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Volumn 18, Issue , 2013, Pages 81-109

Coupling membrane Elasticity and structure to protein function

Author keywords

Ion channels; Lateral pressure profile; Lipid domains; Lipid protein interactions; Membrane elasticity

Indexed keywords


EID: 84883017286     PISSN: 15544516     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-411515-6.00004-7     Document Type: Chapter
Times cited : (7)

References (124)
  • 3
    • 58149194831 scopus 로고    scopus 로고
    • Phase diagrams and lipid domains in multicomponent lipid bilayer mixtures
    • Feigenson G.W. Phase diagrams and lipid domains in multicomponent lipid bilayer mixtures. Biochim. Biophys. Acta 2009, 1788:47-52.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 47-52
    • Feigenson, G.W.1
  • 4
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood D., Simons K. Lipid rafts as a membrane-organizing principle. Science 2010, 327:46-50.
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 5
    • 0022080948 scopus 로고
    • Intrinsic curvature hypothesis for biomembrane lipid composition: a role for nonbilayer lipids
    • Gruner S.M. Intrinsic curvature hypothesis for biomembrane lipid composition: a role for nonbilayer lipids. Proc. Natl. Acad. Sci. U.S.A. 1985, 82:3665-3669.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 3665-3669
    • Gruner, S.M.1
  • 7
    • 47049098589 scopus 로고    scopus 로고
    • Liposome-based biomembrane mimetic systems: implications for lipid-peptide interactions
    • Elsevier, Amsterdam, A. Leitmannova-Liu (Ed.)
    • Lohner K., Sevcsik E., Pabst G. Liposome-based biomembrane mimetic systems: implications for lipid-peptide interactions. Advances in Planar Lipid Bilayers and Liposomes 2008, vol. 6:103-137. Elsevier, Amsterdam. A. Leitmannova-Liu (Ed.).
    • (2008) Advances in Planar Lipid Bilayers and Liposomes , vol.6 , pp. 103-137
    • Lohner, K.1    Sevcsik, E.2    Pabst, G.3
  • 8
    • 0029957467 scopus 로고    scopus 로고
    • Cloning of monoclonal autoantibodies to epitopes of oxidized lipoproteins from apolipoprotein E-deficient mice. Demonstration of epitopes of oxidized low density lipoprotein in human plasma
    • Palinski W., Horkko S., Miller E., Steinbrecher U.P., Powell H.C., Curtiss L.K., Witztum J.L. Cloning of monoclonal autoantibodies to epitopes of oxidized lipoproteins from apolipoprotein E-deficient mice. Demonstration of epitopes of oxidized low density lipoprotein in human plasma. J. Clin. Invest. 1996, 98:800-814.
    • (1996) J. Clin. Invest. , vol.98 , pp. 800-814
    • Palinski, W.1    Horkko, S.2    Miller, E.3    Steinbrecher, U.P.4    Powell, H.C.5    Curtiss, L.K.6    Witztum, J.L.7
  • 9
    • 21444445056 scopus 로고    scopus 로고
    • A role for oxidized phospholipids in atherosclerosis
    • Berliner J.A., Watson A.D. A role for oxidized phospholipids in atherosclerosis. N. Engl. J. Med. 2005, 353:9-11.
    • (2005) N. Engl. J. Med. , vol.353 , pp. 9-11
    • Berliner, J.A.1    Watson, A.D.2
  • 10
    • 0027261307 scopus 로고
    • Presence of foam cells containing oxidised low density lipoprotein in the synovial membrane from patients with rheumatoid arthritis
    • Winyard P.G., Tatzber F., Esterbauer H., Kus M.L., Blake D.R., Morris C.J. Presence of foam cells containing oxidised low density lipoprotein in the synovial membrane from patients with rheumatoid arthritis. Ann. Rheum. Dis. 1993, 52:677-680.
    • (1993) Ann. Rheum. Dis. , vol.52 , pp. 677-680
    • Winyard, P.G.1    Tatzber, F.2    Esterbauer, H.3    Kus, M.L.4    Blake, D.R.5    Morris, C.J.6
  • 15
    • 39149094259 scopus 로고    scopus 로고
    • Interplay between oxidative stress and immunity in the progression of alcohol-mediated liver injury
    • Vidali M., Stewart S.F., Albano E. Interplay between oxidative stress and immunity in the progression of alcohol-mediated liver injury. Trends Mol. Med. 2008, 14:63-71.
    • (2008) Trends Mol. Med. , vol.14 , pp. 63-71
    • Vidali, M.1    Stewart, S.F.2    Albano, E.3
  • 16
    • 77957054958 scopus 로고
    • Polymorphism of lipid water systems
    • Elsevier, North-Holland, Amsterdam, R. Lipowsky, E. Sackmann (Eds.) Structure and Dynamics of Membranes
    • Seddon J.M., Templer R.H. Polymorphism of lipid water systems. Handbook of Biological Physics 1995, vol. 1:97-160. Elsevier, North-Holland, Amsterdam. R. Lipowsky, E. Sackmann (Eds.).
    • (1995) Handbook of Biological Physics , vol.1 , pp. 97-160
    • Seddon, J.M.1    Templer, R.H.2
  • 17
    • 0001098317 scopus 로고    scopus 로고
    • Lateral pressures in cell membranes: a mechanism for modulation of protein function
    • Cantor R.S. Lateral pressures in cell membranes: a mechanism for modulation of protein function. J. Phys. Chem. B 1997, 101:1723-1725.
    • (1997) J. Phys. Chem. B , vol.101 , pp. 1723-1725
    • Cantor, R.S.1
  • 18
    • 0031027931 scopus 로고    scopus 로고
    • The lateral pressure profile in membranes: a physical mechanism of general anesthesia
    • Cantor R.S. The lateral pressure profile in membranes: a physical mechanism of general anesthesia. Biochemistry 1997, 36:2339-2344.
