator of group IVA cytosolic phospholipase A2alpha and enhances the interaction of the enzyme with phosphatidylcholine. J. Biol. Chem. 280: 17601-17607.
    • (2005) J. Biol. Chem. , vol.280 , pp. 17601-17607
    • Subramanian, P.1    Stahelin, R.V.2    Szulc, Z.3    Bielawska, A.4    Cho, W.5    Chalfant, C.E.6
  • 34
    • 0035859939 scopus 로고    scopus 로고
    • Structural requirements of ceramide and sphingosine based inhibitors of mitochondrial ceramidase
    • Usta, J., S. El Bawab, P. Roddy, Z. M. Szulc, Yusuf, A. Hannun, and A. Bielawska. 2001. Structural requirements of ceramide and sphingosine based inhibitors of mitochondrial ceramidase. Biochemistry. 40: 9657-9668.
    • (2001) Biochemistry , vol.40 , pp. 9657-9668
    • Usta, J.1    El Bawab, S.2    Roddy, P.3    Szulc, Z.M.4    Yusuf5    Hannun, A.6    Bielawska, A.7
  • 35
    • 1542723736 scopus 로고    scopus 로고
    • The structural requirements for ceramide activation of serine-threonine protein phosphatases
    • Chalfant, C. E., Z. Szulc, P. Roddy, A. Bielawska, and Y. A. Hannun. 2004. The structural requirements for ceramide activation of serine-threonine protein phosphatases. J. Lipid Res. 45: 496-506.
    • (2004) J. Lipid Res. , vol.45 , pp. 496-506
    • Chalfant, C.E.1    Szulc, Z.2    Roddy, P.3    Bielawska, A.4    Hannun, Y.A.5
  • 36
    • 0027527545 scopus 로고
    • Selectivity of ceramide-mediated biology. Lack of activity of erythro-dihydroceramide
    • Bielawska, A., H. M. Crane, D. Liotta, L. M. Obeid, and Y. A. Hannun. 1993. Selectivity of ceramide-mediated biology. Lack of activity of erythro-dihydroceramide. J. Biol. Chem. 268: 26226-26232.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26226-26232
    • Bielawska, A.1    Crane, H.M.2    Liotta, D.3    Obeid, L.M.4    Hannun, Y.A.5
  • 37
    • 0023838180 scopus 로고
    • Synthesis of D-erythro and D-threo sphingosine derivatives from L-serine
    • Herold, P. E. 1988. Synthesis of D-erythro and D-threo sphingosine derivatives from L-serine. J. Org. Chem. 71: 354-362.
    • (1988) J. Org. Chem. , vol.71 , pp. 354-362
    • Herold, P.E.1
  • 38
    • 0142103304 scopus 로고    scopus 로고
    • Mechanism of group IVA cytosolic phospholipase A(2) activation by phosphorylation
    • Das, S., J. D. Rafter, K. P. Kim, S. P. Gygi, and W. Cho. 2003. Mechanism of group IVA cytosolic phospholipase A(2) activation by phosphorylation. J. Biol. Chem. 278: 41431-41442.
    • (2003) J. Biol. Chem. , vol.278 , pp. 41431-41442
    • Das, S.1    Rafter, J.D.2    Kim, K.P.3    Gygi, S.P.4    Cho, W.5
  • 39
    • 0033515664 scopus 로고    scopus 로고
    • A structure-function study of the C2 domain of cytosolic phospholipase A2. Identification of essential calcium ligands and hydrophobic membrane binding residues
    • Bittova, L., M. Sumandea, and W. Cho. 1999. A structure-function study of the C2 domain of cytosolic phospholipase A2. Identification of essential calcium ligands and hydrophobic membrane binding residues. J. Biol. Chem. 274: 9665-9672.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9665-9672
    • Bittova, L.1    Sumandea, M.2    Cho, W.3
  • 40
    • 0043123256 scopus 로고    scopus 로고
    • A specific ceramide kinase assay to measure cellular levels of ceramide
    • Bektas, M., P. S. Jolly, S. Milstien, and S. Spiegel. 2003. A specific ceramide kinase assay to measure cellular levels of ceramide. Anal. Biochem. 320: 259-265.
