메뉴 건너뛰기




Volumn 197, Issue , 2016, Pages 45-59

Inhibitors of the sphingomyelin cycle: Sphingomyelin synthases and sphingomyelinases

Author keywords

Ceramide; Sphingolipids; Sphingomyelin; Sphingomyelinase; Sphingomyelinase synthase

Indexed keywords

3,3' (1,4 PHENYLENE)BIS[N [4 (4,5 DIHYDRO 1H IMIDAZOL 2 YL)PHENYL]ACRYLAMIDE]; ALKALINE SPHINGOMYELINASE; C 11AG; CERAMIDE; DOFEQUIDAR; ENZYME INHIBITOR; FANTOFARONE; FINGOLIMOD; N (6 AMINOHEXYL) 5 CHLORO 1 NAPHTHALENESULFONAMIDE; SCYPHOSTATIN; SIRAMESINE; SMA 7; SPHINGOMYELIN; SPHINGOMYELIN PHOSPHODIESTERASE; SPHINGOMYELINASE SYNTHASE; SPHINGOSINE; SYNTHETASE; TRICYCLO[4.3.0.1]DECAN 9 YL XANTHOGENATE; UNCLASSIFIED DRUG; PHOSPHATIDYLCHOLINE-CERAMIDE PHOSPHOCHOLINE TRANSFERASE; PHOSPHOTRANSFERASE;

EID: 84960801135     PISSN: 00093084     EISSN: 18732941     Source Type: Journal    
DOI: 10.1016/j.chemphyslip.2015.07.008     Document Type: Review
Times cited : (96)

References (186)
  • 1
    • 0029891058 scopus 로고    scopus 로고
    • A novel enzyme that catalyzes the esterification of N-acetylsphingosine. Metabolism of C2-ceramides
    • A. Abe, J.A. Shayman, and N.S. Radin A novel enzyme that catalyzes the esterification of N-acetylsphingosine. Metabolism of C2-ceramides J. Biol. Chem. 271 1996 14383 14389
    • (1996) J. Biol. Chem. , vol.271 , pp. 14383-14389
    • Abe, A.1    Shayman, J.A.2    Radin, N.S.3
  • 3
    • 84897954191 scopus 로고    scopus 로고
    • Sphingolipid regulation of ezrin, radixin, and moesin proteins family: Implications for cell dynamics
    • M. Adada, D. Canals, Y.A. Hannun, and L.M. Obeid Sphingolipid regulation of ezrin, radixin, and moesin proteins family: implications for cell dynamics Biochim. Biophys. Acta 1841 2014 727 737
    • (2014) Biochim. Biophys. Acta , vol.1841 , pp. 727-737
    • Adada, M.1    Canals, D.2    Hannun, Y.A.3    Obeid, L.M.4
  • 4
    • 84878643872 scopus 로고    scopus 로고
    • Lysosomal cell death at a glance
    • S. Aits, and M. Jaattela Lysosomal cell death at a glance J. Cell Sci. 126 2013 1905 1912
    • (2013) J. Cell Sci. , vol.126 , pp. 1905-1912
    • Aits, S.1    Jaattela, M.2
  • 5
    • 0019723109 scopus 로고
    • Tricyclic antidepressants induce sphingomyelinase deficiency in fibroblast and neuroblastoma cell cultures
    • S. Albouz, J.J. Hauw, Y. Berwald-Netter, J.M. Boutry, R. Bourdon, and N. Baumann Tricyclic antidepressants induce sphingomyelinase deficiency in fibroblast and neuroblastoma cell cultures Biomedicine 35 1981 218 220
    • (1981) Biomedicine , vol.35 , pp. 218-220
    • Albouz, S.1    Hauw, J.J.2    Berwald-Netter, Y.3    Boutry, J.M.4    Bourdon, R.5    Baumann, N.6
  • 6
    • 0038383462 scopus 로고    scopus 로고
    • Neutral sphingomyelinase inhibitor C11AG prevents lipopolysaccharide-induced macrophage activation
    • E. Amtmann, W. Baader, and M. Zoller Neutral sphingomyelinase inhibitor C11AG prevents lipopolysaccharide-induced macrophage activation Drugs Exp. Clin. Res. 29 2003 5 13
    • (2003) Drugs Exp. Clin. Res. , vol.29 , pp. 5-13
    • Amtmann, E.1    Baader, W.2    Zoller, M.3
  • 8
    • 15744376272 scopus 로고    scopus 로고
    • Stimulation of CD95-induced apoptosis in T-cells by a subtype specific neutral sphingomyelinase inhibitor
    • E. Amtmann, and M. Zoller Stimulation of CD95-induced apoptosis in T-cells by a subtype specific neutral sphingomyelinase inhibitor Biochem. Pharmacol. 69 2005 1141 1148
    • (2005) Biochem. Pharmacol. , vol.69 , pp. 1141-1148
    • Amtmann, E.1    Zoller, M.2
  • 9
    • 0342368723 scopus 로고    scopus 로고
    • Neutral sphingomyelinase-inhibiting guanidines prevent herpes simplex virus-1 replication
    • E. Amtmann, M. Zoller, and G. Schilling Neutral sphingomyelinase-inhibiting guanidines prevent herpes simplex virus-1 replication Drugs Exp. Clin. Res. 26 2000 57 65
    • (2000) Drugs Exp. Clin. Res. , vol.26 , pp. 57-65
    • Amtmann, E.1    Zoller, M.2    Schilling, G.3
  • 10
    • 84878526866 scopus 로고    scopus 로고
    • Ceramide 1-phosphate induces macrophage chemoattractant protein-1 release: Involvement in ceramide 1-phosphate-stimulated cell migration
    • L. Arana, M. Ordonez, A. Ouro, I.G. Rivera, P. Gangoiti, M. Trueba, and A. Gomez-Munoz Ceramide 1-phosphate induces macrophage chemoattractant protein-1 release: involvement in ceramide 1-phosphate-stimulated cell migration Am. J. Physiol. Endocrinol. Metab. 304 2013 E1213 E1226
    • (2013) Am. J. Physiol. Endocrinol. Metab. , vol.304 , pp. E1213-E1226
    • Arana, L.1    Ordonez, M.2    Ouro, A.3    Rivera, I.G.4    Gangoiti, P.5    Trueba, M.6    Gomez-Munoz, A.7
  • 11
    • 0034810330 scopus 로고    scopus 로고
    • Synthesis and biochemical investigation of scyphostatin analogues as inhibitors of neutral sphingomyelinase
    • C. Arenz, M. Gartner, V. Wascholowski, and A. Giannis Synthesis and biochemical investigation of scyphostatin analogues as inhibitors of neutral sphingomyelinase Bioorg. Med. Chem. 9 2001 2901 2904
    • (2001) Bioorg. Med. Chem. , vol.9 , pp. 2901-2904
    • Arenz, C.1    Gartner, M.2    Wascholowski, V.3    Giannis, A.4
  • 12
    • 3042586648 scopus 로고    scopus 로고
    • Inflammatory mediator and beta-amyloid (25-35)-induced ceramide generation and iNOS expression are inhibited by vitamin E
    • K. Ayasolla, M. Khan, A.K. Singh, and I. Singh Inflammatory mediator and beta-amyloid (25-35)-induced ceramide generation and iNOS expression are inhibited by vitamin E Free Radic. Biol. Med. 37 2004 325 338
    • (2004) Free Radic. Biol. Med. , vol.37 , pp. 325-338
    • Ayasolla, K.1    Khan, M.2    Singh, A.K.3    Singh, I.4
  • 14
    • 0037382346 scopus 로고    scopus 로고
    • Activation of endothelial nitric-oxide synthase by tumor necrosis factor-alpha: A novel pathway involving sequential activation of neutral sphingomyelinase, phosphatidylinositol-3′ kinase, and Akt
    • R. Barsacchi, C. Perrotta, S. Bulotta, S. Moncada, N. Borgese, and E. Clementi Activation of endothelial nitric-oxide synthase by tumor necrosis factor-alpha: a novel pathway involving sequential activation of neutral sphingomyelinase, phosphatidylinositol-3′ kinase, and Akt Mol. Pharmacol. 63 2003 886 895
    • (2003) Mol. Pharmacol. , vol.63 , pp. 886-895
    • Barsacchi, R.1    Perrotta, C.2    Bulotta, S.3    Moncada, S.4    Borgese, N.5    Clementi, E.6
  • 15
    • 13244259440 scopus 로고    scopus 로고
    • Selective inhibition of juxtanuclear translocation of protein kinase C betaII by a negative feedback mechanism involving ceramide formed from the salvage pathway
    • K.P. Becker, K. Kitatani, J. Idkowiak-Baldys, J. Bielawski, and Y.A. Hannun Selective inhibition of juxtanuclear translocation of protein kinase C betaII by a negative feedback mechanism involving ceramide formed from the salvage pathway J. Biol. Chem. 280 2005 2606 2612
    • (2005) J. Biol. Chem. , vol.280 , pp. 2606-2612
    • Becker, K.P.1    Kitatani, K.2    Idkowiak-Baldys, J.3    Bielawski, J.4    Hannun, Y.A.5
  • 16
    • 0028945215 scopus 로고
    • Tumor necrosis factor (TNF)-alpha activates c-raf-1 kinase via the p55 TNF receptor engaging neutral sphingomyelinase
    • C. Belka, K. Wiegmann, D. Adam, R. Holland, M. Neuloh, F. Herrmann, M. Kronke, and M.A. Brach Tumor necrosis factor (TNF)-alpha activates c-raf-1 kinase via the p55 TNF receptor engaging neutral sphingomyelinase EMBO J. 14 1995 1156 1165
    • (1995) EMBO J. , vol.14 , pp. 1156-1165
    • Belka, C.1    Wiegmann, K.2    Adam, D.3    Holland, R.4    Neuloh, M.5    Herrmann, F.6    Kronke, M.7    Brach, M.A.8
  • 17
    • 0035199418 scopus 로고    scopus 로고
    • Selective hydrolysis of a mitochondrial pool of sphingomyelin induces apoptosis
    • H. Birbes, S. El Bawab, Y.A. Hannun, and L.M. Obeid Selective hydrolysis of a mitochondrial pool of sphingomyelin induces apoptosis FASEB J. 15 2001 2669 2679
    • (2001) FASEB J. , vol.15 , pp. 2669-2679
    • Birbes, H.1    El Bawab, S.2    Hannun, Y.A.3    Obeid, L.M.4
  • 18
    • 0036731938 scopus 로고    scopus 로고
    • Reproductive pathology and sperm physiology in acid sphingomyelinase-deficient mice
    • A. Butler, He, X. Gordon, R.E. Wu, H.S. Gatt, S. Schuchman, and EH Reproductive pathology and sperm physiology in acid sphingomyelinase-deficient mice Am. J. Pathol. 161 2002 1061 1075
    • (2002) Am. J. Pathol. , vol.161 , pp. 1061-1075
    • Butler, A.1    He2    Gordon, X.3    Wu, R.E.4    Gatt, H.S.5    Schuchman, S.6    E, H.7
  • 19
    • 84880413477 scopus 로고    scopus 로고
    • Novel chemotherapeutic drugs in sphingolipid cancer research
    • D. Canals, and Y.A. Hannun Novel chemotherapeutic drugs in sphingolipid cancer research Handb. Exp. Pharmacol. 2013 211 238
    • (2013) Handb. Exp. Pharmacol. , pp. 211-238
    • Canals, D.1    Hannun, Y.A.2
  • 20
    • 77957804651 scopus 로고    scopus 로고
    • Differential effects of ceramide and sphingosine 1-phosphate on ERM phosphorylation: Probing sphingolipid signaling at the outer plasma membrane
    • D. Canals, R.W. Jenkins, P. Roddy, M.J. Hernandez-Corbacho, L.M. Obeid, and Y.A. Hannun Differential effects of ceramide and sphingosine 1-phosphate on ERM phosphorylation: probing sphingolipid signaling at the outer plasma membrane J. Biol. Chem. 285 2010 32476 32485
    • (2010) J. Biol. Chem. , vol.285 , pp. 32476-32485
    • Canals, D.1    Jenkins, R.W.2    Roddy, P.3    Hernandez-Corbacho, M.J.4    Obeid, L.M.5    Hannun, Y.A.6
  • 22
    • 84940046039 scopus 로고    scopus 로고
    • Tackling the biophysical properties of sphingolipids to decipher their biological roles
    • A.C. Carreira, A.E. Ventura, A.R. Varela, and L.C. Silva Tackling the biophysical properties of sphingolipids to decipher their biological roles Biol. Chem. 2015
    • (2015) Biol. Chem.