    • (1997) Biochemistry , vol.36 , pp. 2339-2344
    • Cantor, R.S.1
  • 19
    • 77957046824 scopus 로고
    • Molecular theory of chain packing, elasticity and lipid-protein interaction in lipid bilayers
    • Elsevier, Amsterdam, R. Lipowsky, E. Sackmann (Eds.)
    • Ben Shaul A. Molecular theory of chain packing, elasticity and lipid-protein interaction in lipid bilayers. Handbook of Biological Physics 1995, vol. 1:359-401. Elsevier, Amsterdam. R. Lipowsky, E. Sackmann (Eds.).
    • (1995) Handbook of Biological Physics , vol.1 , pp. 359-401
    • Ben Shaul, A.1
  • 20
    • 77953297286 scopus 로고    scopus 로고
    • Membrane-mediated effect on ion channels induced by the anesthetic drug ketamine
    • Jerabek H., Pabst G., Rappolt M., Stockner T. Membrane-mediated effect on ion channels induced by the anesthetic drug ketamine. J. Am. Chem. Soc. 2010, 132:7990-7997.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 7990-7997
    • Jerabek, H.1    Pabst, G.2    Rappolt, M.3    Stockner, T.4
  • 21
    • 0002780330 scopus 로고
    • Amphiphilic mesophases made of defects
    • North-Holland Publishing, Amsterdam, R. Balian, M. Kleman, J.P. Poirier (Eds.)
    • Helfrich W. Amphiphilic mesophases made of defects. Physics of Defects 1981, 716-755. North-Holland Publishing, Amsterdam. R. Balian, M. Kleman, J.P. Poirier (Eds.).
    • (1981) Physics of Defects , pp. 716-755
    • Helfrich, W.1
  • 22
    • 0001711376 scopus 로고
    • Elastic-moduli for strongly curved monolayers-position of the neutral surface
    • Kozlov M.M., Winterhalter M. Elastic-moduli for strongly curved monolayers-position of the neutral surface. J. Phys. Ii 1991, 1:1077-1084.
    • (1991) J. Phys. Ii , vol.1 , pp. 1077-1084
    • Kozlov, M.M.1    Winterhalter, M.2
  • 24
    • 41149168686 scopus 로고    scopus 로고
    • X-ray structure of a prokaryotic pentameric ligand-gated ion channel
    • Hilf R.J., Dutzler R. X-ray structure of a prokaryotic pentameric ligand-gated ion channel. Nature 2008, 452:375-379.
    • (2008) Nature , vol.452 , pp. 375-379
    • Hilf, R.J.1    Dutzler, R.2
  • 25
    • 58149242730 scopus 로고    scopus 로고
    • Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel
    • Hilf R.J., Dutzler R. Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel. Nature 2009, 457:115-118.
    • (2009) Nature , vol.457 , pp. 115-118
    • Hilf, R.J.1    Dutzler, R.2
  • 26
    • 0032228279 scopus 로고    scopus 로고
    • Sensing isothermal changes in the lateral pressure in model membranes using di-pyrenyl phosphatidylcholine
    • Templer R.H., Castle S.J., Curran A.R., Rumbles G., Klug D.R. Sensing isothermal changes in the lateral pressure in model membranes using di-pyrenyl phosphatidylcholine. Faraday Discuss. 1998, 111:41-53.
    • (1998) Faraday Discuss. , vol.111 , pp. 41-53
    • Templer, R.H.1    Castle, S.J.2    Curran, A.R.3    Rumbles, G.4    Klug, D.R.5
  • 27
    • 0030586178 scopus 로고    scopus 로고
    • NMR investigations of non-lamellar phase promoters in the lamellar phase state
    • Gawrisch K., Holte L.L. NMR investigations of non-lamellar phase promoters in the lamellar phase state. Chem. Phys. Lipids 1996, 81:105-116.
    • (1996) Chem. Phys. Lipids , vol.81 , pp. 105-116
    • Gawrisch, K.1    Holte, L.L.2
  • 28
    • 79955733993 scopus 로고    scopus 로고
    • Lateral pressure profiles in lipid membranes: dependence on molecular composition
    • RSC Publishing, London, M.S. Sansom, P.C. Biggin (Eds.)
    • Ollila O.H., Vattulainen I. Lateral pressure profiles in lipid membranes: dependence on molecular composition. Molecular Simulations and Biomembranes 2010, 26-55. RSC Publishing, London. M.S. Sansom, P.C. Biggin (Eds.).
    • (2010) Molecular Simulations and Biomembranes , pp. 26-55
    • Ollila, O.H.1    Vattulainen, I.2
  • 30
    • 84858764669 scopus 로고    scopus 로고
    • Determining the Gaussian curvature modulus of lipid membranes in simulations
    • Hu M., Briguglio J.J., Deserno M. Determining the Gaussian curvature modulus of lipid membranes in simulations. Biophys. J. 2012, 102:1403-1410.
    • (2012) Biophys. J. , vol.102 , pp. 1403-1410
    • Hu, M.1    Briguglio, J.J.2    Deserno, M.3
  • 31
    • 84873383442 scopus 로고    scopus 로고
    • Inclusion of lateral pressure/curvature stress effects in implicit membrane models
    • Zhan H., Lazaridis T. Inclusion of lateral pressure/curvature stress effects in implicit membrane models. Biophys. J. 2013, 104:643-654.
    • (2013) Biophys. J. , vol.104 , pp. 643-654
    • Zhan, H.1    Lazaridis, T.2
  • 32
    • 84874586270 scopus 로고    scopus 로고
    • How cholesterol tilt modulates the mechanical properties of saturated and unsaturated lipid membranes
    • Khelashvili G., Harries D. How cholesterol tilt modulates the mechanical properties of saturated and unsaturated lipid membranes. J. Phys. Chem. B 2013, 117:2411-2421.
    • (2013) J. Phys. Chem. B , vol.117 , pp. 2411-2421
    • Khelashvili, G.1    Harries, D.2
  • 33
    • 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 1999, 101:45-56.
