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Volumn 110, Issue 1, 2016, Pages 205-213

Oxidized Phospholipids Inhibit the Formation of Cholesterol-Dependent Plasma Membrane Nanoplatforms

Author keywords

[No Author keywords available]

Indexed keywords

1-PALMITOYL-2-(5-OXOVALEROYL)-SN-GLYCERO-3-PHOSPHORYLCHOLINE; 1-PALMITOYL-2-GLUTAROYL-SN-GLYCERO-3-PHOSPHORYLCHOLINE; CHOLESTEROL; ETHER PHOSPHOLIPID; GLYCOSYLPHOSPHATIDYLINOSITOL;

EID: 84953238595     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2015.11.018     Document Type: Article
Times cited : (10)

References (56)
  • 1
    • 43249093987 scopus 로고    scopus 로고
    • Oxidized phospholipids: Emerging lipid mediators in pathophysiology
    • H.P. Deigner, and A. Hermetter Oxidized phospholipids: emerging lipid mediators in pathophysiology Curr. Opin. Lipidol. 19 2008 289 294
    • (2008) Curr. Opin. Lipidol. , vol.19 , pp. 289-294
    • Deigner, H.P.1    Hermetter, A.2
  • 2
    • 84863985396 scopus 로고    scopus 로고
    • Protein modification by aldehydophospholipids and its functional consequences
    • U. Stemmer, and A. Hermetter Protein modification by aldehydophospholipids and its functional consequences Biochim. Biophys. Acta 1818 2012 2436 2445
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 2436-2445
    • Stemmer, U.1    Hermetter, A.2
  • 3
    • 34249991689 scopus 로고    scopus 로고
    • Oxidized phospholipids: From molecular properties to disease
    • G.O. Fruhwirth, A. Loidl, and A. Hermetter Oxidized phospholipids: from molecular properties to disease Biochim. Biophys. Acta 1772 2007 718 736
    • (2007) Biochim. Biophys. Acta , vol.1772 , pp. 718-736
    • Fruhwirth, G.O.1    Loidl, A.2    Hermetter, A.3
  • 4
    • 84863990492 scopus 로고    scopus 로고
    • Protein-oxidized phospholipid interactions in cellular signaling for cell death: From biophysics to clinical correlations
    • P.K. Kinnunen, K. Kaarniranta, and A.K. Mahalka Protein-oxidized phospholipid interactions in cellular signaling for cell death: from biophysics to clinical correlations Biochim. Biophys. Acta 1818 2012 2446 2455
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 2446-2455
    • Kinnunen, P.K.1    Kaarniranta, K.2    Mahalka, A.K.3
  • 5
    • 17944387960 scopus 로고    scopus 로고
    • Structural identification by mass spectrometry of oxidized phospholipids in minimally oxidized low density lipoprotein that induce monocyte/endothelial interactions and evidence for their presence in vivo
    • A.D. Watson, and N. Leitinger J.A. Berliner Structural identification by mass spectrometry of oxidized phospholipids in minimally oxidized low density lipoprotein that induce monocyte/endothelial interactions and evidence for their presence in vivo J. Biol. Chem. 272 1997 13597 13607
    • (1997) J. Biol. Chem. , vol.272 , pp. 13597-13607
    • Watson, A.D.1    Leitinger, N.2    Berliner, J.A.3
  • 6
    • 0033815506 scopus 로고    scopus 로고
    • Localization of apoptotic macrophages at the site of plaque rupture in sudden coronary death
    • F.D. Kolodgie, and J. Narula R. Virmani Localization of apoptotic macrophages at the site of plaque rupture in sudden coronary death Am. J. Pathol. 157 2000 1259 1268
    • (2000) Am. J. Pathol. , vol.157 , pp. 1259-1268
    • Kolodgie, F.D.1    Narula, J.2    Virmani, R.3
  • 7
    • 84865830234 scopus 로고    scopus 로고
