메뉴 건너뛰기




Volumn 10, Issue 10, 2004, Pages 612-621

Interaction between amyloid β-protein aggregates and membranes

Author keywords

Aggregates; Alzheimer's disease; Amyloid protein; Lipid raft; Protein membrane interaction

Indexed keywords

AMYLOID BETA PROTEIN; BUFFER; CHOLESTEROL; DYE; GANGLIOSIDE GM1; MONOSIALOGANGLIOSIDE; SPHINGOMYELIN;

EID: 6944242589     PISSN: 10752617     EISSN: None     Source Type: Journal    
DOI: 10.1002/psc.570     Document Type: Article
Times cited : (59)

References (58)
  • 1
    • 0028170818 scopus 로고
    • Cell biology of the amyloid β-protein precursor and the mechanism of Alzheimer's disease
    • Selkoe DJ. Cell biology of the amyloid β-protein precursor and the mechanism of Alzheimer's disease. Annu. Rev. Cell Biol. 1994; 10: 373-403.
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 373-403
    • Selkoe, D.J.1
  • 2
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper JD, Lansbury PT Jr. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu. Rev. Biochem. 1997; 66: 385-407.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury Jr., P.T.2
  • 3
    • 0344431341 scopus 로고    scopus 로고
    • Structural neurology: Are seeds at the root of neuronal degeneration?
    • Lansbury PT Jr. Structural neurology: are seeds at the root of neuronal degeneration? Neuron 1997; 19: 1151-1154.
    • (1997) Neuron , vol.19 , pp. 1151-1154
    • Lansbury Jr., P.T.1
  • 5
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid β-protein fibrillogenesis. Detection of a protofibrillar intermediate
    • Walsh DM, Lomakin A, Benedek GB, Condron MM, Teplow DB. Amyloid β-protein fibrillogenesis. Detection of a protofibrillar intermediate. J. Biol. Chem. 1997; 272: 22 364-22 372.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22364-22372
    • Walsh, D.M.1    Lomakin, A.2    Benedek, G.B.3    Condron, M.M.4    Teplow, D.B.5
  • 6
    • 0032855484 scopus 로고    scopus 로고
    • Kinetic analysis of amyloid fibril formation
    • Naiki H, Gejyo F. Kinetic analysis of amyloid fibril formation. Methods Enzymol. 1999; 309: 305-318.
    • (1999) Methods Enzymol. , vol.309 , pp. 305-318
    • Naiki, H.1    Gejyo, F.2
  • 8
    • 0027195933 scopus 로고
    • Seeding 'one-dimensional crystallization' of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett JT, Lansbury Jr PT. Seeding 'one-dimensional crystallization' of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 1993; 73: 1055-1058.
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 10
    • 0034700129 scopus 로고    scopus 로고
    • Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of β-sheets in Alzheimer's β -amyloid fibrils
    • Antzukin ON, Balbach JJ, Leapman RD, Rizzo NW, Reed J, Tycko R. Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of β-sheets in Alzheimer's β-amyloid fibrils. Proc. Natl Acad. Sci. USA 2000; 97: 13 045-13 050.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13045-13050
    • Antzukin, O.N.1    Balbach, J.J.2    Leapman, R.D.3    Rizzo, N.W.4    Reed, J.5    Tycko, R.6
  • 11
    • 0035997080 scopus 로고    scopus 로고
    • Supramolecular structure in full-length Alzheimer's β-amyloid fibrils: Evidence for a parallel β-sheet organization from solid-state nuclear magnetic resonance
    • Balbach JJ, Petkova AT, Oyler NA, Antzukin ON, Gordon DJ, Meredith SC, Tycko R. Supramolecular structure in full-length Alzheimer's β-amyloid fibrils: Evidence for a parallel β-sheet organization from solid-state nuclear magnetic resonance. Biophys. J. 2002; 83: 1205-1216.
