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Volumn 48, Issue C, 1999, Pages 23-47

Chapter 2 Structure and Physical Properties of the Lipid Membrane

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EID: 77956668934     PISSN: 00702161     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0070-2161(08)61040-0     Document Type: Article
Times cited : (13)

References (226)
  • 1
    • 0025272239 scopus 로고
    • Membrane contact, fusion, and hexagonal phase transitions in PE liposomes
    • Allen T.M., Hong K., and Papahadjopoulos D. Membrane contact, fusion, and hexagonal phase transitions in PE liposomes. Biochemistry 29 (1990) 2976-2985
    • (1990) Biochemistry , vol.29 , pp. 2976-2985
    • Allen, T.M.1    Hong, K.2    Papahadjopoulos, D.3
  • 2
    • 0026748426 scopus 로고
    • Role of lysophatidyl-choline in T-lymphocyte activation: Involvement of phospholipase A2 in signal transduction through protein kinase C
    • Asaoka Y., Oka M., Yoshida K., Sasaki Y., and Nishizuka Y. Role of lysophatidyl-choline in T-lymphocyte activation: Involvement of phospholipase A2 in signal transduction through protein kinase C. Proc. Natl. Acad. Sci. U.S.A. 89 (1992) 6447-6451
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 6447-6451
    • Asaoka, Y.1    Oka, M.2    Yoshida, K.3    Sasaki, Y.4    Nishizuka, Y.5
  • 4
    • 0021882555 scopus 로고
    • Effects of lipid environment on the light-induced conformational changes of rhodopsin
    • Baldwin P.A., and Hubbell W.L. Effects of lipid environment on the light-induced conformational changes of rhodopsin. Biochemistry 24 (1985) 2633-2639
    • (1985) Biochemistry , vol.24 , pp. 2633-2639
    • Baldwin, P.A.1    Hubbell, W.L.2
  • 5
    • 0025779369 scopus 로고
    • Extensive segregation of acidic phospholipids in membranes induced by protein Kinase C and related proteins
    • Bazzi M.D., and Nelsestuen G.L. Extensive segregation of acidic phospholipids in membranes induced by protein Kinase C and related proteins. Biochemistry 30 (1991) 7961-7969
    • (1991) Biochemistry , vol.30 , pp. 7961-7969
    • Bazzi, M.D.1    Nelsestuen, G.L.2
  • 6
    • 0026525339 scopus 로고
    • Importance of phosphatidylethanolamine for association of protein kinase C and other cytoplasmic proteins with membranes
    • Bazzi M.D., Youakim M.A., and Nelsestuen G.L. Importance of phosphatidylethanolamine for association of protein kinase C and other cytoplasmic proteins with membranes. Biochemistry 31 (1992) 1125-1144
    • (1992) Biochemistry , vol.31 , pp. 1125-1144
    • Bazzi, M.D.1    Youakim, M.A.2    Nelsestuen, G.L.3
  • 8
    • 0022115523 scopus 로고
    • On the correlation between HII phase and the contact-induced destabilization of phosphatidylethanolamine-containing membranes
    • Bentz J., Ellens H., Lai M.-Z., and Szoka F.C. On the correlation between HII phase and the contact-induced destabilization of phosphatidylethanolamine-containing membranes. Proc. Natl. Acad. Sci. U.S.A. 82 (1985) 5742-5745
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 5742-5745
    • Bentz, J.1    Ellens, H.2    Lai, M.-Z.3    Szoka, F.C.4
  • 9
    • 0017396017 scopus 로고
    • Topological asymmetry of phospholipids in membranes
    • Bergelson L.D., and Barsukov L.I. Topological asymmetry of phospholipids in membranes. Science 197 (1977) 224-230
    • (1977) Science , vol.197 , pp. 224-230
    • Bergelson, L.D.1    Barsukov, L.I.2
  • 11
    • 0024453294 scopus 로고
    • Inositol phosphates and cell signalling
    • Berridge M.J., and Irvine R.F. Inositol phosphates and cell signalling. Nature (London) 341 (1989) 197-205
    • (1989) Nature (London) , vol.341 , pp. 197-205
    • Berridge, M.J.1    Irvine, R.F.2
  • 12
    • 0000479632 scopus 로고
    • Modulation of protein function by lipids
    • Bienvenue A., and Marie J.S. Modulation of protein function by lipids. Curr. Top. Membr. 40 (1994) 319-354
    • (1994) Curr. Top. Membr. , vol.40 , pp. 319-354
    • Bienvenue, A.1    Marie, J.S.2
  • 13
    • 0025993884 scopus 로고
    • Physical properties of the fluid-bilayer component of cell membranes: A perspective
    • Bloom M., Evans E., and Mouritsen O.G. Physical properties of the fluid-bilayer component of cell membranes: A perspective. Q. Rev. Biophys. 24 (1991) 293-397
    • (1991) Q. Rev. Biophys. , vol.24 , pp. 293-397
    • Bloom, M.1    Evans, E.2    Mouritsen, O.G.3
  • 14
  • 16
    • 0028124422 scopus 로고
    • Modulation of rhodopsin function by properties of the membrane bilayer
    • Brown M.F. Modulation of rhodopsin function by properties of the membrane bilayer. Chem. Phys. Lipids 73 (1994) 159-180
    • (1994) Chem. Phys. Lipids , vol.73 , pp. 159-180
    • Brown, M.F.1
  • 17
    • 0017927954 scopus 로고
    • Neutron diffraction studies on selectively deuterated phospholipid bilayers
    • Buldt G., Gally H.U., Seelig A., Seelig J., and Zaccai G. Neutron diffraction studies on selectively deuterated phospholipid bilayers. Nature (London) 271 (1978) 182-184
    • (1978) Nature (London) , vol.271 , pp. 182-184
    • Buldt, G.1    Gally, H.U.2    Seelig, A.3    Seelig, J.4    Zaccai, G.5
  • 18
    • 0018792901 scopus 로고
    • Neutron diffraction studies on phosphatidylcholine model membranes. I. Head group conformation
    • Buldt G., Gally H.U., Seelig J., and Zaccai G. Neutron diffraction studies on phosphatidylcholine model membranes. I. Head group conformation. J. Mol. Biol. 134 (1979) 673-691
    • (1979) J. Mol. Biol. , vol.134 , pp. 673-691
    • Buldt, G.1    Gally, H.U.2    Seelig, J.3    Zaccai, G.4
  • 19
    • 0018799289 scopus 로고
    • Fatty acid composition and thermal behavior of natural sphingomyelins
    • Calhoun W.I., and Shipley G.G. Fatty acid composition and thermal behavior of natural sphingomyelins. Biochim. Biophys. Acta 555 (1979) 436-441
    • (1979) Biochim. Biophys. Acta , vol.555 , pp. 436-441
    • Calhoun, W.I.1    Shipley, G.G.2
  • 20
    • 0018405887 scopus 로고
    • Sphingomyelin-lecithin bilayers and interaction with cholesterol
    • Calhoun W.J., and Shipley G.G. Sphingomyelin-lecithin bilayers and interaction with cholesterol. Biochemistry 18 (1979) 1717-1722
    • (1979) Biochemistry , vol.18 , pp. 1717-1722
    • Calhoun, W.J.1    Shipley, G.G.2
  • 21
    • 0345079373 scopus 로고
    • Membrane proteins and membrane structure
    • Capaldi R.A., and Green D.E. Membrane proteins and membrane structure. FEES Lett. 25 (1972) 205-209
    • (1972) FEES Lett. , vol.25 , pp. 205-209
    • Capaldi, R.A.1    Green, D.E.2
  • 22
    • 0015220790 scopus 로고
    • Myelin membrane structure at 10 Å resolution
    • Caspar D.L.D., and Kirschner D.A. Myelin membrane structure at 10 Å resolution. Nature (London) 231 (1971) 46-52
    • (1971) Nature (London) , vol.231 , pp. 46-52
    • Caspar, D.L.D.1    Kirschner, D.A.2
  • 23
    • 0027427634 scopus 로고
    • Electrostatic characterization of liposomes
    • Cevc G. Electrostatic characterization of liposomes. Chem. Phys. Lipids 64 (1993) 163-186
    • (1993) Chem. Phys. Lipids , vol.64 , pp. 163-186
    • Cevc, G.1
  • 24
    • 0016192567 scopus 로고
    • Biomembrane phase transitions. Studies of lipid-water systems using differential scanning calorimetry
    • Chapman D., Urbina J., and Keogh K.M. Biomembrane phase transitions. Studies of lipid-water systems using differential scanning calorimetry. J. Biol. Chem. 249 (1974) 2512-2521
    • (1974) J. Biol. Chem. , vol.249 , pp. 2512-2521
    • Chapman, D.1    Urbina, J.2    Keogh, K.M.3
  • 25
    • 0001482027 scopus 로고
    • Scanning calorimetric evidence for a third phase transition in PC bilayers
    • Chen S.C., Sturtevant J.M., and Gaffney B.J. Scanning calorimetric evidence for a third phase transition in PC bilayers. Proc. Natl. Acad. Sci. U.S.A. 77 (1980) 5060-5063
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 5060-5063
    • Chen, S.C.1    Sturtevant, J.M.2    Gaffney, B.J.3
  • 26
    • 77956698602 scopus 로고
    • Acid-induced fusion of liposomes
    • Plenum, New York
    • Conner J., and Huang L. Acid-induced fusion of liposomes. Cell Fusion. (1987), Plenum, New York
    • (1987) Cell Fusion.
