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Volumn 1788, Issue 1, 2009, Pages 209-224

FRET analysis of domain formation and properties in complex membrane systems

Author keywords

Fluorescence; Lipid bilayer; Lipid raft; Membrane phase separation; Phase diagram

Indexed keywords

CERAMIDE; CHOLESTEROL; LIPID; NANOMATERIAL; PHOSPHOLIPID; PROTEIN;

EID: 58149201036     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2008.10.012     Document Type: Review
Times cited : (46)

References (124)
  • 1
    • 0015514472 scopus 로고
    • The fluid mosaic model of the structure of cell membranes
    • Singer S.J., and Nicholson G.L. The fluid mosaic model of the structure of cell membranes. Science 175 (1972) 720-731
    • (1972) Science , vol.175 , pp. 720-731
    • Singer, S.J.1    Nicholson, G.L.2
  • 4
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K., and Ikonen E. Functional rafts in cell membranes. Nature 387 (1997) 569-572
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 5
    • 0026658542 scopus 로고
    • Lateral diffusion and percolation in two-phase, two-component lipid bilayers. Topology of the solid-phase domains in-plane and across the lipid bilayer
    • Almeida P.F.F., Vaz W.L.C., and Thompson T.E. Lateral diffusion and percolation in two-phase, two-component lipid bilayers. Topology of the solid-phase domains in-plane and across the lipid bilayer. Biochemistry 31 (1992) 7198-7210
    • (1992) Biochemistry , vol.31 , pp. 7198-7210
    • Almeida, P.F.F.1    Vaz, W.L.C.2    Thompson, T.E.3
  • 6
    • 0036154306 scopus 로고    scopus 로고
    • Nonequilibrium phenomena in the phase separation of a two-component lipid bilayer
    • de Almeida R.F.M., Loura L.M.S., Fedorov A., and Prieto M. Nonequilibrium phenomena in the phase separation of a two-component lipid bilayer. Biophys. J. 82 (2002) 823-834
    • (2002) Biophys. J. , vol.82 , pp. 823-834
    • de Almeida, R.F.M.1    Loura, L.M.S.2    Fedorov, A.3    Prieto, M.4
  • 7
    • 0347607292 scopus 로고    scopus 로고
    • Nonequilibrium lipid domain growth in the gel-fluid two phase region of a DC16PC-DC22PC lipid mixture investigated by Monte-Carlo computer simulation, FT-IR and fluorescence spectroscopy
    • Jørgensen K., Klinger A., and Biltonen R.L. Nonequilibrium lipid domain growth in the gel-fluid two phase region of a DC16PC-DC22PC lipid mixture investigated by Monte-Carlo computer simulation, FT-IR and fluorescence spectroscopy. J. Phys. Chem. 104 (2000) 11763-11773
    • (2000) J. Phys. Chem. , vol.104 , pp. 11763-11773
    • Jørgensen, K.1    Klinger, A.2    Biltonen, R.L.3
  • 9
    • 1842536499 scopus 로고    scopus 로고
    • Rafts: scale-dependent, active lipid organization at the cell surface
    • Mayor S., and Rao M. Rafts: scale-dependent, active lipid organization at the cell surface. Traffic 5 (2004) 231-240
    • (2004) Traffic , vol.5 , pp. 231-240
    • Mayor, S.1    Rao, M.2
  • 10
    • 33845901815 scopus 로고    scopus 로고
    • Lipid rafts: at a crossroad between cell biology and physics
    • Jacobson K., Mouritsen O.G., and Anderson R.G. Lipid rafts: at a crossroad between cell biology and physics. Nat. Cell Biol. 9 (2007) 7-14
    • (2007) Nat. Cell Biol. , vol.9 , pp. 7-14
    • Jacobson, K.1    Mouritsen, O.G.2    Anderson, R.G.3
  • 11
    • 17844364513 scopus 로고    scopus 로고
    • Paradigm shift of the plasma membrane concept from the two-dimensional continuum fluid to the partitioned fluid: high-speed single-molecule tracking of membrane molecules
    • Kusumi A., Nakada C., Ritchie K., Murase K., Suzuki K., Murakoshi H., Kasai R.S., Kondo J., and Fujiwara T. Paradigm shift of the plasma membrane concept from the two-dimensional continuum fluid to the partitioned fluid: high-speed single-molecule tracking of membrane molecules. Annu. Rev. Biophys. Biomol. Struct. 34 (2005) 351-378
    • (2005) Annu. Rev. Biophys. Biomol. Struct. , vol.34 , pp. 351-378
    • Kusumi, A.1    Nakada, C.2    Ritchie, K.3    Murase, K.4    Suzuki, K.5    Murakoshi, H.6    Kasai, R.S.7    Kondo, J.8    Fujiwara, T.9
  • 12
    • 0242385346 scopus 로고    scopus 로고
    • Separation of liquid phases in giant vesicles of ternary mixtures of phospholipids and cholesterol
    • Veatch S.L., and Keller S.L. Separation of liquid phases in giant vesicles of ternary mixtures of phospholipids and cholesterol. Biophys. J. 85 (2003) 3074-3083
    • (2003) Biophys. J. , vol.85 , pp. 3074-3083
    • Veatch, S.L.1    Keller, S.L.2
  • 13
    • 18144386926 scopus 로고    scopus 로고
    • Miscibility phase diagrams of giant vesicles containing sphingomyelin
    • Veatch S.L., and Keller S.L. Miscibility phase diagrams of giant vesicles containing sphingomyelin. Phys. Rev. Lett. 94 (2005) 148101-148104
    • (2005) Phys. Rev. Lett. , vol.94 , pp. 148101-148104
    • Veatch, S.L.1    Keller, S.L.2
  • 14
    • 22244490001 scopus 로고    scopus 로고
    • Building up of the liquid-ordered phase formed by sphingomyelin and cholesterol
    • Chachaty C., Rainteau D., Tessier C., Quinn P.J., and Wolf C. Building up of the liquid-ordered phase formed by sphingomyelin and cholesterol. Biophys. J. 88 (2005) 4032-4044
    • (2005) Biophys. J. , vol.88 , pp. 4032-4044
    • Chachaty, C.1    Rainteau, D.2    Tessier, C.3    Quinn, P.J.4    Wolf, C.5
  • 16
    • 33747798009 scopus 로고    scopus 로고
    • STEDy progress
    • Evanko D. STEDy progress. Nat. Methods 3 (2006) 661
    • (2006) Nat. Methods , vol.3 , pp. 661
    • Evanko, D.1
  • 17
    • 34547181885 scopus 로고    scopus 로고
    • Raft domain reorganization driven by short- and long chain ceramide: a combined AFM and FCS study
    • Chiantia S., Kahya N., and Schwille P. Raft domain reorganization driven by short- and long chain ceramide: a combined AFM and FCS study. Langmuir 23 (2007) 7659-7665
    • (2007) Langmuir , vol.23 , pp. 7659-7665
    • Chiantia, S.1    Kahya, N.2    Schwille, P.3
  • 18
    • 17044371853 scopus 로고    scopus 로고
