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Volumn 205, Issue , 2014, Pages 207-220

Model cell membranes: Discerning lipid and protein contributions in shaping the cell

Author keywords

Bilayers; Cell membranes; Lipids; Nanodiscs; Proteins; Vesicles

Indexed keywords

BI-LAYER; DEVELOPMENT AND APPLICATIONS; MEMBRANE COMPOSITION; MICROSCOPIC TECHNIQUES; MODEL MEMBRANE SYSTEMS; NANODISCS; PROTEIN-MEMBRANE INTERACTIONS; VESICLES;

EID: 84900373307     PISSN: 00018686     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cis.2013.10.028     Document Type: Review
Times cited : (53)

References (208)
  • 1
    • 1842756746 scopus 로고    scopus 로고
    • Functional roles of lipids in membranes
    • Chapter 1 Dennis E., J.E.V. Vance, Elsevier
    • Chapter 1 W. Dowhan, and M. Bogdanov Functional roles of lipids in membranes Dennis E., J.E.V. Vance, New comprehensive biochemistry vol. 36 2002 Elsevier 1 35
    • (2002) New Comprehensive Biochemistry , vol.36 , pp. 1-35
    • Dowhan, W.1    Bogdanov, M.2
  • 3
    • 0016900086 scopus 로고
    • Lipid composition and protein profiles of outer and inner membranes from pig heart mitochondria. Comparison with microsomes
    • J. Comte, B. MaÇsterrena, and D.C. Gautheron Lipid composition and protein profiles of outer and inner membranes from pig heart mitochondria. Comparison with microsomes Biochim Biophys Acta 419 1976 271 284
    • (1976) Biochim Biophys Acta , vol.419 , pp. 271-284
    • Comte, J.1    Maçsterrena, B.2    Gautheron, D.C.3
  • 4
    • 0024452509 scopus 로고
    • The lipid composition of mitochondrial outer and inner membranes from the brains of goldfish acclimated at 5 and 30°C
    • DOI 10.1016/0306-4565(89)90005-3
    • M.C.J. Chang, and B.I. Roots The lipid composition of mitochondrial outer and inner membranes from the brains of goldfish acclimated at 5 and 30 C J Therm Biol 14 1989 191 194 (Pubitemid 19233994)
    • (1989) Journal of Thermal Biology , vol.14 , Issue.4 , pp. 191-194
    • Chang, M.C.J.1    Roots, B.I.2
  • 5
    • 51449112852 scopus 로고    scopus 로고
    • Cardiolipin synthesis for the assembly of bacterial and mitochondrial membranes
    • M. Schlame Cardiolipin synthesis for the assembly of bacterial and mitochondrial membranes J Lipid Res 49 2008 1607 1620
    • (2008) J Lipid Res , vol.49 , pp. 1607-1620
    • Schlame, M.1
  • 6
    • 0022418790 scopus 로고
    • Polymorphic behavior of cardiolipin derivates studied by 31P-NMR and X-ray diffraction
    • G.L. Powell, and D. Marsh Polymorphic behavior of cardiolipin derivates studied by 31P-NMR and X-ray diffraction Biochemistry 24 1985 2902 2908
    • (1985) Biochemistry , vol.24 , pp. 2902-2908
    • Powell, G.L.1    Marsh, D.2
  • 7
    • 34547279303 scopus 로고    scopus 로고
    • Polymorphic phase behavior of cardiolipin derivatives studied by course-grained molecular dynamics
    • M. Dahlberg Polymorphic phase behavior of cardiolipin derivatives studied by course-grained molecular dynamics J Phys Chem 111 1997 7194 7200
    • (1997) J Phys Chem , vol.111 , pp. 7194-7200
    • Dahlberg, M.1
  • 8
    • 2442504884 scopus 로고    scopus 로고
    • Thermodynamic and mechanical properties of model mitochondrial membranes
    • DOI 10.1016/j.bbamem.2004.02.002, PII S000527360400046X
    • S. Nichols-Smith, S.Y. Teh, and T. Kuhl Thermodynamic and mechanical properties of model mitochondrial membranes Biochim Biophys Acta 1663 2004 82 88 (Pubitemid 38625582)
    • (2004) Biochimica et Biophysica Acta - Biomembranes , vol.1663 , Issue.1-2 , pp. 82-88
    • Nichols-Smith, S.1    Teh, S.-Y.2    Kuhl, T.L.3
  • 9
    • 63449100931 scopus 로고    scopus 로고
    • Cubic membranes: The missing dimension of cell membrane organization
    • Z.A. Almsherqi, T. Landh, S.D. Kohlwein, and Y. Deng Cubic membranes: the missing dimension of cell membrane organization Int Rev Cell Mol Biol 274 2009 275 342
    • (2009) Int Rev Cell Mol Biol , vol.274 , pp. 275-342
    • Almsherqi, Z.A.1    Landh, T.2    Kohlwein, S.D.3    Deng, Y.4
  • 10
    • 77954315602 scopus 로고    scopus 로고
    • Do viruses subvert cholesterol homeostasis to induce host cubic membranes?
    • Y. Deng, Z.A. Almsherqi, M.M. Ng, and S.D. Kohlwein Do viruses subvert cholesterol homeostasis to induce host cubic membranes? Trends Cell Biol 20 2010 371 379
    • (2010) Trends Cell Biol , vol.20 , pp. 371-379
    • Deng, Y.1    Almsherqi, Z.A.2    Ng, M.M.3    Kohlwein, S.D.4
  • 12
    • 0015514472 scopus 로고
    • The fluid mosaic model of the structure of a cell membrane
    • S.J. Singer, and G.L. Nicolson The fluid mosaic model of the structure of a cell membrane Science 175 1972 720 731
    • (1972) Science , vol.175 , pp. 720-731
    • Singer, S.J.1    Nicolson, G.L.2
  • 13
    • 0028785891 scopus 로고
    • Non-bilayerlipidsare required for efficient protein transport across the plasma membrane of Escherichia coli
    • A.G. Rietveld, M.C. Koorengevel, and B. de Kruijff Non-bilayerlipidsare required for efficient protein transport across the plasma membrane of Escherichia coli EMBO J 14 1995 5506 5513
    • (1995) EMBO J , vol.14 , pp. 5506-5513
    • Rietveld, A.G.1    Koorengevel, M.C.2    De Kruijff, B.3
  • 14
    • 84861217461 scopus 로고    scopus 로고
    • Cardiolipin and mitochondrial phosphatidylethanolamine have overlapping functions in mitochondrial fusion in Saccharomyces cerevisiae
    • A.S. Joshi, M.N. Thompson, N. Fei, M. Hütterman, and M.L. Greenberg Cardiolipin and mitochondrial phosphatidylethanolamine have overlapping functions in mitochondrial fusion in Saccharomyces cerevisiae J Biol Chem 287 2012 17589 17597
    • (2012) J Biol Chem , vol.287 , pp. 17589-17597
    • Joshi, A.S.1    Thompson, M.N.2    Fei, N.3    Hütterman, M.4    Greenberg, M.L.5
  • 15
    • 0028124422 scopus 로고
    • Modulation of rhodopsin function by properties of the membrane bilayer
    • DOI 10.1016/0009-3084(94)90180-5
    • M.F. Brown Modulation of rhodopsin function by properties of the membrane bilayer Chem Phys Lipids 73 1994 159 180 (Pubitemid 24299194)
    • (1994) Chemistry and Physics of Lipids , vol.73 , Issue.1-2 , pp. 159-180
    • Brown, M.F.1
  • 16
    • 84870901092 scopus 로고    scopus 로고
    • Curvature forces in membrane lipid-protein interactions
    • M.F. Brown Curvature forces in membrane lipid-protein interactions Biochemistry 51 2012 9782 9795
    • (2012) Biochemistry , vol.51 , pp. 9782-9795
    • Brown, M.F.1
  • 17
    • 84874053396 scopus 로고    scopus 로고
    • Solvation dynamics of biological water in a single live cell under a confocal microscope
    • D.K. Sasmal, S. Ghosh, A.K. Das, and K. Bhattacharyya Solvation dynamics of biological water in a single live cell under a confocal microscope Langmuir 29 2013 2289 2298
    • (2013) Langmuir , vol.29 , pp. 2289-2298
    • Sasmal, D.K.1    Ghosh, S.2    Das, A.K.3    Bhattacharyya, K.4
  • 19
    • 80055013471 scopus 로고    scopus 로고
    • Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell nuclear magnetic resonance spectroscopy
    • Q. Wang, A. Zhuravleva, and L.M. Gierasch Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell nuclear magnetic resonance spectroscopy Biochemistry 50 2011 9225 9236
    • (2011) Biochemistry , vol.50 , pp. 9225-9236
    • Wang, Q.1    Zhuravleva, A.2    Gierasch, L.M.3
  • 20
    • 33644846421 scopus 로고    scopus 로고
    • How proteins produce cellular membrane curvature
    • Z. Joshua, and M.K. Michael How proteins produce cellular membrane curvature Nat Rev Mol Cell Biol 7 2005 9 19
    • (2005) Nat Rev Mol Cell Biol , vol.7 , pp. 9-19
    • Joshua, Z.1    Michael, M.K.2
  • 21
    • 79953740665 scopus 로고    scopus 로고
    • Thermodynamics and mechanics of membrane curvature generation and sensing by proteins and lipids
    • T. Baumgart, B.R. Capraro, C. Zhu, and S.L. Das Thermodynamics and mechanics of membrane curvature generation and sensing by proteins and lipids Ann Rev Phys Chem 62 2011 483 506
    • (2011) Ann Rev Phys Chem , vol.62 , pp. 483-506
    • Baumgart, T.1    Capraro, B.R.2    Zhu, C.3    Das, S.L.4
  • 23
    • 78049509357 scopus 로고    scopus 로고
    • Factors affecting the viscosity in high concentration solutions of different monoclonal antibodies
    • S. Yadav, S.J. Shire, and D.S. Kalonia Factors affecting the viscosity in high concentration solutions of different monoclonal antibodies J Pharm Sci 99 2010 4812 4829
    • (2010) J Pharm Sci , vol.99 , pp. 4812-4829
    • Yadav, S.1    Shire, S.J.2    Kalonia, D.S.3
  • 26
    • 0027404239 scopus 로고
    • Lipid and water diffusion in bicontinuous cubic phases measured by NMR
    • P.O. Eriksson, and G. Lindblom Lipid and water diffusion in bicontinuous cubic phases measured by NMR Biophys J 64 1993 129 136 (Pubitemid 23063934)
    • (1993) Biophysical Journal , vol.64 , Issue.1 , pp. 129-136
    • Eriksson, P.-O.1    Lindblom, G.2
  • 27
    • 0037390283 scopus 로고    scopus 로고
