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Volumn 7, Issue 4, 1997, Pages 518-527

Small-scale lipid-membrane structure: Simulation versus experiment

Author keywords

[No Author keywords available]

Indexed keywords

COMPUTER SIMULATION; LIPID BILAYER; MEMBRANE STRUCTURE; MOLECULAR DYNAMICS; PRIORITY JOURNAL; REVIEW;

EID: 0030820281     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(97)80116-9     Document Type: Article
Times cited : (118)

References (110)
  • 1
    • 0025993884 scopus 로고
    • Physical properties of the fluid lipid-bilayer component of cell membranes: A perspective
    • Bloom M, Evans E, Mouritsen OG. Physical properties of the fluid lipid-bilayer component of cell membranes: a perspective. Quart Rev Biophys. 24:1991;293-397.
    • (1991) Quart Rev Biophys , vol.24 , pp. 293-397
    • Bloom, M.1    Evans, E.2    Mouritsen, O.G.3
  • 2
    • 0343188780 scopus 로고
    • R. Lipowsky, Sackmann E. Amsterdam: Elsevier
    • Structure and dynamics of membranes. Lipowsky R, Sackmann E. Handbook of Biological Physics. 1a,b:1995;1-1020 Elsevier, Amsterdam.
    • (1995) Handbook of Biological Physics , vol.1 , pp. 1-1020
  • 3
    • 0031027931 scopus 로고    scopus 로고
    • The lateral pressure profile in membranes: A physical mechanism of general anesthesia
    • of outstanding interest. A presentation of an exciting hypothesis that the mechanism of general anaesthesia involves a change in the lateral pressure profile of the membrane.
    • Cantor RS. The lateral pressure profile in membranes: a physical mechanism of general anesthesia. of outstanding interest Biochemistry. 36:1997;2339-2344 A presentation of an exciting hypothesis that the mechanism of general anaesthesia involves a change in the lateral pressure profile of the membrane.
    • (1997) Biochemistry , vol.36 , pp. 2339-2344
    • Cantor, R.S.1
  • 4
    • 0001794260 scopus 로고
    • Detection of lipid domains in biological membranes
    • Tocanne JF. Detection of lipid domains in biological membranes. Comm Mol Cell Biophys. 8:1992;53-72.
    • (1992) Comm Mol Cell Biophys , vol.8 , pp. 53-72
    • Tocanne, J.F.1
  • 5
    • 0002359017 scopus 로고
    • Domain organization in biological membranes
    • L.O. Bergelson, K. Gawrisch, J.A. Feretti, & R. Blumenthal.
    • Bergelson LO, Gawrisch K, Feretti JA, Blumenthal R. Domain organization in biological membranes. Mol Membr Biol. 12:1995;1-162.
    • (1995) Mol Membr Biol , vol.12 , pp. 1-162
  • 6
    • 0028882772 scopus 로고
    • Autocatalytic gene expression occurs via transertion and membrane domain formation and underlies differentiation in bacteria: A model
    • Norris V, Madsen MS. Autocatalytic gene expression occurs via transertion and membrane domain formation and underlies differentiation in bacteria: a model. J Mol Biol. 253:1995;739-748.
    • (1995) J Mol Biol , vol.253 , pp. 739-748
    • Norris, V.1    Madsen, M.S.2
  • 7
    • 10244224044 scopus 로고    scopus 로고
    • Myristoylated alanine-rich C kinase substrate (MARCKS) produces reversible inhibition of phospholipase C by sequestering phosphatidylinositol 4,5-bisphosphate in lateral domains
    • of special interest. Direct fluorescence microscopy imaging of the induction of lipid domains enriched in phosphatidylserine by the MARCKS peptide.
    • Glaser M, Wanaski S, Buser CA, Boguslavsky V, Rashidzada W, Morris A, Rebecchi M, Scarlata SF, Runnels LW, Prestwich GD, et al. Myristoylated alanine-rich C kinase substrate (MARCKS) produces reversible inhibition of phospholipase C by sequestering phosphatidylinositol 4,5-bisphosphate in lateral domains. of special interest J Biol Chem. 271:1996;26187-26193 Direct fluorescence microscopy imaging of the induction of lipid domains enriched in phosphatidylserine by the MARCKS peptide.
    • (1996) J Biol Chem , vol.271 , pp. 26187-26193
    • Glaser, M.1    Wanaski, S.2    Buser, C.A.3    Boguslavsky, V.4    Rashidzada, W.5    Morris, A.6    Rebecchi, M.7    Scarlata, S.F.8    Runnels, L.W.9    Prestwich, G.D.10
  • 8
    • 0029904712 scopus 로고    scopus 로고
    • Formation of membrane domains during the activation of protein kinase C
    • Yang L, Glaser M. Formation of membrane domains during the activation of protein kinase C. Biochemistry. 35:1996;13966-13974.
    • (1996) Biochemistry , vol.35 , pp. 13966-13974
    • Yang, L.1    Glaser, M.2
  • 9
    • 0029987046 scopus 로고    scopus 로고
    • The spatial distribution of phospholipids and glycolipids in the membrane of the bacterium Micrococcus luteus varies during the cell cycle
    • of outstanding interest. The lateral distribution of phospholipids and glycolipids is shown to vary during the cell cycle. This work shows for the first time that changes in the lateral organization of a membrane are involved in membrane biogenesis and cell division.
    • Welby M, Poquet Y, Tocanne JF. The spatial distribution of phospholipids and glycolipids in the membrane of the bacterium Micrococcus luteus varies during the cell cycle. of outstanding interest FEBS Lett. 384:1996;107-111 The lateral distribution of phospholipids and glycolipids is shown to vary during the cell cycle. This work shows for the first time that changes in the lateral organization of a membrane are involved in membrane biogenesis and cell division.
    • (1996) FEBS Lett , vol.384 , pp. 107-111
    • Welby, M.1    Poquet, Y.2    Tocanne, J.F.3
  • 10
    • 0030222116 scopus 로고    scopus 로고
    • Cell surface organization by the membrane skeleton
    • Kusumi A, Yashushi S. Cell surface organization by the membrane skeleton. Curr Opin Cell Biol. 8:1996;566-574.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 566-574
    • Kusumi, A.1    Yashushi, S.2
  • 11
    • 0029740182 scopus 로고    scopus 로고
    • Ligand binding regulates the directed movement of β1 integrins on fibroblasts
    • Felsenfeld DP, Choquet D, Sheetz MP. Ligand binding regulates the directed movement of β1 integrins on fibroblasts. Nature. 383:1996;438-440.
