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Volumn 226, Issue , 2013, Pages 35-44

Using spin-label W-band EPR to study membrane fluidity profiles in samples of small volume

Author keywords

Cholesterol; Membrane fluidity; Saturation recovery; Spin label; Spin lattice relaxation rate; Spin lattice relaxation time; W band

Indexed keywords

MEMBRANE FLUIDITY; SATURATION-RECOVERY; SPIN LABEL; SPIN LATTICE RELAXATION RATES; W-BAND;

EID: 84870170457     PISSN: 10907807     EISSN: 10960856     Source Type: Journal    
DOI: 10.1016/j.jmr.2012.11.001     Document Type: Article
Times cited : (32)

References (65)
  • 3
    • 84944004932 scopus 로고
    • Spin-label saturation-recovery electron spin resonance measurements of oxygen transport in membranes
    • J.J. Yin, and J.S. Hyde Spin-label saturation-recovery electron spin resonance measurements of oxygen transport in membranes Z. Phys. Chem. 153 1987 57 65
    • (1987) Z. Phys. Chem. , vol.153 , pp. 57-65
    • Yin, J.J.1    Hyde, J.S.2
  • 4
    • 0019874035 scopus 로고
    • The diffusion-concentration product of oxygen in lipid bilayers using the spin-label T1 method
    • W.K. Subczynski, and J.S. Hyde The diffusion-concentration product of oxygen in lipid bilayers using the spin-label T1 method Biochim. Biophys. Acta 643 1981 283 291
    • (1981) Biochim. Biophys. Acta , vol.643 , pp. 283-291
    • Subczynski, W.K.1    Hyde, J.S.2
  • 5
    • 0024787356 scopus 로고
    • Conformation of spin-labeled melittin at membrane surfaces investigated by pulse saturation recovery and continuous wave power saturation electron paramagnetic resonance
    • C. Altenbach, W. Froncisz, J.S. Hyde, and W.L. Hubbell Conformation of spin-labeled melittin at membrane surfaces investigated by pulse saturation recovery and continuous wave power saturation electron paramagnetic resonance Biophys. J. 56 1989 1183 1191 (Pubitemid 20017633)
    • (1989) Biophysical Journal , vol.56 , Issue.6 , pp. 1183-1191
    • Altenbach, C.1    Froncisz, W.2    Hyde, J.S.3    Hubbell, W.L.4
  • 7
    • 0009708466 scopus 로고
    • Dependence of the multiquantum EPR signal on the spin lattice relaxation time. Effect of oxygen in spin-label membranes
    • H.S. McHaourab, and J.S. Hyde Dependence of the multiquantum EPR signal on the spin lattice relaxation time. Effect of oxygen in spin-label membranes J. Magn. Reson. B 101 1993 178 184
    • (1993) J. Magn. Reson. B , vol.101 , pp. 178-184
    • McHaourab, H.S.1    Hyde, J.S.2
  • 8
    • 33749166139 scopus 로고    scopus 로고
    • S.S. Eaton, G.R. Eaton, K.M. Salikhov (Eds.) World Scientific Publishing
    • J.S. Hyde, Multiquantum EPR, in: S.S. Eaton, G.R. Eaton, K.M. Salikhov (Eds.), Foundatins of Modern EPR, World Scientific Publishing, 1998, pp. 741-757.
