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Volumn 216, Issue 4, 2017, Pages 1183-1204

Raft-based sphingomyelin interactions revealed by new fluorescent sphingomyelin analogs

Author keywords

[No Author keywords available]

Indexed keywords

CD59 ANTIGEN; CHOLINE; DETERGENT; FC EPSILON RI PROTEIN; GLYCOL; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED PROTEIN; HOMODIMER; MONOMER; PHOSPHOLIPID DERIVATIVE; PROTEIN; SPHINGOMYELIN; UNCLASSIFIED DRUG; CD59 PROTEIN, HUMAN; CHOLESTEROL; FLUORESCENT DYE; GLYCOSYLPHOSPHATIDYLINOSITOL; SPHINGOLIPID;

EID: 85021851513     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201607086     Document Type: Article
Times cited : (105)

References (62)
  • 1
    • 84897954094 scopus 로고    scopus 로고
    • Imaging local sphingomyelin-rich domains in the plasma membrane using specific probes and advanced microscopy
    • Abe, M., and T. Kobayashi. 2014. Imaging local sphingomyelin-rich domains in the plasma membrane using specific probes and advanced microscopy. Biochim. Biophys. Acta. 1841:720-726. http://dx.doi.org/10.1016/j.bbalip.2013.07.003
    • (2014) Biochim. Biophys. Acta , vol.1841 , pp. 720-726
    • Abe, M.1    Kobayashi, T.2
  • 2
    • 77953161754 scopus 로고    scopus 로고
    • A molecular view of the cholesterol condensing effect in DOPC lipid bilayers
    • Alwarawrah, M., J. Dai, and J. Huang. 2010. A molecular view of the cholesterol condensing effect in DOPC lipid bilayers. J. Phys. Chem. B. 114:7516-7523. http://dx.doi.org/10.1021/jp101415g
    • (2010) J. Phys. Chem. B , vol.114 , pp. 7516-7523
    • Alwarawrah, M.1    Dai, J.2    Huang, J.3
  • 5
    • 33847641401 scopus 로고    scopus 로고
    • Large-scale fluid/fluid phase separation of proteins and lipids in giant plasma membrane vesicles
    • Baumgart, T., A.T. Hammond, P. Sengupta, S.T. Hess, D.A. Holowka, B.A. Baird, and W.W. Webb. 2007. Large-scale fluid/fluid phase separation of proteins and lipids in giant plasma membrane vesicles. Proc. Natl. Acad. Sci. USA. 104:3165-3170. http://dx.doi.org/10.1073/pnas.0611357104
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 3165-3170
    • Baumgart, T.1    Hammond, A.T.2    Sengupta, P.3    Hess, S.T.4    Holowka, D.A.5    Baird, B.A.6    Webb, W.W.7
  • 6
    • 84947201684 scopus 로고    scopus 로고
    • Self-calibrated line-scan STED-FCS to quantify lipid dynamics in model and cell membranes
    • Benda, A., Y. Ma, and K. Gaus. 2015. Self-calibrated line-scan STED-FCS to quantify lipid dynamics in model and cell membranes. Biophys. J. 108:596-609. http://dx.doi.org/10.1016/j.bpj.2014.12.007
    • (2015) Biophys. J , vol.108 , pp. 596-609
    • Benda, A.1    Ma, Y.2    Gaus, K.3
  • 8
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh, E.G., and W.J. Dyer. 1959. A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 37:911-917. http://dx.doi.org/10.1139/o59-099
    • (1959) Can. J. Biochem. Physiol , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 9
    • 84921731319 scopus 로고    scopus 로고
    • Interaction of cholesterol in ternary lipid mixtures investigated using single-molecule fluorescence
    • DeWitt, B.N., and R.C. Dunn. 2015. Interaction of cholesterol in ternary lipid mixtures investigated using single-molecule fluorescence. Langmuir. 31:995-1004. http://dx.doi.org/10.1021/la503797w