    • Interaction of cytochrome c with cubic monoolein mesophases at limited hydration conditions: The effects of concentration, temperature and pressure
    • J. Lendermann, and R. Winter Interaction of cytochrome c with cubic monoolein mesophases at limited hydration conditions: the effects of concentration, temperature and pressure Phys Chem Chem Phys 5 2003 1440 1450
    • (2003) Phys Chem Chem Phys , vol.5 , pp. 1440-1450
    • Lendermann, J.1    Winter, R.2
  • 28
    • 22644440788 scopus 로고
    • A cubic structure consisting of a lipid bilayer forming an infinite periodic minimum surface of the gyroid type in the glycerolmonooleat-water system
    • S.T. Hyde, and S. Andersson A cubic structure consisting of a lipid bilayer forming an infinite periodic minimum surface of the gyroid type in the glycerolmonooleat-water system Z Kristallogr 168 1984 213 219
    • (1984) Z Kristallogr , vol.168 , pp. 213-219
    • Hyde, S.T.1    Andersson, S.2
  • 29
    • 23444432501 scopus 로고
    • A three-dimensional reconstruction study of the rough ER-Golgi interface in serial thin sections of the pancreatic acinar cell of the rat
    • A. Sesso, F.P. de Faria, E. Sadayo, M. Iwamura, and H. Correa A three-dimensional reconstruction study of the rough ER-Golgi interface in serial thin sections of the pancreatic acinar cell of the rat J Cell Sci 107 1994 517 528 (Pubitemid 24091858)
    • (1994) Journal of Cell Science , vol.107 , Issue.3 , pp. 517-528
    • Sesso, A.1    De Faria, F.P.2    Miazato Iwamura, E.S.3    Correa, H.4
  • 30
    • 49649084487 scopus 로고    scopus 로고
    • The reticulon and Dp1/Yop1p proteins form immobile oligomers in the tubular endoplasmic reticulum
    • Y. Shibata, C. Voss, J.M. Rist, J. Hu, T.A. Rapoport, and W.A. Prinz et al. The reticulon and Dp1/Yop1p proteins form immobile oligomers in the tubular endoplasmic reticulum J Biol Chem 283 2008 18892 18904
    • (2008) J Biol Chem , vol.283 , pp. 18892-18904
    • Shibata, Y.1    Voss, C.2    Rist, J.M.3    Hu, J.4    Rapoport, T.A.5    Prinz, W.A.6
  • 31
    • 32044445021 scopus 로고    scopus 로고
    • A class of membrane proteins shaping the tubular endoplasmic reticulum
    • DOI 10.1016/j.cell.2005.11.047, PII S0092867406000675
    • G.K. Voeltz, W.A. Prinz, Y. Shibata, J.M. Rist, and T.A. Rapoport A class of membrane proteins shaping the tubular endoplasmic reticulum Cell 124 2006 573 586 (Pubitemid 43199442)
    • (2006) Cell , vol.124 , Issue.3 , pp. 573-586
    • Voeltz, G.K.1    Prinz, W.A.2    Shibata, Y.3    Rist, J.M.4    Rapoport, T.A.5
  • 33
    • 79955025448 scopus 로고    scopus 로고
    • Cardiolipin microdomains localize to negatively curved regions of Escherichia coli membranes
    • L.D. Renner, and D.B. Weibel Cardiolipin microdomains localize to negatively curved regions of Escherichia coli membranes Proc Natl Acad Sci U S A 108 2011 6264 6269
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 6264-6269
    • Renner, L.D.1    Weibel, D.B.2
  • 34
    • 70849086538 scopus 로고    scopus 로고
    • Why and how bacteria localize proteins
    • L. Shapiro, H.H. McAdams, and R. Losick Why and how bacteria localize proteins Science 326 2009 1225 1228
    • (2009) Science , vol.326 , pp. 1225-1228
    • Shapiro, L.1    McAdams, H.H.2    Losick, R.3
  • 35
    • 33745645962 scopus 로고
    • Polymorphism of Lipids
    • V. Luzzati, and P.A. Spegt Polymorphism of Lipids Nature 215 1967 701 704
    • (1967) Nature , vol.215 , pp. 701-704
    • Luzzati, V.1    Spegt, P.A.2
  • 36
    • 0009263054 scopus 로고
    • Cubic lipid-water phases: Structures and biomembrane aspects
    • K. Larsson Cubic lipid-water phases: structures and biomembrane aspects J Phys Chem 93 1989 7304 7314
    • (1989) J Phys Chem , vol.93 , pp. 7304-7314
    • Larsson, K.1
  • 37
    • 0000540387 scopus 로고
    • The cubic phase of monoglyceride-water systems. Arguments for a structure based upon lamellar bilayer units
    • G. Lindblom, K. Larsson, L. Johansson, K. Fontell, and S. Forsen The cubic phase of monoglyceride-water systems. Arguments for a structure based upon lamellar bilayer units J Am Chem Soc 101 1979 5465 5470
    • (1979) J Am Chem Soc , vol.101 , pp. 5465-5470
    • Lindblom, G.1    Larsson, K.2    Johansson, L.3    Fontell, K.4    Forsen, S.5
  • 38
    • 0037939163 scopus 로고
    • X-ray diffraction by liquid crystals ± amphiphilic systems
    • G.W. Gray, P.A. Winsor
    • K. Fontell X-ray diffraction by liquid crystals ± amphiphilic systems G.W. Gray, P.A. Winsor, Liquid crystals and plastic crystals: Ellis Horwood 1974 80 109
    • (1974) Liquid Crystals and Plastic Crystals: Ellis Horwood , pp. 80-109
    • Fontell, K.1
  • 39
  • 40
    • 50849125715 scopus 로고    scopus 로고
    • Evidence that phosphatidylinositol promotes curved membrane interfaces
    • X. Mulet, R.H. Templer, R. Woscholski, and O. Ces Evidence that phosphatidylinositol promotes curved membrane interfaces Langmuir 24 2008 8443 8447
    • (2008) Langmuir , vol.24 , pp. 8443-8447
    • Mulet, X.1    Templer, R.H.2    Woscholski, R.3    Ces, O.4
  • 41
    • 0018133922 scopus 로고
    • 31P NMR study
    • P.R. Cullis, and B. De Kruijff The polymorphic phase behaviour of phosphatidylethanolamines of natural and synthetic origin. A 31P NMR study Biochim Biophys Acta 513 1978 31 42 (Pubitemid 9025753)
    • (1978) Biochimica et Biophysica Acta , vol.513 , Issue.1 , pp. 31-42
    • Cullis, P.R.1    De Kruijff, B.2
  • 42
    • 0030586161 scopus 로고    scopus 로고
    • Non-bilayer lipids and biological fusion intermediates
    • DOI 10.1016/0009-3084(96)02583-2
    • L. Chernomordik Non.bilayer lipids and biological fusion intermediates Chem Phys Lipids 81 1996 203 213 (Pubitemid 26297542)
    • (1996) Chemistry and Physics of Lipids , vol.81 , Issue.2 , pp. 203-213
    • Chernomordik, L.1
  • 43
    • 0034235229 scopus 로고    scopus 로고
    • The internal structure of mitochondria
    • T.G. Frey, and C.A. Mannella The internal structure of mitochondria Trends Biochem Sci 25 2000 319 324
    • (2000) Trends Biochem Sci , vol.25 , pp. 319-324
    • Frey, T.G.1    Mannella, C.A.2
  • 44
    • 0030780275 scopus 로고    scopus 로고
    • Biological significance of lipid polymorphism: The cubic phases
    • DOI 10.1016/S0959-440X(97)80075-9
    • V. Luzzati Biological significance of lipid polymorpholism: the cubic phase commentary Curr Opin Struct Biol 7 1997 661 668 (Pubitemid 27472585)
    • (1997) Current Opinion in Structural Biology , vol.7 , Issue.5 , pp. 661-668
    • Luzzati, V.1
  • 45
    • 33750406161 scopus 로고
    • Theory of self-assembly of hydrocarbon amphiphiles into micelles and bilayers
    • J. Israelachvili, D.J. Mitchell, and B.W. Ninham Theory of self-assembly of hydrocarbon amphiphiles into micelles and bilayers J Chem Soc Faraday Trans 2 1976 1525 1568
    • (1976) J Chem Soc Faraday Trans , vol.2 , pp. 1525-1568
    • Israelachvili, J.1    Mitchell, D.J.2    Ninham, B.W.3
  • 48
    • 0033741262 scopus 로고    scopus 로고
    • Liquid crystals and phase equilibria binary bile salt-water system
    • E.F. Marquez, H. Edlund, C. La Mesa, and A. Khan Liquid crystals and phase equilibria binary bile salt-water system Langmuir 16 2000 5178 5186
    • (2000) Langmuir , vol.16 , pp. 5178-5186
    • Marquez, E.F.1    Edlund, H.2    La Mesa, C.3    Khan, A.4
  • 49
    • 73849159982 scopus 로고
    • The Structure of the liquid-crystalline phases of lipid-water systems
    • V. Luzzati, and F. Husson The Structure of the liquid-crystalline phases of lipid-water systems J Cell Biol 12 1962 207 219
    • (1962) J Cell Biol , vol.12 , pp. 207-219
    • Luzzati, V.1    Husson, F.2
  • 52
    • 34250556040 scopus 로고
    • The greening process in plastids
    • B.E.S. Gunning The greening process in plastids Protoplasma 60 1965 111 130
    • (1965) Protoplasma , vol.60 , pp. 111-130
    • Gunning, B.E.S.1
  • 53
    • 0033328753 scopus 로고    scopus 로고
    • X-ray diffraction study of the effect of the detergent octyl glucoside on the structure of lamellar and nonlamellar lipid/water phases of use for membrane protein reconstitution
    • DOI 10.1021/la9902338
    • B. Angelov, M. Ollivon, and A. Angelova X-ray diffraction study of the effect of the detergent octyl glucoside on the structure of lamellar and nonlamellar lipid/water phases of use for membrane protein reconstitution Langmuir 15 1999 8225 8234 (Pubitemid 30528565)
    • (1999) Langmuir , vol.15 , Issue.23 , pp. 8225-8234
    • Angelov, B.1    Ollivon, M.2    Angelova, A.3
  • 54
    • 0013826995 scopus 로고
    • Phase behavior of aqueous systems of monoglycerides
    • E.S. Lutton Phase behavior of aqueous systems of monoglycerides J Am Oil Chem Soc 42 1965 1068 1070
    • (1965) J Am Oil Chem Soc , vol.42 , pp. 1068-1070
    • Lutton, E.S.1
  • 55
    • 84956220147 scopus 로고
    • Density functional theory of ionic screening: When do like charges attract?