    • Toxicity of oxidized phospholipids in cultured macrophages
    • U. Stemmer, and Z.A. Dunai A. Hermetter Toxicity of oxidized phospholipids in cultured macrophages Lipids Health Dis. 11 2012 110
    • (2012) Lipids Health Dis. , vol.11 , pp. 110
    • Stemmer, U.1    Dunai, Z.A.2    Hermetter, A.3
  • 8
    • 0042858394 scopus 로고    scopus 로고
    • Oxidized phospholipids in minimally modified low density lipoprotein induce apoptotic signaling via activation of acid sphingomyelinase in arterial smooth muscle cells
    • A. Loidl, and E. Sevcsik A. Hermetter Oxidized phospholipids in minimally modified low density lipoprotein induce apoptotic signaling via activation of acid sphingomyelinase in arterial smooth muscle cells J. Biol. Chem. 278 2003 32921 32928
    • (2003) J. Biol. Chem. , vol.278 , pp. 32921-32928
    • Loidl, A.1    Sevcsik, E.2    Hermetter, A.3
  • 9
    • 59049093869 scopus 로고    scopus 로고
    • Plasma membrane fluidity affects transient immobilization of oxidized phospholipids in endocytotic sites for subsequent uptake
    • S. Rhode, and R. Grurl G.J. Schütz Plasma membrane fluidity affects transient immobilization of oxidized phospholipids in endocytotic sites for subsequent uptake J. Biol. Chem. 284 2009 2258 2265
    • (2009) J. Biol. Chem. , vol.284 , pp. 2258-2265
    • Rhode, S.1    Grurl, R.2    Schütz, G.J.3
  • 10
    • 84863984081 scopus 로고    scopus 로고
    • Biophysics of lipid bilayers containing oxidatively modified phospholipids: Insights from fluorescence and EPR experiments and from MD simulations
    • P. Jurkiewicz, and A. Olżyńska M. Hof Biophysics of lipid bilayers containing oxidatively modified phospholipids: insights from fluorescence and EPR experiments and from MD simulations Biochim. Biophys. Acta 1818 2012 2388 2402
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 2388-2402
    • Jurkiewicz, P.1    Olzyńska, A.2    Hof, M.3
  • 11
    • 77951692611 scopus 로고    scopus 로고
    • Oxidation changes physical properties of phospholipid bilayers: Fluorescence spectroscopy and molecular simulations
    • L. Beranova, and L. Cwiklik P. Jungwirth Oxidation changes physical properties of phospholipid bilayers: fluorescence spectroscopy and molecular simulations Langmuir 26 2010 6140 6144
    • (2010) Langmuir , vol.26 , pp. 6140-6144
    • Beranova, L.1    Cwiklik, L.2    Jungwirth, P.3
  • 12
    • 78650336973 scopus 로고    scopus 로고
    • Cholesterol slows down the lateral mobility of an oxidized phospholipid in a supported lipid bilayer
    • B. Plochberger, and T. Stockner G.J. Schütz Cholesterol slows down the lateral mobility of an oxidized phospholipid in a supported lipid bilayer Langmuir 26 2010 17322 17329
    • (2010) Langmuir , vol.26 , pp. 17322-17329
    • Plochberger, B.1    Stockner, T.2    Schütz, G.J.3
  • 13
    • 84891477292 scopus 로고    scopus 로고
    • Pairing of cholesterol with oxidized phospholipid species in lipid bilayers
    • H. Khandelia, and B. Loubet M. Hof Pairing of cholesterol with oxidized phospholipid species in lipid bilayers Soft Matter 10 2014 639 647
    • (2014) Soft Matter , vol.10 , pp. 639-647
    • Khandelia, H.1    Loubet, B.2    Hof, M.3
  • 14
    • 84899037032 scopus 로고    scopus 로고
    • Comprehensive portrait of cholesterol containing oxidized membrane
    • M. Stefl, and R. Sachl M. Hof Comprehensive portrait of cholesterol containing oxidized membrane Biochim. Biophys. Acta 1838 2014 1769 1776
