메뉴 건너뛰기




Volumn 1859, Issue 7, 2017, Pages 1242-1253

Choosing the right fluorophore for single-molecule fluorescence studies in a lipid environment

Author keywords

Adsorption; FCS; Fluorescent dyes; Lipids; Single molecule spectroscopy

Indexed keywords

ALEXA 488; ALEXA 647; ATTO 488; ATTO 532; ATTO 565; ATTO 594; ATTO 647N; CHOLESTEROL; CY5 DYE; FL DYE; FLUORESCENT DYE; LIPID; UNCLASSIFIED DRUG; PROTEIN;

EID: 85017631152     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2017.04.001     Document Type: Article
Times cited : (37)

References (59)
  • 2
    • 79955685287 scopus 로고    scopus 로고
    • Allostery in a disordered protein: oxidative modifications to alpha-synuclein act distally to regulate membrane binding
    • [2] Sevcsik, E., et al. Allostery in a disordered protein: oxidative modifications to alpha-synuclein act distally to regulate membrane binding. J. Am. Chem. Soc. 133:18 (2011), 7152–7158.
    • (2011) J. Am. Chem. Soc. , vol.133 , Issue.18 , pp. 7152-7158
    • Sevcsik, E.1
  • 4
    • 83455177932 scopus 로고    scopus 로고
    • Statistical convergence of equilibrium properties in simulations of molecular solutes embedded in lipid bilayers
    • [4] Neale, C., et al. Statistical convergence of equilibrium properties in simulations of molecular solutes embedded in lipid bilayers. J. Chem. Theory Comput. 7:12 (2011), 4175–4188.
    • (2011) J. Chem. Theory Comput. , vol.7 , Issue.12 , pp. 4175-4188
    • Neale, C.1
  • 5
    • 74049147038 scopus 로고    scopus 로고
    • Monitoring protein interactions and dynamics with solvatochromic fluorophores
    • [5] Loving, G.S., Sainlos, M., Imperiali, B., Monitoring protein interactions and dynamics with solvatochromic fluorophores. Trends Biotechnol. 28:2 (2010), 73–83.
    • (2010) Trends Biotechnol. , vol.28 , Issue.2 , pp. 73-83
    • Loving, G.S.1    Sainlos, M.2    Imperiali, B.3
  • 6
    • 77958455514 scopus 로고    scopus 로고
    • Effects of curvature and composition on α-synuclein binding to lipid vesicles
    • [6] Middleton, E.R., Rhoades, E., Effects of curvature and composition on α-synuclein binding to lipid vesicles. Biophys. J. 99:7 (2010), 2279–2288.
    • (2010) Biophys. J. , vol.99 , Issue.7 , pp. 2279-2288
    • Middleton, E.R.1    Rhoades, E.2
  • 7
    • 65249185574 scopus 로고    scopus 로고
    • Interplay of alpha-synuclein binding and conformational switching probed by single-molecule fluorescence
    • [7] Ferreon, A.C., et al. Interplay of alpha-synuclein binding and conformational switching probed by single-molecule fluorescence. Proc. Natl. Acad. Sci. U. S. A. 106:14 (2009), 5645–5650.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , Issue.14 , pp. 5645-5650
    • Ferreon, A.C.1
  • 8
    • 80051786035 scopus 로고    scopus 로고
    • The effect of variable liposome brightness on quantifying lipid–protein interactions using fluorescence correlation spectroscopy
    • [8] Melo, A.M., Prieto, M., Coutinho, A., The effect of variable liposome brightness on quantifying lipid–protein interactions using fluorescence correlation spectroscopy. Biochim. Biophys. Acta Biomembr. 1808:10 (2011), 2559–2568.
    • (2011) Biochim. Biophys. Acta Biomembr. , vol.1808 , Issue.10 , pp. 2559-2568
    • Melo, A.M.1    Prieto, M.2    Coutinho, A.3
  • 9
    • 0035819204 scopus 로고    scopus 로고
    • Immobilization in surface-tethered lipid vesicles as a new tool for single biomolecule spectroscopy
    • [9] Boukobza, E., Sonnenfeld, A., Haran, G., Immobilization in surface-tethered lipid vesicles as a new tool for single biomolecule spectroscopy. J. Phys. Chem. B 105:48 (2001), 12165–12170.