    • Carreira, A.C.1    Ventura, A.E.2    Varela, A.R.3    Silva, L.C.4
  • 23
    • 77957195392 scopus 로고    scopus 로고
    • Exosome release of beta-catenin: A novel mechanism that antagonizes Wnt signaling
    • A. Chairoungdua, D.L. Smith, P. Pochard, M. Hull, and M.J. Caplan Exosome release of beta-catenin: a novel mechanism that antagonizes Wnt signaling J. Cell Biol. 190 2010 1079 1091
    • (2010) J. Cell Biol. , vol.190 , pp. 1079-1091
    • Chairoungdua, A.1    Smith, D.L.2    Pochard, P.3    Hull, M.4    Caplan, M.J.5
  • 24
    • 34347263714 scopus 로고    scopus 로고
    • PKCzeta protects against UV-C-induced apoptosis by inhibiting acid sphingomyelinase-dependent ceramide production
    • A. Charruyer, C. Jean, A. Colomba, J.P. Jaffrezou, A. Quillet-Mary, G. Laurent, and C. Bezombes PKCzeta protects against UV-C-induced apoptosis by inhibiting acid sphingomyelinase-dependent ceramide production Biochem. J. 405 2007 77 83
    • (2007) Biochem. J. , vol.405 , pp. 77-83
    • Charruyer, A.1    Jean, C.2    Colomba, A.3    Jaffrezou, J.P.4    Quillet-Mary, A.5    Laurent, G.6    Bezombes, C.7
  • 26
    • 84939885251 scopus 로고    scopus 로고
    • Ceramide/sphingomyelin cycle involvement in gentamicin-induced cochlear hair cell death
    • N.U. Chi le, K. Tabuchi, M. Nakamagoe, M. Nakayama, B. Nishimura, and A. Hara Ceramide/sphingomyelin cycle involvement in gentamicin-induced cochlear hair cell death Arch. Toxicol. 89 2015 415 421
    • (2015) Arch. Toxicol. , vol.89 , pp. 415-421
    • Chi Le, N.U.1    Tabuchi, K.2    Nakamagoe, M.3    Nakayama, M.4    Nishimura, B.5    Hara, A.6
  • 27
    • 79958719312 scopus 로고    scopus 로고
    • Neutral sphingomyelinase-2 mediates growth arrest by retinoic acid through modulation of ribosomal S6 kinase
    • C.J. Clarke, K. Mediwala, R.W. Jenkins, C.A. Sutton, B.G. Tholanikunnel, and Y.A. Hannun Neutral sphingomyelinase-2 mediates growth arrest by retinoic acid through modulation of ribosomal S6 kinase J. Biol. Chem. 286 2011 21565 21576
    • (2011) J. Biol. Chem. , vol.286 , pp. 21565-21576
    • Clarke, C.J.1    Mediwala, K.2    Jenkins, R.W.3    Sutton, C.A.4    Tholanikunnel, B.G.5    Hannun, Y.A.6
  • 29
    • 51049124339 scopus 로고    scopus 로고
    • Neutral sphingomyelinase-3 is a DNA damage and nongenotoxic stress-regulated gene that is deregulated in human malignancies
    • C.A. Corcoran, Q. He, S. Ponnusamy, B. Ogretmen, Y. Huang, and M.S. Sheikh Neutral sphingomyelinase-3 is a DNA damage and nongenotoxic stress-regulated gene that is deregulated in human malignancies Mol. Cancer Res. 6 2008 795 807
    • (2008) Mol. Cancer Res. , vol.6 , pp. 795-807
    • Corcoran, C.A.1    He, Q.2    Ponnusamy, S.3    Ogretmen, B.4    Huang, Y.5    Sheikh, M.S.6
  • 30
    • 78650864383 scopus 로고    scopus 로고
    • Gilenya (FTY720) inhibits acid sphingomyelinase by a mechanism similar to tricyclic antidepressants
    • G. Dawson, and J. Qin Gilenya (FTY720) inhibits acid sphingomyelinase by a mechanism similar to tricyclic antidepressants Biochem. Biophys. Res. Commun. 404 2011 321 323
    • (2011) Biochem. Biophys. Res. Commun. , vol.404 , pp. 321-323
    • Dawson, G.1    Qin, J.2
  • 31
    • 33644819311 scopus 로고    scopus 로고
    • Endothelial nitric oxide synthase activation by tumor necrosis factor alpha through neutral sphingomyelinase 2, sphingosine kinase 1, and sphingosine 1 phosphate receptors: A novel pathway relevant to the pathophysiology of endothelium
    • C. De Palma, E. Meacci, C. Perrotta, P. Bruni, and E. Clementi Endothelial nitric oxide synthase activation by tumor necrosis factor alpha through neutral sphingomyelinase 2, sphingosine kinase 1, and sphingosine 1 phosphate receptors: a novel pathway relevant to the pathophysiology of endothelium Arterioscler. Thromb. Vasc. Biol. 26 2006 99 105
    • (2006) Arterioscler. Thromb. Vasc. Biol. , vol.26 , pp. 99-105
    • De Palma, C.1    Meacci, E.2    Perrotta, C.3    Bruni, P.4    Clementi, E.5
  • 33
    • 84867352935 scopus 로고    scopus 로고
    • Characterization of secretory sphingomyelinase activity, lipoprotein sphingolipid content and LDL aggregation in ldlr-/- mice fed on a high-fat diet
    • G.M. Deevska, M. Sunkara, A.J. Morris, and M.N. Nikolova-Karakashian Characterization of secretory sphingomyelinase activity, lipoprotein sphingolipid content and LDL aggregation in ldlr-/- mice fed on a high-fat diet Biosci. Rep. 32 2012 479 490
    • (2012) Biosci. Rep. , vol.32 , pp. 479-490
    • Deevska, G.M.1    Sunkara, M.2    Morris, A.J.3    Nikolova-Karakashian, M.N.4
  • 36
    • 78149436318 scopus 로고    scopus 로고
    • Acid sphingomyelinase deficiency attenuates bleomycin-induced lung inflammation and fibrosis in mice
    • R. Dhami, He, X. Schuchman, and EH Acid sphingomyelinase deficiency attenuates bleomycin-induced lung inflammation and fibrosis in mice Cell. Physiol. Biochem. 26 2010 749 760
    • (2010) Cell. Physiol. Biochem. , vol.26 , pp. 749-760
    • Dhami, R.1    He2    Schuchman, X.3    E, H.4
  • 37
    • 0028304788 scopus 로고
    • Dietary sphingomyelin inhibits 1,2-dimethylhydrazine-induced colon cancer in CF1 mice
    • D.L. Dillehay, S.K. Webb, E.M. Schmelz, and A.H. Merrill Jr. Dietary sphingomyelin inhibits 1,2-dimethylhydrazine-induced colon cancer in CF1 mice J. Nutr. 124 1994 615 620
    • (1994) J. Nutr. , vol.124 , pp. 615-620
    • Dillehay, D.L.1    Webb, S.K.2    Schmelz, E.M.3    Merrill, A.H.4
  • 38
    • 38949191625 scopus 로고    scopus 로고
    • SMS overexpression and knockdown: Impact on cellular sphingomyelin and diacylglycerol metabolism, and cell apoptosis
    • T. Ding, Z. Li, T. Hailemariam, S. Mukherjee, F.R. Maxfield, M.P. Wu, and X.C. Jiang SMS overexpression and knockdown: impact on cellular sphingomyelin and diacylglycerol metabolism, and cell apoptosis J. Lipid Res. 49 2008 376 385
    • (2008) J. Lipid Res. , vol.49 , pp. 376-385
    • Ding, T.1    Li, Z.2    Hailemariam, T.3    Mukherjee, S.4    Maxfield, F.R.5    Wu, M.P.6    Jiang, X.C.7
  • 39
    • 84899968840 scopus 로고    scopus 로고
    • Exosome reduction in vivo is associated with lower amyloid plaque load in the 5XFAD mouse model of Alzheimer's disease
    • M.B. Dinkins, S. Dasgupta, G. Wang, G. Zhu, and E. Bieberich Exosome reduction in vivo is associated with lower amyloid plaque load in the 5XFAD mouse model of Alzheimer's disease Neurobiol. Aging 35 2014 1792 1800
    • (2014) Neurobiol. Aging , vol.35 , pp. 1792-1800
    • Dinkins, M.B.1    Dasgupta, S.2    Wang, G.3    Zhu, G.4    Bieberich, E.5
  • 40
    • 0015731798 scopus 로고
    • Biosynthesis of sphingomyelin. Transfer of phosphorylcholine from phosphatidylcholine to erythro-ceramide in a cell-free system
    • H. Diringer, and M.A. Koch Biosynthesis of sphingomyelin. Transfer of phosphorylcholine from phosphatidylcholine to erythro-ceramide in a cell-free system Hoppe Seylers Z. Physiol. Chem. 354 1973 1661 1665