    • M.J. Stevens, and M.O. Robbins Density functional theory of ionic screening: when do like charges attract? Eur Phys Lett 12 1991 81
    • (1991) Eur Phys Lett , vol.12 , pp. 81
    • Stevens, M.J.1    Robbins, M.O.2
  • 57
    • 0036039757 scopus 로고    scopus 로고
    • Effect of electrostatic interactions on phase stability of cubic phases of biomembranes
    • DOI 10.1023/A:1019927614681
    • S.J. Li, S.M. Masum, Y. Yamashita, Y. Tamba, and M. Yamazaki Effect of electrostatic interactions on phase stability of cubic phases of biomembranes J Biol Phys 28 2001 253 266 (Pubitemid 35012961)
    • (2002) Journal of Biological Physics , vol.28 , Issue.2 , pp. 253-266
    • Li, S.J.1    Masum, S.M.2    Yamashita, Y.3    Tamba, Y.4    Yamazaki, M.5
  • 58
    • 84943997802 scopus 로고
    • Elastic properties of lipid bilayers - Theory and possible experiments
    • W. Helfrich Elastic properties of lipid bilayers - theory and possible experiments Z Naturforsch C 28 1973 693 703
    • (1973) Z Naturforsch C , vol.28 , pp. 693-703
    • Helfrich, W.1
  • 59
    • 84889428831 scopus 로고    scopus 로고
    • Red blood cell shapes and shape transformations: Newtonian mechanics of a composite membrane: Sections 2.1-2.4
    • Wiley-VCH Verlag GmbH & Co. KGaA
    • H.W.G. Lim, M. Wortis, and R. Mukhopadhyay Red blood cell shapes and shape transformations: newtonian mechanics of a composite membrane: sections 2.1-2.4 Soft Matter 2009 Wiley-VCH Verlag GmbH & Co. KGaA 83 139
    • (2009) Soft Matter , pp. 83-139
    • Lim, H.W.G.1    Wortis, M.2    Mukhopadhyay, R.3
  • 60
    • 0030586198 scopus 로고    scopus 로고
    • On the molecular-level mechanisms of peripheral protein-membrane interactions induced by lipids forming inverted non-lamellar phases
    • DOI 10.1016/0009-3084(96)02579-0
    • P.K.J. Kinnunen On the molecular-level mechanisms of peripheral protein-membrane interactions induced by lipids forming inverted non-lamellar phases Chem Phys Lipids 81 1996 151 166 (Pubitemid 26297538)
    • (1996) Chemistry and Physics of Lipids , vol.81 , Issue.2 , pp. 151-166
    • Kinnunen, P.K.J.1
  • 61
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • D. Lingwood, and K. Simons Lipid rafts as a membrane-organizing principle Science 327 2010 46 50
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 62
    • 61349094652 scopus 로고    scopus 로고
    • Direct observation of the nanoscale dynamics of membrane lipids in a living cell
    • C. Eggeling, C. Ringemann, R. Medda, G. Schwarzmann, K. Sandhoff, and S. Polyakova et al. Direct observation of the nanoscale dynamics of membrane lipids in a living cell Nature 457 2009 1159 1162
    • (2009) Nature , vol.457 , pp. 1159-1162
    • Eggeling, C.1    Ringemann, C.2    Medda, R.3    Schwarzmann, G.4    Sandhoff, K.5    Polyakova, S.6
  • 63
    • 84865169456 scopus 로고    scopus 로고
    • The lipid raft hypothesis revisited - New insights on raft composition and function from super-resolution fluorescence microscopy
    • D.M. Owen, A. Magenau, D. Williamson, and K. Gaus The lipid raft hypothesis revisited - new insights on raft composition and function from super-resolution fluorescence microscopy Bioessays 34 2012 739 747
    • (2012) Bioessays , vol.34 , pp. 739-747
    • Owen, D.M.1    Magenau, A.2    Williamson, D.3    Gaus, K.4
  • 64
    • 84880596969 scopus 로고    scopus 로고
    • Direct imaging reveals stable, micrometer-scale lipid domains that segregate proteins in live cell
    • A. Toulmay, and A.P. William Direct imaging reveals stable, micrometer-scale lipid domains that segregate proteins in live cell J Cell Biol 202 2013 35 44
    • (2013) J Cell Biol , vol.202 , pp. 35-44
    • Toulmay, A.1    William, A.P.2
  • 65
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • DOI 10.1038/42408
    • K. Simons, and E. Ikonen Functional rafts in cell membranes Nature 387 1997 569 572 (Pubitemid 27248754)
    • (1997) Nature , vol.387 , Issue.6633 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 66
    • 84859758924 scopus 로고    scopus 로고
    • Co-existence of gel and fluid lipid domains in single-component phospholipid membranes
    • C.L. Armstrong, M.A. Barrett, L. Toppozini, N. Kucerka, Z. Yamani, and J. Katsaras et al. Co-existence of gel and fluid lipid domains in single-component phospholipid membranes Soft Matter 8 2012 4687 4694
    • (2012) Soft Matter , vol.8 , pp. 4687-4694
    • Armstrong, C.L.1    Barrett, M.A.2    Toppozini, L.3    Kucerka, N.4    Yamani, Z.5    Katsaras, J.6
  • 68
    • 78651259664 scopus 로고
    • On the miscibility of cardiolipin with 1,2-diacyl phosphoglycerides: Binary mixtures of dimyristoylphosphatidylethanolamine and tetramyristoylcardiolipin
    • M. Frias, M.G.K. Benesch, R.N.A.H. Lewis, and R.N. McElhaney On the miscibility of cardiolipin with 1,2-diacyl phosphoglycerides: binary mixtures of dimyristoylphosphatidylethanolamine and tetramyristoylcardiolipin Biochim Biophys Acta 2011 1808 774 783
    • (1808) Biochim Biophys Acta , vol.2011 , pp. 774-783
    • Frias, M.1    Benesch, M.G.K.2    Lewis, R.N.A.H.3    McElhaney, R.N.4
  • 69
    • 0026048726 scopus 로고
    • Asymmetric distribution of phosphoinositides and phosphatidic acid in the human erythrocyte membrane
    • P. Gascard, D. Tran, M. Sauvage, J.C. Sulpice, K. Fukami, and T. Takenawa et al. Asymmetric distribution of phosphoinositides and phosphatidic acid in the human erythrocyte membrane Biochim Biophys Acta 1069 1991 27 36
    • (1991) Biochim Biophys Acta , vol.1069 , pp. 27-36
    • Gascard, P.1    Tran, D.2    Sauvage, M.3    Sulpice, J.C.4    Fukami, K.5    Takenawa, T.6
  • 70
  • 71
    • 34249325178 scopus 로고    scopus 로고
    • Aggregation and vesiculation of membrane proteins by curvature-mediated interactions
    • J.R. Benedict, I. Gregoria, A.H. Vagelis, M.M. Martin, K. Kurt, and D. Markus Aggregation and vesiculation of membrane proteins by curvature-mediated interactions Nature 447 2007 461 464
    • (2007) Nature , vol.447 , pp. 461-464
    • Benedict, J.R.1    Gregoria, I.2    Vagelis, A.H.3    Martin, M.M.4    Kurt, K.5    Markus, D.6
  • 72
    • 0017858332 scopus 로고
    • Proteins of rough microsomal membranes related to ribosome binding. I. Identification of ribophorins I and II, membrane proteins characteristic of rough microsomes
    • DOI 10.1083/jcb.77.2.464
    • G. Kreibich, B. Ulrich, and D. Sabatini Proteins of rough microsomal membranes related to ribosome binding. I. Identification of ribophorins I and II, membrane proteins characteristics of rough microsomes J Cell Biol 77 1978 464 487 (Pubitemid 8333466)
    • (1978) Journal of Cell Biology , vol.77 , Issue.2 , pp. 464-487
    • Kreibich, G.1    Ulrich, B.L.2    Sabatini, D.D.3
  • 73
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4A resolution
    • DOI 10.1016/j.jmb.2004.12.031
    • N. Unwin Refined structure of the nicotinic acetylcholine receptor at 4A resolution J Mol Biol 346 2005 967 989 (Pubitemid 40215523)
    • (2005) Journal of Molecular Biology , vol.346 , Issue.4 , pp. 967-989
    • Unwin, N.1
  • 74
    • 84861624344 scopus 로고    scopus 로고
    • Reconstitution of clathrin-coated bud and vesicle formation with minimal components
    • P.N. Dannhauser, and E.J. Ungewickell Reconstitution of clathrin-coated bud and vesicle formation with minimal components Nat Cell Biol 14 2012 634 639
    • (2012) Nat Cell Biol , vol.14 , pp. 634-639
    • Dannhauser, P.N.1    Ungewickell, E.J.2
  • 76
    • 80052462187 scopus 로고    scopus 로고
    • Membrane restructuring by phopholipase A2 is regulated by the presence of lipid domains
    • C. Leidy, J. Ocampo, L. Duelund, O.G. Mouritsen, K. Jørgensen, and G.H. Peters Membrane restructuring by phopholipase A2 is regulated by the presence of lipid domains Biophys J 101 2011 90 99
    • (2011) Biophys J , vol.101 , pp. 90-99
    • Leidy, C.1    Ocampo, J.2    Duelund, L.3    Mouritsen, O.G.4    Jørgensen, K.5    Peters, G.H.6
  • 77
    • 1442299369 scopus 로고    scopus 로고
    • 2 promotes raft budding and fission from giant liposomes
    • DOI 10.1016/j.chemphyslip.2003.11.005, PII S0009308403001932
    • G. Staneva, M.I. Angelova, and K. Koumanov Phospholipase A2 promotes raft budding and fission from giant liposomes Chem Phys Lipids 129 2004 53 62 (Pubitemid 38293249)
    • (2004) Chemistry and Physics of Lipids , vol.129 , Issue.1 , pp. 53-62
    • Staneva, G.1    Angelova, M.I.2    Koumanov, K.3
  • 79
    • 0001718634 scopus 로고
    • Biological membranes as bilayer couples. A molecular mechanism of drug-erythrocyte interactions
    • M.P. Sheetz, and S.J. Singer Biological membranes as bilayer couples. A molecular mechanism of drug-erythrocyte interactions Proc Natl Acad Sci U S A 71 1974 4457 4461
    • (1974) Proc Natl Acad Sci U S A , vol.71 , pp. 4457-4461
    • Sheetz, M.P.1    Singer, S.J.2
  • 80
    • 12144267932 scopus 로고    scopus 로고
    • Langmuir monolayers to study the interactions at model membrane surfaces
    • G. Brezesinski, and H. Möhwald Langmuir monolayers to study the interactions at model membrane surfaces Adv Colloid Interface Sci 100-102 2003 563 584
    • (2003) Adv Colloid Interface Sci , vol.100-102 , pp. 563-584
    • Brezesinski, G.1    Möhwald, H.2
  • 82
    • 0018881828 scopus 로고
    • Comparative properties and methods of preparation of lipid vesicles (liposomes)
    • F.C. Szoka, and D. Papahadjopoulus Comparative properties and methods of preparation of lipid vesicles (liposomes) Ann Rev Biophys Biol 9 1980 467 508
    • (1980) Ann Rev Biophys Biol , vol.9 , pp. 467-508
    • Szoka, F.C.1    Papahadjopoulus, D.2
  • 83
    • 0018719041 scopus 로고
    • Preparation of liposomes of defined size distribution by extrusion through polycarbonate membranes
    • F. Olson, C.A. Hunt, F.C. Szoka, W.J. Vail, and D. Papahadjopoulus Preparation of liposomes of defined size distribution by extrusion through polycarbonate membranes Biochim Biophys Acta 557 1979 9 23 (Pubitemid 10245657)
    • (1979) Biochimica et Biophysica Acta , vol.557 , Issue.1 , pp. 9-23
    • Olson, F.1    Hunt, C.A.2    Szoka, F.C.3
  • 84
    • 0021909644 scopus 로고
    • Production of large unilamellar vesicles by a rapid extrusion procedure. Characterization of size distribution, trapped volume and ability to maintain a membrane potential
    • DOI 10.1016/0005-2736(85)90521-8
    • M.J. Hope, M.B. Bally, G. Webb, and P.R. Cullis Production of large unilamellar vesicles by a rapid extrusion procedure - characterization of size distribution, trapped volume and ability to maintain a membrane-potential Biochim Biophys Acta 812 1985 55 65 (Pubitemid 15159822)
    • (1985) Biochimica et Biophysica Acta - Biomembranes , vol.812 , Issue.1 , pp. 55-65
