메뉴 건너뛰기




Volumn 68, Issue 3, 2016, Pages 570-581

Regulation of sphingomyelin metabolism

Author keywords

Acid sphingomyelinase; Neutral sphingomyelinase; Sphingomyelin; Sphingomyelin synthases

Indexed keywords

ALKALINE SPHINGOMYELINASE; SPHINGOMYELIN; SPHINGOMYELIN PHOSPHODIESTERASE; SPHINGOMYELIN SYNTHASE 1; SPHINGOMYELIN SYNTHASE 2; SPHINGOMYELIN SYNTHASE RELATED PROTEIN; SYNTHETASE; UNCLASSIFIED DRUG; PHOSPHATIDYLCHOLINE-CERAMIDE PHOSPHOCHOLINE TRANSFERASE; PHOSPHOTRANSFERASE;

EID: 84959512133     PISSN: 22995684     EISSN: 22995684     Source Type: Journal    
DOI: 10.1016/j.pharep.2015.12.008     Document Type: Review
Times cited : (143)

References (197)
  • 1
    • 33645992493 scopus 로고    scopus 로고
    • Sphingomyelin structure influences the lateral diffusion and raft formation in lipid bilayers
    • A. Filippov, G. Orädd, and G. Lindblom Sphingomyelin structure influences the lateral diffusion and raft formation in lipid bilayers Biophys J 90 6 2006 2086 2092
    • (2006) Biophys J , vol.90 , Issue.6 , pp. 2086-2092
    • Filippov, A.1    Orädd, G.2    Lindblom, G.3
  • 3
    • 0032411331 scopus 로고    scopus 로고
    • Molecular species of sphingomyelin: Determination by high-performance liquid chromatography/mass spectrometry with electrospray and high-performance liquid chromatography/tandem mass spectrometry with atmospheric pressure chemical ionization
    • A.A. Karlsson, P. Michélsen, and G. Odham Molecular species of sphingomyelin: Determination by high-performance liquid chromatography/mass spectrometry with electrospray and high-performance liquid chromatography/tandem mass spectrometry with atmospheric pressure chemical ionization J Mass Spectrom 33 12 1998 1192 1198
    • (1998) J Mass Spectrom , vol.33 , Issue.12 , pp. 1192-1198
    • Karlsson, A.A.1    Michélsen, P.2    Odham, G.3
  • 4
    • 34547132811 scopus 로고    scopus 로고
    • Ceramides and sphingomyelins with high proportions of very long-chain polyunsaturated fatty acids in mammalian germ cells
    • N.E. Furland, S.R. Zanetti, G.M. Oresti, E.N. Maldonado, and M.I. Aveldanõ Ceramides and sphingomyelins with high proportions of very long-chain polyunsaturated fatty acids in mammalian germ cells J Biol Chem 282 25 2007 18141 18150
    • (2007) J Biol Chem , vol.282 , Issue.25 , pp. 18141-18150
    • Furland, N.E.1    Zanetti, S.R.2    Oresti, G.M.3    Maldonado, E.N.4    Aveldanõ, M.I.5
  • 5
    • 0037201948 scopus 로고    scopus 로고
    • Membrane properties of sphingomyelins
    • B. Ramstedt, and J.P. Slotte Membrane properties of sphingomyelins FEBS Lett 531 1 2002 33 37
    • (2002) FEBS Lett , vol.531 , Issue.1 , pp. 33-37
    • Ramstedt, B.1    Slotte, J.P.2
  • 6
    • 0035033848 scopus 로고    scopus 로고
    • Membrane properties of D-erythro-N-acyl sphingomyelins and their corresponding dihydro species
    • M. Kuikka, B. Ramstedt, H. Ohvo-Rekilä, J. Tuuf, and J.P. Slotte Membrane properties of D-erythro-N-acyl sphingomyelins and their corresponding dihydro species Biophys J 80 5 2001 2327 2337
    • (2001) Biophys J , vol.80 , Issue.5 , pp. 2327-2337
    • Kuikka, M.1    Ramstedt, B.2    Ohvo-Rekilä, H.3    Tuuf, J.4    Slotte, J.P.5
  • 7
    • 0025941734 scopus 로고
    • Interaction of cholesterol with sphingomyelin in bilayer membranes: Evidence that the hydroxy group of sphingomyelin does not modulate the rate of cholesterol exchange between vesicles
    • C.C. Kan, Z.S. Ruan, and R. Bittman Interaction of cholesterol with sphingomyelin in bilayer membranes: Evidence that the hydroxy group of sphingomyelin does not modulate the rate of cholesterol exchange between vesicles Biochemistry 30 31 1991 7759 7766
    • (1991) Biochemistry , vol.30 , Issue.31 , pp. 7759-7766
    • Kan, C.C.1    Ruan, Z.S.2    Bittman, R.3
  • 8
    • 0025150146 scopus 로고
    • Elastic deformation and failure of lipid bilayer membranes containing cholesterol
    • D. Needham, and R.S. Nunn Elastic deformation and failure of lipid bilayer membranes containing cholesterol Biophys J 58 4 1990 997 1009
    • (1990) Biophys J , vol.58 , Issue.4 , pp. 997-1009
    • Needham, D.1    Nunn, R.S.2
  • 9
    • 0031964607 scopus 로고    scopus 로고
    • Cholesterol and sphingolipid enhance the Triton X-100 insolubility of glycosylphosphatidylinositol-anchored proteins by promoting the formation of detergent-insoluble ordered membrane domains
    • R.J. Schroeder, S.N. Ahmed, Y. Zhu, E. London, and D.A. Brown Cholesterol and sphingolipid enhance the Triton X-100 insolubility of glycosylphosphatidylinositol-anchored proteins by promoting the formation of detergent-insoluble ordered membrane domains J Biol Chem 273 2 1998 1150 1157
    • (1998) J Biol Chem , vol.273 , Issue.2 , pp. 1150-1157
    • Schroeder, R.J.1    Ahmed, S.N.2    Zhu, Y.3    London, E.4    Brown, D.A.5
  • 10
    • 0035877706 scopus 로고    scopus 로고
    • Changes in the lipid turnover, composition, and organization, as sphingolipid-enriched membrane domains, in rat cerebellar granule cells developing in vitro
    • A. Prinetti, V. Chigorno, S. Prioni, N. Loberto, N. Marano, G. Tettamanti, and et al. Changes in the lipid turnover, composition, and organization, as sphingolipid-enriched membrane domains, in rat cerebellar granule cells developing in vitro J Biol Chem 276 24 2001 21136 21145
    • (2001) J Biol Chem , vol.276 , Issue.24 , pp. 21136-21145
    • Prinetti, A.1    Chigorno, V.2    Prioni, S.3    Loberto, N.4    Marano, N.5    Tettamanti, G.6
  • 11
    • 0026016879 scopus 로고
    • Intracellular transport and metabolism of sphingomyelin
    • M. Koval, and R.E. Pagano Intracellular transport and metabolism of sphingomyelin Biochim Biophys Acta 1082 2 1991 113 125
    • (1991) Biochim Biophys Acta , vol.1082 , Issue.2 , pp. 113-125
    • Koval, M.1    Pagano, R.E.2
  • 12
    • 0033031744 scopus 로고    scopus 로고
    • Interaction of cholesterol with sphingomyelins and acyl-chain-matched phosphatidylcholines: A comparative study of the effect of the chain length
    • B. Ramstedt, and J.P. Slotte Interaction of cholesterol with sphingomyelins and acyl-chain-matched phosphatidylcholines: A comparative study of the effect of the chain length Biophys J 76 2 1999 908 915
    • (1999) Biophys J , vol.76 , Issue.2 , pp. 908-915
    • Ramstedt, B.1    Slotte, J.P.2
  • 13
    • 0028034850 scopus 로고
    • Interaction of cholesterol with sphingomyelin in monolayers and vesicles
    • R. Bittman, C.R. Kasireddy, P. Mattjus, and J.P. Slotte Interaction of cholesterol with sphingomyelin in monolayers and vesicles Biochemistry 33 39 1994 11776 11781
    • (1994) Biochemistry , vol.33 , Issue.39 , pp. 11776-11781
    • Bittman, R.1    Kasireddy, C.R.2    Mattjus, P.3    Slotte, J.P.4
  • 14
    • 77955656862 scopus 로고    scopus 로고
    • Sphingomyelin analogs with branched N-acyl chains: The position of branching dramatically affects acyl chain order and sterol interactions in bilayer membranes
    • S. Jaikishan, A. Björkbom, and J.P. Slotte Sphingomyelin analogs with branched N-acyl chains: The position of branching dramatically affects acyl chain order and sterol interactions in bilayer membranes Biochim Biophys Acta 1798 10 2010 1987 1994
    • (2010) Biochim Biophys Acta , vol.1798 , Issue.10 , pp. 1987-1994
    • Jaikishan, S.1    Björkbom, A.2    Slotte, J.P.3
  • 15
    • 0032867082 scopus 로고    scopus 로고
    • Comparison of the biophysical properties of racemic and d-erythro-N-acyl sphingomyelins
    • B. Ramstedt, and J.P. Slotte Comparison of the biophysical properties of racemic and d-erythro-N-acyl sphingomyelins Biophys J 77 3 1999 1498 1506
    • (1999) Biophys J , vol.77 , Issue.3 , pp. 1498-1506
    • Ramstedt, B.1    Slotte, J.P.2
  • 16
    • 0347298692 scopus 로고    scopus 로고
    • Extensive temporally regulated reorganization of the lipid raft proteome following T-cell antigen receptor triggering
    • L. Bini, S. Pacini, S. Liberatori, S. Valensin, M. Pellegrini, R. Raggiaschi, and et al. Extensive temporally regulated reorganization of the lipid raft proteome following T-cell antigen receptor triggering Biochem J 369 2 2003 301 309
    • (2003) Biochem J , vol.369 , Issue.2 , pp. 301-309
    • Bini, L.1    Pacini, S.2    Liberatori, S.3    Valensin, S.4    Pellegrini, M.5    Raggiaschi, R.6
  • 17
    • 0034625373 scopus 로고    scopus 로고
    • Structure and function of sphingolipid-and cholesterol-rich membrane rafts
    • D.A. Brown, and E. London Structure and function of sphingolipid-and cholesterol-rich membrane rafts J Biol Chem 275 23 2000 17221 17224
    • (2000) J Biol Chem , vol.275 , Issue.23 , pp. 17221-17224
    • Brown, D.A.1    London, E.2
  • 18
    • 0027787984 scopus 로고
    • Fumonisin B1 inhibits sphingosine (sphinganine) N-acyltransferase and de novo sphingolipid biosynthesis in cultured neurons in situ
    • A.H Merrill Jr., G. van Echten, E. Wang, and K. Sandhoff Fumonisin B1 inhibits sphingosine (sphinganine) N-acyltransferase and de novo sphingolipid biosynthesis in cultured neurons in situ J Biol Chem 268 36 1993 27299 27306
    • (1993) J Biol Chem , vol.268 , Issue.36 , pp. 27299-27306
    • Merrill, A.H.1    Van Echten, G.2    Wang, E.3    Sandhoff, K.4
  • 19
    • 0028101939 scopus 로고
    • Localization of O-glycan initiation, sphingomyelin synthesis, and glucosylceramide synthesis in Vero cells with respect to the endoplasmic reticulum-Golgi intermediate compartment
    • A. Schweizer, H. Clausen, G. van Meer, and H.P. Hauri Localization of O-glycan initiation, sphingomyelin synthesis, and glucosylceramide synthesis in Vero cells with respect to the endoplasmic reticulum-Golgi intermediate compartment J Biol Chem 269 6 1994 4035 4041
    • (1994) J Biol Chem , vol.269 , Issue.6 , pp. 4035-4041
    • Schweizer, A.1    Clausen, H.2    Van Meer, G.3    Hauri, H.P.4
  • 20
    • 0035842889 scopus 로고    scopus 로고
    • Vesicular and nonvesicular transport of ceramide from ER to the Golgi apparatus in yeast
    • K. Funato, and H. Riezman Vesicular and nonvesicular transport of ceramide from ER to the Golgi apparatus in yeast J Cell Biol 155 6 2001 949 959
    • (2001) J Cell Biol , vol.155 , Issue.6 , pp. 949-959
    • Funato, K.1    Riezman, H.2
  • 21
    • 77955112195 scopus 로고    scopus 로고
    • Intracellular trafficking of ceramide by ceramide transfer protein
    • K. Hanada Intracellular trafficking of ceramide by ceramide transfer protein Proc Jpn Acad Ser B Phys Biol Sci 86 4 2010 426 437
    • (2010) Proc Jpn Acad ser B Phys Biol Sci , vol.86 , Issue.4 , pp. 426-437
    • Hanada, K.1
  • 22
    • 59849097154 scopus 로고    scopus 로고
    • Mitochondrial degeneration and not apoptosis is the primary cause of embryonic lethality in ceramide transfer protein mutant mice
    • X. Wang, R.P. Rao, T. Kosakowska-Cholody, M.A. Masood, E. Southon, H. Zhang, and et al. Mitochondrial degeneration and not apoptosis is the primary cause of embryonic lethality in ceramide transfer protein mutant mice J Cell Biol 184 1 2009 143 158
    • (2009) J Cell Biol , vol.184 , Issue.1 , pp. 143-158
    • Wang, X.1    Rao, R.P.2    Kosakowska-Cholody, T.3    Masood, M.A.4    Southon, E.5    Zhang, H.6
  • 23
    • 0025323167 scopus 로고
    • Sphingomyelin synthesis in rat liver occurs predominantly at the cis and medial cisternae of the Golgi apparatus