    • (1999) Chem. Phys. Lipids , vol.101 , pp. 45-56
    • Cantor, R.S.1
  • 35
    • 79959641376 scopus 로고    scopus 로고
    • Protein shape change has a major effect on the gating energy of a mechanosensitive channel
    • Samuli Ollila O.H., Louhivuori M., Marrink S.J., Vattulainen I. Protein shape change has a major effect on the gating energy of a mechanosensitive channel. Biophys. J. 2011, 100:1651-1659.
    • (2011) Biophys. J. , vol.100 , pp. 1651-1659
    • Samuli Ollila, O.H.1    Louhivuori, M.2    Marrink, S.J.3    Vattulainen, I.4
  • 36
  • 37
    • 0004485421 scopus 로고    scopus 로고
    • Liposome phase systems as membrane activity sensors for peptides
    • Springer, Berlin, (Chapter 11), J. Katsaras, T. Gutberlet (Eds.)
    • Laggner P., Lohner K. Liposome phase systems as membrane activity sensors for peptides. Lipid Bilayers: Structure and Interactions, Biological Physics Series 2000, 233-264. Springer, Berlin, (Chapter 11). J. Katsaras, T. Gutberlet (Eds.).
    • (2000) Lipid Bilayers: Structure and Interactions, Biological Physics Series , pp. 233-264
    • Laggner, P.1    Lohner, K.2
  • 38
    • 0034696524 scopus 로고    scopus 로고
    • Tryptophan-anchored transmembrane peptides promote formation of nonlamellar phases in phosphatidylethanolamine model membranes in a mismatch-dependent manner
    • van der Wel P.C., Pott T., Morein S., Greathouse D.V., Koeppe R.E., Killian J.A. Tryptophan-anchored transmembrane peptides promote formation of nonlamellar phases in phosphatidylethanolamine model membranes in a mismatch-dependent manner. Biochemistry 2000, 39:3124-3133.
    • (2000) Biochemistry , vol.39 , pp. 3124-3133
    • van der Wel, P.C.1    Pott, T.2    Morein, S.3    Greathouse, D.V.4    Koeppe, R.E.5    Killian, J.A.6
  • 40
    • 0034713831 scopus 로고    scopus 로고
    • Action of antimicrobial peptides: two-state model
    • Huang H.W. Action of antimicrobial peptides: two-state model. Biochemistry 2000, 39:8347-8352.
    • (2000) Biochemistry , vol.39 , pp. 8347-8352
    • Huang, H.W.1
  • 41
    • 33645705346 scopus 로고
    • Membrane-induced interactions between inclusions
    • Dan N., Pincus P., Safran S.A. Membrane-induced interactions between inclusions. Langmuir 1993, 9:2768-2771.
    • (1993) Langmuir , vol.9 , pp. 2768-2771
    • Dan, N.1    Pincus, P.2    Safran, S.A.3
  • 42
    • 0031679215 scopus 로고    scopus 로고
    • Effect of lipid characteristics on the structure of transmembrane proteins
    • Dan N., Safran S.A. Effect of lipid characteristics on the structure of transmembrane proteins. Biophys. J. 1998, 75:1410-1414.
    • (1998) Biophys. J. , vol.75 , pp. 1410-1414
    • Dan, N.1    Safran, S.A.2
  • 43
    • 0242405501 scopus 로고    scopus 로고
    • Synthetic peptides as models for intrinsic membrane proteins
    • Killian J.A. Synthetic peptides as models for intrinsic membrane proteins. FEBS Lett. 2003, 555:134-138.
    • (2003) FEBS Lett. , vol.555 , pp. 134-138
    • Killian, J.A.1
  • 44
    • 0020486964 scopus 로고
    • Bilayer thickness and enzymatic activity in the mitochondrial cytochrome c oxidase and ATPase complex
    • Montecucco C., Smith G.A., Dabbeni-sala F., Johannsson A., Galante Y.M., Bisson R. Bilayer thickness and enzymatic activity in the mitochondrial cytochrome c oxidase and ATPase complex. FEBS Lett. 1982, 144:145-148.
    • (1982) FEBS Lett. , vol.144 , pp. 145-148
    • Montecucco, C.1    Smith, G.A.2    Dabbeni-sala, F.3    Johannsson, A.4    Galante, Y.M.5    Bisson, R.6
  • 45
    • 0019873916 scopus 로고
    • The effect of bilayer thickness on the activity of (Na+ + K+)-ATPase
    • Johannsson A., Smith G.A., Metcalfe J.C. The effect of bilayer thickness on the activity of (Na+ + K+)-ATPase. Biochim. Biophys. Acta 1981, 641:416-421.
    • (1981) Biochim. Biophys. Acta , vol.641 , pp. 416-421
    • Johannsson, A.1    Smith, G.A.2    Metcalfe, J.C.3
  • 46
    • 0019887787 scopus 로고
    • The effect of bilayer thickness and n-alkanes on the activity of the (Ca2+ + Mg2+)-dependent ATPase of sarcoplasmic reticulum
    • Johannsson A., Keightley C.A., Smith G.A., Richards C.D., Hesketh T.R., Metcalfe J.C. The effect of bilayer thickness and n-alkanes on the activity of the (Ca2+ + Mg2+)-dependent ATPase of sarcoplasmic reticulum. J. Biol. Chem. 1981, 256:1643-1650.
    • (1981) J. Biol. Chem. , vol.256 , pp. 1643-1650
    • Johannsson, A.1    Keightley, C.A.2    Smith, G.A.3    Richards, C.D.4    Hesketh, T.R.5    Metcalfe, J.C.6
  • 47
    • 0022845070 scopus 로고
    • Effects of lipids and long-chain alkyl derivatives on the activity of (Ca2+-Mg2+)-ATPase
    • Froud R.J., East J.M., Jones O.T., Lee A.G. Effects of lipids and long-chain alkyl derivatives on the activity of (Ca2+-Mg2+)-ATPase. Biochemistry 1986, 25:7544-7552.