    • Hope, M.J.1    Bally, M.B.2    Webb, G.3    Cullis, P.R.4
  • 86
    • 0022381164 scopus 로고
    • Preparation and characterization of monodisperse unilamelar phospholipid vesicles with selected diameters of from 300 to 600 nm
    • DOI 10.1016/0005-2736(85)90118-X
    • T.S. Aurora, W. Li, H.Z. Cummins, and T.H. Haines Preparation and characterization of monodisperse unilamellar phospholipid-vesicles with selected diameters of from 300 to 600 nm Biochim Biophys Acta 820 1985 250 258 (Pubitemid 16235003)
    • (1985) Biochimica et Biophysica Acta - Biomembranes , vol.820 , Issue.2 , pp. 250-258
    • Aurora, T.S.1    Li, W.2    Cummins, H.Z.3    Haines, T.H.4
  • 87
    • 0033739343 scopus 로고    scopus 로고
    • Size and stability of catanionic vesicles: Effects of formation path, sonication, and aging
    • E.F. Marquez Size and stability of catanionic vesicles: effects of formation path, sonication, and aging Langmuir 16 2000 4798 4807
    • (2000) Langmuir , vol.16 , pp. 4798-4807
    • Marquez, E.F.1
  • 88
    • 84861122853 scopus 로고    scopus 로고
    • Composition and structure of mixed phospholipid supported bilayers formed by POPC and DPPC
    • A. Åkesson, T. Lind, N. Ehrlich, D. Stamou, H.P. Wacklin, and M. Cardenas Composition and structure of mixed phospholipid supported bilayers formed by POPC and DPPC Soft Matter 8 2012 5658 5665
    • (2012) Soft Matter , vol.8 , pp. 5658-5665
    • Åkesson, A.1    Lind, T.2    Ehrlich, N.3    Stamou, D.4    Wacklin, H.P.5    Cardenas, M.6
  • 89
    • 50949166660 scopus 로고    scopus 로고
    • A fluorescence-based technique to construct size distributions from single-object measurements: Application to the extrusion of lipid vesicles
    • A.H. Kunding, M.W. Mortensen, S.M. Christensen, and D. Stamou A fluorescence-based technique to construct size distributions from single-object measurements: application to the extrusion of lipid vesicles Biophys J 95 2008 1176 1188
    • (2008) Biophys J , vol.95 , pp. 1176-1188
    • Kunding, A.H.1    Mortensen, M.W.2    Christensen, S.M.3    Stamou, D.4
  • 90
    • 0023047980 scopus 로고
    • Vesicles of variable sizes produced by a rapid extrusion procedure
    • L.D. Mayer, M.J. Hope, and P.R. Cullis Vesicles of variable sizes produced by a rapid extrusion procedure Biochim Biophys Acta 858 1986 161 168
    • (1986) Biochim Biophys Acta , vol.858 , pp. 161-168
    • Mayer, L.D.1    Hope, M.J.2    Cullis, P.R.3
  • 92
    • 46449109664 scopus 로고    scopus 로고
    • Giant unilamellar vesicle formation under physiologically relevant conditions
    • T. Pott, H. Bouvrais, and P. Meleard Giant unilamellar vesicle formation under physiologically relevant conditions Chem Phys Lipids 154 2008 115 119
    • (2008) Chem Phys Lipids , vol.154 , pp. 115-119
    • Pott, T.1    Bouvrais, H.2    Meleard, P.3
  • 93
    • 18144386926 scopus 로고    scopus 로고
    • Miscibility phase diagrams of giant vesicles containing sphingomyelin
    • S.L. Veatch, and S.L. Keller Miscibility phase diagrams of giant vesicles containing sphingomyelin Phys Rev Lett 94 2005 148101
    • (2005) Phys Rev Lett , vol.94 , pp. 148101
    • Veatch, S.L.1    Keller, S.L.2
  • 94
    • 0242385346 scopus 로고    scopus 로고
    • Separation of Liquid Phases in Giant Vesicles of Ternary Mixtures of Phospholipids and Cholesterol
    • S.L. Veath, and S.L. Keller Separation of liquid phases in giant vesicles of ternary mixtures of phospholipids and cholesterol Biophys J 85 2003 3074 3083 (Pubitemid 37345795)
    • (2003) Biophysical Journal , vol.85 , Issue.5 , pp. 3074-3083
    • Veatch, S.L.1    Keller, S.L.2
  • 96
    • 0033838965 scopus 로고    scopus 로고
    • Giant phospholipid vesicles: Comparison among the whole lipid sample characteristics using different preparation methods. A two photon fluorescence microscopy study
    • L.A. Bagatolli, T. Parasassi, and E. Gratton Giant phospholipid vesicles: comparison among the whole lipid sample characteristics using different preparation methods. A two photon fluorescence microscopy study Chem Phys Lipids 105 2000 135 147
    • (2000) Chem Phys Lipids , vol.105 , pp. 135-147
    • Bagatolli, L.A.1    Parasassi, T.2    Gratton, E.3
  • 97
    • 17044375415 scopus 로고    scopus 로고
    • Giant vesicles formed by gentle hydration and electroformation: A comparison by fluorescence microscopy
    • N. Rodriguez, and PFCS Giant vesicles formed by gentle hydration and electroformation: a comparison by fluorescence microscopy Colloids Surf B 42 2005 125 130
    • (2005) Colloids Surf B , vol.42 , pp. 125-130
    • Rodriguez, N.1    Pfcs2
  • 98
    • 67249136866 scopus 로고    scopus 로고
    • Giant unilamellar vesicles: A perfect tool to visualize phase separation and lipid rafts in model systems
    • O. Wesolowska, K. Michalak, J. Maniewska, and A.B. Hendrich Giant unilamellar vesicles: a perfect tool to visualize phase separation and lipid rafts in model systems Acta Biochim Pol 56 2009 33 39
    • (2009) Acta Biochim Pol , vol.56 , pp. 33-39
    • Wesolowska, O.1    Michalak, K.2    Maniewska, J.3    Hendrich, A.B.4
  • 99
    • 2342483719 scopus 로고    scopus 로고
    • The microcalorimetry of lipid membranes
    • H. Heerklotz The microcalorimetry of lipid membranes J Phys Condens Matter 16 2004 R441 R467
    • (2004) J Phys Condens Matter , vol.16
    • Heerklotz, H.1
  • 100
    • 0032557205 scopus 로고    scopus 로고
    • Miscibility of phospholipids with identical headgroups and acyl chain lengths differing by two methylene units: Effects of headgroup structure and headgroup charge
    • DOI 10.1016/S0005-2736(98)00005-4, PII S0005273698000054
    • P. Garidel, and A. Blume Miscibility of phospholipids with identical headgroups and acyl chain lengths differing by two methylene units: effects of headgroup structure and headgroup charge Biochim Biophys Acta 1371 1998 83 95 (Pubitemid 28197055)
    • (1998) Biochimica et Biophysica Acta - Biomembranes , vol.1371 , Issue.1 , pp. 83-95
    • Garidel, P.1    Blume, A.2
  • 101
    • 0030891869 scopus 로고    scopus 로고
    • Nonideal mixing and phase separation in phosphatidylcholine- phosphatidic acid mixtures as a function of acyl chain length and pH
    • P. Garidel, C. Johann, and A. Blume Nonideal mixing and phase separation in phosphatidylcholine-phosphatidic acid mixtures as a function of acyl chain length and pH Biophys J 72 1997 2196 2210 (Pubitemid 27184447)
    • (1997) Biophysical Journal , vol.72 , Issue.5 , pp. 2196-2210
    • Garidel, P.1    Johann, C.2    Blume, A.3
  • 102
    • 0030724793 scopus 로고    scopus 로고
    • The mixing behavior of pseudobinary phosphatidylcholine- phosphatidylglycerol mixtures as a function of pH and chain length
    • DOI 10.1007/s002490050099
    • P. Garidel, C. Johann, L. Mennicke, and A. Blume The mixing behavior of pseudobinary phosphatidylcholinephosphatidylglycerol mixtures as a function of pH and chain length Eur Biophys J 26 1997 447 459 (Pubitemid 27509261)
    • (1997) European Biophysics Journal , vol.26 , Issue.6 , pp. 447-459
    • Garidel, P.1    Johann, C.2    Mennicke, L.3    Blume, A.4
  • 103
    • 0001541657 scopus 로고
    • Investigation of phase transitions of lipids and lipid mixtures sensitivity to differential scanning calorimetry
    • S. Mabrey, and J.M. Sturtevant Investigation of phase transitions of lipids and lipid mixtures sensitivity to differential scanning calorimetry Proc Natl Acad Sci U S A 73 1976 3862 3866
    • (1976) Proc Natl Acad Sci U S A , vol.73 , pp. 3862-3866
    • Mabrey, S.1    Sturtevant, J.M.2
  • 104
    • 0000304467 scopus 로고
    • Physical studies of phospholipids. VI. Thermotropic and lyotropic mesomorphism of some 1,2-diacyl-phosphatidylcholines (lecithins)
    • D. Chapman, R.M. Williams, and B.D. Ladbroke Physical studies of phospholipids. VI. Thermotropic and lyotropic mesomorphism of some 1,2-diacyl-phosphatidylcholines (lecithins) Chem Phys Lipids 1 1967 445 475
    • (1967) Chem Phys Lipids , vol.1 , pp. 445-475
    • Chapman, D.1    Williams, R.M.2    Ladbroke, B.D.3
  • 105
    • 0035795722 scopus 로고    scopus 로고
    • Interaction of N-myristoyldimyristoylphosphatidylethanolamine with dimyristoylphosphatidylcholine investigated by differential scanning calorimetry: Binary phase diagram
    • DOI 10.1016/S0005-2736(01)00317-0, PII S0005273601003170
    • M. Ramakrishnan, D. Marsh, and M.J. Swamy Interaction of N-myristoyldimyristoylphosphatidylethanolamine with dimystoylphosphatidylcholine investigated by differential scanning calorimetry: binary phase diagram Biochim Biophys Acta 1512 2001 22 26 (Pubitemid 32378781)
    • (2001) Biochimica et Biophysica Acta - Biomembranes , vol.1512 , Issue.1 , pp. 22-26
    • Ramakrishnan, M.1    Marsh, D.2    Swamy, M.J.3
  • 106
    • 0030868488 scopus 로고    scopus 로고
    • Lipid microdomains in dimyristoylphosphatidylcholine-ceramide liposomes
    • J.M. Holopainen, J.Y.A. Lehtonen, and P.K.J. Kinnunen Lipid microdomains in dimyristoylphosphatidylcholine-ceramide liposomes Chem Phys Lipids 88 1997 1 13
    • (1997) Chem Phys Lipids , vol.88 , pp. 1-13
    • Holopainen, J.M.1    Lehtonen, J.Y.A.2    Kinnunen, P.K.J.3
  • 107
    • 0027723066 scopus 로고
    • Influence of sphingosine on the thermal phase behaviour of neutral and acidic phospholipid liposomes
    • DOI 10.1016/0009-3084(93)90037-4
    • A. Kõiv, P. Mustonen, and P.K.J. Kinnunen Influence of sphingosine on the thermal phase behaviour of neutral and acidic phospholipid liposomes Chem Phys Lipids 66 1993 123 134 (Pubitemid 24002620)
    • (1993) Chemistry and Physics of Lipids , vol.66 , Issue.1-2 , pp. 123-134
    • Koiv, A.1    Mustonen, P.2    Kinnunen, P.K.J.3
  • 108
    • 0242385346 scopus 로고    scopus 로고
    • Separation of Liquid Phases in Giant Vesicles of Ternary Mixtures of Phospholipids and Cholesterol
    • S.L. Veatch, and S.L. Keller Separation of liquid phases in giant vesicles of ternary mixtures of phospholipids and cholesterol Biophys J 85 2003 3074 3083 (Pubitemid 37345795)
    • (2003) Biophysical Journal , vol.85 , Issue.5 , pp. 3074-3083
    • Veatch, S.L.1    Keller, S.L.2
  • 110
    • 38949194335 scopus 로고    scopus 로고
    • Small-angle neutron scattering to detect rafts and lipid domains
    • T.J. McIntosh, SpringerProtocols
    • J. Pencer, T.T. Mills, N. Kucerka, M.-P. Nieh, and J. Katsaras Small-angle neutron scattering to detect rafts and lipid domains T.J. McIntosh, Methods in molecular biology vol. 398 2007 SpringerProtocols 231 244
    • (2007) Methods in Molecular Biology , vol.398 , pp. 231-244
    • Pencer, J.1    Mills, T.T.2    Kucerka, N.3    Nieh, M.-P.4    Katsaras, J.5
  • 111
    • 84900359185 scopus 로고    scopus 로고
    • www.avantilipids.com.