    • (2001) J. Phys. Chem. B , vol.105 , Issue.48 , pp. 12165-12170
    • Boukobza, E.1    Sonnenfeld, A.2    Haran, G.3
  • 10
    • 8844247109 scopus 로고    scopus 로고
    • Two-state folding observed in individual protein molecules
    • [10] Rhoades, E., et al. Two-state folding observed in individual protein molecules. J. Am. Chem. Soc. 126:45 (2004), 14686–14687.
    • (2004) J. Am. Chem. Soc. , vol.126 , Issue.45 , pp. 14686-14687
    • Rhoades, E.1
  • 11
    • 84898741942 scopus 로고    scopus 로고
    • Single molecule FRET reveals pore size and opening mechanism of a mechano-sensitive ion channel
    • [11] Wang, Y., et al. Single molecule FRET reveals pore size and opening mechanism of a mechano-sensitive ion channel. elife, 3, 2014, e01834.
    • (2014) elife , vol.3 , pp. e01834
    • Wang, Y.1
  • 12
    • 84979266089 scopus 로고    scopus 로고
    • Single-molecule patch-clamp-FRET-anisotropy microscopy studies of NMDA receptor ion channel activation and deactivation under agonist ligand binding in living cells
    • [12] Sasmal, D.K., Yadav, R., Lu, H.P., Single-molecule patch-clamp-FRET-anisotropy microscopy studies of NMDA receptor ion channel activation and deactivation under agonist ligand binding in living cells. J. Am. Chem. Soc., 2016.
    • (2016) J. Am. Chem. Soc.
    • Sasmal, D.K.1    Yadav, R.2    Lu, H.P.3
  • 13
    • 0037452963 scopus 로고    scopus 로고
    • Watching proteins fold one molecule at a time
    • [13] Rhoades, E., Gussakovsky, E., Haran, G., Watching proteins fold one molecule at a time. Proc. Natl. Acad. Sci. 100:6 (2003), 3197–3202.
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , Issue.6 , pp. 3197-3202
    • Rhoades, E.1    Gussakovsky, E.2    Haran, G.3
  • 14
    • 7544225920 scopus 로고    scopus 로고
    • Vesicle encapsulation studies reveal that single molecule ribozyme heterogeneities are intrinsic
    • [14] Okumus, B., et al. Vesicle encapsulation studies reveal that single molecule ribozyme heterogeneities are intrinsic. Biophys. J. 87:4 (2004), 2798–2806.
    • (2004) Biophys. J. , vol.87 , Issue.4 , pp. 2798-2806
    • Okumus, B.1
  • 15
    • 77957090469 scopus 로고    scopus 로고
    • Nanovesicle trapping for studying weak protein interactions by single-molecule FRET
    • [15] Benítez, J.J., Keller, A.M., Chen, P., Nanovesicle trapping for studying weak protein interactions by single-molecule FRET. Methods Enzymol. 472 (2010), 41–60.
    • (2010) Methods Enzymol. , vol.472 , pp. 41-60
    • Benítez, J.J.1    Keller, A.M.2    Chen, P.3
  • 16
    • 84856935207 scopus 로고    scopus 로고
    • Single-molecule pull-down for studying protein interactions
    • [16] Jain, A., et al. Single-molecule pull-down for studying protein interactions. Nat. Protoc. 7:3 (2012), 445–452.
    • (2012) Nat. Protoc. , vol.7 , Issue.3 , pp. 445-452
    • Jain, A.1
  • 17
    • 79953838275 scopus 로고    scopus 로고
    • Beyond the random coil: stochastic conformational switching in intrinsically disordered proteins
    • [17] Choi, U.B., et al. Beyond the random coil: stochastic conformational switching in intrinsically disordered proteins. Structure 19:4 (2011), 566–576.
