메뉴 건너뛰기




Volumn 146, Issue 1, 2007, Pages 1-25

Fluorescent sterols as tools in membrane biophysics and cell biology

Author keywords

Cholesterol; Fluorescence; Imaging; Kinetics; Membrane transport; Microscopy

Indexed keywords

CHOLESTEROL; CHOLESTEROL ESTER; DEHYDROERGOSTEROL; ERGOSTEROL; STEROL DERIVATIVE; UNCLASSIFIED DRUG;

EID: 33846867956     PISSN: 00093084     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chemphyslip.2006.12.004     Document Type: Review
Times cited : (127)

References (155)
  • 1
    • 0037429651 scopus 로고    scopus 로고
    • Structural information about organized cholesterol domains from specific antibody recognition
    • Addadi L., Geva M., and Kruth H.S. Structural information about organized cholesterol domains from specific antibody recognition. Biochim. Biophys. Acta 1610 (2003) 208-216
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 208-216
    • Addadi, L.1    Geva, M.2    Kruth, H.S.3
  • 3
    • 0030774479 scopus 로고    scopus 로고
    • On the origin of sphingolipid/cholesterol-rich detergent-insoluble cell membranes: physiological concentrations of cholesterol and sphingolipid induce formation of a detergent-insoluble, liquid-ordered lipid phase in model membranes
    • Ahmed S.N., Brown D.A., and London E. On the origin of sphingolipid/cholesterol-rich detergent-insoluble cell membranes: physiological concentrations of cholesterol and sphingolipid induce formation of a detergent-insoluble, liquid-ordered lipid phase in model membranes. Biochemistry 36 (1997) 10944-10953
    • (1997) Biochemistry , vol.36 , pp. 10944-10953
    • Ahmed, S.N.1    Brown, D.A.2    London, E.3
  • 4
    • 0031228814 scopus 로고    scopus 로고
    • Photochemical reactions and phototoxicity of sterols: novel self-perpetuating mechanisms for lipid photoxidation
    • Albro P.W., Bilski P., Corbett J.T., Schroeder J.L., and Chignell C.F. Photochemical reactions and phototoxicity of sterols: novel self-perpetuating mechanisms for lipid photoxidation. Photochem. Photobiol. 66 (1997) 316-325
    • (1997) Photochem. Photobiol. , vol.66 , pp. 316-325
    • Albro, P.W.1    Bilski, P.2    Corbett, J.T.3    Schroeder, J.L.4    Chignell, C.F.5
  • 5
    • 0020183511 scopus 로고
    • Use of a fluorescent cholesterol derivative to measure lateral mobility of cholesterol in membranes
    • Alecio M.R., Golan D.E., Veatch W.R., and Rando R.R. Use of a fluorescent cholesterol derivative to measure lateral mobility of cholesterol in membranes. Proc. Natl. Acad. Sci. U.S.A. 79 (1982) 5171-5174
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 5171-5174
    • Alecio, M.R.1    Golan, D.E.2    Veatch, W.R.3    Rando, R.R.4
  • 7
    • 3843053654 scopus 로고    scopus 로고
    • Liver fatty acid-binding protein gene ablation inhibits branched-chain fatty acid metabolism in cultured primary hepatocytes
    • Atshaves B.P., McIntosh A.M., Lyuksyutova O.I., Zipfel W., Webb W.W., and Schroeder F. Liver fatty acid-binding protein gene ablation inhibits branched-chain fatty acid metabolism in cultured primary hepatocytes. J. Biol. Chem. 279 (2004) 30954-30965
    • (2004) J. Biol. Chem. , vol.279 , pp. 30954-30965
    • Atshaves, B.P.1    McIntosh, A.M.2    Lyuksyutova, O.I.3    Zipfel, W.4    Webb, W.W.5    Schroeder, F.6
  • 9
    • 33748476306 scopus 로고    scopus 로고
    • Lipid peroxides promote large rafts: effects of excitation of probes in fluorescence microscopy and electrochemical reactions during vesicle formation
    • Ayuyan A.G., and Cohen F.S. Lipid peroxides promote large rafts: effects of excitation of probes in fluorescence microscopy and electrochemical reactions during vesicle formation. Biophys. J. 91 (2006) 2172-2183
    • (2006) Biophys. J. , vol.91 , pp. 2172-2183
    • Ayuyan, A.G.1    Cohen, F.S.2
  • 10
    • 17844392332 scopus 로고    scopus 로고
    • Clathrin-dependent and clathrin-independent endocytosis are differentially sensitive to insertion of poly (ethylene glycol)-derivatized cholesterol in the plasma membrane
    • Baba T., Rauch C., Xue M., Terada N., Fujii Y., Ueda H., Takayama I., Ohno S., Farge E., and Sato S.B. Clathrin-dependent and clathrin-independent endocytosis are differentially sensitive to insertion of poly (ethylene glycol)-derivatized cholesterol in the plasma membrane. Traffic 2 (2001) 501-512
    • (2001) Traffic , vol.2 , pp. 501-512
    • Baba, T.1    Rauch, C.2    Xue, M.3    Terada, N.4    Fujii, Y.5    Ueda, H.6    Takayama, I.7    Ohno, S.8    Farge, E.9    Sato, S.B.10
  • 11
    • 0037429736 scopus 로고    scopus 로고
    • Phospholipid/cholesterol model membranes: formation of cholesterol crystallites
    • Bach D., and Wachtel E. Phospholipid/cholesterol model membranes: formation of cholesterol crystallites. Biochim. Biophys. Acta 1610 (2003) 187-197
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 187-197
    • Bach, D.1    Wachtel, E.2
  • 12
    • 0024400234 scopus 로고
    • Spontaneous transfer between phospholipid bilayers of dehydroergosterol, a fluorescent cholesterol analog
    • Bar L.K., Chong P.L., Barenholz Y., and Thompson T.E. Spontaneous transfer between phospholipid bilayers of dehydroergosterol, a fluorescent cholesterol analog. Biochim. Biophys. Acta 983 (1989) 109-112
    • (1989) Biochim. Biophys. Acta , vol.983 , pp. 109-112
    • Bar, L.K.1    Chong, P.L.2    Barenholz, Y.3    Thompson, T.E.4
  • 14
    • 0021738859 scopus 로고
    • Filipin as a cholesterol probe. I. Morphology of filipin-cholesterol interaction in lipid model systems
    • Behnke O., Tranum-Jensen J., and van Deurs B. Filipin as a cholesterol probe. I. Morphology of filipin-cholesterol interaction in lipid model systems. Eur. J. Cell Biol. 35 (1984) 189-199
    • (1984) Eur. J. Cell Biol. , vol.35 , pp. 189-199
    • Behnke, O.1    Tranum-Jensen, J.2    van Deurs, B.3
  • 15
    • 0021685522 scopus 로고
    • Filipin as a cholesterol probe. II. Filipin-cholesterol interaction in red blood cell membranes
    • Behnke O., Tranum-Jensen J., and van Deurs B. Filipin as a cholesterol probe. II. Filipin-cholesterol interaction in red blood cell membranes. Eur. J. Cell Biol. 35 (1984) 200-215
    • (1984) Eur. J. Cell Biol. , vol.35 , pp. 200-215
    • Behnke, O.1    Tranum-Jensen, J.2    van Deurs, B.3
  • 16
    • 0027181343 scopus 로고
    • Use of fluorescent cholesteryl ester microemulsions in cholesteryl ester transfer protein assays
    • Bisgaier C.L., Minton L.L., Essenburg A.D., White A., and Homan R. Use of fluorescent cholesteryl ester microemulsions in cholesteryl ester transfer protein assays. J. Lipid Res. 34 (1993) 1625-1634
    • (1993) J. Lipid Res. , vol.34 , pp. 1625-1634
    • Bisgaier, C.L.1    Minton, L.L.2    Essenburg, A.D.3    White, A.4    Homan, R.5
  • 17
    • 0018218323 scopus 로고
    • Cholesterol distribution between the two halves of the lipid bilayer of human erythrocyte ghost membranes
    • Blau L., and Bittman R. Cholesterol distribution between the two halves of the lipid bilayer of human erythrocyte ghost membranes. J. Biol. Chem. 253 (1978) 8366-8388
    • (1978) J. Biol. Chem. , vol.253 , pp. 8366-8388
    • Blau, L.1    Bittman, R.2
  • 18
    • 0002380192 scopus 로고
    • The biological synthesis of cholesterol
    • Bloch K. The biological synthesis of cholesterol. Science 150 (1965) 19-28
    • (1965) Science , vol.150 , pp. 19-28
    • Bloch, K.1
  • 20
    • 0033793871 scopus 로고    scopus 로고
    • Regulation of receptor function by cholesterol
    • Burger K., Gimpl G., and Fahrenholz F. Regulation of receptor function by cholesterol. Cell. Mol. Life Sci. 57 (2000) 1577-1592
