메뉴 건너뛰기




Volumn 77, Issue 6, 1999, Pages 3176-3188

Electrostatic properties of membranes containing acidic lipids and adsorbed basic peptides: Theory and experiment

Author keywords

[No Author keywords available]

Indexed keywords

LYSINE DERIVATIVE; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLSERINE;

EID: 0032763121     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77148-1     Document Type: Article
Times cited : (176)

References (69)
  • 1
    • 0029752766 scopus 로고    scopus 로고
    • Preparation of giant liposomes in physiological conditions and their characterization under an optical microscope
    • Akashi, K., H. Miyata, H. Itoh, and K. Kinosita, Jr. 1996. Preparation of giant liposomes in physiological conditions and their characterization under an optical microscope. Biophys. J. 71:3242-3250.
    • (1996) Biophys. J. , vol.71 , pp. 3242-3250
    • Akashi, K.1    Miyata, H.2    Itoh, H.3    Kinosita K., Jr.4
  • 2
    • 0029162389 scopus 로고
    • A role for MARCKS, the α isozyme of protein kinase C and myosin i in zymosan phagocytosis by macrophages
    • Allen, L. A., and A. Aderem. 1995. A role for MARCKS, the α isozyme of protein kinase C and myosin I in zymosan phagocytosis by macrophages. J. Exp. Med. 182:829-840.
    • (1995) J. Exp. Med. , vol.182 , pp. 829-840
    • Allen, L.A.1    Aderem, A.2
  • 4
    • 0002056886 scopus 로고
    • Preparation and use of liposomes: Models of biological membranes
    • Bangham, A. D., M. W. Hill, and N. G. A. Miller. 1974. Preparation and use of liposomes: models of biological membranes. Methods Membr. Biol. 1:1-68.
    • (1974) Methods Membr. Biol. , vol.1 , pp. 1-68
    • Bangham, A.D.1    Hill, M.W.2    Miller, N.G.A.3
  • 5
    • 0004414739 scopus 로고
    • Theory of discreteness of charge effects in the electrolyte compact double layer
    • Barlow, C. A., and J. R. MacDonald. 1967. Theory of discreteness of charge effects in the electrolyte compact double layer. Adv. Electrochem. Electrochem. Eng. 6:1-194.
    • (1967) Adv. Electrochem. Electrochem. Eng. , vol.6 , pp. 1-194
    • Barlow, C.A.1    Macdonald, J.R.2
  • 6
    • 0030754783 scopus 로고    scopus 로고
    • Electrostatic binding of proteins to membranes: Theoretical prediction and experimental results with charybdotoxin and phospholipid vesicles
    • Ben-Tal, N., B. Honig, C. Miller, and S. McLaughlin. 1997. Electrostatic binding of proteins to membranes: theoretical prediction and experimental results with charybdotoxin and phospholipid vesicles. Biophys. J. 73:1717-1727.
    • (1997) Biophys. J. , vol.73 , pp. 1717-1727
    • Ben-Tal, N.1    Honig, B.2    Miller, C.3    McLaughlin, S.4
  • 7
    • 0029757155 scopus 로고    scopus 로고
    • Binding of small basic peptides to membranes containing acidic lipids: Theoretical models and experimental results
    • Ben-Tal, N., B. Honig, R. M. Peitzsch, G. Denisov, and S. McLaughlin. 1996. Binding of small basic peptides to membranes containing acidic lipids: theoretical models and experimental results. Biophys. J. 71: 561-575.
    • (1996) Biophys. J. , vol.71 , pp. 561-575
    • Ben-Tal, N.1    Honig, B.2    Peitzsch, R.M.3    Denisov, G.4    McLaughlin, S.5
  • 8
    • 0031019429 scopus 로고    scopus 로고
    • Understanding covalent modifications of proteins by lipids: Where cell biology and biophysics mingle
    • Bhatnagar, R. S., and J. I. Gordon. 1997. Understanding covalent modifications of proteins by lipids: where cell biology and biophysics mingle. Trends Cell Biol. 7:14-21.