    • (1998) Foundatins of Modern EPR , pp. 741-757
    • Hyde, J.S.1    Multiquantum, E.P.R.2
  • 9
    • 35448961949 scopus 로고    scopus 로고
    • Methods and applications of site-directed spin labeling EPR spectroscopy
    • C.S. Klug, and J.B. Feix Methods and applications of site-directed spin labeling EPR spectroscopy Methods Cell Biol. 84 2008 617 658
    • (2008) Methods Cell Biol. , vol.84 , pp. 617-658
    • Klug, C.S.1    Feix, J.B.2
  • 10
    • 0025006656 scopus 로고
    • Mapping of collision frequencies for stearic acid spin labels by saturation-recovery electron paramagnetic resonance
    • J.J. Yin, J.B. Feix, and J.S. Hyde Mapping of collision frequencies for stearic acid spin labels by saturation-recovery electron paramagnetic resonance Biophys. J. 58 1990 713 720 (Pubitemid 20312928)
    • (1990) Biophysical Journal , vol.58 , Issue.3 , pp. 713-720
    • Yin, J.-J.1    Feix, J.B.2    Hyde, J.S.3
  • 11
    • 77649228493 scopus 로고    scopus 로고
    • Studying lipid organization in biological membranes using liposomes and EPR spin labeling
    • W.K. Subczynski, M. Raguz, and J. Widomska Studying lipid organization in biological membranes using liposomes and EPR spin labeling Methods Mol. Biol. 606 2010 247 269
    • (2010) Methods Mol. Biol. , vol.606 , pp. 247-269
    • Subczynski, W.K.1    Raguz, M.2    Widomska, J.3
  • 12
    • 84855404181 scopus 로고    scopus 로고
    • Spin-label saturation-recovery EPR at W-band: Applications to eye lens lipid membranes
    • L. Mainali, M. Raguz, T.G. Camenisch, J.S. Hyde, and W.K. Subczynski Spin-label saturation-recovery EPR at W-band: applications to eye lens lipid membranes J. Magn. Reson. 212 2011 86 94
    • (2011) J. Magn. Reson. , vol.212 , pp. 86-94
    • Mainali, L.1    Raguz, M.2    Camenisch, T.G.3    Hyde, J.S.4    Subczynski, W.K.5
  • 13
    • 84860390260 scopus 로고    scopus 로고
    • Membrane fluidity profiles as deduced by saturation-recovery EPR measurements of spin-lattice relaxation times of spin labels
    • L. Mainali, J.B. Feix, J.S. Hyde, and W.K. Subczynski Membrane fluidity profiles as deduced by saturation-recovery EPR measurements of spin-lattice relaxation times of spin labels J. Magn. Reson. 212 2011 418 425
    • (2011) J. Magn. Reson. , vol.212 , pp. 418-425
    • Mainali, L.1    Feix, J.B.2    Hyde, J.S.3    Subczynski, W.K.4
  • 18
    • 0037429658 scopus 로고    scopus 로고
    • Dynamics of raft molecules in the cell and artificial membranes: Approaches by pulse EPR spin labeling and single molecule optical microscopy
    • DOI 10.1016/S0005-2736(03)00021-X
    • W.K. Subczynski, and A. Kusumi Dynamics of raft molecules in the cell and artificial membranes: approaches by pulse EPR spin labeling and single molecule optical microscopy Biochim. Biophys. Acta 1610 2003 231 243 (Pubitemid 36324467)
    • (2003) Biochimica et Biophysica Acta - Biomembranes , vol.1610 , Issue.2 , pp. 231-243
    • Subczynski, W.K.1    Kusumi, A.2
  • 19
    • 38949101213 scopus 로고    scopus 로고
    • Saturation-recovery electron paramagnetic resonance discrimination by oxygen transport (DOT) method for characterizing membrane domains
    • Lipid Rafts Humana Press, Totowa
    • W.K. Subczynski, J. Widomska, A. Wisniewska, A. Kusumi, Saturation-recovery electron paramagnetic resonance discrimination by oxygen transport (DOT) method for characterizing membrane domains, in: Methods in Molecular Biology, Lipid Rafts Humana Press, Totowa, 2007, pp. 143-157.