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 1577-1592
    • Burger, K.1    Gimpl, G.2    Fahrenholz, F.3
  • 21
    • 0025260919 scopus 로고
    • Acidic phospholipids strikingly potentiate sterol carrier protein 2 mediated intermembrane sterol transfer
    • Butko P., Hapala I., Scallen T.J., and Schroeder F. Acidic phospholipids strikingly potentiate sterol carrier protein 2 mediated intermembrane sterol transfer. Biochemistry 29 (1990) 4070-4077
    • (1990) Biochemistry , vol.29 , pp. 4070-4077
    • Butko, P.1    Hapala, I.2    Scallen, T.J.3    Schroeder, F.4
  • 22
    • 0033527535 scopus 로고    scopus 로고
    • Unique cellular events occurring during the initial interaction of macrophages with matrix-retained or methylated aggregated low density lipoprotein (LDL). Prolonged cell-surface contact during which ldl-cholesteryl ester hydrolysis exceeds ldl protein degradation
    • Buton X., Mamdouh Z., Ghosh R.N., Du H., Kuriakose G., Beatini N., Grabowski G.A., Maxfield F.R., and Tabas I. Unique cellular events occurring during the initial interaction of macrophages with matrix-retained or methylated aggregated low density lipoprotein (LDL). Prolonged cell-surface contact during which ldl-cholesteryl ester hydrolysis exceeds ldl protein degradation. J. Biol. Chem. 274 (1999) 32112-32121
    • (1999) J. Biol. Chem. , vol.274 , pp. 32112-32121
    • Buton, X.1    Mamdouh, Z.2    Ghosh, R.N.3    Du, H.4    Kuriakose, G.5    Beatini, N.6    Grabowski, G.A.7    Maxfield, F.R.8    Tabas, I.9
  • 23
    • 0037089350 scopus 로고    scopus 로고
    • Protein-disulfide isomerase is a component of an NBD-cholesterol monomerizing protein complex from hamster small intestine
    • Cai T.Q., Guo Q., Wong B., Milot D., Zhang L., and Wright S.D. Protein-disulfide isomerase is a component of an NBD-cholesterol monomerizing protein complex from hamster small intestine. Biochim. Biophys. Acta 1581 (2002) 100-108
    • (2002) Biochim. Biophys. Acta , vol.1581 , pp. 100-108
    • Cai, T.Q.1    Guo, Q.2    Wong, B.3    Milot, D.4    Zhang, L.5    Wright, S.D.6
  • 24
    • 0032857624 scopus 로고    scopus 로고
    • The influence of membrane lateral pressures on simple geometric models of protein conformational equilibria
    • Cantor R.S. The influence of membrane lateral pressures on simple geometric models of protein conformational equilibria. Chem. Phys. Lipids 101 (1999) 45-56
    • (1999) Chem. Phys. Lipids , vol.101 , pp. 45-56
    • Cantor, R.S.1
  • 25
    • 0033028551 scopus 로고    scopus 로고
    • Lipid composition and the lateral pressure profile in bilayers
    • Cantor R.S. Lipid composition and the lateral pressure profile in bilayers. Biophys. J. 76 (1999) 2625-2639
    • (1999) Biophys. J. , vol.76 , pp. 2625-2639
    • Cantor, R.S.1
  • 26
    • 0023652259 scopus 로고
    • Parallax method for direct measurement of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids
    • Chattopadhyay A., and London E. Parallax method for direct measurement of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids. Biochemistry 26 (1987) 39-45
    • (1987) Biochemistry , vol.26 , pp. 39-45
    • Chattopadhyay, A.1    London, E.2
  • 27
    • 0025366661 scopus 로고
    • Chemistry and biology of N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)-labeled lipids: fluorescent probes of biological and model membranes
    • Chattopadhyay A. Chemistry and biology of N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)-labeled lipids: fluorescent probes of biological and model membranes. Chem. Phys. Lipids 53 (1990) 1-15
    • (1990) Chem. Phys. Lipids , vol.53 , pp. 1-15
    • Chattopadhyay, A.1
  • 28
    • 0031036751 scopus 로고    scopus 로고
    • Changes in the spectral properties of a plasma membrane lipid analog during the first seconds of endocytosis in living cells
    • Chen C.S., Martin O.C., and Pagano R.E. Changes in the spectral properties of a plasma membrane lipid analog during the first seconds of endocytosis in living cells. Biophys. J. 72 (1997) 37-50
    • (1997) Biophys. J. , vol.72 , pp. 37-50
    • Chen, C.S.1    Martin, O.C.2    Pagano, R.E.3
  • 29
    • 0042047094 scopus 로고    scopus 로고
    • Fluorescence studies of dehydroergosterol in phosphatidylethanolamine/phosphatidylcholine bilayers
    • Cheng K.H., Virtanen J., and Somerharju P. Fluorescence studies of dehydroergosterol in phosphatidylethanolamine/phosphatidylcholine bilayers. Biophys. J. 77 (1999) 3108-3119
    • (1999) Biophys. J. , vol.77 , pp. 3108-3119
    • Cheng, K.H.1    Virtanen, J.2    Somerharju, P.3
  • 30
    • 0028131711 scopus 로고
    • Evidence for regular distribution of sterols in liquid crystalline phosphatidylcholine bilayers
    • Chong P.L. Evidence for regular distribution of sterols in liquid crystalline phosphatidylcholine bilayers. Proc. Natl. Acad. Sci. U.S.A. 91 (1994) 10069-10073
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 10069-10073
    • Chong, P.L.1
  • 31
    • 0022999176 scopus 로고
    • Depolarization of dehydroergosterol in phospholipid bilayers
    • Chong P.L., and Thompson T.E. Depolarization of dehydroergosterol in phospholipid bilayers. Biochim. Biophys. Acta 863 (1986) 53-62
    • (1986) Biochim. Biophys. Acta , vol.863 , pp. 53-62
    • Chong, P.L.1    Thompson, T.E.2
  • 32
    • 0019561342 scopus 로고    scopus 로고
    • Craig, I.F., Via, D.P., Mantulin, W.W., Pownall, H.J., Gotto Jr., A.M., Smith, L.C., 1981. Low density lipoproteins reconstituted with steroids containing the nitrobenzoxadiazole fluorophore. J. Lipid Res. 22, 687-696.
  • 33
    • 1942519443 scopus 로고    scopus 로고
    • Cholesterol modulates the organization of the gammaM4 transmembrane domain of the muscle nicotinic acetylcholine receptor
    • de Almeida R.F., Loura L.M., Prieto M., Watts A., Fedorov A., and Barrantes F.J. Cholesterol modulates the organization of the gammaM4 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.1    Loura, L.M.2    Prieto, M.3    Watts, A.4    Fedorov, A.5    Barrantes, F.J.6
  • 34
    • 15944426129 scopus 로고    scopus 로고
    • Requirement of sterols in the life cycle of the nematode Caenorhabditis elegans
    • Entchev E.V., and Kurzchalia T.V. Requirement of sterols in the life cycle of the nematode Caenorhabditis elegans. Semin. Cell Dev. Biol. 16 (2005) 175-182
    • (2005) Semin. Cell Dev. Biol. , vol.16 , pp. 175-182
    • Entchev, E.V.1    Kurzchalia, T.V.2
  • 35
    • 0036260632 scopus 로고    scopus 로고
    • Deciphering endocytosis in Caenorhabditis elegans
    • Fares H., and Grant B. Deciphering endocytosis in Caenorhabditis elegans. Traffic 3 (2002) 11-19
    • (2002) Traffic , vol.3 , pp. 11-19
    • Fares, H.1    Grant, B.2
  • 36
    • 0021867669 scopus 로고
    • Fluorescence of delta 5,7,9(11),22-ergostatetraen-3 beta-ol in micelles, sterol carrier protein complexes, and plasma membranes
    • Fischer R.T., Cowlen M.S., Dempsey M.E., and Schroeder F. Fluorescence of delta 5,7,9(11),22-ergostatetraen-3 beta-ol in micelles, sterol carrier protein complexes, and plasma membranes. Biochemistry 24 (1985) 3322-3331
    • (1985) Biochemistry , vol.24 , pp. 3322-3331
    • Fischer, R.T.1    Cowlen, M.S.2    Dempsey, M.E.3    Schroeder, F.4
  • 37
    • 0034724682 scopus 로고    scopus 로고
    • Frolov, A., Petrescu, A., Atshaves, B.P., So, P.T., Gratton, E., Serrero, G., Schroeder, F., 2000. High density lipoprotein-mediated cholesterol uptake and targeting to lipid droplets in intact L-cell fibroblasts. J. Biol. Chem. 275, 12769-12780.