    • A.H. Futerman, B. Stieger, A.L. Hubbard, and R.E. Pagano Sphingomyelin synthesis in rat liver occurs predominantly at the cis and medial cisternae of the Golgi apparatus J Biol Chem 265 15 1990 8650 8657
    • (1990) J Biol Chem , vol.265 , Issue.15 , pp. 8650-8657
    • Futerman, A.H.1    Stieger, B.2    Hubbard, A.L.3    Pagano, R.E.4
  • 24
    • 0034717903 scopus 로고    scopus 로고
    • Sphingolipid transport in eukaryotic cells
    • G. van Meer, and J.C. Holthuis Sphingolipid transport in eukaryotic cells Biochim Biophys Acta 1486 1 2000 145 170
    • (2000) Biochim Biophys Acta , vol.1486 , Issue.1 , pp. 145-170
    • Van Meer, G.1    Holthuis, J.C.2
  • 25
    • 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 13 1991 8531 8539
    • (1991) J Biol Chem , vol.266 , Issue.13 , pp. 8531-8539
    • Schuchman, E.H.1    Suchi, M.2    Takahashi, T.3    Sandhoff, K.4    Desnick, R.J.5
  • 26
    • 78649802553 scopus 로고    scopus 로고
    • Mammalian neutral sphingomyelinases: Regulation and roles in cell signaling responses
    • B.X. Wu, C.J. Clarke, and Y.A. Hannun Mammalian neutral sphingomyelinases: Regulation and roles in cell signaling responses Neuromolecular Med 12 4 2010 320 330
    • (2010) Neuromolecular Med , vol.12 , Issue.4 , pp. 320-330
    • Wu, B.X.1    Clarke, C.J.2    Hannun, Y.A.3
  • 27
    • 77951889353 scopus 로고    scopus 로고
    • Sphingomyelin metabolism at the plasma membrane: Implications for bioactive sphingolipids
    • D. Milhas, C.J. Clarke, and Y.A. Hannun Sphingomyelin metabolism at the plasma membrane: Implications for bioactive sphingolipids FEBS Lett 584 9 2010 1887 1894
    • (2010) FEBS Lett , vol.584 , Issue.9 , pp. 1887-1894
    • Milhas, D.1    Clarke, C.J.2    Hannun, Y.A.3
  • 28
    • 84924584886 scopus 로고    scopus 로고
    • All members in the sphingomyelin synthase gene family have ceramide phosphoethanolamine synthase activity
    • T. Ding, I. Kabir, Y. Li, C. Lou, A. Yazdanyar, J. Xu, and et al. All members in the sphingomyelin synthase gene family have ceramide phosphoethanolamine synthase activity J Lipid Res 56 3 2015 537 545
    • (2015) J Lipid Res , vol.56 , Issue.3 , pp. 537-545
    • Ding, T.1    Kabir, I.2    Li, Y.3    Lou, C.4    Yazdanyar, A.5    Xu, J.6
  • 29
    • 83355164474 scopus 로고    scopus 로고
    • Subcellular targeting domains of sphingomyelin synthase 1 and 2
    • C. Yeang, T. Ding, W.J. Chirico, and X.C. Jiang Subcellular targeting domains of sphingomyelin synthase 1 and 2 Nutr Metab (Lond) 8 2011 89
    • (2011) Nutr Metab (Lond) , vol.8 , pp. 89
    • Yeang, C.1    Ding, T.2    Chirico, W.J.3    Jiang, X.C.4
  • 31
    • 34548604943 scopus 로고    scopus 로고
    • Inhibition of sphingomyelin synthase (SMS) affects intracellular sphingomyelin accumulation and plasma membrane lipid organization
    • Z. Li, T.K. Hailemariam, H. Zhou, Y. Li, D.C. Duckworth, D.A. Peake, and et al. Inhibition of sphingomyelin synthase (SMS) affects intracellular sphingomyelin accumulation and plasma membrane lipid organization Biochim Biophys Acta 1771 9 2007 1186 1194
    • (2007) Biochim Biophys Acta , vol.1771 , Issue.9 , pp. 1186-1194
    • Li, Z.1    Hailemariam, T.K.2    Zhou, H.3    Li, Y.4    Duckworth, D.C.5    Peake, D.A.6
  • 32
    • 34547110137 scopus 로고    scopus 로고
    • Both sphingomyelin synthases SMS1 and SMS2 are required for sphingomyelin homeostasis and growth in human HeLa cells
    • F.G. Tafesse, K. Huitema, M. Hermansson, S. van der Poel, J. van den Dikkenberg, A. Uphoff, and et al. Both sphingomyelin synthases SMS1 and SMS2 are required for sphingomyelin homeostasis and growth in human HeLa cells J Biol Chem 282 24 2007 17537 17547
    • (2007) J Biol Chem , vol.282 , Issue.24 , pp. 17537-17547
    • Tafesse, F.G.1    Huitema, K.2    Hermansson, M.3    Van Der Poel, S.4    Van Den Dikkenberg, J.5    Uphoff, A.6
  • 33
    • 84945907162 scopus 로고    scopus 로고
    • Comparative analysis of sphingomyelin synthase 1 gene expression at the transcriptional and translational levels in human tissues
    • O.Y. Sudarkina, I.B. Filippenkov, I.B. Brodsky, S.A. Limborska, and L.V. Dergunova Comparative analysis of sphingomyelin synthase 1 gene expression at the transcriptional and translational levels in human tissues Mol Cell Biochem 406 1-2 2015 91 99
    • (2015) Mol Cell Biochem , vol.406 , Issue.1-2 , pp. 91-99
    • Sudarkina, O.Y.1    Filippenkov, I.B.2    Brodsky, I.B.3    Limborska, S.A.4    Dergunova, L.V.5
  • 35
    • 33749576963 scopus 로고    scopus 로고
    • The multigenic sphingomyelin synthase family
    • F.G. Tafesse, P. Ternes, and J.C. Holthuis The multigenic sphingomyelin synthase family J Biol Chem 281 40 2006 29421 29425
    • (2006) J Biol Chem , vol.281 , Issue.40 , pp. 29421-29425
    • Tafesse, F.G.1    Ternes, P.2    Holthuis, J.C.3
  • 36
    • 84939885542 scopus 로고    scopus 로고
    • Sphingomyelin synthase 1 regulates neuro-2a cell proliferation and cell cycle progression through modulation of p27 expression and Akt signaling
    • U.V. Wesley, J.F. Hatcher, and R.J. Dempsey Sphingomyelin synthase 1 regulates neuro-2a cell proliferation and cell cycle progression through modulation of p27 expression and Akt signaling Mol Neurobiol 51 3 2015 1530 1541
    • (2015) Mol Neurobiol , vol.51 , Issue.3 , pp. 1530-1541
    • Wesley, U.V.1    Hatcher, J.F.2    Dempsey, R.J.3
  • 37
    • 84897954261 scopus 로고    scopus 로고
    • The role of sphingomyelin and sphingomyelin synthases in cell death, proliferation and migration-from cell and animal models to human disorders
    • M. Taniguchi, and T. Okazaki The role of sphingomyelin and sphingomyelin synthases in cell death, proliferation and migration-from cell and animal models to human disorders Biochim Biophys Acta 1841 5 2014 692 703
    • (2014) Biochim Biophys Acta , vol.1841 , Issue.5 , pp. 692-703
    • Taniguchi, M.1    Okazaki, T.2
  • 38
    • 77949541016 scopus 로고    scopus 로고
    • Caspase-mediated inhibition of sphingomyelin synthesis is involved in FasL-triggered cell death
    • E. Lafont, D. Milhas, S. Carpentier, V. Garcia, Z.X. Jin, H. Umehara, and et al. Caspase-mediated inhibition of sphingomyelin synthesis is involved in FasL-triggered cell death Cell Death Differ 17 4 2010 642 654
    • (2010) Cell Death Differ , vol.17 , Issue.4 , pp. 642-654
    • Lafont, E.1    Milhas, D.2    Carpentier, S.3    Garcia, V.4    Jin, Z.X.5    Umehara, H.6
  • 39
    • 0035918285 scopus 로고    scopus 로고
    • Basic fibroblast growth factor-induced proliferation of primary astrocytes. Evidence for the involvement of sphingomyelin biosynthesis
    • L. Riboni, P. Viani, R. Bassi, P. Giussani, and G. Tettamanti Basic fibroblast growth factor-induced proliferation of primary astrocytes. Evidence for the involvement of sphingomyelin biosynthesis J Biol Chem 276 16 2001 12797 12804
    • (2001) J Biol Chem , vol.276 , Issue.16 , pp. 12797-12804
    • Riboni, L.1    Viani, P.2    Bassi, R.3    Giussani, P.4    Tettamanti, G.5
  • 40
    • 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 23 1998 14550 14559
    • (1998) J Biol Chem , vol.273 , Issue.23 , pp. 14550-14559
    • Luberto, C.1    Hannun, Y.A.2
  • 41
    • 0030948082 scopus 로고    scopus 로고
    • Alteration of the sphingomyelin/ceramide pathway is associated with resistance of human breast carcinoma MCF7 cells to tumor necrosis factor-alpha-mediated cytotoxicity
    • Z. Cai, A. Bettaieb, N.E. Mahdani, L.G. Legrès, R. Stancou, J. Masliah, and et al. Alteration of the sphingomyelin/ceramide pathway is associated with resistance of human breast carcinoma MCF7 cells to tumor necrosis factor-alpha-mediated cytotoxicity J Biol Chem 272 11 1997 6918 6926
    • (1997) J Biol Chem , vol.272 , Issue.11 , pp. 6918-6926
    • Cai, Z.1    Bettaieb, A.2    Mahdani, N.E.3    Legrès, L.G.4    Stancou, R.5    Masliah, J.6
  • 42
    • 8644278972 scopus 로고    scopus 로고
    • Interleukin-2-induced survival of natural killer (NK) cells involving phosphatidylinositol-3 kinase-dependent reduction of ceramide through acid sphingomyelinase, sphingomyelin synthase, and glucosylceramide synthase
    • Y. Taguchi, T. Kondo, M. Watanabe, M. Miyaji, H. Umehara, Y. Kozutsumi, and et al. Interleukin-2-induced survival of natural killer (NK) cells involving phosphatidylinositol-3 kinase-dependent reduction of ceramide through acid sphingomyelinase, sphingomyelin synthase, and glucosylceramide synthase Blood 104 10 2004 3285 3293
    • (2004) Blood , vol.104 , Issue.10 , pp. 3285-3293
    • Taguchi, Y.1    Kondo, T.2    Watanabe, M.3    Miyaji, M.4    Umehara, H.5    Kozutsumi, Y.6
  • 43
    • 84859997471 scopus 로고    scopus 로고
    • CD4+ T-cell dysfunctions through the impaired lipid rafts ameliorate concanavalin A-induced hepatitis in sphingomyelin synthase 1-knockout mice
    • L. Dong, K. Watanabe, M. Itoh, C.R. Huan, X.P. Tong, T. Nakamura, and et al. CD4+ T-cell dysfunctions through the impaired lipid rafts ameliorate concanavalin A-induced hepatitis in sphingomyelin synthase 1-knockout mice Int Immunol 24 5 2012 327 337
    • (2012) Int Immunol , vol.24 , Issue.5 , pp. 327-337
    • Dong, L.1    Watanabe, K.2    Itoh, M.3    Huan, C.R.4    Tong, X.P.5    Nakamura, T.6
  • 44
    • 0039518668 scopus 로고    scopus 로고
    • Structure and functional properties of diacylglycerols in membranes
    • F.M. Goñi, and A. Alonso Structure and functional properties of diacylglycerols in membranes Prog Lipid Res 38 1 1999 1 48
    • (1999) Prog Lipid Res , vol.38 , Issue.1 , pp. 1-48
    • Goñi, F.M.1    Alonso, A.2
  • 45
    • 34247523293 scopus 로고    scopus 로고
    • Nuclear diacylglycerol kinases: Emerging downstream regulators in cell signaling networks
    • C. Evangelisti, R. Bortul, F. Falà, G. Tabellini, K. Goto, and A.M. Martelli Nuclear diacylglycerol kinases: Emerging downstream regulators in cell signaling networks Histol Histopathol 22 5 2007 573 579
    • (2007) Histol Histopathol , vol.22 , Issue.5 , pp. 573-579
    • Evangelisti, C.1    Bortul, R.2    Falà, F.3    Tabellini, G.4    Goto, K.5    Martelli, A.M.6
  • 46
    • 0033004404 scopus 로고    scopus 로고
    • Phosphatidylethanolamine and phosphatidylcholine are sources of diacylglycerol in ras-transformed NIH 3T3 fibroblasts
    • A. Momchilova, and T. Markovska Phosphatidylethanolamine and phosphatidylcholine are sources of diacylglycerol in ras-transformed NIH 3T3 fibroblasts Int J Biochem Cell Biol 31 2 1999 311 318
    • (1999) Int J Biochem Cell Biol , vol.31 , Issue.2 , pp. 311-318
    • Momchilova, A.1    Markovska, T.2
  • 47
    • 62049085281 scopus 로고    scopus 로고
    • Sphingomyelin synthase 2 is palmitoylated at the COOH-terminal tail, which is involved in its localization in plasma membranes
    • M. Tani, and O. Kuge Sphingomyelin synthase 2 is palmitoylated at the COOH-terminal tail, which is involved in its localization in plasma membranes Biochem Biophys Res Commun 381 3 2009 328 332
    • (2009) Biochem Biophys Res Commun , vol.381 , Issue.3 , pp. 328-332
    • Tani, M.1    Kuge, O.2
  • 49
    • 70350383478 scopus 로고    scopus 로고
    • Sphingomyelin synthase SMS2 displays dual activity as ceramide phosphoethanolamine synthase