    • (2002) Biophys. J. , vol.83 , pp. 1205-1216
    • Balbach, J.J.1    Petkova, A.T.2    Oyler, N.A.3    Antzukin, O.N.4    Gordon, D.J.5    Meredith, S.C.6    Tycko, R.7
  • 14
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • Hartley DM, Walsh DM, Ye CP, Diehl T, Vasquez S, Vassilev PM, Teplow DB, Selkoe DJ. Protofibrillar intermediates of amyloid β -protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J. Neurosci. 1999; 19: 8876-8884.
    • (1999) J. Neurosci. , vol.19 , pp. 8876-8884
    • Hartley, D.M.1    Walsh, D.M.2    Ye, C.P.3    Diehl, T.4    Vasquez, S.5    Vassilev, P.M.6    Teplow, D.B.7    Selkoe, D.J.8
  • 15
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligamers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh DM, Kyubin I, Fadeeva JV, Cullen WK, Anwyl R, Wolfe MS, Rowan MJ, Selkoe DJ. Naturally secreted oligamers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo. Nature 2002; 416: 535-539.
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Kyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 16
    • 0037200117 scopus 로고    scopus 로고
    • Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability
    • Dahlgren KN, Manelli AM, Stine JWB, Baker LK, Krafft GA, LaDu MJ. Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability. J. Biol. Chem. 2002; 277: 32 046-32 053.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32046-32053
    • Dahlgren, K.N.1    Manelli, A.M.2    Stine, J.W.B.3    Baker, L.K.4    Krafft, G.A.5    LaDu, M.J.6
  • 17
    • 0037975676 scopus 로고    scopus 로고
    • Spherical aggregates of β-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3β
    • Hoshi M, Sato M, Matsumoto S, Nogichi A, Yasutake K, Yoshida N, Sato K. Spherical aggregates of β-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3β. Proc. Natl Acad. Sci. USA 2003; 100: 6370-6375.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6370-6375
    • Hoshi, M.1    Sato, M.2    Matsumoto, S.3    Nogichi, A.4    Yasutake, K.5    Yoshida, N.6    Sato, K.7
  • 21
    • 0035800087 scopus 로고    scopus 로고
    • Structure-function relationships for inhibitors of β-amyloid toxicity containing the recognition sequence KLVFF
    • Lowe TL, Strzelec A, Kiessling LL, Murphy RM. Structure-function relationships for inhibitors of β-amyloid toxicity containing the recognition sequence KLVFF. Biochemistry 2001; 40 7882-7889.
    • (2001) Biochemistry , vol.40 , pp. 7882-7889
    • Lowe, T.L.1    Strzelec, A.2    Kiessling, L.L.3    Murphy, R.M.4
  • 22
    • 0028885854 scopus 로고
    • GM1 ganglioside-bound amyloid β-protein (Aβ): A possible form of preamyloid in Alzheimer's disease
    • Yanagisawa K, Odaka A, Suzuki N, Ihara Y. GM1 ganglioside-bound amyloid β-protein (Aβ): a possible form of preamyloid in Alzheimer's disease. Nat. Med. 1995; 1: 1062-1066.
    • (1995) Nat. Med. , vol.1 , pp. 1062-1066
    • Yanagisawa, K.1    Odaka, A.2    Suzuki, N.3    Ihara, Y.4
  • 23
    • 0031957080 scopus 로고    scopus 로고
    • GM1 ganglioside-bound amyloid β-protein in Alzheimer's disease brain
    • Yanagisawa K, Ihara Y. GM1 ganglioside-bound amyloid β-protein in Alzheimer's disease brain. Neurobiol. Aging 1998; 19: S65-S67.
    • (1998) Neurobiol. Aging , vol.19
    • Yanagisawa, K.1    Ihara, Y.2
  • 24
    • 0032480771 scopus 로고    scopus 로고
    • The presence of amyloid β-protein in the detergent-insoluble membrane compartment of neuroblastoma cells
    • Morishima-Kawashima M, Ihara Y. The presence of amyloid β-protein in the detergent-insoluble membrane compartment of neuroblastoma cells. Biochemistry 1998; 37: 15 247-15 235.