    • (2015) Langmuir , vol.31 , pp. 995-1004
    • DeWitt, B.N.1    Dunn, R.C.2
  • 10
    • 84902140931 scopus 로고    scopus 로고
    • Membrane raft association is a determinant of plasma membrane localization
    • Diaz-Rohrer, B.B., K.R. Levental, K. Simons, and I. Levental. 2014. Membrane raft association is a determinant of plasma membrane localization. Proc. Natl. Acad. Sci. USA. 111:8500-8505. http://dx.doi.org/10.1073/pnas.1404582111
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 8500-8505
    • Diaz-Rohrer, B.B.1    Levental, K.R.2    Simons, K.3    Levental, I.4
  • 11
    • 50549175610 scopus 로고
    • The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes
    • Dodge, J.T., C. Mitchell, and D.J. Hanahan. 1963. The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes. Arch. Biochem. Biophys. 100:119-130. http://dx.doi.org/10.1016/0003-9861(63)90042-0
    • (1963) Arch. Biochem. Biophys , vol.100 , pp. 119-130
    • Dodge, J.T.1    Mitchell, C.2    Hanahan, D.J.3
  • 13
    • 77957699450 scopus 로고    scopus 로고
    • Precise and millidegree stable temperature control for fluorescence imaging: Application to phase transitions in lipid membranes
    • Farkas, E.R., and W.W. Webb. 2010. Precise and millidegree stable temperature control for fluorescence imaging: Application to phase transitions in lipid membranes. Rev. Sci. Instrum. 81:093704-093708. http://dx.doi.org/10.1063/1.3483263
    • (2010) Rev. Sci. Instrum , vol.81
    • Farkas, E.R.1    Webb, W.W.2
  • 14
    • 1142274304 scopus 로고    scopus 로고
    • Lipid lateral diffusion in ordered and disordered phases in raft mixtures
    • Filippov, A., G. Orädd, and G. Lindblom. 2004. Lipid lateral diffusion in ordered and disordered phases in raft mixtures. Biophys. J. 86:891-896. http://dx.doi.org/10.1016/S0006-3495(04)74164-8
    • (2004) Biophys. J , vol.86 , pp. 891-896
    • Filippov, A.1    Orädd, G.2    Lindblom, G.3
  • 16
    • 84862172488 scopus 로고    scopus 로고
    • Effects of chemical modification of sphingomyelin ammonium group on formation of liquid-ordered phase
    • Goretta, S.A., M. Kinoshita, S. Mori, H. Tsuchikawa, N. Matsumori, and M. Murata. 2012. Effects of chemical modification of sphingomyelin ammonium group on formation of liquid-ordered phase. Bioorg. Med. Chem. 20:4012-4019. http://dx.doi.org/10.1016/j.bmc.2012.05.015
    • (2012) Bioorg. Med. Chem , vol.20 , pp. 4012-4019
    • Goretta, S.A.1    Kinoshita, M.2    Mori, S.3    Tsuchikawa, H.4    Matsumori, N.5    Murata, M.6
  • 17
    • 78649287162 scopus 로고    scopus 로고
    • Comparison of three ternary lipid bilayer mixtures: FRET and ESR reveal nanodomains
    • Heberle, F.A., J. Wu, S.L. Goh, R.S. Petruzielo, and G.W. Feigenson. 2010. Comparison of three ternary lipid bilayer mixtures: FRET and ESR reveal nanodomains. Biophys. J. 99:3309-3318. http://dx.doi.org/10.1016/j.bpj.2010.09.064
    • (2010) Biophys. J , vol.99 , pp. 3309-3318
    • Heberle, F.A.1    Wu, J.2    Goh, S.L.3    Petruzielo, R.S.4    Feigenson, G.W.5
  • 19
    • 84974602679 scopus 로고    scopus 로고
    • Roles for lipid heterogeneity in immunoreceptor signaling