    • Phase behaviour of dipalmitoylphospatidylcholine (DPPC)-cholesterol membranes
    • Karmakar S., Raghunathan V.A., and Mayor S. Phase behaviour of dipalmitoylphospatidylcholine (DPPC)-cholesterol membranes. J. Phys. Condens. Matter 17 (2005) S1177-S1182
    • (2005) J. Phys. Condens. Matter , vol.17
    • Karmakar, S.1    Raghunathan, V.A.2    Mayor, S.3
  • 20
    • 36348937414 scopus 로고    scopus 로고
    • Effect of line tension on the lateral organization of lipid membranes
    • Garcia-Saez A.J., Chiantia S., and Schwille P. Effect of line tension on the lateral organization of lipid membranes. J. Biol. Chem. 282 (2007) 33537-33544
    • (2007) J. Biol. Chem. , vol.282 , pp. 33537-33544
    • Garcia-Saez, A.J.1    Chiantia, S.2    Schwille, P.3
  • 21
    • 41649112141 scopus 로고    scopus 로고
    • Domain nucleation rates and interfacial line tensions in supported bilayers of ternary mixtures containing galactosylceramide
    • Blanchette C.D., Lin W.C., Orme C.A., Ratto T.V., and Longo M.L. Domain nucleation rates and interfacial line tensions in supported bilayers of ternary mixtures containing galactosylceramide. Biophys. J. 94 (2008) 2691-2697
    • (2008) Biophys. J. , vol.94 , pp. 2691-2697
    • Blanchette, C.D.1    Lin, W.C.2    Orme, C.A.3    Ratto, T.V.4    Longo, M.L.5
  • 22
    • 0001528446 scopus 로고    scopus 로고
    • Detection and characterization of membrane microheterogeneity by resonance energy transfer
    • Loura L.M.S., de Almeida R.F.M., and Prieto M. Detection and characterization of membrane microheterogeneity by resonance energy transfer. J. Fluoresc. 11 (2001) 197-209
    • (2001) J. Fluoresc. , vol.11 , pp. 197-209
    • Loura, L.M.S.1    de Almeida, R.F.M.2    Prieto, M.3
  • 23
    • 34547711580 scopus 로고    scopus 로고
    • Methodologies and formalisms of resonance energy transfer in biophysics. Application to membrane model systems
    • Loura L.M.S., de Almeida R.F.M., and Prieto M. Methodologies and formalisms of resonance energy transfer in biophysics. Application to membrane model systems. Int. J. Photoenergy 5 (2003) 223-231
    • (2003) Int. J. Photoenergy , vol.5 , pp. 223-231
    • Loura, L.M.S.1    de Almeida, R.F.M.2    Prieto, M.3
  • 24
    • 84935354375 scopus 로고
    • Experimentelle und theoretische Untersuchung des Zwischenmolekularen übergangs von Elektrinenanregungsenergie
    • Förster T.h. Experimentelle und theoretische Untersuchung des Zwischenmolekularen übergangs von Elektrinenanregungsenergie. Z. Naturforsch. 4a (1949) 321-327
    • (1949) Z. Naturforsch. , vol.4 a , pp. 321-327
    • Förster, T.h.1
  • 26
    • 0017795758 scopus 로고
    • Fluorescence energy transfer as a spectroscopic ruler
    • Stryer L. Fluorescence energy transfer as a spectroscopic ruler. Ann. Rev. Biochem. 47 (1978) 829-846
    • (1978) Ann. Rev. Biochem. , vol.47 , pp. 829-846
    • Stryer, L.1
  • 27
    • 0001102751 scopus 로고
    • Fluorescence quenching and energy transfer in monomolecular films containing chlorophyll
    • Tweet A.G., Bellamy W.D., and Gaines Jr. G.L. Fluorescence quenching and energy transfer in monomolecular films containing chlorophyll. J. Chem. Phys. 41 (1964) 2068-2077
    • (1964) J. Chem. Phys. , vol.41 , pp. 2068-2077
    • Tweet, A.G.1    Bellamy, W.D.2    Gaines Jr., G.L.3
  • 28
    • 0018650688 scopus 로고
    • An analytical solution to the Förster energy transfer problem in two dimensions
    • Wolber P.K., and Hudson B.S. An analytical solution to the Förster energy transfer problem in two dimensions. Biophys. J. 28 (1979) 197-210
    • (1979) Biophys. J. , vol.28 , pp. 197-210
    • Wolber, P.K.1    Hudson, B.S.2
  • 29
    • 0022427470 scopus 로고
    • Transverse location of the fluorescent probe 1,6-diphenyl-1,3,5-hexatriene in model lipid bilayer membrane systems by resonance energy transfer
    • Davenport L., Dale R.E., Bisby R.H., and Cundall R.B. Transverse location of the fluorescent probe 1,6-diphenyl-1,3,5-hexatriene in model lipid bilayer membrane systems by resonance energy transfer. Biochemistry 24 (1985) 4097-4108
    • (1985) Biochemistry , vol.24 , pp. 4097-4108
    • Davenport, L.1    Dale, R.E.2    Bisby, R.H.3    Cundall, R.B.4
  • 30
    • 58149182505 scopus 로고    scopus 로고
    • From lipid phases to membrane protein organization: fluorescence methodologies on the study of lipid-protein interaction
    • Mateo C.R., Gómez J., Villalaín J., and Gónzalez-Ros J.M. (Eds), Springer, New York
    • Mateo C.R., de Almeida R.F.M., Loura L.M.S., and Prieto M. From lipid phases to membrane protein organization: fluorescence methodologies on the study of lipid-protein interaction. In: Mateo C.R., Gómez J., Villalaín J., and Gónzalez-Ros J.M. (Eds). Protein-Lipid Interactions (2006), Springer, New York 1-33
    • (2006) Protein-Lipid Interactions , pp. 1-33
    • Mateo, C.R.1    de Almeida, R.F.M.2    Loura, L.M.S.3    Prieto, M.4
  • 31
    • 0034738620 scopus 로고    scopus 로고
    • Partition of membrane probes in a gel/fluid two-component lipid system: a fluorescence resonance energy transfer study
    • Loura L.M.S., Fedorov A., and Prieto M. Partition of membrane probes in a gel/fluid two-component lipid system: a fluorescence resonance energy transfer study. Biochim. Biophys. Acta 1467 (2000) 101-112
    • (2000) Biochim. Biophys. Acta , vol.1467 , pp. 101-112
    • Loura, L.M.S.1    Fedorov, A.2    Prieto, M.3
  • 32
    • 10144261915 scopus 로고    scopus 로고
    • Global analysis of the fluorescence decays of N,N'-dioctadecyl rhodamine B in Langmuir-Blodgett films of diacylphosphatidic acids
    • Ballet P., Van der Auweraer M., De Schryver F.C., Lemmetyinen H., and Vuorimaa E. Global analysis of the fluorescence decays of N,N'-dioctadecyl rhodamine B in Langmuir-Blodgett films of diacylphosphatidic acids. J. Phys. Chem. 100 (1996) 13701-13715
    • (1996) J. Phys. Chem. , vol.100 , pp. 13701-13715
    • Ballet, P.1    Van der Auweraer, M.2    De Schryver, F.C.3    Lemmetyinen, H.4    Vuorimaa, E.5