    • (1996) Nature , vol.383 , pp. 438-440
    • Felsenfeld, D.P.1    Choquet, D.2    Sheetz, M.P.3
  • 12
    • 0030066514 scopus 로고    scopus 로고
    • Conformational order of phospholipids incorporated into human erythrocytes: An FTIR spectroscopic study
    • Moore DJ, Sills RH, Patel N, Mendelsohn R. Conformational order of phospholipids incorporated into human erythrocytes: an FTIR spectroscopic study. Biochemistry. 35:1996;229-235.
    • (1996) Biochemistry , vol.35 , pp. 229-235
    • Moore, D.J.1    Sills, R.H.2    Patel, N.3    Mendelsohn, R.4
  • 13
    • 0031033945 scopus 로고    scopus 로고
    • Conformational order of specific phospholipids in human erythrocytes: Correlations with changes in cell shape
    • Moore DJ, Sills RH, Mendelsohn R. Conformational order of specific phospholipids in human erythrocytes: correlations with changes in cell shape. Biochemistry. 36:1997;660-664.
    • (1997) Biochemistry , vol.36 , pp. 660-664
    • Moore, D.J.1    Sills, R.H.2    Mendelsohn, R.3
  • 14
    • 0028832436 scopus 로고
    • Temperature-induced changes in fluorescence properties as a probe of porphyrin microenvironment in lipid membranes
    • Richelli F, Gobbo S, Jori G, Salet C, Moreno G. Temperature-induced changes in fluorescence properties as a probe of porphyrin microenvironment in lipid membranes. Eur Biochem J. 233:1995;165-170.
    • (1995) Eur Biochem J , vol.233 , pp. 165-170
    • Richelli, F.1    Gobbo, S.2    Jori, G.3    Salet, C.4    Moreno, G.5
  • 15
    • 0029194215 scopus 로고
    • Micro-, nano- And mesoscale heterogeneity at lipid bilayers and its influence on macroscopic membrane properties
    • Mouritsen OG, Jørgensen K. Micro-, nano- and mesoscale heterogeneity at lipid bilayers and its influence on macroscopic membrane properties. Mol Membr Biol. 12:1995;15-20.
    • (1995) Mol Membr Biol , vol.12 , pp. 15-20
    • Mouritsen, O.G.1    Jørgensen, K.2
  • 17
    • 0029152051 scopus 로고
    • The morphology of lipid membranes
    • Lipowsky R. The morphology of lipid membranes. Curr Opin Struct Biol. 5:1995;531-540.
    • (1995) Curr Opin Struct Biol , vol.5 , pp. 531-540
    • Lipowsky, R.1
  • 18
    • 0342319301 scopus 로고    scopus 로고
    • Morphology and dynamics of vesicles
    • Seifert U. Morphology and dynamics of vesicles. Curr Opin Coll Interface Sci. 1:1996;350-357.
    • (1996) Curr Opin Coll Interface Sci , vol.1 , pp. 350-357
    • Seifert, U.1
  • 19
    • 0003535316 scopus 로고    scopus 로고
    • of special interest. K. Merz, Roux B. Birkhäuser, Boston, A comprehensive collection of papers on membrane structure and dynamics with emphasis on the relation between theoretical calculations, in particular molecular dynamics calculations, and experimental observations made using a great variety of different experimental techniques
    • of special interest Merz K, Roux B. Biological Membranes: A Molecular Perspective from Computation to Experiment. 1996;Birkhäuser, Boston, A comprehensive collection of papers on membrane structure and dynamics with emphasis on the relation between theoretical calculations, in particular molecular dynamics calculations, and experimental observations made using a great variety of different experimental techniques.
    • (1996) Biological Membranes: A Molecular Perspective from Computation to Experiment
  • 20
    • 0028867364 scopus 로고
    • Constant pressure and temperature molecular dynamics simulation of a fully hydrated liquid crystal phase dipalmitoylphosphatidylcholine bilayer
    • Tu K, Tobias DJ, Klein ML. Constant pressure and temperature molecular dynamics simulation of a fully hydrated liquid crystal phase dipalmitoylphosphatidylcholine bilayer. Biophys J. 69:1995;2558-2562.
    • (1995) Biophys J , vol.69 , pp. 2558-2562
    • Tu, K.1    Tobias, D.J.2    Klein, M.L.3
  • 21
    • 22544450619 scopus 로고
    • Molecular dynamics study of a membrane/water interface
    • Zhou F, Schulten K. Molecular dynamics study of a membrane/water interface. J Phys Chem. 99:1995;2194-2207.
    • (1995) J Phys Chem , vol.99 , pp. 2194-2207
    • Zhou, F.1    Schulten, K.2
  • 22
    • 0030031374 scopus 로고    scopus 로고
    • Molecular dynamics investigation of the structure of a fully hydrated gel-phase dipalmitoylphosphatidylcholine bilayer
    • Tu K, Tobias DJ, Blasie K, Klein ML. Molecular dynamics investigation of the structure of a fully hydrated gel-phase dipalmitoylphosphatidylcholine bilayer. Biophys J. 70:1996;595-608.
    • (1996) Biophys J , vol.70 , pp. 595-608
    • Tu, K.1    Tobias, D.J.2    Blasie, K.3    Klein, M.L.4
  • 23
    • 0000112789 scopus 로고    scopus 로고
    • Molecular dynamics simulation of a fully hydrated dipalmitoylphosphatidylcholine bilayer with different macroscopic boundary conditions and parameters
    • Tieleman DP, Berendsen HJC. Molecular dynamics simulation of a fully hydrated dipalmitoylphosphatidylcholine bilayer with different macroscopic boundary conditions and parameters. J Chem Phys. 105:1996;4871-4880.
    • (1996) J Chem Phys , vol.105 , pp. 4871-4880
    • Tieleman, D.P.1    Berendsen, H.J.C.2
  • 24
    • 0000978655 scopus 로고    scopus 로고
    • Free volume properties of a simulated lipid membrane
    • Marrink SJ, Sok RM, Berendsen HJC. Free volume properties of a simulated lipid membrane. J Chem Phys. 104:1996;9090-9099.
    • (1996) J Chem Phys , vol.104 , pp. 9090-9099
    • Marrink, S.J.1    Sok, R.M.2    Berendsen, H.J.C.3
  • 25
    • 0030999097 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature
    • Berger O, Edholm O, Jähnig F. Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature. Biophys J. 27:1997;2002-2013.
    • (1997) Biophys J , vol.27 , pp. 2002-2013
    • Berger, O.1    Edholm, O.2    Jähnig, F.3
  • 26
    • 0030228053 scopus 로고    scopus 로고
    • Commentary: Surface tension of biomembranes
    • Roux B. Commentary: surface tension of biomembranes. Biophys J. 71:1996;1346-1347.