    • Holowka, D., and B. Baird. 2016. Roles for lipid heterogeneity in immunoreceptor signaling. Biochim. Biophys. Acta. 1861(8 Pt B):830-836. http://dx.doi.org/10.1016/j.bbalip.2016.03.019
    • (2016) Biochim. Biophys. Acta , vol.1861 , Issue.8 , pp. 830-836
    • Holowka, D.1    Baird, B.2
  • 21
    • 84872008437 scopus 로고    scopus 로고
    • STED microscopy detects and quantifies liquid phase separation in lipid membranes using a new far-red emitting fluorescent phosphoglycerolipid analogue
    • Honigmann, A., V. Mueller, S.W. Hell, and C. Eggeling. 2013. STED microscopy detects and quantifies liquid phase separation in lipid membranes using a new far-red emitting fluorescent phosphoglycerolipid analogue. Faraday Discuss. 161:77-89. http://dx.doi.org/10.1039/C2FD20107K
    • (2013) Faraday Discuss , vol.161 , pp. 77-89
    • Honigmann, A.1    Mueller, V.2    Hell, S.W.3    Eggeling, C.4
  • 22
    • 84922460988 scopus 로고    scopus 로고
    • Scanning STED-FCS reveals spatiotemporal heterogeneity of lipid interaction in the plasma membrane of living cells
    • Honigmann, A., V. Mueller, H. Ta, A. Schoenle, E. Sezgin, S.W. Hell, and C. Eggeling. 2014. Scanning STED-FCS reveals spatiotemporal heterogeneity of lipid interaction in the plasma membrane of living cells. Nat. Commun. 5:5412. http://dx.doi.org/10.1038/ncomms6412
    • (2014) Nat. Commun , vol.5 , pp. 5412
    • Honigmann, A.1    Mueller, V.2    Ta, H.3    Schoenle, A.4    Sezgin, E.5    Hell, S.W.6    Eggeling, C.7
  • 23
    • 84883073819 scopus 로고    scopus 로고
    • Development of fluorogenic probes for quick no-wash live-cell imaging of intracellular proteins
    • Hori, Y., T. Norinobu, M. Sato, K. Arita, M. Shirakawa, and K. Kikuchi. 2013. Development of fluorogenic probes for quick no-wash live-cell imaging of intracellular proteins. J. Am. Chem. Soc. 135:12360-12365. http://dx.doi.org/10.1021/ja405745v
    • (2013) J. Am. Chem. Soc , vol.135 , pp. 12360-12365
    • Hori, Y.1    Norinobu, T.2    Sato, M.3    Arita, K.4    Shirakawa, M.5    Kikuchi, K.6
  • 24
    • 84926315842 scopus 로고    scopus 로고
    • Effect of receptor dimerization on membrane lipid raft structure continuously quantified on single cells by camera based fluorescence correlation spectroscopy
    • Huang, H., M.F. Simsek, W. Jin, and A. Pralle. 2015. Effect of receptor dimerization on membrane lipid raft structure continuously quantified on single cells by camera based fluorescence correlation spectroscopy. PLoS One. 10:e0121777. http://dx.doi.org/10.1371/journal.pone.0121777
    • (2015) PLoS One , vol.10
    • Huang, H.1    Simsek, M.F.2    Jin, W.3    Pralle, A.4
  • 25
    • 0041461861 scopus 로고    scopus 로고
    • Probing lipid mobility of raft-exhibiting model membranes by fluorescence correlation spectroscopy
    • Kahya, N., D. Scherfeld, K. Bacia, B. Poolman, and P. Schwille. 2003. Probing lipid mobility of raft-exhibiting model membranes by fluorescence correlation spectroscopy. J. Biol. Chem. 278:28109-28115. http://dx.doi.org/10.1074/jbc.M302969200
    • (2003) J. Biol. Chem , vol.278 , pp. 28109-28115
    • Kahya, N.1    Scherfeld, D.2    Bacia, K.3    Poolman, B.4    Schwille, P.5
  • 26
    • 79551711208 scopus 로고    scopus 로고
    • Full characterization of GPCR monomer-dimer dynamic equilibrium by single molecule imaging