    • (1973) Hoppe Seylers Z. Physiol. Chem. , vol.354 , pp. 1661-1665
    • Diringer, H.1    Koch, M.A.2
  • 41
    • 33744809276 scopus 로고    scopus 로고
    • Adenovirus-mediated overexpression of sphingomyelin synthases 1 and 2 increases the atherogenic potential in mice
    • J. Dong, J. Liu, B. Lou, Z. Li, X. Ye, M. Wu, and X.C. Jiang Adenovirus-mediated overexpression of sphingomyelin synthases 1 and 2 increases the atherogenic potential in mice J. Lipid Res. 47 2006 1307 1314
    • (2006) J. Lipid Res. , vol.47 , pp. 1307-1314
    • Dong, J.1    Liu, J.2    Lou, B.3    Li, Z.4    Ye, X.5    Wu, M.6    Jiang, X.C.7
  • 43
    • 34250772801 scopus 로고    scopus 로고
    • Infections with human rhinovirus induce the formation of distinct functional membrane domains
    • S. Dreschers, P. Franz, C. Dumitru, B. Wilker, K. Jahnke, and E. Gulbins Infections with human rhinovirus induce the formation of distinct functional membrane domains Cell. Physiol. Biochem. 20 2007 241 254
    • (2007) Cell. Physiol. Biochem. , vol.20 , pp. 241-254
    • Dreschers, S.1    Franz, P.2    Dumitru, C.3    Wilker, B.4    Jahnke, K.5    Gulbins, E.6
  • 44
    • 0141532169 scopus 로고    scopus 로고
    • Identification of human intestinal alkaline sphingomyelinase as a novel ecto-enzyme related to the nucleotide phosphodiesterase family
    • R.D. Duan, T. Bergman, N. Xu, J. Wu, Y. Cheng, J. Duan, S. Nelander, C. Palmberg, and A. Nilsson Identification of human intestinal alkaline sphingomyelinase as a novel ecto-enzyme related to the nucleotide phosphodiesterase family J. Biol. Chem. 278 2003 38528 38536
    • (2003) J. Biol. Chem. , vol.278 , pp. 38528-38536
    • Duan, R.D.1    Bergman, T.2    Xu, N.3    Wu, J.4    Cheng, Y.5    Duan, J.6    Nelander, S.7    Palmberg, C.8    Nilsson, A.9
  • 46
    • 84899470963 scopus 로고    scopus 로고
    • Diaphragm dysfunction in heart failure is accompanied by increases in neutral sphingomyelinase activity and ceramide content
    • H.M. Empinado, G.M. Deevska, M. Nikolova-Karakashian, J.K. Yoo, D.D. Christou, and L.F. Ferreira Diaphragm dysfunction in heart failure is accompanied by increases in neutral sphingomyelinase activity and ceramide content Eur. J. Heart Fail. 16 2014 519 525
    • (2014) Eur. J. Heart Fail. , vol.16 , pp. 519-525
    • Empinado, H.M.1    Deevska, G.M.2    Nikolova-Karakashian, M.3    Yoo, J.K.4    Christou, D.D.5    Ferreira, L.F.6
  • 49
    • 78149282781 scopus 로고    scopus 로고
    • Selective reduction in the sphingomyelin content of atherogenic lipoproteins inhibits their retention in murine aortas and the subsequent development of atherosclerosis
    • Y. Fan, F. Shi, J. Liu, J. Dong, H.H. Bui, D.A. Peake, M.S. Kuo, G. Cao, and X.C. Jiang Selective reduction in the sphingomyelin content of atherogenic lipoproteins inhibits their retention in murine aortas and the subsequent development of atherosclerosis Arterioscler. Thromb. Vasc. Biol. 30 2010 2114 2120
    • (2010) Arterioscler. Thromb. Vasc. Biol. , vol.30 , pp. 2114-2120
    • Fan, Y.1    Shi, F.2    Liu, J.3    Dong, J.4    Bui, H.H.5    Peake, D.A.6    Kuo, M.S.7    Cao, G.8    Jiang, X.C.9
  • 53
    • 84855290523 scopus 로고    scopus 로고
    • Neutral sphingomyelinase 2 activity and protein stability are modulated by phosphorylation of five conserved serines
    • S. Filosto, M. Ashfaq, S. Chung, W. Fry, and T. Goldkorn Neutral sphingomyelinase 2 activity and protein stability are modulated by phosphorylation of five conserved serines J. Biol. Chem. 287 2012 514 522
    • (2012) J. Biol. Chem. , vol.287 , pp. 514-522
    • Filosto, S.1    Ashfaq, M.2    Chung, S.3    Fry, W.4    Goldkorn, T.5
  • 56
    • 33845346790 scopus 로고    scopus 로고
    • Biophysics of sphingolipids I. Membrane properties of sphingosine, ceramides and other simple sphingolipids
    • F.M. Goni, and A. Alonso Biophysics of sphingolipids I. Membrane properties of sphingosine, ceramides and other simple sphingolipids Biochim. Biophys. Acta 1758 2006 1902 1921
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1902-1921
    • Goni, F.M.1    Alonso, A.2
  • 57
    • 0036236938 scopus 로고    scopus 로고
    • Synthesis and phospholipase C inhibitory activity of D609 diastereomers
    • A. Gonzalez-Roura, J. Casas, and A. Llebaria Synthesis and phospholipase C inhibitory activity of D609 diastereomers Lipids 37 2002 401 406
    • (2002) Lipids , vol.37 , pp. 401-406
    • Gonzalez-Roura, A.1    Casas, J.2    Llebaria, A.3
  • 58
    • 79955829728 scopus 로고    scopus 로고
    • Inhibition of acid ceramidase by a 2-substituted aminoethanol amide synergistically sensitizes prostate cancer cells to N-(4-hydroxyphenyl) retinamide
    • V. Gouaze-Andersson, M. Flowers, R. Karimi, G. Fabrias, A. Delgado, J. Casas, and M.C. Cabot Inhibition of acid ceramidase by a 2-substituted aminoethanol amide synergistically sensitizes prostate cancer cells to N-(4-hydroxyphenyl) retinamide Prostate 71 2011 1064 1073
    • (2011) Prostate , vol.71 , pp. 1064-1073
    • Gouaze-Andersson, V.1    Flowers, M.2    Karimi, R.3    Fabrias, G.4    Delgado, A.5    Casas, J.6    Cabot, M.C.7
  • 61
    • 22544476850 scopus 로고    scopus 로고
    • Rhinoviruses infect human epithelial cells via ceramide-enriched membrane platforms
    • H. Grassme, A. Riehle, B. Wilker, and E. Gulbins Rhinoviruses infect human epithelial cells via ceramide-enriched membrane platforms J. Biol. Chem. 280 2005 26256 26262
    • (2005) J. Biol. Chem. , vol.280 , pp. 26256-26262
    • Grassme, H.1    Riehle, A.2    Wilker, B.3    Gulbins, E.4
  • 62
    • 0030024123 scopus 로고    scopus 로고
    • Development of the lipid-rich core in human atherosclerosis
    • J.R. Guyton, and K.F. Klemp Development of the lipid-rich core in human atherosclerosis Arterioscler. Thromb. Vasc. Biol. 16 1996 4 11
    • (1996) Arterioscler. Thromb. Vasc. Biol. , vol.16 , pp. 4-11
    • Guyton, J.R.1    Klemp, K.F.2
  • 64
    • 0022974603 scopus 로고
    • Sphingosine inhibition of protein kinase C activity and of phorbol dibutyrate binding in vitro and in human platelets
    • Y.A. Hannun, C.R. Loomis, A.H. Merrill Jr., and R.M. Bell Sphingosine inhibition of protein kinase C activity and of phorbol dibutyrate binding in vitro and in human platelets J. Biol. Chem. 261 1986 12604 12609
    • (1986) J. Biol. Chem. , vol.261 , pp. 12604-12609
    • Hannun, Y.A.1    Loomis, C.R.2    Merrill, A.H.3    Bell, R.M.4
  • 65
    • 84930180719 scopus 로고    scopus 로고
    • A new twist to the emerging functions of ceramides in: Novel role for platelet acid sphingomyelinase in cancer metastasis
    • Y.A. Hannun, and B. Newcomb A new twist to the emerging functions of ceramides in: novel role for platelet acid sphingomyelinase in cancer metastasis EMBO Mol. Med. 2015
    • (2015) EMBO Mol. Med.