    • Conner, J.1    Huang, L.2
  • 27
    • 0015524748 scopus 로고
    • Lamellar structure of bleached and unbleached rod photoreceptor membranes
    • Corless J.M. Lamellar structure of bleached and unbleached rod photoreceptor membranes. Nature (London) 237 (1972) 229-231
    • (1972) Nature (London) , vol.237 , pp. 229-231
    • Corless, J.M.1
  • 28
    • 0017871649 scopus 로고
    • Measurement of repulsive forces between charged phospholipid bilayers
    • Cowley A.C., Fuller N.L., Rand R.P., and Parsegian V.A. Measurement of repulsive forces between charged phospholipid bilayers. Biochemistry 17 (1978) 3163-3168
    • (1978) Biochemistry , vol.17 , pp. 3163-3168
    • Cowley, A.C.1    Fuller, N.L.2    Rand, R.P.3    Parsegian, V.A.4
  • 29
    • 0017862842 scopus 로고
    • Polymorphic phase behaviour of lipid mixtures as detected by 31P-NMR. Evidence that cholesterol may destabilize bilayer structure in membrane systems containing PE
    • Cullis P.R., and DeKruijff B. Polymorphic phase behaviour of lipid mixtures as detected by 31P-NMR. Evidence that cholesterol may destabilize bilayer structure in membrane systems containing PE. Biochim. Biophys. Acta 507 (1978) 207-218
    • (1978) Biochim. Biophys. Acta , vol.507 , pp. 207-218
    • Cullis, P.R.1    DeKruijff, B.2
  • 30
    • 0018133922 scopus 로고
    • The polymorphic phase behavior of PEs of natural and synthetic origin
    • Cullis P.R., and DeKruijff B. The polymorphic phase behavior of PEs of natural and synthetic origin. Biochim. Biophys. Acta 513 (1978) 31-42
    • (1978) Biochim. Biophys. Acta , vol.513 , pp. 31-42
    • Cullis, P.R.1    DeKruijff, B.2
  • 31
    • 0018797519 scopus 로고
    • Lipid polymorphism and the functional roles of lipids in biological membranes
    • Cullis P.R., and DeKruijff B. Lipid polymorphism and the functional roles of lipids in biological membranes. Biochim. Biophys. Acta 559 (1979) 399-420
    • (1979) Biochim. Biophys. Acta , vol.559 , pp. 399-420
    • Cullis, P.R.1    DeKruijff, B.2
  • 33
    • 0023663511 scopus 로고
    • The physical properties of glycolipids
    • Curatolo W. The physical properties of glycolipids. Biochim. Biophys. Acta 906 (1987) 111-136
    • (1987) Biochim. Biophys. Acta , vol.906 , pp. 111-136
    • Curatolo, W.1
  • 35
    • 0022356526 scopus 로고
    • Phase behavior of galactocerebrosides from bovine brain
    • Curatolo W., and Jungalwala F.B. Phase behavior of galactocerebrosides from bovine brain. Biochemistry 24 (1985) 6608-6613
    • (1985) Biochemistry , vol.24 , pp. 6608-6613
    • Curatolo, W.1    Jungalwala, F.B.2
  • 36
    • 0017387564 scopus 로고
    • Phase behavior and structural characteristics of hydrated bovine brain gangliosides
    • Curatolo W., Small D.M., and Shipley G.G. Phase behavior and structural characteristics of hydrated bovine brain gangliosides. Biochim. Biophys. Acta 468 (1977) 11-20
    • (1977) Biochim. Biophys. Acta , vol.468 , pp. 11-20
    • Curatolo, W.1    Small, D.M.2    Shipley, G.G.3
  • 37
    • 0000954302 scopus 로고
    • A contribution to the theory of permeability of thin films
    • Danielli J.F., and Davson J. A contribution to the theory of permeability of thin films. J. Cell. Comp. Physiol. 5 (1935) 495-508
    • (1935) J. Cell. Comp. Physiol. , vol.5 , pp. 495-508
    • Danielli, J.F.1    Davson, J.2
  • 39
    • 0029994378 scopus 로고    scopus 로고
    • Endocytosis of GPI-anchored proteins in human lymphocytes: Role of glycolipid-based domains, actin cytoskeleton, and protein kinases
    • Deckert M., Ticchioni M., and Bernard A. Endocytosis of GPI-anchored proteins in human lymphocytes: Role of glycolipid-based domains, actin cytoskeleton, and protein kinases. J. Cell Biol. 133 (1996) 791-799
    • (1996) J. Cell Biol. , vol.133 , pp. 791-799
    • Deckert, M.1    Ticchioni, M.2    Bernard, A.3
  • 40
    • 0027958915 scopus 로고
    • Maintenance and consequences of membrane phospholipid asymmetry
    • Devaux P.F., and Zachowski A. Maintenance and consequences of membrane phospholipid asymmetry. Chem. Phys. Lipids 73 (1994) 107-120
    • (1994) Chem. Phys. Lipids , vol.73 , pp. 107-120
    • Devaux, P.F.1    Zachowski, A.2
  • 41
    • 0023415590 scopus 로고
    • Electron diffraction structure analysis of phospholipids
    • Dorset D.L. Electron diffraction structure analysis of phospholipids. J. Electron Microsc. Tech. 7 (1987) 35-46
    • (1987) J. Electron Microsc. Tech. , vol.7 , pp. 35-46
    • Dorset, D.L.1
  • 42
    • 0023142385 scopus 로고
    • Molecular packing of a crystalline ether-linked phosphatidylcholine an electron diffraction study
    • Dorset D.L. Molecular packing of a crystalline ether-linked phosphatidylcholine an electron diffraction study. Biochim. Biophys. Acta 898 (1987) 121-128
    • (1987) Biochim. Biophys. Acta , vol.898 , pp. 121-128
    • Dorset, D.L.1
  • 43
    • 0025041634 scopus 로고
    • Lamellar packing of a chiral N,N-dimethylphosphatidylethanolamine: Electron diffraction. Evidence for a lecithin-type headgroup conformation
    • Dorset D.L., and Zhang W. Lamellar packing of a chiral N,N-dimethylphosphatidylethanolamine: Electron diffraction. Evidence for a lecithin-type headgroup conformation. Biochim. Biophys. Acta 1028 (1990) 299-303
    • (1990) Biochim. Biophys. Acta , vol.1028 , pp. 299-303
    • Dorset, D.L.1    Zhang, W.2
  • 44
    • 0030957823 scopus 로고    scopus 로고
    • Molecular basis for membrane phospholipid diversity: Why are there so many lipids?
    • Dowhan W. Molecular basis for membrane phospholipid diversity: Why are there so many lipids?. Annu. Rev. Biochem. 66 (1997) 199-232
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 199-232
    • Dowhan, W.1
  • 45
    • 0015805129 scopus 로고
    • Molecular organization in the sarcoplasmic reticulum membrane studied by X-ray diffraction
    • Dupont Y., Harrison S.C., and Hasselbach W. Molecular organization in the sarcoplasmic reticulum membrane studied by X-ray diffraction. Nutiire (London) 244 (1973) 555-558
    • (1973) Nutiire (London) , vol.244 , pp. 555-558
    • Dupont, Y.1    Harrison, S.C.2    Hasselbach, W.3
  • 46
    • 38249038603 scopus 로고
    • The role of the interface in the nonlocal electrostatic theory of hydration force
    • Dzhavakhidze P.G., Kornyshev A.A., and Levadny V.G. The role of the interface in the nonlocal electrostatic theory of hydration force. Phys. Lett. A 118 (1986) 203-208
    • (1986) Phys. Lett. A , vol.118 , pp. 203-208
    • Dzhavakhidze, P.G.1    Kornyshev, A.A.2    Levadny, V.G.3
  • 49
    • 0025021620 scopus 로고
    • Hydrogen bonding and the thermotropic transitions of phosphatidylethanolamines
    • Epand R.M. Hydrogen bonding and the thermotropic transitions of phosphatidylethanolamines. Chem. Phys. Lipids 52 (1990) 227-230
    • (1990) Chem. Phys. Lipids , vol.52 , pp. 227-230
    • Epand, R.M.1
  • 50
    • 0026224081 scopus 로고
    • Entropy-driven tension in vesicle membranes and unbinding of adherent vesicles
    • Evans E. Entropy-driven tension in vesicle membranes and unbinding of adherent vesicles. Lungmuir 7 (1991) 1900-1908
    • (1991) Lungmuir , vol.7 , pp. 1900-1908
    • Evans, E.1
  • 51
    • 0017342853 scopus 로고
    • A solid-liquid composite model of the red cell membranes
    • Evans E.A., and Hochmuth R.M. A solid-liquid composite model of the red cell membranes. J. Membr. Biol. 30 (1977) 351-379
    • (1977) J. Membr. Biol. , vol.30 , pp. 351-379
    • Evans, E.A.1    Hochmuth, R.M.2
  • 52
    • 33845281853 scopus 로고
    • Physical properties of surfactant bilayer membranes: Thermal transitions, elasticity, rigidity, cohesion, and colloidal interactions
    • Evans E., and Needham D. Physical properties of surfactant bilayer membranes: Thermal transitions, elasticity, rigidity, cohesion, and colloidal interactions. J. Phys. Chem. 91 (1987) 4219-4228
    • (1987) J. Phys. Chem. , vol.91 , pp. 4219-4228
    • Evans, E.1    Needham, D.2
  • 53
    • 0001170048 scopus 로고
    • Thermal-mechanical fluctuations enhance repulsion between bimolecular layers
    • Evans E.A., and Parsegian V.A. Thermal-mechanical fluctuations enhance repulsion between bimolecular layers. Proc. Natl. Acad. Sci. U.S.A. 83 (1986) 7132-7136
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 7132-7136
    • Evans, E.A.1    Parsegian, V.A.2
  • 54
    • 0018538681 scopus 로고
    • Mechanics and thermodynamics of biomembranes: Part 2
    • CRC Press, Boca Raton, Florida
    • Evans E.A., and Skalak R. Mechanics and thermodynamics of biomembranes: Part 2. CRC Critical Reviews in Bioengineering. (1979), CRC Press, Boca Raton, Florida
    • (1979) CRC Critical Reviews in Bioengineering.
    • Evans, E.A.1    Skalak, R.2
  • 55
    • 0018538681 scopus 로고
    • Mechanics and Thermodynamics of Biomembranes: Part 1
    • CRC Press, Boca Raton, Florida
    • Evans E.A., and Skalak R. Mechanics and Thermodynamics of Biomembranes: Part 1. CRC Critical Reviews in Bioengineering. (1979), CRC Press, Boca Raton, Florida
    • (1979) CRC Critical Reviews in Bioengineering.