    • (2011) Structure , vol.19 , Issue.4 , pp. 566-576
    • Choi, U.B.1
  • 18
    • 84930662255 scopus 로고    scopus 로고
    • Quantitative interpretation of FRET experiments via molecular simulation: force field and validation
    • [18] Best, R.B., et al. Quantitative interpretation of FRET experiments via molecular simulation: force field and validation. Biophys. J. 108:11 (2015), 2721–2731.
    • (2015) Biophys. J. , vol.108 , Issue.11 , pp. 2721-2731
    • Best, R.B.1
  • 19
    • 84895122929 scopus 로고    scopus 로고
    • Choose your label wisely: water-soluble fluorophores often interact with lipid bilayers
    • [19] Hughes, L.D., Rawle, R.J., Boxer, S.G., Choose your label wisely: water-soluble fluorophores often interact with lipid bilayers. PLoS One, 9(2), 2014, e87649.
    • (2014) PLoS One , vol.9 , Issue.2 , pp. e87649
    • Hughes, L.D.1    Rawle, R.J.2    Boxer, S.G.3
  • 20
    • 79551522926 scopus 로고    scopus 로고
    • On the performance of bioanalytical fluorescence correlation spectroscopy measurements in a multiparameter photon-counting microscope
    • [20] Mazouchi, A., et al. On the performance of bioanalytical fluorescence correlation spectroscopy measurements in a multiparameter photon-counting microscope. Anal. Chim. Acta 688:1 (2011), 61–69.
    • (2011) Anal. Chim. Acta , vol.688 , Issue.1 , pp. 61-69
    • Mazouchi, A.1
  • 21
    • 35949038838 scopus 로고
    • Thermodynamic fluctuations in a reacting system—measurement by fluorescence correlation spectroscopy
    • [21] Magde, D., Elson, E., Webb, W.W., Thermodynamic fluctuations in a reacting system—measurement by fluorescence correlation spectroscopy. Phys. Rev. Lett., 29(11), 1972, 705.
    • (1972) Phys. Rev. Lett. , vol.29 , Issue.11 , pp. 705
    • Magde, D.1    Elson, E.2    Webb, W.W.3
  • 22
    • 84884942553 scopus 로고    scopus 로고
    • Sub-diffusion decays in fluorescence correlation spectroscopy: dye photophysics or protein dynamics?
    • [22] Mazouchi, A., Bahram, A., Gradinaru, C.C., Sub-diffusion decays in fluorescence correlation spectroscopy: dye photophysics or protein dynamics?. J. Phys. Chem. B 117:38 (2013), 11100–11111.
    • (2013) J. Phys. Chem. B , vol.117 , Issue.38 , pp. 11100-11111
    • Mazouchi, A.1    Bahram, A.2    Gradinaru, C.C.3
  • 23
    • 4143120995 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy studies of peptide and protein binding to phospholipid vesicles
    • [23] Rusu, L., et al. Fluorescence correlation spectroscopy studies of peptide and protein binding to phospholipid vesicles. Biophys. J. 87:2 (2004), 1044–1053.
    • (2004) Biophys. J. , vol.87 , Issue.2 , pp. 1044-1053
    • Rusu, L.1
  • 24
    • 33744788870 scopus 로고    scopus 로고
    • Quantification of α-synuclein binding to lipid vesicles using fluorescence correlation spectroscopy
    • [24] Rhoades, E., et al. Quantification of α-synuclein binding to lipid vesicles using fluorescence correlation spectroscopy. Biophys. J. 90:12 (2006), 4692–4700.
    • (2006) Biophys. J. , vol.90 , Issue.12 , pp. 4692-4700
    • Rhoades, E.1
  • 25
    • 25444471284 scopus 로고    scopus 로고
    • Investigation of a novel artificial antimicrobial peptide by fluorescence correlation spectroscopy: an amphipathic cationic pattern is sufficient for selective binding to bacterial type membranes and antimicrobial activity
    • [25] Yu, L., et al. Investigation of a novel artificial antimicrobial peptide by fluorescence correlation spectroscopy: an amphipathic cationic pattern is sufficient for selective binding to bacterial type membranes and antimicrobial activity. Biochim. Biophys. Acta Biomembr. 1716:1 (2005), 29–39.