  • 33
    • 0035129496 scopus 로고    scopus 로고
    • Fluid-fluid membrane micro-heterogeneity: a fluorescence resonance energy transfer study
    • Loura L.M.S., Fedorov A., and Prieto M. Fluid-fluid membrane micro-heterogeneity: a fluorescence resonance energy transfer study. Biophys. J. 80 (2001) 776-788
    • (2001) Biophys. J. , vol.80 , pp. 776-788
    • Loura, L.M.S.1    Fedorov, A.2    Prieto, M.3
  • 34
    • 34248353393 scopus 로고    scopus 로고
    • Determination of membrane domain size by fluorescence resonance energy transfer: effects of domain polydispersity and packing
    • Towles K.B., and Dan N. Determination of membrane domain size by fluorescence resonance energy transfer: effects of domain polydispersity and packing. Langmuir 23 (2007) 4737-4739
    • (2007) Langmuir , vol.23 , pp. 4737-4739
    • Towles, K.B.1    Dan, N.2
  • 35
    • 34547697494 scopus 로고    scopus 로고
    • Steady-state probe-partitioning FRET: A simple and robust tool for the study of membrane phase behavior
    • Buboltz J.T. Steady-state probe-partitioning FRET: A simple and robust tool for the study of membrane phase behavior. Phys. Rev. E 76 (2007) 021903
    • (2007) Phys. Rev. E , vol.76 , pp. 021903
    • Buboltz, J.T.1
  • 36
    • 36849016271 scopus 로고    scopus 로고
    • Stern-Volmer modeling of steady-state Förster energy transfer between dilute, freely diffusing membrane-bound fluorophores
    • Buboltz J.T., Bwalya C., Reyes S., and Kamburov D. Stern-Volmer modeling of steady-state Förster energy transfer between dilute, freely diffusing membrane-bound fluorophores. J. Chem. Phys. 127 (2007) 215101
    • (2007) J. Chem. Phys. , vol.127 , pp. 215101
    • Buboltz, J.T.1    Bwalya, C.2    Reyes, S.3    Kamburov, D.4
  • 37
    • 34447313944 scopus 로고    scopus 로고
    • Effect of membrane microheterogeneity and domain size on fluorescence resonance energy transfer
    • Towles K.B., Brown A.C., Wrenn S.P., and Dan N. Effect of membrane microheterogeneity and domain size on fluorescence resonance energy transfer. Biophys. J. 93 (2007) 655-667
    • (2007) Biophys. J. , vol.93 , pp. 655-667
    • Towles, K.B.1    Brown, A.C.2    Wrenn, S.P.3    Dan, N.4
  • 38
    • 43949165339 scopus 로고
    • Recovery of acceptor concentration distribution in direct energy transfer experiments
    • Liu Y.S., Li L., Ni S., and Winnik M. Recovery of acceptor concentration distribution in direct energy transfer experiments. Chem. Phys. 177 (1993) 579-589
    • (1993) Chem. Phys. , vol.177 , pp. 579-589
    • Liu, Y.S.1    Li, L.2    Ni, S.3    Winnik, M.4
  • 39
    • 0034226955 scopus 로고    scopus 로고
    • Membrane probe distribution heterogeneity: a resonance energy transfer study
    • Loura L.M.S., Fedorov A., and Prieto M. Membrane probe distribution heterogeneity: a resonance energy transfer study. J. Phys. Chem. B. 104 (2000) 6920-6931
    • (2000) J. Phys. Chem. B. , vol.104 , pp. 6920-6931
    • Loura, L.M.S.1    Fedorov, A.2    Prieto, M.3
  • 40
    • 35948954751 scopus 로고    scopus 로고
    • Measuring raft size as a function of membrane composition in PC-based systems: part I- binary systems
    • Brown A.C., Towles K.B., and Wrenn S.P. Measuring raft size as a function of membrane composition in PC-based systems: part I- binary systems. Langmuir 23 (2007) 11180-11187
    • (2007) Langmuir , vol.23 , pp. 11180-11187
    • Brown, A.C.1    Towles, K.B.2    Wrenn, S.P.3
  • 41
    • 0034081731 scopus 로고    scopus 로고
    • Two photon fluorescence microscopy of coexisting lipid domains in giant unilamellar vesicles of binary phospholipid mixtures
    • Bagatolli L., and Gratton E. Two photon fluorescence microscopy of coexisting lipid domains in giant unilamellar vesicles of binary phospholipid mixtures. Biophys. J. 78 (2000) 290-305
    • (2000) Biophys. J. , vol.78 , pp. 290-305
    • Bagatolli, L.1    Gratton, E.2
  • 42
    • 0018278640 scopus 로고
    • Surface density determination in membranes by fluorescence energy transfer
    • Fung B.K., and Stryer L. Surface density determination in membranes by fluorescence energy transfer. Biochemistry 17 (1978) 5241-5248
    • (1978) Biochemistry , vol.17 , pp. 5241-5248
    • Fung, B.K.1    Stryer, L.2
  • 43
    • 0019643914 scopus 로고
    • Quantitation of the Förster energy transfer for two-dimensional systems. I. Lateral phase separation in unilamellar vesicles formed by binary phospholipid mixtures
    • Gutiérrez-Merino C. Quantitation of the Förster energy transfer for two-dimensional systems. I. Lateral phase separation in unilamellar vesicles formed by binary phospholipid mixtures. Biophys. Chem. 14 (1981) 247-257
    • (1981) Biophys. Chem. , vol.14 , pp. 247-257
    • Gutiérrez-Merino, C.1
  • 44
    • 0019639306 scopus 로고
    • Quantitation of the Förster energy transfer for two-dimensional systems. II. Protein distribution and aggregation state in biological membranes
    • Gutiérrez-Merino C. Quantitation of the Förster energy transfer for two-dimensional systems. II. Protein distribution and aggregation state in biological membranes. Biophys. Chem. 14 (1981) 259-266
    • (1981) Biophys. Chem. , vol.14 , pp. 259-266
    • Gutiérrez-Merino, C.1
  • 45
    • 0042845804 scopus 로고    scopus 로고
    • Fluorescence energy transfer reveals microdomain formation at physiological temperatures in lipid mixtures modeling the outer leaflet of the plasma membrane
    • Silvius J. Fluorescence energy transfer reveals microdomain formation at physiological temperatures in lipid mixtures modeling the outer leaflet of the plasma membrane. Biophys. J. 85 (2003) 1034-1045
    • (2003) Biophys. J. , vol.85 , pp. 1034-1045
    • Silvius, J.1
  • 46
    • 0020212826 scopus 로고
    • Fluorescence energy transfer in two dimensions. A numeric solution for random and non-random distributions
    • Snyder B., and Freire E. Fluorescence energy transfer in two dimensions. A numeric solution for random and non-random distributions. Biophys. J. 40 (1982) 137-148