    • Kasai, R.S., K.G.N. Suzuki, E.R. Prossnitz, I. Koyama-Honda, C. Nakada, T.K. Fujiwara, and A. Kusumi. 2011. Full characterization of GPCR monomer-dimer dynamic equilibrium by single molecule imaging. J. Cell Biol. 192:463-480. http://dx.doi.org/10.1083/jcb.201009128
    • (2011) J. Cell Biol , vol.192 , pp. 463-480
    • Kasai, R.S.1    Suzuki, K.G.N.2    Prossnitz, E.R.3    Koyama-Honda, I.4    Nakada, C.5    Fujiwara, T.K.6    Kusumi, A.7
  • 27
    • 84962092460 scopus 로고    scopus 로고
    • Detectors for evaluating the cellular landscape of sphingomyelin-and cholesterol-rich membrane domains
    • Kishimoto, T., R. Ishitsuka, and T. Kobayashi. 2016. Detectors for evaluating the cellular landscape of sphingomyelin-and cholesterol-rich membrane domains. Biochim. Biophys. Acta. 1861(8 Pt B):812-829. http://dx.doi.org/10.1016/j.bbalip.2016.03.013
    • (2016) Biochim. Biophys. Acta , vol.1861 , Issue.8 , pp. 812-829
    • Kishimoto, T.1    Ishitsuka, R.2    Kobayashi, T.3
  • 28
    • 21244442348 scopus 로고    scopus 로고
    • Spatial and functional heterogeneity of sphingolipid-rich membrane domains
    • Kiyokawa, E., T. Baba, N. Otsuka, A. Makino, S. Ohno, and T. Kobayashi. 2005. Spatial and functional heterogeneity of sphingolipid-rich membrane domains. J. Biol. Chem. 280:24072-24084. http://dx.doi.org/10.1074/jbc.M502244200
    • (2005) J. Biol. Chem , vol.280 , pp. 24072-24084
    • Kiyokawa, E.1    Baba, T.2    Otsuka, N.3    Makino, A.4    Ohno, S.5    Kobayashi, T.6
  • 29
    • 84892674236 scopus 로고    scopus 로고
    • Fluorescent probes for lipid rafts: From model membranes to living cells
    • Klymchenko, A.S., and R. Kreder. 2014. Fluorescent probes for lipid rafts: From model membranes to living cells. Chem. Biol. 21:97-113. http://dx.doi.org/10.1016/j.chembiol.2013.11.009
    • (2014) Chem. Biol , vol.21 , pp. 97-113
    • Klymchenko, A.S.1    Kreder, R.2
  • 31
    • 0033587719 scopus 로고    scopus 로고
    • Characterization of lipid bilayer phases by confocal microscopy and fluorescence correlation spectroscopy
    • Korlach, J., P. Schwille, W.W. Webb, and G.W. Feigenson. 1999. Characterization of lipid bilayer phases by confocal microscopy and fluorescence correlation spectroscopy. Proc. Natl. Acad. Sci. USA. 96:8461-8466. http://dx.doi.org/10.1073/pnas.96.15.8461
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8461-8466
    • Korlach, J.1    Schwille, P.2    Webb, W.W.3    Feigenson, G.W.4
  • 32
    • 20544457766 scopus 로고    scopus 로고
    • Fluorescence imaging for monitoring the colocalization of two single molecules in living cells
    • Koyama-Honda, I., K. Ritchie, T. Fujiwara, R. Iino, H. Murakoshi, R.S. Kasai, and A. Kusumi. 2005. Fluorescence imaging for monitoring the colocalization of two single molecules in living cells. Biophys. J. 88:2126-2136. http://dx.doi.org/10.1529/biophysj.104.048967
    • (2005) Biophys. J , vol.88 , pp. 2126-2136
    • Koyama-Honda, I.1    Ritchie, K.2    Fujiwara, T.3    Iino, R.4    Murakoshi, H.5    Kasai, R.S.6    Kusumi, A.7
  • 34
    • 1842432088 scopus 로고    scopus 로고
    • Molecular dynamics and interactions for creation of stimulation-induced stabilized rafts from small unstable steady-state rafts