    • P. Ternes, J.F. Brouwers, J. van den Dikkenberg, and J.C. Holthuis Sphingomyelin synthase SMS2 displays dual activity as ceramide phosphoethanolamine synthase J Lipid Res 50 11 2009 2270 2277
    • (2009) J Lipid Res , vol.50 , Issue.11 , pp. 2270-2277
    • Ternes, P.1    Brouwers, J.F.2    Van Den Dikkenberg, J.3    Holthuis, J.C.4
  • 50
    • 84856017726 scopus 로고    scopus 로고
    • Differential localization of sphingomyelin synthase isoforms in neurons regulates sphingomyelin cluster formation
    • Y. Kidani, K. Ohshima, H. Sakai, T. Kohno, A. Baba, and M. Hattori Differential localization of sphingomyelin synthase isoforms in neurons regulates sphingomyelin cluster formation Biochem Biophys Res Commun 417 3 2012 1014 1017
    • (2012) Biochem Biophys Res Commun , vol.417 , Issue.3 , pp. 1014-1017
    • Kidani, Y.1    Ohshima, K.2    Sakai, H.3    Kohno, T.4    Baba, A.5    Hattori, M.6
  • 51
    • 80955180545 scopus 로고    scopus 로고
    • The effect of sphingomyelin synthase 2 (SMS2) deficiency on the expression of drug transporters in mouse brain
    • Y. Zhang, J. Dong, X. Zhu, W. Wang, and Q. Yang The effect of sphingomyelin synthase 2 (SMS2) deficiency on the expression of drug transporters in mouse brain Biochem Pharmacol 82 3 2011 287 294
    • (2011) Biochem Pharmacol , vol.82 , Issue.3 , pp. 287-294
    • Zhang, Y.1    Dong, J.2    Zhu, X.3    Wang, W.4    Yang, Q.5
  • 52
    • 67449147119 scopus 로고    scopus 로고
    • Sphingomyelin synthase-related protein SMSr controls ceramide homeostasis in the ER
    • A.M. Vacaru, F.G. Tafesse, P. Ternes, V. Kondylis, M. Hermansson, J.F. Brouwers, and et al. Sphingomyelin synthase-related protein SMSr controls ceramide homeostasis in the ER J Cell Biol 185 6 2009 1013 1027
    • (2009) J Cell Biol , vol.185 , Issue.6 , pp. 1013-1027
    • Vacaru, A.M.1    Tafesse, F.G.2    Ternes, P.3    Kondylis, V.4    Hermansson, M.5    Brouwers, J.F.6
  • 53
    • 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 et al. 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 7 1998 4081 4088
    • (1998) J Biol Chem , vol.273 , Issue.7 , pp. 4081-4088
    • Marathe, S.1    Schissel, S.L.2    Yellin, M.J.3    Beatini, N.4    Mintzer, R.5    Williams, K.J.6
  • 54
    • 0029666484 scopus 로고    scopus 로고
    • 2+-stimulated sphingomyelinase is secreted by many cell types and is a product of the acid sphingomyelinase gene
    • 2+-stimulated sphingomyelinase is secreted by many cell types and is a product of the acid sphingomyelinase gene J Biol Chem 271 31 1996 18431 18436
    • (1996) J Biol Chem , vol.271 , Issue.31 , pp. 18431-18436
    • Schissel, S.L.1    Schuchman, E.H.2    Williams, K.J.3    Tabas, I.4
  • 55
    • 0031020869 scopus 로고    scopus 로고
    • Functional characterization of the N-glycosylation sites of human acid sphingomyelinase by site-directed mutagenesis
    • K. Ferlinz, R. Hurwitz, H. Moczall, S. Lansmann, E.H. Schuchman, and K. Sandhoff Functional characterization of the N-glycosylation sites of human acid sphingomyelinase by site-directed mutagenesis Eur J Biochem 243 1-2 1997 511 517
    • (1997) Eur J Biochem , vol.243 , Issue.1-2 , pp. 511-517
    • Ferlinz, K.1    Hurwitz, R.2    Moczall, H.3    Lansmann, S.4    Schuchman, E.H.5    Sandhoff, K.6
  • 56
    • 0032579258 scopus 로고    scopus 로고
    • Secretory sphingomyelinase, a product of the acid sphingomyelinase gene, can hydrolyze atherogenic lipoproteins at neutral pH. Implications for atherosclerotic lesion development
    • S.L. Schissel, X. Jiang, J. Tweedie-Hardman, T. Jeong, E.H. Camejo, J. Najib, and et al. Secretory sphingomyelinase, a product of the acid sphingomyelinase gene, can hydrolyze atherogenic lipoproteins at neutral pH. Implications for atherosclerotic lesion development J Biol Chem 273 5 1998 2738 2746
    • (1998) J Biol Chem , vol.273 , Issue.5 , pp. 2738-2746
    • Schissel, S.L.1    Jiang, X.2    Tweedie-Hardman, J.3    Jeong, T.4    Camejo, E.H.5    Najib, J.6
  • 59
    • 0034268524 scopus 로고    scopus 로고
    • Distribution of acid sphingomyelinase in human various body fluids
    • I. Takahashi, T. Takahashi, T. Abe, W. Watanabe, and G. Takada Distribution of acid sphingomyelinase in human various body fluids Tohoku J Exp Med 192 1 2000 61 66
    • (2000) Tohoku J Exp Med , vol.192 , Issue.1 , pp. 61-66
    • Takahashi, I.1    Takahashi, T.2    Abe, T.3    Watanabe, W.4    Takada, G.5
  • 60
    • 84877066567 scopus 로고    scopus 로고
    • Characterization of acid sphingomyelinase activity in human cerebrospinal fluid
    • C. Mühle, H.B. Huttner, S. Walter, M. Reichel, F. Canneva, P. Lewczuk, and et al. Characterization of acid sphingomyelinase activity in human cerebrospinal fluid PLOS ONE 8 5 2013 e62912
    • (2013) PLOS ONE , vol.8 , Issue.5 , pp. e62912
    • Mühle, C.1    Huttner, H.B.2    Walter, S.3    Reichel, M.4    Canneva, F.5    Lewczuk, P.6
  • 61
    • 0032524380 scopus 로고    scopus 로고
    • Sphingomyelinase activity in human platelets
    • C.G Simon Jr., S. Chatterjee, and A.R. Gear Sphingomyelinase activity in human platelets Thromb Res 90 4 1998 155 161
    • (1998) Thromb Res , vol.90 , Issue.4 , pp. 155-161
    • Simon, C.G.1    Chatterjee, S.2    Gear, A.R.3
  • 62
    • 0033994563 scopus 로고    scopus 로고
    • Characterization of sphingomyelinase activity released by thrombin-stimulated platelets
    • E. Romiti, V. Vasta, E. Meacci, M. Farnararo, T. Linke, K. Ferlinz, and et al. Characterization of sphingomyelinase activity released by thrombin-stimulated platelets Mol Cell Biochem 205 1-2 2000 75 81
    • (2000) Mol Cell Biochem , vol.205 , Issue.1-2 , pp. 75-81
    • Romiti, E.1    Vasta, V.2    Meacci, E.3    Farnararo, M.4    Linke, T.5    Ferlinz, K.6
  • 63
    • 0031398349 scopus 로고    scopus 로고
    • Sphingomyelinase increases 2-deoxyglucose uptake and glucose metabolism of human platelets
    • V. Vasta, E. Meacci, E. Romiti, M. Farnararo, and P. Bruni Sphingomyelinase increases 2-deoxyglucose uptake and glucose metabolism of human platelets Biochem Mol Biol Int 43 1 1997 217 226
    • (1997) Biochem Mol Biol Int , vol.43 , Issue.1 , pp. 217-226
    • Vasta, V.1    Meacci, E.2    Romiti, E.3    Farnararo, M.4    Bruni, P.5
  • 64
    • 84891835630 scopus 로고    scopus 로고
    • Acid sphingomyelinase regulates platelet cell membrane scrambling, secretion, and thrombus formation
    • P. Münzer, O. Borst, B. Walker, E. Schmid, M.A. Feijge, J.M. Cosemans, and et al. Acid sphingomyelinase regulates platelet cell membrane scrambling, secretion, and thrombus formation Arterioscler Thromb Vasc Biol 34 1 2014 61 71
    • (2014) Arterioscler Thromb Vasc Biol , vol.34 , Issue.1 , pp. 61-71
    • Münzer, P.1    Borst, O.2    Walker, B.3    Schmid, E.4    Feijge, M.A.5    Cosemans, J.M.6
  • 65
    • 0034667994 scopus 로고    scopus 로고
    • Acceleration by ceramide of calcium-dependent translocation of phospholipase A2 from cytosol to membranes in platelets
    • K. Kitatani, T. Oka, T. Murata, M. Hayama, S. Akiba, and T. Sato Acceleration by ceramide of calcium-dependent translocation of phospholipase A2 from cytosol to membranes in platelets Arch Biochem Biophys 382 2 2000 296 302
    • (2000) Arch Biochem Biophys , vol.382 , Issue.2 , pp. 296-302
    • Kitatani, K.1    Oka, T.2    Murata, T.3    Hayama, M.4    Akiba, S.5    Sato, T.6
  • 67
    • 0032584153 scopus 로고    scopus 로고
    • Cloned mammalian neutral sphingomyelinase: Functions in sphingolipid signaling?
    • S. Tomiuk, K. Hofmann, M. Nix, M. Zumbansen, and W. Stoffel Cloned mammalian neutral sphingomyelinase: Functions in sphingolipid signaling? Proc Natl Acad Sci USA 95 7 1998 3638 3643
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.7 , pp. 3638-3643
    • Tomiuk, S.1    Hofmann, K.2    Nix, M.3    Zumbansen, M.4    Stoffel, W.5
  • 68
    • 34248221744 scopus 로고    scopus 로고
    • Neutral sphingomyelinase 2 is palmitoylated on multiple cysteine residues. Role of palmitoylation in subcellular localization
    • M. Tani, and Y.A. Hannun Neutral sphingomyelinase 2 is palmitoylated on multiple cysteine residues. Role of palmitoylation in subcellular localization J Biol Chem 282 13 2007 10047 10056
    • (2007) J Biol Chem , vol.282 , Issue.13 , pp. 10047-10056
    • Tani, M.1    Hannun, Y.A.2
  • 69
    • 26444530166 scopus 로고    scopus 로고
    • Age-related changes in neutral sphingomyelin-specific phospholipase C activity in striatum, hippocampus, and frontal cortex: Implication for sensitivity to stress and inflammation
    • N.A. Crivello, I.H. Rosenberg, G.E. Dallal, D. Bielinski, and J.A. Joseph Age-related changes in neutral sphingomyelin-specific phospholipase C activity in striatum, hippocampus, and frontal cortex: Implication for sensitivity to stress and inflammation Neurochem Int 47 8 2005 573 579
    • (2005) Neurochem Int , vol.47 , Issue.8 , pp. 573-579
    • Crivello, N.A.1    Rosenberg, I.H.2    Dallal, G.E.3    Bielinski, D.4    Joseph, J.A.5
  • 70
    • 15444369953 scopus 로고    scopus 로고
    • Neutral sphingomyelinase 2 (smpd3) in the control of postnatal growth and development
    • W. Stoffel, B. Jenke, B. Blöck, M. Zumbansen, and J. Koebke Neutral sphingomyelinase 2 (smpd3) in the control of postnatal growth and development Proc Natl Acad Sci USA 102 12 2005 4554 4559
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.12 , pp. 4554-4559
    • Stoffel, W.1    Jenke, B.2    Blöck, B.3    Zumbansen, M.4    Koebke, J.5
  • 71
    • 65549128703 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha-induced neutral sphingomyelinase-2 modulates synaptic plasticity by controlling the membrane insertion of NMDA receptors
    • D. Wheeler, E. Knapp, V.V. Bandaru, Y. Wang, D. Knorr, C. Poirier, and et al. Tumor necrosis factor-alpha-induced neutral sphingomyelinase-2 modulates synaptic plasticity by controlling the membrane insertion of NMDA receptors J Neurochem 109 5 2009 1237 1249
    • (2009) J Neurochem , vol.109 , Issue.5 , pp. 1237-1249
    • Wheeler, D.1    Knapp, E.2    Bandaru, V.V.3    Wang, Y.4    Knorr, D.5    Poirier, C.6
  • 72
    • 77951915608 scopus 로고    scopus 로고
    • Neutral sphingomyelinase 2 induces dopamine uptake through regulation of intracellular calcium
    • S.K. Kim, K.H. Ahn, J.E. Ji, J.M. Choi, H.J. Jeon, S.Y. Jung, and et al. Neutral sphingomyelinase 2 induces dopamine uptake through regulation of intracellular calcium Cell Signal 22 5 2010 865 870
    • (2010) Cell Signal , vol.22 , Issue.5 , pp. 865-870
    • Kim, S.K.1    Ahn, K.H.2    Ji, J.E.3    Choi, J.M.4    Jeon, H.J.5    Jung, S.Y.6
  • 73
    • 0034042058 scopus 로고    scopus 로고
    • Sphingomyelinase ceramide analogs induce contraction and rises in [Ca(2+)](i) in canine cerebral vascular muscle
    • T. Zheng, W. Li, J. Wang, B.T. Altura, and B.M. Altura Sphingomyelinase ceramide analogs induce contraction and rises in [Ca(2+)](i) in canine cerebral vascular muscle Am J Physiol Heart Circ Physiol 278 5 2000 H1421 H1428
    • (2000) Am J Physiol Heart Circ Physiol , vol.278 , Issue.5 , pp. H1421-H1428
    • Zheng, T.1    Li, W.2    Wang, J.3    Altura, B.T.4    Altura, B.M.5
  • 75
    • 11844265943 scopus 로고    scopus 로고
    • Sphingomyelinase causes endothelium-dependent vasorelaxation through endothelial nitric oxide production without cytosolic Ca(2+) elevation