    • (2014) Biochim. Biophys. Acta , vol.1838 , pp. 1769-1776
    • Stefl, M.1    Sachl, R.2    Hof, M.3
  • 15
    • 84908517990 scopus 로고    scopus 로고
    • Phospholipid lateral diffusion in phosphatidylcholine-sphingomyelin-cholesterol monolayers; Effects of oxidatively truncated phosphatidylcholines
    • 1 PT A
    • P. Parkkila, and M. Stefl P.K. Kinnunen Phospholipid lateral diffusion in phosphatidylcholine-sphingomyelin-cholesterol monolayers; effects of oxidatively truncated phosphatidylcholines Biochim. Biophys. Acta 1848 1 Pt A 2015 167 173
    • (2015) Biochim. Biophys. Acta , vol.1848 , pp. 167-173
    • Parkkila, P.1    Stefl, M.2    Kinnunen, P.K.3
  • 16
    • 67649342849 scopus 로고    scopus 로고
    • Lipid gymnastics: Evidence of complete acyl chain reversal in oxidized phospholipids from molecular simulations
    • H. Khandelia, and O.G. Mouritsen Lipid gymnastics: evidence of complete acyl chain reversal in oxidized phospholipids from molecular simulations Biophys. J. 96 2009 2734 2743
    • (2009) Biophys. J. , vol.96 , pp. 2734-2743
    • Khandelia, H.1    Mouritsen, O.G.2
  • 17
    • 33748474446 scopus 로고    scopus 로고
    • The oxidized phospholipids POVPC and PGPC inhibit growth and induce apoptosis in vascular smooth muscle cells
    • G.O. Fruhwirth, and A. Moumtzi A. Hermetter The oxidized phospholipids POVPC and PGPC inhibit growth and induce apoptosis in vascular smooth muscle cells Biochim. Biophys. Acta 1761 2006 1060 1069
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 1060-1069
    • Fruhwirth, G.O.1    Moumtzi, A.2    Hermetter, A.3
  • 18
    • 84865324247 scopus 로고    scopus 로고
    • Transient GPI-anchored protein homodimers are units for raft organization and function
    • K.G. Suzuki, and R.S. Kasai A. Kusumi Transient GPI-anchored protein homodimers are units for raft organization and function Nat. Chem. Biol. 8 2012 774 783
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 774-783
    • Suzuki, K.G.1    Kasai, R.S.2    Kusumi, A.3
  • 19
    • 84899474201 scopus 로고    scopus 로고
    • Golgi sorting regulates organization and activity of GPI proteins at apical membranes
    • S. Paladino, and S. Lebreton C. Zurzolo Golgi sorting regulates organization and activity of GPI proteins at apical membranes Nat. Chem. Biol. 10 2014 350 357
    • (2014) Nat. Chem. Biol. , vol.10 , pp. 350-357
    • Paladino, S.1    Lebreton, S.2    Zurzolo, C.3
  • 20
    • 78650637436 scopus 로고    scopus 로고
    • Imaging of mobile long-lived nanoplatforms in the live cell plasma membrane
    • M. Brameshuber, and J. Weghuber G.J. Schütz Imaging of mobile long-lived nanoplatforms in the live cell plasma membrane J. Biol. Chem. 285 2010 41765 41771
    • (2010) J. Biol. Chem. , vol.285 , pp. 41765-41771
    • Brameshuber, M.1    Weghuber, J.2    Schütz, G.J.3
  • 21
    • 84904994558 scopus 로고    scopus 로고
    • Multi-protein assemblies underlie the mesoscale organization of the plasma membrane
    • S.K. Saka, and A. Honigmann S.O. Rizzoli Multi-protein assemblies underlie the mesoscale organization of the plasma membrane Nat. Commun. 5 2014 4509
    • (2014) Nat. Commun. , vol.5 , pp. 4509
    • Saka, S.K.1    Honigmann, A.2    Rizzoli, S.O.3
  • 22
    • 84885926967 scopus 로고    scopus 로고
    • Application limits and data correction in number of molecules and brightness analysis