    • Kusumi, A., I. Koyama-Honda, and K. Suzuki. 2004. Molecular dynamics and interactions for creation of stimulation-induced stabilized rafts from small unstable steady-state rafts. Traffic. 5:213-230. http://dx.doi.org/10.1111/j.1600-0854.2004.0178.x
    • (2004) Traffic , vol.5 , pp. 213-230
    • Kusumi, A.1    Koyama-Honda, I.2    Suzuki, K.3
  • 35
    • 84929490384 scopus 로고    scopus 로고
    • Ordered raft domains induced by outer leaflet sphingomyelin in cholesterol-rich asymmetric vesicles
    • Lin, Q., and E. London. 2015. Ordered raft domains induced by outer leaflet sphingomyelin in cholesterol-rich asymmetric vesicles. Biophys. J. 108:2212-2222. http://dx.doi.org/10.1016/j.bpj.2015.03.056
    • (2015) Biophys. J , vol.108 , pp. 2212-2222
    • Lin, Q.1    London, E.2
  • 36
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood, D., and K. Simons. 2010. Lipid rafts as a membrane-organizing principle. Science. 327:46-50. http://dx.doi.org/10.1126/science.1174621
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 37
    • 0021072977 scopus 로고
    • Analysis of brain lipids by high performance thin-layer chromatography and densitometry
    • Macala, L.J., R.K. Yu, and S. Ando. 1983. Analysis of brain lipids by high performance thin-layer chromatography and densitometry. J. Lipid Res. 24:1243-1250
    • (1983) J. Lipid Res , vol.24 , pp. 1243-1250
    • Macala, L.J.1    Yu, R.K.2    Ando, S.3
  • 38
    • 84928562086 scopus 로고    scopus 로고
    • Visualization of the heterogeneous membrane distribution of sphingomyelin associated with cytokinesis, cell polarity, and sphingolipidosis
    • Makino, A., M. Abe, M. Murate, T. Inaba, N. Yilmaz, F. Hullin-Matsuda, T. Kishimoto, N.L. Schieber, T. Taguchi, H. Arai, et al. 2015. Visualization of the heterogeneous membrane distribution of sphingomyelin associated with cytokinesis, cell polarity, and sphingolipidosis. FAS EB J. 29:477-493. http://dx.doi.org/10.1096/fj.13-247585
    • (2015) FAS EB J , vol.29 , pp. 477-493
    • Makino, A.1    Abe, M.2    Murate, M.3    Inaba, T.4    Yilmaz, N.5    Hullin-Matsuda, F.6    Kishimoto, T.7    Schieber, N.L.8    Taguchi, T.9    Arai, H.10
  • 40
    • 84865532003 scopus 로고    scopus 로고
    • Functional convergence of hopanoids and sterols in membrane ordering
    • Sáenz, J.P., E. Sezgin, P. Schwille, and K. Simons. 2012. Functional convergence of hopanoids and sterols in membrane ordering. Proc. Natl. Acad. Sci. USA. 109:14236-14240. http://dx.doi.org/10.1073/pnas.1212141109
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 14236-14240
    • Sáenz, J.P.1    Sezgin, E.2    Schwille, P.3    Simons, K.4
  • 42
    • 77951082775 scopus 로고    scopus 로고
    • Fast molecular tracking maps nanoscale dynamics of plasma membrane lipids
    • Sahl, S.J., M. Leutenegger, M. Hilbert, S.W. Hell, and C. Eggeling. 2010. Fast molecular tracking maps nanoscale dynamics of plasma membrane lipids. Proc. Natl. Acad. Sci. USA. 107:6829-6834. http://dx.doi.org/10.1073/pnas.0912894107
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 6829-6834
    • Sahl, S.J.1    Leutenegger, M.2    Hilbert, M.3    Hell, S.W.4    Eggeling, C.5
  • 43
    • 70449631409 scopus 로고    scopus 로고
    • A modular synthesis of alkynyl-phosphocholine headgroups for labeling sphingomyelin and phosphatidylcholine