    • (2007) Methods in Molecular Biology , pp. 143-157
    • Subczynski, W.K.1    Widomska, J.2    Wisniewska, A.3    Kusumi, A.4
  • 20
    • 33847770910 scopus 로고    scopus 로고
    • Three-dimensional dynamic structure of the liquid-ordered domain in lipid membranes as examined by pulse-EPR oxygen probing
    • DOI 10.1529/biophysj.106.097568
    • W.K. Subczynski, A. Wisniewska, J.S. Hyde, and A. Kusumi Three-dimensional dynamic structure of the liquid-ordered domain in lipid membranes as examined by pulse-EPR oxygen probing Biophys. J. 92 2007 1573 1584 (Pubitemid 46393468)
    • (2007) Biophysical Journal , vol.92 , Issue.5 , pp. 1573-1584
    • Subczynski, W.K.1    Wisniewska, A.2    Hyde, J.S.3    Kusumi, A.4
  • 21
    • 80052432682 scopus 로고    scopus 로고
    • Phase-separation and domain-formation in cholesterol-sphingomyelin mixture: Pulse-EPR oxygen probing
    • L. Mainali, M. Raguz, and W.K. Subczynski Phase-separation and domain-formation in cholesterol-sphingomyelin mixture: pulse-EPR oxygen probing Biophys. J. 101 2011 837 846
    • (2011) Biophys. J. , vol.101 , pp. 837-846
    • Mainali, L.1    Raguz, M.2    Subczynski, W.K.3
  • 22
    • 84857366847 scopus 로고    scopus 로고
    • Phases and domains in sphingomyelin-cholesterol membranes: Structure and properties using EPR spin-labeling methods
    • L. Mainali, M. Raguz, and W.K. Subczynski Phases and domains in sphingomyelin-cholesterol membranes: structure and properties using EPR spin-labeling methods Eur. Biophys. J. 41 2012 147 159
    • (2012) Eur. Biophys. J. , vol.41 , pp. 147-159
    • Mainali, L.1    Raguz, M.2    Subczynski, W.K.3
  • 23
    • 79751538528 scopus 로고
    • The immiscible cholesterol bilayer domain exists as an integral part of phospholipid bilayer membranes
    • M. Raguz, L. Mainali, J. Widomska, and W.K. Subczynski The immiscible cholesterol bilayer domain exists as an integral part of phospholipid bilayer membranes Biochim. Biophys. Acta 2011 1808 1072 1080
    • (1808) Biochim. Biophys. Acta , vol.2011 , pp. 1072-1080
    • Raguz, M.1    Mainali, L.2    Widomska, J.3    Subczynski, W.K.4
  • 24
    • 80255137179 scopus 로고    scopus 로고
    • Using spin-label electron paramagnetic resonance (EPR) to discriminate and characterize the cholesterol bilayer domain
    • M. Raguz, L. Mainali, J. Widomska, and W.K. Subczynski Using spin-label electron paramagnetic resonance (EPR) to discriminate and characterize the cholesterol bilayer domain Chem. Phys. Lipids 164 2011 819 829
    • (2011) Chem. Phys. Lipids , vol.164 , pp. 819-829
    • Raguz, M.1    Mainali, L.2    Widomska, J.3    Subczynski, W.K.4
  • 25
    • 0028341889 scopus 로고
    • Hydrophobic barriers of lipid bilayer membranes formed by reduction of water penetration by alkyl chain unsaturation and cholesterol
    • DOI 10.1021/bi00190a022
    • W.K. Subczynski, A. Wisniewska, J.-J. Yin, J.S. Hyde, and A. Kusumi Hydrophobic barriers of lipid bilayer membranes formed by reduction of water penetration by alkyl chain unsaturation and cholesterol Biochemistry 33 1994 7670 7681 (Pubitemid 24230593)
    • (1994) Biochemistry , vol.33 , Issue.24 , pp. 7670-7681
    • Subczynski, W.K.1    Wisniewska, A.2    Yin, J.-J.3    Hyde, J.S.4    Kusumi, A.5
  • 26
    • 0011841986 scopus 로고
    • ESR and NMR studies of lipid-protein interactions in membranes
    • L.J. Berliner, J. Reuben (Eds.) Plenum Press, New York
    • P.F. Devaux, ESR and NMR studies of lipid-protein interactions in membranes, in: L.J. Berliner, J. Reuben (Eds.), Biological Magnetic Resonance, Plenum Press, New York, 1983, pp. 183-299.