    • (1997) Trends Cell Biol. , vol.7 , pp. 14-21
    • Bhatnagar, R.S.1    Gordon, J.I.2
  • 12
    • 0029970884 scopus 로고    scopus 로고
    • Adsorption of globular proteins on locally planar surfaces: Models for the effect of excluded area and aggregation of adsorbed protein on adsorption equilibria
    • Chatelier, R. C., and A. P. Minton. 1996. Adsorption of globular proteins on locally planar surfaces: models for the effect of excluded area and aggregation of adsorbed protein on adsorption equilibria. Biophys. J. 71:2367-2374.
    • (1996) Biophys. J. , vol.71 , pp. 2367-2374
    • Chatelier, R.C.1    Minton, A.P.2
  • 13
    • 0032522719 scopus 로고    scopus 로고
    • Membrane-targeting sequences on AKAP79 bind phosphatidyl-4,5-bisphosphate
    • Dell'Acqua, M. L., M. C. Faux, J. Thorburn, A. Thorburn, and J. D. Scott. 1998. Membrane-targeting sequences on AKAP79 bind phosphatidyl-4,5-bisphosphate. EMBO J. 17:2246-2260.
    • (1998) EMBO J. , vol.17 , pp. 2246-2260
    • Dell'acqua, M.L.1    Faux, M.C.2    Thorburn, J.3    Thorburn, A.4    Scott, J.D.5
  • 14
    • 0031927361 scopus 로고    scopus 로고
    • Binding of basic peptides to membranes produces lateral domains enriched in the acidic lipids phosphatidylserine and phosphatidylinositol 4,5-bisphosphate: An electrostatic model and experimental results
    • Denisov, G., S. Wanaski, P. Luan, M. Glaser, and S. McLaughlin. 1997. Binding of basic peptides to membranes produces lateral domains enriched in the acidic lipids phosphatidylserine and phosphatidylinositol 4,5-bisphosphate: an electrostatic model and experimental results. Biophys. J. 74:731-744.
    • (1997) Biophys. J. , vol.74 , pp. 731-744
    • Denisov, G.1    Wanaski, S.2    Luan, P.3    Glaser, M.4    McLaughlin, S.5
  • 15
    • 0032168891 scopus 로고    scopus 로고
    • The chirality of phosphatidylserine and the activation of protein kinase C
    • Epand, R. M., C. Stevenson, R. Bruins, V. Schram, and M. Glaser. 1998. The chirality of phosphatidylserine and the activation of protein kinase C. Biochemistry. 37:12068-12073.
    • (1998) Biochemistry , vol.37 , pp. 12068-12073
    • Epand, R.M.1    Stevenson, C.2    Bruins, R.3    Schram, V.4    Glaser, M.5
  • 16
    • 0031614235 scopus 로고    scopus 로고
    • Recent advances and remaining problems in HIV assembly
    • Garnier, L., B. Bowzard, and J. W. Wills. 1998. Recent advances and remaining problems in HIV assembly. AIDS. 12:S5-S16.
    • (1998) AIDS , vol.12
    • Garnier, L.1    Bowzard, B.2    Wills, J.W.3
  • 17
    • 0029127725 scopus 로고
    • Binding of prenylated and polybasic peptides to membranes: Affinities and intervesicle exchange
    • Ghomashchi, F., X. Zhang, L. Liu, and M. H. Gelb. 1995. Binding of prenylated and polybasic peptides to membranes: affinities and intervesicle exchange. Biochemistry. 34:11910-11918.
    • (1995) Biochemistry , vol.34 , pp. 11910-11918
    • Ghomashchi, F.1    Zhang, X.2    Liu, L.3    Gelb, M.H.4
  • 19
    • 0001601692 scopus 로고
    • Discreteness-of-charge-effects in the inner region of the electrical double layer
    • Grahame, D. C. 1958. Discreteness-of-charge-effects in the inner region of the electrical double layer. Z. Elektrochem. 62:264-274.
    • (1958) Z. Elektrochem. , vol.62 , pp. 264-274
    • Grahame, D.C.1
  • 20
    • 0023051521 scopus 로고
    • A test of the discreteness-of-charge effects in phospholipid vesicles
    • Hartsel, S. C., and D. S. Cafiso. 1986. A test of the discreteness-of-charge effects in phospholipid vesicles. Biochemistry. 25:8214-8219.