    • K. Mogami, H. Kishi, and S. Kobayashi Sphingomyelinase causes endothelium-dependent vasorelaxation through endothelial nitric oxide production without cytosolic Ca(2+) elevation FEBS Lett 579 2 2005 393 397
    • (2005) FEBS Lett , vol.579 , Issue.2 , pp. 393-397
    • Mogami, K.1    Kishi, H.2    Kobayashi, S.3
  • 76
    • 84919663439 scopus 로고    scopus 로고
    • Neutral sphingomyelinase in physiological and measles virus induced T cell suppression
    • N. Mueller, E. Avota, L. Collenburg, H. Grassmé, and S. Schneider-Schaulies Neutral sphingomyelinase in physiological and measles virus induced T cell suppression PLoS Pathog 10 12 2014 e1004574
    • (2014) PLoS Pathog , vol.10 , Issue.12 , pp. e1004574
    • Mueller, N.1    Avota, E.2    Collenburg, L.3    Grassmé, H.4    Schneider-Schaulies, S.5
  • 77
    • 84926611875 scopus 로고    scopus 로고
    • Sphingolipid metabolism and its role in the skeletal tissues
    • Z. Khavandgar, and M. Murshed Sphingolipid metabolism and its role in the skeletal tissues Cell Mol Life Sci 72 5 2015 959 969
    • (2015) Cell Mol Life Sci , vol.72 , Issue.5 , pp. 959-969
    • Khavandgar, Z.1    Murshed, M.2
  • 78
    • 23044482222 scopus 로고    scopus 로고
    • A deletion in the gene encoding sphingomyelin phosphodiesterase 3 (Smpd3) results in osteogenesis and dentinogenesis imperfecta in the mouse
    • I. Aubin, C.P. Adams, S. Opsahl, D. Septier, C.E. Bishop, N. Auge, and et al. A deletion in the gene encoding sphingomyelin phosphodiesterase 3 (Smpd3) results in osteogenesis and dentinogenesis imperfecta in the mouse Nat Genet 37 8 2005 803 805
    • (2005) Nat Genet , vol.37 , Issue.8 , pp. 803-805
    • Aubin, I.1    Adams, C.P.2    Opsahl, S.3    Septier, D.4    Bishop, C.E.5    Auge, N.6
  • 79
    • 34547653109 scopus 로고    scopus 로고
    • Neutral sphingomyelinase (SMPD3) deficiency causes a novel form of chondrodysplasia and dwarfism that is rescued by Col2A1-driven smpd3 transgene expression
    • W. Stoffel, B. Jenke, B. Holz, E. Binczek, R.H. Günter, J. Knifka, and et al. Neutral sphingomyelinase (SMPD3) deficiency causes a novel form of chondrodysplasia and dwarfism that is rescued by Col2A1-driven smpd3 transgene expression Am J Pathol 171 1 2007 153 161
    • (2007) Am J Pathol , vol.171 , Issue.1 , pp. 153-161
    • Stoffel, W.1    Jenke, B.2    Holz, B.3    Binczek, E.4    Günter, R.H.5    Knifka, J.6
  • 80
    • 0034102425 scopus 로고    scopus 로고
    • Characterization and subcellular localization of murine and human magnesium-dependent neutral sphingomyelinase
    • S. Tomiuk, M. Zumbansen, and W. Stoffel Characterization and subcellular localization of murine and human magnesium-dependent neutral sphingomyelinase J Biol Chem 275 8 2000 5710 5717
    • (2000) J Biol Chem , vol.275 , Issue.8 , pp. 5710-5717
    • Tomiuk, S.1    Zumbansen, M.2    Stoffel, W.3
  • 81
    • 0034759191 scopus 로고    scopus 로고
    • Nuclear localization of neutral sphingomyelinase 1: Biochemical and immunocytochemical analyses
    • Y. Mizutani, K. Tamiya-Koizumi, N. Nakamura, M. Kobayashi, Y. Hirabayashi, and S. Yoshida Nuclear localization of neutral sphingomyelinase 1: Biochemical and immunocytochemical analyses J Cell Sci 114 Pt 20 2001 3727 3736
    • (2001) J Cell Sci , vol.114 , pp. 3727-3736
    • Mizutani, Y.1    Tamiya-Koizumi, K.2    Nakamura, N.3    Kobayashi, M.4    Hirabayashi, Y.5    Yoshida, S.6
  • 82
    • 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 53 1999 38131 38139
    • (1999) J Biol Chem , vol.274 , Issue.53 , pp. 38131-38139
    • Sawai, H.1    Domae, N.2    Nagan, N.3    Hannun, Y.A.4
  • 83
    • 0036097252 scopus 로고    scopus 로고
    • Neutral sphingomyelinase 1 deficiency in the mouse causes no lipid storage disease
    • M. Zumbansen, and W. Stoffel Neutral sphingomyelinase 1 deficiency in the mouse causes no lipid storage disease Mol Cell Biol 22 11 2002 3633 3638
    • (2002) Mol Cell Biol , vol.22 , Issue.11 , pp. 3633-3638
    • Zumbansen, M.1    Stoffel, W.2
  • 84
    • 0033577806 scopus 로고    scopus 로고
    • A role for neutral sphingomyelinase-mediated ceramide production in T cell receptor-induced apoptosis and mitogen-activated protein kinase-mediated signal transduction
    • L. Tonnetti, M.C. Verí, E. Bonvini, and L. D'Adamio A role for neutral sphingomyelinase-mediated ceramide production in T cell receptor-induced apoptosis and mitogen-activated protein kinase-mediated signal transduction J Exp Med 189 10 1999 1581 1589
    • (1999) J Exp Med , vol.189 , Issue.10 , pp. 1581-1589
    • Tonnetti, L.1    Verí, M.C.2    Bonvini, E.3    D'Adamio, L.4
  • 85
    • 57649210164 scopus 로고    scopus 로고
    • 2+-dependent neutral sphingomyelinase 1 as a mediator of heat stress-induced ceramide generation and apoptosis
    • 2+-dependent neutral sphingomyelinase 1 as a mediator of heat stress-induced ceramide generation and apoptosis J Biol Chem 283 44 2008 29971 29982
    • (2008) J Biol Chem , vol.283 , Issue.44 , pp. 29971-29982
    • Yabu, T.1    Imamura, S.2    Yamashita, M.3    Okazaki, T.4
  • 86
    • 84922749204 scopus 로고    scopus 로고
    • Stress-induced ceramide generation and apoptosis via the phosphorylation and activation of nSMase1 by JNK signaling
    • T. Yabu, H. Shiba, Y. Shibasaki, T. Nakanishi, S. Imamura, K. Touhata, and et al. Stress-induced ceramide generation and apoptosis via the phosphorylation and activation of nSMase1 by JNK signaling Cell Death Differ 22 2 2015 258 273
    • (2015) Cell Death Differ , vol.22 , Issue.2 , pp. 258-273
    • Yabu, T.1    Shiba, H.2    Shibasaki, Y.3    Nakanishi, T.4    Imamura, S.5    Touhata, K.6
  • 87
    • 84922340030 scopus 로고    scopus 로고
    • The neutral sphingomyelinase pathway regulates packaging of the prion protein into exosomes
    • B.B. Guo, S.A. Bellingham, and A.F. Hill The neutral sphingomyelinase pathway regulates packaging of the prion protein into exosomes J Biol Chem 290 6 2015 3455 3467
    • (2015) J Biol Chem , vol.290 , Issue.6 , pp. 3455-3467
    • Guo, B.B.1    Bellingham, S.A.2    Hill, A.F.3
  • 88
    • 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. Krönke Novel tumor necrosis factor-responsive mammalian neutral sphingomyelinase-3 is a C-tail-anchored protein J Biol Chem 281 19 2006 13784 13793
    • (2006) J Biol Chem , vol.281 , Issue.19 , pp. 13784-13793
    • Krut, O.1    Wiegmann, K.2    Kashkar, H.3    Yazdanpanah, B.4    Krönke, M.5
  • 89
    • 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 5 2008 795 807
    • (2008) Mol Cancer Res , vol.6 , Issue.5 , pp. 795-807
    • Corcoran, C.A.1    He, Q.2    Ponnusamy, S.3    Ogretmen, B.4    Huang, Y.5    Sheikh, M.S.6
  • 91
    • 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 23 2010 17993 18002
    • (2010) J Biol Chem , vol.285 , Issue.23 , pp. 17993-18002
    • Wu, B.X.1    Rajagopalan, V.2    Roddy, P.L.3    Clarke, C.J.4    Hannun, Y.A.5
  • 92
    • 84921033866 scopus 로고    scopus 로고
    • Critical determinants of mitochondria-associated neutral sphingomyelinase (MA-nSMase) for mitochondrial localization
    • V. Rajagopalan, D. Canals, C. Luberto, J. Snider, C. Voelkel-Johnson, L.M. Obeid, and et al. Critical determinants of mitochondria-associated neutral sphingomyelinase (MA-nSMase) for mitochondrial localization Biochim Biophys Acta 1850 4 2015 628 639
    • (2015) Biochim Biophys Acta , vol.1850 , Issue.4 , pp. 628-639
    • Rajagopalan, V.1    Canals, D.2    Luberto, C.3    Snider, J.4    Voelkel-Johnson, C.5    Obeid, L.M.6
  • 93
    • 15944425766 scopus 로고    scopus 로고
    • A mitochondrial pool of sphingomyelin is involved in TNFalpha-induced Bax translocation to mitochondria
    • H. Birbes, C. Luberto, Y.T. Hsu, S. El Bawab, Y.A. Hannun, and L.M. Obeid A mitochondrial pool of sphingomyelin is involved in TNFalpha-induced Bax translocation to mitochondria Biochem J 386 Pt 3 2005 445 451
    • (2005) Biochem J , vol.386 , pp. 445-451
    • Birbes, H.1    Luberto, C.2    Hsu, Y.T.3    El Bawab, S.4    Hannun, Y.A.5    Obeid, L.M.6
  • 94
    • 58149471607 scopus 로고    scopus 로고
    • Lipid levels in sperm, eggs, and during fertilization in Xenopus laevis
    • D.W. Petcoff, W.L. Holland, and B.J. Stith Lipid levels in sperm, eggs, and during fertilization in Xenopus laevis J Lipid Res 49 11 2008 2365 2378
    • (2008) J Lipid Res , vol.49 , Issue.11 , pp. 2365-2378
    • Petcoff, D.W.1    Holland, W.L.2    Stith, B.J.3
  • 95
    • 34547125599 scopus 로고    scopus 로고
    • Very long-chain polyunsaturated fatty acids are the major acyl groups of sphingomyelins and ceramides in the head of mammalian spermatozoa
    • N.E. Furland, G.M. Oresti, S.S. Antollini, A. Venturino, E.N. Maldonado, and M.I. Aveldanõ Very long-chain polyunsaturated fatty acids are the major acyl groups of sphingomyelins and ceramides in the head of mammalian spermatozoa J Biol Chem 282 25 2007 18151 18161
    • (2007) J Biol Chem , vol.282 , Issue.25 , pp. 18151-18161
    • Furland, N.E.1    Oresti, G.M.2    Antollini, S.S.3    Venturino, A.4    Maldonado, E.N.5    Aveldanõ, M.I.6
  • 96
    • 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, and et al. Identification of human intestinal alkaline sphingomyelinase as a novel ecto-enzyme related to the nucleotide phosphodiesterase family J Biol Chem 278 40 2003 38528 38536
    • (2003) J Biol Chem , vol.278 , Issue.40 , pp. 38528-38536
    • Duan, R.D.1    Bergman, T.2    Xu, N.3    Wu, J.4    Cheng, Y.5    Duan, J.6
  • 97
    • 0030828425 scopus 로고    scopus 로고
    • Purification of a newly identified alkaline sphingomyelinase in human bile and effects of bile salts and phosphatidylcholine on enzyme activity
    • R.D. Duan, and A. Nilsson Purification of a newly identified alkaline sphingomyelinase in human bile and effects of bile salts and phosphatidylcholine on enzyme activity Hepatology 26 4 1997 823 830
    • (1997) Hepatology , vol.26 , Issue.4 , pp. 823-830
    • Duan, R.D.1    Nilsson, A.2
  • 98
    • 0030964872 scopus 로고    scopus 로고
    • Localization and capacity of sphingomyelin digestion in the rat intestinal tract
    • L. Nyberg, A. Nilsson, P. Lundgren, and R.D. Duan Localization and capacity of sphingomyelin digestion in the rat intestinal tract J Nutr Biochem 8 3 1997 112 118
    • (1997) J Nutr Biochem , vol.8 , Issue.3 , pp. 112-118
    • Nyberg, L.1    Nilsson, A.2    Lundgren, P.3    Duan, R.D.4
  • 99
    • 0029780817 scopus 로고    scopus 로고
    • Sphingomyelin changes in rat cerebral cortex during focal ischemia
    • M. Kubota, K. Narita, T. Nakagomi, A. Tamura, H. Shimasaki, N. Ueta, and et al. Sphingomyelin changes in rat cerebral cortex during focal ischemia Neurol Res 18 4 1996 337 341
    • (1996) Neurol Res , vol.18 , Issue.4 , pp. 337-341
    • Kubota, M.1    Narita, K.2    Nakagomi, T.3    Tamura, A.4    Shimasaki, H.5    Ueta, N.6
  • 100
    • 0034704409 scopus 로고    scopus 로고
    • Lethal forebrain ischemia stimulates sphingomyelin hydrolysis and ceramide generation in the gerbil hippocampus
    • M. Nakane, M. Kubota, T. Nakagomi, A. Tamura, H. Hisaki, H. Shimasaki, and et al. Lethal forebrain ischemia stimulates sphingomyelin hydrolysis and ceramide generation in the gerbil hippocampus Neurosci Lett 296 2-3 2000 89 92