    • Hannun, Y.A.1    Newcomb, B.2
  • 66
    • 38549152194 scopus 로고    scopus 로고
    • Principles of bioactive lipid signalling: Lessons from sphingolipids
    • Y.A. Hannun, and L.M. Obeid Principles of bioactive lipid signalling: lessons from sphingolipids Nat. Rev. Mol. Cell Biol. 9 2008 139 150
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 139-150
    • Hannun, Y.A.1    Obeid, L.M.2
  • 68
    • 0031023763 scopus 로고    scopus 로고
    • Alkaline sphingomyelinase activity is decreased in human colorectal carcinoma
    • E. Hertervig, A. Nilsson, L. Nyberg, and R.D. Duan Alkaline sphingomyelinase activity is decreased in human colorectal carcinoma Cancer 79 1997 448 453
    • (1997) Cancer , vol.79 , pp. 448-453
    • Hertervig, E.1    Nilsson, A.2    Nyberg, L.3    Duan, R.D.4
  • 69
    • 0034705097 scopus 로고    scopus 로고
    • Cloning and characterization of the mammalian brain-specific, Mg2+-dependent neutral sphingomyelinase
    • K. Hofmann, S. Tomiuk, G. Wolff, and W. Stoffel Cloning and characterization of the mammalian brain-specific, Mg2+-dependent neutral sphingomyelinase Proc. Natl. Acad. Sci. U. S. A. 97 2000 5895 5900
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 5895-5900
    • Hofmann, K.1    Tomiuk, S.2    Wolff, G.3    Stoffel, W.4
  • 70
    • 15444367538 scopus 로고    scopus 로고
    • Effect of myriocin on plasma sphingolipid metabolism and atherosclerosis in apoE-deficient mice
    • M.R. Hojjati, Z. Li, H. Zhou, S. Tang, C. Huan, E. Ooi, S. Lu, and X.C. Jiang Effect of myriocin on plasma sphingolipid metabolism and atherosclerosis in apoE-deficient mice J. Biol. Chem. 280 2005 10284 10289
    • (2005) J. Biol. Chem. , vol.280 , pp. 10284-10289
    • Hojjati, M.R.1    Li, Z.2    Zhou, H.3    Tang, S.4    Huan, C.5    Ooi, E.6    Lu, S.7    Jiang, X.C.8
  • 71
    • 78049509565 scopus 로고    scopus 로고
    • Tales and mysteries of the enigmatic sphingomyelin synthase family
    • J.C. Holthuis, and C. Luberto Tales and mysteries of the enigmatic sphingomyelin synthase family Adv. Exp. Med. Biol. 688 2010 72 85
    • (2010) Adv. Exp. Med. Biol. , vol.688 , pp. 72-85
    • Holthuis, J.C.1    Luberto, C.2
  • 74
    • 0025934998 scopus 로고
    • Reversal of multidrug resistance by calcium channel blocker SR. 33. 557 without photoaffinity labeling of P-glycoprotein
    • J.P. Jaffrezou, J.M. Herber, T. Levade, M.N. Gau, P. Chatelain, and G. Laurent Reversal of multidrug resistance by calcium channel blocker SR. 33. 557 without photoaffinity labeling of P-glycoprotein J. Biol. Chem. 266 19 1991 858 19864
    • (1991) J. Biol. Chem. , vol.266 , Issue.19 , pp. 858-19864
    • Jaffrezou, J.P.1    Herber, J.M.2    Levade, T.3    Gau, M.N.4    Chatelain, P.5    Laurent, G.6
  • 75
    • 34247477204 scopus 로고    scopus 로고
    • Oxidative stress kills human primary oligodendrocytes via neutral sphingomyelinase: Implications for multiple sclerosis
    • A. Jana, and K. Pahan Oxidative stress kills human primary oligodendrocytes via neutral sphingomyelinase: implications for multiple sclerosis J. Neuroimmune Pharmacol. 2 2007 184 193
    • (2007) J. Neuroimmune Pharmacol. , vol.2 , pp. 184-193
    • Jana, A.1    Pahan, K.2
  • 76
    • 0028070326 scopus 로고
    • Identification of arachidonic acid as a mediator of sphingomyelin hydrolysis in response to tumor necrosis factor alpha
    • S. Jayadev, C.M. Linardic, and Y.A. Hannun Identification of arachidonic acid as a mediator of sphingomyelin hydrolysis in response to tumor necrosis factor alpha J. Biol. Chem. 269 1994 5757 5763
    • (1994) J. Biol. Chem. , vol.269 , pp. 5757-5763
    • Jayadev, S.1    Linardic, C.M.2    Hannun, Y.A.3
  • 77
    • 62749184862 scopus 로고    scopus 로고
    • Roles and regulation of secretory and lysosomal acid sphingomyelinase
    • R.W. Jenkins, D. Canals, and Y.A. Hannun Roles and regulation of secretory and lysosomal acid sphingomyelinase Cell Signal. 21 2009 836 846
    • (2009) Cell Signal. , vol.21 , pp. 836-846
    • Jenkins, R.W.1    Canals, D.2    Hannun, Y.A.3
  • 80
    • 84884949243 scopus 로고    scopus 로고
    • Acid sphingomyelinase plays a key role in palmitic acid-amplified inflammatory signaling triggered by lipopolysaccharide at low concentrations in macrophages
    • J. Jin, X. Zhang, Z. Lu, D.M. Perry, Y. Li, S.B. Russo, L.A. Cowart, Y.A. Hannun, and Y. Huang Acid sphingomyelinase plays a key role in palmitic acid-amplified inflammatory signaling triggered by lipopolysaccharide at low concentrations in macrophages Am. J. Physiol. Endocrinol. Metab. 305 2013 E853 E867
    • (2013) Am. J. Physiol. Endocrinol. Metab. , vol.305 , pp. E853-E867
    • Jin, J.1    Zhang, X.2    Lu, Z.3    Perry, D.M.4    Li, Y.5    Russo, S.B.6    Cowart, L.A.7    Hannun, Y.A.8    Huang, Y.9
  • 82
    • 84896974492 scopus 로고    scopus 로고
    • Bone morphogenic protein (BMP) signaling up-regulates neutral sphingomyelinase 2 to suppress chondrocyte maturation via the Akt protein signaling pathway as a negative feedback mechanism
    • H. Kakoi, S. Maeda, N. Shinohara, K. Matsuyama, K. Imamura, I. Kawamura, S. Nagano, T. Setoguchi, M. Yokouchi, Y. Ishidou, and S. Komiya Bone morphogenic protein (BMP) signaling up-regulates neutral sphingomyelinase 2 to suppress chondrocyte maturation via the Akt protein signaling pathway as a negative feedback mechanism J. Biol. Chem. 289 2014 8135 8150
    • (2014) J. Biol. Chem. , vol.289 , pp. 8135-8150
    • Kakoi, H.1    Maeda, S.2    Shinohara, N.3    Matsuyama, K.4    Imamura, K.5    Kawamura, I.6    Nagano, S.7    Setoguchi, T.8    Yokouchi, M.9    Ishidou, Y.10    Komiya, S.11
  • 83
    • 0014010321 scopus 로고
    • The metabolism of sphingomyelin. I. Purification and properties of a sphingomyelin-cleaving enzyme from rat liver tissue
    • J.N. Kanfer, O.M. Young, D. Shapiro, and R.O. Brady The metabolism of sphingomyelin. I. Purification and properties of a sphingomyelin-cleaving enzyme from rat liver tissue J. Biol. Chem. 241 1966 1081 1084
    • (1966) J. Biol. Chem. , vol.241 , pp. 1081-1084
    • Kanfer, J.N.1    Young, O.M.2    Shapiro, D.3    Brady, R.O.4
  • 87
    • 84964698520 scopus 로고    scopus 로고
    • Guggulsterone and bexarotene induce secretion of exosome-associated breast cancer resistance protein and reduce doxorubicin resistance in MDA-MB -231 cells
    • J.N. Kong, Q. He, G. Wang, S. Dasgupta, M.B. Dinkins, G. Zhu, A. Kim, S. Spassieva, and E. Bieberich Guggulsterone and bexarotene induce secretion of exosome-associated breast cancer resistance protein and reduce doxorubicin resistance in MDA-MB -231 cells Int. J. Cancer 2015
    • (2015) Int. J. Cancer
    • Kong, J.N.1    He, Q.2    Wang, G.3    Dasgupta, S.4    Dinkins, M.B.5    Zhu, G.6    Kim, A.7    Spassieva, S.8    Bieberich, E.9
  • 88
    • 84886022765 scopus 로고    scopus 로고
    • Unraveling the complexities of the HDL lipidome
    • A. Kontush, M. Lhomme, and M.J. Chapman Unraveling the complexities of the HDL lipidome J. Lipid Res. 54 2013 2950 2963
    • (2013) J. Lipid Res. , vol.54 , pp. 2950-2963
    • Kontush, A.1    Lhomme, M.2    Chapman, M.J.3
  • 89
    • 84876248584 scopus 로고    scopus 로고
    • Neutral sphingomyelinase 2 (nSMase2)-dependent exosomal transfer of angiogenic microRNAs regulate cancer cell metastasis
    • N. Kosaka, H. Iguchi, K. Hagiwara, Y. Yoshioka, F. Takeshita, and T. Ochiya Neutral sphingomyelinase 2 (nSMase2)-dependent exosomal transfer of angiogenic microRNAs regulate cancer cell metastasis J. Biol. Chem. 288 2013 10849 10859
    • (2013) J. Biol. Chem. , vol.288 , pp. 10849-10859
    • Kosaka, N.1    Iguchi, H.2    Hagiwara, K.3    Yoshioka, Y.4    Takeshita, F.5    Ochiya, T.6
  • 90
  • 91
    • 33744953581 scopus 로고    scopus 로고
    • Novel tumor necrosis factor-responsive mammalian neutral sphingomyelinase-3 is a C-tail-anchored protein
    • O. Krut, K. Wiegmann, H. Kashkar, B. Yazdanpanah, and M. Kronke Novel tumor necrosis factor-responsive mammalian neutral sphingomyelinase-3 is a C-tail-anchored protein J. Biol. Chem. 281 2006 13784 13793