    • (2003) Anal. Biochem. , vol.320 , pp. 259-265
    • Bektas, M.1    Jolly, P.S.2    Milstien, S.3    Spiegel, S.4
  • 41
    • 0033790309 scopus 로고    scopus 로고
    • Quantitative determination of ceramide using diglyceride kinase
    • Perry, D. K., A. Bielawska, and Y. A. Hannun. 2000. Quantitative determination of ceramide using diglyceride kinase. Methods Enzymol. 312: 22-31.
    • (2000) Methods Enzymol. , vol.312 , pp. 22-31
    • Perry, D.K.1    Bielawska, A.2    Hannun, Y.A.3
  • 42
    • 3142754843 scopus 로고    scopus 로고
    • Mass spectrometric analysis of ceramide perturbations in brain and fibroblasts of mice and human patients with peroxisomal disorders
    • Pettus, B. J., M. Baes, M. Busman, Y. A. Hannun, and P. P. Van Veldhoven. 2004. Mass spectrometric analysis of ceramide perturbations in brain and fibroblasts of mice and human patients with peroxisomal disorders. Rapid Commun. Mass Spectrom. 18: 1569-1574.
    • (2004) Rapid Commun. Mass Spectrom. , vol.18 , pp. 1569-1574
    • Pettus, B.J.1    Baes, M.2    Busman, M.3    Hannun, Y.A.4    Van Veldhoven, P.P.5
  • 43
    • 0035957921 scopus 로고    scopus 로고
    • Induction of apoptosis through B-cell receptor cross-linking occurs via de novo generated C16-ceramide and involves mitochondria
    • Kroesen, B. J., B. Pettus, C. Luberto, M. Busman, H. Sietsma, L. de Leij, and Y. A. Hannun. 2001. Induction of apoptosis through B-cell receptor cross-linking occurs via de novo generated C16-ceramide and involves mitochondria. J. Biol. Chem. 276: 13606-13614.
    • (2001) J. Biol. Chem. , vol.276 , pp. 13606-13614
    • Kroesen, B.J.1    Pettus, B.2    Luberto, C.3    Busman, M.4    Sietsma, H.5    De Leij, L.6    Hannun, Y.A.7
  • 44
    • 1542319001 scopus 로고    scopus 로고
    • Quantitative measurement of different ceramide species from crude cellular extracts by normal-phase high-performance liquid chromatography coupled to atmospheric pressure ionization mass spectrometry
    • Pettus, B. J., B. J. Kroesen, Z. M. Szulc, A. Bielawska, J. Bielawski, Y. A. Hannun, and M. Busman. 2004. Quantitative measurement of different ceramide species from crude cellular extracts by normal-phase high-performance liquid chromatography coupled to atmospheric pressure ionization mass spectrometry. Rapid Commun. Mass Spectrom. 18: 577-583.
    • (2004) Rapid Commun. Mass Spectrom. , vol.18 , pp. 577-583
    • Pettus, B.J.1    Kroesen, B.J.2    Szulc, Z.M.3    Bielawska, A.4    Bielawski, J.5    Hannun, Y.A.6    Busman, M.7
  • 46
    • 0017745135 scopus 로고
    • Biosynthesis of phytosphingosine by the rat
    • Crossman, M. W., and C. B. Hirschberg. 1977. Biosynthesis of phytosphingosine by the rat. J. Biol. Chem. 252: 5815-5819.
    • (1977) J. Biol. Chem. , vol.252 , pp. 5815-5819
    • Crossman, M.W.1    Hirschberg, C.B.2
  • 47
    • 0020286561 scopus 로고
    • Developmental profiles of glycolipids in mouse small intestine
    • Sato, E., T. Uezato, M. Fujita, and K. Nishimura. 1982. Developmental profiles of glycolipids in mouse small intestine. J. Biochem. (Tokyo). 91: 2013-2019.