    • (1983) Biological Magnetic Resonance , pp. 183-299
    • Devaux, P.F.1
  • 28
    • 0345697981 scopus 로고
    • ESR line width in solution. II. Analysis of spin-rotational relaxation data
    • P.W. Atkins, and D. Kivelson ESR line width in solution. II. Analysis of spin-rotational relaxation data J. Chem. Phys. 44 1966 169 174
    • (1966) J. Chem. Phys. , vol.44 , pp. 169-174
    • Atkins, P.W.1    Kivelson, D.2
  • 29
    • 0028345025 scopus 로고
    • Molecular dynamics in liquids: Spin-lattice relaxation of nitroxide spin labels
    • B.H. Robinson, D.A. Haas, and C. Mailer Molecular dynamics in liquids: spin-lattice relaxation of nitroxide spin labels Science 263 1994 490 493 (New Yark, NY) (Pubitemid 24082747)
    • (1994) Science , vol.263 , Issue.5146 , pp. 490-493
    • Robinson, B.H.1    Haas, D.A.2    Mailer, C.3
  • 30
    • 19944417905 scopus 로고    scopus 로고
    • Explanation of spin-lattice relaxation rates of spin labels obtained with multifrequency saturation recovery EPR
    • DOI 10.1021/jp044671l
    • C. Mailer, R.D. Nielsen, and B.H. Robinson Explanation of spin-lattice relaxation rates of spin labels obtained with multifrequency saturation recovery EPR J. Phys. Chem. A 109 2005 4049 4061 (Pubitemid 40750859)
    • (2005) Journal of Physical Chemistry A , vol.109 , Issue.18 , pp. 4049-4061
    • Mailer, C.1    Nielsen, R.D.2    Robinson, B.H.3
  • 31
    • 0001867405 scopus 로고
    • Calculating slow motional magnetic resonance spectra. A user's guide
    • L.J. Berliner, J. Reuben, Plenum New York
    • D.J. Schneider, and J.H. Freed Calculating slow motional magnetic resonance spectra. A user's guide L.J. Berliner, J. Reuben, Spin Labeling: Theory and Application 1989 Plenum New York 1 76
    • (1989) Spin Labeling: Theory and Application , pp. 1-76
    • Schneider, D.J.1    Freed, J.H.2
  • 32
    • 33845470784 scopus 로고
    • Analysis of slow-motional electron spin resonance spectra in smectic phases in terms of molecular configuration, intermolecular interactions, and dynamics
    • E. Meirovitch, and J.H. Freed Analysis of slow-motional electron spin resonance spectra in smectic phases in terms of molecular configuration, intermolecular interactions, and dynamics J. Phys. Chem. 88 1984 4995 5004
    • (1984) J. Phys. Chem. , vol.88 , pp. 4995-5004
    • Meirovitch, E.1    Freed, J.H.2
  • 34
    • 0000326938 scopus 로고    scopus 로고
    • Nonlinear-least-squares analysis of slow-motion EPR spectra in one and two dimensions using a modified levenberg-marquardt algorithm
    • D.E. Budil, S. Lee, S. Saxena, and J.H. Freed Nonlinear-least-squares analysis of slow-motion EPR spectra in one and two dimensions using a modified Levenberg-Marquardt Algorithm J. Magn. Reson., Ser. A 120 1996 155 189 (Pubitemid 126751752)
    • (1996) Journal of Magnetic Resonance - Series A , vol.120 , Issue.2 , pp. 155-189
    • Budil, D.E.1    Sanghyuk, L.2    Saxena, S.3    Freed, J.H.4
  • 35
    • 0000133712 scopus 로고
    • Electron-spin relaxation and ordering in smectic and supercooled nematic liquid crystals
    • E. Meirovitch, D. Igner, G. More, and J.H. Freed Electron-spin relaxation and ordering in smectic and supercooled nematic liquid crystals J. Chem. Phys. 77 1982 3915 3938
    • (1982) J. Chem. Phys. , vol.77 , pp. 3915-3938
    • Meirovitch, E.1    Igner, D.2    More, G.3    Freed, J.H.4
  • 36
    • 27644561796 scopus 로고    scopus 로고
    • High-field spin-label EPR of lipid membranes
    • DOI 10.1002/mrc.1680, High-Field EPR in Biology, Chemistry and Physics
    • D. Marsh, D. Kurad, V.A. Livshits, High-field spin-label EPR of lipid membranes, Magn. Reson. Chem., 43 Spec no. (2005) S20-S25. (Pubitemid 41578498)
    • (2005) Magnetic Resonance in Chemistry , vol.43 , Issue.SPEC. ISS.