  • 38
    • 0029840406 scopus 로고    scopus 로고
    • Fibroblast membrane sterol kinetic domains: modulation by sterol carrier protein-2 and liver fatty acid binding protein
    • Frolov A., Woodford J.K., Murphy E.J., Billheimer J.T., and Schroeder F. Fibroblast membrane sterol kinetic domains: modulation by sterol carrier protein-2 and liver fatty acid binding protein. J. Lipid Res. 37 (1996) 1862-1874
    • (1996) J. Lipid Res. , vol.37 , pp. 1862-1874
    • Frolov, A.1    Woodford, J.K.2    Murphy, E.J.3    Billheimer, J.T.4    Schroeder, F.5
  • 39
    • 0030037450 scopus 로고    scopus 로고
    • Spontaneous and protein-mediated sterol transfer between intracellular membranes
    • Frolov A., Woodford J.K., Murphy E.J., Billheimer J.T., and Schroeder F. Spontaneous and protein-mediated sterol transfer between intracellular membranes. J. Biol. Chem. 271 (1996) 16075-16083
    • (1996) J. Biol. Chem. , vol.271 , pp. 16075-16083
    • Frolov, A.1    Woodford, J.K.2    Murphy, E.J.3    Billheimer, J.T.4    Schroeder, F.5
  • 40
    • 0032840026 scopus 로고    scopus 로고
    • Characterization by gas chromatography/mass spectrometry of sterols in Saccharomyces cerevisiae during autolysis
    • Fur Y.L., Maume G., Feuillat M., and Maume B.F. Characterization by gas chromatography/mass spectrometry of sterols in Saccharomyces cerevisiae during autolysis. J. Agric. Food Chem. 47 (1999) 2860-2864
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 2860-2864
    • Fur, Y.L.1    Maume, G.2    Feuillat, M.3    Maume, B.F.4
  • 41
    • 0033836520 scopus 로고    scopus 로고
    • The recycling endosome of Madin-Darby canine kidney cells is a mildly acidic compartment rich in raft components
    • Gagescu R., Demaurex N., Parton R.G., Hunziker W., Huber L.A., and Gruenberg J. The recycling endosome of Madin-Darby canine kidney cells is a mildly acidic compartment rich in raft components. Mol. Biol. Cell 11 (2000) 2775-2791
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2775-2791
    • Gagescu, R.1    Demaurex, N.2    Parton, R.G.3    Hunziker, W.4    Huber, L.A.5    Gruenberg, J.6
  • 42
    • 0032975368 scopus 로고    scopus 로고
    • Anisotropic motion of cholesterol in oriented DPPC bilayers studied by quasielastic neutron scattering: the liquid-ordered phase
    • Gliss C., Randel O., Casalta H., Sackmann E., Zorn R., and Bayerl T. Anisotropic motion of cholesterol in oriented DPPC bilayers studied by quasielastic neutron scattering: the liquid-ordered phase. Biophys. J. 77 (1999) 331-340
    • (1999) Biophys. J. , vol.77 , pp. 331-340
    • Gliss, C.1    Randel, O.2    Casalta, H.3    Sackmann, E.4    Zorn, R.5    Bayerl, T.6
  • 43
    • 0020479267 scopus 로고
    • Solubilization and localization of cholesteryl oleate in egg phosphatidylcholine vesicles. A carbon 13 NMR study
    • Hamilton J.A., and Small D.M. Solubilization and localization of cholesteryl oleate in egg phosphatidylcholine vesicles. A carbon 13 NMR study. J. Biol. Chem. 257 (1982) 7318-7321
    • (1982) J. Biol. Chem. , vol.257 , pp. 7318-7321
    • Hamilton, J.A.1    Small, D.M.2
  • 44
    • 0037016677 scopus 로고    scopus 로고
    • Vesicular and non-vesicular sterol transport in living cells. The endocytic recycling compartment is a major sterol storage organelle
    • Hao M., Lin S.X., Karylowski O.J., Wüstner D., McGraw T.E., and Maxfield F.R. Vesicular and non-vesicular sterol transport in living cells. The endocytic recycling compartment is a major sterol storage organelle. J. Biol. Chem. 277 (2002) 609-617
    • (2002) J. Biol. Chem. , vol.277 , pp. 609-617
    • Hao, M.1    Lin, S.X.2    Karylowski, O.J.3    Wüstner, D.4    McGraw, T.E.5    Maxfield, F.R.6
  • 45
    • 0035818530 scopus 로고    scopus 로고
    • Cholesterol depletion induces large scale domain segregation in living cell membranes
    • Hao M., Mukherjee S., and Maxfield F.R. Cholesterol depletion induces large scale domain segregation in living cell membranes. Proc. Natl. Acad. Sci. U.S.A. 98 (2001) 13072-13077
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 13072-13077
    • Hao, M.1    Mukherjee, S.2    Maxfield, F.R.3
  • 46
    • 1842639444 scopus 로고    scopus 로고
    • Effects of cholesterol depletion and increased lipid unsaturation on the properties of endocytic membranes
    • Hao M., Mukherjee S., Sun Y., and Maxfield F.R. Effects of cholesterol depletion and increased lipid unsaturation on the properties of endocytic membranes. J. Biol. Chem. 279 (2004) 14171-14178
    • (2004) J. Biol. Chem. , vol.279 , pp. 14171-14178
    • Hao, M.1    Mukherjee, S.2    Sun, Y.3    Maxfield, F.R.4
  • 47
    • 0028965138 scopus 로고
    • Evidence for transbilayer, tail-to-tail cholesterol dimers in dipalmitoylglycerophosphocholine liposomes
    • Harris J.S., Epps D.E., Davio S.R., and Kezdy F.J. Evidence for transbilayer, tail-to-tail cholesterol dimers in dipalmitoylglycerophosphocholine liposomes. Biochemistry 34 (1995) 3851-3857
    • (1995) Biochemistry , vol.34 , pp. 3851-3857
    • Harris, J.S.1    Epps, D.E.2    Davio, S.R.3    Kezdy, F.J.4
  • 48
    • 0036841874 scopus 로고    scopus 로고
    • Triton promotes domain formation in lipid raft mixtures
    • Heerklotz H. Triton promotes domain formation in lipid raft mixtures. Biophys. J. 83 (2002) 2693-2701
    • (2002) Biophys. J. , vol.83 , pp. 2693-2701
    • Heerklotz, H.1
  • 49
    • 33646178936 scopus 로고    scopus 로고
    • Atomistic simulation studies of cholesteryl oleates: model for the core of lipoprotein particles
    • Heikela M., Vattulainen I., and Hyvonen M.T. Atomistic simulation studies of cholesteryl oleates: model for the core of lipoprotein particles. Biophys. J. 90 (2006) 2247-2257
    • (2006) Biophys. J. , vol.90 , pp. 2247-2257
    • Heikela, M.1    Vattulainen, I.2    Hyvonen, M.T.3
  • 50
    • 0032449839 scopus 로고    scopus 로고
    • Mechanical aspects of membrane thermodynamics. Estimation of the mechanical properties of lipid membranes close to the chain melting transition from calorimetry
    • Heimburg T. Mechanical aspects of membrane thermodynamics. Estimation of the mechanical properties of lipid membranes close to the chain melting transition from calorimetry. Biochim. Biophys. Acta 1415 (1998) 147-162
    • (1998) Biochim. Biophys. Acta , vol.1415 , pp. 147-162
    • Heimburg, T.1
  • 52
    • 0034730730 scopus 로고    scopus 로고
    • Hill, W.G., Zeidel, M.L., 2000. Reconstituting the barrier properties of a water-tight epithelial membrane by design of leaflet-specific liposomes. J. Biol. Chem. 275, 30176-30185.
  • 53
    • 0037381939 scopus 로고    scopus 로고
    • Molecular dynamics simulations of phospholipid bilayers with cholesterol
    • Hofsass C., Lindahl E., and Edholm O. Molecular dynamics simulations of phospholipid bilayers with cholesterol. Biophys. J. 84 (2003) 2192-2206
    • (2003) Biophys. J. , vol.84 , pp. 2192-2206
    • Hofsass, C.1    Lindahl, E.2    Edholm, O.3
  • 54
    • 2442676239 scopus 로고    scopus 로고
    • Products of lipid peroxidation induce missorting of the principal lysosomal protease in retinal pigment epithelium
    • Hoppe G., O'Neil J., Hoff H.F., and Sears J. Products of lipid peroxidation induce missorting of the principal lysosomal protease in retinal pigment epithelium. Biochim. Biophys. Acta 1689 (2004) 33-41
    • (2004) Biochim. Biophys. Acta , vol.1689 , pp. 33-41
    • Hoppe, G.1    O'Neil, J.2    Hoff, H.F.3    Sears, J.4
  • 55
    • 21144453569 scopus 로고    scopus 로고
    • The effect of ergosterol on dipalmitoylphosphatidylcholine bilayers: a deuterium NMR and calorimetric study
    • Hsueh Y.W., Gilbert K., Trandum C., Zuckermann M., and Thewalt J. The effect of ergosterol on dipalmitoylphosphatidylcholine bilayers: a deuterium NMR and calorimetric study. Biophys. J. 88 (2005) 1799-1808
    • (2005) Biophys. J. , vol.88 , pp. 1799-1808
    • Hsueh, Y.W.1    Gilbert, K.2    Trandum, C.3    Zuckermann, M.4    Thewalt, J.5
  • 56
    • 0033065591 scopus 로고    scopus 로고
    • Huang. J., Feigenson, G.W., 1999a. A microscopic interaction model of maximum solubility of cholesterol in lipid bilayers. Biophys. J. 76, 2142-2157.