    • (2006) J. Biol. Chem. , vol.281 , pp. 13784-13793
    • Krut, O.1    Wiegmann, K.2    Kashkar, H.3    Yazdanpanah, B.4    Kronke, M.5
  • 92
    • 84879102853 scopus 로고    scopus 로고
    • Sphingomyelin synthase 2 activity and liver steatosis: An effect of ceramide-mediated peroxisome proliferator-activated receptor gamma2 suppression
    • Y. Li, J. Dong, T. Ding, M.S. Kuo, G. Cao, X.C. Jiang, and Z. Li Sphingomyelin synthase 2 activity and liver steatosis: an effect of ceramide-mediated peroxisome proliferator-activated receptor gamma2 suppression Arterioscler. Thromb. Vasc. Biol. 33 2013 1513 1520
    • (2013) Arterioscler. Thromb. Vasc. Biol. , vol.33 , pp. 1513-1520
    • Li, Y.1    Dong, J.2    Ding, T.3    Kuo, M.S.4    Cao, G.5    Jiang, X.C.6    Li, Z.7
  • 97
    • 0027526903 scopus 로고
    • Characterization of the neutral pH-optimum sphingomyelinase from rat brain: Inhibition by copper II and ganglioside GM3
    • M.D. Lister, C.L. Crawford-Redick, and C.R. Loomis Characterization of the neutral pH-optimum sphingomyelinase from rat brain: inhibition by copper II and ganglioside GM3 Biochim. Biophys. Acta 1165 1993 314 320
    • (1993) Biochim. Biophys. Acta , vol.1165 , pp. 314-320
    • Lister, M.D.1    Crawford-Redick, C.L.2    Loomis, C.R.3
  • 98
    • 0030960327 scopus 로고    scopus 로고
    • Inhibition of the neutral magnesium-dependent sphingomyelinase by glutathione
    • B. Liu, and Y.A. Hannun Inhibition of the neutral magnesium-dependent sphingomyelinase by glutathione J. Biol. Chem. 272 1997 16281 16287
    • (1997) J. Biol. Chem. , vol.272 , pp. 16281-16287
    • Liu, B.1    Hannun, Y.A.2
  • 99
    • 0032545461 scopus 로고    scopus 로고
    • Purification and characterization of a membrane bound neutral pH optimum magnesium-dependent and phosphatidylserine-stimulated sphingomyelinase from rat brain
    • B. Liu, D.F. Hassler, G.K. Smith, K. Weaver, and Y.A. Hannun Purification and characterization of a membrane bound neutral pH optimum magnesium-dependent and phosphatidylserine-stimulated sphingomyelinase from rat brain J. Biol. Chem. 273 1998 34472 34479
    • (1998) J. Biol. Chem. , vol.273 , pp. 34472-34479
    • Liu, B.1    Hassler, D.F.2    Smith, G.K.3    Weaver, K.4    Hannun, Y.A.5
  • 100
    • 84863388132 scopus 로고    scopus 로고
    • Zebrafish in the study of early cardiac development
    • J. Liu, and D.Y. Stainier Zebrafish in the study of early cardiac development Circ. Res. 110 2012 870 874
    • (2012) Circ. Res. , vol.110 , pp. 870-874
    • Liu, J.1    Stainier, D.Y.2
  • 102
    • 84911033540 scopus 로고    scopus 로고
    • Systemic administration of 2-hydroxypropyl-beta-cyclodextrin to symptomatic Npc1-deficient mice slows cholesterol sequestration in the major organs and improves liver function
    • A.M. Lopez, S.J. Terpack, K.S. Posey, B. Liu, C.M. Ramirez, and S.D. Turley Systemic administration of 2-hydroxypropyl-beta-cyclodextrin to symptomatic Npc1-deficient mice slows cholesterol sequestration in the major organs and improves liver function Clin. Exp. Pharmacol. Physiol. 41 2014 780 787
    • (2014) Clin. Exp. Pharmacol. Physiol. , vol.41 , pp. 780-787
    • Lopez, A.M.1    Terpack, S.J.2    Posey, K.S.3    Liu, B.4    Ramirez, C.M.5    Turley, S.D.6
  • 103
    • 84904512058 scopus 로고    scopus 로고
    • Pharmacologic inhibition of sphingomyelin synthase (SMS) activity reduces apolipoprotein-B secretion from hepatocytes and attenuates endotoxin-mediated macrophage inflammation
    • B. Lou, J. Dong, Y. Li, T. Ding, T. Bi, Y. Li, X. Deng, D. Ye, and X.C. Jiang Pharmacologic inhibition of sphingomyelin synthase (SMS) activity reduces apolipoprotein-B secretion from hepatocytes and attenuates endotoxin-mediated macrophage inflammation PLoS One 9 2014 e102641
    • (2014) PLoS One , vol.9
    • Lou, B.1    Dong, J.2    Li, Y.3    Ding, T.4    Bi, T.5    Li, Y.6    Deng, X.7    Ye, D.8    Jiang, X.C.9
  • 105
    • 0032486257 scopus 로고    scopus 로고
    • Sphingomyelin synthase, a potential regulator of intracellular levels of ceramide and diacylglycerol during SV40 transformation. Does sphingomyelin synthase account for the putative phosphatidylcholine-specific phospholipase C?
    • C. Luberto, and Y.A. Hannun Sphingomyelin synthase, a potential regulator of intracellular levels of ceramide and diacylglycerol during SV40 transformation. Does sphingomyelin synthase account for the putative phosphatidylcholine-specific phospholipase C? J. Biol. Chem. 273 1998 14550 14559
    • (1998) J. Biol. Chem. , vol.273 , pp. 14550-14559
    • Luberto, C.1    Hannun, Y.A.2
  • 107
    • 0036695392 scopus 로고    scopus 로고
    • Ceramide regulation of apoptosis versus differentiation: A walk on a fine line. Lessons from neurobiology
    • C. Luberto, J.M. Kraveka, and Y.A. Hannun Ceramide regulation of apoptosis versus differentiation: a walk on a fine line. Lessons from neurobiology Neurochem. Res. 27 2002 609 617
    • (2002) Neurochem. Res. , vol.27 , pp. 609-617
    • Luberto, C.1    Kraveka, J.M.2    Hannun, Y.A.3
  • 108
    • 0032512723 scopus 로고    scopus 로고
    • Human vascular endothelial cells are a rich and regulatable source of secretory sphingomyelinase. Implications for early atherogenesis and ceramide-mediated cell signaling
    • S. Marathe, S.L. Schissel, M.J. Yellin, N. Beatini, R. Mintzer, K.J. Williams, and I. Tabas Human vascular endothelial cells are a rich and regulatable source of secretory sphingomyelinase. Implications for early atherogenesis and ceramide-mediated cell signaling J. Biol. Chem. 273 1998 4081 4088
    • (1998) J. Biol. Chem. , vol.273 , pp. 4081-4088
    • Marathe, S.1    Schissel, S.L.2    Yellin, M.J.3    Beatini, N.4    Mintzer, R.5    Williams, K.J.6    Tabas, I.7
  • 109
    • 0038529730 scopus 로고    scopus 로고
    • Biochemical properties of mammalian neutral sphingomyelinase 2 and its role in sphingolipid metabolism
    • N. Marchesini, C. Luberto, and Y.A. Hannun Biochemical properties of mammalian neutral sphingomyelinase 2 and its role in sphingolipid metabolism J. Biol. Chem. 278 2003 13775 13783
    • (2003) J. Biol. Chem. , vol.278 , pp. 13775-13783
    • Marchesini, N.1    Luberto, C.2    Hannun, Y.A.3
  • 110
    • 2942532249 scopus 로고    scopus 로고
    • Role for mammalian neutral sphingomyelinase 2 in confluence-induced growth arrest of MCF7 cells
    • N. Marchesini, W. Osta, J. Bielawski, C. Luberto, L.M. Obeid, and Y.A. Hannun Role for mammalian neutral sphingomyelinase 2 in confluence-induced growth arrest of MCF7 cells J. Biol. Chem. 279 2004 25101 25111
    • (2004) J. Biol. Chem. , vol.279 , pp. 25101-25111
    • Marchesini, N.1    Osta, W.2    Bielawski, J.3    Luberto, C.4    Obeid, L.M.5    Hannun, Y.A.6
  • 111
    • 0024539606 scopus 로고
    • Calmodulin antagonist W-7 inhibits lysosomal sphingomyelinase activity in C6 glioma cells
    • M. Masson, S. Albouz, J.M. Boutry, B. Spezzatti, M. Castagna, and N. Baumann Calmodulin antagonist W-7 inhibits lysosomal sphingomyelinase activity in C6 glioma cells J. Neurochem. 52 1989 1645 1647
    • (1989) J. Neurochem. , vol.52 , pp. 1645-1647
    • Masson, M.1    Albouz, S.2    Boutry, J.M.3    Spezzatti, B.4    Castagna, M.5    Baumann, N.6
  • 112
    • 80054079107 scopus 로고    scopus 로고
    • Sphingolipid and glycosphingolipid metabolic pathways in the era of sphingolipidomics
    • A.H. Merrill Jr. Sphingolipid and glycosphingolipid metabolic pathways in the era of sphingolipidomics Chem. Rev. 111 2011 6387 6422
    • (2011) Chem. Rev. , vol.111 , pp. 6387-6422
    • Merrill, A.H.1
  • 113
    • 53249156006 scopus 로고    scopus 로고
    • Changes in sphingomyelinases, ceramide, Bax, Bcl(2), and caspase-3 during and after experimental status epilepticus
    • M.A. Mikati, M. Zeinieh, R.A. Habib, J. El Hokayem, A. Rahmeh, M. El Sabban, J. Usta, and G. Dbaibo Changes in sphingomyelinases, ceramide, Bax, Bcl(2), and caspase-3 during and after experimental status epilepticus Epilepsy Res. 81 2008 161 166