    • (2005) Biochim. Biophys. Acta Biomembr. , vol.1716 , Issue.1 , pp. 29-39
    • Yu, L.1
  • 26
    • 77953004116 scopus 로고    scopus 로고
    • The role of the lipid bilayer in tau aggregation
    • [26] Elbaum-Garfinkle, S., Ramlall, T., Rhoades, E., The role of the lipid bilayer in tau aggregation. Biophys. J. 98:11 (2010), 2722–2730.
    • (2010) Biophys. J. , vol.98 , Issue.11 , pp. 2722-2730
    • Elbaum-Garfinkle, S.1    Ramlall, T.2    Rhoades, E.3
  • 27
    • 4244120872 scopus 로고
    • Microdetermination of phosphorus
    • [27] Chen, P. Jr., Toribara, T.t., Warner, H., Microdetermination of phosphorus. Anal. Chem. 28:11 (1956), 1756–1758.
    • (1956) Anal. Chem. , vol.28 , Issue.11 , pp. 1756-1758
    • Chen, P.1    Toribara, T.T.2    Warner, H.3
  • 28
    • 0000154206 scopus 로고
    • The colorimetric determination of phosphorus
    • [28] Fiske, C.H., Subbarow, Y., The colorimetric determination of phosphorus. J. Biol. Chem. 66:2 (1925), 375–400.
    • (1925) J. Biol. Chem. , vol.66 , Issue.2 , pp. 375-400
    • Fiske, C.H.1    Subbarow, Y.2
  • 29
    • 0029087580 scopus 로고
    • Mechanisms of liposome formation
    • [29] Lasic, D.D., Mechanisms of liposome formation. J. Liposome Res. 5:3 (1995), 431–441.
    • (1995) J. Liposome Res. , vol.5 , Issue.3 , pp. 431-441
    • Lasic, D.D.1
  • 30
    • 79959860214 scopus 로고    scopus 로고
    • Artificially induced protein–membrane anchorage with cholesterol-based recognition agents as a new therapeutic concept
    • [30] Avadisian, M., et al. Artificially induced protein–membrane anchorage with cholesterol-based recognition agents as a new therapeutic concept. Angew. Chem. Int. Ed. 50:28 (2011), 6248–6253.
    • (2011) Angew. Chem. Int. Ed. , vol.50 , Issue.28 , pp. 6248-6253
    • Avadisian, M.1
  • 31
    • 84987926250 scopus 로고    scopus 로고
    • Single-molecule analysis of the supramolecular organization of the M2 muscarinic receptor and the galphai1 protein
    • [31] Shivnaraine, R.V., et al. Single-molecule analysis of the supramolecular organization of the M2 muscarinic receptor and the galphai1 protein. J. Am. Chem. Soc. 138:36 (2016), 11583–11598.
    • (2016) J. Am. Chem. Soc. , vol.138 , Issue.36 , pp. 11583-11598
    • Shivnaraine, R.V.1
  • 32
    • 78649600626 scopus 로고    scopus 로고
    • Trapping single molecules in liposomes: surface interactions and freeze-thaw effects
    • [32] Liu, B., Mazouchi, A., Gradinaru, C.C., Trapping single molecules in liposomes: surface interactions and freeze-thaw effects. J. Phys. Chem. B 114:46 (2010), 15191–15198.
    • (2010) J. Phys. Chem. B , vol.114 , Issue.46 , pp. 15191-15198
    • Liu, B.1    Mazouchi, A.2    Gradinaru, C.C.3
  • 33
    • 84898957660 scopus 로고    scopus 로고
    • The effect of intrachain electrostatic repulsion on conformational disorder and dynamics of the sic1 protein
    • [33] Liu, B., et al. The effect of intrachain electrostatic repulsion on conformational disorder and dynamics of the sic1 protein. J. Phys. Chem. B 118:15 (2014), 4088–4097.
    • (2014) J. Phys. Chem. B , vol.118 , Issue.15 , pp. 4088-4097
    • Liu, B.1
  • 34
    • 84963542414 scopus 로고    scopus 로고
    • Conformations of a metastable SH3 domain characterized by smFRET and an excluded-volume polymer model
    • [34] Mazouchi, A., et al. Conformations of a metastable SH3 domain characterized by smFRET and an excluded-volume polymer model. Biophys. J. 110:7 (2016), 1510–1522.