    • (1986) Biochemistry. , vol.25 , pp. 8214-8219
    • Hartsel, S.C.1    Cafiso, D.S.2
  • 21
    • 0033031748 scopus 로고    scopus 로고
    • Binding of peripheral proteins to mixed lipid membranes: Effect of lipid demixing upon binding
    • Heimburg, T., B. Angerstein, and D. Marsh. 1999. Binding of peripheral proteins to mixed lipid membranes: effect of lipid demixing upon binding. Biophys. J. 76:2575-2586.
    • (1999) Biophys. J. , vol.76 , pp. 2575-2586
    • Heimburg, T.1    Angerstein, B.2    Marsh, D.3
  • 22
    • 0028801883 scopus 로고
    • Protein surface-distribution and protein-protein interactions in the binding of peripheral proteins to charged lipid membranes
    • Heimburg, T., and D. Marsh. 1995. Protein surface-distribution and protein-protein interactions in the binding of peripheral proteins to charged lipid membranes. Biophys. J. 68:536-546.
    • (1995) Biophys. J. , vol.68 , pp. 536-546
    • Heimburg, T.1    Marsh, D.2
  • 24
    • 0000525721 scopus 로고
    • Multigrid solution of the Poisson-Boltzmann equation
    • Holst, M., and F. Saied. 1993. Multigrid solution of the Poisson-Boltzmann equation. J. Comp. Chem. 14:105-113.
    • (1993) J. Comp. Chem. , vol.14 , pp. 105-113
    • Holst, M.1    Saied, F.2
  • 25
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • Honig, B. H., and A. Nicholls. 1995. Classical electrostatics in biology and chemistry. Science. 268:1144-1149.
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.H.1    Nicholls, A.2
  • 26
    • 0021909644 scopus 로고
    • Production of large unilamellar vesicles by a rapid extrusion procedure. Characterization of size distribution, trapped volume and ability to maintain a membrane potential
    • Hope, M. J., M. B. Bally, G. Webb, and P. R. Cullis. 1985. Production of large unilamellar vesicles by a rapid extrusion procedure. Characterization of size distribution, trapped volume and ability to maintain a membrane potential. Biochim. Biophys. Acta. 812:55-65.
    • (1985) Biochim. Biophys. Acta. , vol.812 , pp. 55-65
    • Hope, M.J.1    Bally, M.B.2    Webb, G.3    Cullis, P.R.4
  • 28
    • 0025138727 scopus 로고
    • The src protein contains multiple domains for specific attachment to membranes
    • Kaplan, J. M., H. E. Varmus, and J. M. Bishop. 1990. The src protein contains multiple domains for specific attachment to membranes. Mol. Cell. Biol. 10:1000-1009.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 1000-1009
    • Kaplan, J.M.1    Varmus, H.E.2    Bishop, J.M.3
  • 30
    • 0028361026 scopus 로고
    • Phosphorylation reverses the membrane association of peptides that correspond to the basic domains of MARCKS and neuromodulin
    • Kim, J., P. J. Blackshear, J. D. Johnson, and S. McLaughlin. 1994. Phosphorylation reverses the membrane association of peptides that correspond to the basic domains of MARCKS and neuromodulin. Biophys. J. 67:227-237.
    • (1994) Biophys. J. , vol.67 , pp. 227-237
    • Kim, J.1    Blackshear, P.J.2    Johnson, J.D.3    McLaughlin, S.4
  • 31
    • 0025914405 scopus 로고
    • Binding of peptides with basic residues to membranes containing acidic phospholipids
    • Kim, J., M. Mosior, L. A. Chung, H. Wu, and S. McLaughlin. 1991. Binding of peptides with basic residues to membranes containing acidic phospholipids. Biophys. J. 60:135-148.