    • Evans, E.A.1    Skalak, R.2
  • 56
    • 0022342832 scopus 로고
    • Glycosyl-sn-1.2-dimyristoylphosphatidylinositol is covalently linked to Trypanosome brucei variant surface glycoprotein
    • Fergusun M.A.J., Low M.G., and Cross G.A.M. Glycosyl-sn-1.2-dimyristoylphosphatidylinositol is covalently linked to Trypanosome brucei variant surface glycoprotein. J. Biol. Chem. 260 (1985) 14547-14555
    • (1985) J. Biol. Chem. , vol.260 , pp. 14547-14555
    • Fergusun, M.A.J.1    Low, M.G.2    Cross, G.A.M.3
  • 57
    • 0011888116 scopus 로고
    • The determination of the Fourier transform of the myelin layer from a study of the swelling phenomena
    • Finean J.B., and Burge R.E. The determination of the Fourier transform of the myelin layer from a study of the swelling phenomena. J. Mol. Biol. 7 (1963) 672
    • (1963) J. Mol. Biol. , vol.7 , pp. 672
    • Finean, J.B.1    Burge, R.E.2
  • 58
    • 0017230777 scopus 로고
    • Structural analysis of hydrated egg lecithin and cholesterol bilayers I. X-ray diffraction
    • Franks N.P. Structural analysis of hydrated egg lecithin and cholesterol bilayers I. X-ray diffraction. J. Mol. Biol. 100 (1976) 345-358
    • (1976) J. Mol. Biol. , vol.100 , pp. 345-358
    • Franks, N.P.1
  • 59
    • 0018280201 scopus 로고
    • A direct method for determination of membrane electron density profiles on an absolute scale
    • Franks N.P., Arunachalam T., and Caspi E. A direct method for determination of membrane electron density profiles on an absolute scale. Nature (London) 276 (1978) 530-532
    • (1978) Nature (London) , vol.276 , pp. 530-532
    • Franks, N.P.1    Arunachalam, T.2    Caspi, E.3
  • 61
    • 0031057288 scopus 로고    scopus 로고
    • Lipid biochemistry: Functions of glycerolipids and sphingolipids in cellular signaling
    • Ghosh S., Strum J.C., and Bell R.M. Lipid biochemistry: Functions of glycerolipids and sphingolipids in cellular signaling. FASEB J. 11 (1997) 45-50
    • (1997) FASEB J. , vol.11 , pp. 45-50
    • Ghosh, S.1    Strum, J.C.2    Bell, R.M.3
  • 65
    • 0022080948 scopus 로고
    • Intrinsic curvature hypothesis for biomembrane lipid composition: A role for non-bilayer lipids
    • Gruner S.M. Intrinsic curvature hypothesis for biomembrane lipid composition: A role for non-bilayer lipids. Proc. Natl. Acad. Sci. U.S.A. 82 (1985) 3665-3669
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 3665-3669
    • Gruner, S.M.1
  • 66
    • 0011847313 scopus 로고
    • Stability of lyotropic phases with curved interfaces
    • Gruner S.M. Stability of lyotropic phases with curved interfaces. J. Phys. Chem. 93 (1989) 7562-7570
    • (1989) J. Phys. Chem. , vol.93 , pp. 7562-7570
    • Gruner, S.M.1
  • 68
    • 0027213878 scopus 로고
    • Diacylglycerol: Formation and function in phospholipid-mediated signal transduction
    • Haeffner E.W. Diacylglycerol: Formation and function in phospholipid-mediated signal transduction. Comp. Biochem. Physiol. C 105 (1993) 337-345
    • (1993) Comp. Biochem. Physiol. C , vol.105 , pp. 337-345
    • Haeffner, E.W.1
  • 69
    • 0024541436 scopus 로고
    • Functions of sphingolipids and sphingolipid breakdown products in cellular regulation
    • Hannun Y.A., and Bell R.M. Functions of sphingolipids and sphingolipid breakdown products in cellular regulation. Science 243 (1989) 500-507
    • (1989) Science , vol.243 , pp. 500-507
    • Hannun, Y.A.1    Bell, R.M.2
  • 70
    • 0020473245 scopus 로고
    • Structure and thermotropic behavior of PS bilayer membranes
    • Hauser H., Paltauf F., and Shipley G.G. Structure and thermotropic behavior of PS bilayer membranes. Biochemistry 21 (1982) 1061-1067
    • (1982) Biochemistry , vol.21 , pp. 1061-1067
    • Hauser, H.1    Paltauf, F.2    Shipley, G.G.3
  • 71
    • 84943997802 scopus 로고
    • Elastic properties of lipid bilayers: Theory and possible experiments
    • Helfrich W. Elastic properties of lipid bilayers: Theory and possible experiments. Z. Naturforsch 28C (1973) 693-703
    • (1973) Z. Naturforsch , vol.28 C , pp. 693-703
    • Helfrich, W.1
  • 72
    • 51649170084 scopus 로고
    • Undulations, steric interactions and cohesion of fluid membranes
    • Helfrich W., and Servuss R.-M. Undulations, steric interactions and cohesion of fluid membranes. Nuovo Cimento Soc. Ital. Fis. A 3 (1984) 137-151
    • (1984) Nuovo Cimento Soc. Ital. Fis. A , vol.3 , pp. 137-151
    • Helfrich, W.1    Servuss, R.-M.2
  • 73
    • 0014977813 scopus 로고
    • Biological membrane ultrastructure
    • Hendler R.W. Biological membrane ultrastructure. Physiol. Rev. 51 (1971) 66-97
    • (1971) Physiol. Rev. , vol.51 , pp. 66-97
    • Hendler, R.W.1
  • 74
    • 0017749904 scopus 로고
    • A direct analysis of lamellar x-ray diffraction from hydrated oriented multilayers of fully functional sarcoplasmic reticulum
    • Herbette L., Marquardt J., Scarpa A., and Blasie J.K. A direct analysis of lamellar x-ray diffraction from hydrated oriented multilayers of fully functional sarcoplasmic reticulum. Biophys. J. 20 (1977) 245-272
    • (1977) Biophys. J. , vol.20 , pp. 245-272
    • Herbette, L.1    Marquardt, J.2    Scarpa, A.3    Blasie, J.K.4
  • 75
    • 0015501763 scopus 로고
    • Calorimetric studies of dilute aqueous suspensions of bilayers formed from synthetic L-α-lecithin
    • Hinz H.-J., and Sturtevant J.M. Calorimetric studies of dilute aqueous suspensions of bilayers formed from synthetic L-α-lecithin. J. Biol. Chem. 247 (1972) 6071
    • (1972) J. Biol. Chem. , vol.247 , pp. 6071
    • Hinz, H.-J.1    Sturtevant, J.M.2
  • 76
    • 0000048078 scopus 로고
    • Structural chemistry of 1,2-dilauroyl-DL-phosphatidylethanolamine: molecular conformation and intermolecular packing of phospholipids
    • Hitchcock P.B., Mason R., Thomas K.M., and Shipley G.G. Structural chemistry of 1,2-dilauroyl-DL-phosphatidylethanolamine: molecular conformation and intermolecular packing of phospholipids. Proc. Natl. Acad. Sci. U.S.A. 71 (1974) 3036-3040
    • (1974) Proc. Natl. Acad. Sci. U.S.A. , vol.71 , pp. 3036-3040
    • Hitchcock, P.B.1    Mason, R.2    Thomas, K.M.3    Shipley, G.G.4
  • 77
    • 0026603840 scopus 로고
    • Cardiolipins and biomembrane function
    • Hoch F.L. Cardiolipins and biomembrane function. Biochim. Biophys. Acta 1113 (1992) 71-133
    • (1992) Biochim. Biophys. Acta , vol.1113 , pp. 71-133
    • Hoch, F.L.1
  • 79
    • 0023055350 scopus 로고
    • Structure and properties of mixed-chain phospholipid assemblies
    • Huang C.-H., and Mason J.T. Structure and properties of mixed-chain phospholipid assemblies. Biochim. Biophys. Acta 864 (1986) 423-470
    • (1986) Biochim. Biophys. Acta , vol.864 , pp. 423-470
    • Huang, C.-H.1    Mason, J.T.2
  • 80
    • 0027466276 scopus 로고
    • Calorimetric studies of fully hydrated phosphatidylcholines with highly asymmetric acyl chains
    • Huang C., Wang Z.-Q., Lin H.-N., and Brumbaugh E.E. Calorimetric studies of fully hydrated phosphatidylcholines with highly asymmetric acyl chains. Biochim. Biophys. Acta 1145 (1993) 298-310
    • (1993) Biochim. Biophys. Acta , vol.1145 , pp. 298-310
    • Huang, C.1    Wang, Z.-Q.2    Lin, H.-N.3    Brumbaugh, E.E.4
  • 81
    • 0000502524 scopus 로고
    • Non-bilayer-forming lipids: Why are they necessary in biomembranes
    • Hui S.W. Non-bilayer-forming lipids: Why are they necessary in biomembranes. Comments Mol. Cell. Biophys. 4 (1987) 233-248
    • (1987) Comments Mol. Cell. Biophys. , vol.4 , pp. 233-248
    • Hui, S.W.1
  • 82
    • 0019886312 scopus 로고
    • Membrane fusion through point defects in bilayers
    • Hui S.W., Stewart T.P., Boni L.T., and Yeagle P.L. Membrane fusion through point defects in bilayers. Science 212 (1981) 921-922
    • (1981) Science , vol.212 , pp. 921-922
    • Hui, S.W.1    Stewart, T.P.2    Boni, L.T.3    Yeagle, P.L.4
  • 83
    • 0017750496 scopus 로고
    • Refinement of the fluid-mosaic model of membrane structure
    • Israelachvili J.N. Refinement of the fluid-mosaic model of membrane structure. Biochim. Biophys. Acta 469 (1977) 221-225
    • (1977) Biochim. Biophys. Acta , vol.469 , pp. 221-225
    • Israelachvili, J.N.1
  • 84
    • 0022438031 scopus 로고
    • Direct methods for measuring conformational forces (hydration forces) between membrane and other surfaces
    • Packer L. (Ed), Academic Press, San Diego
    • Israelachvili J., and Mama J. Direct methods for measuring conformational forces (hydration forces) between membrane and other surfaces. In: Packer L. (Ed). Methods in Enzymology 127 (1986), Academic Press, San Diego 353-361
    • (1986) Methods in Enzymology , vol.127 , pp. 353-361
    • Israelachvili, J.1    Mama, J.2
  • 85
    • 0000176238 scopus 로고
    • Hydration or steric forces between amphiphilic surfaces?
    • Israelachvili J.N., and Wennerstrom H. Hydration or steric forces between amphiphilic surfaces?. Langmuir 6 (1990) 873-876
    • (1990) Langmuir , vol.6 , pp. 873-876
    • Israelachvili, J.N.1    Wennerstrom, H.2
  • 86
    • 0346845605 scopus 로고
    • Entropic forces between amphiphilic surfaces in liquids
    • Israelachvili J.N., and Wennerstrom H. Entropic forces between amphiphilic surfaces in liquids. J. Phys. Chem. 96 (1992) 520-531
    • (1992) J. Phys. Chem. , vol.96 , pp. 520-531
    • Israelachvili, J.N.1    Wennerstrom, H.2
  • 87
    • 0030052290 scopus 로고    scopus 로고
    • Role of hydration and water structure in biological and colloidal interactions
    • Israelachvili J., and Wennerstrom H. Role of hydration and water structure in biological and colloidal interactions. Nature (London) 379 (1996) 219-225
    • (1996) Nature (London) , vol.379 , pp. 219-225
    • Israelachvili, J.1    Wennerstrom, H.2
  • 88
    • 0000222487 scopus 로고
    • Measurement of forces between two surfaces in aqueous poly(ethylene oxide) solutions
    • Israelachvili J.N., Tandon R.K., and White L.R. Measurement of forces between two surfaces in aqueous poly(ethylene oxide) solutions. Nature (London) 277 (1979) 120-121
    • (1979) Nature (London) , vol.277 , pp. 120-121
    • Israelachvili, J.N.1    Tandon, R.K.2    White, L.R.3
  • 90
    • 0041699626 scopus 로고
    • Role of cholesterol in biomembranes and related systems
    • Academic Press, New York
    • Jain M.K. Role of cholesterol in biomembranes and related systems. Current Topics in Membranes and Ion Transport. (1975), Academic Press, New York
    • (1975) Current Topics in Membranes and Ion Transport.