    • (1996) Biophys J , vol.71 , pp. 1346-1347
    • Roux, B.1
  • 27
    • 0029767694 scopus 로고    scopus 로고
    • On simulating lipid bilayers with an applied surface tension: Periodic boundary conditions and undulations
    • of special interest. This paper includes a discussion of the concept of surface tension in a small system compared with the macroscopic surface tension.
    • Feller SE, Pastor RW. On simulating lipid bilayers with an applied surface tension: periodic boundary conditions and undulations. of special interest Biophys J. 71:1996;1350-1355 This paper includes a discussion of the concept of surface tension in a small system compared with the macroscopic surface tension.
    • (1996) Biophys J , vol.71 , pp. 1350-1355
    • Feller, S.E.1    Pastor, R.W.2
  • 28
    • 0001733886 scopus 로고    scopus 로고
    • Role of water in hydration force acting between lipid bilayers
    • 16PC bilayers indicate that the effect on the water structure due to the interface only shows over a very short range and that the bilayer is rough on the molecular scale. The structures of the solvating water molecules are proposed to be responsible for the different hydration forces that act between the two types of bilayers.
    • 16PC bilayers indicate that the effect on the water structure due to the interface only shows over a very short range and that the bilayer is rough on the molecular scale. The structures of the solvating water molecules are proposed to be responsible for the different hydration forces that act between the two types of bilayers.
    • (1996) Langmuir , vol.12 , pp. 2625-2629
    • Perera, L.1    Essmann, U.2    Berkowitz, M.L.3
  • 30
    • 0029038366 scopus 로고
    • Interaction of an amphiphilic peptide with a phospholipid bilayer surface by molecular dynamics simulation study
    • Huang P, Loew GH. Interaction of an amphiphilic peptide with a phospholipid bilayer surface by molecular dynamics simulation study. J Biomol Struct Dynamics. 12:1995;937-956.
    • (1995) J Biomol Struct Dynamics , vol.12 , pp. 937-956
    • Huang, P.1    Loew, G.H.2
  • 31
    • 0030038849 scopus 로고    scopus 로고
    • Structure, energetics, and dynamics of lipid - protein interactions: A molecular dynamics study of the gramicidin A channel in a DMPC bilayer
    • Wolf TB, Roux B. Structure, energetics, and dynamics of lipid - protein interactions: a molecular dynamics study of the gramicidin A channel in a DMPC bilayer. Proteins. 24:1996;92-114.
    • (1996) Proteins , vol.24 , pp. 92-114
    • Wolf, T.B.1    Roux, B.2
  • 32
    • 0030966534 scopus 로고    scopus 로고
    • Transmembrane helix structure, dynamics and interactions: Multi-nanosecond, molecular dynamics simulations
    • in press
    • Shen L, Bassolino D, Stouch T. Transmembrane helix structure, dynamics and interactions: multi-nanosecond, molecular dynamics simulations. Biophys J. 1997;. in press.
    • (1997) Biophys J
    • Shen, L.1    Bassolino, D.2    Stouch, T.3
  • 34
    • 0029890186 scopus 로고    scopus 로고
    • 2 on a membrane surface
    • of outstanding interest. Full scale molecular dynamics simulation of a lipid bilayer surface showing that desolvation of the lipids takes place in a tightly bound protein - bilayer complex. Furthermore, the simulation provides an explanation for why the activity of the enzyme is enhanced after accumulation of a critical amount of negative reaction products.
    • 2 on a membrane surface. of outstanding interest Proteins. 25:1996;12-27 Full scale molecular dynamics simulation of a lipid bilayer surface showing that desolvation of the lipids takes place in a tightly bound protein - bilayer complex. Furthermore, the simulation provides an explanation for why the activity of the enzyme is enhanced after accumulation of a critical amount of negative reaction products.
    • (1996) Proteins , vol.25 , pp. 12-27
    • Zhou, F.1    Schulten, K.2
  • 35
    • 0029769798 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a protein on hydrophobic and hydrophilic surfaces
    • Tobias DJ, Mar W, Blasie JK, Klein ML. Molecular dynamics simulations of a protein on hydrophobic and hydrophilic surfaces. Biophys J. 71:1996;2933-2941.
    • (1996) Biophys J , vol.71 , pp. 2933-2941
    • Tobias, D.J.1    Mar, W.2    Blasie, J.K.3    Klein, M.L.4
  • 36
    • 0029026347 scopus 로고
    • Structure and fluctuations of a bacteriorhodopsin in the purple membrane: A molecular dynamics study
    • Edholm O, Berger O, Jähnig F. Structure and fluctuations of a bacteriorhodopsin in the purple membrane: a molecular dynamics study. J Mol Biol. 250:1995;94-111.
    • (1995) J Mol Biol , vol.250 , pp. 94-111
    • Edholm, O.1    Berger, O.2    Jähnig, F.3
  • 37
    • 0029782010 scopus 로고    scopus 로고
    • Proton transport across transient single-file water pores in a lipid membrane studied by molecular dynamics simulations
    • Marrink SJ, Jähnig F, Berendsen HJC. Proton transport across transient single-file water pores in a lipid membrane studied by molecular dynamics simulations. Biophys J. 71:1996;632-647.
    • (1996) Biophys J , vol.71 , pp. 632-647
    • Marrink, S.J.1    Jähnig, F.2    Berendsen, H.J.C.3
  • 38
    • 0000951252 scopus 로고    scopus 로고
    • Effect of electrostatic force truncation on interfacial and transport properties of water
    • Feller SE, Pastor RW, Rojnuckarin A, Bogusz S, Brooks BR. Effect of electrostatic force truncation on interfacial and transport properties of water. J Phys Chem. 100:1996;17011-17020.
    • (1996) J Phys Chem , vol.100 , pp. 17011-17020
    • Feller, S.E.1    Pastor, R.W.2    Rojnuckarin, A.3    Bogusz, S.4    Brooks, B.R.5
  • 41
    • 0029738338 scopus 로고    scopus 로고
    • Indirect evidence for lipid-domain formation in the transition region of phospholipid bilayers by two-probe fluorescence energy transfer
    • of special interest. Combined Monte Carlo simulation calculations and fluorescence energy transfer experiments on dipalmitoylphosphatidylcholine lipid bilayers in the temperature region of the main phase transition indicate the existence of a heterogeneous lateral domain structure.
    • Pedersen S, Jørgensen K, Bækmark T, Mouritsen OG. Indirect evidence for lipid-domain formation in the transition region of phospholipid bilayers by two-probe fluorescence energy transfer. of special interest Biophys J. 71:1996;554-560 Combined Monte Carlo simulation calculations and fluorescence energy transfer experiments on dipalmitoylphosphatidylcholine lipid bilayers in the temperature region of the main phase transition indicate the existence of a heterogeneous lateral domain structure.