  • 112
    • 0035016931 scopus 로고    scopus 로고
    • Ternary phase diagram of dipalmitoyl-PC/dilauroyl-PC/cholesterol: Nanoscopic domain formation driven by cholesterol
    • G.W. Feigenson, and J.T. Buboltz Ternary phase diagram of dipalmitoyl-PC/dilauroyl-PC/cholesterol: nanoscopic domain formation driven by cholesterol Biophys J 80 2001 2775 2788 (Pubitemid 32521651)
    • (2001) Biophysical Journal , vol.80 , Issue.6 , pp. 2775-2788
    • Feigenson, G.W.1    Buboltz, J.T.2
  • 113
    • 78649287162 scopus 로고    scopus 로고
    • Comparison of three ternary lipid bilayer mixtures: FRET and ESR reveal nanodomains
    • F.A. Heberle, J. Wu, S.L. Goh, R.S. Petruzielo, and G.W. Feigenson Comparison of three ternary lipid bilayer mixtures: FRET and ESR reveal nanodomains Biophys J 99 2010 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
  • 114
    • 81255123303 scopus 로고    scopus 로고
    • Measurement of lipid nanodomain(raft) formation and size in sphingomyelin/POPC/cholesterol vesicles shows TX-100 and transmembrane helices increase domain size by coalescing preexisting nanodomains but do not induce domain formation
    • P. Pathak, and E. London Measurement of lipid nanodomain(raft) formation and size in sphingomyelin/POPC/cholesterol vesicles shows TX-100 and transmembrane helices increase domain size by coalescing preexisting nanodomains but do not induce domain formation Biophys J 101 2011 2417 2425
    • (2011) Biophys J , vol.101 , pp. 2417-2425
    • Pathak, P.1    London, E.2
  • 115
    • 84859917050 scopus 로고    scopus 로고
    • Phase diagram of ternary cholesterol/palmitoylsphingomyelin/ palmitoyloleoyl-phosphatidylcholine mixtures: Spin-label EPR study of lipid-raft formation
    • I.V. Ionova, V.A. Livshits, and D. Marsh Phase diagram of ternary cholesterol/palmitoylsphingomyelin/palmitoyloleoyl-phosphatidylcholine mixtures: spin-label EPR study of lipid-raft formation Biophys J 102 2012 1856 1865
    • (2012) Biophys J , vol.102 , pp. 1856-1865
    • Ionova, I.V.1    Livshits, V.A.2    Marsh, D.3
  • 117
    • 77952371099 scopus 로고    scopus 로고
    • Steric confinement of proteins on lipid membranes can drive curvature and tubulation
    • J.C. Stachowiak, C.C. Hayden, and D.Y. Sasaki Steric confinement of proteins on lipid membranes can drive curvature and tubulation Proc Natl Acad Sci U S A 107 2010 7781 7786
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 7781-7786
    • Stachowiak, J.C.1    Hayden, C.C.2    Sasaki, D.Y.3
  • 118
    • 34547221056 scopus 로고    scopus 로고
    • Spontaneous formation of asymmetric lipid bilayers by adsorption of vesicles
    • DOI 10.1021/la063476q
    • H.P. Wacklin, and R.K. Thomas Spontaneous formation of asymmetric lipid bilayers by adsorption of vesicles Langmuir 23 2007 7644 7651 (Pubitemid 47116428)
    • (2007) Langmuir , vol.23 , Issue.14 , pp. 7644-7651
    • Wacklin, H.P.1    Thomas, R.K.2
  • 119
    • 79959243061 scopus 로고    scopus 로고
    • Composition and asymmetry in supported membranes formed by vesicle fusion
    • H.P. Wacklin Composition and asymmetry in supported membranes formed by vesicle fusion Langmuir 27 2011 7698 7707
    • (2011) Langmuir , vol.27 , pp. 7698-7707
    • Wacklin, H.P.1
  • 120
    • 0242290843 scopus 로고    scopus 로고
    • Pathways of Lipid Vesicle Deposition on Solid Surfaces: A Combined QCM-D and AFM Study
    • R. Richter, A. Mukhopadhyay, and A. Brisson Pathways of lipid vesicle deposition on solid surfaces: a combined QCM-D and AFM study Biophys J 85 2003 3035 3047 (Pubitemid 37345791)
    • (2003) Biophysical Journal , vol.85 , Issue.5 , pp. 3035-3047
    • Richter, R.1    Mukhopadhyay, A.2    Brisson, A.3
  • 121
    • 77956713459 scopus 로고    scopus 로고
    • Quartz crystal microbalance with dissipation monitoring of supported lipid bilayers on various substrates
    • N.J. Cho, C.W. Frank, B. Kasemo, and F. Hook Quartz crystal microbalance with dissipation monitoring of supported lipid bilayers on various substrates Nat Protoc 5 2010 1096 1106
    • (2010) Nat Protoc , vol.5 , pp. 1096-1106
    • Cho, N.J.1    Frank, C.W.2    Kasemo, B.3    Hook, F.4
  • 122
    • 11144229431 scopus 로고    scopus 로고
    • Vesicle adsorption and lipid bilayer formation on glass studied by atomic force microscopy
    • DOI 10.1021/la049302v
    • H. Schönherr, J.M. Johnson, P. Lenz, C.W. Frank, and S.G. Boxer Vesicle adsorption and lipid bilayer formation on glass studied by atomic force microscopy Langmuir 20 2004 11600 11606 (Pubitemid 40049634)
    • (2004) Langmuir , vol.20 , Issue.26 , pp. 11600-11606
    • Schonherr, H.1    Johnson, J.M.2    Lenz, P.3    Frank, C.W.4    Boxer, S.G.5
  • 123
    • 84882737452 scopus 로고    scopus 로고
    • Simulation of edge facilitated adsorption and critical concentration induced rupture of vesicles at a surface
    • P. Plunkett, B.A. Camley, K.L. Weirich, J. Israelachvili, and P.J. Atzberger Simulation of edge facilitated adsorption and critical concentration induced rupture of vesicles at a surface Soft Matter 9 2013 8420 8427
    • (2013) Soft Matter , vol.9 , pp. 8420-8427
    • Plunkett, P.1    Camley, B.A.2    Weirich, K.L.3    Israelachvili, J.4    Atzberger, P.J.5
  • 124
    • 0001215138 scopus 로고    scopus 로고
    • Formation and spreading of lipid bilayers on planar glass supports
    • P.S. Cremer, and S.G. Boxer Formation and spreading of lipid bilayers on planar glass supports J Phys Chem B 103 1999 2554 2559 (Pubitemid 129702516)
    • (1999) Journal of Physical Chemistry B , vol.103 , Issue.13 , pp. 2554-2559
    • Cremer, P.S.1    Boxer, S.G.2
  • 125
    • 0031679214 scopus 로고    scopus 로고
    • Surface specific kinetics of lipid vesicle adsorption measured with a quartz crystal microbalance
    • C.A. Keller, and B. Kasemo Surface specific kinetics of lipid vesicle adsorption measured with a quartz crystal microbalance Biophys J 75 1998 1397 1402 (Pubitemid 28397608)
    • (1998) Biophysical Journal , vol.75 , Issue.3 , pp. 1397-1402
    • Keller, C.A.1    Kasemo, B.2
  • 126
    • 0033894687 scopus 로고    scopus 로고
    • Formation of supported phospholipid bilayers from unilamellar vesicles investigated by atomic force microscopy
    • DOI 10.1021/la9903043
    • I. Reviakine, and A.R. Brisson Formation of supported phospholipid bilayers from unilamellar vesicles investigated by atomic force microscopy Langmuir 16 2000 1806 1815 (Pubitemid 30590688)
    • (2000) Langmuir , vol.16 , Issue.4 , pp. 1806-1815
    • Reviakine, I.1    Brisson, A.2
  • 127
    • 67149147248 scopus 로고    scopus 로고
    • Formation of supported bacterial lipid membrane mimics
    • C. Merz, W. Knoll, M. Textor, and E. Reimhult Formation of supported bacterial lipid membrane mimics Biointerphases 3 2008 FA41 FA50
    • (2008) Biointerphases , vol.3
    • Merz, C.1    Knoll, W.2    Textor, M.3    Reimhult, E.4
  • 128
    • 80052341509 scopus 로고    scopus 로고
    • Continuous lipid bilayers derived from cell membranes for spatial molecular manipulation
    • L. Simonsson, A. Gunnarsson, P. Wallin, P. Jonsson, and F. Höök Continuous lipid bilayers derived from cell membranes for spatial molecular manipulation J Am Chem Soc 133 2011 14027 14032
    • (2011) J Am Chem Soc , vol.133 , pp. 14027-14032
    • Simonsson, L.1    Gunnarsson, A.2    Wallin, P.3    Jonsson, P.4    Höök, F.5
  • 129
    • 16244379573 scopus 로고    scopus 로고
    • Composition of supported model membranes determined by neutron reflection
    • DOI 10.1021/la047389e
    • H.P. Vacklin, F. Tiberg, G. Fragneto, and R.K. Thomas Composition of supported model membranes determined by neutron reflection Langmuir 21 2005 2827 2837 (Pubitemid 40448945)
    • (2005) Langmuir , vol.21 , Issue.7 , pp. 2827-2837
    • Vacklin, H.P.1    Tiberg, F.2    Fragneto, G.3    Thomas, R.K.4
  • 130
    • 0033825470 scopus 로고    scopus 로고
    • Formation of model lipid bilayers at the silica-water interface by co-adsorption with non-ionic dodecyl maltoside surfactant
    • F. Tiberg, I. Harwigsson, and M. Malmsten Formation of model lipid bilayers at the silica-water interface by co-adsorption with non-ionic dodecyl maltoside surfactant Eur Biophys J 29 2000 196 203
    • (2000) Eur Biophys J , vol.29 , pp. 196-203
    • Tiberg, F.1    Harwigsson, I.2    Malmsten, M.3
  • 132
    • 0021947327 scopus 로고
    • Supported phospholipid bilayers
    • L. Tamm, and H. Mc Connell Supported phospholipid bilayers Biophys J 47 1985 105
    • (1985) Biophys J , vol.47 , pp. 105
    • Tamm, L.1    Mc Connell, H.2
  • 133
    • 84869022510 scopus 로고    scopus 로고
    • Lipid rearrangement in DSPC/DMPC bilayers: A neutron reflectometry study
    • Y. Gerelli, L. Porcar, and G. Fragneto Lipid rearrangement in DSPC/DMPC bilayers: a neutron reflectometry study Langmuir 28 2012 28 15933
    • (2012) Langmuir , vol.28 , pp. 28-15933
    • Gerelli, Y.1    Porcar, L.2    Fragneto, G.3
  • 135
    • 84871033812 scopus 로고    scopus 로고
    • Neutrons and model membranes
    • G. Fragneto Neutrons and model membranes Eur Phys J 213 2012 327 342
    • (2012) Eur Phys J , vol.213 , pp. 327-342
    • Fragneto, G.1
  • 136
    • 34249889554 scopus 로고    scopus 로고
    • Nanoscale imaging of domains in supported lipid membranes
    • DOI 10.1021/la070108t
    • L.J. Johnston Nanoscale imaging of domains in supported lipid membranes Langmuir 23 2007 5886 5895 (Pubitemid 46868654)
    • (2007) Langmuir , vol.23 , Issue.11 , pp. 5886-5895
    • Johnston, L.J.1
  • 137
    • 33751400144 scopus 로고    scopus 로고
    • Lipid diffusion in giant unilamellar vesicles is more than 2 times faster than in supported phospholipid bilayers under identical conditions
    • DOI 10.1021/la061934p