    • Jain, M.K.1
  • 91
    • 0017138422 scopus 로고
    • Nature of the thermal pretransition of synthetic phospholipids: Dimyristoyl- and dipalmitoyllecithin
    • Janiak M.J., Small D.M., and Shipley G.G. Nature of the thermal pretransition of synthetic phospholipids: Dimyristoyl- and dipalmitoyllecithin. Biochemistry 15 (1976) 4575-4580
    • (1976) Biochemistry , vol.15 , pp. 4575-4580
    • Janiak, M.J.1    Small, D.M.2    Shipley, G.G.3
  • 92
    • 0018786933 scopus 로고
    • Temperature and compositional dependence of the structure of dimyristoyl lecithin
    • Janiak M.J., Small D.M., and Shipley G.G. Temperature and compositional dependence of the structure of dimyristoyl lecithin. J. Biol. Chem. 254 (1979) 6068-6078
    • (1979) J. Biol. Chem. , vol.254 , pp. 6068-6078
    • Janiak, M.J.1    Small, D.M.2    Shipley, G.G.3
  • 93
    • 0028027218 scopus 로고
    • Expression and biological functions of sulfoglucuronyl glycolipids (SGGLs) in the nervous system-a review
    • Jungalwala F.B. Expression and biological functions of sulfoglucuronyl glycolipids (SGGLs) in the nervous system-a review. Neurochem. Res. 19 (1994) 945-957
    • (1994) Neurochem. Res. , vol.19 , pp. 945-957
    • Jungalwala, F.B.1
  • 94
    • 0025968110 scopus 로고
    • Cholesterol does not remove the gel-liquid crystalline phase transition of phosphatidylcholines containing two polyenoic acyl chains
    • Kariel N., Davidson E., and Keough K.M.W. Cholesterol does not remove the gel-liquid crystalline phase transition of phosphatidylcholines containing two polyenoic acyl chains. Biochim. Biophys. Acta 1062 (1991) 70-76
    • (1991) Biochim. Biophys. Acta , vol.1062 , pp. 70-76
    • Kariel, N.1    Davidson, E.2    Keough, K.M.W.3
  • 95
    • 0028964069 scopus 로고
    • Range and magnitude of the steric pressure between bilayers containing phospholipids with covalently attached poly(ethyleneglycol)
    • Kenworthy A.K., Hristova K., Needham D., and McIntosh T.J. Range and magnitude of the steric pressure between bilayers containing phospholipids with covalently attached poly(ethyleneglycol). Biophys. J. 68 (1995) 1921-1936
    • (1995) Biophys. J. , vol.68 , pp. 1921-1936
    • Kenworthy, A.K.1    Hristova, K.2    Needham, D.3    McIntosh, T.J.4
  • 96
    • 0018794356 scopus 로고
    • Gel to liquid-crystalline phase transitions in water dispersions of saturated mixed-acid phosphatidylcholines
    • Keogh K.M.W., and Davis P.J. Gel to liquid-crystalline phase transitions in water dispersions of saturated mixed-acid phosphatidylcholines. Biochemistry 18 (1979) 1453-1458
    • (1979) Biochemistry , vol.18 , pp. 1453-1458
    • Keogh, K.M.W.1    Davis, P.J.2
  • 97
    • 0000322787 scopus 로고
    • Small-angle x-ray scattering and electron microscopy of crude dispersions of swelling lipids and the influence of the morphology on the repeat distance
    • Klose G., Konig B., Meyer H.W., Schulze G., and Degovics G. Small-angle x-ray scattering and electron microscopy of crude dispersions of swelling lipids and the influence of the morphology on the repeat distance. Chem. Phys. Lipids 47 (1988) 225-234
    • (1988) Chem. Phys. Lipids , vol.47 , pp. 225-234
    • Klose, G.1    Konig, B.2    Meyer, H.W.3    Schulze, G.4    Degovics, G.5
  • 98
    • 0030771815 scopus 로고    scopus 로고
    • Membrane lateral compressibility determined by NMR and X-ray diffraction: Effect of acyl chain polyunsaturation
    • Koenig B.W., Strey H.H., and Gawrisch K. Membrane lateral compressibility determined by NMR and X-ray diffraction: Effect of acyl chain polyunsaturation. Biophys. J. 73 (1997) 1954-1966
    • (1997) Biophys. J. , vol.73 , pp. 1954-1966
    • Koenig, B.W.1    Strey, H.H.2    Gawrisch, K.3
  • 99
    • 0000995983 scopus 로고
    • Fluctuation theory of hydration forces: The dramatic effect of inhomogeneous boundary conditions
    • Kornyshev A.A., and Leikin S. Fluctuation theory of hydration forces: The dramatic effect of inhomogeneous boundary conditions. Phys. Rev. A 40 (1989) 6431-6437
    • (1989) Phys. Rev. A , vol.40 , pp. 6431-6437
    • Kornyshev, A.A.1    Leikin, S.2
  • 101
    • 0028205738 scopus 로고
    • Modulation of interaction forces between bilayers exposing short-chained ethylene oxide headgroups
    • Kuhl T.L., Leckband D.E., Lasic D.D., and Israelachvili J.N. Modulation of interaction forces between bilayers exposing short-chained ethylene oxide headgroups. Biophys. J. 66 (1994) 1479-1488
    • (1994) Biophys. J. , vol.66 , pp. 1479-1488
    • Kuhl, T.L.1    Leckband, D.E.2    Lasic, D.D.3    Israelachvili, J.N.4
  • 102
    • 0019412881 scopus 로고
    • Thermoelasticity of large lecithin vesicles
    • Kwok R., and Evans E. Thermoelasticity of large lecithin vesicles. Biophys. J. 35 (1981) 637-652
    • (1981) Biophys. J. , vol.35 , pp. 637-652
    • Kwok, R.1    Evans, E.2
  • 103
    • 0014865829 scopus 로고
    • Alteration of membrane deformability in hemolytic anemias
    • LaCelle P.L. Alteration of membrane deformability in hemolytic anemias. Semin. Hematol. 7 (1970) 355-373
    • (1970) Semin. Hematol. , vol.7 , pp. 355-373
    • LaCelle, P.L.1
  • 104
    • 0014645670 scopus 로고
    • Thermal analysis of lipids, proteins, and biological membranes. A review and summary of some recent results
    • Ladbrooke B.D., and Chapman D. Thermal analysis of lipids, proteins, and biological membranes. A review and summary of some recent results. Chem. Phys. Lipids 3 (1969) 304-367
    • (1969) Chem. Phys. Lipids , vol.3 , pp. 304-367
    • Ladbrooke, B.D.1    Chapman, D.2
  • 105
    • 0014434003 scopus 로고
    • Studies on lecithin-cholesterol-water interactions by differential scanning calorimetry and x-ray diffraction
    • Ladbrooke B.D., Williams R.M., and Chapman D. Studies on lecithin-cholesterol-water interactions by differential scanning calorimetry and x-ray diffraction. Biochim. Biophys. Acta 150 (1968) 333-340
    • (1968) Biochim. Biophys. Acta , vol.150 , pp. 333-340
    • Ladbrooke, B.D.1    Williams, R.M.2    Chapman, D.3
  • 106
    • 0344148555 scopus 로고
    • The discocyte-echinocyte transformation of the human red cell: Deformability characteristics
    • Bressis N., Weed R.I., and Leblond P. (Eds), Springer-Verlag, Berlin
    • Leblond P. The discocyte-echinocyte transformation of the human red cell: Deformability characteristics. In: Bressis N., Weed R.I., and Leblond P. (Eds). Red Cell Shape (1973), Springer-Verlag, Berlin 95-129
    • (1973) Red Cell Shape , pp. 95-129
    • Leblond, P.1
  • 107
    • 0014675084 scopus 로고
    • Structure of aqueous mixtures of lecithin and cholesterol
    • Lecuyer H., and Dervichian D.G. Structure of aqueous mixtures of lecithin and cholesterol. J. Mol. Biol. 45 (1969) 39-51
    • (1969) J. Mol. Biol. , vol.45 , pp. 39-51
    • Lecuyer, H.1    Dervichian, D.G.2
  • 108
    • 0001494816 scopus 로고
    • Theory of hydration forces. Nonlocal electrostatic interaction of neutral surfaces
    • Leikin S., and Kornyshev A.A. Theory of hydration forces. Nonlocal electrostatic interaction of neutral surfaces. J. Chem. Phys. 92 (1990) 6890-6898
    • (1990) J. Chem. Phys. , vol.92 , pp. 6890-6898
    • Leikin, S.1    Kornyshev, A.A.2
  • 109
    • 35949008368 scopus 로고
    • Mean-field theory of dehydration transitions
    • Leikin S., and Kornyshev A.A. Mean-field theory of dehydration transitions. Phys. Rev. A 44 (1991) 1156-1168
    • (1991) Phys. Rev. A , vol.44 , pp. 1156-1168
    • Leikin, S.1    Kornyshev, A.A.2
  • 111
    • 0017336501 scopus 로고
    • Measurement and modification of forces between lecithin bilayers
    • LeNeveu D.M., Rand R.P., Parsegian V.A., and Gingell D. Measurement and modification of forces between lecithin bilayers. Biophys. J. 18 (1977) 209-230
    • (1977) Biophys. J. , vol.18 , pp. 209-230
    • LeNeveu, D.M.1    Rand, R.P.2    Parsegian, V.A.3    Gingell, D.4
  • 112
    • 0015356040 scopus 로고
    • X-ray diffraction studies of lecithin bimolecular leaflets with incorporated fluorescent probes
    • Lesslauer W., Cain J.E., and Blasie J.K. X-ray diffraction studies of lecithin bimolecular leaflets with incorporated fluorescent probes. Proc. Nutl. Acad. Sci. U.S.A. 69 (1972) 1499-1503
    • (1972) Proc. Nutl. Acad. Sci. U.S.A. , vol.69 , pp. 1499-1503
    • Lesslauer, W.1    Cain, J.E.2    Blasie, J.K.3
  • 114
    • 0014407981 scopus 로고
    • Multilayers of phospholipid bimolecular leaflets
    • Levine Y.K., Bailey A.I., and Wilkins M.H.F. Multilayers of phospholipid bimolecular leaflets. Nature (London) 220 (1968) 577-578
    • (1968) Nature (London) , vol.220 , pp. 577-578
    • Levine, Y.K.1    Bailey, A.I.2    Wilkins, M.H.F.3
  • 115
    • 0021104058 scopus 로고
    • Lipid bilayer thickness varies linearly with acyl chain length in fluid phosphatidylcholine vesicles
    • Lewis B.A., and Engelman D.M. Lipid bilayer thickness varies linearly with acyl chain length in fluid phosphatidylcholine vesicles. J. Mol. Biol. 166 (1983) 211-217
    • (1983) J. Mol. Biol. , vol.166 , pp. 211-217
    • Lewis, B.A.1    Engelman, D.M.2