    • (1996) Biophys J , vol.71 , pp. 554-560
    • Pedersen, S.1    Jørgensen, K.2    Bækmark, T.3    Mouritsen, O.G.4
  • 42
    • 0029993253 scopus 로고    scopus 로고
    • Entropy-driven instability and rupture of fluid membranes
    • of special interest. This Monte Carlo simulation study shows the conditions for hole formation in a bilayer model that is subject to external stress.
    • Shillcock JC, Boal DH. Entropy-driven instability and rupture of fluid membranes. of special interest Biophys J. 71:1996;317-326 This Monte Carlo simulation study shows the conditions for hole formation in a bilayer model that is subject to external stress.
    • (1996) Biophys J , vol.71 , pp. 317-326
    • Shillcock, J.C.1    Boal, D.H.2
  • 43
    • 4243344129 scopus 로고    scopus 로고
    • Kinetics of phase ordering in a two-component fluid membrane
    • in press
    • Kumar PBS, Rao M. Kinetics of phase ordering in a two-component fluid membrane. Phys Rev E. 1997;. in press.
    • (1997) Phys Rev e
    • Kumar, P.B.S.1    Rao, M.2
  • 44
    • 0030270331 scopus 로고    scopus 로고
    • Random surface discretizations and the renormalization of the bending rigidity
    • Gompper G, Kroll DM. Random surface discretizations and the renormalization of the bending rigidity. J Phys I. 6:1996;1305-1320.
    • (1996) J Phys I , vol.6 , pp. 1305-1320
    • Gompper, G.1    Kroll, D.M.2
  • 45
    • 5244279227 scopus 로고    scopus 로고
    • Self-avoiding tethered membranes with quenched random internal disorders
    • Mori S: Self-avoiding tethered membranes with quenched random internal disorders. Phys Rev E 54:338-348.
    • Phys Rev e , vol.54 , pp. 338-348
    • Mori, S.1
  • 46
    • 0000844063 scopus 로고    scopus 로고
    • Phase transitions and anisotropic responses of planar triangular nets under large deformation
    • in press
    • Discher DE, Boal DH, Boey SK. Phase transitions and anisotropic responses of planar triangular nets under large deformation. Phys Rev E. 1997;. in press.
    • (1997) Phys Rev e
    • Discher, D.E.1    Boal, D.H.2    Boey, S.K.3
  • 47
    • 0343188775 scopus 로고    scopus 로고
    • Vesicle ensembles in two dimensions
    • of special interest size distribution as functions of density and bending rigidity
    • Dammann B, Ipsen JH. Vesicle ensembles in two dimensions. of special interest Europhys Lett. 1997; The first Monte Carlo simulation of a whole ensemble of vesicles leads to the phase equilibria and the vesicle-size distribution as functions of density and bending rigidity.
    • (1997) Europhys Lett
    • Dammann, B.1    Ipsen, J.H.2
  • 48
    • 0030050141 scopus 로고    scopus 로고
    • Anomalous diffusion due to binding: A Monte Carlo study
    • Saxton MJ. Anomalous diffusion due to binding: a Monte Carlo study. Biophys J. 70:1996;1250-1262.
    • (1996) Biophys J , vol.70 , pp. 1250-1262
    • Saxton, M.J.1
  • 49
    • 0029993064 scopus 로고    scopus 로고
    • Simulations of reversible protein aggregate and crystal structure
    • Patro SY, Przybycien TM. Simulations of reversible protein aggregate and crystal structure. Biophys J. 70:1996;2888-2902.
    • (1996) Biophys J , vol.70 , pp. 2888-2902
    • Patro, S.Y.1    Przybycien, T.M.2
  • 50
    • 0030071247 scopus 로고    scopus 로고
    • A Monte Carlo simulation study of protein-induced heat capacity changes and lipid-induced protein clustering
    • Hemiburg T, Biltonen RL. A Monte Carlo simulation study of protein-induced heat capacity changes and lipid-induced protein clustering. Biophys J. 70:1996;84-96.
    • (1996) Biophys J , vol.70 , pp. 84-96
    • Hemiburg, T.1    Biltonen, R.L.2
  • 51
    • 0030771336 scopus 로고    scopus 로고
    • Wetting and capillary condensation as means of protein organization in membranes
    • in press
    • Gil T, Sabra M, Ipsen JH, Mouritsen OG. Wetting and capillary condensation as means of protein organization in membranes. Biophys J. 1997;. in press.
    • (1997) Biophys J
    • Gil, T.1    Sabra, M.2    Ipsen, J.H.3    Mouritsen, O.G.4
  • 52
    • 0029762032 scopus 로고    scopus 로고
    • Insertion and hairpin formation of membrane proteins: A Monte Carlo study
    • Baumgärtner A. Insertion and hairpin formation of membrane proteins: a Monte Carlo study. Biophys J. 71:1996;1248-1255.
    • (1996) Biophys J , vol.71 , pp. 1248-1255
    • Baumgärtner, A.1
  • 53
    • 0029791045 scopus 로고    scopus 로고
    • Resonance energy transfer in a model system of membranes: Application to gel and liquid crystalline phases
    • Loura LMS, Fedorov A, Prieto M. Resonance energy transfer in a model system of membranes: application to gel and liquid crystalline phases. Biophys J. 71:1996;1823-1836.
    • (1996) Biophys J , vol.71 , pp. 1823-1836
    • Loura, L.M.S.1    Fedorov, A.2    Prieto, M.3
  • 54
    • 0029863717 scopus 로고    scopus 로고
    • Evidence for the formation of microdomains in liquid crystalline large unilamellar vesicles caused by hydrophobic mismatch of the constituent phospholipids
    • of special interest. Changes in the eximer-to-monomer fluorescence emission spectra are taken as evidence for the enrichment of probes within lipid domains to which they are less well matched hydrophobically.
    • Lehtonen JYA, Holopainen JM, Kinnunen PKJ. Evidence for the formation of microdomains in liquid crystalline large unilamellar vesicles caused by hydrophobic mismatch of the constituent phospholipids. of special interest Biophys J. 70:1996;1753-1760 Changes in the eximer-to-monomer fluorescence emission spectra are taken as evidence for the enrichment of probes within lipid domains to which they are less well matched hydrophobically.
    • (1996) Biophys J , vol.70 , pp. 1753-1760
    • Lehtonen, J.Y.A.1    Holopainen, J.M.2    Kinnunen, P.K.J.3
  • 55
    • 0001206434 scopus 로고    scopus 로고
    • Small-angle neutron scattering from multilamellar lipid bilayers: Theory, model, and experiment
    • Lemmich J, Mortensen K, Ipsen JH, Hønger T, Bauer R, Mouritsen OG. Small-angle neutron scattering from multilamellar lipid bilayers: theory, model, and experiment. Phys Rev E. 53:1996;5169-5180.