    • (1998) Biochemistry , vol.37 , pp. 15235-15247
    • Morishima-Kawashima, M.1    Ihara, Y.2
  • 25
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K, Ikonen E. Functional rafts in cell membranes. Nature 1997; 385: 569-572.
    • (1997) Nature , vol.385 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 26
    • 0030823756 scopus 로고    scopus 로고
    • Acceleration of amyloid fibril formation by specific binding of Aβ-(1-40) peptide to ganglioside-containing membrane vesicles
    • ChooSmith L-P, Garzon-Rodriguez W, Glabe CG, Surewicz WK. Acceleration of amyloid fibril formation by specific binding of Aβ-(1-40) peptide to ganglioside-containing membrane vesicles. J. Biol. Chem. 1997; 272: 22 987-22 990.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22987-22990
    • ChooSmith, L.-P.1    Garzon-Rodriguez, W.2    Glabe, C.G.3    Surewicz, W.K.4
  • 27
    • 0032548943 scopus 로고    scopus 로고
    • Structural transitions associated with the interaction of Alzheimer β-amyloid peptides with gangliosides
    • McLaurin J, Franklin T, Fraser PE, Chakrabartty A. Structural transitions associated with the interaction of Alzheimer β-amyloid peptides with gangliosides. J. Biol. Chem. 1998; 273: 4506-4515.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4506-4515
    • McLaurin, J.1    Franklin, T.2    Fraser, P.E.3    Chakrabartty, A.4
  • 28
    • 0037062582 scopus 로고    scopus 로고
    • Interactions of amyloid β-protein with various gangliosides in raft-like membranes: Importance of GM1 ganglioside-bound form as an endogenous seed for Alzheimer amyloid
    • Kakio A, Nishimoto S, Yanagisawa K, Kozutsumi Y, Matsuzaki K. Interactions of amyloid β-protein with various gangliosides in raft-like membranes: Importance of GM1 ganglioside-bound form as an endogenous seed for Alzheimer amyloid. Biochemistry 2002; 41: 7385-7390.
    • (2002) Biochemistry , vol.41 , pp. 7385-7390
    • Kakio, A.1    Nishimoto, S.2    Yanagisawa, K.3    Kozutsumi, Y.4    Matsuzaki, K.5
  • 29
    • 0034663858 scopus 로고    scopus 로고
    • Accelerated accumulation of amyloid β proteins on oxidatively damaged lipid membranes
    • Koppaka V, Axelsen PH. Accelerated accumulation of amyloid β proteins on oxidatively damaged lipid membranes. Biochemistry 2000; 39: 10 011-10 016.
    • (2000) Biochemistry , vol.39 , pp. 10011-10016
    • Koppaka, V.1    Axelsen, P.H.2
  • 30
    • 0033598697 scopus 로고    scopus 로고
    • Interactions between Aβ(1-42) and Aβ(1-40) in Alzheimer's β-amyloid fibril formation in vitro
    • Hasegawa K, Yamaguchi I, Omata S, Gejyo F, Naiki H. Interactions between Aβ(1-42) and Aβ(1-40) in Alzheimer's β-amyloid fibril formation in vitro. Biochemistry 1999; 38: 15 514-15 521.
    • (1999) Biochemistry , vol.38 , pp. 15514-15521
    • Hasegawa, K.1    Yamaguchi, I.2    Omata, S.3    Gejyo, F.4    Naiki, H.5
  • 31
    • 0035816709 scopus 로고    scopus 로고
    • Cholesterol-dependent formation of GM1 ganglioside-bound amyloid β-protein, an endogenous seed for Alzheimer amyloid
    • Kakio A, Nishimoto S, Yanagisawa K, Kozutsumi Y, Matsuzaki K. Cholesterol-dependent formation of GM1 ganglioside-bound amyloid β-protein, an endogenous seed for Alzheimer amyloid. J. Biol. Chem. 2001; 276: 24 985-24 990.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24985-24990
    • Kakio, A.1    Nishimoto, S.2    Yanagisawa, K.3    Kozutsumi, Y.4    Matsuzaki, K.5
  • 32
    • 70449246528 scopus 로고
    • Phosphorus assay in column chromatography
    • Bartlett GR. Phosphorus assay in column chromatography. J. Biol. Chem. 1959; 234: 466-468.