  • 116
    • 0023662539 scopus 로고
    • A differential scanning calorimetry study of the thermotropic phase behavior of model membranes composed of phosphatidylcholine containing linear saturated fatty acyl chains
    • Lewis R.N.A., Mak N., and McElhaney R.N. A differential scanning calorimetry study of the thermotropic phase behavior of model membranes composed of phosphatidylcholine containing linear saturated fatty acyl chains. Biochemistry 26 (1987) 6118-6126
    • (1987) Biochemistry , vol.26 , pp. 6118-6126
    • Lewis, R.N.A.1    Mak, N.2    McElhaney, R.N.3
  • 117
    • 0029077617 scopus 로고
    • Phosphatidylcholine hydrolysis and DNA synthesis in cultured retinal capillary pericytes
    • Li W., Liu X., and Yanoff M. Phosphatidylcholine hydrolysis and DNA synthesis in cultured retinal capillary pericytes. Microvasc. Res. 49 (1995) 350-363
    • (1995) Microvasc. Res. , vol.49 , pp. 350-363
    • Li, W.1    Liu, X.2    Yanoff, M.3
  • 118
    • 0024603546 scopus 로고
    • Cubic phases and isotropic structures formed by membrane lipids-possible biological relevance
    • Lindblom G., and Rilfors L. Cubic phases and isotropic structures formed by membrane lipids-possible biological relevance. Biochim. Biophys. Acta 988 (1989) 221-256
    • (1989) Biochim. Biophys. Acta , vol.988 , pp. 221-256
    • Lindblom, G.1    Rilfors, L.2
  • 119
    • 14544292821 scopus 로고
    • Hydration vs. protrusion forces between lipid bilayers
    • Lipowsky R., and Grotehans S. Hydration vs. protrusion forces between lipid bilayers. Europhys. Lett. 23 (1993) 599-604
    • (1993) Europhys. Lett. , vol.23 , pp. 599-604
    • Lipowsky, R.1    Grotehans, S.2
  • 120
    • 0027518207 scopus 로고
    • Phospholi-pase D-mediated hydrolysis of phosphatidylcholine role in cell signalling
    • Liscovitch M., Ben-Av P., Danin M., Faiman G., Eldar H., and Livneh E. Phospholi-pase D-mediated hydrolysis of phosphatidylcholine role in cell signalling. J. Lipid Mediators 8 (1993) 177-182
    • (1993) J. Lipid Mediators , vol.8 , pp. 177-182
    • Liscovitch, M.1    Ben-Av, P.2    Danin, M.3    Faiman, G.4    Eldar, H.5    Livneh, E.6
  • 121
    • 0029976262 scopus 로고    scopus 로고
    • A role for phospholipid polyunsaturation in modulating membrane protein function
    • Litman B.J., and Mitchell D.C. A role for phospholipid polyunsaturation in modulating membrane protein function. Lipids 31 (1996) S193-S197
    • (1996) Lipids , vol.31
    • Litman, B.J.1    Mitchell, D.C.2
  • 122
    • 0023351919 scopus 로고
    • Thermal phase behavior and structure of hydrated mixtures between DPPC and DHPC
    • Lohner K., Schuster A., Degovics G., Muller K., and Laggner P. Thermal phase behavior and structure of hydrated mixtures between DPPC and DHPC. Chem. Phys. Lipids 44 (1987) 61-70
    • (1987) Chem. Phys. Lipids , vol.44 , pp. 61-70
    • Lohner, K.1    Schuster, A.2    Degovics, G.3    Muller, K.4    Laggner, P.5
  • 123
    • 0018473783 scopus 로고
    • The phase behavior of hydrated cholesterol
    • Loomis C.R., Shipley G.G., and Small D.M. The phase behavior of hydrated cholesterol. J. Lipid Res. 20 (1979) 525-535
    • (1979) J. Lipid Res. , vol.20 , pp. 525-535
    • Loomis, C.R.1    Shipley, G.G.2    Small, D.M.3
  • 124
    • 0022366934 scopus 로고
    • Phosphatidylinositol is the membrane-anchoring domain of the Thy-1 glycoprotein
    • Low M.G., and Kincaid P.W. Phosphatidylinositol is the membrane-anchoring domain of the Thy-1 glycoprotein. Nature (London) 318 (1985) 62-64
    • (1985) Nature (London) , vol.318 , pp. 62-64
    • Low, M.G.1    Kincaid, P.W.2
  • 125
    • 0024286552 scopus 로고
    • Structural and functional roles of glycosyl-phosphatidyl- inositol in membranes
    • Low M.G., and Saltiel A.R. Structural and functional roles of glycosyl-phosphatidyl- inositol in membranes. Science 239 (1988) 268-275
    • (1988) Science , vol.239 , pp. 268-275
    • Low, M.G.1    Saltiel, A.R.2
  • 126
    • 50549200191 scopus 로고
    • Globular lipid micelles and cell membranes
    • Lucy J.A. Globular lipid micelles and cell membranes. J. Theor. Biol. 7 (1964) 360-373
    • (1964) J. Theor. Biol. , vol.7 , pp. 360-373
    • Lucy, J.A.1
  • 127
    • 0002787636 scopus 로고
    • X-ray diffraction studies of lipid-water systems
    • Academic Press, New York
    • Luzzati V. X-ray diffraction studies of lipid-water systems. Biological Membranes. (1968), Academic Press, New York
    • (1968) Biological Membranes.
    • Luzzati, V.1
  • 129
    • 0001541657 scopus 로고
    • Investigation of phase transitions of lipids and lipid mixtures by sensitivity differential scanning calorimetry
    • Mabrey S., and Sturtevant J.M. Investigation of phase transitions of lipids and lipid mixtures by sensitivity 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
  • 130
    • 0018170195 scopus 로고
    • The effect of cholesterol on the structure of phosphatidylcholine bilayers
    • Mclntosh T.J. The effect of cholesterol on the structure of phosphatidylcholine bilayers. Biochim. Biophys. Acta 513 (1978) 43-58
    • (1978) Biochim. Biophys. Acta , vol.513 , pp. 43-58
    • Mclntosh, T.J.1
  • 131
    • 0024543281 scopus 로고
    • Cholesterol modifies the short-range repulsive interactions between phosphatidylcholine membranes
    • McIntosh T.J., Magid A.D., and Simon S.A. Cholesterol modifies the short-range repulsive interactions between phosphatidylcholine membranes. Biochemistry 28 (1989) 17-25
    • (1989) Biochemistry , vol.28 , pp. 17-25
    • McIntosh, T.J.1    Magid, A.D.2    Simon, S.A.3
  • 132
    • 0023057572 scopus 로고
    • Area per molecule and distribution of water in fully hydrated dilauroylphosphatidylethanolamine bilayers
    • McIntosh T.J., and Simon S.A. Area per molecule and distribution of water in fully hydrated dilauroylphosphatidylethanolamine bilayers. Biochemistry 25 (1986) 4948-4952
    • (1986) Biochemistry , vol.25 , pp. 4948-4952
    • McIntosh, T.J.1    Simon, S.A.2
  • 133
    • 0022512564 scopus 로고
    • The hydration force and bilayer deformation: A reevaluation
    • McIntosh T.J., and Simon S.A. The hydration force and bilayer deformation: A reevaluation. Biochemistry 25 (1986) 4058-4066
    • (1986) Biochemistry , vol.25 , pp. 4058-4066
    • McIntosh, T.J.1    Simon, S.A.2
  • 134
    • 0027284002 scopus 로고
    • Contribution of hydration and steric (entropic) pressures to the interaction between phosphatidylcholine bilayers: Experiments with the subgel phase
    • Mclntosh T.J., and Simon S.A. Contribution of hydration and steric (entropic) pressures to the interaction between phosphatidylcholine bilayers: Experiments with the subgel phase. Biochemistry 32 (1993) 8374-8384
    • (1993) Biochemistry , vol.32 , pp. 8374-8384
    • Mclntosh, T.J.1    Simon, S.A.2
  • 135
    • 0028304679 scopus 로고
    • Hydration and steric pressures between phospholipid bilayers
    • McIntosh T.J., and Simon S.A. Hydration and steric pressures between phospholipid bilayers. Annu. Rev. Biophys. Biomol. Struct. 23 (1994) 27-51
    • (1994) Annu. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 27-51
    • McIntosh, T.J.1    Simon, S.A.2
  • 136
    • 0028092897 scopus 로고
    • Long- and short-range interactions between phospholipid/ganglioside GMl bilayers
    • McIntosh T.J., and Simon S.A. Long- and short-range interactions between phospholipid/ganglioside GMl bilayers. Biochemistry 33 (1994) 10477-10486
    • (1994) Biochemistry , vol.33 , pp. 10477-10486
    • McIntosh, T.J.1    Simon, S.A.2
  • 138
    • 0003266076 scopus 로고    scopus 로고
    • Adhesion between phosphatidylethanolamine bilayers
    • McIntosh T.J., and Simon S.A. Adhesion between phosphatidylethanolamine bilayers. Langmuir 12 (1996) 3622-4630
    • (1996) Langmuir , vol.12 , pp. 3622-4630
    • McIntosh, T.J.1    Simon, S.A.2
  • 139
    • 0023658631 scopus 로고
    • Steric repulsion between phosphatidyl choline bilayers
    • McIntosh T.J., Magid A.D., and Simon S.A. Steric repulsion between phosphatidyl choline bilayers. Biochemistry 26 (1987) 7325-7332
    • (1987) Biochemistry , vol.26 , pp. 7325-7332
    • McIntosh, T.J.1    Magid, A.D.2    Simon, S.A.3
  • 140
    • 0029063594 scopus 로고
    • Experimental tests for protrusion and undulation pressures in phospholipid bilayers
    • McIntosh T.J., Advani S., Burton R.E., Zhelev D.V., Needham D., and Simon S.A. Experimental tests for protrusion and undulation pressures in phospholipid bilayers. Biochemistry 34 (1995) 8520-8532
    • (1995) Biochemistry , vol.34 , pp. 8520-8532
    • McIntosh, T.J.1    Advani, S.2    Burton, R.E.3    Zhelev, D.V.4    Needham, D.5    Simon, S.A.6
  • 141
    • 0013016216 scopus 로고
    • Measurement of the range and magnitude of the repulsive pressure between PEG-coated liposomes
    • CRC Press, Boca Raton, Florida
    • McIntosh T.J., Kenworthy A.K., and Needham D. Measurement of the range and magnitude of the repulsive pressure between PEG-coated liposomes. Stealth Liposomes. (1995), CRC Press, Boca Raton, Florida
    • (1995) Stealth Liposomes.