    • (2016) Biophys. J. , vol.110 , Issue.7 , pp. 1510-1522
    • Mazouchi, A.1
  • 35
    • 84924370371 scopus 로고    scopus 로고
    • Single lipid bilayer deposition on polymer surfaces using bicelles
    • [35] Saleem, Q., et al. Single lipid bilayer deposition on polymer surfaces using bicelles. Biomacromolecules 16:3 (2015), 1032–1039.
    • (2015) Biomacromolecules , vol.16 , Issue.3 , pp. 1032-1039
    • Saleem, Q.1
  • 36
    • 0039025943 scopus 로고
    • Fluorescence correlation spectroscopy of triplet states in solution: a theoretical and experimental study
    • [36] Widengren, J., Mets, U., Rigler, R., Fluorescence correlation spectroscopy of triplet states in solution: a theoretical and experimental study. J. Phys. Chem. 99:36 (1995), 13368–13379.
    • (1995) J. Phys. Chem. , vol.99 , Issue.36 , pp. 13368-13379
    • Widengren, J.1    Mets, U.2    Rigler, R.3
  • 37
    • 84859899534 scopus 로고    scopus 로고
    • Photophysics of fluorescent probes for single-molecule biophysics and super-resolution imaging
    • [37] Ha, T., Tinnefeld, P., Photophysics of fluorescent probes for single-molecule biophysics and super-resolution imaging. Annu. Rev. Phys. Chem. 63 (2012), 595–617.
    • (2012) Annu. Rev. Phys. Chem. , vol.63 , pp. 595-617
    • Ha, T.1    Tinnefeld, P.2
  • 38
    • 0028464119 scopus 로고
    • Computer automated log P calculations based on an extended group contribution approach
    • [38] Klopman, G., et al. Computer automated log P calculations based on an extended group contribution approach. J. Chem. Inf. Comput. Sci. 34:4 (1994), 752–781.
    • (1994) J. Chem. Inf. Comput. Sci. , vol.34 , Issue.4 , pp. 752-781
    • Klopman, G.1
  • 39
    • 0032321726 scopus 로고    scopus 로고
    • Energetics of peptide–bilayer interactions
    • [39] White, S.H., Wimley, W.C., Ladokhin, A.S., Energetics of peptide–bilayer interactions. Methods Enzymol. 295 (1998), 62–87.
    • (1998) Methods Enzymol. , vol.295 , pp. 62-87
    • White, S.H.1    Wimley, W.C.2    Ladokhin, A.S.3
  • 40
    • 33845962369 scopus 로고    scopus 로고
    • A versatile method for determining the molar ligand-membrane partition coefficient
    • [40] Parry, M.J., et al. A versatile method for determining the molar ligand-membrane partition coefficient. J. Fluoresc. 17:1 (2007), 97–103.
    • (2007) J. Fluoresc. , vol.17 , Issue.1 , pp. 97-103
    • Parry, M.J.1
  • 41
    • 0030876951 scopus 로고    scopus 로고
    • Phosphatidylcholine acyl unsaturation modulates the decrease in interfacial elasticity induced by cholesterol
    • [41] Smaby, J.M., et al. Phosphatidylcholine acyl unsaturation modulates the decrease in interfacial elasticity induced by cholesterol. Biophys. J., 73(3), 1997, 1492.
    • (1997) Biophys. J. , vol.73 , Issue.3 , pp. 1492
    • Smaby, J.M.1
  • 42
    • 0032823058 scopus 로고    scopus 로고
    • Alexa dyes, a series of new fluorescent dyes that yield exceptionally bright, photostable conjugates
    • [42] Panchuk-Voloshina, N., et al. Alexa dyes, a series of new fluorescent dyes that yield exceptionally bright, photostable conjugates. J. Histochem. Cytochem. 47:9 (1999), 1179–1188.