    • (1986) Biochemistry , vol.25 , pp. 7544-7552
    • Froud, R.J.1    East, J.M.2    Jones, O.T.3    Lee, A.G.4
  • 48
    • 0036725152 scopus 로고    scopus 로고
    • Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating
    • Perozo E., Kloda A., Cortes D.M., Martinac B. Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating. Nat. Struct. Biol. 2002, 9:696-703.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 696-703
    • Perozo, E.1    Kloda, A.2    Cortes, D.M.3    Martinac, B.4
  • 49
    • 0023018907 scopus 로고
    • Deformation free energy of bilayer membrane and its effect on gramicidin channel lifetime
    • Huang H.W. Deformation free energy of bilayer membrane and its effect on gramicidin channel lifetime. Biophys. J. 1986, 50:1061-1070.
    • (1986) Biophys. J. , vol.50 , pp. 1061-1070
    • Huang, H.W.1
  • 50
    • 0033737385 scopus 로고    scopus 로고
    • Inclusion-induced bilayer deformations: effects of monolayer equilibrium curvature
    • Nielsen C., Andersen O.S. Inclusion-induced bilayer deformations: effects of monolayer equilibrium curvature. Biophys. J. 2000, 79:2583-2604.
    • (2000) Biophys. J. , vol.79 , pp. 2583-2604
    • Nielsen, C.1    Andersen, O.S.2
  • 51
    • 43849083897 scopus 로고    scopus 로고
    • Energetics of hydrophobic matching in lipid-protein interactions
    • Marsh D. Energetics of hydrophobic matching in lipid-protein interactions. Biophys. J. 2008, 94:3996-4013.
    • (2008) Biophys. J. , vol.94 , pp. 3996-4013
    • Marsh, D.1
  • 53
    • 80455164853 scopus 로고    scopus 로고
    • Quantitative modeling of membrane deformations by multihelical membrane proteins: application to G-protein coupled receptors
    • Mondal S., Khelashvili G., Shan J., Andersen O.S., Weinstein H. Quantitative modeling of membrane deformations by multihelical membrane proteins: application to G-protein coupled receptors. Biophys. J. 2011, 101:2092-2101.
    • (2011) Biophys. J. , vol.101 , pp. 2092-2101
    • Mondal, S.1    Khelashvili, G.2    Shan, J.3    Andersen, O.S.4    Weinstein, H.5
  • 54
    • 80054690502 scopus 로고    scopus 로고
    • Probing the lipid-protein interface using model transmembrane peptides with a covalently linked acyl chain
    • Nyholm T.K., van Duyl B., Rijkers D.T., Liskamp R.M., Killian J.A. Probing the lipid-protein interface using model transmembrane peptides with a covalently linked acyl chain. Biophys. J. 2011, 101:1959-1967.
    • (2011) Biophys. J. , vol.101 , pp. 1959-1967
    • Nyholm, T.K.1    van Duyl, B.2    Rijkers, D.T.3    Liskamp, R.M.4    Killian, J.A.5
  • 55
    • 34447284723 scopus 로고    scopus 로고
    • Different effects of lipid chain length on the two sides of a membrane and the lipid annulus of MscL
    • Powl A.M., East J.M., Lee A.G. Different effects of lipid chain length on the two sides of a membrane and the lipid annulus of MscL. Biophys. J. 2007, 93:113-122.
    • (2007) Biophys. J. , vol.93 , pp. 113-122
    • Powl, A.M.1    East, J.M.2    Lee, A.G.3
  • 56
    • 36849039435 scopus 로고    scopus 로고
    • Lateral pressure profile, spontaneous curvature frustration, and the incorporation and conformation of proteins in membranes
    • Marsh D. Lateral pressure profile, spontaneous curvature frustration, and the incorporation and conformation of proteins in membranes. Biophys. J. 2007, 93:3884-3899.
    • (2007) Biophys. J. , vol.93 , pp. 3884-3899
    • Marsh, D.1
  • 57
    • 7044241302 scopus 로고    scopus 로고
    • How lipids affect the activities of integral membrane proteins
    • Lee A.G. How lipids affect the activities of integral membrane proteins. Biochim. Biophys. Acta 2004, 1666:62-87.
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 62-87
    • Lee, A.G.1
  • 58
    • 45449105164 scopus 로고    scopus 로고
    • Protein modulation of lipids, and vice-versa, in membranes
    • Marsh D. Protein modulation of lipids, and vice-versa, in membranes. Biochim. Biophys. Acta 2008, 1778:1545-1575.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1545-1575
    • Marsh, D.1
  • 59
    • 26644444070 scopus 로고    scopus 로고
    • How lipids and proteins interact in a membrane: a molecular approach
    • Lee A.G. How lipids and proteins interact in a membrane: a molecular approach. Mol. Biosyst. 2005, 1:203-212.
    • (2005) Mol. Biosyst. , vol.1 , pp. 203-212
    • Lee, A.G.1
  • 61
    • 32344451858 scopus 로고    scopus 로고
    • Alamethicin influence on the membrane bending elasticity
    • Vitkova V., Meleard P., Pott T., Bivas I. Alamethicin influence on the membrane bending elasticity. Eur. Biophys. J. 2006, 35:281-286.
    • (2006) Eur. Biophys. J. , vol.35 , pp. 281-286
    • Vitkova, V.1    Meleard, P.2    Pott, T.3    Bivas, I.4
  • 62
    • 36248957675 scopus 로고    scopus 로고
    • Entropy-driven softening of fluid lipid bilayers by alamethicin
    • Pabst G., Danner S., Podgornik R., Katsaras J. Entropy-driven softening of fluid lipid bilayers by alamethicin. Langmuir 2007, 23:11705-11711.
    • (2007) Langmuir , vol.23 , pp. 11705-11711
    • Pabst, G.1    Danner, S.2    Podgornik, R.3    Katsaras, J.4
  • 64
    • 0000505505 scopus 로고    scopus 로고
    • Activity of transmembrane proteins induces magnification of shape fluctuations of lipid membranes
    • Manneville J.B., Bassereau P., Levy D., Prost J. Activity of transmembrane proteins induces magnification of shape fluctuations of lipid membranes. Phys. Rev. Lett. 1999, 82:4356-4359.