    • Marsh, D.1    Kurad, D.2    Livshits, V.A.3
  • 37
    • 3142687524 scopus 로고    scopus 로고
    • Simulation studies on high-field EPR spectra of lipid spin labels in cholesterol-containing membranes
    • V.A. Livshits, D. Kurad, and D. Marsh Simulation studies on high-field EPR spectra of lipid spin labels in cholesterol-containing membranes J. Phys. Chem. B 108 2004 9403 9411
    • (2004) J. Phys. Chem. B , vol.108 , pp. 9403-9411
    • Livshits, V.A.1    Kurad, D.2    Marsh, D.3
  • 38
    • 0001061501 scopus 로고
    • Lipid spin labels in biological membranes
    • L.J. Berliner, Academic Press New York
    • O.H. Griffith, and P.C. Jost Lipid spin labels in biological membranes L.J. Berliner, Spin Labeling Theory and Applications 1976 Academic Press New York 453 523
    • (1976) Spin Labeling Theory and Applications , pp. 453-523
    • Griffith, O.H.1    Jost, P.C.2
  • 39
    • 0344981517 scopus 로고    scopus 로고
    • Hydration, Structure, and Molecular Interactions in the Headgroup Region of Dioleoylphosphatidylcholine Bilayers: An Electron Spin Resonance Study
    • M. Ge, and J.H. Freed Hydration, structure, and molecular interactions in the headgroup region of dioleoylphosphatidylcholine bilayers: an electron spin resonance study Biophys. J. 85 2003 4023 4040 (Pubitemid 37490311)
    • (2003) Biophysical Journal , vol.85 , Issue.6 , pp. 4023-4040
    • Ge, M.1    Freed, J.H.2
  • 40
    • 84859018504 scopus 로고    scopus 로고
    • Dynamics and ordering of lipid spin-labels along the coexistence curve of two membrane phases: An ESR study
    • A.K. Smith, and J.H. Freed Dynamics and ordering of lipid spin-labels along the coexistence curve of two membrane phases: an ESR study Chem. Phys. Lipids 165 2012 348 361
    • (2012) Chem. Phys. Lipids , vol.165 , pp. 348-361
    • Smith, A.K.1    Freed, J.H.2
  • 42
    • 12844268420 scopus 로고    scopus 로고
    • Dynamic molecular structure of DPPC-DLPC-cholesterol ternary lipid system by spin-label electron spin resonance
    • Y.W. Chiang, Y. Shimoyama, G.W. Feigenson, and J.H. Freed Dynamic molecular structure of DPPC-DLPC-cholesterol ternary lipid system by spin-label electron spin resonance Biophys. J. 87 2004 2483 2496
    • (2004) Biophys. J. , vol.87 , pp. 2483-2496
    • Chiang, Y.W.1    Shimoyama, Y.2    Feigenson, G.W.3    Freed, J.H.4
  • 43
    • 0038449652 scopus 로고    scopus 로고
    • Comparative spin label spectra at X-band and W-band
    • L. Berliner (Ed.) Springer, US
    • A. Smirnov, R. Belford, R. Clarkson, Comparative spin label spectra at X-band and W-band, in: L. Berliner (Ed.), Biological Magnetic Resonance, Springer, US, 2002, pp. 83-107.