    • (1959) J. Biol. Chem. , vol.234 , pp. 466-468
    • Bartlett, G.R.1
  • 33
    • 0000757008 scopus 로고
    • The conformation of dynorphin A-(1-13) in aqueous solution as studied by Fourier transform infrared spectroscopy
    • Surewicz WK, Mantsch HH. The conformation of dynorphin A-(1-13) in aqueous solution as studied by Fourier transform infrared spectroscopy. J. Mol. Struct. 1989; 214: 143-147.
    • (1989) J. Mol. Struct. , vol.214 , pp. 143-147
    • Surewicz, W.K.1    Mantsch, H.H.2
  • 34
    • 0000113382 scopus 로고    scopus 로고
    • Replies to the editor
    • Kaneko I, Tutumi S. Replies to the editor. J. Neurochem. 1997; 68: 438-439.
    • (1997) J. Neurochem. , vol.68 , pp. 438-439
    • Kaneko, I.1    Tutumi, S.2
  • 35
    • 0032968077 scopus 로고    scopus 로고
    • Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes
    • Goormaghtigh E, Raussens V, Ruysschaert J-M. Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes. Biochim. Biophys. Acta 1999; 1422: 105-185.
    • (1999) Biochim. Biophys. Acta , vol.1422 , pp. 105-185
    • Goormaghtigh, E.1    Raussens, V.2    Ruysschaert, J.-M.3
  • 36
    • 0038176528 scopus 로고    scopus 로고
    • In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis
    • Stine JWB, Dahlgren KN, Krafft GA, LaDu MJ. In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis. J. Biol. Chem. 2003; 278: 11 612-11 622.
    • (2003) J. Biol. Chem. , vol.278 , pp. 11612-11622
    • Stine, J.W.B.1    Dahlgren, K.N.2    Krafft, G.A.3    LaDu, M.J.4
  • 39
    • 0037137225 scopus 로고    scopus 로고
    • Kinetic modeling and determination of reaction constants of Alzheimer's β-amyloid fibril extension and dissociation using surface plasmon resonance
    • Hasegawa K, Ono K, Yamada M, Naiki H. Kinetic modeling and determination of reaction constants of Alzheimer's β-amyloid fibril extension and dissociation using surface plasmon resonance. Biochemistry 2002; 41: 13 489-13 498.
    • (2002) Biochemistry , vol.41 , pp. 13489-13498
    • Hasegawa, K.1    Ono, K.2    Yamada, M.3    Naiki, H.4
  • 41
    • 0002104663 scopus 로고
    • The flattening of the absorption spectrum of suspensions, as compared to that of solutions
    • Duysens LNM. The flattening of the absorption spectrum of suspensions, as compared to that of solutions. Biochim. Biophys. Acta 1956; 19: 1-12.
    • (1956) Biochim. Biophys. Acta , vol.19 , pp. 1-12
    • Duysens, L.N.M.1
  • 42
    • 4243898367 scopus 로고
    • Perturbation treatment of the characteristic vibrations of polypeptide chains in various configurations
    • Miyazawa T. Perturbation treatment of the characteristic vibrations of polypeptide chains in various configurations. J. Chem. Phys. 1960; 32: 1647-1652.
    • (1960) J. Chem. Phys. , vol.32 , pp. 1647-1652
    • Miyazawa, T.1
  • 43
    • 0343532738 scopus 로고
    • The infrared spectra of polypeptides in various conformations: Amide I and II bands
    • Miyazawa T, Blout ER. The infrared spectra of polypeptides in various conformations: amide I and II bands. J. Am. Chem. Soc. 1961; 83: 712-719.