    • A. Trullo, and V. Corti M. Zamai Application limits and data correction in number of molecules and brightness analysis Microsc. Res. Tech. 76 2013 1135 1146
    • (2013) Microsc. Res. Tech. , vol.76 , pp. 1135-1146
    • Trullo, A.1    Corti, V.2    Zamai, M.3
  • 24
    • 84904255214 scopus 로고    scopus 로고
    • Membrane microdomains in immunoreceptor signaling
    • V. Horejsi, and M. Hrdinka Membrane microdomains in immunoreceptor signaling FEBS Lett. 588 2014 2392 2397
    • (2014) FEBS Lett. , vol.588 , pp. 2392-2397
    • Horejsi, V.1    Hrdinka, M.2
  • 25
    • 80755188911 scopus 로고    scopus 로고
    • Hierarchical mesoscale domain organization of the plasma membrane
    • A. Kusumi, and K.G. Suzuki T.K. Fujiwara Hierarchical mesoscale domain organization of the plasma membrane Trends Biochem. Sci. 36 2011 604 615
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 604-615
    • Kusumi, A.1    Suzuki, K.G.2    Fujiwara, T.K.3
  • 26
    • 84870188756 scopus 로고    scopus 로고
    • Dynamic organizing principles of the plasma membrane that regulate signal transduction: Commemorating the fortieth anniversary of Singer and Nicolson's fluid-mosaic model
    • A. Kusumi, and T.K. Fujiwara K.G. Suzuki Dynamic organizing principles of the plasma membrane that regulate signal transduction: commemorating the fortieth anniversary of Singer and Nicolson's fluid-mosaic model Annu. Rev. Cell Dev. Biol. 28 2012 215 250
    • (2012) Annu. Rev. Cell Dev. Biol. , vol.28 , pp. 215-250
    • Kusumi, A.1    Fujiwara, T.K.2    Suzuki, K.G.3
  • 27
    • 84861770491 scopus 로고    scopus 로고
    • Lipid rafts generate digital-like signal transduction in cell plasma membranes
    • K.G. Suzuki Lipid rafts generate digital-like signal transduction in cell plasma membranes Biotechnol. J. 7 2012 753 761
    • (2012) Biotechnol. J. , vol.7 , pp. 753-761
    • Suzuki, K.G.1
  • 28
    • 0036498797 scopus 로고    scopus 로고
    • Lipid raft heterogeneity in human peripheral blood T lymphoblasts: A mechanism for regulating the initiation of TCR signal transduction
    • A.E. Schade, and A.D. Levine Lipid raft heterogeneity in human peripheral blood T lymphoblasts: a mechanism for regulating the initiation of TCR signal transduction J. Immunol. 168 2002 2233 2239
    • (2002) J. Immunol. , vol.168 , pp. 2233-2239
    • Schade, A.E.1    Levine, A.D.2
  • 29
    • 80051937076 scopus 로고    scopus 로고
    • Intracellular lipid flux and membrane microdomains as organizing principles in inflammatory cell signaling
    • M.B. Fessler, and J.S. Parks Intracellular lipid flux and membrane microdomains as organizing principles in inflammatory cell signaling J. Immunol. 187 2011 1529 1535
    • (2011) J. Immunol. , vol.187 , pp. 1529-1535
    • Fessler, M.B.1    Parks, J.S.2
  • 30
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • K. Simons, and E. Ikonen Functional rafts in cell membranes Nature 387 1997 569 572
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 32
    • 84928404203 scopus 로고    scopus 로고
    • GPI-anchored proteins do not reside in ordered domains in the live cell plasma membrane
    • E. Sevcsik, and M. Brameshuber G.J. Schütz GPI-anchored proteins do not reside in ordered domains in the live cell plasma membrane Nat. Commun. 6 2015 6969
    • (2015) Nat. Commun. , vol.6 , pp. 6969
    • Sevcsik, E.1    Brameshuber, M.2    Schütz, G.J.3