    • (1996) Phys Rev e , vol.53 , pp. 5169-5180
    • Lemmich, J.1    Mortensen, K.2    Ipsen, J.H.3    Hønger, T.4    Bauer, R.5    Mouritsen, O.G.6
  • 56
    • 0030031119 scopus 로고    scopus 로고
    • Small angle X-ray scattering from lipid bilayers is well described by modified Caillé theory, but not by paracrystalline theory
    • Zhang R, Tristram-Nagle S, Sun W-J, Headrick RL, Irving TC, Suter RM, Nagle JF. Small angle X-ray scattering from lipid bilayers is well described by modified Caillé theory, but not by paracrystalline theory. Biophys J. 70:1996;349-357.
    • (1996) Biophys J , vol.70 , pp. 349-357
    • Zhang, R.1    Tristram-Nagle, S.2    Sun, W.-J.3    Headrick, R.L.4    Irving, T.C.5    Suter, R.M.6    Nagle, J.F.7
  • 58
    • 0030849774 scopus 로고    scopus 로고
    • The effect of cholesterol in small amounts on lipid-bilayer softness in the region of the main phase transition
    • Lemmich J, Mortensen K, Ipsen JH, Hønger T, Bauer R, Mouritsen OG. The effect of cholesterol in small amounts on lipid-bilayer softness in the region of the main phase transition. Eur Biophys J. 25:1997;293-304.
    • (1997) Eur Biophys J , vol.25 , pp. 293-304
    • Lemmich, J.1    Mortensen, K.2    Ipsen, J.H.3    Hønger, T.4    Bauer, R.5    Mouritsen, O.G.6
  • 59
    • 0028825706 scopus 로고
    • IR spectroscopic determination of gel state miscibility in long-chain phosphatidylcholine mixtures
    • Mendelsohn R, Liang GL, Strauss HL, Snyder RG. IR spectroscopic determination of gel state miscibility in long-chain phosphatidylcholine mixtures. Biophys J. 69:1995;1987-1998.
    • (1995) Biophys J , vol.69 , pp. 1987-1998
    • Mendelsohn, R.1    Liang, G.L.2    Strauss, H.L.3    Snyder, R.G.4
  • 60
    • 0028077246 scopus 로고
    • Detection of phase separation in fluid phosphatidylserine/phosphatidylcholine mixtures
    • Hinderliter AK, Huang J, Feigenson GW. Detection of phase separation in fluid phosphatidylserine/phosphatidylcholine mixtures. Biophys J. 67:1994;1906-1911.
    • (1994) Biophys J , vol.67 , pp. 1906-1911
    • Hinderliter, A.K.1    Huang, J.2    Feigenson, G.W.3
  • 61
    • 0029738420 scopus 로고    scopus 로고
    • Fluorescence-quenching study of percolation and compartmentalization in two-phase lipid bilayers
    • Piknová B, Marsh D, Thompson TE. Fluorescence-quenching study of percolation and compartmentalization in two-phase lipid bilayers. Biophys J. 71:1996;892-897.
    • (1996) Biophys J , vol.71 , pp. 892-897
    • Piknová, B.1    Marsh, D.2    Thompson, T.E.3
  • 62
    • 0029816063 scopus 로고    scopus 로고
    • Topology of gel-phase domains and lipid mixing properties in phase separated two-component phosphatidylcholine bilayers
    • of outstanding interest. A combined Monte Carlo simulation study and fluorescence recovery after photobleaching experiment of the local domain structure in the gel/fluid phase coexistence region of a series of binary lipid mixtures.
    • Schram V, Lin HN, Thompson TE. Topology of gel-phase domains and lipid mixing properties in phase separated two-component phosphatidylcholine bilayers. of outstanding interest Biophys J. 71:1996;1811-1822 A combined Monte Carlo simulation study and fluorescence recovery after photobleaching experiment of the local domain structure in the gel/fluid phase coexistence region of a series of binary lipid mixtures.
    • (1996) Biophys J , vol.71 , pp. 1811-1822
    • Schram, V.1    Lin, H.N.2    Thompson, T.E.3
  • 63
    • 0031121546 scopus 로고    scopus 로고
    • Lipid domains as obstacles for lateral diffusion in supported bilayers probed at different time and length scales by two-dimensional exchange and field gradient solid state NMR
    • Dolainsky C, Karakatsanis P, Bayerl TM. Lipid domains as obstacles for lateral diffusion in supported bilayers probed at different time and length scales by two-dimensional exchange and field gradient solid state NMR. Phys Rev E. 55:1997;4512-4521.
    • (1997) Phys Rev e , vol.55 , pp. 4512-4521
    • Dolainsky, C.1    Karakatsanis, P.2    Bayerl, T.M.3
  • 64
    • 0030053808 scopus 로고    scopus 로고
    • The effects of increasing membrane curvature on the phase transition and mixing behavior of a DMPC-d54/DSPC (1:1) lipid mixture as studied by Fourier-transform infrared spectroscopy and differential-scanning calorimetry
    • Brumm T, Jørgensen K, Mouritsen OG, Bayerl T. The effects of increasing membrane curvature on the phase transition and mixing behavior of a DMPC-d54/DSPC (1:1) lipid mixture as studied by Fourier-transform infrared spectroscopy and differential-scanning calorimetry. Biophys J. 70:1996;1373-1379.
    • (1996) Biophys J , vol.70 , pp. 1373-1379
    • Brumm, T.1    Jørgensen, K.2    Mouritsen, O.G.3    Bayerl, T.4
  • 65
    • 2542436287 scopus 로고
    • Curvature-induced lateral phase separation in two-component vesicles
    • Seifert U. Curvature-induced lateral phase separation in two-component vesicles. Phys Rev Lett. 70:1993;1335-1338.
    • (1993) Phys Rev Lett , vol.70 , pp. 1335-1338
    • Seifert, U.1
  • 66
    • 0029127450 scopus 로고
    • Phase separation dynamics and lateral organization of two-component lipid membranes
    • Jørgensen K, Mouritsen OG. Phase separation dynamics and lateral organization of two-component lipid membranes. Biophys J. 95:1995;942-954.
    • (1995) Biophys J , vol.95 , pp. 942-954
    • Jørgensen, K.1    Mouritsen, O.G.2
  • 67
    • 33751155423 scopus 로고    scopus 로고
    • Slow nonequilibrium dynamical rearrangement of the lateral structure of a lipid membrane
    • of outstanding interest. A combined Monte Carlo and experimental study of the time evolution of a phase separating lipid bilayer indicates for the first time that the relaxation time is extremely long - of the order of hours.
    • Jørgensen K, Klinger A, Braiman M, Biltonen RL. Slow nonequilibrium dynamical rearrangement of the lateral structure of a lipid membrane. of outstanding interest J Phys Chem. 100:1996;2766-2769 A combined Monte Carlo and experimental study of the time evolution of a phase separating lipid bilayer indicates for the first time that the relaxation time is extremely long - of the order of hours.