    • (2008) Epilepsy Res. , vol.81 , pp. 161-166
    • Mikati, M.A.1    Zeinieh, M.2    Habib, R.A.3    El Hokayem, J.4    Rahmeh, A.5    El Sabban, M.6    Usta, J.7    Dbaibo, G.8
  • 118
    • 84855918312 scopus 로고    scopus 로고
    • Ceramide synthases at the centre of sphingolipid metabolism and biology
    • T.D. Mullen, Y.A. Hannun, and L.M. Obeid Ceramide synthases at the centre of sphingolipid metabolism and biology Biochem. J. 441 2012 789 802
    • (2012) Biochem. J. , vol.441 , pp. 789-802
    • Mullen, T.D.1    Hannun, Y.A.2    Obeid, L.M.3
  • 119
    • 0024327349 scopus 로고
    • Interruption of TPA-induced signals by an antiviral and antitumoral xanthate compound: Inhibition of a phospholipase C-type reaction
    • K. Muller-Decker Interruption of TPA-induced signals by an antiviral and antitumoral xanthate compound: inhibition of a phospholipase C-type reaction Biochem. Biophys. Res. Commun. 162 1989 198 205
    • (1989) Biochem. Biophys. Res. Commun. , vol.162 , pp. 198-205
    • Muller-Decker, K.1
  • 121
    • 0032817681 scopus 로고    scopus 로고
    • Scyphostatin, a neutral sphingomyelinase inhibitor from a discomycete, Trichopeziza mollissima: Taxonomy of the producing organism, fermentation, isolation, and physico-chemical properties
    • F. Nara, M. Tanaka, T. Hosoya, K. Suzuki-Konagai, and T. Ogita Scyphostatin, a neutral sphingomyelinase inhibitor from a discomycete, Trichopeziza mollissima: taxonomy of the producing organism, fermentation, isolation, and physico-chemical properties J. Antibiot. (Tokyo) 52 1999 525 530
    • (1999) J. Antibiot. (Tokyo) , vol.52 , pp. 525-530
    • Nara, F.1    Tanaka, M.2    Hosoya, T.3    Suzuki-Konagai, K.4    Ogita, T.5
  • 124
    • 0029778534 scopus 로고    scopus 로고
    • Functional analysis of the glycosylation of murine acid sphingomyelinase
    • D. Newrzella, and W. Stoffel Functional analysis of the glycosylation of murine acid sphingomyelinase J. Biol. Chem. 271 1996 32089 32095
    • (1996) J. Biol. Chem. , vol.271 , pp. 32089-32095
    • Newrzella, D.1    Stoffel, W.2
  • 125
    • 0034879931 scopus 로고    scopus 로고
    • A new quinoline derivative MS-209 reverses multidrug resistance and inhibits multiorgan metastases by P-glycoprotein-expressing human small cell lung cancer cells
    • H. Nokihara, S. Yano, Y. Nishioka, M. Hanibuchi, T. Higasida, T. Tsuruo, and S. Sone A new quinoline derivative MS-209 reverses multidrug resistance and inhibits multiorgan metastases by P-glycoprotein-expressing human small cell lung cancer cells Jpn. J. Cancer Res. 92 2001 785 792
    • (2001) Jpn. J. Cancer Res. , vol.92 , pp. 785-792
    • Nokihara, H.1    Yano, S.2    Nishioka, Y.3    Hanibuchi, M.4    Higasida, T.5    Tsuruo, T.6    Sone, S.7
  • 126
    • 79960117964 scopus 로고    scopus 로고
    • Novel pathway of ceramide production in mitochondria: Thioesterase and neutral ceramidase produce ceramide from sphingosine and acyl-CoA
    • S.A. Novgorodov, B.X. Wu, T.I. Gudz, J. Bielawski, T.V. Ovchinnikova, Y.A. Hannun, and L.M. Obeid Novel pathway of ceramide production in mitochondria: thioesterase and neutral ceramidase produce ceramide from sphingosine and acyl-CoA J. Biol. Chem. 286 2011 25352 25362
    • (2011) J. Biol. Chem. , vol.286 , pp. 25352-25362
    • Novgorodov, S.A.1    Wu, B.X.2    Gudz, T.I.3    Bielawski, J.4    Ovchinnikova, T.V.5    Hannun, Y.A.6    Obeid, L.M.7
  • 127
    • 0029913677 scopus 로고    scopus 로고
    • Identification of an alkaline sphingomyelinase activity in human bile
    • L. Nyberg, R.D. Duan, J. Axelson, and A. Nilsson Identification of an alkaline sphingomyelinase activity in human bile Biochim. Biophys. Acta 1300 1996 42 48
    • (1996) Biochim. Biophys. Acta , vol.1300 , pp. 42-48
    • Nyberg, L.1    Duan, R.D.2    Axelson, J.3    Nilsson, A.4
  • 128
  • 130
    • 0024795059 scopus 로고
    • Sphingomyelin turnover induced by vitamin D3 in HL-60 cells. Role in cell differentiation
    • T. Okazaki, R.M. Bell, and Y.A. Hannun Sphingomyelin turnover induced by vitamin D3 in HL-60 cells. Role in cell differentiation J. Biol. Chem. 264 1989 19076 19080
    • (1989) J. Biol. Chem. , vol.264 , pp. 19076-19080
    • Okazaki, T.1    Bell, R.M.2    Hannun, Y.A.3
  • 131
    • 84919723483 scopus 로고    scopus 로고
    • Acid sphingomyelinase activity is regulated by membrane lipids and facilitates cholesterol transfer by NPC2
    • V.O. Oninla, B. Breiden, J.O. Babalola, and K. Sandhoff Acid sphingomyelinase activity is regulated by membrane lipids and facilitates cholesterol transfer by NPC2 J. Lipid Res. 55 2014 2606 2619
    • (2014) J. Lipid Res. , vol.55 , pp. 2606-2619
    • Oninla, V.O.1    Breiden, B.2    Babalola, J.O.3    Sandhoff, K.4
  • 132
    • 0029014350 scopus 로고
    • Acid sphingomyelinase-deficient mice mimic the neurovisceral form of human lysosomal storage disease (Niemann-Pick disease)
    • B. Otterbach, and W. Stoffel Acid sphingomyelinase-deficient mice mimic the neurovisceral form of human lysosomal storage disease (Niemann-Pick disease) Cell 81 1995 1053 1061
    • (1995) Cell , vol.81 , pp. 1053-1061
    • Otterbach, B.1    Stoffel, W.2
  • 133
    • 0347695003 scopus 로고    scopus 로고
    • Ceramide pathways modulate ethanol-induced cell death in astrocytes
    • M. Pascual, S.L. Valles, J. Renau-Piqueras, and C. Guerri Ceramide pathways modulate ethanol-induced cell death in astrocytes J. Neurochem. 87 2003 1535 1545
    • (2003) J. Neurochem. , vol.87 , pp. 1535-1545
    • Pascual, M.1    Valles, S.L.2    Renau-Piqueras, J.3    Guerri, C.4
  • 134
    • 84977983435 scopus 로고
    • A comparison between the molecular weights of protagon and of the phosphatide and cerebrosides obtainable from it
    • A.L. Pearson A comparison between the molecular weights of protagon and of the phosphatide and cerebrosides obtainable from it Biochem. J. 8 1914 616 627
    • (1914) Biochem. J. , vol.8 , pp. 616-627
    • Pearson, A.L.1
  • 136
    • 0842326180 scopus 로고    scopus 로고
    • The role of de novo ceramide synthesis in the mechanism of action of the tricyclic xanthate D609
    • R.J. Perry, and N.D. Ridgway The role of de novo ceramide synthesis in the mechanism of action of the tricyclic xanthate D609 J. Lipid Res. 45 2004 164 173
    • (2004) J. Lipid Res. , vol.45 , pp. 164-173
    • Perry, R.J.1    Ridgway, N.D.2
  • 139
    • 83655167166 scopus 로고    scopus 로고
    • Glycosphingolipids in signaling and development: From liposomes to model organisms
    • S.M. Pontier, and F. Schweisguth Glycosphingolipids in signaling and development: from liposomes to model organisms Dev. Dyn. 241 2012 92 106
    • (2012) Dev. Dyn. , vol.241 , pp. 92-106
    • Pontier, S.M.1    Schweisguth, F.2
  • 140
    • 0028353499 scopus 로고
    • Acid sphingomyelinase possesses a domain homologous to its activator proteins: Saposins B and D
    • C.P. Ponting Acid sphingomyelinase possesses a domain homologous to its activator proteins: saposins B and D Protein Sci. 3 1994 359 361
    • (1994) Protein Sci. , vol.3 , pp. 359-361
    • Ponting, C.P.1
  • 141
    • 32044439625 scopus 로고    scopus 로고
    • CD161 (human NKR-P1A) signaling in NK cells involves the activation of acid sphingomyelinase
    • D. Pozo, M. Vales-Gomez, N. Mavaddat, S.C. Williamson, S.E. Chisholm, and H. Reyburn CD161 (human NKR-P1A) signaling in NK cells involves the activation of acid sphingomyelinase J. Immunol. 176 2006 2397 2406
    • (2006) J. Immunol. , vol.176 , pp. 2397-2406
    • Pozo, D.1    Vales-Gomez, M.2    Mavaddat, N.3    Williamson, S.C.4    Chisholm, S.E.5    Reyburn, H.6
  • 142
    • 84860008997 scopus 로고    scopus 로고
    • Neutral sphingomyelinase 2 deficiency increases hyaluronan synthesis by up-regulation of Hyaluronan synthase 2 through decreased ceramide production and activation of Akt