  • 33
    • 33746581138 scopus 로고    scopus 로고
    • Dynamic molecular confinement in the plasma membrane by microdomains and the cytoskeleton meshwork
    • P.F. Lenne, and L. Wawrezinieck D. Marguet Dynamic molecular confinement in the plasma membrane by microdomains and the cytoskeleton meshwork EMBO J. 25 2006 3245 3256
    • (2006) EMBO J. , vol.25 , pp. 3245-3256
    • Lenne, P.F.1    Wawrezinieck, L.2    Marguet, D.3
  • 34
    • 1342306818 scopus 로고    scopus 로고
    • Nanoscale organization of multiple GPI-anchored proteins in living cell membranes
    • P. Sharma, and R. Varma S. Mayor Nanoscale organization of multiple GPI-anchored proteins in living cell membranes Cell 116 2004 577 589
    • (2004) Cell , vol.116 , pp. 577-589
    • Sharma, P.1    Varma, R.2    Mayor, S.3
  • 35
    • 57149125825 scopus 로고    scopus 로고
    • Nanoclusters of GPI-anchored proteins are formed by cortical actin-driven activity
    • D. Goswami, and K. Gowrishankar S. Mayor Nanoclusters of GPI-anchored proteins are formed by cortical actin-driven activity Cell 135 2008 1085 1097
    • (2008) Cell , vol.135 , pp. 1085-1097
    • Goswami, D.1    Gowrishankar, K.2    Mayor, S.3
  • 36
    • 84928392356 scopus 로고    scopus 로고
    • Transbilayer lipid interactions mediate nanoclustering of lipid-anchored proteins
    • R. Raghupathy, and A.A. Anilkumar S. Mayor Transbilayer lipid interactions mediate nanoclustering of lipid-anchored proteins Cell 161 2015 581 594
    • (2015) Cell , vol.161 , pp. 581-594
    • Raghupathy, R.1    Anilkumar, A.A.2    Mayor, S.3
  • 37
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • R. Varma, and S. Mayor GPI-anchored proteins are organized in submicron domains at the cell surface Nature 394 1998 798 801
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 38
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • D.A. Zacharias, and J.D. Violin R.Y. Tsien Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells Science 296 2002 913 916
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Tsien, R.Y.3
  • 39
    • 29744438833 scopus 로고    scopus 로고
    • Thinning out clusters while conserving stoichiometry of labeling
    • M. Moertelmaier, and M. Brameshuber H. Stockinger Thinning out clusters while conserving stoichiometry of labeling Appl. Phys. Lett. 87 2005 263903
    • (2005) Appl. Phys. Lett. , vol.87 , pp. 263903
    • Moertelmaier, M.1    Brameshuber, M.2    Stockinger, H.3
  • 40
    • 0030398406 scopus 로고    scopus 로고
    • Local stoichiometries determined by counting individual molecules
    • T. Schmidt, and G.J. Schütz H. Schindler Local stoichiometries determined by counting individual molecules Anal. Chem. 68 1996 4397 4401
    • (1996) Anal. Chem. , vol.68 , pp. 4397-4401
    • Schmidt, T.1    Schütz, G.J.2    Schindler, H.3
  • 41
    • 84856458463 scopus 로고    scopus 로고
    • Detection and quantification of biomolecular association in living cells using single-molecule microscopy
    • M. Brameshuber, and G.J. Schütz Detection and quantification of biomolecular association in living cells using single-molecule microscopy Methods Enzymol. 505 2012 159 186
    • (2012) Methods Enzymol. , vol.505 , pp. 159-186
    • Brameshuber, M.1    Schütz, G.J.2
  • 42
    • 84942683840 scopus 로고    scopus 로고
    • Lipidomic analysis reveals a radiosensitizing role of gamma-linolenic acid in glioma cells