    • Sandbhor, M.S., J.A. Key, I.S. Strelkov, and C.W. Cairo. 2009. A modular synthesis of alkynyl-phosphocholine headgroups for labeling sphingomyelin and phosphatidylcholine. J. Org. Chem. 74:8669-8674. http://dx.doi.org/10.1021/jo901824h
    • (2009) J. Org. Chem , vol.74 , pp. 8669-8674
    • Sandbhor, M.S.1    Key, J.A.2    Strelkov, I.S.3    Cairo, C.W.4
  • 46
    • 0038363367 scopus 로고    scopus 로고
    • The adipocyte plasma membrane caveolin functional/structural organization is necessary for the efficient endocytosis of GLUT4
    • Shigematsu, S., R.T. Watson, A.H. Khan, and J.E. Pessin. 2003. The adipocyte plasma membrane caveolin functional/structural organization is necessary for the efficient endocytosis of GLUT4. J. Biol. Chem. 278:10683-10690. http://dx.doi.org/10.1074/jbc.M208563200
    • (2003) J. Biol. Chem , vol.278 , pp. 10683-10690
    • Shigematsu, S.1    Watson, R.T.2    Khan, A.H.3    Pessin, J.E.4
  • 47
    • 84956657733 scopus 로고    scopus 로고
    • Cell membranes: A subjective perspective
    • Simons, K. 2016. Cell membranes: A subjective perspective. Biochim. Biophys. Acta. 1858:2569-2572. http://dx.doi.org/10.1016/j.bbamem.2016.01.023
    • (2016) Biochim. Biophys. Acta , vol.1858 , pp. 2569-2572
    • Simons, K.1
  • 48
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K., and E. Ikonen. 1997. Functional rafts in cell membranes. Nature. 387:569-572. http://dx.doi.org/10.1038/42408
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 49
    • 0029162080 scopus 로고
    • Detection of temporary lateral confinement of membrane proteins using single-particle tracking analysis
    • Simson, R., E.D. Sheets, and K. Jacobson. 1995. Detection of temporary lateral confinement of membrane proteins using single-particle tracking analysis. Biophys. J. 69:989-993 http://dx.doi.org/10.1016%2FS0006-3495(95)79972-6. http://dx.doi.org/10.1016/S0006-3495(95)79972-6
    • (1995) Biophys. J , vol.69 , pp. 989-993
    • Simson, R.1    Sheets, E.D.2    Jacobson, K.3
  • 50
    • 0020588514 scopus 로고
    • Biomedical image processing
    • Sternberg, R.S. 1983. Biomedical image processing. Computer 16:22-34. http://dx.doi.org/10.1109/MC.1983.1654163
    • (1983) Computer , vol.16 , pp. 22-34
    • Sternberg, R.S.1
  • 51
    • 34249066421 scopus 로고    scopus 로고
    • GPI-anchored receptor clusters transiently recruit Lyn and G a for temporary cluster immobilization and Lyn activation: Single-molecule tracking study 1
    • Suzuki, K.G.N., T.K. Fujiwara, F. Sanematsu, R. Iino, M. Edidin, and A. Kusumi. 2007. GPI-anchored receptor clusters transiently recruit Lyn and G a for temporary cluster immobilization and Lyn activation: Single-molecule tracking study 1. J. Cell Biol. 177:717-730. http://dx.doi.org/10.1083/jcb.200609174
    • (2007) J. Cell Biol , vol.177 , pp. 717-730
    • Suzuki, K.G.N.1    Fujiwara, T.K.2    Sanematsu, F.3    Iino, R.4    Edidin, M.5    Kusumi, A.6
  • 52
    • 34249074042 scopus 로고    scopus 로고
    • Dynamic recruitment of phospholipase C γ at transiently immobilized GPIanchored receptor clusters induces IP3-Ca2+ signaling: Single-molecule tracking study 2