  • 57
    • 0033029569 scopus 로고    scopus 로고
    • Huang, J., Buboltz, J.T., Feigenson, G.W., 1999b. Maximum solubility of cholesterol in phosphatidylcholine and phosphatidylethanolamine bilayers. Biochim. Biophys. Acta 1417, 89-100.
  • 61
    • 0025945569 scopus 로고
    • Intracellular sterol distribution in transfected mouse L-cell fibroblasts expressing rat liver fatty acid-binding protein
    • Jefferson J.R., Slotte J.P., Nemecz G., Pastuszyn A., Scallen T.J., and Schroeder F. Intracellular sterol distribution in transfected mouse L-cell fibroblasts expressing rat liver fatty acid-binding protein. J. Biol. Chem. 266 (1991) 5486-5496
    • (1991) J. Biol. Chem. , vol.266 , pp. 5486-5496
    • Jefferson, J.R.1    Slotte, J.P.2    Nemecz, G.3    Pastuszyn, A.4    Scallen, T.J.5    Schroeder, F.6
  • 62
    • 7244244196 scopus 로고    scopus 로고
    • Lipids do influence protein function-the hydrophobic matching hypothesis revisited
    • Jensen M.O., and Mouritsen O.G. Lipids do influence protein function-the hydrophobic matching hypothesis revisited. Biochim. Biophys. Acta 1666 (2004) 205-226
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 205-226
    • Jensen, M.O.1    Mouritsen, O.G.2
  • 63
    • 0033585115 scopus 로고    scopus 로고
    • Hepatic scavenger receptor BI promotes rapid clearance of high density lipoprotein free cholesterol and its transport into bile
    • Ji Y., Wang N., Ramakrishnan R., Sehayek E., Huszar D., Breslow J.L., and Tall A.R. Hepatic scavenger receptor BI promotes rapid clearance of high density lipoprotein free cholesterol and its transport into bile. J. Biol. Chem. 274 (1999) 33398-33402
    • (1999) J. Biol. Chem. , vol.274 , pp. 33398-33402
    • Ji, Y.1    Wang, N.2    Ramakrishnan, R.3    Sehayek, E.4    Huszar, D.5    Breslow, J.L.6    Tall, A.R.7
  • 64
    • 0036708461 scopus 로고    scopus 로고
    • Rapid transbilayer movement of the fluorescent sterol dehydroergosterol in lipid membranes
    • John K., Kubelt J., Müller P., Wüstner D., and Herrmann A. Rapid transbilayer movement of the fluorescent sterol dehydroergosterol in lipid membranes. Biophys. J. 83 (2002) 1525-1534
    • (2002) Biophys. J. , vol.83 , pp. 1525-1534
    • John, K.1    Kubelt, J.2    Müller, P.3    Wüstner, D.4    Herrmann, A.5
  • 65
    • 0032532696 scopus 로고    scopus 로고
    • Determination of the depth of BODIPY probes in model membranes by parallax analysis of fluorescence quenching
    • Kaiser R.D., and London E. Determination of the depth of BODIPY probes in model membranes by parallax analysis of fluorescence quenching. Biochim. Biophys. Acta 1375 (1998) 13-22
    • (1998) Biochim. Biophys. Acta , vol.1375 , pp. 13-22
    • Kaiser, R.D.1    London, E.2
  • 66
    • 0028212559 scopus 로고
    • Erythrocyte membrane lateral sterol domains: a dehydroergosterol fluorescence polarization study
    • Kavecansky J., Joiner C.H., and Schroeder F. Erythrocyte membrane lateral sterol domains: a dehydroergosterol fluorescence polarization study. Biochemistry 33 (1994) 2880-2890
    • (1994) Biochemistry , vol.33 , pp. 2880-2890
    • Kavecansky, J.1    Joiner, C.H.2    Schroeder, F.3
  • 68
    • 0034535076 scopus 로고    scopus 로고
    • Lipid bilayers as osmotic response elements
    • Kinnunen P.K.J. Lipid bilayers as osmotic response elements. Cell. Physiol. Biochem. 10 (2000) 243-250
    • (2000) Cell. Physiol. Biochem. , vol.10 , pp. 243-250
    • Kinnunen, P.K.J.1
  • 69
    • 0034769264 scopus 로고    scopus 로고
    • Water permeability of asymmetric planar lipid bilayers: leaflets of different composition offer independent and additive resistance to permeation
    • Krylov A.V., Pohl P., Zeidel M.L., and Hill W.G. Water permeability of asymmetric planar lipid bilayers: leaflets of different composition offer independent and additive resistance to permeation. J. Gen. Physiol. 118 (2001) 333-339
    • (2001) J. Gen. Physiol. , vol.118 , pp. 333-339
    • Krylov, A.V.1    Pohl, P.2    Zeidel, M.L.3    Hill, W.G.4
  • 70
    • 0033384957 scopus 로고    scopus 로고
    • Regulation of endoplasmic reticulum cholesterol by plasma membrane cholesterol
    • Lange Y., Ye J., Rigney M., and Steck T.L. Regulation of endoplasmic reticulum cholesterol by plasma membrane cholesterol. J. Lipid Res. 40 (1999) 2264-2270
    • (1999) J. Lipid Res. , vol.40 , pp. 2264-2270
    • Lange, Y.1    Ye, J.2    Rigney, M.3    Steck, T.L.4
  • 71
    • 4143069270 scopus 로고    scopus 로고
    • How cholesterol homeostasis is regulated by plasma membrane cholesterol in excess of phospholipids
    • Lange Y., Ye J., and Steck T.L. How cholesterol homeostasis is regulated by plasma membrane cholesterol in excess of phospholipids. Proc. Natl. Acad. Sci. U.S.A. 101 (2004) 11664-11667
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 11664-11667
    • Lange, Y.1    Ye, J.2    Steck, T.L.3
  • 72
    • 0034815625 scopus 로고    scopus 로고
    • Use of cyclodextrins to monitor transbilayer movement and differential lipid affinities of cholesterol
    • Leventis R., and Silvius J.R. Use of cyclodextrins to monitor transbilayer movement and differential lipid affinities of cholesterol. Biophys. J. 81 (2001) 2257-2267
    • (2001) Biophys. J. , vol.81 , pp. 2257-2267
    • Leventis, R.1    Silvius, J.R.2
  • 73
    • 7244238074 scopus 로고    scopus 로고
    • ATP-binding cassette (ABC) transporters mediate non-vesicular, raft-modulated sterol movement from the plasma membrane to the endoplasmic reticulum
    • Li Y., and Prinz W.A. ATP-binding cassette (ABC) transporters mediate non-vesicular, raft-modulated sterol movement from the plasma membrane to the endoplasmic reticulum. J. Biol. Chem. 279 (2004) 45226-45234
    • (2004) J. Biol. Chem. , vol.279 , pp. 45226-45234
    • Li, Y.1    Prinz, W.A.2
  • 74
    • 0034271962 scopus 로고    scopus 로고
    • Spatial and energetic-entropic decomposition of surface tension in lipid bilayers from molecular dynamics simulations
    • Lindahl E., and Edholm O. Spatial and energetic-entropic decomposition of surface tension in lipid bilayers from molecular dynamics simulations. J. Chem. Phys. 113 (2000) 3882-3893
    • (2000) J. Chem. Phys. , vol.113 , pp. 3882-3893
    • Lindahl, E.1    Edholm, O.2
  • 75
    • 33846089323 scopus 로고    scopus 로고
    • Linder, M.D., Uronen, R.L., Holtta-Vuori, M., van der Sluijs, P., Peranen, J., Ikonen, E., 2006. Rab8-dependent recycling promotes endosomal cholesterol removal in normal and sphingolipidosis cells. Mol. Biol. Cell, in press.