    • (1999) Phys. Rev. Lett. , vol.82 , pp. 4356-4359
    • Manneville, J.B.1    Bassereau, P.2    Levy, D.3    Prost, J.4
  • 65
    • 18144412391 scopus 로고    scopus 로고
    • Passive or active fluctuations in membranes containing proteins
    • Girard P., Prost J., Bassereau P. Passive or active fluctuations in membranes containing proteins. Phys. Rev. Lett. 2005, 94:088102.
    • (2005) Phys. Rev. Lett. , vol.94 , pp. 088102
    • Girard, P.1    Prost, J.2    Bassereau, P.3
  • 67
    • 58149178875 scopus 로고    scopus 로고
    • Thermodynamics of lipid interactions in complex bilayers
    • Almeida P.F. Thermodynamics of lipid interactions in complex bilayers. Biochim. Biophys. Acta 2009, 1788:72-85.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 72-85
    • Almeida, P.F.1
  • 68
    • 70349481144 scopus 로고    scopus 로고
    • Cholesterol-induced fluid membrane domains: a compendium of lipid-raft ternary phase diagrams
    • Marsh D. Cholesterol-induced fluid membrane domains: a compendium of lipid-raft ternary phase diagrams. Biochim. Biophys. Acta 2009, 1788:2114-2123.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 2114-2123
    • Marsh, D.1
  • 70
    • 20644454019 scopus 로고    scopus 로고
    • Line tension and interaction energies of membrane rafts calculated from lipid splay and tilt
    • Kuzmin P.I., Akimov S.A., Chizmadzhev Y.A., Zimmerberg J., Cohen F.S. Line tension and interaction energies of membrane rafts calculated from lipid splay and tilt. Biophys. J. 2005, 88:1120-1133.
    • (2005) Biophys. J. , vol.88 , pp. 1120-1133
    • Kuzmin, P.I.1    Akimov, S.A.2    Chizmadzhev, Y.A.3    Zimmerberg, J.4    Cohen, F.S.5
  • 71
    • 36048943430 scopus 로고    scopus 로고
    • Flicker spectroscopy of thermal lipid bilayer domain boundary fluctuations
    • Esposito C., Tian A., Melamed S., Johnson C., Tee S.Y., Baumgart T. Flicker spectroscopy of thermal lipid bilayer domain boundary fluctuations. Biophys. J. 2007, 93:3169-3181.
    • (2007) Biophys. J. , vol.93 , pp. 3169-3181
    • Esposito, C.1    Tian, A.2    Melamed, S.3    Johnson, C.4    Tee, S.Y.5    Baumgart, T.6
  • 72
    • 34547260394 scopus 로고    scopus 로고
    • Line tension at fluid membrane domain boundaries measured by micropipette aspiration
    • Tian A., Johnson C., Wang W., Baumgart T. Line tension at fluid membrane domain boundaries measured by micropipette aspiration. Phys. Rev. Lett. 2007, 98:208102.
    • (2007) Phys. Rev. Lett. , vol.98 , pp. 208102
    • Tian, A.1    Johnson, C.2    Wang, W.3    Baumgart, T.4
  • 75
    • 49149101045 scopus 로고    scopus 로고
    • Critical exponents for line tension and dipole density difference from lipid monolayer domain boundary fluctuations
    • Heinrich M.C., Levental I., Gelman H., Janmey P.A., Baumgart T. Critical exponents for line tension and dipole density difference from lipid monolayer domain boundary fluctuations. J. Phys. Chem. B 2008, 112:8063-8068.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 8063-8068
    • Heinrich, M.C.1    Levental, I.2    Gelman, H.3    Janmey, P.A.4    Baumgart, T.5
  • 76
    • 29144531904 scopus 로고    scopus 로고
    • Seeing spots: complex phase behavior in simple membranes
    • Veatch S.L., Keller S.L. Seeing spots: complex phase behavior in simple membranes. Biochim. Biophys. Acta 2005, 1746:172-185.
    • (2005) Biochim. Biophys. Acta , vol.1746 , pp. 172-185
    • Veatch, S.L.1    Keller, S.L.2
  • 77
    • 76749161946 scopus 로고    scopus 로고
    • Liquid-ordered phases induced by cholesterol: a compendium of binary phase diagrams
    • Marsh D. Liquid-ordered phases induced by cholesterol: a compendium of binary phase diagrams. Biochim. Biophys. Acta 2010, 1798:688-699.
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 688-699
    • Marsh, D.1
  • 79
    • 0025128695 scopus 로고
    • Phase equilibria of cholesterol/dipalmitoylphosphatidylcholine mixtures: 2H nuclear magnetic resonance and differential scanning calorimetry
    • Vist M.R., Davis J.H. Phase equilibria of cholesterol/dipalmitoylphosphatidylcholine mixtures: 2H nuclear magnetic resonance and differential scanning calorimetry. Biochemistry 1990, 29:451-464.
    • (1990) Biochemistry , vol.29 , pp. 451-464
    • Vist, M.R.1    Davis, J.H.2
  • 80
    • 69449096258 scopus 로고    scopus 로고
    • Hybrid lipids as a biological surface-active component
    • Brewster R., Pincus P.A., Safran S.A. Hybrid lipids as a biological surface-active component. Biophys. J. 2009, 97:1087-1094.
    • (2009) Biophys. J. , vol.97 , pp. 1087-1094
    • Brewster, R.1    Pincus, P.A.2    Safran, S.A.3
  • 81
    • 77949574022 scopus 로고    scopus 로고
    • Line active hybrid lipids determine domain size in phase separation of saturated and unsaturated lipids
    • Brewster R., Safran S.A. Line active hybrid lipids determine domain size in phase separation of saturated and unsaturated lipids. Biophys. J. 2010, 98:L21-L23.