    • (1961) J. Am. Chem. Soc. , vol.83 , pp. 712-719
    • Miyazawa, T.1    Blout, E.R.2
  • 44
    • 0026101636 scopus 로고
    • Aggregation and secondary structure of synthetic amyloid βA4 peptides of Alzheimer's disease
    • Hilbich C, Kisters-Woike B, Reed J, Masters CL, Beyreuter K. Aggregation and secondary structure of synthetic amyloid βA4 peptides of Alzheimer's disease. J. Mol. Biol. 1991; 218: 149-163.
    • (1991) J. Mol. Biol. , vol.218 , pp. 149-163
    • Hilbich, C.1    Kisters-Woike, B.2    Reed, J.3    Masters, C.L.4    Beyreuter, K.5
  • 45
    • 0025648652 scopus 로고
    • 2O) solutions. II. Amide absorption bands of polypeptides and fibrous proteins in α-,β- and random coil conformations
    • 2O) solutions. II. Amide absorption bands of polypeptides and fibrous proteins in α-,β - and random coil conformations. Biopolymers 1990; 30: 1259-1271.
    • (1990) Biopolymers , vol.30 , pp. 1259-1271
    • Venyaminov, S.Y.1    Kalnin, N.N.2
  • 46
    • 0029839357 scopus 로고    scopus 로고
    • In situ characterization of β-amyloid in Alzheimer's diseased tissue by synchrotron Fourier transform infrared microspectroscopy
    • Choo L-P, Wetzel DL, Halliday WC, Jackson M, LeVine SM, Mantsch HH. In situ characterization of β-amyloid in Alzheimer's diseased tissue by synchrotron Fourier transform infrared microspectroscopy. Biophys. J. 1996; 71: 1672-1679.
    • (1996) Biophys. J. , vol.71 , pp. 1672-1679
    • Choo, L.-P.1    Wetzel, D.L.2    Halliday, W.C.3    Jackson, M.4    LeVine, S.M.5    Mantsch, H.H.6
  • 47
    • 0029117442 scopus 로고
    • Theory and application of fluorescence homotransfer to melittin oligomerization
    • Runnels LW, Scarlata SF. Theory and application of fluorescence homotransfer to melittin oligomerization. Biophys. J. 1995; 69: 1569-1583.
    • (1995) Biophys. J. , vol.69 , pp. 1569-1583
    • Runnels, L.W.1    Scarlata, S.F.2
  • 49
    • 0028982292 scopus 로고
    • Self-association of β-amyloid peptide (1-40) in solution and binding to lipid membranes
    • Terzi E, Hölzmann G, Seelig J. Self-association of β-amyloid peptide (1-40) in solution and binding to lipid membranes. J. Mol. Biol. 1995; 252: 633-642.
    • (1995) J. Mol. Biol. , vol.252 , pp. 633-642
    • Terzi, E.1    Hölzmann, G.2    Seelig, J.3
  • 50
    • 0033616779 scopus 로고    scopus 로고
    • Interactions of amyloid β-peptide (1-40) with ganglioside-containing membranes
    • Matsuzaki K, Horikiri C. Interactions of amyloid β-peptide (1-40) with ganglioside-containing membranes. Biochemistry 1999; 38: 4137-4142.
    • (1999) Biochemistry , vol.38 , pp. 4137-4142
    • Matsuzaki, K.1    Horikiri, C.2
  • 52
    • 0037155235 scopus 로고    scopus 로고
    • Cholesterol is an important factor affecting the membrane insertion of β-amyloid peptide (Aβ1-40), which may potentially inhibit the fibril formation
    • Ji S-R, Wu Y, Sui S-F. Cholesterol is an important factor affecting the membrane insertion of β-amyloid peptide (Aβ1-40 , which may potentially inhibit the fibril formation. J. Biol. Chem. 2002; 277: 6273-6279.