  • 76
    • 0033616731 scopus 로고    scopus 로고
    • Evidence for a regulatory role of cholesterol superlattices in the hydrolytic activity of secretory phospholipase A2 in lipid membranes
    • Liu F., and Chong P.L. Evidence for a regulatory role of cholesterol superlattices in the hydrolytic activity of secretory phospholipase A2 in lipid membranes. Biochemistry 38 (1999) 3867-3873
    • (1999) Biochemistry , vol.38 , pp. 3867-3873
    • Liu, F.1    Chong, P.L.2
  • 77
    • 0030947939 scopus 로고    scopus 로고
    • Cholesterol and ergosterol superlattices in three-component liquid crystalline lipid bilayers as revealed by dehydroergosterol fluorescence
    • Liu F., Sugar I.P., and Chong P.L. Cholesterol and ergosterol superlattices in three-component liquid crystalline lipid bilayers as revealed by dehydroergosterol fluorescence. Biophys. J. 72 (1997) 2243-2254
    • (1997) Biophys. J. , vol.72 , pp. 2243-2254
    • Liu, F.1    Sugar, I.P.2    Chong, P.L.3
  • 78
    • 0030892178 scopus 로고    scopus 로고
    • Dehydroergosterol structural organization in aqueous medium and in a model system of membranes
    • Loura L.M., and Prieto M. Dehydroergosterol structural organization in aqueous medium and in a model system of membranes. Biophys. J. 72 (1997) 2226-2236
    • (1997) Biophys. J. , vol.72 , pp. 2226-2236
    • Loura, L.M.1    Prieto, M.2
  • 79
    • 0035795019 scopus 로고    scopus 로고
    • Exclusion of a cholesterol analog from the cholesterol-rich phase in model membranes
    • Loura L.M.S., Fedorov A., and Prieto M. Exclusion of a cholesterol analog from the cholesterol-rich phase in model membranes. Biochim. Biophys. Acta 1511 (2001) 236-243
    • (2001) Biochim. Biophys. Acta , vol.1511 , pp. 236-243
    • Loura, L.M.S.1    Fedorov, A.2    Prieto, M.3
  • 80
    • 0035169890 scopus 로고    scopus 로고
    • Artefacts in restored images due to intensity loss in three-dimensional fluorescence microscopy
    • Markham J., and Conchello J.A. Artefacts in restored images due to intensity loss in three-dimensional fluorescence microscopy. J. Microsc. 204 (2001) 93-98
    • (2001) J. Microsc. , vol.204 , pp. 93-98
    • Markham, J.1    Conchello, J.A.2
  • 81
    • 0030606012 scopus 로고    scopus 로고
    • Lateral pressures in membranes
    • Marsh D. Lateral pressures in membranes. Biochim. Biophys. Acta 1286 (1996) 183-223
    • (1996) Biochim. Biophys. Acta , vol.1286 , pp. 183-223
    • Marsh, D.1
  • 83
    • 0036702299 scopus 로고    scopus 로고
    • Plasma membrane microdomains
    • Maxfield F.R. Plasma membrane microdomains. Curr. Opin. Cell Biol. 14 (2002) 483-487
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 483-487
    • Maxfield, F.R.1
  • 84
    • 0036791574 scopus 로고    scopus 로고
    • Intracellular cholesterol transport
    • Maxfield F.R., and Wüstner D. Intracellular cholesterol transport. J. Clin. Invest. 110 (2002) 891-898
    • (2002) J. Clin. Invest. , vol.110 , pp. 891-898
    • Maxfield, F.R.1    Wüstner, D.2
  • 85
    • 0029044628 scopus 로고
    • Insolubility and redistribution of GPI-anchored proteins at the cell surface after detergent treatment
    • Mayor S., and Maxfield F.R. Insolubility and redistribution of GPI-anchored proteins at the cell surface after detergent treatment. Mol. Biol. Cell 6 (1995) 929-944
    • (1995) Mol. Biol. Cell , vol.6 , pp. 929-944
    • Mayor, S.1    Maxfield, F.R.2
  • 86
    • 0037458554 scopus 로고    scopus 로고
    • Fluorescence and multiphoton imaging resolve unique structural forms of sterol in membranes of living cells
    • McIntosh A.L., Gallegos A.M., Atshaves B.P., Storey S.M., Kannoju D., and Schroeder F. Fluorescence and multiphoton imaging resolve unique structural forms of sterol in membranes of living cells. J. Biol. Chem. 278 (2003) 6384-6403
    • (2003) J. Biol. Chem. , vol.278 , pp. 6384-6403
    • McIntosh, A.L.1    Gallegos, A.M.2    Atshaves, B.P.3    Storey, S.M.4    Kannoju, D.5    Schroeder, F.6
  • 88
    • 12344270987 scopus 로고    scopus 로고
    • What's so special about cholesterol?
    • Mouritsen O.G., and Zuckermann M.J. What's so special about cholesterol?. Lipids 39 (2004) 1101-1113
    • (2004) Lipids , vol.39 , pp. 1101-1113
    • Mouritsen, O.G.1    Zuckermann, M.J.2
  • 89
    • 14744278408 scopus 로고    scopus 로고
    • Monitoring cholesterol organization in membranes at low concentrations utilizing the wavelength-selective fluorescence approach
    • Mukherjee S., and Chattopadhyay A. Monitoring cholesterol organization in membranes at low concentrations utilizing the wavelength-selective fluorescence approach. Chem. Phys. Lett. 134 (2005) 79-84
    • (2005) Chem. Phys. Lett. , vol.134 , pp. 79-84
    • Mukherjee, S.1    Chattopadhyay, A.2
  • 91
    • 0031687965 scopus 로고    scopus 로고
    • Cholesterol distribution in living cells: fluorescence imaging using dehydroergosterol as a fluorescent cholesterol analog
    • Mukherjee S., Zha X., Tabas I., and Maxfield F.R. Cholesterol distribution in living cells: fluorescence imaging using dehydroergosterol as a fluorescent cholesterol analog. Biophys. J. 75 (1998) 1915-1925
    • (1998) Biophys. J. , vol.75 , pp. 1915-1925
    • Mukherjee, S.1    Zha, X.2    Tabas, I.3    Maxfield, F.R.4
  • 93
    • 0038620205 scopus 로고    scopus 로고
    • Recycling compartments and the internal vesicles of multivesicular bodies harbor most of the cholesterol found in the endocytic pathway
    • Möbius W., van Donselaar E., Ohno-Iwashita Y., Shimada Y., Heijnen H.F., Slot J.W., and Geuze H.J. Recycling compartments and the internal vesicles of multivesicular bodies harbor most of the cholesterol found in the endocytic pathway. Traffic 4 (2003) 222-231
    • (2003) Traffic , vol.4 , pp. 222-231
    • Möbius, W.1    van Donselaar, E.2    Ohno-Iwashita, Y.3    Shimada, Y.4    Heijnen, H.F.5    Slot, J.W.6    Geuze, H.J.7
  • 94
    • 0024298866 scopus 로고
    • Thermomechanical and transition properties of dimyristoylphosphatidylcholine/cholesterol bilayers
    • Needham D., McIntosh T.J., and Evans E. Thermomechanical and transition properties of dimyristoylphosphatidylcholine/cholesterol bilayers. Biochemistry 27 (1988) 4668-4673
    • (1988) Biochemistry , vol.27 , pp. 4668-4673
    • Needham, D.1    McIntosh, T.J.2    Evans, E.3
  • 95
    • 4344680331 scopus 로고    scopus 로고
    • Silver deposition on freeze-dried cells allows subcellular localization of cholesterol with imaging TOF-SIMS
    • Nygren H., and Malmberg P. Silver deposition on freeze-dried cells allows subcellular localization of cholesterol with imaging TOF-SIMS. J. Microsc. 215 (2004) 156-161
    • (2004) J. Microsc. , vol.215 , pp. 156-161
    • Nygren, H.1    Malmberg, P.2
  • 96
    • 0033838771 scopus 로고    scopus 로고
    • Cyclodextrin-catalyzed extraction of fluorescent sterols from monolayer membranes and small unilamellar vesicles
    • Ohvo-Rekila H., Akerlund B., and Slotte J.P. Cyclodextrin-catalyzed extraction of fluorescent sterols from monolayer membranes and small unilamellar vesicles. Chem. Phys. Lipids 105 (2000) 167-178
    • (2000) Chem. Phys. Lipids , vol.105 , pp. 167-178
    • Ohvo-Rekila, H.1    Akerlund, B.2    Slotte, J.P.3
  • 98
    • 13544274125 scopus 로고    scopus 로고
    • Role of sterol superlattice in free radical-induced sterol oxidation in lipid membranes
    • Olsher M., Yoon S.I., and Chong P.L. Role of sterol superlattice in free radical-induced sterol oxidation in lipid membranes. Biochemistry 44 (2005) 2080-2087
    • (2005) Biochemistry , vol.44 , pp. 2080-2087
    • Olsher, M.1    Yoon, S.I.2    Chong, P.L.3
  • 99
    • 0018369993 scopus 로고
    • Lipid Asymmetry in Membranes
    • op den Kamp J.A.F. Lipid Asymmetry in Membranes. Biochemistry 48 (1979) 47-71
    • (1979) Biochemistry , vol.48 , pp. 47-71
    • op den Kamp, J.A.F.1
  • 100
    • 1542375302 scopus 로고    scopus 로고