    • (1996) J Phys Chem , vol.100 , pp. 2766-2769
    • Jørgensen, K.1    Klinger, A.2    Braiman, M.3    Biltonen, R.L.4
  • 68
    • 0021869659 scopus 로고
    • 1-Palmitoyl-2-pyrenedecanoyl glycerophospholipids as membrane probes: Evidence for regular distribution in liquid crystalline phosphatidylcholine bilayers
    • Somerharju P, Virtanen JA, Eklund KK, Vainio P, Kinnunen PKJ. 1-Palmitoyl-2-pyrenedecanoyl glycerophospholipids as membrane probes: evidence for regular distribution in liquid crystalline phosphatidylcholine bilayers. Biochemistry. 24:1985;2773-2781.
    • (1985) Biochemistry , vol.24 , pp. 2773-2781
    • Somerharju, P.1    Virtanen, J.A.2    Eklund, K.K.3    Vainio, P.4    Kinnunen, P.K.J.5
  • 69
    • 0001317132 scopus 로고    scopus 로고
    • Fluorescence evidence for cholesterol regular distribution in phosphatidylcholine and in sphingomyelin lipid bilayers
    • Chong PL-G, Liu F, Wang MM, Truong K, Sugar IP, Brown RE. Fluorescence evidence for cholesterol regular distribution in phosphatidylcholine and in sphingomyelin lipid bilayers. J Fluorescence. 6:1996;221-230.
    • (1996) J Fluorescence , vol.6 , pp. 221-230
    • Chong, P.-G.1    Liu, F.2    Wang, M.M.3    Truong, K.4    Sugar, I.P.5    Brown, R.E.6
  • 70
    • 0343188772 scopus 로고    scopus 로고
    • Evidence for superlattice-like lateral organization in fluid phosphatidylcholine phosphatidylethanolamine bilayers [abstract]
    • Cheng KH, Ruonale M, Virtanen, Somerharju P. Evidence for superlattice-like lateral organization in fluid phosphatidylcholine phosphatidylethanolamine bilayers [abstract]. Biophys J. 72:1997;A403.
    • (1997) Biophys J , vol.72 , pp. 403
    • Cheng, K.H.1    Ruonale, M.2    Virtanen3    Somerharju, P.4
  • 71
    • 0343624351 scopus 로고    scopus 로고
    • Cholesterol regular distribution and its effect on solute partitioning in lipid membranes [abstract]
    • Wang MM, Chong PL-G. Cholesterol regular distribution and its effect on solute partitioning in lipid membranes [abstract]. Biophys J. 72:1997;A71.
    • (1997) Biophys J , vol.72 , pp. 71
    • Wang, M.M.1    Chong, P.-G.2
  • 74
    • 0030560392 scopus 로고    scopus 로고
    • Fluctuation-induced interactions between rods on membranes and interfaces
    • Golestanian R, Goulian M, Kardar M. Fluctuation-induced interactions between rods on membranes and interfaces. Europhys Lett. 33:1996;241-245.
    • (1996) Europhys Lett , vol.33 , pp. 241-245
    • Golestanian, R.1    Goulian, M.2    Kardar, M.3
  • 75
    • 0029669955 scopus 로고    scopus 로고
    • Free-energy determinants of an α-helix insertion into lipid bilayers
    • Ben-Tal N, Ben-Shaul A, Nicholls A, Honig B. Free-energy determinants of an α-helix insertion into lipid bilayers. Biophys J. 70:1996;1803-1812.
    • (1996) Biophys J , vol.70 , pp. 1803-1812
    • Ben-Tal, N.1    Ben-Shaul, A.2    Nicholls, A.3    Honig, B.4
  • 76
    • 0029938187 scopus 로고    scopus 로고
    • Statistical thermodynamic analysis of peptide and protein insertion into lipid membranes
    • Ben-Shaul A, Ben-Tal N, Honig B. Statistical thermodynamic analysis of peptide and protein insertion into lipid membranes. Biophys J. 71:1996;130-137.
    • (1996) Biophys J , vol.71 , pp. 130-137
    • Ben-Shaul, A.1    Ben-Tal, N.2    Honig, B.3
  • 78
    • 0029768644 scopus 로고    scopus 로고
    • Helix - helix interactions in lipid bilayers
    • Ben-Tal N, Honig B. Helix - helix interactions in lipid bilayers. Biophys J. 71:1996;3046-3050.
    • (1996) Biophys J , vol.71 , pp. 3046-3050
    • Ben-Tal, N.1    Honig, B.2
  • 79
    • 0000908857 scopus 로고    scopus 로고
    • Fluctuation-induced interactions between rods on a membrane
    • Golestanian R, Goulian M, Kardar M. Fluctuation-induced interactions between rods on a membrane. Phys Rev E. 54:1996;6725-6734.
    • (1996) Phys Rev e , vol.54 , pp. 6725-6734
    • Golestanian, R.1    Goulian, M.2    Kardar, M.3
  • 81
    • 0030978356 scopus 로고    scopus 로고
    • Fluorescence quenching and ESR study of percolation in a two-phase lipid bilayer containing bacteriorhodopsin
    • 18PC has a marked influence on the structure of the lipid domains formed in the gel/fluid coexistence region.
    • 18PC has a marked influence on the structure of the lipid domains formed in the gel/fluid coexistence region.
    • (1997) Biophys J , vol.72 , pp. 2660-2668
    • Piknová, B.1    Marsh, D.2    Thompson, T.E.3
  • 82
    • 0030933012 scopus 로고    scopus 로고
    • Influence of the intrinsic membrane protein bacteriorhodopsin on the gel phase domain topology in two-component phase-separated bilayers
    • Schram V, Thompson TE. Influence of the intrinsic membrane protein bacteriorhodopsin on the gel phase domain topology in two-component phase-separated bilayers. Biophys J. 72:1997;2217-2225.
    • (1997) Biophys J , vol.72 , pp. 2217-2225
    • Schram, V.1    Thompson, T.E.2
  • 83
    • 85030296892 scopus 로고    scopus 로고
    • Molecular sorting of lipids by bacteriorhodopsin in DLPC/DSPC lipid bilayers
    • of special interest bilayer mixtures provides evidence for enrichment at the protein/lipid interface of the lipid species that, under the thermodynamic conditions given, provides the best hydrophobic match to the the hydrophobic face of bacteriorhodopsin
    • 18PC lipid-bilayer mixtures provides evidence for enrichment at the protein/lipid interface of the lipid species that, under the thermodynamic conditions given, provides the best hydrophobic match to the the hydrophobic face of bacteriorhodopsin.