    • (1982) Biophys. J. , vol.40 , pp. 137-148
    • Snyder, B.1    Freire, E.2
  • 47
    • 0034228089 scopus 로고    scopus 로고
    • Resonance energy transfer in heterogeneous planar and bilayer systems: theory and simulation
    • Loura L.M.S., and Prieto M. Resonance energy transfer in heterogeneous planar and bilayer systems: theory and simulation. J. Phys. Chem. B 104 (2000) 6911-6919
    • (2000) J. Phys. Chem. B , vol.104 , pp. 6911-6919
    • Loura, L.M.S.1    Prieto, M.2
  • 49
    • 3042771646 scopus 로고    scopus 로고
    • Quantification of protein-lipid selectivity using FRET. Application to the M13 major coat protein
    • Fernandes F.M., Loura L.M.S., Koehorst R., Spruijt R.B., Hemminga M.A., and Prieto M. Quantification of protein-lipid selectivity using FRET. Application to the M13 major coat protein. Biophys. J. 87 (2004) 344-352
    • (2004) Biophys. J. , vol.87 , pp. 344-352
    • Fernandes, F.M.1    Loura, L.M.S.2    Koehorst, R.3    Spruijt, R.B.4    Hemminga, M.A.5    Prieto, M.6
  • 50
    • 33646715369 scopus 로고    scopus 로고
    • Non-uniform membrane probe distribution in resonance energy transfer: application to protein-lipid selectivity
    • Capeta R.C., Poveda J.A., and Loura L.M.S. Non-uniform membrane probe distribution in resonance energy transfer: application to protein-lipid selectivity. J. Fluoresc. 16 (2006) 161-172
    • (2006) J. Fluoresc. , vol.16 , pp. 161-172
    • Capeta, R.C.1    Poveda, J.A.2    Loura, L.M.S.3
  • 51
    • 0029791045 scopus 로고    scopus 로고
    • Resonance energy transfer in a model system of membranes: application to gel and liquid crystalline phases
    • Loura L.M.S., Fedorov A., and Prieto M. Resonance energy transfer in a model system of membranes: application to gel and liquid crystalline phases. Biophys. J. 71 (1996) 1823-1836
    • (1996) Biophys. J. , vol.71 , pp. 1823-1836
    • Loura, L.M.S.1    Fedorov, A.2    Prieto, M.3
  • 52
    • 24144491634 scopus 로고    scopus 로고
    • pH-dependent domain formation in phosphatidylinositol polyphosphate/phosphatidylcholine mixed vesicles
    • Redfern D.A., and Gericke A. pH-dependent domain formation in phosphatidylinositol polyphosphate/phosphatidylcholine mixed vesicles. J. Lipid Res. 46 (2005) 504-515
    • (2005) J. Lipid Res. , vol.46 , pp. 504-515
    • Redfern, D.A.1    Gericke, A.2
  • 53
    • 33746058677 scopus 로고    scopus 로고
    • Absence of clustering of phosphatidylinositol-(4,5)-bisphosphate in fluid phosphatidylcholine
    • Fernandes F., Loura L.M.S., Fedorov A., and Prieto M. Absence of clustering of phosphatidylinositol-(4,5)-bisphosphate in fluid phosphatidylcholine. J. Lipid Res. 47 (2006) 1521-1525
    • (2006) J. Lipid Res. , vol.47 , pp. 1521-1525
    • Fernandes, F.1    Loura, L.M.S.2    Fedorov, A.3    Prieto, M.4
  • 55
    • 1942519443 scopus 로고    scopus 로고
    • Cholesterol modulates the organization of the γM4 transmembrane domain of the muscle nicotinic acetylcholine receptor
    • de Almeida R.F.M., Loura L.M.S., Prieto M., Watts A., Fedorov A., and Barrantes F.J. Cholesterol modulates the organization of the γM4 transmembrane domain of the muscle nicotinic acetylcholine receptor. Biophys. J. 86 (2004) 2261-2272
    • (2004) Biophys. J. , vol.86 , pp. 2261-2272
    • de Almeida, R.F.M.1    Loura, L.M.S.2    Prieto, M.3    Watts, A.4    Fedorov, A.5    Barrantes, F.J.6
  • 57
    • 0001541657 scopus 로고
    • Investigation of phase transitions of lipids and lipid mixtures by high sensitivity differential scanning calorimetry
    • Mabrey S., and Sturtevant J.M. Investigation of phase transitions of lipids and lipid mixtures by high sensitivity differential scanning calorimetry. Proc. Natl. Acad. Sci. 73 (1976) 3862-3866
    • (1976) Proc. Natl. Acad. Sci. , vol.73 , pp. 3862-3866
    • Mabrey, S.1    Sturtevant, J.M.2
  • 58
    • 0028067399 scopus 로고
    • Dynamical order and disorder in lipid bilayers
    • Mouritsen O.G., and Jørgensen K. Dynamical order and disorder in lipid bilayers. Chem. Phys. Lipids 73 (1994) 3-25
    • (1994) Chem. Phys. Lipids , vol.73 , pp. 3-25
    • Mouritsen, O.G.1    Jørgensen, K.2
  • 59
    • 3843139379 scopus 로고    scopus 로고
    • Rituximab antiproliferative effect in B-lymphoma cells is associated with acid-sphingomyelinase activation in raft microdomains
    • Bezombes C., Grazide S., Garret C., Fabre C., Quillet-Mary A., Müller S., Jaffrézou J.-P., and Laurent G. Rituximab antiproliferative effect in B-lymphoma cells is associated with acid-sphingomyelinase activation in raft microdomains. Blood 104 (2004) 1166-1173
    • (2004) Blood , vol.104 , pp. 1166-1173
    • Bezombes, C.1    Grazide, S.2    Garret, C.3    Fabre, C.4    Quillet-Mary, A.5    Müller, S.6    Jaffrézou, J.-P.7    Laurent, G.8
  • 60
    • 0032211769 scopus 로고    scopus 로고
    • Signal transduction of stress via ceramide
    • Mathias S., Peña L.A., and Kolesnick R.N. 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
  • 61
    • 0037401894 scopus 로고    scopus 로고
    • Intracellular signal transduction pathways activated by ceramide and its metabolites
    • Ruvolo P.P. Intracellular signal transduction pathways activated by ceramide and its metabolites. Pharmacol. Res. 47 (2003) 383-392
    • (2003) Pharmacol. Res. , vol.47 , pp. 383-392
    • Ruvolo, P.P.1
  • 62
    • 0033884050 scopus 로고    scopus 로고
    • Compartmentalization of ceramide signaling: physical foundation and biological effects
    • Kolesnick R.N., Gõni F.M., and Alonso A. Compartmentalization of ceramide signaling: physical foundation and biological effects. J. Cell. Physiol. 184 (2000) 285-300
    • (2000) J. Cell. Physiol. , vol.184 , pp. 285-300
    • Kolesnick, R.N.1    Gõni, F.M.2    Alonso, A.3
  • 63
    • 0037201936 scopus 로고    scopus 로고
    • Role of sphingomyelinase and ceramide in modulating rafts: do biophysical properties determine biological outcome?