    • (1991) Biophys. J. , vol.60 , pp. 135-148
    • Kim, J.1    Mosior, M.2    Chung, L.A.3    Wu, H.4    McLaughlin, S.5
  • 32
    • 0030731891 scopus 로고    scopus 로고
    • Spin-label electron spin resonance studies on the interactions of lysine peptides with phospholipid membranes
    • Kleinschmidt, J. H., and D. Marsh. 1997. Spin-label electron spin resonance studies on the interactions of lysine peptides with phospholipid membranes. Biophys. J. 73:2546-2555.
    • (1997) Biophys. J. , vol.73 , pp. 2546-2555
    • Kleinschmidt, J.H.1    Marsh, D.2
  • 33
    • 0030667028 scopus 로고    scopus 로고
    • The N terminus of the Drosophila Numb protein directs membrane association and actin-dependent asymmetric localization
    • Knoblich, J. A., L. Y. Jan, and Y. N. Jan. 1997. The N terminus of the Drosophila Numb protein directs membrane association and actin-dependent asymmetric localization. Proc. Natl. Acad. Sci. USA. 94: 13005-13010.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13005-13010
    • Knoblich, J.A.1    Jan, L.Y.2    Jan, Y.N.3
  • 34
    • 0019412881 scopus 로고
    • Thermoelasticity of large lecithin bilayer vesicles
    • Kwok, R., and E. Evans. 1981. Thermoelasticity of large lecithin bilayer vesicles. Biophys. J. 35:637-652.
    • (1981) Biophys. J. , vol.35 , pp. 637-652
    • Kwok, R.1    Evans, E.2
  • 35
    • 0032546549 scopus 로고    scopus 로고
    • Lipid-binding characteristics of the polybasic carboxy-terminal sequence of K-ras4B
    • Leventis, R., and J. R. Silvius. 1998. Lipid-binding characteristics of the polybasic carboxy-terminal sequence of K-ras4B. Biochemistry. 37: 7640-7648.
    • (1998) Biochemistry , vol.37 , pp. 7640-7648
    • Leventis, R.1    Silvius, J.R.2
  • 36
    • 33645480232 scopus 로고
    • The discrete ion-effect in ionic double-layer theory
    • Levine, S., J. Mingins, and G. M. Bell. 1967. The discrete ion-effect in ionic double-layer theory. J. Electroanal. Chem. 13:280-329.
    • (1967) J. Electroanal. Chem. , vol.13 , pp. 280-329
    • Levine, S.1    Mingins, J.2    Bell, G.M.3
  • 37
    • 0030936016 scopus 로고    scopus 로고
    • Organized endothelial cell surface signal transduction in caveołae distinct from glycosylphosphatidylinositol-anchored protein microdomains
    • Liu, J., P. Oh, T. Horner, R. A. Rogers, and J. E. Schnitzer. 1997. Organized endothelial cell surface signal transduction in caveołae distinct from glycosylphosphatidylinositol-anchored protein microdomains. J. Biol. Chem. 272:7211-7222.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7211-7222
    • Liu, J.1    Oh, P.2    Horner, T.3    Rogers, R.A.4    Schnitzer, J.E.5
  • 38
    • 0032576969 scopus 로고    scopus 로고
    • Compartmentalization of phosphatidlyinositol 4,5-bisphosphate in low-density membrane domains in the absence of caveolin
    • Liu, Y., L. Casey, and L. J. Pike. 1998. Compartmentalization of phosphatidlyinositol 4,5-bisphosphate in low-density membrane domains in the absence of caveolin. Biochem. Biophys. Res. Commun. 245: 684-690.
    • (1998) Biochem. Biophys. Res. Commun. , vol.245 , pp. 684-690
    • Liu, Y.1    Casey, L.2    Pike, L.J.3
  • 39
    • 0043043663 scopus 로고    scopus 로고
    • Conformation and self-diffusion of single DNA molecules confined to two dimensions
    • Maier, B., and J. O. Rädler. 1999. Conformation and self-diffusion of single DNA molecules confined to two dimensions. Phys. Rev. Lett. 82:1911-1914.
    • (1999) Phys. Rev. Lett. , vol.82 , pp. 1911-1914
    • Maier, B.1    Rädler, J.O.2
  • 40
    • 0032407241 scopus 로고    scopus 로고
    • Phosphoinositide lipids as signaling molecules: Common themes for signal transduction, cytoskeletal regulation, and membrane trafficking
    • Martin, T. F. J. 1998. Phosphoinositide lipids as signaling molecules: common themes for signal transduction, cytoskeletal regulation, and membrane trafficking. Annu. Rev. Cell Dev. Biol. 14:231-264.