    • J. Qin, E. Berdyshev, C. Poirer, N.B. Schwartz, and G. Dawson Neutral sphingomyelinase 2 deficiency increases hyaluronan synthesis by up-regulation of Hyaluronan synthase 2 through decreased ceramide production and activation of Akt J. Biol. Chem. 287 2012 13620 13632
    • (2012) J. Biol. Chem. , vol.287 , pp. 13620-13632
    • Qin, J.1    Berdyshev, E.2    Poirer, C.3    Schwartz, N.B.4    Dawson, G.5
  • 143
    • 68949201124 scopus 로고    scopus 로고
    • Oxidized phosphatidylcholine formation and action in oligodendrocytes
    • J. Qin, F.D. Testai, S. Dawson, J. Kilkus, and G. Dawson Oxidized phosphatidylcholine formation and action in oligodendrocytes J. Neurochem. 110 2009 1388 1399
    • (2009) J. Neurochem. , vol.110 , pp. 1388-1399
    • Qin, J.1    Testai, F.D.2    Dawson, S.3    Kilkus, J.4    Dawson, G.5
  • 144
    • 0025866614 scopus 로고
    • Human acid sphingomyelinase from human urine
    • L.E. Quintern, and K. Sandhoff Human acid sphingomyelinase from human urine Methods Enzymol. 197 1991 536 540
    • (1991) Methods Enzymol. , vol.197 , pp. 536-540
    • Quintern, L.E.1    Sandhoff, K.2
  • 145
    • 0024379291 scopus 로고
    • The urine from patients with peritonitis as a rich source for purifying human acid sphingomyelinase and other lysosomal enzymes
    • L.E. Quintern, T.S. Zenk, and K. Sandhoff The urine from patients with peritonitis as a rich source for purifying human acid sphingomyelinase and other lysosomal enzymes Biochim. Biophys. Acta 1003 1989 121 124
    • (1989) Biochim. Biophys. Acta , vol.1003 , pp. 121-124
    • Quintern, L.E.1    Zenk, T.S.2    Sandhoff, K.3
  • 148
    • 34248666988 scopus 로고    scopus 로고
    • Inhibition of lipopolysaccharide-induced release of interleukin-8 from intestinal epithelial cells by SMA, a novel inhibitor of sphingomyelinase and its therapeutic effect on dextran sulphate sodium-induced colitis in mice
    • A. Sakata, K. Yasuda, T. Ochiai, H. Shimeno, S. Hikishima, T. Yokomatsu, S. Shibuya, and S. Soeda Inhibition of lipopolysaccharide-induced release of interleukin-8 from intestinal epithelial cells by SMA, a novel inhibitor of sphingomyelinase and its therapeutic effect on dextran sulphate sodium-induced colitis in mice Cell Immunol. 245 2007 24 31
    • (2007) Cell Immunol. , vol.245 , pp. 24-31
    • Sakata, A.1    Yasuda, K.2    Ochiai, T.3    Shimeno, H.4    Hikishima, S.5    Yokomatsu, T.6    Shibuya, S.7    Soeda, S.8
  • 149
    • 84878418606 scopus 로고    scopus 로고
    • Recombinant human acid sphingomyelinase as an adjuvant to sorafenib treatment of experimental liver cancer
    • R. Savic, He, X. Fiel, I. Schuchman, and EH Recombinant human acid sphingomyelinase as an adjuvant to sorafenib treatment of experimental liver cancer PLoS One 8 2013 e65620
    • (2013) PLoS One , vol.8
    • Savic, R.1    He2    Fiel, X.3    Schuchman, I.4    E, H.5
  • 150
    • 84871817869 scopus 로고    scopus 로고
    • Use of acid sphingomyelinase for cancer therapy
    • R. Savic, and E.H. Schuchman Use of acid sphingomyelinase for cancer therapy Adv. Cancer Res. 117 2013 91 115
    • (2013) Adv. Cancer Res. , vol.117 , pp. 91-115
    • Savic, R.1    Schuchman, E.H.2
  • 151
    • 0033621471 scopus 로고    scopus 로고
    • Function of the cloned putative neutral sphingomyelinase as lyso-platelet activating factor-phospholipase C
    • H. Sawai, N. Domae, N. Nagan, and Y.A. Hannun Function of the cloned putative neutral sphingomyelinase as lyso-platelet activating factor-phospholipase C J. Biol. Chem. 274 1999 38131 38139
    • (1999) J. Biol. Chem. , vol.274 , pp. 38131-38139
    • Sawai, H.1    Domae, N.2    Nagan, N.3    Hannun, Y.A.4
  • 152
    • 0014083339 scopus 로고
    • Sphingomyelinase in normal human spleens and in spleens from subjects with Niemann-Pick disease
    • P.B. Schneider, and E.P. Kennedy Sphingomyelinase in normal human spleens and in spleens from subjects with Niemann-Pick disease J. Lipid Res. 8 1967 202 209
    • (1967) J. Lipid Res. , vol.8 , pp. 202-209
    • Schneider, P.B.1    Kennedy, E.P.2
  • 153
    • 77951893147 scopus 로고    scopus 로고
    • Acid sphingomyelinase, cell membranes and human disease: Lessons from Niemann-Pick disease
    • E.H. Schuchman Acid sphingomyelinase, cell membranes and human disease: lessons from Niemann-Pick disease FEBS Lett. 584 2010 1895 1900
    • (2010) FEBS Lett. , vol.584 , pp. 1895-1900
    • Schuchman, E.H.1
  • 154
    • 0026577992 scopus 로고
    • Structural organization and complete nucleotide sequence of the gene encoding human acid sphingomyelinase (SMPD1)
    • E.H. Schuchman, O. Levran, L.V. Pereira, and R.J. Desnick Structural organization and complete nucleotide sequence of the gene encoding human acid sphingomyelinase (SMPD1) Genomics 12 1992 197 205
    • (1992) Genomics , vol.12 , pp. 197-205
    • Schuchman, E.H.1    Levran, O.2    Pereira, L.V.3    Desnick, R.J.4
  • 155
    • 0025819971 scopus 로고
    • Human acid sphingomyelinase. Isolation, nucleotide sequence and expression of the full-length and alternatively spliced cDNAs
    • E.H. Schuchman, M. Suchi, T. Takahashi, K. Sandhoff, and R.J. Desnick Human acid sphingomyelinase. Isolation, nucleotide sequence and expression of the full-length and alternatively spliced cDNAs J. Biol. Chem. 266 1991 8531 8539
    • (1991) J. Biol. Chem. , vol.266 , pp. 8531-8539
    • Schuchman, E.H.1    Suchi, M.2    Takahashi, T.3    Sandhoff, K.4    Desnick, R.J.5
  • 156
    • 84920856216 scopus 로고    scopus 로고
    • Roles and regulation of neutral sphingomyelinase-2 in cellular and pathological processes
    • A.A. Shamseddine, M.V. Airola, and Y.A. Hannun Roles and regulation of neutral sphingomyelinase-2 in cellular and pathological processes Adv. Biol. Regul. 57 2015 24 41
    • (2015) Adv. Biol. Regul. , vol.57 , pp. 24-41
    • Shamseddine, A.A.1    Airola, M.V.2    Hannun, Y.A.3
  • 158
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • K. Simons, and E. Ikonen Functional rafts in cell membranes Nature 387 1997 569 572
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 159
    • 54049092827 scopus 로고    scopus 로고
    • The unexpected role of acid sphingomyelinase in cell death and the pathophysiology of common diseases
    • E.L. Smith, and E.H. Schuchman The unexpected role of acid sphingomyelinase in cell death and the pathophysiology of common diseases FASEB J. 22 2008 3419 3431
    • (2008) FASEB J. , vol.22 , pp. 3419-3431
    • Smith, E.L.1    Schuchman, E.H.2
  • 160
    • 80054072283 scopus 로고    scopus 로고
    • The gut-to-breast connection - Interdependence of sterols and sphingolipids in multidrug resistance and breast cancer therapy
    • S. Spassieva, and E. Bieberich The gut-to-breast connection - interdependence of sterols and sphingolipids in multidrug resistance and breast cancer therapy Anticancer Agents Med. Chem. 11 2011 882 890
    • (2011) Anticancer Agents Med. Chem. , vol.11 , pp. 882-890
    • Spassieva, S.1    Bieberich, E.2
  • 161
  • 163
    • 84989350484 scopus 로고    scopus 로고
    • Lysosomal ceramide generated by acid sphingomyelinase triggers cytosolic cathepsin B-mediated degradation of X-linked inhibitor of apoptosis protein in natural killer/T lymphoma cell apoptosis
    • M. Taniguchi, H. Ogiso, T. Takeuchi, K. Kitatani, H. Umehara, and T. Okazaki Lysosomal ceramide generated by acid sphingomyelinase triggers cytosolic cathepsin B-mediated degradation of X-linked inhibitor of apoptosis protein in natural killer/T lymphoma cell apoptosis Cell Death Dis. 6 2015 e1717
    • (2015) Cell Death Dis. , vol.6
    • Taniguchi, M.1    Ogiso, H.2    Takeuchi, T.3    Kitatani, K.4    Umehara, H.5    Okazaki, T.6
  • 165
    • 84884742613 scopus 로고    scopus 로고
    • Ceramides: A potential therapeutic target in pulmonary emphysema
    • J. Tibboel, I. Reiss, J.C. de Jongste, and M. Post Ceramides: a potential therapeutic target in pulmonary emphysema Respir. Res. 14 2013 96
    • (2013) Respir. Res. , vol.14 , pp. 96