    • M. Przybylo, J. Sykora, J. Humpolickova, A. Benda, A. Zan, and M. Hof Lipid diffusion in giant unilamellar vesicles is more than 2 times faster than in supported phospholipid bilayers under identical conditions Langmuir 22 2006 9096 9099 (Pubitemid 44818493)
    • (2006) Langmuir , vol.22 , Issue.22 , pp. 9096-9099
    • Przybylo, M.1    Sykora, J.2    Humpolicova, J.3    Benda, A.4    Zan, A.5    Hof, M.6
  • 138
    • 0141732168 scopus 로고    scopus 로고
    • Swelling of phospholipid floating bilayers: The effect of chain length
    • G. Fragneto, T. Charitat, E. Bellet-Amalric, R. Cubitt, and F. Graner Swelling of phospholipid floating bilayers: the effect of chain length Langmuir 19 2003 7695 7702
    • (2003) Langmuir , vol.19 , pp. 7695-7702
    • Fragneto, G.1    Charitat, T.2    Bellet-Amalric, E.3    Cubitt, R.4    Graner, F.5
  • 139
    • 0029664490 scopus 로고    scopus 로고
    • 2 and glass surfaces with ultrathin dextran films and deposition of lipid bilayers
    • DOI 10.1016/0956-5663(96)83292-1
    • G. Elender, M. Kühner, and E. Sackmann Functionalisation of Si/Si02 and glass surfaces with ultrathin dextran films and deposition of lipid bilayers Biosens Bioelectron 11 1996 565 577 (Pubitemid 26155144)
    • (1996) Biosensors and Bioelectronics , vol.11 , Issue.6-7 , pp. 565-577
    • Elender, G.1    Kuhner, M.2    Sackmann, E.3
  • 140
    • 0033950785 scopus 로고    scopus 로고
    • Supported membranes on soft polymer cushions: Fabrication, characterization and applications
    • DOI 10.1016/S0167-7799(99)01412-2, PII S0167779999014122
    • E. Sackmann, and M. Tanaka Supported membranes on soft polymer cushions: fabrication, characterization and applications Trends Biotechnol 18 2000 58 64 (Pubitemid 30084697)
    • (2000) Trends in Biotechnology , vol.18 , Issue.2 , pp. 58-64
    • Sackmann, E.1    Tanaka, M.2
  • 141
    • 14744306063 scopus 로고    scopus 로고
    • Combined study of X-ray reflectivity and atomic force microscopy on a surface-grafted phospholipid monolayer on a solid
    • DOI 10.1016/j.jcis.2004.09.068, PII S0021979704009993
    • K. Kim, Y. Byun, C. Kim, T. Chul Kim, D. Young Noh, and K. Shin Combined study of X-ray reflectivity and atomic force microscopy on a surface-grafted phospholipid monolayer on a solid J Colloid Interface Sci 284 2005 107 113 (Pubitemid 40332454)
    • (2005) Journal of Colloid and Interface Science , vol.284 , Issue.1 , pp. 107-113
    • Kim, K.1    Byun, Y.2    Kim, C.3    Kim, T.C.4    Noh, D.Y.5    Shin, K.6
  • 142
    • 41849103442 scopus 로고    scopus 로고
    • Floating lipid bilayers deposited on chemically grafted phosphatidylcholine surfaces
    • DOI 10.1021/la702050b
    • A.V. Hughes, J.R. Howse, A. Dabkowska, R.A. Jones, M.J. Lawrence, and S.J. Roser Floating lipid bilayers deposited on chemically grafted phosphatidylcholine surfaces Langmuir 24 2008 1989 1999 (Pubitemid 351500958)
    • (2008) Langmuir , vol.24 , Issue.5 , pp. 1989-1999
    • Hughes, A.V.1    Howse, J.R.2    Dabkowska, A.3    Jones, R.A.L.4    Lawrence, M.J.5    Roser, S.J.6
  • 143
    • 69949171713 scopus 로고    scopus 로고
    • An ion-channel-containing model membrane: Structural determination by magnetic contrast neutron reflectometry
    • S.A. Holt, A.P. Le Brun, C.F. Majkrzak, D.J. McGillivray, F. Heinrich, and M. Lösche et al. An ion-channel-containing model membrane: structural determination by magnetic contrast neutron reflectometry Soft Matter 5 2009 2576 2586
    • (2009) Soft Matter , vol.5 , pp. 2576-2586
    • Holt, S.A.1    Le Brun, A.P.2    Majkrzak, C.F.3    McGillivray, D.J.4    Heinrich, F.5    Lösche, M.6
  • 144
    • 62649144191 scopus 로고    scopus 로고
    • Structure of functional Staphylococcus aureus alpha-hemolysin channels in tethered bilayer lipid membranes
    • D.J. McGillivray, G. Valincius, F. Heinrich, J.W. Robertson, D.J. Vanderah, and W. Febo-Ayala et al. Structure of functional Staphylococcus aureus alpha-hemolysin channels in tethered bilayer lipid membranes Biophys J 96 2009 1547 1553
    • (2009) Biophys J , vol.96 , pp. 1547-1553
    • McGillivray, D.J.1    Valincius, G.2    Heinrich, F.3    Robertson, J.W.4    Vanderah, D.J.5    Febo-Ayala, W.6
  • 146
    • 26944478236 scopus 로고    scopus 로고
    • Polymer-supported membranes as models of the cell surface
    • DOI 10.1038/nature04164, PII N04164
    • M. Tanaka, and E. Sackmann Polymer-supported membranes as models of the cell surface Nature 437 2005 656 663 (Pubitemid 41486528)
    • (2005) Nature , vol.437 , Issue.7059 , pp. 656-663
    • Tanaka, M.1    Sackmann, E.2
  • 147
    • 10344265554 scopus 로고    scopus 로고
    • Oriented attachment and membrane reconstitution of his-tagged cytochrome c oxidase to a gold electrode: In situ monitoring by surface-enhanced infrared absorption spectroscopy
    • DOI 10.1021/ja045951h
    • K. Ataka, F. Giess, W. Knoll, R. Naumann, S. Haber-Pohlmeier, and B. Richter et al. Oriented attachment and membrane reconstitution of his-tagged cytochrome c oxidase to a gold electrode: in situ monitoring by surface-enhanced infrared absorption spectroscopy J Am Chem Soc 126 2004 16199 16206 (Pubitemid 39627631)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.49 , pp. 16199-16206
    • Ataka, K.1    Giess, F.2    Knoll, W.3    Naumann, R.4    Haber-Pohlmeier, S.5    Richter, B.6    Heberle, J.7
  • 148
    • 2442551468 scopus 로고    scopus 로고
    • Supported membranes with well-defined polymer tethers - Incorporation of cell receptors
    • O. Perrucker, A. Förtig, R. Jordan, and M. T Supported membranes with well-defined polymer tethers - incorporation of cell receptors Chem Phys Chem 5 2004 327 335
    • (2004) Chem Phys Chem , vol.5 , pp. 327-335
    • Perrucker, O.1    Förtig, A.2    Jordan, R.3
  • 149
    • 79955378059 scopus 로고    scopus 로고
    • A thethered bilayer assembled on top of immobilized calmodulin to mimic cellular compartmentalization
    • C. Rossi, S. Doumiati, C. Lazzarelli, M. Davi, F. Meddar, and D. Ladant et al. A thethered bilayer assembled on top of immobilized calmodulin to mimic cellular compartmentalization PLoS ONE 6 2011 e19101
    • (2011) PLoS ONE , vol.6 , pp. 19101
    • Rossi, C.1    Doumiati, S.2    Lazzarelli, C.3    Davi, M.4    Meddar, F.5    Ladant, D.6
  • 151
    • 0029975929 scopus 로고    scopus 로고
    • Wild-type Escherichia coli cells regulate the membrane lipid composition in a window between gel and non-lamellar structures
    • S. Morein, A.-S. Andersson, L. Rilfors, and G. Lindblom Wild-type Escherichia coli cells regulate the membrane lipid composition in a window between gel and non-lamellar structures J Biol Chem 271 1996 6801 6809
    • (1996) J Biol Chem , vol.271 , pp. 6801-6809
    • Morein, S.1    Andersson, A.-S.2    Rilfors, L.3    Lindblom, G.4
  • 152
    • 0028869015 scopus 로고
    • Influence of monoglucosyldiacylglycerol and monoacylmonoglucosyldiacylglycerol on the lipid bilayer of the membrane from Acholeplasma laidlawii strain A-EF22
    • A.R. Niemi, L. Rilfors, and G. Lindblom Influence of monoglucosyldiacylglycerol and monoacylmonoglucosyldiacylglycerol on the lipid bilayer of the membrane from Acholeplasma laidlawii strain A-EF22 Biochim Biophys Acta 1239 1995 186 194
    • (1995) Biochim Biophys Acta , vol.1239 , pp. 186-194
    • Niemi, A.R.1    Rilfors, L.2    Lindblom, G.3
  • 153
    • 0036071939 scopus 로고    scopus 로고
    • Regulation of lipid composition in biological membranes - Biophysical studies of lipids and lipid synthesizing enzymes
    • DOI 10.1016/S0927-7765(01)00310-1, PII S0927776501003101
    • L. Rilfors, and G. Lindblom Regulation of lipid composition in biological membranes - biophysical studies of lipids and lipid synthesizing enzymes Colloids Surf B Biointerfaces 26 2002 112 124 (Pubitemid 34792712)
    • (2002) Colloids and Surfaces B: Biointerfaces , vol.26 , Issue.1-2 , pp. 112-124
    • Rilfors, L.1    Lindblom, G.2
  • 154
    • 0019459269 scopus 로고
    • 2H, and diffusion nuclear magnetic resonance measurements
    • DOI 10.1021/bi00507a010
    • A. Wieslander, L. Rilfors, L.B.A. Johansson, and G. Lindblom Reversed cubic phase with membrane glucolipids from acholeplasma-laidlawii - h-1, h-2, and diffusion nuclear magnetic-resonance measurements Biochemistry 20 1981 730 735 (Pubitemid 11097544)
    • (1981) Biochemistry , vol.20 , Issue.4 , pp. 730-735
    • Wieslander, A.1    Rilfors, L.2    Johansson, L.B.A.3    Lindblom, G.4
  • 155
    • 0019317536 scopus 로고
    • Lipid bilayer stability in membranes. Regulation of lipid composition in Acholeplasma laidlawii as governed by molecular shape
    • A. Wieslander, A. Christiansson, L. Rilfors, and G. Lindblom Lipid bilayer stability in membranes. Regulation of lipid composition in Acholeplasma laidlawii as governed by molecular shape Biochemistry 19 1980 3650 3655
    • (1980) Biochemistry , vol.19 , pp. 3650-3655
    • Wieslander, A.1    Christiansson, A.2    Rilfors, L.3    Lindblom, G.4
  • 156
    • 0010461793 scopus 로고    scopus 로고
    • The physical properties of thylakoid membrane lipids and their relation to photosynthesis
    • P.A. Siegenthaler, N. Murata, Kluwer Academic Publishers Dordrecht
    • W.P. Williams The physical properties of thylakoid membrane lipids and their relation to photosynthesis P.A. Siegenthaler, N. Murata, Advances in photosynthesis lipids in photosynthesis 1998 Kluwer Academic Publishers Dordrecht 103 118
    • (1998) Advances in Photosynthesis Lipids in Photosynthesis , pp. 103-118
    • Williams, W.P.1
  • 157
    • 48749149469 scopus 로고
    • Monogalactosyldiacylglycerol: The most abundant polar lipid in nature
    • K. Gounaris, and J. Barner Monogalactosyldiacylglycerol: the most abundant polar lipid in nature Trends Biochem Sci 8 1983 378 381
    • (1983) Trends Biochem Sci , vol.8 , pp. 378-381