    • Cremesti A.E., Gõni F.M., and Kolesnick R.N. Role of sphingomyelinase and ceramide in modulating rafts: do biophysical properties determine biological outcome?. FEBS Lett. 531 (2002) 47-53
    • (2002) FEBS Lett. , vol.531 , pp. 47-53
    • Cremesti, A.E.1    Gõni, F.M.2    Kolesnick, R.N.3
  • 64
    • 33646880484 scopus 로고    scopus 로고
    • Ceramide-platform formation and-induced biophysical changes in a fluid phospholipid membrane
    • Silva L., de Almeida R.F.M., Matos A.P., Fedorov A., and Prieto M. Ceramide-platform formation and-induced biophysical changes in a fluid phospholipid membrane. Mol. Membr. Biol. 23 (2006) 137-150
    • (2006) Mol. Membr. Biol. , vol.23 , pp. 137-150
    • Silva, L.1    de Almeida, R.F.M.2    Matos, A.P.3    Fedorov, A.4    Prieto, M.5
  • 65
    • 0027365642 scopus 로고
    • Lipid clustering in bilayers detected by the fluorescence kinetics and anisotropy of trans-parinaric acid
    • Mateo C.R., Brochon J.-C., Lillo M.P., and Acuña A.U. Lipid clustering in bilayers detected by the fluorescence kinetics and anisotropy of trans-parinaric acid. Biophys. J. 65 (1993) 2237-2247
    • (1993) Biophys. J. , vol.65 , pp. 2237-2247
    • Mateo, C.R.1    Brochon, J.-C.2    Lillo, M.P.3    Acuña, A.U.4
  • 66
    • 0002255381 scopus 로고
    • Membrane "fluidity" from fluorescence anisotropy measurements
    • Loew L. (Ed), CRC, Boca Raton, FL
    • Lentz B. Membrane "fluidity" from fluorescence anisotropy measurements. In: Loew L. (Ed). Spectroscopic Membrane Probes: Volume I, CRC (1988), CRC, Boca Raton, FL 13-41
    • (1988) Spectroscopic Membrane Probes: Volume I, CRC , pp. 13-41
    • Lentz, B.1
  • 67
    • 0030917558 scopus 로고    scopus 로고
    • Fluorescence probes for studying membrane heterogeneity
    • Davenport L. Fluorescence probes for studying membrane heterogeneity. Meth. Enzymol. 278 (1997) 487-512
    • (1997) Meth. Enzymol. , vol.278 , pp. 487-512
    • Davenport, L.1
  • 68
    • 0000656268 scopus 로고    scopus 로고
    • Fluorescence spectroscopic studies on phase heterogeneity in lipid bilayer membranes
    • Vaz W.L.C., and Melo E. Fluorescence spectroscopic studies on phase heterogeneity in lipid bilayer membranes. J. Fluoresc. 11 (2002) 255-271
    • (2002) J. Fluoresc. , vol.11 , pp. 255-271
    • Vaz, W.L.C.1    Melo, E.2
  • 69
    • 0025128695 scopus 로고
    • Phase equilibria of cholesterol/dipalmitoylphosphatidylcholine mixtures: 2 H nuclear magnetic resonance and differential scanning calorimetry
    • Vist M.R., and Davis J.H. Phase equilibria of cholesterol/dipalmitoylphosphatidylcholine mixtures: 2 H nuclear magnetic resonance and differential scanning calorimetry. Biochemistry 29 (1990) 451-464
    • (1990) Biochemistry , vol.29 , pp. 451-464
    • Vist, M.R.1    Davis, J.H.2
  • 70
    • 0026058545 scopus 로고
    • Cholesterol-induced fluid-phase immiscibility in membranes
    • Sankaram M.B., and Thompson T.E. Cholesterol-induced fluid-phase immiscibility in membranes. Proc. Natl. Acad. Sci. U. S. A. 88 (1991) 8686-8690
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 8686-8690
    • Sankaram, M.B.1    Thompson, T.E.2
  • 71
    • 33847090828 scopus 로고    scopus 로고
    • Direct measurement of phase coexistence in DPPC/cholesterol vesicles using Raman spectroscopy
    • de Lange M.J.L., Bonn M., and Müller M. Direct measurement of phase coexistence in DPPC/cholesterol vesicles using Raman spectroscopy. Chem. Phys. Lipids 146 (2007) 76-84
    • (2007) Chem. Phys. Lipids , vol.146 , pp. 76-84
    • de Lange, M.J.L.1    Bonn, M.2    Müller, M.3
  • 72
    • 35148830015 scopus 로고    scopus 로고
    • Dynamic molecular structure and phase diagram of DPPC-cholesterol binary mixtures: a 2D-ELDOR study
    • Chiang Y.-W., Costa-Filho A.J., and Freed J.H. Dynamic molecular structure and phase diagram of DPPC-cholesterol binary mixtures: a 2D-ELDOR study. J. Phys. Chem. B 111 (2007) 11260-11270
    • (2007) J. Phys. Chem. B , vol.111 , pp. 11260-11270
    • Chiang, Y.-W.1    Costa-Filho, A.J.2    Freed, J.H.3
  • 73
    • 0026767199 scopus 로고
    • Lateral diffusion in the liquid-phases of dimyristoylphosphatidylcholine/cholesterol lipid bilayers- a free-volume analysis
    • Almeida P.F.F., Vaz W.L.C., and Thompson T.E. Lateral diffusion in the liquid-phases of dimyristoylphosphatidylcholine/cholesterol lipid bilayers- a free-volume analysis. Biochemistry 31 (1992) 6739-6747
    • (1992) Biochemistry , vol.31 , pp. 6739-6747
    • Almeida, P.F.F.1    Vaz, W.L.C.2    Thompson, T.E.3
  • 74
    • 0028936858 scopus 로고
    • Liquid-crystalline phases of cholesterol lipid bilayers as revealed by the fluorescence of trans-parinaric acid
    • Mateo C.R., Acuna A.U., and Brochon J.-C. Liquid-crystalline phases of cholesterol lipid bilayers as revealed by the fluorescence of trans-parinaric acid. Biophys. J. 68 (1995) 978-987
    • (1995) Biophys. J. , vol.68 , pp. 978-987
    • Mateo, C.R.1    Acuna, A.U.2    Brochon, J.-C.3
  • 75
    • 0026700004 scopus 로고
    • Phosphatidylcholine-cholesterol phase-diagrams
    • Thewalt J.L., and Bloom M. Phosphatidylcholine-cholesterol phase-diagrams. Biophys. J. 63 (1992) 1176-1181
    • (1992) Biophys. J. , vol.63 , pp. 1176-1181
    • Thewalt, J.L.1    Bloom, M.2
  • 76
    • 0141642121 scopus 로고    scopus 로고
    • Sphingomyelin/Phosphatidylcholine/Cholesterol phase diagram: boundaries and composition of lipid rafts
    • de Almeida R.F.M., Fedorov A., and Prieto M. Sphingomyelin/Phosphatidylcholine/Cholesterol phase diagram: boundaries and composition of lipid rafts. Biophys. J. 85 (2003) 2406-2416
    • (2003) Biophys. J. , vol.85 , pp. 2406-2416
    • de Almeida, R.F.M.1    Fedorov, A.2    Prieto, M.3
  • 77
    • 33646201285 scopus 로고    scopus 로고
    • Competitive binding of cholesterol and ergosterol to the polyene antibiotic nystatin. A fluorescence study
    • Silva L., Coutinho A., Fedorov A., and Prieto M. Competitive binding of cholesterol and ergosterol to the polyene antibiotic nystatin. A fluorescence study. Biophys. J. 90 (2006) 3625-3631