    • (2010) Biophys. J. , vol.98
    • Brewster, R.1    Safran, S.A.2
  • 82
    • 84858793657 scopus 로고    scopus 로고
    • Control of a nanoscopic-to-macroscopic transition: modulated phases in four-component DSPC/DOPC/POPC/Chol giant unilamellar vesicles
    • Konyakhina T.M., Goh S.L., Amazon J., Heberle F.A., Wu J., Feigenson G.W. Control of a nanoscopic-to-macroscopic transition: modulated phases in four-component DSPC/DOPC/POPC/Chol giant unilamellar vesicles. Biophys. J. 2011, 101:L8-L10.
    • (2011) Biophys. J. , vol.101
    • Konyakhina, T.M.1    Goh, S.L.2    Amazon, J.3    Heberle, F.A.4    Wu, J.5    Feigenson, G.W.6
  • 83
    • 84874135722 scopus 로고    scopus 로고
    • Toward a better raft model: modulated phases in the four-component bilayer, DSPC/DOPC/POPC/CHOL
    • Goh S.L., Amazon J.J., Feigenson G.W. Toward a better raft model: modulated phases in the four-component bilayer, DSPC/DOPC/POPC/CHOL. Biophys. J. 2013, 104:853-862.
    • (2013) Biophys. J. , vol.104 , pp. 853-862
    • Goh, S.L.1    Amazon, J.J.2    Feigenson, G.W.3
  • 85
    • 79959736474 scopus 로고    scopus 로고
    • Stable and unstable lipid domains in ceramide containing membranes
    • Boulgaropoulos B., Arsov Z., Laggner P., Pabst G. Stable and unstable lipid domains in ceramide containing membranes. Biophys. J. 2011, 100:2160-2168.
    • (2011) Biophys. J. , vol.100 , pp. 2160-2168
    • Boulgaropoulos, B.1    Arsov, Z.2    Laggner, P.3    Pabst, G.4
  • 86
    • 60549102443 scopus 로고    scopus 로고
    • Membrane microdomains: role of ceramides in the maintenance of their structure and functions
    • Staneva G., Momchilova A., Wolf C., Quinn P.J., Koumanov K. Membrane microdomains: role of ceramides in the maintenance of their structure and functions. Biochim. Biophys. Acta 2009, 1788:666-675.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 666-675
    • Staneva, G.1    Momchilova, A.2    Wolf, C.3    Quinn, P.J.4    Koumanov, K.5
  • 87
    • 78649287162 scopus 로고    scopus 로고
    • Comparison of three ternary lipid bilayer mixtures: FRET and ESR reveal nanodomains
    • Heberle F.A., Wu J., Goh S.L., Petruzielo R.S., Feigenson G.W. Comparison of three ternary lipid bilayer mixtures: FRET and ESR reveal nanodomains. Biophys. J. 2010, 99:3309-3318.
    • (2010) Biophys. J. , vol.99 , pp. 3309-3318
    • Heberle, F.A.1    Wu, J.2    Goh, S.L.3    Petruzielo, R.S.4    Feigenson, G.W.5
  • 88
    • 78650364986 scopus 로고    scopus 로고
    • Orientation of tie-lines in the phase diagram of DOPC/DPPC/cholesterol model biomembranes
    • Uppamoochikkal P., Tristram-Nagle S., Nagle J.F. Orientation of tie-lines in the phase diagram of DOPC/DPPC/cholesterol model biomembranes. Langmuir 2010, 26:17363-17368.
    • (2010) Langmuir , vol.26 , pp. 17363-17368
    • Uppamoochikkal, P.1    Tristram-Nagle, S.2    Nagle, J.F.3
  • 89
    • 84859917050 scopus 로고    scopus 로고
    • Phase diagram of ternary cholesterol/palmitoylsphingomyelin/palmitoyloleoyl-phosphatidylcholine mixtures: spin-label EPR study of lipid-raft formation
    • Ionova I.V., Livshits V.A., Marsh D. Phase diagram of ternary cholesterol/palmitoylsphingomyelin/palmitoyloleoyl-phosphatidylcholine mixtures: spin-label EPR study of lipid-raft formation. Biophys. J. 2012, 102:1856-1865.
    • (2012) Biophys. J. , vol.102 , pp. 1856-1865
    • Ionova, I.V.1    Livshits, V.A.2    Marsh, D.3
  • 90
    • 77954214722 scopus 로고    scopus 로고
    • Applications of neutron and X-ray scattering to the study of biologically relevant model membranes
    • Pabst G., Kucerka N., Nieh M.P., Rheinstadter M.C., Katsaras J. Applications of neutron and X-ray scattering to the study of biologically relevant model membranes. Chem. Phys. Lipids 2010, 163:460-479.
    • (2010) Chem. Phys. Lipids , vol.163 , pp. 460-479
    • Pabst, G.1    Kucerka, N.2    Nieh, M.P.3    Rheinstadter, M.C.4    Katsaras, J.5
  • 91
    • 85101470689 scopus 로고    scopus 로고
    • Flexibility and structure of fluid bilayer interfaces
    • Wiley, Hoboken, NJ, K. Nag (Ed.)
    • Rappolt M., Pabst G. Flexibility and structure of fluid bilayer interfaces. Structure and Dynamics of Membranous Interfaces 2008, 45-82. Wiley, Hoboken, NJ. K. Nag (Ed.).
    • (2008) Structure and Dynamics of Membranous Interfaces , pp. 45-82
    • Rappolt, M.1    Pabst, G.2
  • 92
    • 77957802343 scopus 로고
    • Interaction in membrane assemblies
    • Elsevier, Amsterdam, R. Lipowsky, E. Sackmann (Eds.)
    • Parsegian V.A., Rand R.P. Interaction in membrane assemblies. Handbook of Biological Physics 1995, vol. 2:643-690. Elsevier, Amsterdam. R. Lipowsky, E. Sackmann (Eds.).
    • (1995) Handbook of Biological Physics , vol.2 , pp. 643-690
    • Parsegian, V.A.1    Rand, R.P.2
  • 93
    • 0022459444 scopus 로고
    • Osmotic stress for the direct measurement of intermolecular forces
    • Parsegian V.A., Rand R.P., Fuller N.L., Rau D.C. Osmotic stress for the direct measurement of intermolecular forces. Methods Enzymol. 1986, 127:400-416.