    • (1997) Biophys J
    • Dumas, F.1    Sperotto, M.M.2    Lebrun, C.3    Tocanne, J.-F.4    Mouritsen, O.G.5
  • 84
    • 0031049676 scopus 로고    scopus 로고
    • Evidence for phospholipid microdomain formation in liquid crystalline liposomes reconstituted with Escherichia coli lactose permease
    • of special interest. Evidence is provided for the accumulation of lipids that hydrophobically match the protein hydrophobic domain at the protein/lipid interface.
    • Lehtonen JYA, Kinnunen PKJ. Evidence for phospholipid microdomain formation in liquid crystalline liposomes reconstituted with Escherichia coli lactose permease. of special interest Biophys J. 72:1997;1247-1257 Evidence is provided for the accumulation of lipids that hydrophobically match the protein hydrophobic domain at the protein/lipid interface.
    • (1997) Biophys J , vol.72 , pp. 1247-1257
    • Lehtonen, J.Y.A.1    Kinnunen, P.K.J.2
  • 85
    • 0029024418 scopus 로고
    • Exclusion of SP-C, but not SP-B, by gel phase palmitoyl lipids
    • Horowitz AD. Exclusion of SP-C, but not SP-B, by gel phase palmitoyl lipids. Chem Phys Lipids. 76:1995;27-39.
    • (1995) Chem Phys Lipids , vol.76 , pp. 27-39
    • Horowitz, A.D.1
  • 86
    • 0029893610 scopus 로고    scopus 로고
    • 2 activity and dynamic lipid bilayer heterogeneity
    • 18PC unilamellar vesicles is controlled by the small-scale structure of the lipid bilayer.
    • 18PC unilamellar vesicles is controlled by the small-scale structure of the lipid bilayer.
    • (1996) Biochemistry , vol.35 , pp. 9003-9006
    • Hønger, T.1    Jørgensen, K.2    Biltonen, R.L.3    Mouritsen, O.G.4
  • 90
    • 0029859762 scopus 로고    scopus 로고
    • Origin of the lag period in the phospholipase C cleavage of phospholipids in membranes. Concomitant vesicle aggregation and enzyme activation
    • Basanez G, Nieva J-L, Goñi M, Alonso A. Origin of the lag period in the phospholipase C cleavage of phospholipids in membranes. Concomitant vesicle aggregation and enzyme activation. Biochemistry. 35:1996;15183-15187.
    • (1996) Biochemistry , vol.35 , pp. 15183-15187
    • Basanez, G.1    Nieva, J.-L.2    Goñi, M.3    Alonso, A.4
  • 91
    • 0029792683 scopus 로고    scopus 로고
    • Lipid lateral heterogeneity in phosphatidylcholine/phosphatidylserine/diacylglycerol vesicles and its influence on protein kinase C activation
    • of special interest. The authors argue that the reason why small amounts of diacylglycerol are sufficient to activate protein kinase C is that it accumulates in domains in the membrane and that the kinase activity is controlled by the interfaces between domains that are rich in and poor in diacylglycerol.
    • Dibble ARG, Hinderleiter AK, Sando JJ, Biltonen RL. Lipid lateral heterogeneity in phosphatidylcholine/phosphatidylserine/diacylglycerol vesicles and its influence on protein kinase C activation. of special interest Biophys J. 71:1996;1877-1890 The authors argue that the reason why small amounts of diacylglycerol are sufficient to activate protein kinase C is that it accumulates in domains in the membrane and that the kinase activity is controlled by the interfaces between domains that are rich in and poor in diacylglycerol.
    • (1996) Biophys J , vol.71 , pp. 1877-1890
    • Dibble, A.R.G.1    Hinderleiter, A.K.2    Sando, J.J.3    Biltonen, R.L.4
  • 92
    • 0030920192 scopus 로고    scopus 로고
    • Activation of protein kinase C by coexisting diacylglycerol/enriched and diacylglycerol-poor lipid domains
    • Hinderleiter AK, Dibble ARG, Biltonen RL, Sando JJ. Activation of protein kinase C by coexisting diacylglycerol/enriched and diacylglycerol-poor lipid domains. Biochemistry. 36:1997;6141-6148.
    • (1997) Biochemistry , vol.36 , pp. 6141-6148
    • Hinderleiter, A.K.1    Dibble, A.R.G.2    Biltonen, R.L.3    Sando, J.J.4
  • 93
    • 0029968851 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptor channels are influenced by the physical state of their membrane environment
    • Zanell LP, Aztiria E, Antollini S, Barrantes FJ. Nicotinic acetylcholine receptor channels are influenced by the physical state of their membrane environment. Biophys J. 70:1996;2155-2164.
    • (1996) Biophys J , vol.70 , pp. 2155-2164
    • Zanell, L.P.1    Aztiria, E.2    Antollini, S.3    Barrantes, F.J.4
  • 94
    • 0029743074 scopus 로고    scopus 로고
    • Correlation between bilayer lipid dynamics and activity of the diglucosyldiacylglycerol synthase from Acholeplasma laidlawii membranes
    • of special interest. The activator phosphatidylglycerol of the diglucosyldiacylglycerol synthase in Acholeplasma laidlawii is suggested to be enriched in domains induced by a hydrophobic mismatch with the membrane lipids.
    • Karlsson OP, Rytömaa M, Dahlqvist A, Kinnunen PKJ, Wieslander A. Correlation between bilayer lipid dynamics and activity of the diglucosyldiacylglycerol synthase from Acholeplasma laidlawii membranes. of special interest Biochemistry. 35:1996;10094-10102 The activator phosphatidylglycerol of the diglucosyldiacylglycerol synthase in Acholeplasma laidlawii is suggested to be enriched in domains induced by a hydrophobic mismatch with the membrane lipids.
    • (1996) Biochemistry , vol.35 , pp. 10094-10102
    • Karlsson, O.P.1    Rytömaa, M.2    Dahlqvist, A.3    Kinnunen, P.K.J.4    Wieslander, A.5
  • 95
    • 0029836721 scopus 로고    scopus 로고
    • The properties and biological roles of non-lamellar forming lipids
    • of special interest. R.M. Epand. A collection of papers on the importance of non-lamellar-forming lipids for both the physical and functional properties of membranes.
    • of special interest Epand RM. The properties and biological roles of non-lamellar forming lipids. Chem Phys Lipids. 81:1996;101-264 A collection of papers on the importance of non-lamellar-forming lipids for both the physical and functional properties of membranes.
    • (1996) Chem Phys Lipids , vol.81 , pp. 101-264
  • 96
    • 0029927812 scopus 로고    scopus 로고
    • Intrinsic curvature in normal and inverted lipid structures and in membranes
    • Marsh D. Intrinsic curvature in normal and inverted lipid structures and in membranes. Biophys J. 70:1996;2248-2255.