    • (2006) Biophys. J. , vol.90 , pp. 3625-3631
    • Silva, L.1    Coutinho, A.2    Fedorov, A.3    Prieto, M.4
  • 79
    • 0025602953 scopus 로고
    • Interaction of cholesterol with various glycerophospholipids and sphingomyelin
    • Sankaram M.B., and Thompson T.E. Interaction of cholesterol with various glycerophospholipids and sphingomyelin. Biochemistry 29 (1990) 10670-10675
    • (1990) Biochemistry , vol.29 , pp. 10670-10675
    • Sankaram, M.B.1    Thompson, T.E.2
  • 80
    • 15444373407 scopus 로고    scopus 로고
    • Domain formation in sphingomyelin/cholesterol mixed membranes studied by spin-label electron spin resonance spectroscopy
    • Collado M.I., Goñi F.M., Alonso A., and Marsh D. Domain formation in sphingomyelin/cholesterol mixed membranes studied by spin-label electron spin resonance spectroscopy. Biochemistry 44 (2005) 4911-4918
    • (2005) Biochemistry , vol.44 , pp. 4911-4918
    • Collado, M.I.1    Goñi, F.M.2    Alonso, A.3    Marsh, D.4
  • 81
    • 40949088604 scopus 로고    scopus 로고
    • Detection of lipid phase coexistence and lipid interactions in sphingomyelin/cholesterol membranes by ATR-FTIR spectroscopy
    • Arsov Z., and Quaroni L. Detection of lipid phase coexistence and lipid interactions in sphingomyelin/cholesterol membranes by ATR-FTIR spectroscopy. Biochim. Biophys. Acta 1778 (2008) 880-889
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 880-889
    • Arsov, Z.1    Quaroni, L.2
  • 82
    • 34447326993 scopus 로고    scopus 로고
    • Complexity of lipid domains and rafts in giant unilamellar vesicles revealed by combining imaging and microscopic and macroscopic time-resolved fluorescence
    • de Almeida R.F.M., Borst J., Fedorov A., Prieto M., and Visser A.J.W.G. Complexity of lipid domains and rafts in giant unilamellar vesicles revealed by combining imaging and microscopic and macroscopic time-resolved fluorescence. Biophys. J. 93 (2007) 539-553
    • (2007) Biophys. J. , vol.93 , pp. 539-553
    • de Almeida, R.F.M.1    Borst, J.2    Fedorov, A.3    Prieto, M.4    Visser, A.J.W.G.5
  • 83
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma R., and Mayor S. 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
  • 84
    • 0037455589 scopus 로고    scopus 로고
    • Direct visualization of Ras proteins in spatially distinct cell surface microdomains
    • Prior I.A., Muncke C., Parton R.G., and Hancock J.F. Direct visualization of Ras proteins in spatially distinct cell surface microdomains. J. Cell Biol. 160 (2003) 165-170
    • (2003) J. Cell Biol. , vol.160 , pp. 165-170
    • Prior, I.A.1    Muncke, C.2    Parton, R.G.3    Hancock, J.F.4
  • 85
    • 33645241165 scopus 로고    scopus 로고
    • Identifying optimal lipid raft characteristics required to promote nanoscale protein-protein interactions on the plasma membrane
    • Nicolau Jr. D.V., Burrage K., Parton R.G., and Hancock J.F. Identifying optimal lipid raft characteristics required to promote nanoscale protein-protein interactions on the plasma membrane. Mol. Cell. Biol. 26 (2006) 313-323
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 313-323
    • Nicolau Jr., D.V.1    Burrage, K.2    Parton, R.G.3    Hancock, J.F.4
  • 86
    • 34247863869 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer between lipid probes detects nanoscopic heterogeneity in the plasma membrane of live cells
    • Sengupta P., Holowka D., and Baird B. Fluorescence resonance energy transfer between lipid probes detects nanoscopic heterogeneity in the plasma membrane of live cells. Biophys. J. 92 (2007) 3564-3574
    • (2007) Biophys. J. , vol.92 , pp. 3564-3574
    • Sengupta, P.1    Holowka, D.2    Baird, B.3
  • 88
    • 13544250813 scopus 로고    scopus 로고
    • Lipid rafts have different sizes depending on membrane composition: a time-resolved fluorescence resonance energy transfer study
    • de Almeida R.F.M., Loura L.M.S., Fedorov A., and Prieto M. Lipid rafts have different sizes depending on membrane composition: a time-resolved fluorescence resonance energy transfer study. J. Mol. Biol. 346 (2005) 1109-1120
    • (2005) J. Mol. Biol. , vol.346 , pp. 1109-1120
    • de Almeida, R.F.M.1    Loura, L.M.S.2    Fedorov, A.3    Prieto, M.4
  • 89
    • 33846411845 scopus 로고    scopus 로고
    • Ceramide-domain formation and collapse in lipid rafts: membrane reorganization by an apoptotic lipid
    • Silva L.C., de Almeida R.F.M., Castro B.M., Fedorov A., and Prieto M. Ceramide-domain formation and collapse in lipid rafts: membrane reorganization by an apoptotic lipid. Biophys. J. 92 (2007) 502-516
    • (2007) Biophys. J. , vol.92 , pp. 502-516
    • Silva, L.C.1    de Almeida, R.F.M.2    Castro, B.M.3    Fedorov, A.4    Prieto, M.5
  • 90
    • 34047195768 scopus 로고    scopus 로고
    • Investigation of domain formation in sphingomyelin/cholesterol/POPC mixtures by fluorescence resonance energy transfer and Monte Carlo simulations
    • Frazier M.L., Wright J.R., Pokorny A., and Almeida P.F.F. Investigation of domain formation in sphingomyelin/cholesterol/POPC mixtures by fluorescence resonance energy transfer and Monte Carlo simulations. Biophys. J. 92 (2007) 2422-2433
    • (2007) Biophys. J. , vol.92 , pp. 2422-2433
    • Frazier, M.L.1    Wright, J.R.2    Pokorny, A.3    Almeida, P.F.F.4
  • 91
    • 33748465151 scopus 로고    scopus 로고
    • Temperature and composition dependence of the interaction of d-lysin with ternary mixtures of sphingomyelin/cholesterol/ POPC
    • Pokorny A., Yandek L.E., Elegbede A.I., Hinderliter A., and Almeida P.F.F. Temperature and composition dependence of the interaction of d-lysin with ternary mixtures of sphingomyelin/cholesterol/ POPC. Biophys. J. 91 (2006) 2184-2197
    • (2006) Biophys. J. , vol.91 , pp. 2184-2197
    • Pokorny, A.1    Yandek, L.E.2    Elegbede, A.I.3    Hinderliter, A.4    Almeida, P.F.F.5
  • 92
    • 36649022647 scopus 로고    scopus 로고
    • High-resolution mapping of phase behavior in a ternary lipid mixture: do lipid-raft phase boundaries depend on the sample preparation procedure?