    • Gounaris, K.1    Barner, J.2
  • 158
    • 0019886680 scopus 로고
    • The structure and thermotropic properties of pure 1,2- diacylgalactosylglycerols in aqueous systems
    • A. Sen, W.P. Williams, and P.J. Quinn The structure and thermotropic properties of pure 1,2-diacylgalactosylglycerols in aqueous systems Biochim Biophys Acta 663 1981 380 381
    • (1981) Biochim Biophys Acta , vol.663 , pp. 380-381
    • Sen, A.1    Williams, W.P.2    Quinn, P.J.3
  • 159
    • 0019328329 scopus 로고
    • Cytochrome c specifically induces non-bilayer structures in cardiolipin-containing model membranes
    • B. de Kruijff, and P.R. Cullis Cytochrome c specifically induces non-bilayer structures in cardiolipin-containing model membranes Biochim Biophys Acta 602 1980 477 490
    • (1980) Biochim Biophys Acta , vol.602 , pp. 477-490
    • De Kruijff, B.1    Cullis, P.R.2
  • 160
    • 0141919273 scopus 로고    scopus 로고
    • Cytochrome c is reduced mainly by plastoquinol and not by superoxide in thylakoid membranes at low and medium light intensities: Its specific interaction with thylakoid membrane lipids
    • DOI 10.1042/BJ20021820
    • J. Kruk, M. Jemioła-Rzemińska, and K. Strzałka Cytochrome c is reduced mainly by plastoquinol and not by superoxide in thylakoid membranes at low and medium light intensities: its specific interaction with thylakoid membrane lipids Biochem J 375 2003 215 220 (Pubitemid 37255398)
    • (2003) Biochemical Journal , vol.375 , Issue.1 , pp. 215-220
    • Kruk, J.1    Jemiola-Rzeminska, M.2    Strzalka, K.3
  • 161
    • 77957337176 scopus 로고    scopus 로고
    • Cytochrome c-lipid interactions: New insights from resonance energy transfer
    • V.M. Trusova, G.P. Gorbenko, J.G. Molotkovsky, and P.K.J. Kinnunen Cytochrome c-lipid interactions: new insights from resonance energy transfer Biophys J 99 2010 1754 1763
    • (2010) Biophys J , vol.99 , pp. 1754-1763
    • Trusova, V.M.1    Gorbenko, G.P.2    Molotkovsky, J.G.3    Kinnunen, P.K.J.4
  • 162
    • 33744942614 scopus 로고    scopus 로고
    • Cytochrome c interaction with cardiolipin/phosphatidylcholine model membranes: Effect of cardiolipin protonation
    • DOI 10.1529/biophysj.105.080150
    • G.P. Gorbenko, J.G. Molotkovsky, and P.K.J. Kinnunen Cytochrome c interaction with cardiolipin/phosphatidylcholine model membranes: effect of cardiolipin protonation Biophys J 90 2006 4093 4103 (Pubitemid 43846124)
    • (2006) Biophysical Journal , vol.90 , Issue.11 , pp. 4093-4103
    • Gorbenko, G.P.1    Molotkovsky, J.G.2    Kinnunen, P.K.J.3
  • 164
    • 0043007514 scopus 로고    scopus 로고
    • Self-Assembly of Discoidal Phospholipid Bilayer Nanoparticles with Membrane Scaffold Proteins
    • DOI 10.1021/nl025623k
    • T.H. Bayburt, Y.V. Grinkova, and S.G. Sligar Self-assembly of discoidal phospholipid bilayer nanoparticles with membrane scaffold proteins Nano Lett 2 2002 853 856 (Pubitemid 135706448)
    • (2002) Nano Letters , vol.2 , Issue.8 , pp. 853-856
    • Bayburt, T.H.1    Grinkova, Y.V.2    Sligar, S.G.3
  • 165
    • 77951903021 scopus 로고    scopus 로고
    • Membrane proteins assembly into nanodiscs
    • T.H. Bayburt, and S.G. Sligar Membrane proteins assembly into nanodiscs FEBS Lett 584 2009 1721 1727
    • (2009) FEBS Lett , vol.584 , pp. 1721-1727
    • Bayburt, T.H.1    Sligar, S.G.2
  • 166
  • 167
    • 33744928866 scopus 로고    scopus 로고
    • Assembly of single bacteriorhodopsin trimers in bilayer nanodiscs
    • DOI 10.1016/j.abb.2006.03.013, PII S0003986106001093
    • T.H. Bayburt, Y.V. Grinkova, and S.G. Sligar Assembly of single bacteriorhodopsin trimers in bilayer nanodiscs Arch Biochem Biophys 450 2006 215 222 (Pubitemid 43849624)
    • (2006) Archives of Biochemistry and Biophysics , vol.450 , Issue.2 , pp. 215-222
    • Bayburt, T.H.1    Grinkova, Y.V.2    Sligar, S.G.3
  • 168
    • 0042691480 scopus 로고    scopus 로고
    • Direct solubilization of heterologously expressed membrane proteins by incorporation into nanoscale lipid bilayers
    • 55660
    • N.R. Civjan, T.H. Bayburt, M.A. Schuler, and S.G. Sligar Direct solubilization of heterologously expressed membrane proteins by incorporation into nanoscale lipid bilayers Biotechniques 35 556-60 2003 62 63
    • (2003) Biotechniques , vol.35 , pp. 62-63
    • Civjan, N.R.1    Bayburt, T.H.2    Schuler, M.A.3    Sligar, S.G.4
  • 170
    • 84867261080 scopus 로고    scopus 로고
    • Monitoring shifts in the conformation equilibrium of the membrane protein cytochrome P450 reductase (POR) in nanodiscs
    • M. Wadsäter, T. Laursen, A. Singha, N.S. Hatzakis, R. Barker, and K. Mortensen et al. Monitoring shifts in the conformation equilibrium of the membrane protein cytochrome P450 reductase (POR) in nanodiscs J Biol Chem 297 2012 34596 34603
    • (2012) J Biol Chem , vol.297 , pp. 34596-34603
    • Wadsäter, M.1    Laursen, T.2    Singha, A.3    Hatzakis, N.S.4    Barker, R.5    Mortensen, K.6
  • 171
    • 33745511381 scopus 로고    scopus 로고
    • Functional reconstitution of â2-adrenergic receptors utilizing self-assembling nanodisc technology
    • A.J. Leitz, T.H. Bayburt, A.N. Barnakov, B.A. Springer, and S.G. Sligar Functional reconstitution of â2-adrenergic receptors utilizing self-assembling nanodisc technology Biotechniques 40 2006 601 602
    • (2006) Biotechniques , vol.40 , pp. 601-602
    • Leitz, A.J.1    Bayburt, T.H.2    Barnakov, A.N.3    Springer, B.A.4    Sligar, S.G.5
  • 172
    • 70349437270 scopus 로고    scopus 로고
    • The nanodisc: A novel tool for membrane protein studies
    • J. Borch, and T. Hamann The nanodisc: a novel tool for membrane protein studies J Biol Chem 390 2009 805 814
    • (2009) J Biol Chem , vol.390 , pp. 805-814
    • Borch, J.1    Hamann, T.2
  • 173
    • 84874587577 scopus 로고    scopus 로고
    • Effect of phospholipid composition and phase on nanodisc films at the solid-liquid interface as studied by neutron reflectivity
    • M. Wadsäter, R. Barker, K. Mortensen, R. Feidenhans'l, and M. Cárdenas Effect of phospholipid composition and phase on nanodisc films at the solid-liquid interface as studied by neutron reflectivity Langmuir 29 2013 2871 2880
    • (2013) Langmuir , vol.29 , pp. 2871-2880
    • Wadsäter, M.1    Barker, R.2    Mortensen, K.3    Feidenhans'L, R.4    Cárdenas, M.5
  • 174
    • 7244244196 scopus 로고    scopus 로고
    • Lipids do influence protein function - The hydrophobic matching hypothesis revisited
    • DOI 10.1016/j.bbamem.2004.06.009, PII S0005273604001634, Lipid-Protein Interactions
    • M.∅. Jensen, and O.G. Mouritsen Lipids do influence protein function - the hydrophobic matching hypothesis revisited Biochim Biophys Acta 1666 2004 205 226 (Pubitemid 39429479)
    • (2004) Biochimica et Biophysica Acta - Biomembranes , vol.1666 , Issue.1-2 , pp. 205-226
    • Jensen, M.O.1    Mouritsen, O.G.2
  • 176
    • 66249083118 scopus 로고    scopus 로고
    • Emerging roles for lipids in shaping membrane-protein function
    • R. Phillips, T. Ursell, P. Wiggins, and P. Sens Emerging roles for lipids in shaping membrane-protein function Nature 459 2009 379 385
    • (2009) Nature , vol.459 , pp. 379-385
    • Phillips, R.1    Ursell, T.2    Wiggins, P.3    Sens, P.4
  • 177
    • 0032541084 scopus 로고    scopus 로고
    • G Protein-coupled receptors II. Mechanism of agonist activation
    • U. Gether, and B.K. Kobilka G Protein-coupled receptors II. Mechanism of agonist activation J Biol Chem 273 1998 17979 17982
    • (1998) J Biol Chem , vol.273 , pp. 17979-17982
    • Gether, U.1    Kobilka, B.K.2
  • 179
    • 4444297536 scopus 로고    scopus 로고
    • Homotropic cooperativity of monomeric cytochrome P450 3A4 in a nanoscale native bilayer environment
    • DOI 10.1016/j.abb.2004.07.003, PII S0003986104003819
    • B.J. Baas, I.G. Denisov, and S.G. Sligar Homotropiccooperativity of monomeric cytochrome P450 3A4 in a nanoscale native bilayer environment Arch Biochem Biophys 430 2004 218 228 (Pubitemid 39208969)
    • (2004) Archives of Biochemistry and Biophysics , vol.430 , Issue.2 , pp. 218-228
    • Baas, B.J.1    Denisov, I.G.2    Sligar, S.G.3
  • 180
    • 34147112191 scopus 로고    scopus 로고
    • Cooperativity in cytochrome P450 3A4: Linkages in substrate binding, spin state, uncoupling, and product formation
    • DOI 10.1074/jbc.M609589200
    • I.G. Denisov, B.J. Baas, Y.V. Grinkova, and S.G. Sligar Cooperativity in cytochrome P450 3A4: linkages in substrate binding, spin state, uncoupling and product formation J Biol Chem 282 2007 7066 7076 (Pubitemid 47093646)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.10 , pp. 7066-7076
    • Denisov, I.G.1    Baas, B.J.2    Grinkova, Y.V.3    Sligar, S.G.4
  • 182
    • 1642463798 scopus 로고    scopus 로고
    • Co-incorporation of heterologously expressed Arabidopsis cytochrome P450 and P450 reductase into soluble nanoscale lipid bilayers
    • DOI 10.1016/j.abb.2004.02.010, PII S0003986104000633
    • H. Duan, N.R. Civjan, S.G. Sligar, and M.A. Schuler Co-incorporation of heterologously expressed Arabidopsis cytochrome P450 and P450 reductase into soluble nanoscale lipid bilayers Arch Biochem Biophys 424 2004 141 153 (Pubitemid 38401947)
    • (2004) Archives of Biochemistry and Biophysics , vol.424 , Issue.2 , pp. 141-153
    • Duan, H.1    Civjan, N.R.2    Sligar, S.G.3    Schuler, M.A.4
  • 183
    • 84877012043 scopus 로고
    • The maltose ABC transporter: Action of membrane lipids on the transporter stability, coupling and ATPase activity
    • H. Bao, K. Dalal, V. Wang, I. Rouiller, and F. Duong The maltose ABC transporter: action of membrane lipids on the transporter stability, coupling and ATPase activity Biochim Biophys Acta 2013 1828 1723 1730
    • (1828) Biochim Biophys Acta , vol.2013 , pp. 1723-1730