    • (2000) Neurosci Lett , vol.296 , Issue.2-3 , pp. 89-92
    • Nakane, M.1    Kubota, M.2    Nakagomi, T.3    Tamura, A.4    Hisaki, H.5    Shimasaki, H.6
  • 101
    • 70450198177 scopus 로고    scopus 로고
    • Sphingomyelinase-induced ceramide production stimulate calcium-independent JNK and PP2A activation following cerebral ischemia
    • H.P. Tian, T.Z. Qiu, J. Zhao, L.X. Li, and J. Guo Sphingomyelinase-induced ceramide production stimulate calcium-independent JNK and PP2A activation following cerebral ischemia Brain Inj 23 13-14 2009 1073 1080
    • (2009) Brain Inj , vol.23 , Issue.13-14 , pp. 1073-1080
    • Tian, H.P.1    Qiu, T.Z.2    Zhao, J.3    Li, L.X.4    Guo, J.5
  • 102
    • 3042599022 scopus 로고    scopus 로고
    • Inhibition of sphingomyelinase activity helps to prevent neuron death caused by ischemic stress
    • S. Soeda, Y. Tsuji, T. Ochiai, K. Mishima, K. Iwasaki, M. Fujiwara, and et al. Inhibition of sphingomyelinase activity helps to prevent neuron death caused by ischemic stress Neurochem Int 45 5 2004 619 626
    • (2004) Neurochem Int , vol.45 , Issue.5 , pp. 619-626
    • Soeda, S.1    Tsuji, Y.2    Ochiai, T.3    Mishima, K.4    Iwasaki, K.5    Fujiwara, M.6
  • 103
    • 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 51 1998 34472 34479
    • (1998) J Biol Chem , vol.273 , Issue.51 , pp. 34472-34479
    • Liu, B.1    Hassler, D.F.2    Smith, G.K.3    Weaver, K.4    Hannun, Y.A.5
  • 104
    • 15144359445 scopus 로고    scopus 로고
    • Ceramide formation leads to caspase-3 activation during hypoxic PC12 cell death. Inhibitory effects of Bcl-2 on ceramide formation and caspase-3 activation
    • S. Yoshimura, Y. Banno, S. Nakashima, K. Takenaka, H. Sakai, Y. Nishimura, and et al. Ceramide formation leads to caspase-3 activation during hypoxic PC12 cell death. Inhibitory effects of Bcl-2 on ceramide formation and caspase-3 activation J Biol Chem 273 12 1998 6921 6927
    • (1998) J Biol Chem , vol.273 , Issue.12 , pp. 6921-6927
    • Yoshimura, S.1    Banno, Y.2    Nakashima, S.3    Takenaka, K.4    Sakai, H.5    Nishimura, Y.6
  • 105
    • 0032797821 scopus 로고    scopus 로고
    • Inhibition of neutral sphingomyelinase activation and ceramide formation by glutathione in hypoxic PC12 cell death
    • S. Yoshimura, Y. Banno, S. Nakashima, K. Hayashi, H. Yamakawa, M. Sawada, and et al. Inhibition of neutral sphingomyelinase activation and ceramide formation by glutathione in hypoxic PC12 cell death J Neurochem 73 2 1999 675 683
    • (1999) J Neurochem , vol.73 , Issue.2 , pp. 675-683
    • Yoshimura, S.1    Banno, Y.2    Nakashima, S.3    Hayashi, K.4    Yamakawa, H.5    Sawada, M.6
  • 106
    • 0034677881 scopus 로고    scopus 로고
    • Purification and characterization of a magnesium-dependent neutral sphingomyelinase from bovine brain
    • K. Bernardo, O. Krut, K. Wiegmann, D. Kreder, M. Micheli, R. Schäfer, and et al. Purification and characterization of a magnesium-dependent neutral sphingomyelinase from bovine brain J Biol Chem 275 11 2000 7641 7647
    • (2000) J Biol Chem , vol.275 , Issue.11 , pp. 7641-7647
    • Bernardo, K.1    Krut, O.2    Wiegmann, K.3    Kreder, D.4    Micheli, M.5    Schäfer, R.6
  • 107
    • 84883261205 scopus 로고    scopus 로고
    • Early activation of nSMase2/ceramide pathway in astrocytes is involved in ischemia-associated neuronal damage via inflammation in rat hippocampi
    • L. Gu, B. Huang, W. Shen, L. Gao, Z. Ding, H. Wu, and et al. Early activation of nSMase2/ceramide pathway in astrocytes is involved in ischemia-associated neuronal damage via inflammation in rat hippocampi J Neuroinflammation 10 2013 109
    • (2013) J Neuroinflammation , vol.10 , pp. 109
    • Gu, L.1    Huang, B.2    Shen, W.3    Gao, L.4    Ding, Z.5    Wu, H.6
  • 108
    • 4444374382 scopus 로고    scopus 로고
    • Upregulation of ceramide and its regulating mechanism in a rat model of chronic cerebral ischemia
    • R. Ohtani, H. Tomimoto, T. Kondo, H. Wakita, I. Akiguchi, H. Shibasaki, and et al. Upregulation of ceramide and its regulating mechanism in a rat model of chronic cerebral ischemia Brain Res 1023 1 2004 31 40
    • (2004) Brain Res , vol.1023 , Issue.1 , pp. 31-40
    • Ohtani, R.1    Tomimoto, H.2    Kondo, T.3    Wakita, H.4    Akiguchi, I.5    Shibasaki, H.6
  • 109
    • 84977918350 scopus 로고    scopus 로고
    • Calpain-mediated Hsp70.1 cleavage in monkey CA1 after ischemia induces similar 'lysosomal vesiculosis' to Alzheimer neurons
    • T. Yamashima, A. Mathivanan, M.Y. Dazortsava, S. Sakai, S. Kurimoto, H. Zhu, and et al. Calpain-mediated Hsp70.1 cleavage in monkey CA1 after ischemia induces similar 'lysosomal vesiculosis' to Alzheimer neurons J Alzheimers Dis Parkinsonism 4 2014 139
    • (2014) J Alzheimers Dis Parkinsonism , vol.4 , pp. 139
    • Yamashima, T.1    Mathivanan, A.2    Dazortsava, M.Y.3    Sakai, S.4    Kurimoto, S.5    Zhu, H.6
  • 110
    • 0034488193 scopus 로고    scopus 로고
    • Pivotal role for acidic sphingomyelinase in cerebral ischemia-induced ceramide and cytokine production, and neuronal apoptosis
    • Z.F. Yu, M. Nikolova-Karakashian, D. Zhou, G. Cheng, E.H. Schuchman, and M.P. Mattson Pivotal role for acidic sphingomyelinase in cerebral ischemia-induced ceramide and cytokine production, and neuronal apoptosis J Mol Neurosci 15 2 2000 85 97
    • (2000) J Mol Neurosci , vol.15 , Issue.2 , pp. 85-97
    • Yu, Z.F.1    Nikolova-Karakashian, M.2    Zhou, D.3    Cheng, G.4    Schuchman, E.H.5    Mattson, M.P.6
  • 111
    • 34548478108 scopus 로고    scopus 로고
    • JNK3 signaling pathway activates ceramide synthase leading to mitochondrial dysfunction
    • J. Yu, S.A. Novgorodov, D. Chudakova, H. Zhu, A. Bielawska, J. Bielawski, and et al. JNK3 signaling pathway activates ceramide synthase leading to mitochondrial dysfunction J Biol Chem 282 35 2007 25940 25949
    • (2007) J Biol Chem , vol.282 , Issue.35 , pp. 25940-25949
    • Yu, J.1    Novgorodov, S.A.2    Chudakova, D.3    Zhu, H.4    Bielawska, A.5    Bielawski, J.6
  • 112
    • 55549135019 scopus 로고    scopus 로고
    • Ceramide generated by sphingomyelin hydrolysis and the salvage pathway is involved in hypoxia/reoxygenation-induced Bax redistribution to mitochondria in NT-2 cells
    • J. Jin, Q. Hou, T.D. Mullen, Y.H. Zeidan, J. Bielawski, J.M. Kraveka, and et al. Ceramide generated by sphingomyelin hydrolysis and the salvage pathway is involved in hypoxia/reoxygenation-induced Bax redistribution to mitochondria in NT-2 cells J Biol Chem 283 39 2008 26509 26517
    • (2008) J Biol Chem , vol.283 , Issue.39 , pp. 26509-26517
    • Jin, J.1    Hou, Q.2    Mullen, T.D.3    Zeidan, Y.H.4    Bielawski, J.5    Kraveka, J.M.6
  • 113
    • 84903820413 scopus 로고    scopus 로고
    • Brain lipidomes of subcortical ischemic vascular dementia and mixed dementia
    • S.M. Lam, Y. Wang, X. Duan, M.R. Wenk, R.N. Kalaria, C.P. Chen, and et al. Brain lipidomes of subcortical ischemic vascular dementia and mixed dementia Neurobiol Aging 35 10 2014 2369 2381
    • (2014) Neurobiol Aging , vol.35 , Issue.10 , pp. 2369-2381
    • Lam, S.M.1    Wang, Y.2    Duan, X.3    Wenk, M.R.4    Kalaria, R.N.5    Chen, C.P.6
  • 114
    • 84856072382 scopus 로고    scopus 로고
    • Comparative lipidomic analysis of mouse and human brain with Alzheimer disease
    • R.B. Chan, T.G. Oliveira, E.P. Cortes, L.S. Honig, K.E. Duff, S.A. Small, and et al. Comparative lipidomic analysis of mouse and human brain with Alzheimer disease J Biol Chem 287 4 2012 2678 2688
    • (2012) J Biol Chem , vol.287 , Issue.4 , pp. 2678-2688
    • Chan, R.B.1    Oliveira, T.G.2    Cortes, E.P.3    Honig, L.S.4    Duff, K.E.5    Small, S.A.6
  • 115
    • 80051927751 scopus 로고    scopus 로고
    • Encephalopathy caused by ablation of very long acyl chain ceramide synthesis may be largely due to reduced galactosylceramide levels
    • O. Ben-David, Y. Pewzner-Jung, O. Brenner, E.L. Laviad, A. Kogot-Levin, I. Weissberg, and et al. Encephalopathy caused by ablation of very long acyl chain ceramide synthesis may be largely due to reduced galactosylceramide levels J Biol Chem 286 34 2011 30022 30033
    • (2011) J Biol Chem , vol.286 , Issue.34 , pp. 30022-30033
    • Ben-David, O.1    Pewzner-Jung, Y.2    Brenner, O.3    Laviad, E.L.4    Kogot-Levin, A.5    Weissberg, I.6
  • 116
    • 0030595340 scopus 로고    scopus 로고
    • FAN, a novel WD-repeat protein, couples the p55 TNF-receptor to neutral sphingomyelinase
    • S. Adam-Klages, D. Adam, K. Wiegmann, S. Struve, W. Kolanus, J. Schneider-Mergener, and et al. FAN, a novel WD-repeat protein, couples the p55 TNF-receptor to neutral sphingomyelinase Cell 86 6 1996 937 947
    • (1996) Cell , vol.86 , Issue.6 , pp. 937-947
    • Adam-Klages, S.1    Adam, D.2    Wiegmann, K.3    Struve, S.4    Kolanus, W.5    Schneider-Mergener, J.6
  • 119
    • 77955920223 scopus 로고    scopus 로고
    • Vitamin E regulates SMase activity, GSH levels, and inhibits neuronal death in stroke-prone spontaneously hypertensive rats during hypoxia and reoxygenation
    • K. Yamagata, S. Ichinose, C. Tagawa, and M. Tagami Vitamin E regulates SMase activity, GSH levels, and inhibits neuronal death in stroke-prone spontaneously hypertensive rats during hypoxia and reoxygenation J Exp Stroke Transl Med 2 2 2009 41 48
    • (2009) J Exp Stroke Transl Med , vol.2 , Issue.2 , pp. 41-48
    • Yamagata, K.1    Ichinose, S.2    Tagawa, C.3    Tagami, M.4
  • 120
    • 33646589316 scopus 로고    scopus 로고
    • Sphingolipid signaling and redox regulation
    • J.S. Won, and I. Singh Sphingolipid signaling and redox regulation Free Radic Biol Med 40 11 2006 1875 1888
    • (2006) Free Radic Biol Med , vol.40 , Issue.11 , pp. 1875-1888
    • Won, J.S.1    Singh, I.2
  • 121
    • 84864807841 scopus 로고    scopus 로고
    • Oxidative stress triggers Ca-dependent lysosome trafficking and activation of acid sphingomyelinase
    • X. Li, E. Gulbins, and Y. Zhang Oxidative stress triggers Ca-dependent lysosome trafficking and activation of acid sphingomyelinase Cell Physiol Biochem 30 4 2012 815 826
    • (2012) Cell Physiol Biochem , vol.30 , Issue.4 , pp. 815-826
    • Li, X.1    Gulbins, E.2    Zhang, Y.3
  • 122
    • 84871830994 scopus 로고    scopus 로고
    • Blocking A2B adenosine receptor alleviates pathogenesis of experimental autoimmune encephalomyelitis via inhibition of IL-6 production and Th17 differentiation
    • W. Wei, C. Du, J. Lv, G. Zhao, Z. Li, Z. Wu, and et al. Blocking A2B adenosine receptor alleviates pathogenesis of experimental autoimmune encephalomyelitis via inhibition of IL-6 production and Th17 differentiation J Immunol 190 1 2013 138 146
    • (2013) J Immunol , vol.190 , Issue.1 , pp. 138-146
    • Wei, W.1    Du, C.2    Lv, J.3    Zhao, G.4    Li, Z.5    Wu, Z.6
  • 124
    • 0037010285 scopus 로고    scopus 로고
    • Alzheimer's disease: Beta-amyloid protein and tau
    • M. Morishima-Kawashima, and Y. Ihara Alzheimer's disease: Beta-amyloid protein and tau J Neurosci Res 70 2002 392 401
    • (2002) J Neurosci Res , vol.70 , pp. 392-401
    • Morishima-Kawashima, M.1    Ihara, Y.2
  • 127
    • 84866077130 scopus 로고    scopus 로고
    • Serum ceramides increase the risk of Alzheimer disease: The Women's Health and Aging Study II