    • Buboltz J.T., Bwalya C., Williams K., and Schutzer M. High-resolution mapping of phase behavior in a ternary lipid mixture: do lipid-raft phase boundaries depend on the sample preparation procedure?. Langmuir 23 (2007) 11968-11971
    • (2007) Langmuir , vol.23 , pp. 11968-11971
    • Buboltz, J.T.1    Bwalya, C.2    Williams, K.3    Schutzer, M.4
  • 93
    • 2142651634 scopus 로고    scopus 로고
    • Liquid domains in vesicles investigated by NMR and fluorescence microscopy
    • Veatch S.L., Polozov I.V., Gawrisch K., and Keller S.L. Liquid domains in vesicles investigated by NMR and fluorescence microscopy. Biophys. J. 86 (2004) 2910-2922
    • (2004) Biophys. J. , vol.86 , pp. 2910-2922
    • Veatch, S.L.1    Polozov, I.V.2    Gawrisch, K.3    Keller, S.L.4
  • 94
    • 35948973545 scopus 로고    scopus 로고
    • Measuring raft size as a function of membrane composition in PC-based systems: part II- ternary systems
    • Brown A.C., Towles K.B., and Wrenn S.P. Measuring raft size as a function of membrane composition in PC-based systems: part II- ternary systems. Langmuir 23 (2007) 11188-11196
    • (2007) Langmuir , vol.23 , pp. 11188-11196
    • Brown, A.C.1    Towles, K.B.2    Wrenn, S.P.3
  • 95
    • 47349125098 scopus 로고    scopus 로고
    • Cholesterol packing around lipids with saturated and unsaturated chains: a simulation study
    • Pandit S.A., Chiu S.-W., Jakobsson E., Grama A., and Scott H.L. Cholesterol packing around lipids with saturated and unsaturated chains: a simulation study. Langmuir 24 (2008) 6858-6865
    • (2008) Langmuir , vol.24 , pp. 6858-6865
    • Pandit, S.A.1    Chiu, S.-W.2    Jakobsson, E.3    Grama, A.4    Scott, H.L.5
  • 96
    • 0141785142 scopus 로고    scopus 로고
    • Dependence of M13 major coat protein oligomerization and lateral segregation on bilayer composition
    • Fernandes F., Loura L.M.S., Prieto M., Koehorst R., Spruijt R., and Hemminga M.A. Dependence of M13 major coat protein oligomerization and lateral segregation on bilayer composition. Biophys. J. 85 (2003) 2430-2441
    • (2003) Biophys. J. , vol.85 , pp. 2430-2441
    • Fernandes, F.1    Loura, L.M.S.2    Prieto, M.3    Koehorst, R.4    Spruijt, R.5    Hemminga, M.A.6
  • 97
    • 55549135378 scopus 로고    scopus 로고
    • Membrane domain formation, interdigitation and morphological alterations induced by the very long chain asymmetric C24:1 ceramide
    • Pinto S.N., Silva L.C., de Almeida R.F.M., and Prieto M. Membrane domain formation, interdigitation and morphological alterations induced by the very long chain asymmetric C24:1 ceramide. Biophys. J. 95 (2008) 2867-2879
    • (2008) Biophys. J. , vol.95 , pp. 2867-2879
    • Pinto, S.N.1    Silva, L.C.2    de Almeida, R.F.M.3    Prieto, M.4
  • 98
    • 0036109677 scopus 로고    scopus 로고
    • The effect of ceramide on phosphatidylcholine membranes: a deuterium NMR study
    • Hsueh Y.W., Giles R., Kitson N., and Thewalt J. The effect of ceramide on phosphatidylcholine membranes: a deuterium NMR study. Biophys. J. 82 (2002) 3089-3095
    • (2002) Biophys. J. , vol.82 , pp. 3089-3095
    • Hsueh, Y.W.1    Giles, R.2    Kitson, N.3    Thewalt, J.4
  • 99
    • 0034105994 scopus 로고    scopus 로고
    • Dimyristoylphosphatidylcholine/C16:0-ceramide binary liposomes studied by differential scanning calorimetry and wide- and small-angle X-ray scattering
    • Holopainen J.M., Lemmich J., Richter F., Mouritsen O.G., Rapp G., and Kinnunen P.K.J. Dimyristoylphosphatidylcholine/C16:0-ceramide binary liposomes studied by differential scanning calorimetry and wide- and small-angle X-ray scattering. Biophys. J. 78 (2000) 2459-2469
    • (2000) Biophys. J. , vol.78 , pp. 2459-2469
    • Holopainen, J.M.1    Lemmich, J.2    Richter, F.3    Mouritsen, O.G.4    Rapp, G.5    Kinnunen, P.K.J.6
  • 100
    • 0035146779 scopus 로고    scopus 로고
    • Interfacial interactions of ceramide with dimyristoylphosphatidylcholine: impact of the N-acyl chain
    • Holopainen J.M., Brockman H.L., Brown R.E., and Kinnunen P.K.J. Interfacial interactions of ceramide with dimyristoylphosphatidylcholine: impact of the N-acyl chain. Biophys. J. 80 (2001) 765-775
    • (2001) Biophys. J. , vol.80 , pp. 765-775
    • Holopainen, J.M.1    Brockman, H.L.2    Brown, R.E.3    Kinnunen, P.K.J.4
  • 101
    • 33646181561 scopus 로고    scopus 로고
    • Effects of a short-chain ceramide on bilayer domain formation, thickness, and chain mobililty: DMPC and asymmetric ceramide mixtures
    • Carrer D.C., Schreier S., Patrito M., and Maggio B. Effects of a short-chain ceramide on bilayer domain formation, thickness, and chain mobililty: DMPC and asymmetric ceramide mixtures. Biophys. J. 90 (2006) 2394-2403
    • (2006) Biophys. J. , vol.90 , pp. 2394-2403
    • Carrer, D.C.1    Schreier, S.2    Patrito, M.3    Maggio, B.4
  • 102
    • 0032745772 scopus 로고    scopus 로고
    • Phase behavior and molecular interactions in mixtures of ceramide with dipalmitoylphosphatidylcholine
    • Carrer D.C., and Maggio B. Phase behavior and molecular interactions in mixtures of ceramide with dipalmitoylphosphatidylcholine. J. Lipid Res. 40 (1999) 1978-1989
    • (1999) J. Lipid Res. , vol.40 , pp. 1978-1989
    • Carrer, D.C.1    Maggio, B.2
  • 103
    • 33646179776 scopus 로고    scopus 로고
    • Detergent-resistant, ceramide-enriched domains in sphingomyelin/ceramide bilayers
    • Sot J., Bagatolli L.A., Goñi F.M., and Alonso A. Detergent-resistant, ceramide-enriched domains in sphingomyelin/ceramide bilayers. Biophys. J. 90 (2006) 903-914
    • (2006) Biophys. J. , vol.90 , pp. 903-914
    • Sot, J.1    Bagatolli, L.A.2    Goñi, F.M.3    Alonso, A.4
  • 104
    • 34548629303 scopus 로고    scopus 로고
    • Formation of Ceramide/Sphingomyelin gel domains in the presence of an unsaturated phospholipid: a quantitative multiprobe approach
    • Castro B.M., de Almeida R.F.M., Silva L.C., Fedorov A., and Prieto M. Formation of Ceramide/Sphingomyelin gel domains in the presence of an unsaturated phospholipid: a quantitative multiprobe approach. Biophys. J. 93 (2007) 1639-1650
    • (2007) Biophys. J. , vol.93 , pp. 1639-1650
    • Castro, B.M.1    de Almeida, R.F.M.2    Silva, L.C.3    Fedorov, A.4    Prieto, M.5
  • 106