    • (1986) Methods Enzymol. , vol.127 , pp. 400-416
    • Parsegian, V.A.1    Rand, R.P.2    Fuller, N.L.3    Rau, D.C.4
  • 94
    • 0022512564 scopus 로고
    • Hydration force and bilayer deformation: a reevaluation
    • McIntosh T.J., Simon S.A. Hydration force and bilayer deformation: a reevaluation. Biochemistry 1986, 25:4058-4066.
    • (1986) Biochemistry , vol.25 , pp. 4058-4066
    • McIntosh, T.J.1    Simon, S.A.2
  • 95
    • 0000579371 scopus 로고
    • Water at the macromolecular surface-solvation energy and functional control
    • Parsegian V.A., Rand R.P., Colombo M., Rau D.C. Water at the macromolecular surface-solvation energy and functional control. Biomembr. Electrochem. 1994, 235:177-196.
    • (1994) Biomembr. Electrochem. , vol.235 , pp. 177-196
    • Parsegian, V.A.1    Rand, R.P.2    Colombo, M.3    Rau, D.C.4
  • 97
    • 84938081949 scopus 로고
    • Steric interaction of fluid membranes in multilayer systems
    • Helfrich W. Steric interaction of fluid membranes in multilayer systems. Z. Naturforsch. 1978, 33a:305-315.
    • (1978) Z. Naturforsch. , vol.33 a , pp. 305-315
    • Helfrich, W.1
  • 102
    • 33745632777 scopus 로고    scopus 로고
    • Nonadditivity in van der Waals interactions within multilayers
    • Podgornik R., French R.H., Parsegian V.A. Nonadditivity in van der Waals interactions within multilayers. J. Chem. Phys. 2006, 124:044709.
    • (2006) J. Chem. Phys. , vol.124 , pp. 044709
    • Podgornik, R.1    French, R.H.2    Parsegian, V.A.3
  • 103
    • 33646446451 scopus 로고    scopus 로고
    • Structure of fully hydrated fluid phase lipid bilayers with monounsaturated chains
    • Kucerka N., Tristram-Nagle S., Nagle J.F. Structure of fully hydrated fluid phase lipid bilayers with monounsaturated chains. J. Membr. Biol. 2005, 208:193-202.
    • (2005) J. Membr. Biol. , vol.208 , pp. 193-202
    • Kucerka, N.1    Tristram-Nagle, S.2    Nagle, J.F.3
  • 104
    • 0026572810 scopus 로고
    • X-ray diffraction reconstruction of the inverted hexagonal (HII) phase in lipid-water systems
    • Turner D.C., Gruner S.M. X-ray diffraction reconstruction of the inverted hexagonal (HII) phase in lipid-water systems. Biochemistry 1992, 31:1340-1355.
    • (1992) Biochemistry , vol.31 , pp. 1340-1355
    • Turner, D.C.1    Gruner, S.M.2
  • 105
    • 0029914157 scopus 로고    scopus 로고
    • Measured effects of diacylglycerol on structural and elastic properties of phospholipid membranes
    • Leikin S., Kozlov M.M., Fuller N.L., Rand R.P. Measured effects of diacylglycerol on structural and elastic properties of phospholipid membranes. Biophys. J. 1996, 71:2623-2632.
    • (1996) Biophys. J. , vol.71 , pp. 2623-2632
    • Leikin, S.1    Kozlov, M.M.2    Fuller, N.L.3    Rand, R.P.4
  • 106
    • 0025105212 scopus 로고
    • Membrane curvature, lipid segregation, and structural transitions for phospholipids under dual-solvent stress
    • Rand R.P., Fuller N.L., Gruner S.M., Parsegian V.A. Membrane curvature, lipid segregation, and structural transitions for phospholipids under dual-solvent stress. Biochemistry 1990, 29:76-87.
    • (1990) Biochemistry , vol.29 , pp. 76-87
    • Rand, R.P.1    Fuller, N.L.2    Gruner, S.M.3    Parsegian, V.A.4
  • 107
    • 45049084344 scopus 로고    scopus 로고
    • X-ray diffraction measurement of the monolayer spontaneous curvature of dioleoyl phosphatidylglycerol
    • Alley S.H., Ces O., Barahona M., Templer R.H. X-ray diffraction measurement of the monolayer spontaneous curvature of dioleoyl phosphatidylglycerol. Chem. Phys. Lipids 2008, 154:64-67.
    • (2008) Chem. Phys. Lipids , vol.154 , pp. 64-67
    • Alley, S.H.1    Ces, O.2    Barahona, M.3    Templer, R.H.4
  • 108
    • 45049083404 scopus 로고    scopus 로고
    • The biologically relevant lipid mesophases as "seen" by X-rays
    • Elsevier, Amsterdam, A. Leitmannova-Liu (Ed.)
    • Rappolt M. The biologically relevant lipid mesophases as "seen" by X-rays. Advances in Planar Lipid Bilayers and Liposomes 2006, vol. 5:253-283. Elsevier, Amsterdam. A. Leitmannova-Liu (Ed.).
    • (2006) Advances in Planar Lipid Bilayers and Liposomes , vol.5 , pp. 253-283
    • Rappolt, M.1
  • 109
    • 0034188584 scopus 로고    scopus 로고
    • The bending elasticity of 1-monoolein upon relief of packing stress
    • Vacklin H.P., Khoo B.J., Madan K.H., Seddon J.M., Templer R.H. The bending elasticity of 1-monoolein upon relief of packing stress. Langmuir 2000, 16:4741-4748.
    • (2000) Langmuir , vol.16 , pp. 4741-4748
    • Vacklin, H.P.1    Khoo, B.J.2    Madan, K.H.3    Seddon, J.M.4    Templer, R.H.5
  • 110
    • 0030949722 scopus 로고    scopus 로고
    • The influence of cholesterol on phospholipid membrane curvature and bending elasticity
    • Chen Z., Rand R.P. The influence of cholesterol on phospholipid membrane curvature and bending elasticity. Biophys. J. 1997, 73:267-276.