    • (2002) Biological Magnetic Resonance , pp. 83-107
    • Smirnov, A.1    Belford, R.2    Clarkson, R.3
  • 44
    • 33744797629 scopus 로고    scopus 로고
    • Coexisting domains in the plasma membranes of live cells characterized by spin-label ESR spectroscopy
    • DOI 10.1529/biophysj.105.070839
    • M.J. Swamy, L. Ciani, M. Ge, A.K. Smith, D. Holowka, B. Baird, and J.H. Freed Coexisting domains in the plasma membranes of live cells characterized by spin-label ESR spectroscopy Biophys. J. 90 2006 4452 4465 (Pubitemid 43830891)
    • (2006) Biophysical Journal , vol.90 , Issue.12 , pp. 4452-4465
    • Swamy, M.J.1    Ciani, L.2    Ge, M.3    Smith, A.K.4    Holowka, D.5    Baird, B.6    Freed, J.H.7
  • 45
    • 0041343028 scopus 로고    scopus 로고
    • Ordered and disordered phases coexist in plasma membrane vesicles of RBL-2H3 mast cells. An ESR study
    • M. Ge, A. Gidwani, H.A. Brown, D. Holowka, B. Baird, and J.H. Freed Ordered and disordered phases coexist in plasma membrane vesicles of RBL-2H3 mast cells. An ESR study Biophys. J. 85 2003 1278 1288 (Pubitemid 36909688)
    • (2003) Biophysical Journal , vol.85 , Issue.2 , pp. 1278-1288
    • Ge, M.1    Gidwani, A.2    Brown, H.A.3    Holowka, D.4    Baird, B.5    Freed, J.H.6
  • 46
    • 0022134146 scopus 로고
    • Electron spin resonance and electron-spin-echo study of oriented multilayers of L alpha-dipalmitoylphosphatidylcholine water systems
    • L. Kar, E. Ney-Igner, and J.H. Freed Electron spin resonance and electron-spin-echo study of oriented multilayers of L alpha- dipalmitoylphosphatidylcholine water systems Biophys. J. 48 1985 569 595
    • (1985) Biophys. J. , vol.48 , pp. 569-595
    • Kar, L.1    Ney-Igner, E.2    Freed, J.H.3
  • 48
    • 0015241658 scopus 로고
    • Molecular motion in spin-labeled phospholipids and membranes
    • W.L. Hubbell, and H.M. McConnell Molecular motion in spin-labeled phospholipids and membranes J. Am. Chem. Soc. 93 1971 314 326
    • (1971) J. Am. Chem. Soc. , vol.93 , pp. 314-326
    • Hubbell, W.L.1    McConnell, H.M.2
  • 49
    • 0025241477 scopus 로고
    • Modulation of the orientational order profile of the lipid acyl chain in the L alpha phase
    • M. Lafleur, P.R. Cullis, and M. Bloom Modulation of the orientational order profile of the lipid acyl chain in the L alpha phase Eur. Biophys. J. 19 1990 55 62
    • (1990) Eur. Biophys. J. , vol.19 , pp. 55-62
    • Lafleur, M.1    Cullis, P.R.2    Bloom, M.3
  • 51
    • 58149479521 scopus 로고    scopus 로고
    • Cholesterol containing model membranes studied by multinuclear sold state NMR spectroscopy
    • J.A. Clarke, J.M. Seddon, and R.V. Law Cholesterol containing model membranes studied by multinuclear sold state NMR spectroscopy Soft Matter 5 2009 369 378
    • (2009) Soft Matter , vol.5 , pp. 369-378
    • Clarke, J.A.1    Seddon, J.M.2    Law, R.V.3
  • 52
    • 0034805275 scopus 로고    scopus 로고
    • Cholesterol effects on the phosphatidylcholine bilayer nonpolar region: A molecular simulation study