    • (2002) J. Biol. Chem. , vol.277 , pp. 6273-6279
    • Ji, S.-R.1    Wu, Y.2    Sui, S.-F.3
  • 53
    • 0034702813 scopus 로고    scopus 로고
    • Correlation of β-amyloid aggregate size and hydrophobicity with decreased bilayer fluidity of model membranes
    • Kremer JJ, Pallitto MM, Sklansky DJ, Murphy RM. Correlation of β-amyloid aggregate size and hydrophobicity with decreased bilayer fluidity of model membranes. Biochemistry 2000; 39: 10 309-10 318.
    • (2000) Biochemistry , vol.39 , pp. 10309-10318
    • Kremer, J.J.1    Pallitto, M.M.2    Sklansky, D.J.3    Murphy, R.M.4
  • 54
    • 0030928650 scopus 로고    scopus 로고
    • Lipid binding to amyloid β-peptide aggregates: Preferential binding of cholesterol as compared with phosphatidylcholine and fatty acids
    • Avdulov NA, Chochina SV, Igbavboa U, Warden CS, Vassiliev AV, Wood WG. Lipid binding to amyloid β-peptide aggregates: Preferential binding of cholesterol as compared with phosphatidylcholine and fatty acids. J. Neurochem. 1997; 69: 1746-1752.
    • (1997) J. Neurochem. , vol.69 , pp. 1746-1752
    • Avdulov, N.A.1    Chochina, S.V.2    Igbavboa, U.3    Warden, C.S.4    Vassiliev, A.V.5    Wood, W.G.6
  • 55
    • 0033526118 scopus 로고    scopus 로고
    • Synthesis, aggregation, and neurotoxicity of the Alzheimer's Aβ1-42 amyloid peptide and its isoaspartyl isomers
    • Fukuda H, Shimizu T, Nakajima M, Mori H, Shirasawa T. Synthesis, aggregation, and neurotoxicity of the Alzheimer's Aβ1-42 amyloid peptide and its isoaspartyl isomers. Bioorg. Med. Chem. Lett. 1999; 9: 953-956.
    • (1999) Bioorg. Med. Chem. Lett. , vol.9 , pp. 953-956
    • Fukuda, H.1    Shimizu, T.2    Nakajima, M.3    Mori, H.4    Shirasawa, T.5
  • 56
    • 0019755974 scopus 로고
    • Molecular behaviour of glycosphingolipids in interfaces. Possible participation in some properties of native membranes
    • Maggio B, Cumar FA, Caputto R. Molecular behaviour of glycosphingolipids in interfaces. Possible participation in some properties of native membranes. Biochim. Biophys. Acta 1981; 650 69-87.
    • (1981) Biochim. Biophys. Acta , vol.650 , pp. 69-87
    • Maggio, B.1    Cumar, F.A.2    Caputto, R.3
  • 57
    • 0035815982 scopus 로고    scopus 로고
    • Lipid phase separation in phospholipid bilayers and monolayers modeling the plasma membrane
    • Shaikh SR, Dumaual AC, Jenski LJ, Stillwell W. Lipid phase separation in phospholipid bilayers and monolayers modeling the plasma membrane. Biochim. Biophys. Acta 2001; 1512: 317-328.
    • (2001) Biochim. Biophys. Acta , vol.1512 , pp. 317-328
    • Shaikh, S.R.1    Dumaual, A.C.2    Jenski, L.J.3    Stillwell, W.4
  • 58
    • 0041821528 scopus 로고    scopus 로고
    • Determination of asymmetric structure of ganglioside-DPPC mixed vesicles using SANS, SAX, and DLS
    • Hirai M, Iwase H, Hayakawa T, Koizumi M, Takahashi H. Determination of asymmetric structure of ganglioside-DPPC mixed vesicles using SANS, SAX, and DLS. Biophys. J. 2003; 85: 1600-1610.
    • (2003) Biophys. J. , vol.85 , pp. 1600-1610
    • Hirai, M.1    Iwase, H.2    Hayakawa, T.3    Koizumi, M.4    Takahashi, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.