    • M.M. Mielke, V.V. Bandaru, N.J. Haughey, J. Xia, L.P. Fried, S. Yasar, and et al. Serum ceramides increase the risk of Alzheimer disease: The Women's Health and Aging Study II Neurology 79 7 2012 633 641
    • (2012) Neurology , vol.79 , Issue.7 , pp. 633-641
    • Mielke, M.M.1    Bandaru, V.V.2    Haughey, N.J.3    Xia, J.4    Fried, L.P.5    Yasar, S.6
  • 128
    • 78650171191 scopus 로고    scopus 로고
    • Nano-HPLC-MS analysis of phospholipids in cerebrospinal fluid of Alzheimer's disease patients-A pilot study
    • M. Kosicek, S. Kirsch, R. Bene, Z. Trkanjec, M. Titlic, L. Bindila, and et al. Nano-HPLC-MS analysis of phospholipids in cerebrospinal fluid of Alzheimer's disease patients-a pilot study Anal Bioanal Chem 398 7-8 2010 2929 2937
    • (2010) Anal Bioanal Chem , vol.398 , Issue.7-8 , pp. 2929-2937
    • Kosicek, M.1    Kirsch, S.2    Bene, R.3    Trkanjec, Z.4    Titlic, M.5    Bindila, L.6
  • 129
    • 84860488306 scopus 로고    scopus 로고
    • Elevated cerebrospinal fluid sphingomyelin levels in prodromal Alzheimer's disease
    • M. Kosicek, H. Zetterberg, N. Andreasen, J. Peter-Katalinic, and S. Hecimovic Elevated cerebrospinal fluid sphingomyelin levels in prodromal Alzheimer's disease Neurosci Lett 516 2 2012 302 305
    • (2012) Neurosci Lett , vol.516 , Issue.2 , pp. 302-305
    • Kosicek, M.1    Zetterberg, H.2    Andreasen, N.3    Peter-Katalinic, J.4    Hecimovic, S.5
  • 130
    • 84922957221 scopus 로고    scopus 로고
    • Cerebrospinal fluid sphingolipids, β-amyloid, and tau in adults at risk for Alzheimer's disease
    • M.M. Mielke, N.J. Haughey, V.V. Bandaru, H. Zetterberg, K. Blennow, U. Andreasson, and et al. Cerebrospinal fluid sphingolipids, β-amyloid, and tau in adults at risk for Alzheimer's disease Neurobiol Aging 35 11 2014 2486 2494
    • (2014) Neurobiol Aging , vol.35 , Issue.11 , pp. 2486-2494
    • Mielke, M.M.1    Haughey, N.J.2    Bandaru, V.V.3    Zetterberg, H.4    Blennow, K.5    Andreasson, U.6
  • 131
    • 0029979095 scopus 로고    scopus 로고
    • Reductions in membrane proteins and lipids in basal ganglia of classic Alzheimer disease patients
    • C.G. Gottfries, B. Jungbjer, I. Karlsson, and L. Svennerholm Reductions in membrane proteins and lipids in basal ganglia of classic Alzheimer disease patients Alzheimer Dis Assoc Disord 10 2 1996 77 81
    • (1996) Alzheimer Dis Assoc Disord , vol.10 , Issue.2 , pp. 77-81
    • Gottfries, C.G.1    Jungbjer, B.2    Karlsson, I.3    Svennerholm, L.4
  • 132
    • 0026732790 scopus 로고
    • Lipid composition in different regions of the brain in Alzheimer's disease/senile dementia of Alzheimer's type
    • M. Söderberg, C. Edlund, I. Alafuzoff, K. Kristensson, and G. Dallner Lipid composition in different regions of the brain in Alzheimer's disease/senile dementia of Alzheimer's type J Neurochem 59 5 1992 1646 1653
    • (1992) J Neurochem , vol.59 , Issue.5 , pp. 1646-1653
    • Söderberg, M.1    Edlund, C.2    Alafuzoff, I.3    Kristensson, K.4    Dallner, G.5
  • 133
    • 74149083982 scopus 로고    scopus 로고
    • Deregulation of sphingolipid metabolism in Alzheimer's disease
    • X. He, Y. Huang, B. Li, C.X. Gong, and E.H. Schuchman Deregulation of sphingolipid metabolism in Alzheimer's disease Neurobiol Aging 31 3 2010 398 408
    • (2010) Neurobiol Aging , vol.31 , Issue.3 , pp. 398-408
    • He, X.1    Huang, Y.2    Li, B.3    Gong, C.X.4    Schuchman, E.H.5
  • 134
    • 0037401647 scopus 로고    scopus 로고
    • Regulation of death receptor signaling and apoptosis by ceramide
    • E. Gulbins Regulation of death receptor signaling and apoptosis by ceramide Pharmacol Res 47 2003 393 399
    • (2003) Pharmacol Res , vol.47 , pp. 393-399
    • Gulbins, E.1
  • 136
    • 84908689746 scopus 로고    scopus 로고
    • Region-specific metabolic alterations in the brain of the APP/PS1 transgenic mice of Alzheimer's disease
    • R. González-Domínguez, T. Garciá-Barrera, J. Vitorica, and J.L. Gómez-Ariza Region-specific metabolic alterations in the brain of the APP/PS1 transgenic mice of Alzheimer's disease Biochim Biophys Acta 1842 12 Pt A 2014 2395 2402
    • (2014) Biochim Biophys Acta , vol.1842 , Issue.12 , pp. 2395-2402
    • González-Domínguez, R.1    Garciá-Barrera, T.2    Vitorica, J.3    Gómez-Ariza, J.L.4
  • 137
    • 84877111087 scopus 로고    scopus 로고
    • Lipidomic analysis of brain tissues and plasma in a mouse model expressing mutated human amyloid precursor protein/tau for Alzheimer's disease
    • Y. Tajima, M. Ishikawa, K. Maekawa, M. Murayama, Y. Senoo, T. Nishimaki-Mogami, and et al. Lipidomic analysis of brain tissues and plasma in a mouse model expressing mutated human amyloid precursor protein/tau for Alzheimer's disease Lipids Health Dis 12 2013 68
    • (2013) Lipids Health Dis , vol.12 , pp. 68
    • Tajima, Y.1    Ishikawa, M.2    Maekawa, K.3    Murayama, M.4    Senoo, Y.5    Nishimaki-Mogami, T.6
  • 138
    • 33645299023 scopus 로고    scopus 로고
    • The involvement of lipid rafts in Alzheimer's disease
    • J.M. Cordy, N.M. Hooper, and A.J. Turner The involvement of lipid rafts in Alzheimer's disease Mol Membr Biol 23 1 2006 111 122
    • (2006) Mol Membr Biol , vol.23 , Issue.1 , pp. 111-122
    • Cordy, J.M.1    Hooper, N.M.2    Turner, A.J.3
  • 139
    • 77952320968 scopus 로고    scopus 로고
    • Lipid rafts: Keys to neurodegeneration
    • C.L. Schengrund Lipid rafts: Keys to neurodegeneration Brain Res Bull 82 1-2 2010 7 17
    • (2010) Brain Res Bull , vol.82 , Issue.1-2 , pp. 7-17
    • Schengrund, C.L.1
  • 140
    • 84899966426 scopus 로고    scopus 로고
    • Altered lipid composition in cortical lipid rafts occurs at early stages of sporadic Alzheimer's disease and facilitates APP/BACE1 interactions
    • N. Fabelo, V. Martín, R. Marín, D. Moreno, I. Ferrer, and M. Diáz Altered lipid composition in cortical lipid rafts occurs at early stages of sporadic Alzheimer's disease and facilitates APP/BACE1 interactions Neurobiol Aging 35 8 2014 1801 1812
    • (2014) Neurobiol Aging , vol.35 , Issue.8 , pp. 1801-1812
    • Fabelo, N.1    Martín, V.2    Marín, R.3    Moreno, D.4    Ferrer, I.5    Diáz, M.6
  • 141
    • 84909638254 scopus 로고    scopus 로고
    • Biophysical alterations in lipid rafts from human cerebral cortex associate with increased BACE1/AβPP interaction in early stages of Alzheimer's disease
    • M. Diáz, N. Fabelo, V. Martín, I. Ferrer, T. Gómez, and R. Marín Biophysical alterations in lipid rafts from human cerebral cortex associate with increased BACE1/AβPP interaction in early stages of Alzheimer's disease J Alzheimers Dis 43 4 2015 1185 1198
    • (2015) J Alzheimers Dis , vol.43 , Issue.4 , pp. 1185-1198
    • Diáz, M.1    Fabelo, N.2    Martín, V.3    Ferrer, I.4    Gómez, T.5    Marín, R.6
  • 142
    • 77950337738 scopus 로고    scopus 로고
    • Oxidative stress resistance in hippocampal cells is associated with altered membrane fluidity and enhanced nonamyloidogenic cleavage of endogenous amyloid precursor protein
    • A.B. Clement, G. Gimpl, and C. Behl Oxidative stress resistance in hippocampal cells is associated with altered membrane fluidity and enhanced nonamyloidogenic cleavage of endogenous amyloid precursor protein Free Radic Biol Med 48 9 2010 1236 1241
    • (2010) Free Radic Biol Med , vol.48 , Issue.9 , pp. 1236-1241
    • Clement, A.B.1    Gimpl, G.2    Behl, C.3
  • 143
    • 3042586648 scopus 로고    scopus 로고
    • Inflammatory mediator and beta-amyloid (25e35)-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 (25e35)-induced ceramide generation and iNOS expression are inhibited by vitamin E Free Radic Biol Med 37 3 2004 325 338
    • (2004) Free Radic Biol Med , vol.37 , Issue.3 , pp. 325-338
    • Ayasolla, K.1    Khan, M.2    Singh, A.K.3    Singh, I.4
  • 144
    • 28644451007 scopus 로고    scopus 로고
    • Regulation of cholesterol and sphingomyelin metabolism by amyloid-beta and presenilin
    • M.O. Grimm, H.S. Grimm, A.J. Pätzold, E.G. Zinser, R. Halonen, M. Duering, and et al. Regulation of cholesterol and sphingomyelin metabolism by amyloid-beta and presenilin Nat Cell Biol 7 11 2005 1118 1123
    • (2005) Nat Cell Biol , vol.7 , Issue.11 , pp. 1118-1123
    • Grimm, M.O.1    Grimm, H.S.2    Pätzold, A.J.3    Zinser, E.G.4    Halonen, R.5    Duering, M.6
  • 145
    • 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 8 2014 1792 1800
    • (2014) Neurobiol Aging , vol.35 , Issue.8 , pp. 1792-1800
    • Dinkins, M.B.1    Dasgupta, S.2    Wang, G.3    Zhu, G.4    Bieberich, E.5
  • 146
    • 84859499570 scopus 로고    scopus 로고
    • Sphingolipid-modulated exosome secretion promotes clearance of amyloid-β by microglia
    • K. Yuyama, H. Sun, S. Mitsutake, and Y. Igarashi Sphingolipid-modulated exosome secretion promotes clearance of amyloid-β by microglia J Biol Chem 287 14 2012 10977 10989
    • (2012) J Biol Chem , vol.287 , Issue.14 , pp. 10977-10989
    • Yuyama, K.1    Sun, H.2    Mitsutake, S.3    Igarashi, Y.4
  • 147
    • 84905111905 scopus 로고    scopus 로고
    • Acid sphingomyelinase modulates the autophagic process by controlling lysosomal biogenesis in Alzheimer's disease
    • J.K. Lee, H.K. Jin, M.H. Park, B.R. Kim, P.H. Lee, H. Nakauchi, and et al. Acid sphingomyelinase modulates the autophagic process by controlling lysosomal biogenesis in Alzheimer's disease J Exp Med 211 8 2014 1551 1570
    • (2014) J Exp Med , vol.211 , Issue.8 , pp. 1551-1570
    • Lee, J.K.1    Jin, H.K.2    Park, M.H.3    Kim, B.R.4    Lee, P.H.5    Nakauchi, H.6
  • 148
    • 61649120841 scopus 로고    scopus 로고
    • ApoE4 disrupts sterol and sphingolipid metabolism in Alzheimer's but not normal brain
    • V.V. Bandaru, J. Troncoso, D. Wheeler, O. Pletnikova, J. Wang, K. Conant, and et al. ApoE4 disrupts sterol and sphingolipid metabolism in Alzheimer's but not normal brain Neurobiol Aging 30 4 2009 591 599
    • (2009) Neurobiol Aging , vol.30 , Issue.4 , pp. 591-599
    • Bandaru, V.V.1    Troncoso, J.2    Wheeler, D.3    Pletnikova, O.4    Wang, J.5    Conant, K.6
  • 149
    • 0030971159 scopus 로고    scopus 로고
    • Lower serum high-density lipoprotein cholesterol (HDL-C) in major depression and in depressed men with serious suicidal attempts: Relationship with immune-inflammatory markers
    • M. Maes, R. Smith, A. Christophe, E. Vandoolaeghe, A. Van Gastel, H. Neels, and et al. Lower serum high-density lipoprotein cholesterol (HDL-C) in major depression and in depressed men with serious suicidal attempts: Relationship with immune-inflammatory markers Acta Psychiatr Scand 95 3 1997 212 221
    • (1997) Acta Psychiatr Scand , vol.95 , Issue.3 , pp. 212-221
    • Maes, M.1    Smith, R.2    Christophe, A.3    Vandoolaeghe, E.4    Van Gastel, A.5    Neels, H.6
  • 150
    • 0031822289 scopus 로고    scopus 로고
    • The relationship of depression to cardiovascular disease: Epidemiology, biology, and treatment
    • D.L. Musselman, D.L. Evans, and C.B. Nemeroff The relationship of depression to cardiovascular disease: Epidemiology, biology, and treatment Arch Gen Psychiatry 55 7 1998 580 592
    • (1998) Arch Gen Psychiatry , vol.55 , Issue.7 , pp. 580-592
    • Musselman, D.L.1    Evans, D.L.2    Nemeroff, C.B.3
  • 151
    • 0035403020 scopus 로고    scopus 로고
    • Depression: A major, unrecognized risk factor for osteoporosis?