    • T. Rog, and M. Pasenkiewicz-Gierula Cholesterol effects on the phosphatidylcholine bilayer nonpolar region: a molecular simulation study Biophys. J. 81 2001 2190 2202 (Pubitemid 32917168)
    • (2001) Biophysical Journal , vol.81 , Issue.4 , pp. 2190-2202
    • Rog, T.1    Pasenkiewicz-Gierula, M.2
  • 54
    • 0017008120 scopus 로고
    • A deuterium nuclear magnetic resonance study of the condensing effect of cholesterol on egg phosphatidylcholine bilayer membranes. I. Perdeuterated fatty acid probes
    • G.W. Stockton, and I.C. Smith A deuterium nuclear magnetic resonance study of the condensing effect of cholesterol on egg phosphatidylcholine bilayer membranes. I. Perdeuterated fatty acid probes Chem. Phys. Lipids 17 1976 251 263
    • (1976) Chem. Phys. Lipids , vol.17 , pp. 251-263
    • Stockton, G.W.1    Smith, I.C.2
  • 55
    • 0024512257 scopus 로고
    • Dynamic imaging of lateral diffusion by electron spin resonance and study of rotational dynamics in model membranes. Effect of cholesterol
    • Y.K. Shin, and J.H. Freed Dynamic imaging of lateral diffusion by electron spin resonance and study of rotational dynamics in model membranes. Effect of cholesterol Biophys. J. 55 1989 537 550 (Pubitemid 19073741)
    • (1989) Biophysical Journal , vol.55 , Issue.3 , pp. 537-550
    • Shin, Y.-K.1    Freed, J.H.2
  • 56
    • 58149473633 scopus 로고    scopus 로고
    • The liquid-ordered phase in membranes
    • P.J. Quinn, and C. Wolf The liquid-ordered phase in membranes Biochim. Biophys. Acta 1788 2009 33 46
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 33-46
    • Quinn, P.J.1    Wolf, C.2
  • 57
    • 34250355206 scopus 로고    scopus 로고
    • The condensing effect of cholesterol in lipid bilayers
    • DOI 10.1529/biophysj.106.099234
    • W.C. Hung, M.T. Lee, F.Y. Chen, and H.W. Huang The condensing effect of cholesterol in lipid bilayers Biophys. J. 92 2007 3960 3967 (Pubitemid 46910582)
    • (2007) Biophysical Journal , vol.92 , Issue.11 , pp. 3960-3967
    • Hung, W.-C.1    Lee, M.-T.2    Chen, F.-Y.3    Huang, H.W.4
  • 58
    • 0024968857 scopus 로고
    • Slow-motion ESR study of order and dynamics in oriented lipid multibilayers: Effects of unsaturation and hydration
    • L.J. Korstanje, E.E. Van Faassen, and Y.K. Levine Slow-motion ESR study of order and dynamics in oriented lipid multibilayers: effects of unsaturation and hydration Biochim. Biophys. Acta 980 1989 225 233
    • (1989) Biochim. Biophys. Acta , vol.980 , pp. 225-233
    • Korstanje, L.J.1    Van Faassen, E.E.2    Levine, Y.K.3
  • 59
    • 0029761813 scopus 로고    scopus 로고
    • Effects of lutein and cholesterol on alkyl chain bending in lipid bilayers: A pulse electron spin resonance spin labeling study
    • J.J. Yin, and W.K. Subczynski Effects of lutein and cholesterol on alkyl chain bending in lipid bilayers: a pulse electron spin resonance spin labeling study Biophys. J. 71 1996 832 839 (Pubitemid 26289166)
    • (1996) Biophysical Journal , vol.71 , Issue.2 , pp. 832-839
    • Yin, J.-J.1    Subczynski, W.K.2
  • 60
    • 84862288169 scopus 로고    scopus 로고