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 231-264
    • Martin, T.F.J.1
  • 41
    • 0344955341 scopus 로고
    • Structures and transitions in lipid monolayers at the air-water interface
    • McConnell, H. M. 1991. Structures and transitions in lipid monolayers at the air-water interface. Annu. Rev. Phys. Chem. 42:171-195.
    • (1991) Annu. Rev. Phys. Chem. , vol.42 , pp. 171-195
    • McConnell, H.M.1
  • 42
    • 0025733796 scopus 로고
    • A continuous fluorescence assay for protein kinase C
    • McIlroy, B. K., J. D. Walters, and J. D. Johnson. 1991. A continuous fluorescence assay for protein kinase C. Anal. Biochem. 195:148-152.
    • (1991) Anal. Biochem. , vol.195 , pp. 148-152
    • McIlroy, B.K.1    Walters, J.D.2    Johnson, J.D.3
  • 44
    • 0029058605 scopus 로고
    • The myristoyl-electrostatic switch: A modulator of reversible protein-membrane interactions
    • McLaughlin, S., and A. Aderem. 1995. The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions. Trends Biochem. Sci. 20:272-276.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 272-276
    • McLaughlin, S.1    Aderem, A.2
  • 45
    • 0019475925 scopus 로고
    • Adsorption of divalent cations to bilayer membranes containing phosphatidylserine
    • McLaughlin, S., N. Mulrine, T. Gresalfi, G. Vaio, and A. McLaughlin. 1981. Adsorption of divalent cations to bilayer membranes containing phosphatidylserine. J. Gen. Physiol. 77:445-473.
    • (1981) J. Gen. Physiol. , vol.77 , pp. 445-473
    • McLaughlin, S.1    Mulrine, N.2    Gresalfi, T.3    Vaio, G.4    McLaughlin, A.5
  • 46
    • 0025579948 scopus 로고
    • Phospholipid and phospholipid-protein monolayers and the air/water interface
    • Möhwald, H. 1990. Phospholipid and phospholipid-protein monolayers and the air/water interface. Annu. Rev. Phys. Chem. 41:441-476.
    • (1990) Annu. Rev. Phys. Chem. , vol.41 , pp. 441-476
    • Möhwald, H.1
  • 47
    • 0025743856 scopus 로고
    • Peptides that mimic the pseudosubstrate region of protein kinase C bind to acidic lipids in membranes
    • Mosior, M., and S. McLaughlin. 1991. Peptides that mimic the pseudosubstrate region of protein kinase C bind to acidic lipids in membranes. Biophys. J. 60:149-159.
    • (1991) Biophys. J. , vol.60 , pp. 149-159
    • Mosior, M.1    McLaughlin, S.2
  • 48
    • 0026572082 scopus 로고
    • Binding of basic peptides to acidic lipids in membranes: Effects of inserting alanine(s) between the basic residues
    • Mosior, M., and S. McLaughlin. 1992. Binding of basic peptides to acidic lipids in membranes: effects of inserting alanine(s) between the basic residues. Biochemistry. 31:1767-1773.
    • (1992) Biochemistry , vol.31 , pp. 1767-1773
    • Mosior, M.1    McLaughlin, S.2
  • 49
    • 0030820281 scopus 로고    scopus 로고
    • Small-scale lipid-membrane structure: Simulation versus experiment
    • Mouritsen, O. G., and K. Jørgensen. 1997. Small-scale lipid-membrane structure: simulation versus experiment. Curr. Opin. Struct. Biol. 7:518-527.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 518-527
    • Mouritsen, O.G.1    Jørgensen, K.2
  • 50
    • 0031571632 scopus 로고    scopus 로고
    • Electrostatic interaction of myristoylated proteins with membranes: Simple physics, complicated biology
    • Murray, D., N. Ben-Tal, B. Honig, and S. McLaughlin. 1997. Electrostatic interaction of myristoylated proteins with membranes: simple physics, complicated biology. Structure. 5:985-989.