    • O. Antal, and M. Péter L.G. Puskás Lipidomic analysis reveals a radiosensitizing role of gamma-linolenic acid in glioma cells Biochim. Biophys. Acta 1851 2015 1271 1282
    • (2015) Biochim. Biophys. Acta , vol.1851 , pp. 1271-1282
    • Antal, O.1    Péter, M.2    Puskás, L.G.3
  • 43
    • 0028800947 scopus 로고
    • Early redistribution of plasma membrane phosphatidylserine is a general feature of apoptosis regardless of the initiating stimulus: Inhibition by overexpression of Bcl-2 and Abl
    • S.J. Martin, and C.P. Reutelingsperger D.R. Green Early redistribution of plasma membrane phosphatidylserine is a general feature of apoptosis regardless of the initiating stimulus: inhibition by overexpression of Bcl-2 and Abl J. Exp. Med. 182 1995 1545 1556
    • (1995) J. Exp. Med. , vol.182 , pp. 1545-1556
    • Martin, S.J.1    Reutelingsperger, C.P.2    Green, D.R.3
  • 44
    • 0026352248 scopus 로고
    • GPI-anchored cell-surface molecules complexed to protein tyrosine kinases
    • I. Stefanová, and V. Horejsí H. Stockinger GPI-anchored cell-surface molecules complexed to protein tyrosine kinases Science 254 1991 1016 1019
    • (1991) Science , vol.254 , pp. 1016-1019
    • Stefanová, I.1    Horejsí, V.2    Stockinger, H.3
  • 45
    • 84898635046 scopus 로고    scopus 로고
    • Lck mediates signal transmission from CD59 to the TCR/CD3 pathway in Jurkat T cells
    • A.M. Lipp, and K. Juhasz A. Sonnleitner Lck mediates signal transmission from CD59 to the TCR/CD3 pathway in Jurkat T cells PLoS One 9 2014 e85934
    • (2014) PLoS One , vol.9 , pp. e85934
    • Lipp, A.M.1    Juhasz, K.2    Sonnleitner, A.3
  • 46
    • 34249074042 scopus 로고    scopus 로고
    • Dynamic recruitment of phospholipase C gamma at transiently immobilized GPI-anchored receptor clusters induces IP3-Ca2+ signaling: Single-molecule tracking study 2
    • K.G. Suzuki, and T.K. Fujiwara A. Kusumi Dynamic recruitment of phospholipase C gamma at transiently immobilized GPI-anchored receptor clusters induces IP3-Ca2+ signaling: single-molecule tracking study 2 J. Cell Biol. 177 2007 731 742
    • (2007) J. Cell Biol. , vol.177 , pp. 731-742
    • Suzuki, K.G.1    Fujiwara, T.K.2    Kusumi, A.3
  • 47
    • 34249066421 scopus 로고    scopus 로고
    • GPI-anchored receptor clusters transiently recruit Lyn and G alpha for temporary cluster immobilization and Lyn activation: Single-molecule tracking study 1
    • K.G. Suzuki, and T.K. Fujiwara A. Kusumi GPI-anchored receptor clusters transiently recruit Lyn and G alpha for temporary cluster immobilization and Lyn activation: single-molecule tracking study 1 J. Cell Biol. 177 2007 717 730
    • (2007) J. Cell Biol. , vol.177 , pp. 717-730
    • Suzuki, K.G.1    Fujiwara, T.K.2    Kusumi, A.3
  • 48
    • 44449119583 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometry identifies substrates and products of lipoprotein-associated phospholipase A2 in oxidized human low density lipoprotein
    • B. Davis, and G. Koster A.D. Postle Electrospray ionization mass spectrometry identifies substrates and products of lipoprotein-associated phospholipase A2 in oxidized human low density lipoprotein J. Biol. Chem. 283 2008 6428 6437
    • (2008) J. Biol. Chem. , vol.283 , pp. 6428-6437
    • Davis, B.1    Koster, G.2    Postle, A.D.3
  • 49
    • 0033065591 scopus 로고    scopus 로고