    • (1997) Biophys. J. , vol.73 , pp. 267-276
    • Chen, Z.1    Rand, R.P.2
  • 111
    • 33745686034 scopus 로고    scopus 로고
    • Determining the ratio of the Gaussian curvature and bending elastic moduli of phospholipids from Q(II) phase unit cell dimensions
    • Siegel D.P. Determining the ratio of the Gaussian curvature and bending elastic moduli of phospholipids from Q(II) phase unit cell dimensions. Biophys. J. 2006, 91:608-618.
    • (2006) Biophys. J. , vol.91 , pp. 608-618
    • Siegel, D.P.1
  • 112
    • 3042776328 scopus 로고    scopus 로고
    • The Gaussian curvature elastic modulus of N-monomethylated dioleoylphosphatidylethanolamine: relevance to membrane fusion and lipid phase behavior
    • Siegel D.P., Kozlov M.M. The Gaussian curvature elastic modulus of N-monomethylated dioleoylphosphatidylethanolamine: relevance to membrane fusion and lipid phase behavior. Biophys. J. 2004, 87:366-374.
    • (2004) Biophys. J. , vol.87 , pp. 366-374
    • Siegel, D.P.1    Kozlov, M.M.2
  • 113
    • 58149355792 scopus 로고    scopus 로고
    • The Gaussian curvature elastic energy of intermediates in membrane fusion
    • Siegel D.P. The Gaussian curvature elastic energy of intermediates in membrane fusion. Biophys. J. 2008, 95:5200-5215.
    • (2008) Biophys. J. , vol.95 , pp. 5200-5215
    • Siegel, D.P.1
  • 114
    • 0032302898 scopus 로고    scopus 로고
    • Gaussian curvature modulus of an amphiphilic monolayer
    • Templer R.H., Khoo B.J., Seddon J.M. Gaussian curvature modulus of an amphiphilic monolayer. Langmuir 1998, 14:7427-7434.
    • (1998) Langmuir , vol.14 , pp. 7427-7434
    • Templer, R.H.1    Khoo, B.J.2    Seddon, J.M.3
  • 115
    • 38549152194 scopus 로고    scopus 로고
    • Principles of bioactive lipid signalling: lessons from sphingolipids
    • Hannun Y.A., Obeid L.M. Principles of bioactive lipid signalling: lessons from sphingolipids. Nat. Rev. Mol. Cell Biol. 2008, 9:139-150.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 139-150
    • Hannun, Y.A.1    Obeid, L.M.2
  • 116
    • 77955123824 scopus 로고    scopus 로고
    • Implication of sphingomyelin/ceramide molar ratio on the biological activity of sphingomyelinase
    • Boulgaropoulos B., Amenitsch H., Laggner P., Pabst G. Implication of sphingomyelin/ceramide molar ratio on the biological activity of sphingomyelinase. Biophys. J. 2010, 99:499-506.
    • (2010) Biophys. J. , vol.99 , pp. 499-506
    • Boulgaropoulos, B.1    Amenitsch, H.2    Laggner, P.3    Pabst, G.4
  • 117
    • 0037429735 scopus 로고    scopus 로고
    • Role of cholesterol in lipid raft formation: lessons from lipid model systems
    • Silvius J.R. Role of cholesterol in lipid raft formation: lessons from lipid model systems. Biochim. Biophys. Acta 2003, 1610:174-183.
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 174-183
    • Silvius, J.R.1
  • 118
    • 70349153375 scopus 로고    scopus 로고
    • Effect of cholesterol on structural and mechanical properties of membranes depends on lipid chain saturation
    • Pan J., Tristram-Nagle S., Nagle J.F. Effect of cholesterol on structural and mechanical properties of membranes depends on lipid chain saturation. Phys. Rev. E Stat. Nonlin. Soft Matter Phys. 2009, 80:021931.
    • (2009) Phys. Rev. E Stat. Nonlin. Soft Matter Phys. , vol.80 , pp. 021931
    • Pan, J.1    Tristram-Nagle, S.2    Nagle, J.F.3
  • 119
    • 80054978938 scopus 로고    scopus 로고
    • Impact of sterol tilt on membrane bending rigidity in cholesterol and 7-DHC containing DMPC membranes
    • Khelashvili G., Rappolt M., Chiu S.W., Pabst G., Harries D. Impact of sterol tilt on membrane bending rigidity in cholesterol and 7-DHC containing DMPC membranes. Soft Matter 2011, 7:10299-10312.
    • (2011) Soft Matter , vol.7 , pp. 10299-10312
    • Khelashvili, G.1    Rappolt, M.2    Chiu, S.W.3    Pabst, G.4    Harries, D.5
  • 120
    • 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. 1999, 76:2625-2639.
    • (1999) Biophys. J. , vol.76 , pp. 2625-2639
    • Cantor, R.S.1
  • 121
    • 84872325526 scopus 로고    scopus 로고
    • Altering hydrophobic sequence lengths shows that hydrophobic mismatch controls affinity for ordered lipid domains (rafts) in the multitransmembrane strand protein perfringolysin o
    • Lin Q., London E. Altering hydrophobic sequence lengths shows that hydrophobic mismatch controls affinity for ordered lipid domains (rafts) in the multitransmembrane strand protein perfringolysin o. J. Biol. Chem. 2013, 288:1340-1352.
    • (2013) J. Biol. Chem. , vol.288 , pp. 1340-1352
    • Lin, Q.1    London, E.2
  • 123
    • 65249187350 scopus 로고    scopus 로고
    • Preparation and properties of asymmetric vesicles that mimic cell membranes: effect upon lipid raft formation and transmembrane helix orientation
    • Cheng H.T., Megha, London E. Preparation and properties of asymmetric vesicles that mimic cell membranes: effect upon lipid raft formation and transmembrane helix orientation. J. Biol. Chem. 2009, 284:6079-6092.
    • (2009) J. Biol. Chem. , vol.284 , pp. 6079-6092
    • Cheng, H.T.1    Megha2    London, E.3


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