    • Tibboel, J.1    Reiss, I.2    De Jongste, J.C.3    Post, M.4
  • 169
    • 0032866201 scopus 로고    scopus 로고
    • Alutenusin, a specific neutral sphingomyelinase inhibitor, produced by Penicillium sp. FO-7436
    • R. Uchida, H. Tomoda, Y. Dong, and S. Omura Alutenusin, a specific neutral sphingomyelinase inhibitor, produced by Penicillium sp. FO-7436 J. Antibiot. (Tokyo) 52 1999 572 574
    • (1999) J. Antibiot. (Tokyo) , vol.52 , pp. 572-574
    • Uchida, R.1    Tomoda, H.2    Dong, Y.3    Omura, S.4
  • 170
    • 84876533831 scopus 로고    scopus 로고
    • Ceramide phosphoethanolamine biosynthesis in Drosophila is mediated by a unique ethanolamine phosphotransferase in the Golgi lumen
    • A.M. Vacaru, J. van den Dikkenberg, P. Ternes, and J.C. Holthuis Ceramide phosphoethanolamine biosynthesis in Drosophila is mediated by a unique ethanolamine phosphotransferase in the Golgi lumen J. Biol. Chem. 288 2013 11520 11530
    • (2013) J. Biol. Chem. , vol.288 , pp. 11520-11530
    • Vacaru, A.M.1    Van Den Dikkenberg, J.2    Ternes, P.3    Holthuis, J.C.4
  • 171
    • 33846526677 scopus 로고    scopus 로고
    • Resistance to alkyl-lysophospholipid-induced apoptosis due to downregulated sphingomyelin synthase 1 expression with consequent sphingomyelin- and cholesterol-deficiency in lipid rafts
    • A.H. Van der Luit, M. Budde, S. Zerp, W. Caan, J.B. Klarenbeek, M. Verheij, and W.J. Van Blitterswijk Resistance to alkyl-lysophospholipid-induced apoptosis due to downregulated sphingomyelin synthase 1 expression with consequent sphingomyelin- and cholesterol-deficiency in lipid rafts Biochem. J. 401 2007 541 549
    • (2007) Biochem. J. , vol.401 , pp. 541-549
    • Van Der Luit, A.H.1    Budde, M.2    Zerp, S.3    Caan, W.4    Klarenbeek, J.B.5    Verheij, M.6    Van Blitterswijk, W.J.7
  • 172
    • 0028055154 scopus 로고
    • Conversion of diacylglycerol to phosphatidylcholine on the basolateral surface of epithelial (Madin-Darby canine kidney) cells. Evidence for the reverse action of a sphingomyelin synthase
    • A. van Helvoort, W. van't Hof, T. Ritsema, A. Sandra, and G. van Meer Conversion of diacylglycerol to phosphatidylcholine on the basolateral surface of epithelial (Madin-Darby canine kidney) cells. Evidence for the reverse action of a sphingomyelin synthase J. Biol. Chem. 269 1994 1763 1769
    • (1994) J. Biol. Chem. , vol.269 , pp. 1763-1769
    • Van Helvoort, A.1    Van't Hof, W.2    Ritsema, T.3    Sandra, A.4    Van Meer, G.5
  • 174
    • 84862274671 scopus 로고    scopus 로고
    • Astrocytes secrete exosomes enriched with proapoptotic ceramide and prostate apoptosis response 4 (PAR-4): Potential mechanism of apoptosis induction in Alzheimer disease (AD)
    • G. Wang, M. Dinkins, Q. He, G. Zhu, C. Poirier, A. Campbell, M. Mayer-Proschel, and E. Bieberich Astrocytes secrete exosomes enriched with proapoptotic ceramide and prostate apoptosis response 4 (PAR-4): potential mechanism of apoptosis induction in Alzheimer disease (AD) J. Biol. Chem. 287 2012 21384 21395
    • (2012) J. Biol. Chem. , vol.287 , pp. 21384-21395
    • Wang, G.1    Dinkins, M.2    He, Q.3    Zhu, G.4    Poirier, C.5    Campbell, A.6    Mayer-Proschel, M.7    Bieberich, E.8
  • 175
    • 33746630883 scopus 로고    scopus 로고
    • Influence of the scyphostatin side chain on the mode of inhibition of neutral sphingomyelinase
    • V. Wascholowski, A. Giannis, and E.N. Pitsinos Influence of the scyphostatin side chain on the mode of inhibition of neutral sphingomyelinase ChemMedChem 1 2006 718 721
    • (2006) ChemMedChem , vol.1 , pp. 718-721
    • Wascholowski, V.1    Giannis, A.2    Pitsinos, E.N.3
  • 176
    • 84884992556 scopus 로고    scopus 로고
    • Targeting ovarian cancer and chemoresistance through selective inhibition of sphingosine kinase-2 with ABC294640
    • M.D. White, L. Chan, J.W. Antoon, and B.S. Beckman Targeting ovarian cancer and chemoresistance through selective inhibition of sphingosine kinase-2 with ABC294640 Anticancer Res. 33 2013 3573 3579
    • (2013) Anticancer Res. , vol.33 , pp. 3573-3579
    • White, M.D.1    Chan, L.2    Antoon, J.W.3    Beckman, B.S.4
  • 178
    • 77952937382 scopus 로고    scopus 로고
    • Identification and characterization of murine mitochondria-associated neutral sphingomyelinase (MA-nSMase), the mammalian sphingomyelin phosphodiesterase 5
    • B.X. Wu, V. Rajagopalan, P.L. Roddy, C.J. Clarke, and Y.A. Hannun Identification and characterization of murine mitochondria-associated neutral sphingomyelinase (MA-nSMase), the mammalian sphingomyelin phosphodiesterase 5 J. Biol. Chem. 285 2010 17993 18002
    • (2010) J. Biol. Chem. , vol.285 , pp. 17993-18002
    • Wu, B.X.1    Rajagopalan, V.2    Roddy, P.L.3    Clarke, C.J.4    Hannun, Y.A.5
  • 179
    • 4344656249 scopus 로고    scopus 로고
    • Identification of one exon deletion of intestinal alkaline sphingomyelinase in colon cancer HT-29 cells and a differentiation-related expression of the wild-type enzyme in Caco-2 cells
    • J. Wu, Y. Cheng, A. Nilsson, and R.D. Duan Identification of one exon deletion of intestinal alkaline sphingomyelinase in colon cancer HT-29 cells and a differentiation-related expression of the wild-type enzyme in Caco-2 cells Carcinogenesis 25 2004 1327 1333
    • (2004) Carcinogenesis , vol.25 , pp. 1327-1333
    • Wu, J.1    Cheng, Y.2    Nilsson, A.3    Duan, R.D.4
  • 180
    • 67749120148 scopus 로고    scopus 로고
    • A novel mitochondrial sphingomyelinase in zebrafish cells
    • T. Yabu, A. Shimuzu, and M. Yamashita A novel mitochondrial sphingomyelinase in zebrafish cells J. Biol. Chem. 284 2009 20349 20363
    • (2009) J. Biol. Chem. , vol.284 , pp. 20349-20363
    • Yabu, T.1    Shimuzu, A.2    Yamashita, M.3
  • 183
    • 77649121670 scopus 로고    scopus 로고
    • Association of plasma sphingomyelin levels and incident coronary heart disease events in an adult population: Multi-Ethnic Study of Atherosclerosis
    • J. Yeboah, C. McNamara, X.C. Jiang, I. Tabas, D.M. Herrington, G.L. Burke, and S. Shea Association of plasma sphingomyelin levels and incident coronary heart disease events in an adult population: Multi-Ethnic Study of Atherosclerosis Arterioscler. Thromb. Vasc. Biol. 30 2010 628 633
    • (2010) Arterioscler. Thromb. Vasc. Biol. , vol.30 , pp. 628-633
    • Yeboah, J.1    McNamara, C.2    Jiang, X.C.3    Tabas, I.4    Herrington, D.M.5    Burke, G.L.6    Shea, S.7
  • 184
    • 0022367017 scopus 로고
    • Reduction of acid sphingomyelinase activity in human fibroblasts induced by AY-9944 and other cationic amphiphilic drugs
    • Y. Yoshida, K. Arimoto, M. Sato, N. Sakuragawa, M. Arima, and E. Satoyoshi Reduction of acid sphingomyelinase activity in human fibroblasts induced by AY-9944 and other cationic amphiphilic drugs J. Biochem. 98 1985 1669 1679
    • (1985) J. Biochem. , vol.98 , pp. 1669-1679
    • Yoshida, Y.1    Arimoto, K.2    Sato, M.3    Sakuragawa, N.4    Arima, M.5    Satoyoshi, E.6
  • 186
    • 64149110203 scopus 로고    scopus 로고
    • Ceramide synthase inhibition by fumonisin B1 causes accumulation of 1-deoxysphinganine: A novel category of bioactive 1-deoxysphingoid bases and 1-deoxydihydroceramides biosynthesized by mammalian cell lines and animals
    • N.C. Zitomer, T. Mitchell, K.A. Voss, G.S. Bondy, S.T. Pruett, E.C. Garnier-Amblard, L.S. Liebeskind, H. Park, E. Wang, M.C. Sullards, A.H. Jr. Merrill, and R.T. Riley Ceramide synthase inhibition by fumonisin B1 causes accumulation of 1-deoxysphinganine: a novel category of bioactive 1-deoxysphingoid bases and 1-deoxydihydroceramides biosynthesized by mammalian cell lines and animals J. Biol. Chem. 284 2009 4786 4795
    • (2009) J. Biol. Chem. , vol.284 , pp. 4786-4795
    • Zitomer, N.C.1    Mitchell, T.2    Voss, K.A.3    Bondy, G.S.4    Pruett, S.T.5    Garnier-Amblard, E.C.6    Liebeskind, L.S.7    Park, H.8    Wang, E.9    Sullards, M.C.10    Merrill, A.H.11    Riley, R.T.12


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.