    • McIntosh, T.J.1    Kenworthy, A.K.2    Needham, D.3
  • 142
    • 0028121281 scopus 로고
    • The surface behavior of glycosphingolipids in biomembranes: A new frontier of molecular biology
    • Maggio B. The surface behavior of glycosphingolipids in biomembranes: A new frontier of molecular biology. Prog. Biophys. Mol. Biol. 62 (1994) 55-117
    • (1994) Prog. Biophys. Mol. Biol. , vol.62 , pp. 55-117
    • Maggio, B.1
  • 143
    • 0022432688 scopus 로고
    • Thermotropic behavior of glycosphingolipids in aqueous dispersions
    • Maggio B., Ariga T., Sturtevant J.M., and Yu R.K. Thermotropic behavior of glycosphingolipids in aqueous dispersions. Biochemistry 24 (1985) 1084-1092
    • (1985) Biochemistry , vol.24 , pp. 1084-1092
    • Maggio, B.1    Ariga, T.2    Sturtevant, J.M.3    Yu, R.K.4
  • 145
    • 0024370782 scopus 로고
    • Dystrophin-the gene and its product
    • Mandel J.L. Dystrophin-the gene and its product. Nature (London) 339 (1989) 584-586
    • (1989) Nature (London) , vol.339 , pp. 584-586
    • Mandel, J.L.1
  • 146
    • 0000067520 scopus 로고
    • Repulsion of interfaces due to boundary water
    • Marcelja S., and Radic N. Repulsion of interfaces due to boundary water. Chem. Phys. Lett. 42 (1976) 129-130
    • (1976) Chem. Phys. Lett. , vol.42 , pp. 129-130
    • Marcelja, S.1    Radic, N.2
  • 147
    • 0014934363 scopus 로고
    • Physical and chemical properties of a protein isolated from red cell membranes
    • Marchesi S.L., Steers E., Marchesi V.T., and Tillack T.W. Physical and chemical properties of a protein isolated from red cell membranes. Biochemistry 9 (1970) 50-63
    • (1970) Biochemistry , vol.9 , pp. 50-63
    • Marchesi, S.L.1    Steers, E.2    Marchesi, V.T.3    Tillack, T.W.4
  • 148
    • 0024279520 scopus 로고
    • Cubic phases of lipid-containing systems. Structure analysis and biological implications
    • Mariani P., Luzzati V., and Delacroix H. Cubic phases of lipid-containing systems. Structure analysis and biological implications. J. Mol. Biol. 204 (1988) 165-189
    • (1988) J. Mol. Biol. , vol.204 , pp. 165-189
    • Mariani, P.1    Luzzati, V.2    Delacroix, H.3
  • 149
    • 0023024664 scopus 로고
    • Direct measurement of the interaction between phosphatidylglycerol bilayers in aqueous electrolyte solutions
    • Marra J. Direct measurement of the interaction between phosphatidylglycerol bilayers in aqueous electrolyte solutions. Biophys. J. 50 (1986) 815-825
    • (1986) Biophys. J. , vol.50 , pp. 815-825
    • Marra, J.1
  • 150
    • 0021972793 scopus 로고
    • Direct measurements offorces between phosphatidylcholine and phosphatidylethanolamine bilayers in aqueous electrolyte solutions
    • Marra J., and Israelachvili J. Direct measurements offorces between phosphatidylcholine and phosphatidylethanolamine bilayers in aqueous electrolyte solutions. Biochemistry 24 (1985) 4608-4618
    • (1985) Biochemistry , vol.24 , pp. 4608-4618
    • Marra, J.1    Israelachvili, J.2
  • 152
    • 0019879350 scopus 로고
    • Calorimetric investigations of saturated mixed-chain phosphatidylcholine bilayer dispersions
    • Mason J.T., Huang C.-H., and Biltonen R.L. Calorimetric investigations of saturated mixed-chain phosphatidylcholine bilayer dispersions. Biochemistry 20 (1981) 6086-6092
    • (1981) Biochemistry , vol.20 , pp. 6086-6092
    • Mason, J.T.1    Huang, C.-H.2    Biltonen, R.L.3
  • 153
    • 0024551019 scopus 로고
    • Phospholipids in signal transduction of mesangial cells
    • Mene P., Simonson M.S., and Dunn M.J. Phospholipids in signal transduction of mesangial cells. Am. J. Physiol. 256 (1989) F375-F386
    • (1989) Am. J. Physiol. , vol.256
    • Mene, P.1    Simonson, M.S.2    Dunn, M.J.3
  • 154
    • 0026022563 scopus 로고
    • Cell regulation by sphingosine and more complex sphingolipids
    • Merrill A.H. Cell regulation by sphingosine and more complex sphingolipids. J. Bioenerg. Biomembr. 23 (1991) 83-104
    • (1991) J. Bioenerg. Biomembr. , vol.23 , pp. 83-104
    • Merrill, A.H.1
  • 155
    • 0025283928 scopus 로고
    • An update of the enzymology and regulation of sphingomyelin metabolism
    • Merrill A.H., and Jones D.D. An update of the enzymology and regulation of sphingomyelin metabolism. Biochim. Biophys. Acta 1044 (1990) 1-12
    • (1990) Biochim. Biophys. Acta , vol.1044 , pp. 1-12
    • Merrill, A.H.1    Jones, D.D.2
  • 156
  • 157
    • 0000968818 scopus 로고
    • The mechanical properties of the cell surface. I. The cell elastimeter
    • Mitchison J.M., and Swann M.M. The mechanical properties of the cell surface. I. The cell elastimeter. J. Exp. Biol. 31 (1954) 443-460
    • (1954) J. Exp. Biol. , vol.31 , pp. 443-460
    • Mitchison, J.M.1    Swann, M.M.2
  • 158
    • 0019887626 scopus 로고
    • Effect of lipid membrane structure on the adenosine 5′-triphosphate hydrolyzing activity of the calcium-stimulate adenosine triphosphatase of sacroplasmic reticulum
    • Moore B.M., Lentz B.R., Hoechli M., and Meissner G. Effect of lipid membrane structure on the adenosine 5′-triphosphate hydrolyzing activity of the calcium-stimulate adenosine triphosphatase of sacroplasmic reticulum. Biochemistry 20 (1981) 6810-6817
    • (1981) Biochemistry , vol.20 , pp. 6810-6817
    • Moore, B.M.1    Lentz, B.R.2    Hoechli, M.3    Meissner, G.4
  • 159
    • 0027251833 scopus 로고
    • Area/lipid of bilayers from NMR
    • Nagle J.F. Area/lipid of bilayers from NMR. Biophys. J. 64 (1993) 1476-1481
    • (1993) Biophys. J. , vol.64 , pp. 1476-1481
    • Nagle, J.F.1
  • 160
    • 0024280716 scopus 로고
    • Structure of fully hydrated bilayer dispersions
    • Nagle J.F., and Wiener M.C. Structure of fully hydrated bilayer dispersions. Biochim. Biophys. Acta 942 (1988) 1-10
    • (1988) Biochim. Biophys. Acta , vol.942 , pp. 1-10
    • Nagle, J.F.1    Wiener, M.C.2
  • 161
    • 0030033065 scopus 로고    scopus 로고
    • X-ray structure determination of fully hydrated Lα phase dipalmitoylphosphatidylcholine bilayers
    • Nagle J.F., Zhang R., Tristram-Nagle S., Sun W., Petrache H.I., and Suter R.M. X-ray structure determination of fully hydrated Lα phase dipalmitoylphosphatidylcholine bilayers. Biophys. J. 70 (1996) 1419-1431
    • (1996) Biophys. J. , vol.70 , pp. 1419-1431
    • Nagle, J.F.1    Zhang, R.2    Tristram-Nagle, S.3    Sun, W.4    Petrache, H.I.5    Suter, R.M.6
  • 162
    • 0024671189 scopus 로고
    • Electro-mechanical permeabiliation of lipid vesicles. Role of membrane tension and compressibility
    • Needham D., and Hochmuth R.M. Electro-mechanical permeabiliation of lipid vesicles. Role of membrane tension and compressibility. Biophys. J. 55 (1989) 1001-1009
    • (1989) Biophys. J. , vol.55 , pp. 1001-1009
    • Needham, D.1    Hochmuth, R.M.2
  • 163
    • 0025150146 scopus 로고
    • Elastic deformation and failure of lipid bilayer membranes containing cholesterol
    • Needham D., and Nunn R.S. Elastic deformation and failure of lipid bilayer membranes containing cholesterol. Biophys. J. 58 (1990) 997-1009
    • (1990) Biophys. J. , vol.58 , pp. 997-1009
    • Needham, D.1    Nunn, R.S.2
  • 164
    • 0001019097 scopus 로고    scopus 로고
    • The mechanochemistry of lipid vesicles examined by micropipet manipulation techniques
    • Rosoff M. (Ed), Dekker, New York
    • Needham D., and Zhelev D.V. The mechanochemistry of lipid vesicles examined by micropipet manipulation techniques. In: Rosoff M. (Ed). Vesicles (1996), Dekker, New York 373-439
    • (1996) Vesicles , pp. 373-439
    • Needham, D.1    Zhelev, D.V.2
  • 165
    • 0026710312 scopus 로고
    • Repulsive interactions and mechanical stability of polymer-grafted lipid membranes
    • Needham D., McIntosh T.J., and Lasic D.D. Repulsive interactions and mechanical stability of polymer-grafted lipid membranes. Biochim. Biophys. Acta 1108 (1992) 40-48
    • (1992) Biochim. Biophys. Acta , vol.1108 , pp. 40-48
    • Needham, D.1    McIntosh, T.J.2    Lasic, D.D.3
  • 166
    • 0021227676 scopus 로고
    • The role of protein kinase C in cell surface signal transduction and tumour production
    • Nishizuka Y. The role of protein kinase C in cell surface signal transduction and tumour production. Nature (London) 308 (1984) 693-697
    • (1984) Nature (London) , vol.308 , pp. 693-697
    • Nishizuka, Y.1
  • 167
    • 0023052241 scopus 로고
    • Structure and properties of protein kinase C
    • Nishizuka Y. Structure and properties of protein kinase C. Science 233 (1986) 305-333
    • (1986) Science , vol.233 , pp. 305-333
    • Nishizuka, Y.1
  • 168
    • 0011338984 scopus 로고
    • X-ray diffraction studies of lipide emulsions
    • Palmer K.J., and Schmitt F.O. X-ray diffraction studies of lipide emulsions. J. Cell. Comp. Physiol. 17 (1941) 385-394
    • (1941) J. Cell. Comp. Physiol. , vol.17 , pp. 385-394
    • Palmer, K.J.1    Schmitt, F.O.2
  • 169
    • 0020987492 scopus 로고
    • Membrane interaction and deformability
    • Parsegian V.A., and Rand R.P. Membrane interaction and deformability. Ann. N.Y. Acad. Sci. 416 (1983) 1-12
    • (1983) Ann. N.Y. Acad. Sci. , vol.416 , pp. 1-12
    • Parsegian, V.A.1    Rand, R.P.2
  • 171
    • 0000853942 scopus 로고
    • Measured work of deformation and repulsion of lecithin bilayers
    • Parsegian V.A., Fuller N., and Rand R.P. Measured work of deformation and repulsion of lecithin bilayers. Proc. Natl. Acad. Sci. U.S.A. 76 (1979) 2750-2754
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 2750-2754
    • Parsegian, V.A.1    Fuller, N.2    Rand, R.P.3
  • 172
    • 33751500709 scopus 로고
    • Direct osmotic stress measurements of hydration and electrostatic double layer forces between bilayers of double-chained ammonium acetate surfactants
    • Parsegian V.A., Rand R.P., and Fuller N.L. Direct osmotic stress measurements of hydration and electrostatic double layer forces between bilayers of double-chained ammonium acetate surfactants. J. Phys. Chem. 95 (1991) 4777-4782