    • G. Cizza, P. Ravn, G.P. Chrousos, and P.W. Gold Depression: A major, unrecognized risk factor for osteoporosis? Trends Endocrinol Metab 12 5 2001 198 203
    • (2001) Trends Endocrinol Metab , vol.12 , Issue.5 , pp. 198-203
    • Cizza, G.1    Ravn, P.2    Chrousos, G.P.3    Gold, P.W.4
  • 152
    • 84873525686 scopus 로고    scopus 로고
    • Plasma phosphatidylcholine and sphingomyelin concentrations are associated with depression and anxiety symptoms in a Dutch family-based lipidomics study
    • A. Demirkan, A. Isaacs, P. Ugocsai, G. Liebisch, M. Struchalin, I. Rudan, and et al. Plasma phosphatidylcholine and sphingomyelin concentrations are associated with depression and anxiety symptoms in a Dutch family-based lipidomics study J Psychiatr Res 47 3 2013 357 362
    • (2013) J Psychiatr Res , vol.47 , Issue.3 , pp. 357-362
    • Demirkan, A.1    Isaacs, A.2    Ugocsai, P.3    Liebisch, G.4    Struchalin, M.5    Rudan, I.6
  • 155
    • 0036106266 scopus 로고    scopus 로고
    • Tianeptine: 5-HT uptake sites and 5-HT(1-7) receptors modulate memory formation in an autoshaping Pavlovian/instrumental task
    • A. Meneses Tianeptine: 5-HT uptake sites and 5-HT(1-7) receptors modulate memory formation in an autoshaping Pavlovian/instrumental task Neurosci Biobehav Rev 26 3 2002 309 319
    • (2002) Neurosci Biobehav Rev , vol.26 , Issue.3 , pp. 309-319
    • Meneses, A.1
  • 156
    • 34147098474 scopus 로고    scopus 로고
    • Depletion of the lipid raft constituents, sphingomyelin and ganglioside, decreases serotonin binding at human 5-HT7(a) receptors in HeLa cells
    • B. Sjögren, and P. Svenningsson Depletion of the lipid raft constituents, sphingomyelin and ganglioside, decreases serotonin binding at human 5-HT7(a) receptors in HeLa cells Acta Physiol (Oxf) 190 1 2007 47 53
    • (2007) Acta Physiol (Oxf) , vol.190 , Issue.1 , pp. 47-53
    • Sjögren, B.1    Svenningsson, P.2
  • 157
    • 84937800845 scopus 로고    scopus 로고
    • Lipidomic analysis of p-chlorophenylalanine-treated mice using continuous-flow two-dimensional liquid chromatography/quadrupole time-of-flight mass spectrometry
    • R. Weng, S. Shen, L. Yang, M. Li, Y. Tian, Y. Bai, and et al. Lipidomic analysis of p-chlorophenylalanine-treated mice using continuous-flow two-dimensional liquid chromatography/quadrupole time-of-flight mass spectrometry Rapid Commun Mass Spectrom 29 16 2015 1491 1500
    • (2015) Rapid Commun Mass Spectrom , vol.29 , Issue.16 , pp. 1491-1500
    • Weng, R.1    Shen, S.2    Yang, L.3    Li, M.4    Tian, Y.5    Bai, Y.6
  • 158
    • 77952908473 scopus 로고    scopus 로고
    • Functional Inhibitors of Acid Sphingomyelinase (FIASMAs): A novel pharmacological group of drugs with broad clinical applications
    • J. Kornhuber, P. Tripal, M. Reichel, C. Mühle, C. Rhein, M. Muehlbacher, and et al. Functional Inhibitors of Acid Sphingomyelinase (FIASMAs): A novel pharmacological group of drugs with broad clinical applications Cell Physiol Biochem 26 1 2010 9 20
    • (2010) Cell Physiol Biochem , vol.26 , Issue.1 , pp. 9-20
    • Kornhuber, J.1    Tripal, P.2    Reichel, M.3    Mühle, C.4    Rhein, C.5    Muehlbacher, M.6
  • 159
    • 84880269973 scopus 로고    scopus 로고
    • Acid sphingomyelinase-ceramide system mediates effects of antidepressant drugs
    • E. Gulbins, M. Palmada, M. Reichel, A. Lüth, C. Böhmer, D. Amato, and et al. Acid sphingomyelinase-ceramide system mediates effects of antidepressant drugs Nat Med 19 7 2013 934 938
    • (2013) Nat Med , vol.19 , Issue.7 , pp. 934-938
    • Gulbins, E.1    Palmada, M.2    Reichel, M.3    Lüth, A.4    Böhmer, C.5    Amato, D.6
  • 161
    • 0035477446 scopus 로고    scopus 로고
    • Phospholipid patterns of erythrocytes in schizophrenia: Relationships to symptomatology
    • A.M. Ponizovsky, I. Modai, Y. Nechamkin, G. Barshtein, M.S. Ritsner, S. Yedgar, and et al. Phospholipid patterns of erythrocytes in schizophrenia: Relationships to symptomatology Schizophr Res 52 1-2 2001 121 126
    • (2001) Schizophr Res , vol.52 , Issue.1-2 , pp. 121-126
    • Ponizovsky, A.M.1    Modai, I.2    Nechamkin, Y.3    Barshtein, G.4    Ritsner, M.S.5    Yedgar, S.6
  • 162
    • 3042522884 scopus 로고    scopus 로고
    • Altered thalamic membrane phospholipids in schizophrenia: A postmortem study
    • A. Schmitt, K. Wilczek, K. Blennow, A. Maras, A. Jatzko, G. Petroianu, and et al. Altered thalamic membrane phospholipids in schizophrenia: A postmortem study Biol Psychiatry 56 1 2004 41 45
    • (2004) Biol Psychiatry , vol.56 , Issue.1 , pp. 41-45
    • Schmitt, A.1    Wilczek, K.2    Blennow, K.3    Maras, A.4    Jatzko, A.5    Petroianu, G.6
  • 163
    • 79959769576 scopus 로고    scopus 로고
    • α7 nicotinic acetylcholine receptor function in hippocampal neurons is regulated by the lipid composition of the plasma membrane
    • J.O. Colón-Saéz, and Yakel J.L. The α7 nicotinic acetylcholine receptor function in hippocampal neurons is regulated by the lipid composition of the plasma membrane J Physiol 589 Pt 13 2011 3163 3174
    • (2011) J Physiol , vol.589 , pp. 3163-3174
    • Colón-Saéz, J.O.1    The, Y.J.L.2
  • 164
    • 14844325779 scopus 로고    scopus 로고
    • Molecular pathogenesis of Parkinson disease
    • J.L. Eriksen, Z. Wszolek, and L. Petrucelli Molecular pathogenesis of Parkinson disease Arch Neurol 62 3 2005 353 357
    • (2005) Arch Neurol , vol.62 , Issue.3 , pp. 353-357
    • Eriksen, J.L.1    Wszolek, Z.2    Petrucelli, L.3
  • 165
    • 53549118274 scopus 로고    scopus 로고
    • Alpha-synuclein degradation by autophagic pathways: A potential key to Parkinson's disease pathogenesis
    • M. Xilouri, T. Vogiatzi, K. Vekrellis, and L. Stefanis Alpha-synuclein degradation by autophagic pathways: A potential key to Parkinson's disease pathogenesis Autophagy 4 7 2008 917 919
    • (2008) Autophagy , vol.4 , Issue.7 , pp. 917-919
    • Xilouri, M.1    Vogiatzi, T.2    Vekrellis, K.3    Stefanis, L.4
  • 166
    • 84940614604 scopus 로고    scopus 로고
    • The contribution of Niemann-Pick SMPD1 mutations to Parkinson disease in Ashkenazi Jews
    • E. Dagan, I. Schlesinger, M. Ayoub, A. Mory, M. Nassar, A. Kurolap, and et al. The contribution of Niemann-Pick SMPD1 mutations to Parkinson disease in Ashkenazi Jews Parkinsonism Relat Disord 21 9 2015 1067 1071
    • (2015) Parkinsonism Relat Disord , vol.21 , Issue.9 , pp. 1067-1071
    • Dagan, E.1    Schlesinger, I.2    Ayoub, M.3    Mory, A.4    Nassar, M.5    Kurolap, A.6
  • 167
    • 84884126614 scopus 로고    scopus 로고
    • Rare lysosomal enzyme gene SMPD1 variant (p.R591C) associates with Parkinson's disease
    • 2890.e13-5
    • J.N. Foo, H. Liany, J.X. Bei, X.Q. Yu, J. Liu, W.L. Au, and et al. Rare lysosomal enzyme gene SMPD1 variant (p.R591C) associates with Parkinson's disease Neurobiol Aging 34 12 2013 2890.e13-5
    • (2013) Neurobiol Aging , vol.34 , Issue.12
    • Foo, J.N.1    Liany, H.2    Bei, J.X.3    Yu, X.Q.4    Liu, J.5    Au, W.L.6
  • 168
    • 84878911804 scopus 로고    scopus 로고
    • The p.L302P mutation in the lysosomal enzyme gene SMPD1 is a risk factor for Parkinson disease
    • Z. Gan-Or, L.J. Ozelius, A. Bar-Shira, R. Saunders-Pullman, A. Mirelman, R. Kornreich, and et al. The p.L302P mutation in the lysosomal enzyme gene SMPD1 is a risk factor for Parkinson disease Neurology 80 17 2013 1606 1610
    • (2013) Neurology , vol.80 , Issue.17 , pp. 1606-1610
    • Gan-Or, Z.1    Ozelius, L.J.2    Bar-Shira, A.3    Saunders-Pullman, R.4    Mirelman, A.5    Kornreich, R.6
  • 169
    • 84930985102 scopus 로고    scopus 로고
    • Effect of amyloids on the vesicular machinery: Implications for somatic neurotransmission
    • A.K. Das, R. Pandit, and S. Maiti Effect of amyloids on the vesicular machinery: Implications for somatic neurotransmission Philos Trans R Soc Lond B Biol Sci 370 1672 2015
    • (2015) Philos Trans R Soc Lond B Biol Sci , vol.370 , Issue.1672
    • Das, A.K.1    Pandit, R.2    Maiti, S.3
  • 170
    • 84880919761 scopus 로고    scopus 로고
    • 13C NMR reveals annealing of raft-like membranes containing cholesterol by the intrinsically disordered protein α-Synuclein
    • 13C NMR reveals annealing of raft-like membranes containing cholesterol by the intrinsically disordered protein α-Synuclein J Mol Biol 425 16 2013 2973 2987
    • (2013) J Mol Biol , vol.425 , Issue.16 , pp. 2973-2987
    • Leftin, A.1    Job, C.2    Beyer, K.3    Brown, M.F.4
  • 172
    • 84931412885 scopus 로고    scopus 로고
    • No evidence for substrate accumulation in Parkinson brains with GBA mutations
    • Jul
    • M.E. Gegg, L. Sweet, B.H. Wang, L.S. Shihabuddin, S.P. Sardi, and A.H. Schapira No evidence for substrate accumulation in Parkinson brains with GBA mutations Mov Disord 30 8 2015 Jul 1085 1089
    • (2015) Mov Disord , vol.30 , Issue.8 , pp. 1085-1089
    • Gegg, M.E.1    Sweet, L.2    Wang, B.H.3    Shihabuddin, L.S.4    Sardi, S.P.5    Schapira, A.H.6
  • 173
    • 84855973361 scopus 로고    scopus 로고
    • Severe alterations in lipid composition of frontal cortex lipid rafts from Parkinson's disease and incidental Parkinson's disease
    • N. Fabelo, V. Martín, G. Santpere, R. Marín, L. Torrent, I. Ferrer, and et al. Severe alterations in lipid composition of frontal cortex lipid rafts from Parkinson's disease and incidental Parkinson's disease Mol Med 17 9-10 2011 1107 1118
    • (2011) Mol Med , vol.17 , Issue.9-10 , pp. 1107-1118
    • Fabelo, N.1    Martín, V.2    Santpere, G.3    Marín, R.4    Torrent, L.5    Ferrer, I.6
  • 174
    • 84898057274 scopus 로고    scopus 로고
    • Altered ceramide acyl chain length and ceramide synthase gene expression in Parkinson's disease
    • S.K. Abbott, H. Li, S.S. Munõz, B. Knoch, M. Batterham, K.E. Murphy, and et al. Altered ceramide acyl chain length and ceramide synthase gene expression in Parkinson's disease Mov Disord 29 4 2014 518 526
    • (2014) Mov Disord , vol.29 , Issue.4 , pp. 518-526
    • Abbott, S.K.1    Li, H.2    Munõz, S.S.3    Knoch, B.4    Batterham, M.5    Murphy, K.E.6
  • 175
    • 84944044033 scopus 로고    scopus 로고
    • Neuroinflammation in Parkinson's disease and its potential as therapeutic target
    • Q. Wang, Y. Liu, and J. Zhou Neuroinflammation in Parkinson's disease and its potential as therapeutic target Transl Neurodegener 4 2015 19
    • (2015) Transl Neurodegener , vol.4 , pp. 19
    • Wang, Q.1    Liu, Y.2    Zhou, J.3
  • 176
    • 0030842085 scopus 로고    scopus 로고
    • Nuclear translocation of NF-kappaB is increased in dopaminergic neurons of patients with Parkinson disease
    • S. Hunot, B. Brugg, D. Ricard, P.P. Michel, M.P. Muriel, M. Ruberg, and et al. Nuclear translocation of NF-kappaB is increased in dopaminergic neurons of patients with Parkinson disease Proc Natl Acad Sci USA 94 14 1997 7531 7536