    • Bao, H.1    Dalal, K.2    Wang, V.3    Rouiller, I.4    Duong, F.5
  • 184
    • 77954643681 scopus 로고    scopus 로고
    • Functional reconstitution of an ABC transporter in nanodiscs for use in electron paramagnetic resonance spectroscopy
    • F.J.D. Alvarez, C. Orelle, and A.L. Davidson Functional reconstitution of an ABC transporter in nanodiscs for use in electron paramagnetic resonance spectroscopy J Am Chem Soc 132 2010 9513 9515
    • (2010) J Am Chem Soc , vol.132 , pp. 9513-9515
    • Alvarez, F.J.D.1    Orelle, C.2    Davidson, A.L.3
  • 185
    • 78649688361 scopus 로고    scopus 로고
    • Direct observation of stepped proteolipid ring rotation in E. Coli FoF1-ATP synthase
    • R. Ishmukhametov, T. Hornung, and D. Spetzler Direct observation of stepped proteolipid ring rotation in E. coli FoF1-ATP synthase EMBO J 29 2010 3911 3923
    • (2010) EMBO J , vol.29 , pp. 3911-3923
    • Ishmukhametov, R.1    Hornung, T.2    Spetzler, D.3
  • 186
    • 80655125018 scopus 로고    scopus 로고
    • Conformational analysis of human ATP-binding cassette transporter ABCB1 in lipid nanodiscs and inhibition by the antibodies MRK16 and UIC2
    • T.K. Ritchie, H. Kwon, and W.M. Atkins Conformational analysis of human ATP-binding cassette transporter ABCB1 in lipid nanodiscs and inhibition by the antibodies MRK16 and UIC2 J Biol Chem 286 2011 39489 39496
    • (2011) J Biol Chem , vol.286 , pp. 39489-39496
    • Ritchie, T.K.1    Kwon, H.2    Atkins, W.M.3
  • 187
    • 80855144109 scopus 로고    scopus 로고
    • Catalytic activity of MsbA reconstituted in nanodisc particles is modulated by remote interactions with the bilayer
    • T. Kawai, J.M.M. Caaveiro, R. Abe, T. Katagiri, and K. Tsumoto Catalytic activity of MsbA reconstituted in nanodisc particles is modulated by remote interactions with the bilayer FEBS Lett 585 2011 3533 3537
    • (2011) FEBS Lett , vol.585 , pp. 3533-3537
    • Kawai, T.1    Caaveiro, J.M.M.2    Abe, R.3    Katagiri, T.4    Tsumoto, K.5
  • 189
    • 84875771594 scopus 로고    scopus 로고
    • Isolation of monodisperse nanodisc-reconstituted membrane proteins using free flow electrophoresis
    • B.H. Justesen, T. Laursen, G. Weber, A.T. Fuglsang, B.L. Møller, and Pomorski T. Günther Isolation of monodisperse nanodisc-reconstituted membrane proteins using free flow electrophoresis Anal Chem 85 2013 3497 3500
    • (2013) Anal Chem , vol.85 , pp. 3497-3500
    • Justesen, B.H.1    Laursen, T.2    Weber, G.3    Fuglsang, A.T.4    Møller, B.L.5    Günther, P.T.6
  • 190
    • 84856228232 scopus 로고    scopus 로고
    • Ultra-thin layer MALDI mass spectrometry of membrane proteins in nanodiscs
    • M.T. Marty, A. Das, and S.G. Sligar Ultra-thin layer MALDI mass spectrometry of membrane proteins in nanodiscs Anal Bioanal Chem 402 2012 721 729
    • (2012) Anal Bioanal Chem , vol.402 , pp. 721-729
    • Marty, M.T.1    Das, A.2    Sligar, S.G.3
  • 191
    • 84873339680 scopus 로고    scopus 로고
    • The effect of using binary mixtures of zwitterionic and charged lipids on the nanodisc formation and stability
    • M. Wadsäter, M. Selma, J. Simonsen, K. Mortensen, and M. Cárdenas The effect of using binary mixtures of zwitterionic and charged lipids on the nanodisc formation and stability Soft Matter 9 2013 2329 2337
    • (2013) Soft Matter , vol.9 , pp. 2329-2337
    • Wadsäter, M.1    Selma, M.2    Simonsen, J.3    Mortensen, K.4    Cárdenas, M.5
  • 192
    • 33646362534 scopus 로고    scopus 로고
    • Asymmetric distribution of phosphatidyl serine in supported phospholipid bilayers on titanium dioxide
    • DOI 10.1021/la053000r
    • F. Rossetti, M. Textor, and I. Reviakine Asymmetric distribution of phosphatidyl serine in supported phospholipid bilayers on titanium dioxide Langmuir 22 2006 3467 3473 (Pubitemid 43672509)
    • (2006) Langmuir , vol.22 , Issue.8 , pp. 3467-3473
    • Rossetti, F.F.1    Textor, M.2    Reviakine, I.3
  • 195
    • 78651257243 scopus 로고    scopus 로고
    • Asymmetric GUVs prepared by Mbeta CD-mediated lipid exchange: An FCS study
    • S. Chiantia, P. Schwille, A.S. Klymchenko, and E. London Asymmetric GUVs prepared by Mbeta CD-mediated lipid exchange: an FCS study Biophys J 100 2011 LO1 LO3
    • (2011) Biophys J , vol.100
    • Chiantia, S.1    Schwille, P.2    Klymchenko, A.S.3    London, E.4
  • 196
    • 38349184772 scopus 로고    scopus 로고
    • Tuning lipid mixtures to induce or suppress domain formation across leaflets of unsupported asymmetric bilayers
    • M.D. Collins, and S.L. Keller Tuning lipid mixtures to induce or suppress domain formation across leaflets of unsupported asymmetric bilayers Proc Natl Acad Sci U S A 105 2008 124 128
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 124-128
    • Collins, M.D.1    Keller, S.L.2
  • 197
    • 79960286601 scopus 로고    scopus 로고
    • Observation of inhomogeneity in the lipid composition of individual nanoscale liposomes
    • J. Larsen, N.S. Hatzakis, and D. Stamou Observation of inhomogeneity in the lipid composition of individual nanoscale liposomes J Am Chem Soc 133 2011 10685 10687
    • (2011) J Am Chem Soc , vol.133 , pp. 10685-10687
    • Larsen, J.1    Hatzakis, N.S.2    Stamou, D.3
  • 198
    • 79957492827 scopus 로고    scopus 로고
    • Surfactant-free purification of membrane proteins with intact native membrane environment
    • M. Jamshad, Y.P. Lin, T.J. Knowles, R.A. Parslow, C. Harris, and M. Wheathley et al. Surfactant-free purification of membrane proteins with intact native membrane environment Biochem Soc Trans 39 2011 813 818
    • (2011) Biochem Soc Trans , vol.39 , pp. 813-818
    • Jamshad, M.1    Lin, Y.P.2    Knowles, T.J.3    Parslow, R.A.4    Harris, C.5    Wheathley, M.6
  • 199
    • 67650541090 scopus 로고    scopus 로고
    • Membrane proteins solubilized intact in lipid containing nanoparticles bounded by styrene maleic acid copolymer
    • T.J. Knowles, R. Finka, C. Smith, Y.P. Lin, T. Dafforn, and M. Overduin Membrane proteins solubilized intact in lipid containing nanoparticles bounded by styrene maleic acid copolymer J Am Chem Soc 131 2009 7484 7485
    • (2009) J Am Chem Soc , vol.131 , pp. 7484-7485
    • Knowles, T.J.1    Finka, R.2    Smith, C.3    Lin, Y.P.4    Dafforn, T.5    Overduin, M.6
  • 200
    • 84889375828 scopus 로고    scopus 로고
    • Simulations and models of lipid bilayers
    • Wiley-VCH Verlag GmbH & Co. KGaA
    • S.A. Pandit, and H.L. Scott Simulations and models of lipid bilayers Soft Matter 2009 Wiley-VCH Verlag GmbH & Co. KGaA 1 82
    • (2009) Soft Matter , pp. 1-82
    • Pandit, S.A.1    Scott, H.L.2
  • 201
    • 36549043460 scopus 로고    scopus 로고
    • Model membrane systems and their applications
    • DOI 10.1016/j.cbpa.2007.09.020, PII S1367593107001457, Model Systems/Bioplymers
    • Y.H. Chan, and S.G. Boxer Model membrane systems and their applications Curr Opin Chem Biol 11 2007 581 587 (Pubitemid 350180578)
    • (2007) Current Opinion in Chemical Biology , vol.11 , Issue.6 , pp. 581-587
    • Chan, Y.-H.M.1    Boxer, S.G.2
  • 202
    • 38949115007 scopus 로고    scopus 로고
    • Atomistic and coarse-grained computer simulations of raft-like lipid mixtures
    • T. McIntosh, Humana Press [Chapter 19]
    • S. Pandit, and H.L. Scott Atomistic and coarse-grained computer simulations of raft-like lipid mixtures T. McIntosh, Lipid rafts vol. 398 2007 Humana Press 283 302 [Chapter 19]
    • (2007) Lipid Rafts , vol.398 , pp. 283-302
    • Pandit, S.1    Scott, H.L.2
  • 203
    • 84859768063 scopus 로고    scopus 로고
    • A simulation study of the self-assembly of coarse-grained skin lipids
    • K.R. Hadley, and Cabe C. Mc A simulation study of the self-assembly of coarse-grained skin lipids Soft Matter 8 2012 4802 4814
    • (2012) Soft Matter , vol.8 , pp. 4802-4814
    • Hadley, K.R.1    Mc, C.C.2
  • 204
    • 38549168897 scopus 로고    scopus 로고
    • Coarse-grained molecular dynamics simulations of phase transitions in mixed lipid systems containing LPA, DOPA, and DOPE lipids
    • E.R. May, D.I. Kopelevich, and A. Narang Coarse-grained molecular dynamics simulations of phase transitions in mixed lipid systems containing LPA, DOPA, and DOPE lipids Biophys J 94 2008 878 890
    • (2008) Biophys J , vol.94 , pp. 878-890
    • May, E.R.1    Kopelevich, D.I.2    Narang, A.3
  • 205
    • 34249325178 scopus 로고    scopus 로고
    • Aggregation and vesiculation of membrane proteins by curvature-mediated interactions
    • DOI 10.1038/nature05840, PII NATURE05840
    • B.J. Reynwar, G. Illya, V.A. Harmandaris, M.M. Müller, K. Kremer, and M. Deserno Aggregation and vesiculation of membrane proteins by curvature-mediated interactions Nature 447 2007 461 464 (Pubitemid 46816743)
    • (2007) Nature , vol.447 , Issue.7143 , pp. 461-464
    • Reynwar, B.J.1    Illya, G.2    Harmandaris, V.A.3    Muller, M.M.4    Kremer, K.5    Deserno, M.6
  • 206
    • 84862530752 scopus 로고    scopus 로고
    • Mesoscale simulations of curvature-inducing protein partitioning on lipid bilayer membranes in the presence of mean curvature fields
    • J. Liu, R. Tourdot, V. Ramanan, N.J. Agrawal, and R. Radhakrishanan Mesoscale simulations of curvature-inducing protein partitioning on lipid bilayer membranes in the presence of mean curvature fields Mol Phys 110 2012 1127 1137
    • (2012) Mol Phys , vol.110 , pp. 1127-1137
    • Liu, J.1    Tourdot, R.2    Ramanan, V.3    Agrawal, N.J.4    Radhakrishanan, R.5
  • 207
    • 77951903021 scopus 로고    scopus 로고
    • Membrane protein assembly into nanodiscs
    • T.H. Bayburt, and S.G. Sligar Membrane protein assembly into nanodiscs FEBS Lett 584 2010 1721 1727
    • (2010) FEBS Lett , vol.584 , pp. 1721-1727
    • Bayburt, T.H.1    Sligar, S.G.2


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