    • (1982) J. Biochem. (Tokyo) , vol.91 , pp. 2013-2019
    • Sato, E.1    Uezato, T.2    Fujita, M.3    Nishimura, K.4
  • 50
    • 0035980050 scopus 로고    scopus 로고
    • Detergents as tools in membrane biochemistry
    • Garavito, R. M., and S. Ferguson-Miller. 2001. Detergents as tools in membrane biochemistry. J. Biol. Chem. 276: 32403-32406.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32403-32406
    • Garavito, R.M.1    Ferguson-Miller, S.2
  • 51
    • 0011299293 scopus 로고
    • Dual role of interfacial phospholipid in phospholipase A2 catalysis
    • Roberts, M. F., R. A. Deems, and E. A. Dennis. 1977. Dual role of interfacial phospholipid in phospholipase A2 catalysis. Proc. Natl. Acad. Sci. USA. 74: 1950-1954.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 1950-1954
    • Roberts, M.F.1    Deems, R.A.2    Dennis, E.A.3
  • 52
    • 0021111031 scopus 로고
    • Solubilization of phospholipids by detergents. Structural and kinetic aspects
    • Lichtenberg, D., R. J. Robson, and E. A. Dennis. 1983. Solubilization of phospholipids by detergents. Structural and kinetic aspects. Biochim. Biophys. Acta. 737: 285-304.
    • (1983) Biochim. Biophys. Acta , vol.737 , pp. 285-304
    • Lichtenberg, D.1    Robson, R.J.2    Dennis, E.A.3
  • 53
    • 0001688951 scopus 로고
    • Micelles of nonionic detergents and mixed micelles with phospholipids
    • Robson, R. J., and E. A. Dennis. 1983. Micelles of nonionic detergents and mixed micelles with phospholipids. Accts. Chem. Res. 16: 251-258.
    • (1983) Accts. Chem. Res. , vol.16 , pp. 251-258
    • Robson, R.J.1    Dennis, E.A.2
  • 54
    • 0018797853 scopus 로고
    • Mixed micelles of sphingomyelin and phosphatidylcholine with nonionic surfactants. Effect of temperature and surfactant polydispersity
    • Robson, R. J., and E. A. Dennis. 1979. Mixed micelles of sphingomyelin and phosphatidylcholine with nonionic surfactants. Effect of temperature and surfactant polydispersity. Biochim. Biophys. Acta. 573: 489-500.
    • (1979) Biochim. Biophys. Acta , vol.573 , pp. 489-500
    • Robson, R.J.1    Dennis, E.A.2
  • 55
    • 0022341259 scopus 로고
    • Activation of protein kinase C by Triton X-100 mixed micelles containing diacylglycerol and phosphatidylserine
    • Hannun, Y. A., C. R. Loomis, and R. M. Bell. 1985. Activation of protein kinase C by Triton X-100 mixed micelles containing diacylglycerol and phosphatidylserine. J. Biol. Chem. 260: 10039-10043.
    • (1985) J. Biol. Chem. , vol.260 , pp. 10039-10043
    • Hannun, Y.A.1    Loomis, C.R.2    Bell, R.M.3
  • 56
    • 0030048470 scopus 로고    scopus 로고
    • Purification and characterization of UDP-glucose:ceramide glucosyltransferase from rat liver Golgi membranes
    • Paul, P., Y. Kamisaka, D. L. Marks, and R. E. Pagano. 1996. Purification and characterization of UDP-glucose:ceramide glucosyltransferase from rat liver Golgi membranes. J. Biol. Chem. 271: 2287-2293.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2287-2293
    • Paul, P.1    Kamisaka, Y.2    Marks, D.L.3    Pagano, R.E.4
  • 57
    • 0018965399 scopus 로고
    • Studies in vitro on the biosynthesis of ceramide and sphingomyelin. A reevaluation of proposed pathways
    • Stoffel, W., and I. Melzner. 1980. Studies in vitro on the biosynthesis of ceramide and sphingomyelin. A reevaluation of proposed pathways. Hoppe Seylers Z. Physiol. Chem. 361: 755-771.
    • (1980) Hoppe Seylers Z. Physiol. Chem. , vol.361 , pp. 755-771
    • Stoffel, W.1    Melzner, I.2
  • 58
    • 10044236607 scopus 로고    scopus 로고
    • The role of sphingosine and ceramide kinases in inflammatory responses
    • Baumruker, T., F. Bornancin, and A. Billich. 2005. The role of sphingosine and ceramide kinases in inflammatory responses. Immunol. Lett. 96: 175-185.
    • (2005) Immunol. Lett. , vol.96 , pp. 175-185
    • Baumruker, T.1    Bornancin, F.2    Billich, A.3
  • 59


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