    • (1997) Proc Natl Acad Sci USA , vol.94 , Issue.14 , pp. 7531-7536
    • Hunot, S.1    Brugg, B.2    Ricard, D.3    Michel, P.P.4    Muriel, M.P.5    Ruberg, M.6
  • 177
    • 0035876022 scopus 로고    scopus 로고
    • An enzymatic assay for quantifying sphingomyelin in tissues and plasma from humans and mice with Niemann-Pick disease
    • X. He, F. Chen, S. Gatt, and E.H. Schuchman An enzymatic assay for quantifying sphingomyelin in tissues and plasma from humans and mice with Niemann-Pick disease Anal Biochem 293 2 2001 204 211
    • (2001) Anal Biochem , vol.293 , Issue.2 , pp. 204-211
    • He, X.1    Chen, F.2    Gatt, S.3    Schuchman, E.H.4
  • 179
    • 0025870103 scopus 로고
    • A frequent missense mutation in the acid sphingomyelinase gene of Ashkenazi Jewish type A and B patients
    • O. Levran, R.J. Desnick, and E.H. Schuchman A frequent missense mutation in the acid sphingomyelinase gene of Ashkenazi Jewish type A and B patients Proc Natl Acad Sci USA 88 9 1991 3748 3752
    • (1991) Proc Natl Acad Sci USA , vol.88 , Issue.9 , pp. 3748-3752
    • Levran, O.1    Desnick, R.J.2    Schuchman, E.H.3
  • 180
    • 0036914191 scopus 로고    scopus 로고
    • The demographics and distribution of type B Niemann-Pick disease: Novel mutations lead to new genotype/phenotype correlations
    • C.M. Simonaro, R.J. Desnick, M.M. McGovern, M.P. Wasserstein, and E.H. Schuchman The demographics and distribution of type B Niemann-Pick disease: Novel mutations lead to new genotype/phenotype correlations Am J Hum Genet 71 6 2002 1413 1419
    • (2002) Am J Hum Genet , vol.71 , Issue.6 , pp. 1413-1419
    • Simonaro, C.M.1    Desnick, R.J.2    McGovern, M.M.3    Wasserstein, M.P.4    Schuchman, E.H.5
  • 181
    • 85060737282 scopus 로고    scopus 로고
    • Molecular genetic characterization of novel sphingomyelin phosphodiesterase 1 mutations causing Niemann-Pick disease
    • B. Tóth, M. Erdos, A. Székely, L. Ritli, P. Bagossi, J. Sümegi, and et al. Molecular genetic characterization of novel sphingomyelin phosphodiesterase 1 mutations causing Niemann-Pick disease JIMD Rep 3 2012 125 129
    • (2012) JIMD Rep , vol.3 , pp. 125-129
    • Tóth, B.1    Erdos, M.2    Székely, A.3    Ritli, L.4    Bagossi, P.5    Sümegi, J.6
  • 182
    • 84872789314 scopus 로고    scopus 로고
    • Identification of a distinct mutation spectrum in the SMPD1 gene of Chinese patients with acid sphingomyelinase-deficient Niemann-Pick disease
    • H. Zhang, Y. Wang, Z. Gong, X. Li, W. Qiu, L. Han, and et al. Identification of a distinct mutation spectrum in the SMPD1 gene of Chinese patients with acid sphingomyelinase-deficient Niemann-Pick disease Orphanet J Rare Dis 8 2013 15
    • (2013) Orphanet J Rare Dis , vol.8 , pp. 15
    • Zhang, H.1    Wang, Y.2    Gong, Z.3    Li, X.4    Qiu, W.5    Han, L.6
  • 183
    • 84883764158 scopus 로고    scopus 로고
    • Identification of seven novel SMPD1 mutations causing Niemann-Pick disease types A and B
    • P. Irun, M. Mallén, C. Dominguez, V. Rodriguez-Sureda, L.A. Alvarez-Sala, N. Arslan, and et al. Identification of seven novel SMPD1 mutations causing Niemann-Pick disease types A and B Clin Genet 84 4 2013 356 361
    • (2013) Clin Genet , vol.84 , Issue.4 , pp. 356-361
    • Irun, P.1    Mallén, M.2    Dominguez, C.3    Rodriguez-Sureda, V.4    Alvarez-Sala, L.A.5    Arslan, N.6
  • 184
    • 84925872815 scopus 로고    scopus 로고
    • Four novel p.N385K, p.V36A, c.1033-1034insT and c.1417-1418delCT mutations in the sphingomyelin phosphodiesterase 1 (SMPD1) gene in patients with types A and B Niemann-Pick disease (NPD)
    • M.D. Manshadi, B. Kamalidehghan, F. Keshavarzi, O. Aryani, S. Dadgar, A. Arastehkani, and et al. Four novel p.N385K, p.V36A, c.1033-1034insT and c.1417-1418delCT mutations in the sphingomyelin phosphodiesterase 1 (SMPD1) gene in patients with types A and B Niemann-Pick disease (NPD) Int J Mol Sci 16 4 2015 6668 6676
    • (2015) Int J Mol Sci , vol.16 , Issue.4 , pp. 6668-6676
    • Manshadi, M.D.1    Kamalidehghan, B.2    Keshavarzi, F.3    Aryani, O.4    Dadgar, S.5    Arastehkani, A.6
  • 185
    • 67549105629 scopus 로고    scopus 로고
    • Structure of N-terminal domain of NPC1 reveals distinct subdomains for binding and transfer of cholesterol
    • H.J. Kwon, L. Abi-Mosleh, M.L. Wang, J. Deisenhofer, J.L. Goldstein, M.S. Brown, and et al. Structure of N-terminal domain of NPC1 reveals distinct subdomains for binding and transfer of cholesterol Cell 137 7 2009 1213 1224
    • (2009) Cell , vol.137 , Issue.7 , pp. 1213-1224
    • Kwon, H.J.1    Abi-Mosleh, L.2    Wang, M.L.3    Deisenhofer, J.4    Goldstein, J.L.5    Brown, M.S.6
  • 186
    • 4744350864 scopus 로고    scopus 로고
    • Structure and function of the NPC2 protein
    • M.T. Vanier, and G. Millat Structure and function of the NPC2 protein Biochim Biophys Acta 1685 1-3 2004 14 21
    • (2004) Biochim Biophys Acta , vol.1685 , Issue.1-3 , pp. 14-21
    • Vanier, M.T.1    Millat, G.2
  • 187
    • 0024474453 scopus 로고
    • Correction of sphingomyelinase deficiency in Niemann-Pick type C fibroblasts by removal of lipoprotein fraction from culture media
    • G.H. Thomas, C.M. Tuck-Muller, C.S. Miller, and L.W. Reynolds Correction of sphingomyelinase deficiency in Niemann-Pick type C fibroblasts by removal of lipoprotein fraction from culture media J Inherit Metab Dis 12 2 1989 139 151
    • (1989) J Inherit Metab Dis , vol.12 , Issue.2 , pp. 139-151
    • Thomas, G.H.1    Tuck-Muller, C.M.2    Miller, C.S.3    Reynolds, L.W.4
  • 189
    • 33644921804 scopus 로고    scopus 로고
    • Natural history of type A Niemann-Pick disease; possible endpoints for therapeutic trials
    • M.M. McGovern, A. Aron, S.E. Brodie, R.J. Desnick, and M.P. Wasserstein Natural history of type A Niemann-Pick disease; possible endpoints for therapeutic trials Neurology 66 2 2006 228 232
    • (2006) Neurology , vol.66 , Issue.2 , pp. 228-232
    • McGovern, M.M.1    Aron, A.2    Brodie, S.E.3    Desnick, R.J.4    Wasserstein, M.P.5
  • 190
    • 16644401487 scopus 로고    scopus 로고
    • The natural history of type B Niemann-Pick disease: Results from a 10-year longitudinal study
    • M.P. Wasserstein, R.J. Desnick, E.H. Schuchman, S. Hossain, S. Wallenstein, C. Lamm, and et al. The natural history of type B Niemann-Pick disease: Results from a 10-year longitudinal study Pediatrics 114 6 2004 e672 e677
    • (2004) Pediatrics , vol.114 , Issue.6 , pp. e672-e677
    • Wasserstein, M.P.1    Desnick, R.J.2    Schuchman, E.H.3    Hossain, S.4    Wallenstein, S.5    Lamm, C.6
  • 192
    • 0034641594 scopus 로고    scopus 로고
    • Creation of a mouse model for non-neurological (type B) Niemann-Pick disease by stable, low level expression of lysosomal sphingomyelinase in the absence of secretory sphingomyelinase: Relationship between brain intra-lysosomal enzyme activity and central nervous system function
    • S. Marathe, S.R. Miranda, C. Devlin, A. Johns, G. Kuriakose, K.J. Williams, and et al. Creation of a mouse model for non-neurological (type B) Niemann-Pick disease by stable, low level expression of lysosomal sphingomyelinase in the absence of secretory sphingomyelinase: Relationship between brain intra-lysosomal enzyme activity and central nervous system function Hum Mol Genet 9 13 2000 1967 1976
    • (2000) Hum Mol Genet , vol.9 , Issue.13 , pp. 1967-1976
    • Marathe, S.1    Miranda, S.R.2    Devlin, C.3    Johns, A.4    Kuriakose, G.5    Williams, K.J.6
  • 193
    • 84899957348 scopus 로고    scopus 로고
    • High sphingomyelin levels induce lysosomal damage and autophagy dysfunction in Niemann Pick disease type A
    • E. Gabandé-Rodríguez, P. Boya, V. Labrador, C.G. Dotti, and M.D. Ledesma High sphingomyelin levels induce lysosomal damage and autophagy dysfunction in Niemann Pick disease type A Cell Death Differ 21 6 2014 864 875
    • (2014) Cell Death Differ , vol.21 , Issue.6 , pp. 864-875
    • Gabandé-Rodríguez, E.1    Boya, P.2    Labrador, V.3    Dotti, C.G.4    Ledesma, M.D.5
  • 194
    • 56349145208 scopus 로고    scopus 로고
    • Neuropathology of the acid sphingomyelinase knockout mouse model of Niemann-Pick A disease including structure-function studies associated with cerebellar Purkinje cell degeneration
    • S.L. Macauley, R.L. Sidman, E.H. Schuchman, T. Taksir, and G.R. Stewart Neuropathology of the acid sphingomyelinase knockout mouse model of Niemann-Pick A disease including structure-function studies associated with cerebellar Purkinje cell degeneration Exp Neurol 214 2 2008 181 192
    • (2008) Exp Neurol , vol.214 , Issue.2 , pp. 181-192
    • MacAuley, S.L.1    Sidman, R.L.2    Schuchman, E.H.3    Taksir, T.4    Stewart, G.R.5
  • 195
    • 0033810516 scopus 로고    scopus 로고
    • Infusion of recombinant human acid sphingomyelinase into Niemann-Pick disease mice leads to visceral, but not neurological, correction of the pathophysiology
    • S.R. Miranda, X. He, C.M. Simonaro, S. Gatt, A. Dagan, R.J. Desnick, and et al. Infusion of recombinant human acid sphingomyelinase into Niemann-Pick disease mice leads to visceral, but not neurological, correction of the pathophysiology FASEB J 14 13 2000 1988 1995
    • (2000) FASEB J , vol.14 , Issue.13 , pp. 1988-1995
    • Miranda, S.R.1    He, X.2    Simonaro, C.M.3    Gatt, S.4    Dagan, A.5    Desnick, R.J.6
  • 196
    • 58149500258 scopus 로고    scopus 로고
    • Intracerebroventricular infusion of acid sphingomyelinase corrects CNS manifestations in a mouse model of Niemann-Pick A disease
    • J.C. Dodge, J. Clarke, C.M. Treleaven, T.V. Taksir, D.A. Griffiths, W. Yang, and et al. Intracerebroventricular infusion of acid sphingomyelinase corrects CNS manifestations in a mouse model of Niemann-Pick A disease Exp Neurol 215 2 2009 349 357
    • (2009) Exp Neurol , vol.215 , Issue.2 , pp. 349-357
    • Dodge, J.C.1    Clarke, J.2    Treleaven, C.M.3    Taksir, T.V.4    Griffiths, D.A.5    Yang, W.6
  • 197
    • 84921790971 scopus 로고    scopus 로고
    • Nonclinical safety assessment of recombinant human acid sphingomyelinase (rhASM) for the treatment of acid sphingomyelinase deficiency: The utility of animal models of disease in the toxicological evaluation of potential therapeutics
    • J.M. Murray, A.M. Thompson, A. Vitsky, M. Hawes, W.L. Chuang, J. Pacheco, and et al. Nonclinical safety assessment of recombinant human acid sphingomyelinase (rhASM) for the treatment of acid sphingomyelinase deficiency: The utility of animal models of disease in the toxicological evaluation of potential therapeutics Mol Genet Metab 114 2 2015 217 225
    • (2015) Mol Genet Metab , vol.114 , Issue.2 , pp. 217-225
    • Murray, J.M.1    Thompson, A.M.2    Vitsky, A.3    Hawes, M.4    Chuang, W.L.5    Pacheco, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.