    • Lateral distribution of cholesterol in dioleoylphosphatidylcholine lipid bilayers: cholesterol-phospholipid interactions at high cholesterol limit
    • Parker A., Miles K., Cheng K.H., and Huang J. Lateral distribution of cholesterol in dioleoylphosphatidylcholine lipid bilayers: cholesterol-phospholipid interactions at high cholesterol limit. Biophys. J. 86 (2004) 1532-1544
    • (2004) Biophys. J. , vol.86 , pp. 1532-1544
    • Parker, A.1    Miles, K.2    Cheng, K.H.3    Huang, J.4
  • 101
    • 0018713650 scopus 로고
    • Synthesis of saturated, unsaturated, spin-labeled, and fluorescent cholesteryl esters: acylation of cholesterol using fatty acid anhydride and 4-pyrrolidinopyridine
    • Patel K.M., Sklar L.A., Currie R., Pownall H.J., Morrisett J.D., and Sparrow J.T. Synthesis of saturated, unsaturated, spin-labeled, and fluorescent cholesteryl esters: acylation of cholesterol using fatty acid anhydride and 4-pyrrolidinopyridine. Lipids 14 (1979) 816-818
    • (1979) Lipids , vol.14 , pp. 816-818
    • Patel, K.M.1    Sklar, L.A.2    Currie, R.3    Pownall, H.J.4    Morrisett, J.D.5    Sparrow, J.T.6
  • 102
    • 33244458202 scopus 로고    scopus 로고
    • Automated microscopy screening for compounds that partially revert cholesterol accumulation in Niemann-Pick C cells
    • Pipalia N.H., Huang A., Ralph H., Rujoi M., and Maxfield F.R. Automated microscopy screening for compounds that partially revert cholesterol accumulation in Niemann-Pick C cells. J. Lipid Res. 47 (2006) 284-301
    • (2006) J. Lipid Res. , vol.47 , pp. 284-301
    • Pipalia, N.H.1    Huang, A.2    Ralph, H.3    Rujoi, M.4    Maxfield, F.R.5
  • 103
    • 1642378564 scopus 로고    scopus 로고
    • Tracking down lipid flippases and their biological functions
    • Pomorski T., Holthuis J.C., Herrmann A., and van Meer G. Tracking down lipid flippases and their biological functions. J. Cell Sci. 117 (2004) 805-813
    • (2004) J. Cell Sci. , vol.117 , pp. 805-813
    • Pomorski, T.1    Holthuis, J.C.2    Herrmann, A.3    van Meer, G.4
  • 104
    • 0034611005 scopus 로고    scopus 로고
    • Sphingolipid-cholesterol rafts diffuse as small entities in the plasma membrane of mammalian cells
    • Pralle A., Keller P., Florin E.L., Simons K., and Horber J.K. Sphingolipid-cholesterol rafts diffuse as small entities in the plasma membrane of mammalian cells. J. Cell Biol. 148 (2000) 997-1008
    • (2000) J. Cell Biol. , vol.148 , pp. 997-1008
    • Pralle, A.1    Keller, P.2    Florin, E.L.3    Simons, K.4    Horber, J.K.5
  • 105
    • 0347572922 scopus 로고    scopus 로고
    • Direct evidence for cholesterol crystalline domains in biological membranes: role in human pathobiology
    • Preston Mason R., Tulenko T.N., and Jacob R.F. Direct evidence for cholesterol crystalline domains in biological membranes: role in human pathobiology. Biochim. Biophys. Acta 1610 (2003) 198-207
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 198-207
    • Preston Mason, R.1    Tulenko, T.N.2    Jacob, R.F.3
  • 106
    • 0033203501 scopus 로고    scopus 로고
    • Cholesterol modulates membrane traffic along the endocytic pathway in sphingolipid-storage diseases
    • Puri V., Watanabe R., Dominguez M., Sun X., Wheatley C.L., Marks D.L., and Pagano R.E. Cholesterol modulates membrane traffic along the endocytic pathway in sphingolipid-storage diseases. Nat. Cell Biol. 1 (1999) 386-388
    • (1999) Nat. Cell Biol. , vol.1 , pp. 386-388
    • Puri, V.1    Watanabe, R.2    Dominguez, M.3    Sun, X.4    Wheatley, C.L.5    Marks, D.L.6    Pagano, R.E.7
  • 107
    • 0034682556 scopus 로고    scopus 로고
    • Chemical activity of cholesterol in membranes
    • Radhakrishnan A., and McConnell H.M. Chemical activity of cholesterol in membranes. Biochemistry 39 (2000) 8119-8124
    • (2000) Biochemistry , vol.39 , pp. 8119-8124
    • Radhakrishnan, A.1    McConnell, H.M.2
  • 108
    • 15244358803 scopus 로고    scopus 로고
    • Interaction of melittin with membrane cholesterol: a fluorescence approach
    • Raghuraman H., and Chattopadhyay A. Interaction of melittin with membrane cholesterol: a fluorescence approach. Biophys. J. 87 (2004) 2419-2432
    • (2004) Biophys. J. , vol.87 , pp. 2419-2432
    • Raghuraman, H.1    Chattopadhyay, A.2
  • 109
    • 0036886885 scopus 로고    scopus 로고
    • Mapping cholesteryl ester analogue uptake and intracellular flow in Paramecium by confocal fluorescence microscopy
    • Ramoino P., Fronte P., Fato M., Beltrame F., and Diaspro A. Mapping cholesteryl ester analogue uptake and intracellular flow in Paramecium by confocal fluorescence microscopy. J. Microsc. 208 (2002) 167-176
    • (2002) J. Microsc. , vol.208 , pp. 167-176
    • Ramoino, P.1    Fronte, P.2    Fato, M.3    Beltrame, F.4    Diaspro, A.5
  • 110
    • 0035852757 scopus 로고    scopus 로고
    • Expression of scavenger receptor class B type 1 (SR-BI) promotes microvillar channel formation and selective cholesteryl ester transport in a heterologous reconstituted system
    • Reaven E., Leers-Sucheta S., Nomoto A., and Azhar S. Expression of scavenger receptor class B type 1 (SR-BI) promotes microvillar channel formation and selective cholesteryl ester transport in a heterologous reconstituted system. Proc. Natl. Acad. Sci. U.S.A. 98 (2001) 1613-1618
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 1613-1618
    • Reaven, E.1    Leers-Sucheta, S.2    Nomoto, A.3    Azhar, S.4
  • 111
    • 0030057435 scopus 로고    scopus 로고
    • Intracellular events in the "selective" transport of lipoprotein-derived cholesteryl esters
    • Reaven E., Tsai L., and Azhar S. Intracellular events in the "selective" transport of lipoprotein-derived cholesteryl esters. J. Biol. Chem. 271 (1996) 16208-16217
    • (1996) J. Biol. Chem. , vol.271 , pp. 16208-16217
    • Reaven, E.1    Tsai, L.2    Azhar, S.3
  • 112
    • 27844463048 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae, a model to study sterol uptake and transport in eukaryotes
    • Reiner S., Micolod D., and Schneiter R. Saccharomyces cerevisiae, a model to study sterol uptake and transport in eukaryotes. Biochem. Soc. Trans. 33 (2005) 1186-1188
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 1186-1188
    • Reiner, S.1    Micolod, D.2    Schneiter, R.3
  • 113
    • 0032947969 scopus 로고    scopus 로고
    • Delineation of a novel hepatic route for the selective transfer of unesterified sterols from high-density lipoproteins to bile: studies using the perfused rat liver
    • Robins S.J., and Fasulo J.M. Delineation of a novel hepatic route for the selective transfer of unesterified sterols from high-density lipoproteins to bile: studies using the perfused rat liver. Hepatology 29 (1999) 1541-1548
    • (1999) Hepatology , vol.29 , pp. 1541-1548
    • Robins, S.J.1    Fasulo, J.M.2
  • 114
    • 0018378526 scopus 로고
    • The organisation of cholesterol and ergosterol in lipid bilayers based on studies using non-perturbing fluorescent sterol probes
    • Rogers J., Lee A.G., and Wilton D.C. The organisation of cholesterol and ergosterol in lipid bilayers based on studies using non-perturbing fluorescent sterol probes. Biochim. Biophys. Acta 552 (1979) 23-37
    • (1979) Biochim. Biophys. Acta , vol.552 , pp. 23-37
    • Rogers, J.1    Lee, A.G.2    Wilton, D.C.3
  • 115
    • 0032413903 scopus 로고    scopus 로고
    • Free-radical and cyclooxygenase-catalyzed lipid peroxidation in membranes of blood cells under UV irradiation
    • Roshchupkin D.I., and Murina M.A. Free-radical and cyclooxygenase-catalyzed lipid peroxidation in membranes of blood cells under UV irradiation. Membr. Cell Biol. 12 (1998) 279-286
    • (1998) Membr. Cell Biol. , vol.12 , pp. 279-286
    • Roshchupkin, D.I.1    Murina, M.A.2
  • 116
    • 0034810547 scopus 로고    scopus 로고