    • (1991) J. Phys. Chem. , vol.95 , pp. 4777-4782
    • Parsegian, V.A.1    Rand, R.P.2    Fuller, N.L.3
  • 173
    • 0000764022 scopus 로고
    • Molecular arrangements in sphingolipids. The crystal structure of cerebroside
    • Pascher I., and Sundell S. Molecular arrangements in sphingolipids. The crystal structure of cerebroside. Chem. Phys. Lipids 20 (1977) 175-191
    • (1977) Chem. Phys. Lipids , vol.20 , pp. 175-191
    • Pascher, I.1    Sundell, S.2
  • 174
    • 0018788297 scopus 로고
    • The molecular structure of lecithin dihydrate
    • Pearson R.H., and Pascher I. The molecular structure of lecithin dihydrate. Nature (London) 281 (1979) 499-501
    • (1979) Nature (London) , vol.281 , pp. 499-501
    • Pearson, R.H.1    Pascher, I.2
  • 175
    • 0019885444 scopus 로고
    • The relationship between plasma membrane lipid composition and physical properties. II. Effect of phospholipid fatty acid modulation on plasma membrane physical properties and enzymatic activities
    • Poon R., Richards J.M., and Clark W.R. The relationship between plasma membrane lipid composition and physical properties. II. Effect of phospholipid fatty acid modulation on plasma membrane physical properties and enzymatic activities. Biochim. Biophys. Acta 649 (1981) 58-66
    • (1981) Biochim. Biophys. Acta , vol.649 , pp. 58-66
    • Poon, R.1    Richards, J.M.2    Clark, W.R.3
  • 177
    • 0014244969 scopus 로고
    • X-ray diffraction study in water of lipids extracted from human erythrocytes. The position of cholesterol in the lipid lamellae
    • Rand R.P., and Luzzati V. X-ray diffraction study in water of lipids extracted from human erythrocytes. The position of cholesterol in the lipid lamellae. Biophys. J. 8 (1968) 125-137
    • (1968) Biophys. J. , vol.8 , pp. 125-137
    • Rand, R.P.1    Luzzati, V.2
  • 178
    • 0024378918 scopus 로고
    • Hydration forces between phospholipid bilayers
    • Rand R.P., and Parsegian V.A. Hydration forces between phospholipid bilayers. Biochim. Biophys. Acta 988 (1989) 351-376
    • (1989) Biochim. Biophys. Acta , vol.988 , pp. 351-376
    • Rand, R.P.1    Parsegian, V.A.2
  • 179
    • 0015502332 scopus 로고
    • Cardiolipin forms hexagonal structures with divalent cations
    • Rand R.P., and Segupta S. Cardiolipin forms hexagonal structures with divalent cations. Biochim. Biophys. Acta 255 (1972) 484-492
    • (1972) Biochim. Biophys. Acta , vol.255 , pp. 484-492
    • Rand, R.P.1    Segupta, S.2
  • 180
    • 0023682461 scopus 로고
    • Variation in hydration forces between neutral phospholipid bilayers: Evidence for hydration attraction
    • Rand R.P., Fuller N., Parsegian V.A., and Rau D.C. Variation in hydration forces between neutral phospholipid bilayers: Evidence for hydration attraction. Biochemistry 27 (1988) 7711-7722
    • (1988) Biochemistry , vol.27 , pp. 7711-7722
    • Rand, R.P.1    Fuller, N.2    Parsegian, V.A.3    Rau, D.C.4
  • 181
    • 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., and Parsegian V.A. Membrane curvature, lipid segregation, and structural transitions for phospholipids under dual-solvent stress. Biochemistry 29 (1990) 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
  • 182
    • 0024501591 scopus 로고
    • Effect of chain unsaturation on the structure and thermotropic properties of galactocerebrosides
    • Reed R.A., and Shipley G.G. Effect of chain unsaturation on the structure and thermotropic properties of galactocerebrosides. Biophys. J. 55 (1989) 281-292
    • (1989) Biophys. J. , vol.55 , pp. 281-292
    • Reed, R.A.1    Shipley, G.G.2
  • 183
    • 0014202481 scopus 로고
    • Structure des phases liquide-cristallines de differents phospholipides, monoglycerides, sphingolipides, anydres ou en presence d'eau
    • Reiss-Husson F. Structure des phases liquide-cristallines de differents phospholipides, monoglycerides, sphingolipides, anydres ou en presence d'eau. J. Mol. Biol. 25 (1967) 363-382
    • (1967) J. Mol. Biol. , vol.25 , pp. 363-382
    • Reiss-Husson, F.1
  • 184
    • 4244212122 scopus 로고
    • The cell membrane concept
    • Robertson J.D. The cell membrane concept. J. Physiol. (London) 140 (1957) 58-59
    • (1957) J. Physiol. (London) , vol.140 , pp. 58-59
    • Robertson, J.D.1
  • 185
    • 77956660284 scopus 로고
    • Current problems of unit membrane structure and substructure
    • Japan Society for Cell Biology, Okayama, Japan
    • Robertson J.D. Current problems of unit membrane structure and substructure. Intracellular Membranous Structure. (1965), Japan Society for Cell Biology, Okayama, Japan
    • (1965) Intracellular Membranous Structure.
    • Robertson, J.D.1
  • 186
    • 0024403249 scopus 로고
    • Growth hormone activates phospholipase C in proximal tubular basolateral membranes from canine kidney
    • Rogers S.A., and Hammerman M.R. Growth hormone activates phospholipase C in proximal tubular basolateral membranes from canine kidney. Proc. Natl. Acad. Sci. U.S.A. 86 (1989) 6363-6369
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 6363-6369
    • Rogers, S.A.1    Hammerman, M.R.2
  • 187
    • 0024294407 scopus 로고
    • Phosphatidylinositol-glycan anchors of membrane proteins: Potential precursors of insulin mediators
    • Romero G. Phosphatidylinositol-glycan anchors of membrane proteins: Potential precursors of insulin mediators. Science 240 (1988) 509-511
    • (1988) Science , vol.240 , pp. 509-511
    • Romero, G.1
  • 188
    • 0017356323 scopus 로고
    • Membrane asymmetry
    • Rothman J.E., and Lenard J. Membrane asymmetry. Science 195 (1977) 743-753
    • (1977) Science , vol.195 , pp. 743-753
    • Rothman, J.E.1    Lenard, J.2
  • 189
    • 0024373072 scopus 로고
    • Coenzyme binding by 3-hydroxybutyrate dehydogenase, a lipid-requiring enzyme: Lecithin acts as an allosteric modulator to enhance the affinity for coenzyme
    • Rudy B., Dubois H., Mink R., Trommer W.E., McIntyre J.O., and Fleischer S. Coenzyme binding by 3-hydroxybutyrate dehydogenase, a lipid-requiring enzyme: Lecithin acts as an allosteric modulator to enhance the affinity for coenzyme. Biochemistry 28 (1989) 5354-5366
    • (1989) Biochemistry , vol.28 , pp. 5354-5366
    • Rudy, B.1    Dubois, H.2    Mink, R.3    Trommer, W.E.4    McIntyre, J.O.5    Fleischer, S.6
  • 190
    • 0022518425 scopus 로고
    • Thermal and structural behavior of natural cerebroside 3-sulfate in bilayer membranes
    • Ruocco M.J., and Shipley G.G. Thermal and structural behavior of natural cerebroside 3-sulfate in bilayer membranes. Biochim. Biophys. Acta 859 (1986) 246-256
    • (1986) Biochim. Biophys. Acta , vol.859 , pp. 246-256
    • Ruocco, M.J.1    Shipley, G.G.2
  • 191
    • 0020791847 scopus 로고
    • Galactocerebroside-phospholipid interaction in bilayer membranes
    • Ruocco M.J., Shipley G.G., and Oldfield E. Galactocerebroside-phospholipid interaction in bilayer membranes. Biophys. J. 43 (1983) 91-101
    • (1983) Biophys. J. , vol.43 , pp. 91-101
    • Ruocco, M.J.1    Shipley, G.G.2    Oldfield, E.3
  • 192
    • 0011230942 scopus 로고
    • X-ray study on egg-yolk lecithin: Unit cell data and electron density profile
    • Sakurai I., Iwayanagi S., Sakurai T., and Seto T. X-ray study on egg-yolk lecithin: Unit cell data and electron density profile. J. Mol. Biol. 117 (1977) 285-291
    • (1977) J. Mol. Biol. , vol.117 , pp. 285-291
    • Sakurai, I.1    Iwayanagi, S.2    Sakurai, T.3    Seto, T.4
  • 193
    • 0038731458 scopus 로고
    • The role of the polarization layers in hydration forces
    • Schiby D., and Ruckenstein E. The role of the polarization layers in hydration forces. Chem. Phys. Lett. 95 (1983) 435-438
    • (1983) Chem. Phys. Lett. , vol.95 , pp. 435-438
    • Schiby, D.1    Ruckenstein, E.2
  • 194
  • 195
    • 0025134135 scopus 로고
    • Structure of the inverted hexagonal phase, and non-lamellar phase transitions of lipids
    • Seddon J.M. Structure of the inverted hexagonal phase, and non-lamellar phase transitions of lipids. Biochim. Biophys. Acta 1031 (1990) 1-69
    • (1990) Biochim. Biophys. Acta , vol.1031 , pp. 1-69
    • Seddon, J.M.1
  • 196
    • 0020724194 scopus 로고
    • Calorimetric studies of the the gel-fluid and lamellar-inverted hexagonal phase transition in dialkyl- and diacylPEs
    • Seddon J.M., Cevc G., and Marsh D. Calorimetric studies of the the gel-fluid and lamellar-inverted hexagonal phase transition in dialkyl- and diacylPEs. Biochemistry 22 (1983) 1280-1289
    • (1983) Biochemistry , vol.22 , pp. 1280-1289
    • Seddon, J.M.1    Cevc, G.2    Marsh, D.3
  • 197
    • 0021755646 scopus 로고
    • X-ray diffraction study of the polymorphism of hydrated diacyl- and dialkylphosphatidylethanolamines
    • Seddon J.M., Cevc G., Kaye R.D., and Marsh D. X-ray diffraction study of the polymorphism of hydrated diacyl- and dialkylphosphatidylethanolamines. Biochemistry 23 (1984) 2634-2644
    • (1984) Biochemistry , vol.23 , pp. 2634-2644
    • Seddon, J.M.1    Cevc, G.2    Kaye, R.D.3    Marsh, D.4
  • 198
    • 0024282583 scopus 로고
    • The major Fc receptor in blood has a phosphatidylinositoyl anchor and is deficient in paroxysmal nocturnal haemoglobinuria
    • Selvaraj P., Rosse W.F., Silber R., and Springer T.A. The major Fc receptor in blood has a phosphatidylinositoyl anchor and is deficient in paroxysmal nocturnal haemoglobinuria. Nature (London) 333 (1988) 565-567
    • (1988) Nature (London) , vol.333 , pp. 565-567
    • Selvaraj, P.1    Rosse, W.F.2    Silber, R.3    Springer, T.A.4
  • 199
    • 0015971891 scopus 로고
    • Phase behavior and structure of aqueous dispersions of sphingomyelin
    • Shipley G.G., Avecilla L.S., and Small D.M. Phase behavior and structure of aqueous dispersions of sphingomyelin. J. Lipid Res. 15 (1974) 124-131
    • (1974) J. Lipid Res. , vol.15 , pp. 124-131