    • (1996) Biophys J , vol.70 , pp. 2248-2255
    • Marsh, D.1
  • 98
    • 0030586198 scopus 로고    scopus 로고
    • On the molecular-level mechanics of peripheral protein - membrane interactions induced by lipids forming inverted non-lamellar phases
    • Kinnunen PKJ. On the molecular-level mechanics of peripheral protein - membrane interactions induced by lipids forming inverted non-lamellar phases. Chem Phys Lipids. 81:1996;151-166.
    • (1996) Chem Phys Lipids , vol.81 , pp. 151-166
    • Kinnunen, P.K.J.1
  • 99
    • 0029921355 scopus 로고    scopus 로고
    • Chemical specificity and physical properties of the lipid bilayer in the regulation of protein kinase C by anionic phospholipids: Evidence for the lack of a specific binding site for phosphatidylserine
    • Mosior M, Golini ES, Epand RM. Chemical specificity and physical properties of the lipid bilayer in the regulation of protein kinase C by anionic phospholipids: evidence for the lack of a specific binding site for phosphatidylserine. Proc Natl Acad Sci USA. 93:1996;1907-1912.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1907-1912
    • Mosior, M.1    Golini, E.S.2    Epand, R.M.3
  • 100
    • 0028124422 scopus 로고
    • Modulation of rhodopsin function by properties of the membrane bilayer
    • Brown MF. 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
  • 101
    • 0029053249 scopus 로고
    • Lipid extracts from membranes of Acholeplasma laidlawii A grown with different fatty acids have a nearly constant spontaneous curvature
    • Österberg F, Rilfors L, Wieslander Å, Linblom G, Gruner SM. Lipid extracts from membranes of Acholeplasma laidlawii A grown with different fatty acids have a nearly constant spontaneous curvature. Biochem Biophys Acta. 1257:1995;18-24.
    • (1995) Biochem Biophys Acta , vol.1257 , pp. 18-24
    • Österberg, F.1    Rilfors, L.2    Wieslander, Å.3    Linblom, G.4    Gruner, S.M.5
  • 102
    • 0028053841 scopus 로고
    • Lysophospholipids modulate channel function by altering the mechanical properties of lipid bilayers
    • Lundbæk JS, Andersen OS. Lysophospholipids modulate channel function by altering the mechanical properties of lipid bilayers. J Gen Physiol. 104:1994;645-673.
    • (1994) J Gen Physiol , vol.104 , pp. 645-673
    • Lundbæk, J.S.1    Andersen, O.S.2
  • 103
    • 0029879111 scopus 로고    scopus 로고
    • Membrane stiffness and channel function
    • of outstanding interest. An elegant demonstration in a simple model membrane system of the importance of non-lamellar-forming lipids for the activity of an ion channel.
    • Lundbæk JS, Birn P, Girshman J, Hansen AJ, Andersen OS. Membrane stiffness and channel function. of outstanding interest Biochemistry. 35:1996;3825-3830 An elegant demonstration in a simple model membrane system of the importance of non-lamellar-forming lipids for the activity of an ion channel.
    • (1996) Biochemistry , vol.35 , pp. 3825-3830
    • Lundbæk, J.S.1    Birn, P.2    Girshman, J.3    Hansen, A.J.4    Andersen, O.S.5
  • 104
    • 0342754110 scopus 로고
    • The persistence length in a random surface model
    • Ipsen JH, Jeppesen C. The persistence length in a random surface model. J Phys I. 5:1995;1563-1571.
    • (1995) J Phys I , vol.5 , pp. 1563-1571
    • Ipsen, J.H.1    Jeppesen, C.2
  • 105
    • 0029981514 scopus 로고    scopus 로고
    • Sorting of newly synthesized galactosphingolipids to the two surface domains of epithelial cells
    • Van der Bijl P, Lopes-Cardozo M, van Meer G. Sorting of newly synthesized galactosphingolipids to the two surface domains of epithelial cells. J Cell Biol. 132:1996;813-821.
    • (1996) J Cell Biol , vol.132 , pp. 813-821
    • Van Der Bijl, P.1    Lopes-Cardozo, M.2    Van Meer, G.3
  • 106
    • 0029021712 scopus 로고
    • Progress in high resolution atomic force microscopy in biology
    • Shao Z, Yang J. Progress in high resolution atomic force microscopy in biology. Q Rev Biophys. 28:1995;195-251.
    • (1995) Q Rev Biophys , vol.28 , pp. 195-251
    • Shao, Z.1    Yang, J.2
  • 107
    • 0028842124 scopus 로고
    • The structure and stability of phospholipid bilayers by atomic force microscopy
    • Hui SW, Viswanathan R, Zasadzinski JA, Israelachvili J. The structure and stability of phospholipid bilayers by atomic force microscopy. Biophys J. 68:1995;171-178.
    • (1995) Biophys J , vol.68 , pp. 171-178
    • Hui, S.W.1    Viswanathan, R.2    Zasadzinski, J.A.3    Israelachvili, J.4
  • 108
    • 0031012630 scopus 로고    scopus 로고
    • High-resolution scanning tunneling microscopy of fully hydrated ripple-phase bilayers
    • Woodward JT IV, Zasadzinski JA. High-resolution scanning tunneling microscopy of fully hydrated ripple-phase bilayers. Biophys J. 72:1997;964-976.
    • (1997) Biophys J , vol.72 , pp. 964-976
    • Woodward J.T. IV1    Zasadzinski, J.A.2
  • 109
    • 0029062769 scopus 로고
    • Sensitive force technique to probe molecular adhesion and structural linkages at biological interfaces
    • Evans E, Ritchie K, Merkel R. Sensitive force technique to probe molecular adhesion and structural linkages at biological interfaces. Biophys J. 68:1995;2580-2587.
    • (1995) Biophys J , vol.68 , pp. 2580-2587
    • Evans, E.1    Ritchie, K.2    Merkel, R.3
  • 110
    • 0031001349 scopus 로고    scopus 로고
    • Dynamic strength of molecular adhesion bonds
    • of outstanding interest. This paper demonstrates how soft-probe microscopy, recently invented by the authors, can be used to measure the strength of very weak bonds involved in molecular adhesion and shows that the strength of a bond depends crucially on the rate by which the bond is loaded.
    • Evans E, Richie K. Dynamic strength of molecular adhesion bonds. of outstanding interest Biophys J. 72:1997;1541-1555 This paper demonstrates how soft-probe microscopy, recently invented by the authors, can be used to measure the strength of very weak bonds involved in molecular adhesion and shows that the strength of a bond depends crucially on the rate by which the bond is loaded.
    • (1997) Biophys J , vol.72 , pp. 1541-1555
    • Evans, E.1    Richie, K.2


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