    • (1999) J. Histochem. Cytochem. , vol.47 , Issue.9 , pp. 1179-1188
    • Panchuk-Voloshina, N.1
  • 43
    • 0026334736 scopus 로고
    • Partition coefficients of fluorescent probes with phospholipid membranes
    • [43] Huang, Z., Haugland, R.P., Partition coefficients of fluorescent probes with phospholipid membranes. Biochem. Biophys. Res. Commun. 181:1 (1991), 166–171.
    • (1991) Biochem. Biophys. Res. Commun. , vol.181 , Issue.1 , pp. 166-171
    • Huang, Z.1    Haugland, R.P.2
  • 44
    • 0036777641 scopus 로고    scopus 로고
    • Envelope disorder of Escherichia coli cells lacking phosphatidylglycerol
    • [44] Suzuki, M., Hara, H., Matsumoto, K., Envelope disorder of Escherichia coli cells lacking phosphatidylglycerol. J. Bacteriol. 184:19 (2002), 5418–5425.
    • (2002) J. Bacteriol. , vol.184 , Issue.19 , pp. 5418-5425
    • Suzuki, M.1    Hara, H.2    Matsumoto, K.3
  • 45
    • 84885006979 scopus 로고    scopus 로고
    • Phosphatidylserine-mediated cellular signaling
    • Springer
    • [45] Kay, J.G., Grinstein, S., Phosphatidylserine-mediated cellular signaling. Lipid-mediated Protein Signaling, 2013, Springer, 177–193.
    • (2013) Lipid-mediated Protein Signaling , pp. 177-193
    • Kay, J.G.1    Grinstein, S.2
  • 46
    • 0019878604 scopus 로고
    • Hexagonal phases in phospholipids with saturated chains: phosphatidylethanolamines and phosphatidic acids
    • [46] Harlos, K., Eibl, H., Hexagonal phases in phospholipids with saturated chains: phosphatidylethanolamines and phosphatidic acids. Biochemistry 20:10 (1981), 2888–2892.
    • (1981) Biochemistry , vol.20 , Issue.10 , pp. 2888-2892
    • Harlos, K.1    Eibl, H.2
  • 47
    • 53049096504 scopus 로고    scopus 로고
    • Examining the contributions of lipid shape and headgroup charge on bilayer behavior
    • [47] Dickey, A., Faller, R., Examining the contributions of lipid shape and headgroup charge on bilayer behavior. Biophys. J. 95:6 (2008), 2636–2646.
    • (2008) Biophys. J. , vol.95 , Issue.6 , pp. 2636-2646
    • Dickey, A.1    Faller, R.2
  • 48
    • 68149100633 scopus 로고    scopus 로고
    • Membrane Structural Biology: With Biochemical and Biophysical Foundations
    • Cambridge University Press
    • [48] Luckey, M., Membrane Structural Biology: With Biochemical and Biophysical Foundations. 2014, Cambridge University Press.
    • (2014)
    • Luckey, M.1
  • 49
    • 79960203369 scopus 로고    scopus 로고
    • Effect of preparation method and cholesterol on drug encapsulation studies by phospholipid liposomes
    • [49] Cagdas, F.M., et al. Effect of preparation method and cholesterol on drug encapsulation studies by phospholipid liposomes. Pharm. Dev. Technol. 16:4 (2011), 408–414.
    • (2011) Pharm. Dev. Technol. , vol.16 , Issue.4 , pp. 408-414
    • Cagdas, F.M.1
  • 50
    • 77954422006 scopus 로고    scopus 로고
    • Development of a liposomal nanodelivery system for nevirapine
    • [50] Ramana, L.N., et al. Development of a liposomal nanodelivery system for nevirapine. J. Biomed. Sci., 17(1), 2010, 1.
    • (2010) J. Biomed. Sci. , vol.17 , Issue.1 , pp. 1
    • Ramana, L.N.1
  • 51
    • 33750246866 scopus 로고    scopus 로고
    • Phase behavior of lipid mixtures
    • [51] Feigenson, G.W., Phase behavior of lipid mixtures. Nat. Chem. Biol. 2:11 (2006), 560–563.