    • A microscopic interaction model of maximum solubility of cholesterol in lipid bilayers
    • J. Huang, and G.W. Feigenson A microscopic interaction model of maximum solubility of cholesterol in lipid bilayers Biophys. J. 76 1999 2142 2157
    • (1999) Biophys. J. , vol.76 , pp. 2142-2157
    • Huang, J.1    Feigenson, G.W.2
  • 50
    • 0032211769 scopus 로고    scopus 로고
    • Signal transduction of stress via ceramide
    • S. Mathias, L.A. Peña, and R.N. Kolesnick Signal transduction of stress via ceramide Biochem. J. 335 1998 465 480
    • (1998) Biochem. J. , vol.335 , pp. 465-480
    • Mathias, S.1    Peña, L.A.2    Kolesnick, R.N.3
  • 51
    • 1642293929 scopus 로고    scopus 로고
    • Ceramide selectively displaces cholesterol from ordered lipid domains (rafts): Implications for lipid raft structure and function
    • Megha, and E. London Ceramide selectively displaces cholesterol from ordered lipid domains (rafts): implications for lipid raft structure and function J. Biol. Chem. 279 2004 9997 10004
    • (2004) J. Biol. Chem. , vol.279 , pp. 9997-10004
    • Megha1    London, E.2
  • 52
    • 33746855864 scopus 로고    scopus 로고
    • Cholesterol precursors stabilize ordinary and ceramide-rich ordered lipid domains (lipid rafts) to different degrees. Implications for the Bloch hypothesis and sterol biosynthesis disorders
    • O.B. Megha, O. Bakht, and E. London Cholesterol precursors stabilize ordinary and ceramide-rich ordered lipid domains (lipid rafts) to different degrees. Implications for the Bloch hypothesis and sterol biosynthesis disorders J. Biol. Chem. 281 2006 21903 21913
    • (2006) J. Biol. Chem. , vol.281 , pp. 21903-21913
    • Megha, O.B.1    Bakht, O.2    London, E.3
  • 53
    • 34250742501 scopus 로고    scopus 로고
    • Biological aspects of ceramide-enriched membrane domains
    • H. Grassmé, J. Riethmüller, and E. Gulbins Biological aspects of ceramide-enriched membrane domains Prog. Lipid Res. 46 2007 161 170
    • (2007) Prog. Lipid Res. , vol.46 , pp. 161-170
    • Grassmé, H.1    Riethmüller, J.2    Gulbins, E.3
  • 54
    • 58149204290 scopus 로고    scopus 로고
    • Ceramide-enriched membrane domains - Structure and function
    • Y. Zhang, and X. Li E. Gulbins Ceramide-enriched membrane domains - structure and function Biochim. Biophys. Acta 1788 2009 178 183
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 178-183
    • Zhang, Y.1    Li, X.2    Gulbins, E.3
  • 55
    • 0024419722 scopus 로고
    • Effects of sphingomyelin degradation on cell cholesterol oxidizability and steady-state distribution between the cell surface and the cell interior
    • J.P. Slotte, and G. Hedström S. Ekman Effects of sphingomyelin degradation on cell cholesterol oxidizability and steady-state distribution between the cell surface and the cell interior Biochim. Biophys. Acta 985 1989 90 96
    • (1989) Biochim. Biophys. Acta , vol.985 , pp. 90-96
    • Slotte, J.P.1    Hedström, G.2    Ekman, S.3
  • 56
    • 61349094652 scopus 로고    scopus 로고
    • Direct observation of the nanoscale dynamics of membrane lipids in a living cell
    • C. Eggeling, and C. Ringemann S.W. Hell Direct observation of the nanoscale dynamics of membrane lipids in a living cell Nature 457 2009 1159 1162
    • (2009) Nature , vol.457 , pp. 1159-1162
    • Eggeling, C.1    Ringemann, C.2    Hell, S.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.