    • Cholesterol organization in membranes at low concentrations: effects of curvature stress and membrane thickness
    • Rukmini R., Rawat S.S., Biswas S.C., and Chattopadhyay A. Cholesterol organization in membranes at low concentrations: effects of curvature stress and membrane thickness. Biophys. J. 81 (2001) 2122-2134
    • (2001) Biophys. J. , vol.81 , pp. 2122-2134
    • Rukmini, R.1    Rawat, S.S.2    Biswas, S.C.3    Chattopadhyay, A.4
  • 117
    • 2542493177 scopus 로고    scopus 로고
    • Distribution and transport of cholesterol-rich membrane domains monitored by a membrane-impermeant fluorescent polyethylene glycol-derivatized cholesterol
    • Sato S.B., Ishii K., Makino A., Iwabuchi K., Yamaji-Hasegawa A., Senoh Y., Nagaoka I., Sakuraba H., and Kobayashi T. Distribution and transport of cholesterol-rich membrane domains monitored by a membrane-impermeant fluorescent polyethylene glycol-derivatized cholesterol. J. Biol. Chem. 279 (2004) 23790-23796
    • (2004) J. Biol. Chem. , vol.279 , pp. 23790-23796
    • Sato, S.B.1    Ishii, K.2    Makino, A.3    Iwabuchi, K.4    Yamaji-Hasegawa, A.5    Senoh, Y.6    Nagaoka, I.7    Sakuraba, H.8    Kobayashi, T.9
  • 118
    • 25844447174 scopus 로고    scopus 로고
    • Diffusion of cholesterol and its precursors in lipid membranes studied by 1H pulsed field gradient magic angle spinning NMR
    • Scheidt H.A., Huster D., and Gawrisch K. Diffusion of cholesterol and its precursors in lipid membranes studied by 1H pulsed field gradient magic angle spinning NMR. Biophys. J. 89 (2005) 2504-2512
    • (2005) Biophys. J. , vol.89 , pp. 2504-2512
    • Scheidt, H.A.1    Huster, D.2    Gawrisch, K.3
  • 119
    • 0242580832 scopus 로고    scopus 로고
    • The potential of fluorescent and spin-labeled steroid analogs to mimic natural cholesterol
    • Scheidt H.A., Müller P., Herrmann A., and Huster D. The potential of fluorescent and spin-labeled steroid analogs to mimic natural cholesterol. J. Biol. Chem. 278 (2003) 45563-45569
    • (2003) J. Biol. Chem. , vol.278 , pp. 45563-45569
    • Scheidt, H.A.1    Müller, P.2    Herrmann, A.3    Huster, D.4
  • 120
    • 0025129177 scopus 로고
    • Interaction of fluorescent delta 5,7,9(11),22-ergostatetraen-3 beta-ol with sterol carrier protein-2
    • Schroeder F., Butko P., Nemecz G., and Scallen T.J. Interaction of fluorescent delta 5,7,9(11),22-ergostatetraen-3 beta-ol with sterol carrier protein-2. J. Biol. Chem. 265 (1990) 151-157
    • (1990) J. Biol. Chem. , vol.265 , pp. 151-157
    • Schroeder, F.1    Butko, P.2    Nemecz, G.3    Scallen, T.J.4
  • 121
    • 0021923008 scopus 로고
    • Sterol and squalene carrier protein interactions with fluorescent delta 5,7,9(11)-cholestatrien-3 beta-ol
    • Schroeder F., Dempsey M.E., and Fischer R.T. Sterol and squalene carrier protein interactions with fluorescent delta 5,7,9(11)-cholestatrien-3 beta-ol. J. Biol. Chem. 260 (1985) 2904-2911
    • (1985) J. Biol. Chem. , vol.260 , pp. 2904-2911
    • Schroeder, F.1    Dempsey, M.E.2    Fischer, R.T.3
  • 123
    • 0017752553 scopus 로고
    • Deuterium magnetic resonance: theory and application to lipid membranes
    • Seelig J. Deuterium magnetic resonance: theory and application to lipid membranes. Quart. Rev. Biophys. 10 (1977) 353-418
    • (1977) Quart. Rev. Biophys. , vol.10 , pp. 353-418
    • Seelig, J.1
  • 124
    • 33645967519 scopus 로고    scopus 로고
    • Correlated fluorescence-atomic force microscopy of membrane domains: structure of fluorescence probes determines lipid localization
    • Shaw J.E., Epand R.F., Epand R.M., Li Z., Bittman R., and Yip C.M. Correlated fluorescence-atomic force microscopy of membrane domains: structure of fluorescence probes determines lipid localization. Biophys. J. 90 (2006) 2170-2178
    • (2006) Biophys. J. , vol.90 , pp. 2170-2178
    • Shaw, J.E.1    Epand, R.F.2    Epand, R.M.3    Li, Z.4    Bittman, R.5    Yip, C.M.6
  • 126
    • 0035816645 scopus 로고    scopus 로고
    • High density lipoprotein (HDL) particle uptake mediated by scavenger receptor class B type 1 results in selective sorting of HDL cholesterol from protein and polarized cholesterol secretion
    • Silver D.L., Wang N., Xiao X., and Tall A.R. High density lipoprotein (HDL) particle uptake mediated by scavenger receptor class B type 1 results in selective sorting of HDL cholesterol from protein and polarized cholesterol secretion. J. Biol. Chem. 276 (2001) 25287-25293
    • (2001) J. Biol. Chem. , vol.276 , pp. 25287-25293
    • Silver, D.L.1    Wang, N.2    Xiao, X.3    Tall, A.R.4
  • 127
    • 0029906007 scopus 로고    scopus 로고
    • Cholesterol at different bilayer concentrations can promote or antagonize lateral segregation of phospholipids of differing acyl chain length
    • Silvius J.R., del Giudice D., and Lafleur M. Cholesterol at different bilayer concentrations can promote or antagonize lateral segregation of phospholipids of differing acyl chain length. Biochemistry 35 (1996) 15198-15208
    • (1996) Biochemistry , vol.35 , pp. 15198-15208
    • Silvius, J.R.1    del Giudice, D.2    Lafleur, M.3
  • 128
    • 0023788823 scopus 로고
    • Lipid sorting in epithelial cells
    • Simons K., and van Meer G. Lipid sorting in epithelial cells. Biochemistry 27 (1988) 6197-6202
    • (1988) Biochemistry , vol.27 , pp. 6197-6202
    • Simons, K.1    van Meer, G.2
  • 129
    • 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
  • 130
    • 0035073937 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the structure of dimyristoylphosphatidylcholine bilayers with cholesterol, ergosterol, and lanosterol
    • Smondyrev A.M., and Berkowitz M.L. Molecular dynamics simulation of the structure of dimyristoylphosphatidylcholine bilayers with cholesterol, ergosterol, and lanosterol. Biophys. J. 80 (2001) 1649-1658
    • (2001) Biophys. J. , vol.80 , pp. 1649-1658
    • Smondyrev, A.M.1    Berkowitz, M.L.2
  • 131
    • 0022999003 scopus 로고
    • Physical properties of the fluorescent sterol probe dehydroergosterol
    • Smutzer G., Crawford B.F., and Yeagle P.L. Physical properties of the fluorescent sterol probe dehydroergosterol. Biochim. Biophys. Acta 862 (1986) 361-371
    • (1986) Biochim. Biophys. Acta , vol.862 , pp. 361-371
    • Smutzer, G.1    Crawford, B.F.2    Yeagle, P.L.3
  • 132
    • 0022423303 scopus 로고
    • A fluorescence anisotropy study on the phase behaviour of dimyristoylphosphatidylcholine / cholesterol mixtures
    • Smutzer G., and Yeagle P.L. A fluorescence anisotropy study on the phase behaviour of dimyristoylphosphatidylcholine / cholesterol mixtures. Biochim. Biophys. Acta 814 (1985) 274-280
    • (1985) Biochim. Biophys. Acta , vol.814 , pp. 274-280
    • Smutzer, G.1    Yeagle, P.L.2
  • 133
    • 0032817738 scopus 로고    scopus 로고
    • Lateral organisation of membrane lipids. The superlattice view
    • Somerharju P., Virtanen J.A., and Cheng K.H. Lateral organisation of membrane lipids. The superlattice view. Biochim. Biophys. Acta 1440 (1999) 32-48
    • (1999) Biochim. Biophys. Acta , vol.1440 , pp. 32-48
    • Somerharju, P.1    Virtanen, J.A.2    Cheng, K.H.3
  • 134
    • 0027217613 scopus 로고
    • Bile canaliculus formation in cultured HEPG2 cells
    • Sormunen R., Eskelinen S., and Lehto V.P. Bile canaliculus formation in cultured HEPG2 cells. Lab. Invest. 68 (1993) 652-662
    • (1993) Lab. Invest. , vol.68 , pp. 652-662
    • Sormunen, R.1    Eskelinen, S.2    Lehto, V.P.3
  • 135
    • 0029876525 scopus 로고    scopus 로고
    • Thermodynamics of transfer of cholesterol from gel to fluid phases of phospholipid bilayers
    • Spink C.H., Manley S., and Breed M. Thermodynamics of transfer of cholesterol from gel to fluid phases of phospholipid bilayers. Biochim. Biophys. Acta 1279 (1996) 190-196
    • (1996) Biochim. Biophys. Acta , vol.1279 , pp. 190-196
    • Spink, C.H.1    Manley, S.2    Breed, M.3
  • 136