    • (1997) Structure , vol.5 , pp. 985-989
    • Murray, D.1    Ben-Tal, N.2    Honig, B.3    McLaughlin, S.4
  • 52
    • 0027237719 scopus 로고
    • Measurement of interbilayer adhesion energies
    • Needham, D. 1993. Measurement of interbilayer adhesion energies. Methods Enzymol. 220:111-129.
    • (1993) Methods Enzymol. , vol.220 , pp. 111-129
    • Needham, D.1
  • 53
    • 0032555778 scopus 로고    scopus 로고
    • Protein kinase C: A paradigm for regulation of protein function by two membrane-targeting modules
    • Newton, A. C., and J. E. Johnson. 1998. Protein kinase C: a paradigm for regulation of protein function by two membrane-targeting modules. Biochim. Biophys. Acta. 1376:155-172.
    • (1998) Biochim. Biophys. Acta. , vol.1376 , pp. 155-172
    • Newton, A.C.1    Johnson, J.E.2
  • 54
    • 0028954965 scopus 로고
    • Calculations of the electrostatic potential adjacent to model phospholipid bilayers
    • Peitzsch, R. M., M. Eisenberg, K. A. Sharp, and S. McLaughlin. 1995. Calculations of the electrostatic potential adjacent to model phospholipid bilayers. Biophys. J. 68:729-738.
    • (1995) Biophys. J. , vol.68 , pp. 729-738
    • Peitzsch, R.M.1    Eisenberg, M.2    Sharp, K.A.3    McLaughlin, S.4
  • 56
    • 0021112116 scopus 로고
    • Synthesis, spectral properties, and use of 6-acryloyl-2-dimethyiaminonaphthalene (acrylodan)
    • Prendergast, F. G., M. Meyer, G. L. Carlson, S. Iida, and J. D. Potter. 1983. Synthesis, spectral properties, and use of 6-acryloyl-2-dimethyIaminonaphthalene (acrylodan). J. Biol. Chem. 258:7541-7544.
    • (1983) J. Biol. Chem. , vol.258 , pp. 7541-7544
    • Prendergast, F.G.1    Meyer, M.2    Carlson, G.L.3    Iida, S.4    Potter, J.D.5
  • 57
    • 0030250003 scopus 로고    scopus 로고
    • Regulation of cellular signalling by fatty acid acylation and prenylation of signal transduction proteins
    • Resh, M. D. 1996. Regulation of cellular signalling by fatty acid acylation and prenylation of signal transduction proteins. Cell. Signal. 8:403-412.
    • (1996) Cell. Signal , vol.8 , pp. 403-412
    • Resh, M.D.1
  • 59
    • 0032544230 scopus 로고    scopus 로고
    • Structure of type IIβ phosphatidylinositol phosphate kinase: A protein kinase fold flattened for interfacial phosphorylation
    • Roa, V. D., S. Misra, I. V. Boronenkov, R. A. Anderson, and J. H. Hurley. 1998. Structure of type IIβ phosphatidylinositol phosphate kinase: a protein kinase fold flattened for interfacial phosphorylation. Cell. 94: 829-839.
    • (1998) Cell , vol.94 , pp. 829-839
    • Roa, V.D.1    Misra, S.2    Boronenkov, I.V.3    Anderson, R.A.4    Hurley, J.H.5
  • 60
    • 0025096430 scopus 로고
    • Activation of protein kinase C results in the displacement of its myristoylated, alanine-rich substrate from punctate structures in macrophage filopodia
    • Rosen, A., K. F. Keenan, M. Thelen, A. C. Nairn, and A. Aderem. 1990. Activation of protein kinase C results in the displacement of its myristoylated, alanine-rich substrate from punctate structures in macrophage filopodia. J. Exp. Med. 172:1211-1215.