    • Conformational distributions and hydrogen bonding in gel and Frozen lipid bilayers: A high frequency spin-label ESR study
    • B. Dzikovski, D. Tipikin, and J. Freed Conformational distributions and hydrogen bonding in gel and Frozen lipid bilayers: a high frequency spin-label ESR study J. Phys. Chem. B 116 2012 6694 6706
    • (2012) J. Phys. Chem. B , vol.116 , pp. 6694-6706
    • Dzikovski, B.1    Tipikin, D.2    Freed, J.3
  • 61
    • 0023154401 scopus 로고
    • Dynamic fluorescence quenching studies on lipid mobilities in phosphatidylcholine-cholesterol membranes
    • DOI 10.1016/0005-2736(87)90420-2
    • H. Merkle, W.K. Subczynski, and A. Kusumi Dynamic fluorescence quenching studies on lipid mobilities in phosphatidylcholine-cholesterol membranes Biochim. Biophys. Acta 897 1987 238 248 (Pubitemid 17038870)
    • (1987) Biochimica et Biophysica Acta - Biomembranes , vol.897 , Issue.2 , pp. 238-248
    • Merkle, H.1    Subczynski, W.K.2    Kusumi, A.3
  • 62
    • 0035957941 scopus 로고    scopus 로고
    • Evidence for distinct cholesterol domains in fiber cell membranes from cataractous human lenses
    • R.F. Jacob, R.J. Cenedella, and R.P. Mason Evidence for distinct cholesterol domains in fiber cell membranes from cataractous human lenses J. Biol. Chem. 276 2001 13573 13578
    • (2001) J. Biol. Chem. , vol.276 , pp. 13573-13578
    • Jacob, R.F.1    Cenedella, R.J.2    Mason, R.P.3
  • 63
    • 0033615688 scopus 로고    scopus 로고
    • Direct evidence for immiscible cholesterol domains in human ocular lens fiber cell plasma membranes
    • R.F. Jacob, R.J. Cenedella, and R.P. Mason Direct evidence for immiscible cholesterol domains in human ocular lens fiber cell plasma membranes J. Biol. Chem. 274 1999 31613 31618
    • (1999) J. Biol. Chem. , vol.274 , pp. 31613-31618
    • Jacob, R.F.1    Cenedella, R.J.2    Mason, R.P.3
  • 64
    • 0031899062 scopus 로고    scopus 로고
    • Physical effects of cholesterol on arterial smooth muscle membranes: Evidence of immiscible cholesterol domains and alterations in bilayer width during atherogenesis
    • T.N. Tulenko, M. Chen, P.E. Mason, and R.P. Mason Physical effects of cholesterol on arterial smooth muscle membranes: evidence of immiscible cholesterol domains and alterations in bilayer width during atherogenesis J. Lipid Res. 39 1998 947 956 (Pubitemid 28221998)
    • (1998) Journal of Lipid Research , vol.39 , Issue.5 , pp. 947-956
    • Tulenko, T.N.1    Chen, M.2    Mason, P.E.3    Mason, R.P.4
  • 65
    • 0347572922 scopus 로고    scopus 로고
    • Direct evidence for cholesterol crystalline domains in biological membranes: Role in human pathobiology
    • DOI 10.1016/S0005-2736(03)00018-X
    • R. Mason, T.N. Tulenko, and R.F. Jacob Direct evidence for cholesterol crystalline domains in biological membranes: role in human pathobiology Biochim. Biophys. Acta 1610 2003 198 207 (Pubitemid 36324464)
    • (2003) Biochimica et Biophysica Acta - Biomembranes , vol.1610 , Issue.2 , pp. 198-207
    • Mason, R.P.1    Tulenko, T.N.2    Jacob, R.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.