    • 0036789540 scopus 로고    scopus 로고
    • Probing red cell membrane cholesterol movement with cyclodextrin
    • Steck T.L., Ye J., and Lange Y. Probing red cell membrane cholesterol movement with cyclodextrin. Biophys. J. 83 (2002) 2118-2125
    • (2002) Biophys. J. , vol.83 , pp. 2118-2125
    • Steck, T.L.1    Ye, J.2    Lange, Y.3
  • 137
    • 0033806452 scopus 로고    scopus 로고
    • Sterol balance in the Smith-Lemli-Opitz syndrome. Reduction in whole body cholesterol synthesis and normal bile acid production
    • Steiner R.D., Linck L.M., Flavell D.P., Lin D.S., and Connor W.E. Sterol balance in the Smith-Lemli-Opitz syndrome. Reduction in whole body cholesterol synthesis and normal bile acid production. J. Lipid Res. 41 (2000) 1437-1447
    • (2000) J. Lipid Res. , vol.41 , pp. 1437-1447
    • Steiner, R.D.1    Linck, L.M.2    Flavell, D.P.3    Lin, D.S.4    Connor, W.E.5
  • 138
    • 0033544895 scopus 로고    scopus 로고
    • Holo-sterol carrier protein-2. (13)C NMR investigation of cholesterol and fatty acid binding sites
    • Stolowich N., Frolov A., Petrescu A.D., Scott A.I., Billheimer J.T., and Schroeder F. Holo-sterol carrier protein-2. (13)C NMR investigation of cholesterol and fatty acid binding sites. J. Biol. Chem. 274 (1999) 35425-35433
    • (1999) J. Biol. Chem. , vol.274 , pp. 35425-35433
    • Stolowich, N.1    Frolov, A.2    Petrescu, A.D.3    Scott, A.I.4    Billheimer, J.T.5    Schroeder, F.6
  • 139
    • 0019874707 scopus 로고
    • Use of resonance energy transfer to monitor membrane fusion
    • Struck D.K., Hoekstra D., and Pagano R.E. Use of resonance energy transfer to monitor membrane fusion. Biochemistry 20 (1981) 4093-4099
    • (1981) Biochemistry , vol.20 , pp. 4093-4099
    • Struck, D.K.1    Hoekstra, D.2    Pagano, R.E.3
  • 140
    • 0034672703 scopus 로고    scopus 로고
    • Cholesterol and phospholipid metabolism in macrophages
    • Tabas I. Cholesterol and phospholipid metabolism in macrophages. Biochim. Biophys. Acta 1529 (2000) 164-174
    • (2000) Biochim. Biophys. Acta , vol.1529 , pp. 164-174
    • Tabas, I.1
  • 141
    • 0030443383 scopus 로고    scopus 로고
    • The binding of cholesterol and bile salts to recombinant rat liver fatty acid-binding protein
    • Thumser A.E., and Wilton D.C. The binding of cholesterol and bile salts to recombinant rat liver fatty acid-binding protein. Biochem. J. 320 (1996) 729-733
    • (1996) Biochem. J. , vol.320 , pp. 729-733
    • Thumser, A.E.1    Wilton, D.C.2
  • 142
    • 33644871685 scopus 로고    scopus 로고
    • Significance of sterol structural specificity. Desmosterol cannot replace cholesterol in lipid rafts
    • Vainio S., Jansen M., Koivusalo M., Rog T., Karttunen M., Vattulainen I., and Ikonen E. Significance of sterol structural specificity. Desmosterol cannot replace cholesterol in lipid rafts. J. Biol. Chem. 281 (2006) 348-355
    • (2006) J. Biol. Chem. , vol.281 , pp. 348-355
    • Vainio, S.1    Jansen, M.2    Koivusalo, M.3    Rog, T.4    Karttunen, M.5    Vattulainen, I.6    Ikonen, E.7
  • 143
    • 0025128695 scopus 로고
    • Phase equilibria of cholesterol/dipalmitoylphosphatidylcholine mixtures: 2H nuclear magnetic resonance and differential scanning calorimetry
    • Vist M.R., and Davis J.H. Phase equilibria of cholesterol/dipalmitoylphosphatidylcholine mixtures: 2H 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
  • 144
    • 0037389276 scopus 로고    scopus 로고
    • Transport of plasma membrane-derived cholesterol and the function of Niemann-Pick C1 Protein
    • Wiegand V., Chang T.Y., Strauss J.F.r., Fahrenholz F., and Gimpl G. Transport of plasma membrane-derived cholesterol and the function of Niemann-Pick C1 Protein. FASEB J. 17 (2003) 782-784
    • (2003) FASEB J. , vol.17 , pp. 782-784
    • Wiegand, V.1    Chang, T.Y.2    Strauss, J.F.r.3    Fahrenholz, F.4    Gimpl, G.5
  • 145
  • 146
    • 0032776578 scopus 로고    scopus 로고
    • A fluorescence energy transfer study of lecithin-cholesterol vesicles in the presence of phospholipase C
    • Wrenn S.P., Kaler E.W., and Lee S.P. A fluorescence energy transfer study of lecithin-cholesterol vesicles in the presence of phospholipase C. J. Lipid Res. 40 (1999) 1483-1494
    • (1999) J. Lipid Res. , vol.40 , pp. 1483-1494
    • Wrenn, S.P.1    Kaler, E.W.2    Lee, S.P.3
  • 147
    • 27944453100 scopus 로고    scopus 로고
    • Improved visualization and quantitative analysis of fluorescent membrane sterol in polarized hepatic cells
    • Wüstner D. Improved visualization and quantitative analysis of fluorescent membrane sterol in polarized hepatic cells. J. Microsc. 220 (2005) 47-64
    • (2005) J. Microsc. , vol.220 , pp. 47-64
    • Wüstner, D.1
  • 148
    • 14844307609 scopus 로고    scopus 로고
    • Mathematical analysis of hepatic high density lipoprotein transport based on quantitative imaging data
    • Wüstner D. Mathematical analysis of hepatic high density lipoprotein transport based on quantitative imaging data. J. Biol. Chem. 280 (2005) 6766-6779
    • (2005) J. Biol. Chem. , vol.280 , pp. 6766-6779
    • Wüstner, D.1
  • 149
    • 33846056461 scopus 로고    scopus 로고
    • Plasma membrane sterol distribution resembles the surface topography of living cells
    • Wüstner D. Plasma membrane sterol distribution resembles the surface topography of living cells. Mol. Biol. Cell 18 (2007) 211-228
    • (2007) Mol. Biol. Cell , vol.18 , pp. 211-228
    • Wüstner, D.1
  • 150
    • 0037119406 scopus 로고    scopus 로고
    • Rapid non-vesicular transport of sterol between the plasma membrane domains of polarized hepatic cells
    • Wüstner D., Herrmann A., Hao M., and Maxfield F.R. Rapid non-vesicular transport of sterol between the plasma membrane domains of polarized hepatic cells. J. Biol. Chem. 277 (2002) 30325-30336
    • (2002) J. Biol. Chem. , vol.277 , pp. 30325-30336
    • Wüstner, D.1    Herrmann, A.2    Hao, M.3    Maxfield, F.R.4
  • 151
    • 12144286290 scopus 로고    scopus 로고
    • Different transport routes for high density lipoprotein and its associated free sterol in polarized hepatic cells
    • Wüstner D., Mondal M., Huang A., and Maxfield F.R. Different transport routes for high density lipoprotein and its associated free sterol in polarized hepatic cells. J. Lipid Res. 45 (2004) 427-437
    • (2004) J. Lipid Res. , vol.45 , pp. 427-437
    • Wüstner, D.1    Mondal, M.2    Huang, A.3    Maxfield, F.R.4
  • 152
    • 17444368686 scopus 로고    scopus 로고
    • Direct observation of rapid internalization and intracellular transport of sterol by macrophage foam cells
    • Wüstner D., Mondal M., Tabas I., and Maxfield F.R. Direct observation of rapid internalization and intracellular transport of sterol by macrophage foam cells. Traffic 6 (2005) 396-412
    • (2005) Traffic , vol.6 , pp. 396-412
    • Wüstner, D.1    Mondal, M.2    Tabas, I.3    Maxfield, F.R.4
  • 153
    • 0026077761 scopus 로고
    • Lipoproteins activate acyl-coenzyme A:cholesterol acyltransferase in macrophages only after cellular cholesterol pools are expanded to a critical threshold level
    • Xu X.X., and Tabas I. Lipoproteins activate acyl-coenzyme A:cholesterol acyltransferase in macrophages only after cellular cholesterol pools are expanded to a critical threshold level. J. Biol. Chem. 266 (1991) 17040-17048
    • (1991) J. Biol. Chem. , vol.266 , pp. 17040-17048
    • Xu, X.X.1    Tabas, I.2
  • 154
    • 0020359871 scopus 로고
    • Molecular packing of cholesterol in phospholipid vesicles as probed by dehydroergosterol
    • Yeagle P.L., Bensen J., Boni L., and Hui S.W. Molecular packing of cholesterol in phospholipid vesicles as probed by dehydroergosterol. Biochim. Biophys. Acta 692 (1982) 139-146
    • (1982) Biochim. Biophys. Acta , vol.692 , pp. 139-146
    • Yeagle, P.L.1    Bensen, J.2    Boni, L.3    Hui, S.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.