    • (2006) Nat. Chem. Biol. , vol.2 , Issue.11 , pp. 560-563
    • Feigenson, G.W.1
  • 52
    • 0024544477 scopus 로고
    • Calorimetric studies of the effects of cholesterol on the phase transition of C (18): C (10) phosphatidylcholine
    • [52] Chong, P., Choate, D., Calorimetric studies of the effects of cholesterol on the phase transition of C (18): C (10) phosphatidylcholine. Biophys. J., 55(3), 1989, 551.
    • (1989) Biophys. J. , vol.55 , Issue.3 , pp. 551
    • Chong, P.1    Choate, D.2
  • 53
    • 18944407057 scopus 로고    scopus 로고
    • Changes in the morphology of cell-size liposomes in the presence of cholesterol: formation of neuron-like tubes and liposome networks
    • [53] Shin-ichiro, M.N., et al. Changes in the morphology of cell-size liposomes in the presence of cholesterol: formation of neuron-like tubes and liposome networks. Biochim. Biophys. Acta Biomembr. 1669:2 (2005), 164–169.
    • (2005) Biochim. Biophys. Acta Biomembr. , vol.1669 , Issue.2 , pp. 164-169
    • Shin-ichiro, M.N.1
  • 54
    • 0033029569 scopus 로고    scopus 로고
    • Maximum solubility of cholesterol in phosphatidylcholine and phosphatidylethanolamine bilayers
    • [54] Huang, J., Buboltz, J.T., Feigenson, G.W., Maximum solubility of cholesterol in phosphatidylcholine and phosphatidylethanolamine bilayers. Biochim. Biophys. Acta Biomembr. 1417:1 (1999), 89–100.
    • (1999) Biochim. Biophys. Acta Biomembr. , vol.1417 , Issue.1 , pp. 89-100
    • Huang, J.1    Buboltz, J.T.2    Feigenson, G.W.3
  • 55
    • 80155134165 scopus 로고    scopus 로고
    • Fluorescence anisotropy based single liposome assay to measure molecule–membrane interactions
    • [55] Ehrlich, N., Christensen, A.L., Stamou, D., Fluorescence anisotropy based single liposome assay to measure molecule–membrane interactions. Anal. Chem. 83:21 (2011), 8169–8176.
    • (2011) Anal. Chem. , vol.83 , Issue.21 , pp. 8169-8176
    • Ehrlich, N.1    Christensen, A.L.2    Stamou, D.3
  • 56
    • 70349338893 scopus 로고    scopus 로고
    • A photostable, pH-invariant fluorescein derivative for single-molecule microscopy
    • [56] Liu, B., et al. A photostable, pH-invariant fluorescein derivative for single-molecule microscopy. J. Fluoresc. 19:5 (2009), 915–920.
    • (2009) J. Fluoresc. , vol.19 , Issue.5 , pp. 915-920
    • Liu, B.1
  • 57
    • 0019315497 scopus 로고
    • Spectrin-phospholipid interaction: a monolayer study
    • [57] Mombers, C., et al. Spectrin-phospholipid interaction: a monolayer study. Biochim. Biophys. Acta Biomembr. 603:1 (1980), 52–62.
    • (1980) Biochim. Biophys. Acta Biomembr. , vol.603 , Issue.1 , pp. 52-62
    • Mombers, C.1
  • 58
    • 71749093279 scopus 로고    scopus 로고
    • Structural and thermodynamic determinants of chain-melting transition temperatures for phospholipid and glycolipids membranes
    • [58] Marsh, D., Structural and thermodynamic determinants of chain-melting transition temperatures for phospholipid and glycolipids membranes. Biochim. Biophys. Acta Biomembr. 1798:1 (2010), 40–51.
    • (2010) Biochim. Biophys. Acta Biomembr. , vol.1798 , Issue.1 , pp. 40-51
    • Marsh, D.1
  • 59
    • 4444355183 scopus 로고    scopus 로고
    • In situ thermal denaturation of proteins in dunning AT-1 prostate cancer cells: implication for hyperthermic cell injury
    • [59] He, X., et al. In situ thermal denaturation of proteins in dunning AT-1 prostate cancer cells: implication for hyperthermic cell injury. Ann. Biomed. Eng. 32:10 (2004), 1384–1398.
    • (2004) Ann. Biomed. Eng. , vol.32 , Issue.10 , pp. 1384-1398
    • He, X.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.