    • 33846348624 scopus 로고    scopus 로고
    • Ceramide promotes restructuring of model raft membranes
    • Johnston I., and Johnston L.J. Ceramide promotes restructuring of model raft membranes. Langmuir 22 (2006) 11284-11289
    • (2006) Langmuir , vol.22 , pp. 11284-11289
    • Johnston, I.1    Johnston, L.J.2
  • 107
    • 38149085341 scopus 로고    scopus 로고
    • Sphingomyelinase generation of ceramide promotes clustering of nanoscale domains in supported bilayer membranes
    • Johnston I., and Johnston L.J. Sphingomyelinase generation of ceramide promotes clustering of nanoscale domains in supported bilayer membranes. Biochim. Biophys. Acta 1778 (2008) 185-197
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 185-197
    • Johnston, I.1    Johnston, L.J.2
  • 108
    • 33744804799 scopus 로고    scopus 로고
    • Effects of ceramide on liquid-ordered domains investigated by simultaneous AFM and FCS
    • Chiantia S., Kahya N., Ries J., and Schwille P. Effects of ceramide on liquid-ordered domains investigated by simultaneous AFM and FCS. Biophys. J. 90 (2006) 4500-4508
    • (2006) Biophys. J. , vol.90 , pp. 4500-4508
    • Chiantia, S.1    Kahya, N.2    Ries, J.3    Schwille, P.4
  • 110
    • 32344453443 scopus 로고    scopus 로고
    • Two-dimensional Förster resonance energy transfer (2-D FRET) and the membrane raft hypothesis
    • Acasandrei M.A., Dale R.E., VandeVen M., and Ameloot M. Two-dimensional Förster resonance energy transfer (2-D FRET) and the membrane raft hypothesis. Chem. Phys. Lett. 419 (2006) 469-473
    • (2006) Chem. Phys. Lett. , vol.419 , pp. 469-473
    • Acasandrei, M.A.1    Dale, R.E.2    VandeVen, M.3    Ameloot, M.4
  • 111
    • 0032514258 scopus 로고    scopus 로고
    • Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of < 100 Å using imaging fluorescence resonance energy transfer
    • Kenworthy A.K., and Edidin M. Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of < 100 Å using imaging fluorescence resonance energy transfer. J. Cell Biol. 142 (1998) 69-84
    • (1998) J. Cell Biol. , vol.142 , pp. 69-84
    • Kenworthy, A.K.1    Edidin, M.2
  • 112
    • 33144473025 scopus 로고    scopus 로고
    • FRET imaging reveals that functional neurokinin-1 receptors are monomeric and reside in membrane microdomains of live cells
    • Meyer B.H., Segura J.-M., Martinez K.L., Hovius R., George N., Johnsson K., and Vogel H. FRET imaging reveals that functional neurokinin-1 receptors are monomeric and reside in membrane microdomains of live cells. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 2138-2143
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 2138-2143
    • Meyer, B.H.1    Segura, J.-M.2    Martinez, K.L.3    Hovius, R.4    George, N.5    Johnsson, K.6    Vogel, H.7
  • 113
    • 33748333139 scopus 로고    scopus 로고
    • Live cell imaging of phosphoinositide dynamics with fluorescent protein domains
    • Várnai P., and Balla T. Live cell imaging of phosphoinositide dynamics with fluorescent protein domains. Biochim. Biophys. Acta 1761 (2006) 957-967
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 957-967
    • Várnai, P.1    Balla, T.2
  • 114
    • 48849099899 scopus 로고    scopus 로고
    • Resonance energy transfer in cells: a new look at fixation effect and receptor aggregation on cell membrane
    • Anikovsky M., Dale L., Ferguson S., and Petersen N. Resonance energy transfer in cells: a new look at fixation effect and receptor aggregation on cell membrane. Biophys. J. 95 (2008) 1349-1359
    • (2008) Biophys. J. , vol.95 , pp. 1349-1359
    • Anikovsky, M.1    Dale, L.2    Ferguson, S.3    Petersen, N.4
  • 115
    • 0035168442 scopus 로고    scopus 로고
    • Lipid rafts act as specialized domains for tetanus toxin binding and internalization into neurons
    • Herreros J., Ng T., and Schiavo G. Lipid rafts act as specialized domains for tetanus toxin binding and internalization into neurons. Mol. Biol. Cell 12 (2001) 2947-2960
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2947-2960
    • Herreros, J.1    Ng, T.2    Schiavo, G.3
  • 118
    • 0037303456 scopus 로고    scopus 로고
    • Emergence and evolution of functional heavy-chain antibodies in Camelidae
    • Conrath K.E., Wernery U., Muyldermans S., and Nguyen V.K. Emergence and evolution of functional heavy-chain antibodies in Camelidae. Dev. Comp. Immunol. 27 (2003) 87-103
    • (2003) Dev. Comp. Immunol. , vol.27 , pp. 87-103
    • Conrath, K.E.1    Wernery, U.2    Muyldermans, S.3    Nguyen, V.K.4
  • 119
    • 35649027327 scopus 로고    scopus 로고
    • Optical techniques for imaging membrane lipid microdomains in living cells
    • Owen D.M., Neil M.A.A., French P.M.W., and Magee A.I. Optical techniques for imaging membrane lipid microdomains in living cells. Sem. Cell Develop. Biol. 18 (2007) 591-598
    • (2007) Sem. Cell Develop. Biol. , vol.18 , pp. 591-598
    • Owen, D.M.1    Neil, M.A.A.2    French, P.M.W.3    Magee, A.I.4
  • 120
    • 33748545640 scopus 로고    scopus 로고
    • Imaging molecular interactions in living cells by FRET microscopy
    • Jares-Erijman E.A., and Jovin T.M. Imaging molecular interactions in living cells by FRET microscopy. Curr. Opin. Chem. Biol. 10 (2006) 409-416
    • (2006) Curr. Opin. Chem. Biol. , vol.10 , pp. 409-416
    • Jares-Erijman, E.A.1    Jovin, T.M.2
  • 121
    • 29144533892 scopus 로고    scopus 로고
    • Use of Forster's resonance energy transfer microscopy to study lipid rafts
    • Rao M., and Mayor S. Use of Forster's resonance energy transfer microscopy to study lipid rafts. Biochim. Biophys. Acta 1746 (2005) 221-233
    • (2005) Biochim. Biophys. Acta , vol.1746 , pp. 221-233
    • Rao, M.1    Mayor, S.2
  • 122
    • 55549111893 scopus 로고    scopus 로고
    • Quantitative FRET analysis by fast acquisition time domain FLIM at high spatial resolution in living cells
    • Padilla-Parra S., Auduge N., Coppey-Moisan M., and Tramier M. Quantitative FRET analysis by fast acquisition time domain FLIM at high spatial resolution in living cells. Biophys. J. 95 (2008) 2976-2988
    • (2008) Biophys. J. , vol.95 , pp. 2976-2988
    • Padilla-Parra, S.1    Auduge, N.2    Coppey-Moisan, M.3    Tramier, M.4
  • 123


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