    • Suzuki, K.G.N., T.K. Fujiwara, M. Edidin, and A. Kusumi. 2007. Dynamic recruitment of phospholipase C γ at transiently immobilized GPIanchored receptor clusters induces IP3-Ca2+ signaling: Single-molecule tracking study 2. J. Cell Biol. 177:731-742. http://dx.doi.org/10.1083/jcb.200609175
    • (2007) J. Cell Biol , vol.177 , pp. 731-742
    • Suzuki, K.G.N.1    Fujiwara, T.K.2    Edidin, M.3    Kusumi, A.4
  • 54
    • 77951912441 scopus 로고    scopus 로고
    • Sphingolipid topology and the dynamic organization and function of membrane proteins
    • van Meer, G., and S. Hoetzl. 2010. Sphingolipid topology and the dynamic organization and function of membrane proteins. FEBS Lett. 584:1800-1805. http://dx.doi.org/10.1016/j.febslet.2009.10.020
    • (2010) FEBS Lett , vol.584 , pp. 1800-1805
    • van Meer, G.1    Hoetzl, S.2
  • 57
    • 84926443144 scopus 로고    scopus 로고
    • Hemagglutinin clusters in the plasma membrane are not enriched with cholesterol and sphingolipids
    • Wilson, R.L., J.F. Frisz, H.A. Klitzing, J. Zimmerberg, P.K. Weber, and M.L. Kraft. 2015. Hemagglutinin clusters in the plasma membrane are not enriched with cholesterol and sphingolipids. Biophys. J. 108:1652-1659 http://dx.doi.org//10.1016/j.bpj.2015.02.026. http://dx.doi.org/10.1016/j.bpj.2015.02.026
    • (2015) Biophys. J , vol.108 , pp. 1652-1659
    • Wilson, R.L.1    Frisz, J.F.2    Klitzing, H.A.3    Zimmerberg, J.4    Weber, P.K.5    Kraft, M.L.6
  • 58
    • 84878282705 scopus 로고    scopus 로고
    • Microarrays of phospholipid bilayers generated by inkjet printing
    • Yamada, M., H. Imaishi, and K. Morigaki. 2013. Microarrays of phospholipid bilayers generated by inkjet printing. Langmuir. 29:6404-6408. http://dx.doi.org/10.1021/la400570h
    • (2013) Langmuir , vol.29 , pp. 6404-6408
    • Yamada, M.1    Imaishi, H.2    Morigaki, K.3
  • 59
    • 84893496183 scopus 로고    scopus 로고
    • Detailed comparison of deuterium quadrupole profiles between sphingomyelin and phosphatidylcholine bilayers
    • Yasuda, T., M. Kinoshita, M. Murata, and N. Matsumori. 2014. Detailed comparison of deuterium quadrupole profiles between sphingomyelin and phosphatidylcholine bilayers. Biophys. J. 106:631-638. http://dx.doi.org/10.1016/j.bpj.2013.12.034
    • (2014) Biophys. J , vol.106 , pp. 631-638
    • Yasuda, T.1    Kinoshita, M.2    Murata, M.3    Matsumori, N.4
  • 60
    • 84930001051 scopus 로고    scopus 로고
    • Deuterium NMR of raft model membranes reveals domain-specific order profiles and compositional distribution
    • Yasuda, T., H. Tsuchikawa, M. Murata, and N. Matsumori. 2015. Deuterium NMR of raft model membranes reveals domain-specific order profiles and compositional distribution. Biophys. J. 108:2502-2506. http://dx.doi.org/10.1016/j.bpj.2015.04.008
    • (2015) Biophys. J , vol.108 , pp. 2502-2506
    • Yasuda, T.1    Tsuchikawa, H.2    Murata, M.3    Matsumori, N.4
  • 62
    • 84969377019 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol-anchored proteins: Membrane organization and transport
    • Zurzolo, C., and K. Simons. 2016. Glycosylphosphatidylinositol-anchored proteins: Membrane organization and transport. Biochim. Biophys. Acta. 1858:632-639. http://dx.doi.org/10.1016/j.bbamem.2015.12.018
    • (2016) Biochim. Biophys. Acta , vol.1858 , pp. 632-639
    • Zurzolo, C.1    Simons, K.2


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