    • (1990) J. Exp. Med. , vol.172 , pp. 1211-1215
    • Rosen, A.1    Keenan, K.F.2    Thelen, M.3    Nairn, A.C.4    Aderem, A.5
  • 61
    • 0029780527 scopus 로고    scopus 로고
    • Molecular determinants of the myristoyl-electrostatic switch of MARCKS
    • Seykora, J. T., M. M. Myat, L. A. Allen, J. V. Ravetch, and A. Aderem. 1996. Molecular determinants of the myristoyl-electrostatic switch of MARCKS. J. Biol. Chem. 271:18797-18802.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18797-18802
    • Seykora, J.T.1    Myat, M.M.2    Allen, L.A.3    Ravetch, J.V.4    Aderem, A.5
  • 62
    • 0028053759 scopus 로고
    • The amino terminal basic residues of Src mediate membrane binding through electrostatic interaction with acidic phospholipids
    • Sigal, C. T., W. Zhou, C. A. Buser, S. McLaughlin, and M. D. Resh. 1994. The amino terminal basic residues of Src mediate membrane binding through electrostatic interaction with acidic phospholipids. Proc. Natl. Acad. Sci. USA. 91:12253-12257.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12253-12257
    • Sigal, C.T.1    Zhou, W.2    Buser, C.A.3    McLaughlin, S.4    Resh, M.D.5
  • 63
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
    • Sutton, R. B., D. Fasshauer, R. Jahn, and A. T. Brunger. 1998. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution. Nature. 395:347-353.
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 64
    • 0029831440 scopus 로고    scopus 로고
    • Myristoylation-dependent and electrostatic interactions exert independent effects on the membrane association of the myristoylated alanine-rich C-kinase substrate
    • Swierczynski, S. L., and P. J. Blackshear. 1996. Myristoylation-dependent and electrostatic interactions exert independent effects on the membrane association of the myristoylated alanine-rich C-kinase substrate. J. Biol. Chem. 271:23424-23430.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23424-23430
    • Swierczynski, S.L.1    Blackshear, P.J.2
  • 65
    • 0024293197 scopus 로고
    • Adsorption of cations to phosphatidylinositol 4,5-bisphosphate
    • Toner, M., G. Vaio, A. McLaughlin, and S. McLaughlin. 1988. Adsorption of cations to phosphatidylinositol 4,5-bisphosphate. Biochemistry. 27: 7435-7443.
    • (1988) Biochemistry , vol.27 , pp. 7435-7443
    • Toner, M.1    Vaio, G.2    McLaughlin, A.3    McLaughlin, S.4
  • 66
    • 0023051529 scopus 로고
    • An experimental test of the discreteness-of-charge effect in positive and negative lipid bilayers
    • Winiski, A. P., A. C. McLaughlin, R. V. McDaniel, M. Eisenberg, and S. McLaughlin. 1986. An experimental test of the discreteness-of-charge effect in positive and negative lipid bilayers. Biochemistry. 25: 8206-8214.
    • (1986) Biochemistry , vol.25 , pp. 8206-8214
    • Winiski, A.P.1    McLaughlin, A.C.2    McDaniel, R.V.3    Eisenberg, M.4    McLaughlin, S.5
  • 67
    • 0028952293 scopus 로고
    • Membrane domains containing phosphatidylserine and substrate can be important for the activation of protein kinase C
    • Yang, L., and M. Glaser. 1995. Membrane domains containing phosphatidylserine and substrate can be important for the activation of protein kinase C. Biochemistry. 34:1500-1506.
    • (1995) Biochemistry , vol.34 , pp. 1500-1506
    • Yang, L.1    Glaser, M.2
  • 68
    • 0029904712 scopus 로고    scopus 로고
    • Formation of membrane domains during the activation of protein kinase C
    • Yang, L., and M. Glaser. 1996. Formation of membrane domains during the activation of protein kinase C. Biochemistry. 35:13966-13974.
    • (1996) Biochemistry , vol.35 , pp. 13966-13974
    • Yang, L.1    Glaser, M.2
  • 69
    • 0028218274 scopus 로고
    • Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipids
    • Zhou, W., L. J. Parent, J. W. Wills, and M. D. Resh. 1994. Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipids. J. Virol. 68:2556-2569.
    • (1994) J. Virol. , vol.68 , pp. 2556-2569
    • Zhou, W.1    Parent, L.J.2    Wills, J.W.3    Resh, M.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.