    • Shipley, G.G.1    Avecilla, L.S.2    Small, D.M.3
  • 200
    • 0022487880 scopus 로고
    • The depth of water penetration into lipid bilayers
    • Packer L. (Ed), Academic Press, San Diego
    • Simon S.A., and McIntosh T.J. The depth of water penetration into lipid bilayers. In: Packer L. (Ed). Methods in Enzymology 127 (1986), Academic Press, San Diego 511-521
    • (1986) Methods in Enzymology , vol.127 , pp. 511-521
    • Simon, S.A.1    McIntosh, T.J.2
  • 201
    • 0020040448 scopus 로고
    • Influence of cholesterol on water penetration into bilayers
    • Simon S.A., McIntosh T.J., and Latorre R. Influence of cholesterol on water penetration into bilayers. Science 216 (1982) 65-67
    • (1982) Science , vol.216 , pp. 65-67
    • Simon, S.A.1    McIntosh, T.J.2    Latorre, R.3
  • 202
    • 0015514472 scopus 로고
    • The fluid mosaic model of the structure of cell membranes
    • Singer S.J., and Nicolson G.L. The fluid mosaic model of the structure of cell membranes. Science 175 (1972) 720-731
    • (1972) Science , vol.175 , pp. 720-731
    • Singer, S.J.1    Nicolson, G.L.2
  • 203
    • 37049041267 scopus 로고
    • A new repeat structural element of mitochondrial and certain cytoplasmic membranes
    • Sjostrand F.S. A new repeat structural element of mitochondrial and certain cytoplasmic membranes. Nuture (London) 199 (1963) 1262-1271
    • (1963) Nuture (London) , vol.199 , pp. 1262-1271
    • Sjostrand, F.S.1
  • 204
    • 0014831444 scopus 로고
    • A new model for mitochondrial membranes based on structural and on biochemical evidence
    • Sjostrand F.S., and Barajas L. A new model for mitochondrial membranes based on structural and on biochemical evidence. J. Ultrustruct. Res. 32 (1970) 293-306
    • (1970) J. Ultrustruct. Res. , vol.32 , pp. 293-306
    • Sjostrand, F.S.1    Barajas, L.2
  • 205
    • 0014146912 scopus 로고
    • Phase equilibria and structure of dry and hydrated egg lecithin
    • Small D.M. Phase equilibria and structure of dry and hydrated egg lecithin. J. Lipid Res. 8 (1967) 551-557
    • (1967) J. Lipid Res. , vol.8 , pp. 551-557
    • Small, D.M.1
  • 206
    • 0022181816 scopus 로고
    • Membrane lipid composition and cellular function
    • Spector A.A., and Yorek M.A. Membrane lipid composition and cellular function. J. Lipid Res. 26 (1985) 1015-1035
    • (1985) J. Lipid Res. , vol.26 , pp. 1015-1035
    • Spector, A.A.1    Yorek, M.A.2
  • 207
    • 0016372224 scopus 로고
    • Topographical distribution of complex carbohydrates in the erythrocyte membrane
    • Steck T.L., and Dawson G. Topographical distribution of complex carbohydrates in the erythrocyte membrane. J. Biol. Chem. 249 (1974) 2135-2146
    • (1974) J. Biol. Chem. , vol.249 , pp. 2135-2146
    • Steck, T.L.1    Dawson, G.2
  • 208
    • 0014572123 scopus 로고
    • Current models for the structure of biological membranes
    • Stoeckenius W., and Engelman D.M. Current models for the structure of biological membranes. J. Cell Biol. 42 (1969) 613-646
    • (1969) J. Cell Biol. , vol.42 , pp. 613-646
    • Stoeckenius, W.1    Engelman, D.M.2
  • 209
    • 0021107614 scopus 로고
    • X-ray analysis and calorimetry on phosphatidylcholine model membranes. The influence of length and position of acyl chains upon structure and phase behavior
    • Stumpel J., Eibl H., and Nicksch A. X-ray analysis and calorimetry on phosphatidylcholine model membranes. The influence of length and position of acyl chains upon structure and phase behavior. Biochim. Biophys. Acta 727 (1983) 246-254
    • (1983) Biochim. Biophys. Acta , vol.727 , pp. 246-254
    • Stumpel, J.1    Eibl, H.2    Nicksch, A.3
  • 210
    • 0029758886 scopus 로고    scopus 로고
    • Structure of gel phase saturated lecithin bilayers: Temperature and chain length dependence
    • Sun W.-J., Tristram-Nagle S., Suter R.M., and Nagle J.F. Structure of gel phase saturated lecithin bilayers: Temperature and chain length dependence. Biophys. J. 71 (1996) 885-891
    • (1996) Biophys. J. , vol.71 , pp. 885-891
    • Sun, W.-J.1    Tristram-Nagle, S.2    Suter, R.M.3    Nagle, J.F.4
  • 211
    • 0015935391 scopus 로고
    • Structure and polymorphism of the hydrocarbon chains of lipids: A study of lecithin-water phases
    • Tardieu A., Luzzati V., and Reman F.C. Structure and polymorphism of the hydrocarbon chains of lipids: A study of lecithin-water phases. J. Mol. Biol. 75 (1973) 711-733
    • (1973) J. Mol. Biol. , vol.75 , pp. 711-733
    • Tardieu, A.1    Luzzati, V.2    Reman, F.C.3
  • 212
    • 0017086345 scopus 로고
    • X-ray diffraction studies of lecithin bilayers
    • Torbet J., and Wilkins M.H.F. X-ray diffraction studies of lecithin bilayers. J. Mol. Biol. 62 (1976) 447-458
    • (1976) J. Mol. Biol. , vol.62 , pp. 447-458
    • Torbet, J.1    Wilkins, M.H.F.2
  • 213
    • 0017054840 scopus 로고
    • Viscoelastic properties of erythrocyte membranes of differe vertebrate animals
    • Waugh R., and Evans E. Viscoelastic properties of erythrocyte membranes of differe vertebrate animals. Microvusc. Res. 12 (1976) 291-321
    • (1976) Microvusc. Res. , vol.12 , pp. 291-321
    • Waugh, R.1    Evans, E.2
  • 214
    • 0026683431 scopus 로고
    • Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of x-ray and neutron diffraction data. II. Distribution and packing of terminal methyl groups
    • Wiener M.C., and White S.H. Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of x-ray and neutron diffraction data. II. Distribution and packing of terminal methyl groups. Biophys. J. 61 (1992) 428-433
    • (1992) Biophys. J. , vol.61 , pp. 428-433
    • Wiener, M.C.1    White, S.H.2
  • 215
    • 0026729232 scopus 로고
    • Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of x-ray and neutron diffraction data. III. Complete structure
    • Wiener M.C., and White S.H. Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of x-ray and neutron diffraction data. III. Complete structure. Biophys. J. 61 (1992) 434-447
    • (1992) Biophys. J. , vol.61 , pp. 434-447
    • Wiener, M.C.1    White, S.H.2
  • 216
    • 0026048378 scopus 로고
    • Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of x-ray and neutron diffraction data.I. Scaling of neutron data and the distributions of double bonds and water
    • Wiener M.C., King G.I., and White S.H. Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of x-ray and neutron diffraction data.I. Scaling of neutron data and the distributions of double bonds and water. Biophys. J. 60 (1991) 568-576
    • (1991) Biophys. J. , vol.60 , pp. 568-576
    • Wiener, M.C.1    King, G.I.2    White, S.H.3
  • 218
    • 0017232478 scopus 로고
    • Structural analysis of hydrated egg lecithin and cholesterol bilayers II. Neutron diffraction
    • Worcester D.L., and Franks N.P. Structural analysis of hydrated egg lecithin and cholesterol bilayers II. Neutron diffraction. J. Mol. Biol. 100 (1976) 359-378
    • (1976) J. Mol. Biol. , vol.100 , pp. 359-378
    • Worcester, D.L.1    Franks, N.P.2
  • 219
    • 0014533507 scopus 로고
    • A structural analysis of nerve myelin
    • Worthington C.R., and Blaurock A.E. A structural analysis of nerve myelin. Biophy J. 9 (1969) 970
    • (1969) Biophy J. , vol.9 , pp. 970
    • Worthington, C.R.1    Blaurock, A.E.2
  • 220
    • 0015653504 scopus 로고
    • Structure of sarcoplasmic reticulum membranes at low resolution (17 Å)
    • Worthington C.R., and Liu S.C. Structure of sarcoplasmic reticulum membranes at low resolution (17 Å). Arch. Biochem. Biophys. 157 (1973) 573-579
    • (1973) Arch. Biochem. Biophys. , vol.157 , pp. 573-579
    • Worthington, C.R.1    Liu, S.C.2
  • 221
    • 0024599261 scopus 로고
    • Lipid regulation of cell membrane structure and function
    • Yeagle P.L. Lipid regulation of cell membrane structure and function. FASEB J. 3 (1989) 1833-1842
    • (1989) FASEB J. , vol.3 , pp. 1833-1842
    • Yeagle, P.L.1
  • 222
    • 0032502032 scopus 로고    scopus 로고
    • Molecular forces between membranes displaying neutral glycosphingolipids: Evidence for carbohydrate attraction
    • Yu Z.W., Calvert T.L., and Leckband D. Molecular forces between membranes displaying neutral glycosphingolipids: Evidence for carbohydrate attraction. Biochemistry 37 (1998) 1540-1550
    • (1998) Biochemistry , vol.37 , pp. 1540-1550
    • Yu, Z.W.1    Calvert, T.L.2    Leckband, D.3
  • 223
    • 0016633210 scopus 로고
    • Neutron diffraction studies on the location of water in lecithin bilayer model membranes
    • Zaccai G., Blasie J.K., and Schoenborn B.P. Neutron diffraction studies on the location of water in lecithin bilayer model membranes. Proc. Natl. Acad. Sci. U.S.A. 72 (1975) 376-380
    • (1975) Proc. Natl. Acad. Sci. U.S.A. , vol.72 , pp. 376-380
    • Zaccai, G.1    Blasie, J.K.2    Schoenborn, B.P.3
  • 224
    • 0018792917 scopus 로고
    • Neutron diffraction studies on phospha dylcholine model membranes II. Chain conformation and segmental disorder
    • Zaccai G., Buldt G., Seelig A., and Seelig J. Neutron diffraction studies on phospha dylcholine model membranes II. Chain conformation and segmental disorder. J. Mol. Biol. 134 (1979) 693-706
    • (1979) J. Mol. Biol. , vol.134 , pp. 693-706
    • Zaccai, G.1    Buldt, G.2    Seelig, A.3    Seelig, J.4
  • 225
    • 0027536597 scopus 로고
    • Choline phospholipids: Signal transduction and carcinogenesis
    • Zeisel S.H. Choline phospholipids: Signal transduction and carcinogenesis. FASE J. 7 (1993) 551-557
    • (1993) FASE J. , vol.7 , pp. 551-557
    • Zeisel, S.H.1
  • 226
    • 0026659409 scopus 로고
    • Gangliosides as modulators of cell function
    • Zeller C.B., and Marchase R.B. Gangliosides as modulators of cell function. Am. J. Physiol. 262 (1992) C1341-C1355
    • (1992) Am. J. Physiol. , vol.262
    • Zeller, C.B.1    Marchase, R.B.2


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